data_7HH2
# 
_entry.id   7HH2 
# 
_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   7HH2         pdb_00007hh2 10.2210/pdb7hh2/pdb 
WWPDB D_1001407464 ?            ?                   
# 
_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                        7HH2 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    2   ? ?    ? ? 
4 non-polymer syn N,N-dimethylpiperazine-1-carboxamide               157.213   1   ? ?    ? ? 
5 water       nat water                                              18.015    259 ? ?    ? ? 
# 
_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-dimethylpiperazine-1-carboxamide A1AKB 
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 
A1AKB non-polymer         . N,N-dimethylpiperazine-1-carboxamide ?                 'C7 H15 N3 O'    157.213 
ALA   'L-peptide linking' y ALANINE                              ?                 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                             ?                 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                           ?                 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                      ?                 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                             ?                 'C3 H7 N O2 S'   121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL                       'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN   'L-peptide linking' y GLUTAMINE                            ?                 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                      ?                 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                              ?                 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                            ?                 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                ?                 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                           ?                 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                              ?                 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                               ?                 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                           ?                 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                        ?                 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                              ?                 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                               ?                 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION'                        ?                 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                            ?                 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                           ?                 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                             ?                 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                               ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 29 ALA ALA 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 ?  ?   ?   B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 ?  ?   ?   C . n 
C 1 29 ILE 29 28 ?  ?   ?   C . n 
C 1 30 ALA 30 29 ?  ?   ?   C . n 
C 1 31 ASP 31 30 ?  ?   ?   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        A1AKB 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AKB 
_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 3 EDO   1   101 101 EDO   EDO B . 
I 2 SO4   1   102 1   SO4   SO4 B . 
J 2 SO4   1   103 3   SO4   SO4 B . 
K 2 SO4   1   101 5   SO4   SO4 C . 
L 4 A1AKB 1   102 101 A1AKB LIG C . 
M 5 HOH   1   201 333 HOH   HOH A . 
M 5 HOH   2   202 336 HOH   HOH A . 
M 5 HOH   3   203 307 HOH   HOH A . 
M 5 HOH   4   204 84  HOH   HOH A . 
M 5 HOH   5   205 202 HOH   HOH A . 
M 5 HOH   6   206 344 HOH   HOH A . 
M 5 HOH   7   207 335 HOH   HOH A . 
M 5 HOH   8   208 87  HOH   HOH A . 
M 5 HOH   9   209 347 HOH   HOH A . 
M 5 HOH   10  210 26  HOH   HOH A . 
M 5 HOH   11  211 55  HOH   HOH A . 
M 5 HOH   12  212 289 HOH   HOH A . 
M 5 HOH   13  213 97  HOH   HOH A . 
M 5 HOH   14  214 95  HOH   HOH A . 
M 5 HOH   15  215 299 HOH   HOH A . 
M 5 HOH   16  216 94  HOH   HOH A . 
M 5 HOH   17  217 37  HOH   HOH A . 
M 5 HOH   18  218 91  HOH   HOH A . 
M 5 HOH   19  219 304 HOH   HOH A . 
M 5 HOH   20  220 190 HOH   HOH A . 
M 5 HOH   21  221 139 HOH   HOH A . 
M 5 HOH   22  222 188 HOH   HOH A . 
M 5 HOH   23  223 66  HOH   HOH A . 
M 5 HOH   24  224 340 HOH   HOH A . 
M 5 HOH   25  225 71  HOH   HOH A . 
M 5 HOH   26  226 23  HOH   HOH A . 
M 5 HOH   27  227 86  HOH   HOH A . 
M 5 HOH   28  228 274 HOH   HOH A . 
M 5 HOH   29  229 260 HOH   HOH A . 
M 5 HOH   30  230 111 HOH   HOH A . 
M 5 HOH   31  231 8   HOH   HOH A . 
M 5 HOH   32  232 293 HOH   HOH A . 
M 5 HOH   33  233 41  HOH   HOH A . 
M 5 HOH   34  234 7   HOH   HOH A . 
M 5 HOH   35  235 165 HOH   HOH A . 
M 5 HOH   36  236 28  HOH   HOH A . 
M 5 HOH   37  237 32  HOH   HOH A . 
M 5 HOH   38  238 2   HOH   HOH A . 
M 5 HOH   39  239 199 HOH   HOH A . 
M 5 HOH   40  240 12  HOH   HOH A . 
M 5 HOH   41  241 18  HOH   HOH A . 
M 5 HOH   42  242 167 HOH   HOH A . 
M 5 HOH   43  243 99  HOH   HOH A . 
M 5 HOH   44  244 343 HOH   HOH A . 
M 5 HOH   45  245 301 HOH   HOH A . 
M 5 HOH   46  246 34  HOH   HOH A . 
M 5 HOH   47  247 38  HOH   HOH A . 
M 5 HOH   48  248 1   HOH   HOH A . 
M 5 HOH   49  249 21  HOH   HOH A . 
M 5 HOH   50  250 290 HOH   HOH A . 
M 5 HOH   51  251 288 HOH   HOH A . 
M 5 HOH   52  252 296 HOH   HOH A . 
M 5 HOH   53  253 203 HOH   HOH A . 
M 5 HOH   54  254 267 HOH   HOH A . 
M 5 HOH   55  255 278 HOH   HOH A . 
M 5 HOH   56  256 292 HOH   HOH A . 
M 5 HOH   57  257 116 HOH   HOH A . 
M 5 HOH   58  258 27  HOH   HOH A . 
M 5 HOH   59  259 318 HOH   HOH A . 
M 5 HOH   60  260 143 HOH   HOH A . 
M 5 HOH   61  261 93  HOH   HOH A . 
M 5 HOH   62  262 77  HOH   HOH A . 
M 5 HOH   63  263 287 HOH   HOH A . 
M 5 HOH   64  264 300 HOH   HOH A . 
M 5 HOH   65  265 60  HOH   HOH A . 
M 5 HOH   66  266 145 HOH   HOH A . 
M 5 HOH   67  267 20  HOH   HOH A . 
M 5 HOH   68  268 14  HOH   HOH A . 
M 5 HOH   69  269 19  HOH   HOH A . 
M 5 HOH   70  270 222 HOH   HOH A . 
M 5 HOH   71  271 179 HOH   HOH A . 
M 5 HOH   72  272 164 HOH   HOH A . 
M 5 HOH   73  273 9   HOH   HOH A . 
M 5 HOH   74  274 115 HOH   HOH A . 
M 5 HOH   75  275 345 HOH   HOH A . 
M 5 HOH   76  276 78  HOH   HOH A . 
M 5 HOH   77  277 31  HOH   HOH A . 
M 5 HOH   78  278 151 HOH   HOH A . 
M 5 HOH   79  279 47  HOH   HOH A . 
M 5 HOH   80  280 109 HOH   HOH A . 
M 5 HOH   81  281 131 HOH   HOH A . 
M 5 HOH   82  282 58  HOH   HOH A . 
M 5 HOH   83  283 16  HOH   HOH A . 
M 5 HOH   84  284 42  HOH   HOH A . 
M 5 HOH   85  285 64  HOH   HOH A . 
M 5 HOH   86  286 218 HOH   HOH A . 
M 5 HOH   87  287 113 HOH   HOH A . 
M 5 HOH   88  288 281 HOH   HOH A . 
M 5 HOH   89  289 22  HOH   HOH A . 
M 5 HOH   90  290 63  HOH   HOH A . 
M 5 HOH   91  291 337 HOH   HOH A . 
M 5 HOH   92  292 210 HOH   HOH A . 
M 5 HOH   93  293 327 HOH   HOH A . 
M 5 HOH   94  294 35  HOH   HOH A . 
M 5 HOH   95  295 211 HOH   HOH A . 
M 5 HOH   96  296 208 HOH   HOH A . 
M 5 HOH   97  297 341 HOH   HOH A . 
M 5 HOH   98  298 73  HOH   HOH A . 
M 5 HOH   99  299 83  HOH   HOH A . 
M 5 HOH   100 300 185 HOH   HOH A . 
M 5 HOH   101 301 152 HOH   HOH A . 
M 5 HOH   102 302 108 HOH   HOH A . 
M 5 HOH   103 303 357 HOH   HOH A . 
M 5 HOH   104 304 259 HOH   HOH A . 
M 5 HOH   105 305 342 HOH   HOH A . 
M 5 HOH   106 306 75  HOH   HOH A . 
M 5 HOH   107 307 219 HOH   HOH A . 
M 5 HOH   108 308 205 HOH   HOH A . 
M 5 HOH   109 309 57  HOH   HOH A . 
M 5 HOH   110 310 156 HOH   HOH A . 
M 5 HOH   111 311 283 HOH   HOH A . 
M 5 HOH   112 312 206 HOH   HOH A . 
M 5 HOH   113 313 125 HOH   HOH A . 
M 5 HOH   114 314 332 HOH   HOH A . 
N 5 HOH   1   201 89  HOH   HOH B . 
N 5 HOH   2   202 331 HOH   HOH B . 
N 5 HOH   3   203 242 HOH   HOH B . 
N 5 HOH   4   204 329 HOH   HOH B . 
N 5 HOH   5   205 258 HOH   HOH B . 
N 5 HOH   6   206 184 HOH   HOH B . 
N 5 HOH   7   207 272 HOH   HOH B . 
N 5 HOH   8   208 352 HOH   HOH B . 
N 5 HOH   9   209 17  HOH   HOH B . 
N 5 HOH   10  210 98  HOH   HOH B . 
N 5 HOH   11  211 123 HOH   HOH B . 
N 5 HOH   12  212 117 HOH   HOH B . 
N 5 HOH   13  213 249 HOH   HOH B . 
N 5 HOH   14  214 320 HOH   HOH B . 
N 5 HOH   15  215 247 HOH   HOH B . 
N 5 HOH   16  216 69  HOH   HOH B . 
N 5 HOH   17  217 338 HOH   HOH B . 
N 5 HOH   18  218 182 HOH   HOH B . 
N 5 HOH   19  219 6   HOH   HOH B . 
N 5 HOH   20  220 137 HOH   HOH B . 
N 5 HOH   21  221 54  HOH   HOH B . 
N 5 HOH   22  222 59  HOH   HOH B . 
N 5 HOH   23  223 5   HOH   HOH B . 
N 5 HOH   24  224 10  HOH   HOH B . 
N 5 HOH   25  225 215 HOH   HOH B . 
N 5 HOH   26  226 169 HOH   HOH B . 
N 5 HOH   27  227 280 HOH   HOH B . 
N 5 HOH   28  228 25  HOH   HOH B . 
N 5 HOH   29  229 68  HOH   HOH B . 
N 5 HOH   30  230 223 HOH   HOH B . 
N 5 HOH   31  231 261 HOH   HOH B . 
N 5 HOH   32  232 175 HOH   HOH B . 
N 5 HOH   33  233 177 HOH   HOH B . 
N 5 HOH   34  234 150 HOH   HOH B . 
N 5 HOH   35  235 224 HOH   HOH B . 
N 5 HOH   36  236 172 HOH   HOH B . 
N 5 HOH   37  237 319 HOH   HOH B . 
N 5 HOH   38  238 356 HOH   HOH B . 
N 5 HOH   39  239 119 HOH   HOH B . 
N 5 HOH   40  240 24  HOH   HOH B . 
N 5 HOH   41  241 36  HOH   HOH B . 
N 5 HOH   42  242 13  HOH   HOH B . 
N 5 HOH   43  243 217 HOH   HOH B . 
N 5 HOH   44  244 74  HOH   HOH B . 
N 5 HOH   45  245 168 HOH   HOH B . 
N 5 HOH   46  246 157 HOH   HOH B . 
N 5 HOH   47  247 339 HOH   HOH B . 
N 5 HOH   48  248 61  HOH   HOH B . 
N 5 HOH   49  249 44  HOH   HOH B . 
N 5 HOH   50  250 197 HOH   HOH B . 
N 5 HOH   51  251 79  HOH   HOH B . 
N 5 HOH   52  252 153 HOH   HOH B . 
N 5 HOH   53  253 170 HOH   HOH B . 
N 5 HOH   54  254 72  HOH   HOH B . 
N 5 HOH   55  255 120 HOH   HOH B . 
N 5 HOH   56  256 76  HOH   HOH B . 
N 5 HOH   57  257 46  HOH   HOH B . 
N 5 HOH   58  258 214 HOH   HOH B . 
N 5 HOH   59  259 101 HOH   HOH B . 
N 5 HOH   60  260 96  HOH   HOH B . 
N 5 HOH   61  261 315 HOH   HOH B . 
N 5 HOH   62  262 303 HOH   HOH B . 
N 5 HOH   63  263 104 HOH   HOH B . 
N 5 HOH   64  264 316 HOH   HOH B . 
N 5 HOH   65  265 163 HOH   HOH B . 
N 5 HOH   66  266 279 HOH   HOH B . 
N 5 HOH   67  267 322 HOH   HOH B . 
N 5 HOH   68  268 291 HOH   HOH B . 
N 5 HOH   69  269 201 HOH   HOH B . 
N 5 HOH   70  270 353 HOH   HOH B . 
N 5 HOH   71  271 295 HOH   HOH B . 
N 5 HOH   72  272 160 HOH   HOH B . 
N 5 HOH   73  273 314 HOH   HOH B . 
N 5 HOH   74  274 107 HOH   HOH B . 
N 5 HOH   75  275 312 HOH   HOH B . 
O 5 HOH   1   201 323 HOH   HOH C . 
O 5 HOH   2   202 321 HOH   HOH C . 
O 5 HOH   3   203 254 HOH   HOH C . 
O 5 HOH   4   204 161 HOH   HOH C . 
O 5 HOH   5   205 348 HOH   HOH C . 
O 5 HOH   6   206 354 HOH   HOH C . 
O 5 HOH   7   207 226 HOH   HOH C . 
O 5 HOH   8   208 148 HOH   HOH C . 
O 5 HOH   9   209 49  HOH   HOH C . 
O 5 HOH   10  210 271 HOH   HOH C . 
O 5 HOH   11  211 134 HOH   HOH C . 
O 5 HOH   12  212 349 HOH   HOH C . 
O 5 HOH   13  213 269 HOH   HOH C . 
O 5 HOH   14  214 85  HOH   HOH C . 
O 5 HOH   15  215 317 HOH   HOH C . 
O 5 HOH   16  216 53  HOH   HOH C . 
O 5 HOH   17  217 189 HOH   HOH C . 
O 5 HOH   18  218 90  HOH   HOH C . 
O 5 HOH   19  219 173 HOH   HOH C . 
O 5 HOH   20  220 118 HOH   HOH C . 
O 5 HOH   21  221 48  HOH   HOH C . 
O 5 HOH   22  222 142 HOH   HOH C . 
O 5 HOH   23  223 334 HOH   HOH C . 
O 5 HOH   24  224 198 HOH   HOH C . 
O 5 HOH   25  225 298 HOH   HOH C . 
O 5 HOH   26  226 302 HOH   HOH C . 
O 5 HOH   27  227 275 HOH   HOH C . 
O 5 HOH   28  228 15  HOH   HOH C . 
O 5 HOH   29  229 102 HOH   HOH C . 
O 5 HOH   30  230 309 HOH   HOH C . 
O 5 HOH   31  231 43  HOH   HOH C . 
O 5 HOH   32  232 132 HOH   HOH C . 
O 5 HOH   33  233 40  HOH   HOH C . 
O 5 HOH   34  234 45  HOH   HOH C . 
O 5 HOH   35  235 4   HOH   HOH C . 
O 5 HOH   36  236 328 HOH   HOH C . 
O 5 HOH   37  237 146 HOH   HOH C . 
O 5 HOH   38  238 65  HOH   HOH C . 
O 5 HOH   39  239 130 HOH   HOH C . 
O 5 HOH   40  240 126 HOH   HOH C . 
O 5 HOH   41  241 82  HOH   HOH C . 
O 5 HOH   42  242 149 HOH   HOH C . 
O 5 HOH   43  243 122 HOH   HOH C . 
O 5 HOH   44  244 56  HOH   HOH C . 
O 5 HOH   45  245 284 HOH   HOH C . 
O 5 HOH   46  246 171 HOH   HOH C . 
O 5 HOH   47  247 358 HOH   HOH C . 
O 5 HOH   48  248 305 HOH   HOH C . 
O 5 HOH   49  249 294 HOH   HOH C . 
O 5 HOH   50  250 67  HOH   HOH C . 
O 5 HOH   51  251 135 HOH   HOH C . 
O 5 HOH   52  252 241 HOH   HOH C . 
O 5 HOH   53  253 62  HOH   HOH C . 
O 5 HOH   54  254 359 HOH   HOH C . 
O 5 HOH   55  255 360 HOH   HOH C . 
O 5 HOH   56  256 325 HOH   HOH C . 
O 5 HOH   57  257 324 HOH   HOH C . 
O 5 HOH   58  258 270 HOH   HOH C . 
O 5 HOH   59  259 209 HOH   HOH C . 
O 5 HOH   60  260 70  HOH   HOH C . 
O 5 HOH   61  261 330 HOH   HOH C . 
O 5 HOH   62  262 355 HOH   HOH C . 
O 5 HOH   63  263 350 HOH   HOH C . 
O 5 HOH   64  264 103 HOH   HOH C . 
O 5 HOH   65  265 361 HOH   HOH C . 
O 5 HOH   66  266 246 HOH   HOH C . 
O 5 HOH   67  267 310 HOH   HOH C . 
O 5 HOH   68  268 92  HOH   HOH C . 
O 5 HOH   69  269 346 HOH   HOH C . 
O 5 HOH   70  270 313 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 73 ? CD  ? A LYS 74 CD  
2  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
3  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
4  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
5  1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
6  1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
7  1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
8  1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
9  1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
10 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
11 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
12 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
13 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
14 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
15 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
16 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
17 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
18 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
19 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
20 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
21 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
22 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
23 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
24 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
25 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
26 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
27 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
28 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
29 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
30 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
31 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
32 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
33 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
34 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
35 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
36 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
37 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
38 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
39 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
40 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
41 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
42 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
43 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' XDS     .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HH2 
_cell.length_a           41.605 
_cell.length_b           42.286 
_cell.length_c           159.243 
_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                         7HH2 
_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          7HH2 
_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                     7HH2 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             79.62 
_reflns.d_resolution_high            1.78 
_reflns.number_obs                   24619 
_reflns.percent_possible_obs         88.6 
_reflns.pdbx_Rmerge_I_obs            0.138 
_reflns.pdbx_netI_over_sigmaI        6.5 
_reflns.pdbx_redundancy              4.2 
_reflns.pdbx_Rrim_I_all              0.157 
_reflns.pdbx_Rpim_I_all              0.074 
_reflns.pdbx_CC_half                 0.993 
_reflns.pdbx_number_measured_all     102617 
_reflns.pdbx_chi_squared             0.95 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.78 
_reflns_shell.d_res_low                   1.88 
_reflns_shell.number_measured_all         14853 
_reflns_shell.number_unique_obs           3783 
_reflns_shell.Rmerge_I_obs                1.500 
_reflns_shell.pdbx_chi_squared            0.88 
_reflns_shell.pdbx_redundancy             3.9 
_reflns_shell.percent_possible_obs        95.4 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             1.733 
_reflns_shell.pdbx_Rpim_I_all             0.846 
_reflns_shell.pdbx_CC_half                0.382 
_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                                 7HH2 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     23077 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             79.62 
_refine.ls_d_res_high                            1.78 
_refine.ls_percent_reflns_obs                    87.70 
_refine.ls_R_factor_obs                          0.20093 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.19809 
_refine.ls_R_factor_R_free                       0.25124 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_number_reflns_R_free                  1265 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.962 
_refine.correlation_coeff_Fo_to_Fc_free          0.938 
_refine.B_iso_mean                               41.213 
_refine.aniso_B[1][1]                            0.79 
_refine.aniso_B[2][2]                            -0.29 
_refine.aniso_B[3][3]                            -0.50 
_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                       0.162 
_refine.pdbx_overall_ESU_R_Free                  0.155 
_refine.overall_SU_ML                            0.142 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             5.036 
_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        2134 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         49 
_refine_hist.number_atoms_solvent             259 
_refine_hist.number_atoms_total               2442 
_refine_hist.d_res_high                       1.78 
_refine_hist.d_res_low                        79.62 
# 
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             0.008  0.012  ? 2286 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.713  1.840  ? 3108 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.260  5.000  ? 264  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       7.389  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.629 10.000 ? 308  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.124  0.200  ? 283  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 1876 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  3.710  3.879  ? 1066 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 5.331  6.917  ? 1327 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.738  4.172  ? 1220 '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       10.283 55.83  ? 3614 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.782 
_refine_ls_shell.d_res_low                        1.829 
_refine_ls_shell.number_reflns_R_work             1794 
_refine_ls_shell.R_factor_R_work                  0.346 
_refine_ls_shell.percent_reflns_obs               92.87 
_refine_ls_shell.R_factor_R_free                  0.339 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             94 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HH2 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z1238477757' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HH2 
_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 3 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HH2 A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HH2 B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HH2 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 7HH2 GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HH2 SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HH2 GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HH2 SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HH2 GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HH2 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                   7HH2 
_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 218 ? ? O A HOH 224 ? ? 1.61 
2  1 O   A HOH 215 ? ? O C HOH 223 ? ? 1.66 
3  1 O   B HOH 227 ? ? O B HOH 267 ? ? 1.86 
4  1 O   A HOH 220 ? ? O A HOH 305 ? ? 1.89 
5  1 OD1 C ASP 9   ? ? O C HOH 201 ? ? 2.07 
6  1 O2  C SO4 101 ? ? O C HOH 202 ? ? 2.12 
7  1 O   C HOH 202 ? ? O C HOH 263 ? ? 2.13 
8  1 O   C HOH 237 ? ? O C HOH 257 ? ? 2.17 
9  1 O2  C SO4 101 ? ? O C HOH 203 ? ? 2.18 
10 1 OD1 A ASP 66  ? A O A 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 256 ? ? 1_555 O A HOH 270 ? ? 4_545 1.90 
2 1 O A HOH 209 ? ? 1_555 O C HOH 257 ? ? 4_445 1.96 
3 1 O A HOH 294 ? ? 1_555 O A HOH 311 ? ? 4_545 2.13 
4 1 O A HOH 301 ? ? 1_555 O A HOH 307 ? ? 4_545 2.15 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -153.24 65.87  
2 1 HIS B 20 ? ? -38.93  123.13 
3 1 ASN B 38 ? ? 77.69   -2.19  
4 1 ASN B 87 ? ? -154.67 59.62  
5 1 ASN C 87 ? ? -141.64 56.29  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    11 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    12 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            148.80 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    C 
_pdbx_validate_planes.auth_seq_id     74 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.103 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       314 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.96 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 ASP 30 ? B ASP 31 
4  1 Y 1 B GLY 31 ? B GLY 32 
5  1 Y 1 B ALA 32 ? B ALA 33 
6  1 Y 1 B VAL 33 ? B VAL 34 
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 ASP 27 ? C ASP 28 
11 1 Y 1 C ILE 28 ? C ILE 29 
12 1 Y 1 C ALA 29 ? C ALA 30 
13 1 Y 1 C ASP 30 ? C ASP 31 
14 1 Y 1 C GLY 31 ? C GLY 32 
15 1 Y 1 C ALA 32 ? C ALA 33 
16 1 Y 1 C VAL 33 ? C VAL 34 
17 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 
A1AKB N1   N N N 1   
A1AKB C4   C N N 2   
A1AKB C5   C N N 3   
A1AKB C6   C N N 4   
A1AKB O    O N N 5   
A1AKB C2   C N N 6   
A1AKB N    N N N 7   
A1AKB C1   C N N 8   
A1AKB C    C N N 9   
A1AKB N2   N N N 10  
A1AKB C3   C N N 11  
A1AKB H9   H N N 12  
A1AKB H8   H N N 13  
A1AKB H12  H N N 14  
A1AKB H11  H N N 15  
A1AKB H14  H N N 16  
A1AKB H13  H N N 17  
A1AKB H3   H N N 18  
A1AKB H4   H N N 19  
A1AKB H5   H N N 20  
A1AKB H2   H N N 21  
A1AKB H1   H N N 22  
A1AKB H    H N N 23  
A1AKB H15  H N N 24  
A1AKB H7   H N N 25  
A1AKB H6   H N N 26  
ALA   N    N N N 27  
ALA   CA   C N S 28  
ALA   C    C N N 29  
ALA   O    O N N 30  
ALA   CB   C N N 31  
ALA   OXT  O N N 32  
ALA   H    H N N 33  
ALA   H2   H N N 34  
ALA   HA   H N N 35  
ALA   HB1  H N N 36  
ALA   HB2  H N N 37  
ALA   HB3  H N N 38  
ALA   HXT  H N N 39  
ARG   N    N N N 40  
ARG   CA   C N S 41  
ARG   C    C N N 42  
ARG   O    O N N 43  
ARG   CB   C N N 44  
ARG   CG   C N N 45  
ARG   CD   C N N 46  
ARG   NE   N N N 47  
ARG   CZ   C N N 48  
ARG   NH1  N N N 49  
ARG   NH2  N N N 50  
ARG   OXT  O N N 51  
ARG   H    H N N 52  
ARG   H2   H N N 53  
ARG   HA   H N N 54  
ARG   HB2  H N N 55  
ARG   HB3  H N N 56  
ARG   HG2  H N N 57  
ARG   HG3  H N N 58  
ARG   HD2  H N N 59  
ARG   HD3  H N N 60  
ARG   HE   H N N 61  
ARG   HH11 H N N 62  
ARG   HH12 H N N 63  
ARG   HH21 H N N 64  
ARG   HH22 H N N 65  
ARG   HXT  H N N 66  
ASN   N    N N N 67  
ASN   CA   C N S 68  
ASN   C    C N N 69  
ASN   O    O N N 70  
ASN   CB   C N N 71  
ASN   CG   C N N 72  
ASN   OD1  O N N 73  
ASN   ND2  N N N 74  
ASN   OXT  O N N 75  
ASN   H    H N N 76  
ASN   H2   H N N 77  
ASN   HA   H N N 78  
ASN   HB2  H N N 79  
ASN   HB3  H N N 80  
ASN   HD21 H N N 81  
ASN   HD22 H N N 82  
ASN   HXT  H N N 83  
ASP   N    N N N 84  
ASP   CA   C N S 85  
ASP   C    C N N 86  
ASP   O    O N N 87  
ASP   CB   C N N 88  
ASP   CG   C N N 89  
ASP   OD1  O N N 90  
ASP   OD2  O N N 91  
ASP   OXT  O N N 92  
ASP   H    H N N 93  
ASP   H2   H N N 94  
ASP   HA   H N N 95  
ASP   HB2  H N N 96  
ASP   HB3  H N N 97  
ASP   HD2  H N N 98  
ASP   HXT  H N N 99  
CYS   N    N N N 100 
CYS   CA   C N R 101 
CYS   C    C N N 102 
CYS   O    O N N 103 
CYS   CB   C N N 104 
CYS   SG   S N N 105 
CYS   OXT  O N N 106 
CYS   H    H N N 107 
CYS   H2   H N N 108 
CYS   HA   H N N 109 
CYS   HB2  H N N 110 
CYS   HB3  H N N 111 
CYS   HG   H N N 112 
CYS   HXT  H N N 113 
EDO   C1   C N N 114 
EDO   O1   O N N 115 
EDO   C2   C N N 116 
EDO   O2   O N N 117 
EDO   H11  H N N 118 
EDO   H12  H N N 119 
EDO   HO1  H N N 120 
EDO   H21  H N N 121 
EDO   H22  H N N 122 
EDO   HO2  H N N 123 
GLN   N    N N N 124 
GLN   CA   C N S 125 
GLN   C    C N N 126 
GLN   O    O N N 127 
GLN   CB   C N N 128 
GLN   CG   C N N 129 
GLN   CD   C N N 130 
GLN   OE1  O N N 131 
GLN   NE2  N N N 132 
GLN   OXT  O N N 133 
GLN   H    H N N 134 
GLN   H2   H N N 135 
GLN   HA   H N N 136 
GLN   HB2  H N N 137 
GLN   HB3  H N N 138 
GLN   HG2  H N N 139 
GLN   HG3  H N N 140 
GLN   HE21 H N N 141 
GLN   HE22 H N N 142 
GLN   HXT  H N N 143 
GLU   N    N N N 144 
GLU   CA   C N S 145 
GLU   C    C N N 146 
GLU   O    O N N 147 
GLU   CB   C N N 148 
GLU   CG   C N N 149 
GLU   CD   C N N 150 
GLU   OE1  O N N 151 
GLU   OE2  O N N 152 
GLU   OXT  O N N 153 
GLU   H    H N N 154 
GLU   H2   H N N 155 
GLU   HA   H N N 156 
GLU   HB2  H N N 157 
GLU   HB3  H N N 158 
GLU   HG2  H N N 159 
GLU   HG3  H N N 160 
GLU   HE2  H N N 161 
GLU   HXT  H N N 162 
GLY   N    N N N 163 
GLY   CA   C N N 164 
GLY   C    C N N 165 
GLY   O    O N N 166 
GLY   OXT  O N N 167 
GLY   H    H N N 168 
GLY   H2   H N N 169 
GLY   HA2  H N N 170 
GLY   HA3  H N N 171 
GLY   HXT  H N N 172 
HIS   N    N N N 173 
HIS   CA   C N S 174 
HIS   C    C N N 175 
HIS   O    O N N 176 
HIS   CB   C N N 177 
HIS   CG   C Y N 178 
HIS   ND1  N Y N 179 
HIS   CD2  C Y N 180 
HIS   CE1  C Y N 181 
HIS   NE2  N Y N 182 
HIS   OXT  O N N 183 
HIS   H    H N N 184 
HIS   H2   H N N 185 
HIS   HA   H N N 186 
HIS   HB2  H N N 187 
HIS   HB3  H N N 188 
HIS   HD1  H N N 189 
HIS   HD2  H N N 190 
HIS   HE1  H N N 191 
HIS   HE2  H N N 192 
HIS   HXT  H N N 193 
HOH   O    O N N 194 
HOH   H1   H N N 195 
HOH   H2   H N N 196 
ILE   N    N N N 197 
ILE   CA   C N S 198 
ILE   C    C N N 199 
ILE   O    O N N 200 
ILE   CB   C N S 201 
ILE   CG1  C N N 202 
ILE   CG2  C N N 203 
ILE   CD1  C N N 204 
ILE   OXT  O N N 205 
ILE   H    H N N 206 
ILE   H2   H N N 207 
ILE   HA   H N N 208 
ILE   HB   H N N 209 
ILE   HG12 H N N 210 
ILE   HG13 H N N 211 
ILE   HG21 H N N 212 
ILE   HG22 H N N 213 
ILE   HG23 H N N 214 
ILE   HD11 H N N 215 
ILE   HD12 H N N 216 
ILE   HD13 H N N 217 
ILE   HXT  H N N 218 
LEU   N    N N N 219 
LEU   CA   C N S 220 
LEU   C    C N N 221 
LEU   O    O N N 222 
LEU   CB   C N N 223 
LEU   CG   C N N 224 
LEU   CD1  C N N 225 
LEU   CD2  C N N 226 
LEU   OXT  O N N 227 
LEU   H    H N N 228 
LEU   H2   H N N 229 
LEU   HA   H N N 230 
LEU   HB2  H N N 231 
LEU   HB3  H N N 232 
LEU   HG   H N N 233 
LEU   HD11 H N N 234 
LEU   HD12 H N N 235 
LEU   HD13 H N N 236 
LEU   HD21 H N N 237 
LEU   HD22 H N N 238 
LEU   HD23 H N N 239 
LEU   HXT  H N N 240 
LYS   N    N N N 241 
LYS   CA   C N S 242 
LYS   C    C N N 243 
LYS   O    O N N 244 
LYS   CB   C N N 245 
LYS   CG   C N N 246 
LYS   CD   C N N 247 
LYS   CE   C N N 248 
LYS   NZ   N N N 249 
LYS   OXT  O N N 250 
LYS   H    H N N 251 
LYS   H2   H N N 252 
LYS   HA   H N N 253 
LYS   HB2  H N N 254 
LYS   HB3  H N N 255 
LYS   HG2  H N N 256 
LYS   HG3  H N N 257 
LYS   HD2  H N N 258 
LYS   HD3  H N N 259 
LYS   HE2  H N N 260 
LYS   HE3  H N N 261 
LYS   HZ1  H N N 262 
LYS   HZ2  H N N 263 
LYS   HZ3  H N N 264 
LYS   HXT  H N N 265 
MET   N    N N N 266 
MET   CA   C N S 267 
MET   C    C N N 268 
MET   O    O N N 269 
MET   CB   C N N 270 
MET   CG   C N N 271 
MET   SD   S N N 272 
MET   CE   C N N 273 
MET   OXT  O N N 274 
MET   H    H N N 275 
MET   H2   H N N 276 
MET   HA   H N N 277 
MET   HB2  H N N 278 
MET   HB3  H N N 279 
MET   HG2  H N N 280 
MET   HG3  H N N 281 
MET   HE1  H N N 282 
MET   HE2  H N N 283 
MET   HE3  H N N 284 
MET   HXT  H N N 285 
PHE   N    N N N 286 
PHE   CA   C N S 287 
PHE   C    C N N 288 
PHE   O    O N N 289 
PHE   CB   C N N 290 
PHE   CG   C Y N 291 
PHE   CD1  C Y N 292 
PHE   CD2  C Y N 293 
PHE   CE1  C Y N 294 
PHE   CE2  C Y N 295 
PHE   CZ   C Y N 296 
PHE   OXT  O N N 297 
PHE   H    H N N 298 
PHE   H2   H N N 299 
PHE   HA   H N N 300 
PHE   HB2  H N N 301 
PHE   HB3  H N N 302 
PHE   HD1  H N N 303 
PHE   HD2  H N N 304 
PHE   HE1  H N N 305 
PHE   HE2  H N N 306 
PHE   HZ   H N N 307 
PHE   HXT  H N N 308 
PRO   N    N N N 309 
PRO   CA   C N S 310 
PRO   C    C N N 311 
PRO   O    O N N 312 
PRO   CB   C N N 313 
PRO   CG   C N N 314 
PRO   CD   C N N 315 
PRO   OXT  O N N 316 
PRO   H    H N N 317 
PRO   HA   H N N 318 
PRO   HB2  H N N 319 
PRO   HB3  H N N 320 
PRO   HG2  H N N 321 
PRO   HG3  H N N 322 
PRO   HD2  H N N 323 
PRO   HD3  H N N 324 
PRO   HXT  H N N 325 
SER   N    N N N 326 
SER   CA   C N S 327 
SER   C    C N N 328 
SER   O    O N N 329 
SER   CB   C N N 330 
SER   OG   O N N 331 
SER   OXT  O N N 332 
SER   H    H N N 333 
SER   H2   H N N 334 
SER   HA   H N N 335 
SER   HB2  H N N 336 
SER   HB3  H N N 337 
SER   HG   H N N 338 
SER   HXT  H N N 339 
SO4   S    S N N 340 
SO4   O1   O N N 341 
SO4   O2   O N N 342 
SO4   O3   O N N 343 
SO4   O4   O N N 344 
THR   N    N N N 345 
THR   CA   C N S 346 
THR   C    C N N 347 
THR   O    O N N 348 
THR   CB   C N R 349 
THR   OG1  O N N 350 
THR   CG2  C N N 351 
THR   OXT  O N N 352 
THR   H    H N N 353 
THR   H2   H N N 354 
THR   HA   H N N 355 
THR   HB   H N N 356 
THR   HG1  H N N 357 
THR   HG21 H N N 358 
THR   HG22 H N N 359 
THR   HG23 H N N 360 
THR   HXT  H N N 361 
TRP   N    N N N 362 
TRP   CA   C N S 363 
TRP   C    C N N 364 
TRP   O    O N N 365 
TRP   CB   C N N 366 
TRP   CG   C Y N 367 
TRP   CD1  C Y N 368 
TRP   CD2  C Y N 369 
TRP   NE1  N Y N 370 
TRP   CE2  C Y N 371 
TRP   CE3  C Y N 372 
TRP   CZ2  C Y N 373 
TRP   CZ3  C Y N 374 
TRP   CH2  C Y N 375 
TRP   OXT  O N N 376 
TRP   H    H N N 377 
TRP   H2   H N N 378 
TRP   HA   H N N 379 
TRP   HB2  H N N 380 
TRP   HB3  H N N 381 
TRP   HD1  H N N 382 
TRP   HE1  H N N 383 
TRP   HE3  H N N 384 
TRP   HZ2  H N N 385 
TRP   HZ3  H N N 386 
TRP   HH2  H N N 387 
TRP   HXT  H N N 388 
TYR   N    N N N 389 
TYR   CA   C N S 390 
TYR   C    C N N 391 
TYR   O    O N N 392 
TYR   CB   C N N 393 
TYR   CG   C Y N 394 
TYR   CD1  C Y N 395 
TYR   CD2  C Y N 396 
TYR   CE1  C Y N 397 
TYR   CE2  C Y N 398 
TYR   CZ   C Y N 399 
TYR   OH   O N N 400 
TYR   OXT  O N N 401 
TYR   H    H N N 402 
TYR   H2   H N N 403 
TYR   HA   H N N 404 
TYR   HB2  H N N 405 
TYR   HB3  H N N 406 
TYR   HD1  H N N 407 
TYR   HD2  H N N 408 
TYR   HE1  H N N 409 
TYR   HE2  H N N 410 
TYR   HH   H N N 411 
TYR   HXT  H N N 412 
VAL   N    N N N 413 
VAL   CA   C N S 414 
VAL   C    C N N 415 
VAL   O    O N N 416 
VAL   CB   C N N 417 
VAL   CG1  C N N 418 
VAL   CG2  C N N 419 
VAL   OXT  O N N 420 
VAL   H    H N N 421 
VAL   H2   H N N 422 
VAL   HA   H N N 423 
VAL   HB   H N N 424 
VAL   HG11 H N N 425 
VAL   HG12 H N N 426 
VAL   HG13 H N N 427 
VAL   HG21 H N N 428 
VAL   HG22 H N N 429 
VAL   HG23 H N N 430 
VAL   HXT  H N N 431 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1AKB C   N    sing N N 1   
A1AKB C1  N    sing N N 2   
A1AKB N   C2   sing N N 3   
A1AKB C2  O    doub N N 4   
A1AKB N1  C2   sing N N 5   
A1AKB N1  C3   sing N N 6   
A1AKB C3  C4   sing N N 7   
A1AKB C4  N2   sing N N 8   
A1AKB N2  C5   sing N N 9   
A1AKB C5  C6   sing N N 10  
A1AKB C6  N1   sing N N 11  
A1AKB C4  H9   sing N N 12  
A1AKB C4  H8   sing N N 13  
A1AKB C5  H12  sing N N 14  
A1AKB C5  H11  sing N N 15  
A1AKB C6  H14  sing N N 16  
A1AKB C6  H13  sing N N 17  
A1AKB C1  H3   sing N N 18  
A1AKB C1  H4   sing N N 19  
A1AKB C1  H5   sing N N 20  
A1AKB C   H2   sing N N 21  
A1AKB C   H1   sing N N 22  
A1AKB C   H    sing N N 23  
A1AKB N2  H15  sing N N 24  
A1AKB C3  H7   sing N N 25  
A1AKB C3  H6   sing N N 26  
ALA   N   CA   sing N N 27  
ALA   N   H    sing N N 28  
ALA   N   H2   sing N N 29  
ALA   CA  C    sing N N 30  
ALA   CA  CB   sing N N 31  
ALA   CA  HA   sing N N 32  
ALA   C   O    doub N N 33  
ALA   C   OXT  sing N N 34  
ALA   CB  HB1  sing N N 35  
ALA   CB  HB2  sing N N 36  
ALA   CB  HB3  sing N N 37  
ALA   OXT HXT  sing N N 38  
ARG   N   CA   sing N N 39  
ARG   N   H    sing N N 40  
ARG   N   H2   sing N N 41  
ARG   CA  C    sing N N 42  
ARG   CA  CB   sing N N 43  
ARG   CA  HA   sing N N 44  
ARG   C   O    doub N N 45  
ARG   C   OXT  sing N N 46  
ARG   CB  CG   sing N N 47  
ARG   CB  HB2  sing N N 48  
ARG   CB  HB3  sing N N 49  
ARG   CG  CD   sing N N 50  
ARG   CG  HG2  sing N N 51  
ARG   CG  HG3  sing N N 52  
ARG   CD  NE   sing N N 53  
ARG   CD  HD2  sing N N 54  
ARG   CD  HD3  sing N N 55  
ARG   NE  CZ   sing N N 56  
ARG   NE  HE   sing N N 57  
ARG   CZ  NH1  sing N N 58  
ARG   CZ  NH2  doub N N 59  
ARG   NH1 HH11 sing N N 60  
ARG   NH1 HH12 sing N N 61  
ARG   NH2 HH21 sing N N 62  
ARG   NH2 HH22 sing N N 63  
ARG   OXT HXT  sing N N 64  
ASN   N   CA   sing N N 65  
ASN   N   H    sing N N 66  
ASN   N   H2   sing N N 67  
ASN   CA  C    sing N N 68  
ASN   CA  CB   sing N N 69  
ASN   CA  HA   sing N N 70  
ASN   C   O    doub N N 71  
ASN   C   OXT  sing N N 72  
ASN   CB  CG   sing N N 73  
ASN   CB  HB2  sing N N 74  
ASN   CB  HB3  sing N N 75  
ASN   CG  OD1  doub N N 76  
ASN   CG  ND2  sing N N 77  
ASN   ND2 HD21 sing N N 78  
ASN   ND2 HD22 sing N N 79  
ASN   OXT HXT  sing N N 80  
ASP   N   CA   sing N N 81  
ASP   N   H    sing N N 82  
ASP   N   H2   sing N N 83  
ASP   CA  C    sing N N 84  
ASP   CA  CB   sing N N 85  
ASP   CA  HA   sing N N 86  
ASP   C   O    doub N N 87  
ASP   C   OXT  sing N N 88  
ASP   CB  CG   sing N N 89  
ASP   CB  HB2  sing N N 90  
ASP   CB  HB3  sing N N 91  
ASP   CG  OD1  doub N N 92  
ASP   CG  OD2  sing N N 93  
ASP   OD2 HD2  sing N N 94  
ASP   OXT HXT  sing N N 95  
CYS   N   CA   sing N N 96  
CYS   N   H    sing N N 97  
CYS   N   H2   sing N N 98  
CYS   CA  C    sing N N 99  
CYS   CA  CB   sing N N 100 
CYS   CA  HA   sing N N 101 
CYS   C   O    doub N N 102 
CYS   C   OXT  sing N N 103 
CYS   CB  SG   sing N N 104 
CYS   CB  HB2  sing N N 105 
CYS   CB  HB3  sing N N 106 
CYS   SG  HG   sing N N 107 
CYS   OXT HXT  sing N N 108 
EDO   C1  O1   sing N N 109 
EDO   C1  C2   sing N N 110 
EDO   C1  H11  sing N N 111 
EDO   C1  H12  sing N N 112 
EDO   O1  HO1  sing N N 113 
EDO   C2  O2   sing N N 114 
EDO   C2  H21  sing N N 115 
EDO   C2  H22  sing N N 116 
EDO   O2  HO2  sing N N 117 
GLN   N   CA   sing N N 118 
GLN   N   H    sing N N 119 
GLN   N   H2   sing N N 120 
GLN   CA  C    sing N N 121 
GLN   CA  CB   sing N N 122 
GLN   CA  HA   sing N N 123 
GLN   C   O    doub N N 124 
GLN   C   OXT  sing N N 125 
GLN   CB  CG   sing N N 126 
GLN   CB  HB2  sing N N 127 
GLN   CB  HB3  sing N N 128 
GLN   CG  CD   sing N N 129 
GLN   CG  HG2  sing N N 130 
GLN   CG  HG3  sing N N 131 
GLN   CD  OE1  doub N N 132 
GLN   CD  NE2  sing N N 133 
GLN   NE2 HE21 sing N N 134 
GLN   NE2 HE22 sing N N 135 
GLN   OXT HXT  sing N N 136 
GLU   N   CA   sing N N 137 
GLU   N   H    sing N N 138 
GLU   N   H2   sing N N 139 
GLU   CA  C    sing N N 140 
GLU   CA  CB   sing N N 141 
GLU   CA  HA   sing N N 142 
GLU   C   O    doub N N 143 
GLU   C   OXT  sing N N 144 
GLU   CB  CG   sing N N 145 
GLU   CB  HB2  sing N N 146 
GLU   CB  HB3  sing N N 147 
GLU   CG  CD   sing N N 148 
GLU   CG  HG2  sing N N 149 
GLU   CG  HG3  sing N N 150 
GLU   CD  OE1  doub N N 151 
GLU   CD  OE2  sing N N 152 
GLU   OE2 HE2  sing N N 153 
GLU   OXT HXT  sing N N 154 
GLY   N   CA   sing N N 155 
GLY   N   H    sing N N 156 
GLY   N   H2   sing N N 157 
GLY   CA  C    sing N N 158 
GLY   CA  HA2  sing N N 159 
GLY   CA  HA3  sing N N 160 
GLY   C   O    doub N N 161 
GLY   C   OXT  sing N N 162 
GLY   OXT HXT  sing N N 163 
HIS   N   CA   sing N N 164 
HIS   N   H    sing N N 165 
HIS   N   H2   sing N N 166 
HIS   CA  C    sing N N 167 
HIS   CA  CB   sing N N 168 
HIS   CA  HA   sing N N 169 
HIS   C   O    doub N N 170 
HIS   C   OXT  sing N N 171 
HIS   CB  CG   sing N N 172 
HIS   CB  HB2  sing N N 173 
HIS   CB  HB3  sing N N 174 
HIS   CG  ND1  sing Y N 175 
HIS   CG  CD2  doub Y N 176 
HIS   ND1 CE1  doub Y N 177 
HIS   ND1 HD1  sing N N 178 
HIS   CD2 NE2  sing Y N 179 
HIS   CD2 HD2  sing N N 180 
HIS   CE1 NE2  sing Y N 181 
HIS   CE1 HE1  sing N N 182 
HIS   NE2 HE2  sing N N 183 
HIS   OXT HXT  sing N N 184 
HOH   O   H1   sing N N 185 
HOH   O   H2   sing N N 186 
ILE   N   CA   sing N N 187 
ILE   N   H    sing N N 188 
ILE   N   H2   sing N N 189 
ILE   CA  C    sing N N 190 
ILE   CA  CB   sing N N 191 
ILE   CA  HA   sing N N 192 
ILE   C   O    doub N N 193 
ILE   C   OXT  sing N N 194 
ILE   CB  CG1  sing N N 195 
ILE   CB  CG2  sing N N 196 
ILE   CB  HB   sing N N 197 
ILE   CG1 CD1  sing N N 198 
ILE   CG1 HG12 sing N N 199 
ILE   CG1 HG13 sing N N 200 
ILE   CG2 HG21 sing N N 201 
ILE   CG2 HG22 sing N N 202 
ILE   CG2 HG23 sing N N 203 
ILE   CD1 HD11 sing N N 204 
ILE   CD1 HD12 sing N N 205 
ILE   CD1 HD13 sing N N 206 
ILE   OXT HXT  sing N N 207 
LEU   N   CA   sing N N 208 
LEU   N   H    sing N N 209 
LEU   N   H2   sing N N 210 
LEU   CA  C    sing N N 211 
LEU   CA  CB   sing N N 212 
LEU   CA  HA   sing N N 213 
LEU   C   O    doub N N 214 
LEU   C   OXT  sing N N 215 
LEU   CB  CG   sing N N 216 
LEU   CB  HB2  sing N N 217 
LEU   CB  HB3  sing N N 218 
LEU   CG  CD1  sing N N 219 
LEU   CG  CD2  sing N N 220 
LEU   CG  HG   sing N N 221 
LEU   CD1 HD11 sing N N 222 
LEU   CD1 HD12 sing N N 223 
LEU   CD1 HD13 sing N N 224 
LEU   CD2 HD21 sing N N 225 
LEU   CD2 HD22 sing N N 226 
LEU   CD2 HD23 sing N N 227 
LEU   OXT HXT  sing N N 228 
LYS   N   CA   sing N N 229 
LYS   N   H    sing N N 230 
LYS   N   H2   sing N N 231 
LYS   CA  C    sing N N 232 
LYS   CA  CB   sing N N 233 
LYS   CA  HA   sing N N 234 
LYS   C   O    doub N N 235 
LYS   C   OXT  sing N N 236 
LYS   CB  CG   sing N N 237 
LYS   CB  HB2  sing N N 238 
LYS   CB  HB3  sing N N 239 
LYS   CG  CD   sing N N 240 
LYS   CG  HG2  sing N N 241 
LYS   CG  HG3  sing N N 242 
LYS   CD  CE   sing N N 243 
LYS   CD  HD2  sing N N 244 
LYS   CD  HD3  sing N N 245 
LYS   CE  NZ   sing N N 246 
LYS   CE  HE2  sing N N 247 
LYS   CE  HE3  sing N N 248 
LYS   NZ  HZ1  sing N N 249 
LYS   NZ  HZ2  sing N N 250 
LYS   NZ  HZ3  sing N N 251 
LYS   OXT HXT  sing N N 252 
MET   N   CA   sing N N 253 
MET   N   H    sing N N 254 
MET   N   H2   sing N N 255 
MET   CA  C    sing N N 256 
MET   CA  CB   sing N N 257 
MET   CA  HA   sing N N 258 
MET   C   O    doub N N 259 
MET   C   OXT  sing N N 260 
MET   CB  CG   sing N N 261 
MET   CB  HB2  sing N N 262 
MET   CB  HB3  sing N N 263 
MET   CG  SD   sing N N 264 
MET   CG  HG2  sing N N 265 
MET   CG  HG3  sing N N 266 
MET   SD  CE   sing N N 267 
MET   CE  HE1  sing N N 268 
MET   CE  HE2  sing N N 269 
MET   CE  HE3  sing N N 270 
MET   OXT HXT  sing N N 271 
PHE   N   CA   sing N N 272 
PHE   N   H    sing N N 273 
PHE   N   H2   sing N N 274 
PHE   CA  C    sing N N 275 
PHE   CA  CB   sing N N 276 
PHE   CA  HA   sing N N 277 
PHE   C   O    doub N N 278 
PHE   C   OXT  sing N N 279 
PHE   CB  CG   sing N N 280 
PHE   CB  HB2  sing N N 281 
PHE   CB  HB3  sing N N 282 
PHE   CG  CD1  doub Y N 283 
PHE   CG  CD2  sing Y N 284 
PHE   CD1 CE1  sing Y N 285 
PHE   CD1 HD1  sing N N 286 
PHE   CD2 CE2  doub Y N 287 
PHE   CD2 HD2  sing N N 288 
PHE   CE1 CZ   doub Y N 289 
PHE   CE1 HE1  sing N N 290 
PHE   CE2 CZ   sing Y N 291 
PHE   CE2 HE2  sing N N 292 
PHE   CZ  HZ   sing N N 293 
PHE   OXT HXT  sing N N 294 
PRO   N   CA   sing N N 295 
PRO   N   CD   sing N N 296 
PRO   N   H    sing N N 297 
PRO   CA  C    sing N N 298 
PRO   CA  CB   sing N N 299 
PRO   CA  HA   sing N N 300 
PRO   C   O    doub N N 301 
PRO   C   OXT  sing N N 302 
PRO   CB  CG   sing N N 303 
PRO   CB  HB2  sing N N 304 
PRO   CB  HB3  sing N N 305 
PRO   CG  CD   sing N N 306 
PRO   CG  HG2  sing N N 307 
PRO   CG  HG3  sing N N 308 
PRO   CD  HD2  sing N N 309 
PRO   CD  HD3  sing N N 310 
PRO   OXT HXT  sing N N 311 
SER   N   CA   sing N N 312 
SER   N   H    sing N N 313 
SER   N   H2   sing N N 314 
SER   CA  C    sing N N 315 
SER   CA  CB   sing N N 316 
SER   CA  HA   sing N N 317 
SER   C   O    doub N N 318 
SER   C   OXT  sing N N 319 
SER   CB  OG   sing N N 320 
SER   CB  HB2  sing N N 321 
SER   CB  HB3  sing N N 322 
SER   OG  HG   sing N N 323 
SER   OXT HXT  sing N N 324 
SO4   S   O1   doub N N 325 
SO4   S   O2   doub N N 326 
SO4   S   O3   sing N N 327 
SO4   S   O4   sing N N 328 
THR   N   CA   sing N N 329 
THR   N   H    sing N N 330 
THR   N   H2   sing N N 331 
THR   CA  C    sing N N 332 
THR   CA  CB   sing N N 333 
THR   CA  HA   sing N N 334 
THR   C   O    doub N N 335 
THR   C   OXT  sing N N 336 
THR   CB  OG1  sing N N 337 
THR   CB  CG2  sing N N 338 
THR   CB  HB   sing N N 339 
THR   OG1 HG1  sing N N 340 
THR   CG2 HG21 sing N N 341 
THR   CG2 HG22 sing N N 342 
THR   CG2 HG23 sing N N 343 
THR   OXT HXT  sing N N 344 
TRP   N   CA   sing N N 345 
TRP   N   H    sing N N 346 
TRP   N   H2   sing N N 347 
TRP   CA  C    sing N N 348 
TRP   CA  CB   sing N N 349 
TRP   CA  HA   sing N N 350 
TRP   C   O    doub N N 351 
TRP   C   OXT  sing N N 352 
TRP   CB  CG   sing N N 353 
TRP   CB  HB2  sing N N 354 
TRP   CB  HB3  sing N N 355 
TRP   CG  CD1  doub Y N 356 
TRP   CG  CD2  sing Y N 357 
TRP   CD1 NE1  sing Y N 358 
TRP   CD1 HD1  sing N N 359 
TRP   CD2 CE2  doub Y N 360 
TRP   CD2 CE3  sing Y N 361 
TRP   NE1 CE2  sing Y N 362 
TRP   NE1 HE1  sing N N 363 
TRP   CE2 CZ2  sing Y N 364 
TRP   CE3 CZ3  doub Y N 365 
TRP   CE3 HE3  sing N N 366 
TRP   CZ2 CH2  doub Y N 367 
TRP   CZ2 HZ2  sing N N 368 
TRP   CZ3 CH2  sing Y N 369 
TRP   CZ3 HZ3  sing N N 370 
TRP   CH2 HH2  sing N N 371 
TRP   OXT HXT  sing N N 372 
TYR   N   CA   sing N N 373 
TYR   N   H    sing N N 374 
TYR   N   H2   sing N N 375 
TYR   CA  C    sing N N 376 
TYR   CA  CB   sing N N 377 
TYR   CA  HA   sing N N 378 
TYR   C   O    doub N N 379 
TYR   C   OXT  sing N N 380 
TYR   CB  CG   sing N N 381 
TYR   CB  HB2  sing N N 382 
TYR   CB  HB3  sing N N 383 
TYR   CG  CD1  doub Y N 384 
TYR   CG  CD2  sing Y N 385 
TYR   CD1 CE1  sing Y N 386 
TYR   CD1 HD1  sing N N 387 
TYR   CD2 CE2  doub Y N 388 
TYR   CD2 HD2  sing N N 389 
TYR   CE1 CZ   doub Y N 390 
TYR   CE1 HE1  sing N N 391 
TYR   CE2 CZ   sing Y N 392 
TYR   CE2 HE2  sing N N 393 
TYR   CZ  OH   sing N N 394 
TYR   OH  HH   sing N N 395 
TYR   OXT HXT  sing N N 396 
VAL   N   CA   sing N N 397 
VAL   N   H    sing N N 398 
VAL   N   H2   sing N N 399 
VAL   CA  C    sing N N 400 
VAL   CA  CB   sing N N 401 
VAL   CA  HA   sing N N 402 
VAL   C   O    doub N N 403 
VAL   C   OXT  sing N N 404 
VAL   CB  CG1  sing N N 405 
VAL   CB  CG2  sing N N 406 
VAL   CB  HB   sing N N 407 
VAL   CG1 HG11 sing N N 408 
VAL   CG1 HG12 sing N N 409 
VAL   CG1 HG13 sing N N 410 
VAL   CG2 HG21 sing N N 411 
VAL   CG2 HG22 sing N N 412 
VAL   CG2 HG23 sing N N 413 
VAL   OXT HXT  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                    7HH2 
_atom_sites.fract_transf_matrix[1][1]   0.024036 
_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]   0.023648 
_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]   0.006280 
_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  ? 1.190   4.086   2.627   1.00 62.88  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? 0.060   3.533   1.836   1.00 62.24  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? 0.566   2.470   0.854   1.00 57.08  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 1.659   2.591   0.307   1.00 55.06  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -0.728  4.655   1.149   1.00 70.05  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -1.788  5.307   2.043   1.00 91.54  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -3.281  4.380   2.478   1.00 93.72  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -4.145  5.572   3.511   1.00 87.36  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? -0.184  1.355   0.659   1.00 52.95  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? 0.179   0.296   -0.300  1.00 51.50  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? 0.427   0.638   -1.774  1.00 48.79  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? -0.247  1.477   -2.371  1.00 47.45  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -1.038  -0.680  -0.138  1.00 51.40  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -1.463  -0.490  1.308   1.00 50.39  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -1.395  1.018   1.432   1.00 50.62  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 1.392   -0.060  -2.367  1.00 42.61  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 1.614   0.001   -3.801  1.00 42.01  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 1.010   -1.267  -4.396  1.00 38.07  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? 0.482   -2.096  -3.656  1.00 38.17  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 3.116   0.152   -4.083  1.00 50.61  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 3.722   1.442   -3.577  1.00 65.60  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 3.479   1.975   -2.325  1.00 71.44  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 4.576   2.301   -4.169  1.00 67.68  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 4.141   3.116   -2.182  1.00 63.38  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 4.818   3.330   -3.287  1.00 66.39  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 1.060   -1.417  -5.723  1.00 32.80  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? 0.834   -2.720  -6.321  1.00 32.30  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 1.953   -3.675  -5.930  1.00 29.72  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 3.024   -3.246  -5.512  1.00 29.05  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? 0.727   -2.615  -7.822  1.00 35.70  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 1.696   -4.962  -6.140  1.00 28.03  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 2.688   -5.986  -5.882  1.00 32.86  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 3.860   -5.788  -6.840  1.00 34.88  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 3.671   -5.353  -7.984  1.00 33.75  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 2.181   -7.427  -5.987  1.00 27.15  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 1.428   -7.812  -4.718  1.00 32.26  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 2.111   -8.100  -3.538  1.00 28.43  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? 0.029   -7.880  -4.712  1.00 31.89  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 1.421   -8.439  -2.374  1.00 30.04  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -0.653  -8.240  -3.557  1.00 25.08  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? 0.034   -8.469  -2.383  1.00 30.06  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 5.060   -6.126  -6.358  1.00 29.93  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 6.216   -6.046  -7.233  1.00 30.20  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 7.146   -7.224  -6.950  1.00 25.77  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 7.131   -7.788  -5.869  1.00 23.92  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 6.874   -4.677  -7.064  1.00 30.28  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 7.557   -4.580  -5.728  1.00 31.89  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 8.302   -3.268  -5.488  1.00 39.39  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 8.872   -3.276  -4.100  1.00 40.68  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 7.797   -3.167  -3.104  1.00 35.70  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 8.014   -7.600  -7.908  1.00 27.48  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 8.986   -8.674  -7.680  1.00 25.29  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 9.788   -8.390  -6.411  1.00 25.42  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 10.216  -7.255  -6.157  1.00 27.98  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 9.864   -8.581  -8.976  1.00 26.69  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 8.899   -8.032  -10.019 1.00 26.84  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 8.168   -6.938  -9.228  1.00 27.74  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 10.003  -9.446  -5.618  1.00 25.91  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 10.734  -9.341  -4.376  1.00 23.83  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 9.786   -9.266  -3.175  1.00 27.57  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 10.210  -9.501  -2.030  1.00 25.19  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 8.507   -8.910  -3.417  1.00 20.74  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 7.590   -8.794  -2.288  1.00 22.32  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 7.352   -10.164 -1.647  1.00 20.95  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 7.119   -11.135 -2.357  1.00 19.86  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 6.228   -8.232  -2.711  1.00 22.19  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 6.181   -6.727  -2.909  1.00 26.70  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 7.135   -6.031  -2.466  1.00 24.73  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 5.189   -6.244  -3.515  1.00 26.15  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 7.256   -10.216 -0.306  1.00 21.09  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 7.061   -11.476 0.402   1.00 20.90  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 5.591   -11.558 0.822   1.00 24.54  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 5.027   -10.553 1.305   1.00 24.85  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 8.018   -11.467 1.596   1.00 22.73  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 9.496   -11.268 1.222   1.00 20.73  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 10.320  -11.255 2.523   1.00 22.33  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 9.929   -12.402 0.248   1.00 21.14  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 4.997   -12.761 0.682   1.00 22.25  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 3.568   -12.940 0.928   1.00 21.92  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 3.333   -14.310 1.560   1.00 24.15  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 4.239   -15.148 1.645   1.00 21.68  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 2.747   -12.810 -0.371  1.00 23.96  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 2.829   -11.393 -0.944  1.00 19.71  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 3.226   -13.831 -1.417  1.00 23.91  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 2.105   -14.516 2.031   1.00 22.00  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 1.558   -15.851 2.088   1.00 22.56  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? 0.602   -15.950 0.910   1.00 23.26  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? -0.207  -15.039 0.719   1.00 22.87  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? 0.810   -16.244 3.374   1.00 23.10  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 1.728   -16.322 4.582   1.00 24.69  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 2.074   -15.179 5.298   1.00 26.58  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 2.248   -17.538 4.992   1.00 24.44  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 2.972   -15.252 6.353   1.00 31.45  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 3.144   -17.606 6.062   1.00 27.15  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 3.483   -16.474 6.747   1.00 28.01  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? 0.730   -17.051 0.143   1.00 23.73  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? -0.051  -17.205 -1.078  1.00 27.78  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -1.039  -18.359 -0.898  1.00 28.60  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -0.671  -19.426 -0.398  1.00 24.48  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? 0.826   -17.414 -2.321  1.00 22.63  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -2.301  -18.102 -1.281  1.00 26.74  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -3.358  -19.051 -0.998  1.00 26.49  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -3.717  -19.796 -2.277  1.00 29.54  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -3.977  -19.185 -3.306  1.00 30.68  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -4.585  -18.446 -0.306  1.00 26.78  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -5.564  -19.558 0.137   1.00 29.77  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -5.033  -20.461 1.249   1.00 29.93  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -6.174  -21.293 1.824   1.00 33.03  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -6.724  -22.216 0.819   1.00 34.22  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -3.653  -21.124 -2.187  1.00 27.35  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -4.152  -21.978 -3.247  1.00 31.77  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -5.145  -22.980 -2.677  1.00 33.73  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -4.984  -23.412 -1.544  1.00 30.62  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -2.962  -22.693 -3.881  1.00 35.18  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -2.274  -21.668 -4.757  1.00 39.59  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -1.423  -22.331 -6.168  1.00 46.84  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -2.457  -23.580 -6.935  1.00 59.75  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -6.121  -23.376 -3.506  1.00 41.91  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -7.191  -24.295 -3.135  1.00 40.74  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -6.597  -25.570 -2.553  1.00 40.66  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -5.670  -26.144 -3.130  1.00 37.23  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -8.020  -24.664 -4.367  1.00 48.96  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -9.178  -25.618 -4.114  1.00 50.88  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -9.514  -26.341 -5.412  1.00 58.28  ? 16  LYS   A CD  1 
ATOM   125  C CE  . LYS   A 1 17 ? -10.698 -27.241 -5.382  1.00 65.42  ? 16  LYS   A CE  1 
ATOM   126  N NZ  . LYS   A 1 17 ? -11.166 -27.379 -6.767  1.00 66.22  ? 16  LYS   A NZ  1 
ATOM   127  N N   . GLY   A 1 18 ? -7.112  -25.967 -1.379  1.00 35.19  ? 17  GLY   A N   1 
ATOM   128  C CA  . GLY   A 1 18 ? -6.715  -27.222 -0.770  1.00 39.26  ? 17  GLY   A CA  1 
ATOM   129  C C   . GLY   A 1 18 ? -5.338  -27.151 -0.119  1.00 44.82  ? 17  GLY   A C   1 
ATOM   130  O O   . GLY   A 1 18 ? -4.795  -28.177 0.279   1.00 47.52  ? 17  GLY   A O   1 
ATOM   131  N N   . TYR   A 1 19 ? -4.774  -25.940 -0.002  1.00 36.97  ? 18  TYR   A N   1 
ATOM   132  C CA  . TYR   A 1 19 ? -3.508  -25.805 0.684   1.00 35.67  ? 18  TYR   A CA  1 
ATOM   133  C C   . TYR   A 1 19 ? -3.620  -24.680 1.696   1.00 29.97  ? 18  TYR   A C   1 
ATOM   134  O O   . TYR   A 1 19 ? -4.334  -23.721 1.442   1.00 30.22  ? 18  TYR   A O   1 
ATOM   135  C CB  . TYR   A 1 19 ? -2.455  -25.341 -0.325  1.00 42.30  ? 18  TYR   A CB  1 
ATOM   136  C CG  . TYR   A 1 19 ? -1.867  -26.383 -1.263  1.00 40.64  ? 18  TYR   A CG  1 
ATOM   137  C CD1 . TYR   A 1 19 ? -0.714  -27.074 -0.916  1.00 48.25  ? 18  TYR   A CD1 1 
ATOM   138  C CD2 . TYR   A 1 19 ? -2.414  -26.623 -2.521  1.00 50.96  ? 18  TYR   A CD2 1 
ATOM   139  C CE1 . TYR   A 1 19 ? -0.142  -28.001 -1.775  1.00 51.07  ? 18  TYR   A CE1 1 
ATOM   140  C CE2 . TYR   A 1 19 ? -1.845  -27.540 -3.399  1.00 51.29  ? 18  TYR   A CE2 1 
ATOM   141  C CZ  . TYR   A 1 19 ? -0.705  -28.236 -3.019  1.00 54.79  ? 18  TYR   A CZ  1 
ATOM   142  O OH  . TYR   A 1 19 ? -0.112  -29.153 -3.854  1.00 62.21  ? 18  TYR   A OH  1 
ATOM   143  N N   . PRO   A 1 20 ? -2.876  -24.719 2.822   1.00 28.53  ? 19  PRO   A N   1 
ATOM   144  C CA  . PRO   A 1 20 ? -2.857  -23.598 3.766   1.00 31.61  ? 19  PRO   A CA  1 
ATOM   145  C C   . PRO   A 1 20 ? -2.133  -22.429 3.097   1.00 33.51  ? 19  PRO   A C   1 
ATOM   146  O O   . PRO   A 1 20 ? -1.330  -22.667 2.215   1.00 32.51  ? 19  PRO   A O   1 
ATOM   147  C CB  . PRO   A 1 20 ? -2.082  -24.115 4.969   1.00 33.96  ? 19  PRO   A CB  1 
ATOM   148  C CG  . PRO   A 1 20 ? -1.212  -25.231 4.377   1.00 33.53  ? 19  PRO   A CG  1 
ATOM   149  C CD  . PRO   A 1 20 ? -1.967  -25.817 3.208   1.00 33.45  ? 19  PRO   A CD  1 
ATOM   150  N N   . HIS   A 1 21 ? -2.421  -21.202 3.554   1.00 29.41  ? 20  HIS   A N   1 
ATOM   151  C CA  . HIS   A 1 21 ? -1.690  -19.997 3.197   1.00 29.52  ? 20  HIS   A CA  1 
ATOM   152  C C   . HIS   A 1 21 ? -0.196  -20.266 3.331   1.00 30.07  ? 20  HIS   A C   1 
ATOM   153  O O   . HIS   A 1 21 ? 0.302   -20.610 4.415   1.00 28.01  ? 20  HIS   A O   1 
ATOM   154  C CB  . HIS   A 1 21 ? -2.139  -18.829 4.079   1.00 31.41  ? 20  HIS   A CB  1 
ATOM   155  C CG  . HIS   A 1 21 ? -3.588  -18.493 3.922   1.00 29.37  ? 20  HIS   A CG  1 
ATOM   156  N ND1 . HIS   A 1 21 ? -4.583  -19.111 4.656   1.00 30.60  ? 20  HIS   A ND1 1 
ATOM   157  C CD2 . HIS   A 1 21 ? -4.201  -17.578 3.136   1.00 29.00  ? 20  HIS   A CD2 1 
ATOM   158  C CE1 . HIS   A 1 21 ? -5.757  -18.584 4.316   1.00 31.20  ? 20  HIS   A CE1 1 
ATOM   159  N NE2 . HIS   A 1 21 ? -5.546  -17.651 3.390   1.00 33.58  ? 20  HIS   A NE2 1 
ATOM   160  N N   . TRP   A 1 22 ? 0.522   -20.085 2.218   1.00 28.25  ? 21  TRP   A N   1 
ATOM   161  C CA  . TRP   A 1 22 ? 1.857   -20.664 2.097   1.00 25.81  ? 21  TRP   A CA  1 
ATOM   162  C C   . TRP   A 1 22 ? 2.921   -19.574 1.938   1.00 23.83  ? 21  TRP   A C   1 
ATOM   163  O O   . TRP   A 1 22 ? 2.811   -18.725 1.083   1.00 21.51  ? 21  TRP   A O   1 
ATOM   164  C CB  . TRP   A 1 22 ? 1.905   -21.592 0.878   1.00 28.29  ? 21  TRP   A CB  1 
ATOM   165  C CG  . TRP   A 1 22 ? 2.993   -22.638 0.927   1.00 29.13  ? 21  TRP   A CG  1 
ATOM   166  C CD1 . TRP   A 1 22 ? 4.327   -22.481 0.651   1.00 31.69  ? 21  TRP   A CD1 1 
ATOM   167  C CD2 . TRP   A 1 22 ? 2.807   -24.027 1.245   1.00 29.33  ? 21  TRP   A CD2 1 
ATOM   168  N NE1 . TRP   A 1 22 ? 4.985   -23.678 0.786   1.00 27.42  ? 21  TRP   A NE1 1 
ATOM   169  C CE2 . TRP   A 1 22 ? 4.072   -24.650 1.135   1.00 32.38  ? 21  TRP   A CE2 1 
ATOM   170  C CE3 . TRP   A 1 22 ? 1.692   -24.812 1.583   1.00 37.61  ? 21  TRP   A CE3 1 
ATOM   171  C CZ2 . TRP   A 1 22 ? 4.256   -26.014 1.397   1.00 32.68  ? 21  TRP   A CZ2 1 
ATOM   172  C CZ3 . TRP   A 1 22 ? 1.871   -26.167 1.810   1.00 38.41  ? 21  TRP   A CZ3 1 
ATOM   173  C CH2 . TRP   A 1 22 ? 3.141   -26.760 1.718   1.00 40.15  ? 21  TRP   A CH2 1 
ATOM   174  N N   . PRO   A 1 23 ? 4.079   -19.657 2.623   1.00 21.90  ? 22  PRO   A N   1 
ATOM   175  C CA  . PRO   A 1 23 ? 5.118   -18.630 2.436   1.00 22.73  ? 22  PRO   A CA  1 
ATOM   176  C C   . PRO   A 1 23 ? 5.627   -18.622 0.980   1.00 22.32  ? 22  PRO   A C   1 
ATOM   177  O O   . PRO   A 1 23 ? 5.979   -19.669 0.396   1.00 23.96  ? 22  PRO   A O   1 
ATOM   178  C CB  . PRO   A 1 23 ? 6.192   -19.086 3.465   1.00 24.09  ? 22  PRO   A CB  1 
ATOM   179  C CG  . PRO   A 1 23 ? 6.024   -20.619 3.585   1.00 21.36  ? 22  PRO   A CG  1 
ATOM   180  C CD  . PRO   A 1 23 ? 4.481   -20.757 3.508   1.00 23.47  ? 22  PRO   A CD  1 
ATOM   181  N N   . ALA   A 1 24 ? 5.694   -17.420 0.392   1.00 22.92  ? 23  ALA   A N   1 
ATOM   182  C CA  . ALA   A 1 24 ? 6.003   -17.274 -1.022  1.00 22.43  ? 23  ALA   A CA  1 
ATOM   183  C C   . ALA   A 1 24 ? 6.566   -15.887 -1.309  1.00 21.82  ? 23  ALA   A C   1 
ATOM   184  O O   . ALA   A 1 24 ? 6.589   -15.012 -0.442  1.00 22.40  ? 23  ALA   A O   1 
ATOM   185  C CB  . ALA   A 1 24 ? 4.771   -17.571 -1.864  1.00 21.27  ? 23  ALA   A CB  1 
ATOM   186  N N   . ARG   A 1 25 ? 7.067   -15.705 -2.538  1.00 23.60  ? 24  ARG   A N   1 
ATOM   187  C CA  . ARG   A 1 25 ? 7.449   -14.370 -2.968  1.00 22.44  ? 24  ARG   A CA  1 
ATOM   188  C C   . ARG   A 1 25 ? 6.900   -14.137 -4.375  1.00 23.57  ? 24  ARG   A C   1 
ATOM   189  O O   . ARG   A 1 25 ? 6.578   -15.102 -5.079  1.00 22.53  ? 24  ARG   A O   1 
ATOM   190  C CB  . ARG   A 1 25 ? 8.967   -14.240 -2.954  1.00 21.96  ? 24  ARG   A CB  1 
ATOM   191  C CG  . ARG   A 1 25 ? 9.694   -15.130 -3.959  1.00 21.12  ? 24  ARG   A CG  1 
ATOM   192  C CD  . ARG   A 1 25 ? 11.227  -14.924 -3.884  1.00 23.77  ? 24  ARG   A CD  1 
ATOM   193  N NE  . ARG   A 1 25 ? 11.935  -15.732 -4.893  1.00 22.98  ? 24  ARG   A NE  1 
ATOM   194  C CZ  . ARG   A 1 25 ? 13.179  -16.194 -4.750  1.00 24.70  ? 24  ARG   A CZ  1 
ATOM   195  N NH1 . ARG   A 1 25 ? 13.864  -16.006 -3.617  1.00 21.50  ? 24  ARG   A NH1 1 
ATOM   196  N NH2 . ARG   A 1 25 ? 13.718  -16.890 -5.737  1.00 24.79  ? 24  ARG   A NH2 1 
ATOM   197  N N   . ILE   A 1 26 ? 6.794   -12.861 -4.759  1.00 23.83  ? 25  ILE   A N   1 
ATOM   198  C CA  . ILE   A 1 26 ? 6.560   -12.480 -6.145  1.00 25.47  ? 25  ILE   A CA  1 
ATOM   199  C C   . ILE   A 1 26 ? 7.896   -12.637 -6.857  1.00 27.61  ? 25  ILE   A C   1 
ATOM   200  O O   . ILE   A 1 26 ? 8.872   -12.030 -6.421  1.00 26.72  ? 25  ILE   A O   1 
ATOM   201  C CB  . ILE   A 1 26 ? 6.082   -11.015 -6.254  1.00 28.21  ? 25  ILE   A CB  1 
ATOM   202  C CG1 . ILE   A 1 26 ? 4.961   -10.683 -5.274  1.00 30.78  ? 25  ILE   A CG1 1 
ATOM   203  C CG2 . ILE   A 1 26 ? 5.717   -10.626 -7.707  1.00 25.45  ? 25  ILE   A CG2 1 
ATOM   204  C CD1 . ILE   A 1 26 ? 3.617   -11.222 -5.677  1.00 33.49  ? 25  ILE   A CD1 1 
ATOM   205  N N   . ASP   A 1 27 ? 7.926   -13.429 -7.932  1.00 24.91  ? 26  ASP   A N   1 
ATOM   206  C CA  . ASP   A 1 27 ? 9.167   -13.605 -8.684  1.00 28.67  ? 26  ASP   A CA  1 
ATOM   207  C C   . ASP   A 1 27 ? 9.313   -12.577 -9.805  1.00 33.09  ? 26  ASP   A C   1 
ATOM   208  O O   . ASP   A 1 27 ? 8.351   -11.928 -10.243 1.00 27.52  ? 26  ASP   A O   1 
ATOM   209  C CB  . ASP   A 1 27 ? 9.332   -14.994 -9.287  1.00 27.46  ? 26  ASP   A CB  1 
ATOM   210  C CG  . ASP   A 1 27 ? 10.287  -15.931 -8.575  1.00 32.13  ? 26  ASP   A CG  1 
ATOM   211  O OD1 . ASP   A 1 27 ? 10.890  -15.519 -7.573  1.00 34.26  ? 26  ASP   A OD1 1 
ATOM   212  O OD2 . ASP   A 1 27 ? 10.417  -17.058 -9.024  1.00 30.85  ? 26  ASP   A OD2 1 
ATOM   213  N N   . ASP   A 1 28 ? 10.580  -12.400 -10.228 1.00 33.19  ? 27  ASP   A N   1 
ATOM   214  C CA  . ASP   A 1 28 ? 10.873  -11.790 -11.510 1.00 34.27  ? 27  ASP   A CA  1 
ATOM   215  C C   . ASP   A 1 28 ? 10.488  -12.768 -12.620 1.00 34.08  ? 27  ASP   A C   1 
ATOM   216  O O   . ASP   A 1 28 ? 10.320  -13.964 -12.393 1.00 34.05  ? 27  ASP   A O   1 
ATOM   217  C CB  . ASP   A 1 28 ? 12.354  -11.444 -11.625 1.00 40.81  ? 27  ASP   A CB  1 
ATOM   218  C CG  . ASP   A 1 28 ? 12.789  -10.190 -10.875 1.00 47.46  ? 27  ASP   A CG  1 
ATOM   219  O OD1 . ASP   A 1 28 ? 12.387  -9.082  -11.312 1.00 47.51  ? 27  ASP   A OD1 1 
ATOM   220  O OD2 . ASP   A 1 28 ? 13.498  -10.330 -9.837  1.00 52.56  ? 27  ASP   A OD2 1 
ATOM   221  N N   . ILE   A 1 29 ? 10.319  -12.238 -13.828 1.00 33.13  ? 28  ILE   A N   1 
ATOM   222  C CA  . ILE   A 1 29 ? 10.267  -13.101 -14.998 1.00 38.97  ? 28  ILE   A CA  1 
ATOM   223  C C   . ILE   A 1 29 ? 11.605  -12.906 -15.705 1.00 36.70  ? 28  ILE   A C   1 
ATOM   224  O O   . ILE   A 1 29 ? 11.967  -11.765 -15.984 1.00 36.28  ? 28  ILE   A O   1 
ATOM   225  C CB  . ILE   A 1 29 ? 9.102   -12.675 -15.902 1.00 37.95  ? 28  ILE   A CB  1 
ATOM   226  C CG1 . ILE   A 1 29 ? 7.775   -12.712 -15.141 1.00 40.46  ? 28  ILE   A CG1 1 
ATOM   227  C CG2 . ILE   A 1 29 ? 9.062   -13.523 -17.177 1.00 36.24  ? 28  ILE   A CG2 1 
ATOM   228  C CD1 . ILE   A 1 29 ? 6.728   -11.741 -15.663 1.00 37.34  ? 28  ILE   A CD1 1 
ATOM   229  N N   . ALA   A 1 30 ? 12.346  -14.000 -15.908 1.00 41.78  ? 29  ALA   A N   1 
ATOM   230  C CA  . ALA   A 1 30 ? 13.634  -13.947 -16.600 1.00 38.75  ? 29  ALA   A CA  1 
ATOM   231  C C   . ALA   A 1 30 ? 13.419  -13.595 -18.076 1.00 39.32  ? 29  ALA   A C   1 
ATOM   232  O O   . ALA   A 1 30 ? 12.400  -13.948 -18.675 1.00 38.02  ? 29  ALA   A O   1 
ATOM   233  C CB  . ALA   A 1 30 ? 14.363  -15.264 -16.455 1.00 38.37  ? 29  ALA   A CB  1 
ATOM   234  N N   . ASP   A 1 31 ? 14.398  -12.888 -18.651 1.00 40.61  ? 30  ASP   A N   1 
ATOM   235  C CA  . ASP   A 1 31 ? 14.471  -12.708 -20.093 1.00 40.12  ? 30  ASP   A CA  1 
ATOM   236  C C   . ASP   A 1 31 ? 14.274  -14.056 -20.756 1.00 31.63  ? 30  ASP   A C   1 
ATOM   237  O O   . ASP   A 1 31 ? 14.887  -15.032 -20.363 1.00 37.19  ? 30  ASP   A O   1 
ATOM   238  C CB  . ASP   A 1 31 ? 15.809  -12.127 -20.516 1.00 37.62  ? 30  ASP   A CB  1 
ATOM   239  C CG  . ASP   A 1 31 ? 15.949  -10.636 -20.276 1.00 41.09  ? 30  ASP   A CG  1 
ATOM   240  O OD1 . ASP   A 1 31 ? 14.918  -9.975  -20.080 1.00 41.88  ? 30  ASP   A OD1 1 
ATOM   241  O OD2 . ASP   A 1 31 ? 17.103  -10.164 -20.258 1.00 49.85  ? 30  ASP   A OD2 1 
ATOM   242  N N   . GLY   A 1 32 ? 13.333  -14.096 -21.688 1.00 37.31  ? 31  GLY   A N   1 
ATOM   243  C CA  . GLY   A 1 32 ? 13.097  -15.256 -22.525 1.00 38.11  ? 31  GLY   A CA  1 
ATOM   244  C C   . GLY   A 1 32 ? 12.174  -16.281 -21.884 1.00 43.21  ? 31  GLY   A C   1 
ATOM   245  O O   . GLY   A 1 32 ? 11.902  -17.310 -22.490 1.00 41.59  ? 31  GLY   A O   1 
ATOM   246  N N   . ALA   A 1 33 ? 11.750  -16.020 -20.642 1.00 37.18  ? 32  ALA   A N   1 
ATOM   247  C CA  . ALA   A 1 33 ? 10.954  -16.988 -19.912 1.00 38.99  ? 32  ALA   A CA  1 
ATOM   248  C C   . ALA   A 1 33 ? 9.465   -16.690 -20.119 1.00 37.79  ? 32  ALA   A C   1 
ATOM   249  O O   . ALA   A 1 33 ? 9.078   -15.572 -20.490 1.00 37.20  ? 32  ALA   A O   1 
ATOM   250  C CB  . ALA   A 1 33 ? 11.369  -16.972 -18.437 1.00 38.85  ? 32  ALA   A CB  1 
ATOM   251  N N   . VAL   A 1 34 ? 8.637   -17.717 -19.879 1.00 40.01  ? 33  VAL   A N   1 
ATOM   252  C CA  . VAL   A 1 34 ? 7.179   -17.676 -19.991 1.00 40.13  ? 33  VAL   A CA  1 
ATOM   253  C C   . VAL   A 1 34 ? 6.581   -16.608 -19.064 1.00 37.69  ? 33  VAL   A C   1 
ATOM   254  O O   . VAL   A 1 34 ? 6.862   -16.588 -17.869 1.00 37.85  ? 33  VAL   A O   1 
ATOM   255  C CB  . VAL   A 1 34 ? 6.606   -19.075 -19.659 1.00 44.74  ? 33  VAL   A CB  1 
ATOM   256  C CG1 . VAL   A 1 34 ? 5.083   -19.095 -19.718 1.00 50.25  ? 33  VAL   A CG1 1 
ATOM   257  C CG2 . VAL   A 1 34 ? 7.178   -20.164 -20.565 1.00 43.08  ? 33  VAL   A CG2 1 
ATOM   258  N N   . LYS   A 1 35 ? 5.734   -15.743 -19.629 1.00 36.02  ? 34  LYS   A N   1 
ATOM   259  C CA  . LYS   A 1 35 ? 5.109   -14.642 -18.912 1.00 38.55  ? 34  LYS   A CA  1 
ATOM   260  C C   . LYS   A 1 35 ? 3.821   -15.140 -18.268 1.00 40.36  ? 34  LYS   A C   1 
ATOM   261  O O   . LYS   A 1 35 ? 3.233   -16.092 -18.751 1.00 37.92  ? 34  LYS   A O   1 
ATOM   262  C CB  . LYS   A 1 35 ? 4.754   -13.466 -19.829 1.00 39.27  ? 34  LYS   A CB  1 
ATOM   263  C CG  . LYS   A 1 35 ? 5.957   -12.640 -20.260 1.00 43.22  ? 34  LYS   A CG  1 
ATOM   264  C CD  . LYS   A 1 35 ? 5.649   -11.450 -21.163 1.00 50.36  ? 34  LYS   A CD  1 
ATOM   265  C CE  . LYS   A 1 35 ? 5.235   -11.847 -22.552 1.00 48.49  ? 34  LYS   A CE  1 
ATOM   266  N NZ  . LYS   A 1 35 ? 4.832   -10.677 -23.333 1.00 48.27  ? 34  LYS   A NZ  1 
ATOM   267  N N   . PRO   A 1 36 ? 3.327   -14.527 -17.171 1.00 43.05  ? 35  PRO   A N   1 
ATOM   268  C CA  . PRO   A 1 36 ? 2.072   -14.982 -16.557 1.00 42.16  ? 35  PRO   A CA  1 
ATOM   269  C C   . PRO   A 1 36 ? 0.894   -14.422 -17.357 1.00 39.31  ? 35  PRO   A C   1 
ATOM   270  O O   . PRO   A 1 36 ? 1.052   -13.448 -18.094 1.00 38.00  ? 35  PRO   A O   1 
ATOM   271  C CB  . PRO   A 1 36 ? 2.136   -14.430 -15.118 1.00 39.70  ? 35  PRO   A CB  1 
ATOM   272  C CG  . PRO   A 1 36 ? 3.135   -13.276 -15.167 1.00 46.17  ? 35  PRO   A CG  1 
ATOM   273  C CD  . PRO   A 1 36 ? 3.921   -13.378 -16.476 1.00 44.13  ? 35  PRO   A CD  1 
ATOM   274  N N   . PRO   A 1 37 ? -0.332  -14.982 -17.217 1.00 39.88  ? 36  PRO   A N   1 
ATOM   275  C CA  . PRO   A 1 37 ? -1.506  -14.419 -17.889 1.00 39.22  ? 36  PRO   A CA  1 
ATOM   276  C C   . PRO   A 1 37 ? -1.661  -12.991 -17.398 1.00 42.62  ? 36  PRO   A C   1 
ATOM   277  O O   . PRO   A 1 37 ? -1.113  -12.666 -16.341 1.00 37.15  ? 36  PRO   A O   1 
ATOM   278  C CB  . PRO   A 1 37 ? -2.697  -15.292 -17.437 1.00 37.23  ? 36  PRO   A CB  1 
ATOM   279  C CG  . PRO   A 1 37 ? -2.069  -16.532 -16.820 1.00 40.77  ? 36  PRO   A CG  1 
ATOM   280  C CD  . PRO   A 1 37 ? -0.648  -16.170 -16.403 1.00 38.61  ? 36  PRO   A CD  1 
ATOM   281  N N   . PRO   A 1 38 ? -2.436  -12.121 -18.101 1.00 45.01  ? 37  PRO   A N   1 
ATOM   282  C CA  . PRO   A 1 38 ? -2.702  -10.760 -17.624 1.00 47.18  ? 37  PRO   A CA  1 
ATOM   283  C C   . PRO   A 1 38 ? -3.246  -10.767 -16.200 1.00 38.02  ? 37  PRO   A C   1 
ATOM   284  O O   . PRO   A 1 38 ? -3.983  -11.668 -15.820 1.00 39.52  ? 37  PRO   A O   1 
ATOM   285  C CB  . PRO   A 1 38 ? -3.753  -10.196 -18.620 1.00 44.61  ? 37  PRO   A CB  1 
ATOM   286  C CG  . PRO   A 1 38 ? -4.312  -11.415 -19.303 1.00 43.67  ? 37  PRO   A CG  1 
ATOM   287  C CD  . PRO   A 1 38 ? -3.152  -12.410 -19.361 1.00 51.50  ? 37  PRO   A CD  1 
ATOM   288  N N   . ASN   A 1 39 ? -2.829  -9.779  -15.413 1.00 41.52  ? 38  ASN   A N   1 
ATOM   289  C CA  . ASN   A 1 39 ? -3.341  -9.573  -14.068 1.00 39.14  ? 38  ASN   A CA  1 
ATOM   290  C C   . ASN   A 1 39 ? -2.854  -10.661 -13.106 1.00 31.97  ? 38  ASN   A C   1 
ATOM   291  O O   . ASN   A 1 39 ? -3.260  -10.657 -11.942 1.00 31.44  ? 38  ASN   A O   1 
ATOM   292  C CB  . ASN   A 1 39 ? -4.863  -9.464  -14.064 1.00 48.91  ? 38  ASN   A CB  1 
ATOM   293  C CG  . ASN   A 1 39 ? -5.336  -8.298  -14.903 1.00 53.26  ? 38  ASN   A CG  1 
ATOM   294  O OD1 . ASN   A 1 39 ? -5.174  -7.142  -14.500 1.00 53.64  ? 38  ASN   A OD1 1 
ATOM   295  N ND2 . ASN   A 1 39 ? -5.919  -8.577  -16.055 1.00 53.48  ? 38  ASN   A ND2 1 
ATOM   296  N N   . LYS   A 1 40 ? -2.037  -11.614 -13.574 1.00 30.22  ? 39  LYS   A N   1 
ATOM   297  C CA  . LYS   A 1 40 ? -1.477  -12.591 -12.633 1.00 25.36  ? 39  LYS   A CA  1 
ATOM   298  C C   . LYS   A 1 40 ? -0.001  -12.299 -12.383 1.00 30.76  ? 39  LYS   A C   1 
ATOM   299  O O   . LYS   A 1 40 ? 0.654   -11.609 -13.186 1.00 30.53  ? 39  LYS   A O   1 
ATOM   300  C CB  . LYS   A 1 40 ? -1.669  -14.048 -13.071 1.00 28.53  ? 39  LYS   A CB  1 
ATOM   301  C CG  . LYS   A 1 40 ? -3.104  -14.479 -13.349 1.00 33.35  ? 39  LYS   A CG  1 
ATOM   302  C CD  . LYS   A 1 40 ? -4.035  -14.131 -12.190 1.00 39.50  ? 39  LYS   A CD  1 
ATOM   303  C CE  . LYS   A 1 40 ? -5.502  -14.409 -12.445 1.00 43.24  ? 39  LYS   A CE  1 
ATOM   304  N NZ  . LYS   A 1 40 ? -5.727  -15.857 -12.532 1.00 46.67  ? 39  LYS   A NZ  1 
ATOM   305  N N   . TYR   A 1 41 ? 0.512   -12.856 -11.273 1.00 26.15  ? 40  TYR   A N   1 
ATOM   306  C CA  . TYR   A 1 41 ? 1.909   -12.709 -10.909 1.00 26.72  ? 40  TYR   A CA  1 
ATOM   307  C C   . TYR   A 1 41 ? 2.541   -14.085 -10.774 1.00 25.82  ? 40  TYR   A C   1 
ATOM   308  O O   . TYR   A 1 41 ? 1.889   -15.039 -10.322 1.00 26.55  ? 40  TYR   A O   1 
ATOM   309  C CB  . TYR   A 1 41 ? 2.046   -12.068 -9.523  1.00 23.50  ? 40  TYR   A CB  1 
ATOM   310  C CG  . TYR   A 1 41 ? 1.557   -10.634 -9.512  1.00 28.13  ? 40  TYR   A CG  1 
ATOM   311  C CD1 . TYR   A 1 41 ? 0.199   -10.354 -9.383  1.00 36.70  ? 40  TYR   A CD1 1 
ATOM   312  C CD2 . TYR   A 1 41 ? 2.439   -9.572  -9.619  1.00 32.48  ? 40  TYR   A CD2 1 
ATOM   313  C CE1 . TYR   A 1 41 ? -0.259  -9.052  -9.428  1.00 38.02  ? 40  TYR   A CE1 1 
ATOM   314  C CE2 . TYR   A 1 41 ? 1.997   -8.262  -9.647  1.00 35.02  ? 40  TYR   A CE2 1 
ATOM   315  C CZ  . TYR   A 1 41 ? 0.644   -8.013  -9.520  1.00 36.47  ? 40  TYR   A CZ  1 
ATOM   316  O OH  . TYR   A 1 41 ? 0.187   -6.743  -9.593  1.00 39.93  ? 40  TYR   A OH  1 
ATOM   317  N N   . PRO   A 1 42 ? 3.851   -14.217 -11.088 1.00 25.74  ? 41  PRO   A N   1 
ATOM   318  C CA  . PRO   A 1 42 ? 4.557   -15.475 -10.860 1.00 25.66  ? 41  PRO   A CA  1 
ATOM   319  C C   . PRO   A 1 42 ? 4.878   -15.589 -9.373  1.00 25.19  ? 41  PRO   A C   1 
ATOM   320  O O   . PRO   A 1 42 ? 5.568   -14.724 -8.827  1.00 26.05  ? 41  PRO   A O   1 
ATOM   321  C CB  . PRO   A 1 42 ? 5.825   -15.372 -11.704 1.00 23.25  ? 41  PRO   A CB  1 
ATOM   322  C CG  . PRO   A 1 42 ? 6.008   -13.915 -11.961 1.00 24.94  ? 41  PRO   A CG  1 
ATOM   323  C CD  . PRO   A 1 42 ? 4.725   -13.150 -11.609 1.00 28.97  ? 41  PRO   A CD  1 
ATOM   324  N N   . ILE   A 1 43 ? 4.334   -16.621 -8.724  1.00 25.52  ? 42  ILE   A N   1 
ATOM   325  C CA  . ILE   A 1 43 ? 4.535   -16.800 -7.292  1.00 22.94  ? 42  ILE   A CA  1 
ATOM   326  C C   . ILE   A 1 43 ? 5.495   -17.975 -7.096  1.00 27.01  ? 42  ILE   A C   1 
ATOM   327  O O   . ILE   A 1 43 ? 5.220   -19.071 -7.590  1.00 26.10  ? 42  ILE   A O   1 
ATOM   328  C CB  . ILE   A 1 43 ? 3.198   -17.079 -6.575  1.00 24.53  ? 42  ILE   A CB  1 
ATOM   329  C CG1 . ILE   A 1 43 ? 2.145   -15.984 -6.915  1.00 22.57  ? 42  ILE   A CG1 1 
ATOM   330  C CG2 . ILE   A 1 43 ? 3.433   -17.239 -5.063  1.00 20.05  ? 42  ILE   A CG2 1 
ATOM   331  C CD1 . ILE   A 1 43 ? 2.571   -14.534 -6.622  1.00 21.46  ? 42  ILE   A CD1 1 
ATOM   332  N N   . PHE   A 1 44 ? 6.602   -17.725 -6.376  1.00 20.88  ? 43  PHE   A N   1 
ATOM   333  C CA  . PHE   A 1 44 ? 7.512   -18.784 -5.986  1.00 22.96  ? 43  PHE   A CA  1 
ATOM   334  C C   . PHE   A 1 44 ? 7.219   -19.181 -4.544  1.00 24.49  ? 43  PHE   A C   1 
ATOM   335  O O   . PHE   A 1 44 ? 7.335   -18.354 -3.627  1.00 26.32  ? 43  PHE   A O   1 
ATOM   336  C CB  . PHE   A 1 44 ? 8.938   -18.231 -6.126  1.00 23.57  ? 43  PHE   A CB  1 
ATOM   337  C CG  . PHE   A 1 44 ? 9.954   -19.274 -5.711  1.00 25.62  ? 43  PHE   A CG  1 
ATOM   338  C CD1 . PHE   A 1 44 ? 10.303  -20.306 -6.599  1.00 25.34  ? 43  PHE   A CD1 1 
ATOM   339  C CD2 . PHE   A 1 44 ? 10.533  -19.242 -4.437  1.00 27.80  ? 43  PHE   A CD2 1 
ATOM   340  C CE1 . PHE   A 1 44 ? 11.265  -21.250 -6.243  1.00 25.98  ? 43  PHE   A CE1 1 
ATOM   341  C CE2 . PHE   A 1 44 ? 11.483  -20.209 -4.078  1.00 32.03  ? 43  PHE   A CE2 1 
ATOM   342  C CZ  . PHE   A 1 44 ? 11.846  -21.208 -4.982  1.00 27.80  ? 43  PHE   A CZ  1 
ATOM   343  N N   . PHE   A 1 45 ? 6.854   -20.460 -4.352  1.00 24.72  ? 44  PHE   A N   1 
ATOM   344  C CA  . PHE   A 1 45 ? 6.484   -20.963 -3.039  1.00 22.80  ? 44  PHE   A CA  1 
ATOM   345  C C   . PHE   A 1 45 ? 7.750   -21.490 -2.376  1.00 26.54  ? 44  PHE   A C   1 
ATOM   346  O O   . PHE   A 1 45 ? 8.441   -22.365 -2.931  1.00 23.36  ? 44  PHE   A O   1 
ATOM   347  C CB  . PHE   A 1 45 ? 5.486   -22.126 -3.207  1.00 26.54  ? 44  PHE   A CB  1 
ATOM   348  C CG  . PHE   A 1 45 ? 4.139   -21.623 -3.700  1.00 25.22  ? 44  PHE   A CG  1 
ATOM   349  C CD1 . PHE   A 1 45 ? 3.896   -21.457 -5.053  1.00 26.39  ? 44  PHE   A CD1 1 
ATOM   350  C CD2 . PHE   A 1 45 ? 3.126   -21.304 -2.797  1.00 25.56  ? 44  PHE   A CD2 1 
ATOM   351  C CE1 . PHE   A 1 45 ? 2.666   -20.997 -5.496  1.00 26.17  ? 44  PHE   A CE1 1 
ATOM   352  C CE2 . PHE   A 1 45 ? 1.913   -20.814 -3.243  1.00 23.72  ? 44  PHE   A CE2 1 
ATOM   353  C CZ  . PHE   A 1 45 ? 1.679   -20.678 -4.579  1.00 26.43  ? 44  PHE   A CZ  1 
ATOM   354  N N   . PHE   A 1 46 ? 8.057   -20.929 -1.204  1.00 23.75  ? 45  PHE   A N   1 
ATOM   355  C CA  . PHE   A 1 46 ? 9.213   -21.420 -0.469  1.00 28.28  ? 45  PHE   A CA  1 
ATOM   356  C C   . PHE   A 1 46 ? 8.996   -22.878 -0.048  1.00 28.82  ? 45  PHE   A C   1 
ATOM   357  O O   . PHE   A 1 46 ? 7.852   -23.336 0.114   1.00 24.05  ? 45  PHE   A O   1 
ATOM   358  C CB  . PHE   A 1 46 ? 9.419   -20.465 0.716   1.00 24.03  ? 45  PHE   A CB  1 
ATOM   359  C CG  . PHE   A 1 46 ? 9.877   -19.061 0.326   1.00 24.91  ? 45  PHE   A CG  1 
ATOM   360  C CD1 . PHE   A 1 46 ? 11.137  -18.850 -0.228  1.00 23.56  ? 45  PHE   A CD1 1 
ATOM   361  C CD2 . PHE   A 1 46 ? 9.063   -17.943 0.544   1.00 23.89  ? 45  PHE   A CD2 1 
ATOM   362  C CE1 . PHE   A 1 46 ? 11.548  -17.575 -0.579  1.00 20.31  ? 45  PHE   A CE1 1 
ATOM   363  C CE2 . PHE   A 1 46 ? 9.505   -16.650 0.219   1.00 21.78  ? 45  PHE   A CE2 1 
ATOM   364  C CZ  . PHE   A 1 46 ? 10.753  -16.466 -0.302  1.00 21.52  ? 45  PHE   A CZ  1 
ATOM   365  N N   . GLY   A 1 47 ? 10.113  -23.585 0.150   1.00 27.25  ? 46  GLY   A N   1 
ATOM   366  C CA  . GLY   A 1 47 ? 10.078  -24.936 0.670   1.00 28.14  ? 46  GLY   A CA  1 
ATOM   367  C C   . GLY   A 1 47 ? 9.802   -25.922 -0.469  1.00 35.96  ? 46  GLY   A C   1 
ATOM   368  O O   . GLY   A 1 47 ? 10.647  -26.755 -0.771  1.00 33.72  ? 46  GLY   A O   1 
ATOM   369  N N   . THR   A 1 48 ? 8.647   -25.797 -1.142  1.00 34.11  ? 47  THR   A N   1 
ATOM   370  C CA  . THR   A 1 48 ? 8.383   -26.640 -2.307  1.00 35.47  ? 47  THR   A CA  1 
ATOM   371  C C   . THR   A 1 48 ? 9.217   -26.174 -3.497  1.00 36.62  ? 47  THR   A C   1 
ATOM   372  O O   . THR   A 1 48 ? 9.560   -26.976 -4.368  1.00 34.91  ? 47  THR   A O   1 
ATOM   373  C CB  . THR   A 1 48 ? 6.896   -26.688 -2.680  1.00 34.13  ? 47  THR   A CB  1 
ATOM   374  O OG1 . THR   A 1 48 ? 6.476   -25.373 -3.023  1.00 35.17  ? 47  THR   A OG1 1 
ATOM   375  C CG2 . THR   A 1 48 ? 5.996   -27.266 -1.604  1.00 30.01  ? 47  THR   A CG2 1 
ATOM   376  N N   . HIS   A 1 49 ? 9.479   -24.863 -3.565  1.00 31.23  ? 48  HIS   A N   1 
ATOM   377  C CA  . HIS   A 1 49 ? 10.149  -24.253 -4.702  1.00 31.73  ? 48  HIS   A CA  1 
ATOM   378  C C   . HIS   A 1 49 ? 9.327   -24.412 -5.981  1.00 34.13  ? 48  HIS   A C   1 
ATOM   379  O O   . HIS   A 1 49 ? 9.897   -24.370 -7.067  1.00 33.16  ? 48  HIS   A O   1 
ATOM   380  C CB  . HIS   A 1 49 ? 11.583  -24.788 -4.876  1.00 29.66  ? 48  HIS   A CB  1 
ATOM   381  C CG  . HIS   A 1 49 ? 12.352  -24.788 -3.600  1.00 35.92  ? 48  HIS   A CG  1 
ATOM   382  N ND1 . HIS   A 1 49 ? 13.288  -25.740 -3.269  1.00 34.21  ? 48  HIS   A ND1 1 
ATOM   383  C CD2 . HIS   A 1 49 ? 12.298  -23.937 -2.546  1.00 33.84  ? 48  HIS   A CD2 1 
ATOM   384  C CE1 . HIS   A 1 49 ? 13.753  -25.486 -2.054  1.00 37.67  ? 48  HIS   A CE1 1 
ATOM   385  N NE2 . HIS   A 1 49 ? 13.182  -24.394 -1.601  1.00 38.79  ? 48  HIS   A NE2 1 
ATOM   386  N N   . GLU   A 1 50 ? 7.997   -24.555 -5.878  1.00 31.94  ? 49  GLU   A N   1 
ATOM   387  C CA  . GLU   A 1 50 ? 7.191   -24.522 -7.100  1.00 34.39  ? 49  GLU   A CA  1 
ATOM   388  C C   . GLU   A 1 50 ? 6.747   -23.094 -7.448  1.00 33.48  ? 49  GLU   A C   1 
ATOM   389  O O   . GLU   A 1 50 ? 6.809   -22.187 -6.615  1.00 29.08  ? 49  GLU   A O   1 
ATOM   390  C CB  . GLU   A 1 50 ? 5.952   -25.387 -6.899  1.00 42.01  ? 49  GLU   A CB  1 
ATOM   391  C CG  . GLU   A 1 50 ? 6.284   -26.805 -6.455  1.00 46.62  ? 49  GLU   A CG  1 
ATOM   392  C CD  . GLU   A 1 50 ? 5.067   -27.591 -5.990  1.00 52.27  ? 49  GLU   A CD  1 
ATOM   393  O OE1 . GLU   A 1 50 ? 3.920   -27.117 -6.114  1.00 51.44  ? 49  GLU   A OE1 1 
ATOM   394  O OE2 . GLU   A 1 50 ? 5.291   -28.703 -5.479  1.00 59.95  ? 49  GLU   A OE2 1 
ATOM   395  N N   . THR   A 1 51 ? 6.277   -22.901 -8.688  1.00 27.81  ? 50  THR   A N   1 
ATOM   396  C CA  . THR   A 1 51 ? 5.729   -21.622 -9.121  1.00 27.81  ? 50  THR   A CA  1 
ATOM   397  C C   . THR   A 1 51 ? 4.283   -21.840 -9.548  1.00 29.13  ? 50  THR   A C   1 
ATOM   398  O O   . THR   A 1 51 ? 3.967   -22.828 -10.197 1.00 31.79  ? 50  THR   A O   1 
ATOM   399  C CB  . THR   A 1 51 ? 6.544   -21.068 -10.284 1.00 29.90  ? 50  THR   A CB  1 
ATOM   400  O OG1 . THR   A 1 51 ? 7.827   -20.744 -9.767  1.00 32.47  ? 50  THR   A OG1 1 
ATOM   401  C CG2 . THR   A 1 51 ? 5.994   -19.770 -10.881 1.00 33.11  ? 50  THR   A CG2 1 
ATOM   402  N N   . ALA   A 1 52 ? 3.401   -20.906 -9.189  1.00 28.28  ? 51  ALA   A N   1 
ATOM   403  C CA  . ALA   A 1 52 ? 2.085   -20.878 -9.792  1.00 27.24  ? 51  ALA   A CA  1 
ATOM   404  C C   . ALA   A 1 52 ? 1.782   -19.419 -10.100 1.00 31.68  ? 51  ALA   A C   1 
ATOM   405  O O   . ALA   A 1 52 ? 2.538   -18.538 -9.686  1.00 27.50  ? 51  ALA   A O   1 
ATOM   406  C CB  . ALA   A 1 52 ? 1.052   -21.524 -8.892  1.00 31.38  ? 51  ALA   A CB  1 
ATOM   407  N N   . PHE   A 1 53 ? 0.714   -19.178 -10.877 1.00 27.22  ? 52  PHE   A N   1 
ATOM   408  C CA  . PHE   A 1 53 ? 0.341   -17.817 -11.228 1.00 26.07  ? 52  PHE   A CA  1 
ATOM   409  C C   . PHE   A 1 53 ? -0.915  -17.462 -10.452 1.00 30.15  ? 52  PHE   A C   1 
ATOM   410  O O   . PHE   A 1 53 ? -1.850  -18.257 -10.414 1.00 32.26  ? 52  PHE   A O   1 
ATOM   411  C CB  . PHE   A 1 53 ? 0.034   -17.796 -12.728 1.00 30.35  ? 52  PHE   A CB  1 
ATOM   412  C CG  . PHE   A 1 53 ? 1.240   -18.126 -13.595 1.00 29.68  ? 52  PHE   A CG  1 
ATOM   413  C CD1 . PHE   A 1 53 ? 2.362   -17.302 -13.578 1.00 33.88  ? 52  PHE   A CD1 1 
ATOM   414  C CD2 . PHE   A 1 53 ? 1.228   -19.210 -14.470 1.00 34.39  ? 52  PHE   A CD2 1 
ATOM   415  C CE1 . PHE   A 1 53 ? 3.472   -17.578 -14.391 1.00 37.87  ? 52  PHE   A CE1 1 
ATOM   416  C CE2 . PHE   A 1 53 ? 2.335   -19.485 -15.278 1.00 36.66  ? 52  PHE   A CE2 1 
ATOM   417  C CZ  . PHE   A 1 53 ? 3.449   -18.660 -15.252 1.00 33.91  ? 52  PHE   A CZ  1 
ATOM   418  N N   . LEU   A 1 54 ? -0.894  -16.309 -9.770  1.00 26.24  ? 53  LEU   A N   1 
ATOM   419  C CA  . LEU   A 1 54 ? -1.965  -15.954 -8.853  1.00 25.39  ? 53  LEU   A CA  1 
ATOM   420  C C   . LEU   A 1 54 ? -2.249  -14.464 -8.979  1.00 28.60  ? 53  LEU   A C   1 
ATOM   421  O O   . LEU   A 1 54 ? -1.359  -13.656 -9.292  1.00 23.79  ? 53  LEU   A O   1 
ATOM   422  C CB  . LEU   A 1 54 ? -1.558  -16.275 -7.406  1.00 26.63  ? 53  LEU   A CB  1 
ATOM   423  C CG  . LEU   A 1 54 ? -1.578  -17.747 -6.983  1.00 30.10  ? 53  LEU   A CG  1 
ATOM   424  C CD1 . LEU   A 1 54 ? -1.222  -17.793 -5.487  1.00 29.18  ? 53  LEU   A CD1 1 
ATOM   425  C CD2 . LEU   A 1 54 ? -2.968  -18.328 -7.209  1.00 30.24  ? 53  LEU   A CD2 1 
ATOM   426  N N   . GLY   A 1 55 ? -3.514  -14.108 -8.726  1.00 23.76  ? 54  GLY   A N   1 
ATOM   427  C CA  . GLY   A 1 55 ? -3.854  -12.698 -8.664  1.00 25.65  ? 54  GLY   A CA  1 
ATOM   428  C C   . GLY   A 1 55 ? -3.808  -12.218 -7.208  1.00 25.38  ? 54  GLY   A C   1 
ATOM   429  O O   . GLY   A 1 55 ? -3.732  -13.031 -6.269  1.00 26.21  ? 54  GLY   A O   1 
ATOM   430  N N   . PRO   A 1 56 ? -3.863  -10.890 -7.000  1.00 25.74  ? 55  PRO   A N   1 
ATOM   431  C CA  . PRO   A 1 56 ? -3.860  -10.301 -5.649  1.00 24.66  ? 55  PRO   A CA  1 
ATOM   432  C C   . PRO   A 1 56 ? -4.842  -10.850 -4.610  1.00 25.87  ? 55  PRO   A C   1 
ATOM   433  O O   . PRO   A 1 56 ? -4.563  -10.815 -3.409  1.00 22.25  ? 55  PRO   A O   1 
ATOM   434  C CB  . PRO   A 1 56 ? -4.120  -8.830  -5.962  1.00 25.38  ? 55  PRO   A CB  1 
ATOM   435  C CG  . PRO   A 1 56 ? -3.454  -8.656  -7.307  1.00 26.36  ? 55  PRO   A CG  1 
ATOM   436  C CD  . PRO   A 1 56 ? -3.875  -9.888  -8.091  1.00 23.30  ? 55  PRO   A CD  1 
ATOM   437  N N   . LYS   A 1 57 ? -5.981  -11.411 -5.053  1.00 25.19  ? 56  LYS   A N   1 
ATOM   438  C CA  . LYS   A 1 57 ? -6.941  -11.909 -4.066  1.00 25.57  ? 56  LYS   A CA  1 
ATOM   439  C C   . LYS   A 1 57 ? -6.343  -13.034 -3.226  1.00 26.17  ? 56  LYS   A C   1 
ATOM   440  O O   . LYS   A 1 57 ? -6.799  -13.268 -2.103  1.00 26.50  ? 56  LYS   A O   1 
ATOM   441  C CB  . LYS   A 1 57 ? -8.263  -12.412 -4.673  1.00 28.76  ? 56  LYS   A CB  1 
ATOM   442  C CG  . LYS   A 1 57 ? -8.072  -13.588 -5.618  1.00 34.54  ? 56  LYS   A CG  1 
ATOM   443  C CD  . LYS   A 1 57 ? -9.361  -14.056 -6.298  1.00 38.81  ? 56  LYS   A CD  1 
ATOM   444  C CE  . LYS   A 1 57 ? -9.203  -15.245 -7.204  1.00 44.88  ? 56  LYS   A CE  1 
ATOM   445  N NZ  . LYS   A 1 57 ? -8.895  -16.473 -6.452  1.00 46.42  ? 56  LYS   A NZ  1 
ATOM   446  N N   . ASP   A 1 58 ? -5.326  -13.733 -3.769  1.00 25.29  ? 57  ASP   A N   1 
ATOM   447  C CA  . ASP   A 1 58 ? -4.745  -14.872 -3.098  1.00 24.85  ? 57  ASP   A CA  1 
ATOM   448  C C   . ASP   A 1 58 ? -3.396  -14.552 -2.447  1.00 25.68  ? 57  ASP   A C   1 
ATOM   449  O O   . ASP   A 1 58 ? -2.680  -15.490 -2.069  1.00 23.58  ? 57  ASP   A O   1 
ATOM   450  C CB  . ASP   A 1 58 ? -4.663  -16.052 -4.066  1.00 27.01  ? 57  ASP   A CB  1 
ATOM   451  C CG  . ASP   A 1 58 ? -6.054  -16.611 -4.377  1.00 31.57  ? 57  ASP   A CG  1 
ATOM   452  O OD1 . ASP   A 1 58 ? -6.872  -16.634 -3.428  1.00 31.09  ? 57  ASP   A OD1 1 
ATOM   453  O OD2 . ASP   A 1 58 ? -6.320  -16.992 -5.545  1.00 29.96  ? 57  ASP   A OD2 1 
ATOM   454  N N   . LEU   A 1 59 ? -3.067  -13.254 -2.353  1.00 24.27  ? 58  LEU   A N   1 
ATOM   455  C CA  . LEU   A 1 59 ? -1.742  -12.796 -1.933  1.00 23.34  ? 58  LEU   A CA  1 
ATOM   456  C C   . LEU   A 1 59 ? -1.879  -11.922 -0.674  1.00 20.56  ? 58  LEU   A C   1 
ATOM   457  O O   . LEU   A 1 59 ? -2.450  -10.828 -0.706  1.00 20.66  ? 58  LEU   A O   1 
ATOM   458  C CB  . LEU   A 1 59 ? -1.070  -12.019 -3.081  1.00 21.72  ? 58  LEU   A CB  1 
ATOM   459  C CG  . LEU   A 1 59 ? -0.872  -12.770 -4.410  1.00 22.51  ? 58  LEU   A CG  1 
ATOM   460  C CD1 . LEU   A 1 59 ? -0.148  -11.896 -5.424  1.00 23.33  ? 58  LEU   A CD1 1 
ATOM   461  C CD2 . LEU   A 1 59 ? -0.043  -14.041 -4.221  1.00 23.56  ? 58  LEU   A CD2 1 
ATOM   462  N N   . PHE   A 1 60 ? -1.338  -12.403 0.444   1.00 21.70  ? 59  PHE   A N   1 
ATOM   463  C CA  . PHE   A 1 60 ? -1.433  -11.667 1.699   1.00 23.70  ? 59  PHE   A CA  1 
ATOM   464  C C   . PHE   A 1 60 ? -0.038  -11.190 2.090   1.00 23.82  ? 59  PHE   A C   1 
ATOM   465  O O   . PHE   A 1 60 ? 0.829   -12.022 2.354   1.00 27.50  ? 59  PHE   A O   1 
ATOM   466  C CB  . PHE   A 1 60 ? -1.877  -12.689 2.744   1.00 21.49  ? 59  PHE   A CB  1 
ATOM   467  C CG  . PHE   A 1 60 ? -3.308  -13.168 2.498   1.00 25.61  ? 59  PHE   A CG  1 
ATOM   468  C CD1 . PHE   A 1 60 ? -3.587  -14.059 1.469   1.00 26.10  ? 59  PHE   A CD1 1 
ATOM   469  C CD2 . PHE   A 1 60 ? -4.369  -12.684 3.271   1.00 24.40  ? 59  PHE   A CD2 1 
ATOM   470  C CE1 . PHE   A 1 60 ? -4.895  -14.493 1.216   1.00 28.25  ? 59  PHE   A CE1 1 
ATOM   471  C CE2 . PHE   A 1 60 ? -5.675  -13.116 3.019   1.00 27.46  ? 59  PHE   A CE2 1 
ATOM   472  C CZ  . PHE   A 1 60 ? -5.935  -14.045 2.021   1.00 25.26  ? 59  PHE   A CZ  1 
ATOM   473  N N   . PRO   A 1 61 ? 0.216   -9.872  2.220   1.00 28.58  ? 60  PRO   A N   1 
ATOM   474  C CA  . PRO   A 1 61 ? 1.567   -9.404  2.586   1.00 24.98  ? 60  PRO   A CA  1 
ATOM   475  C C   . PRO   A 1 61 ? 2.120   -10.088 3.843   1.00 26.69  ? 60  PRO   A C   1 
ATOM   476  O O   . PRO   A 1 61 ? 1.418   -10.293 4.821   1.00 25.33  ? 60  PRO   A O   1 
ATOM   477  C CB  . PRO   A 1 61 ? 1.333   -7.877  2.719   1.00 25.51  ? 60  PRO   A CB  1 
ATOM   478  C CG  . PRO   A 1 61 ? 0.305   -7.621  1.591   1.00 29.33  ? 60  PRO   A CG  1 
ATOM   479  C CD  . PRO   A 1 61 ? -0.693  -8.764  1.872   1.00 26.11  ? 60  PRO   A CD  1 
ATOM   480  N N   . TYR   A 1 62 ? 3.412   -10.453 3.797   1.00 25.53  ? 61  TYR   A N   1 
ATOM   481  C CA  . TYR   A 1 62 ? 4.001   -11.351 4.778   1.00 26.34  ? 61  TYR   A CA  1 
ATOM   482  C C   . TYR   A 1 62 ? 4.007   -10.718 6.174   1.00 25.17  ? 61  TYR   A C   1 
ATOM   483  O O   . TYR   A 1 62 ? 3.646   -11.352 7.167   1.00 28.25  ? 61  TYR   A O   1 
ATOM   484  C CB  . TYR   A 1 62 ? 5.427   -11.672 4.308   1.00 26.37  ? 61  TYR   A CB  1 
ATOM   485  C CG  . TYR   A 1 62 ? 6.190   -12.440 5.381   1.00 26.88  ? 61  TYR   A CG  1 
ATOM   486  C CD1 . TYR   A 1 62 ? 5.954   -13.796 5.603   1.00 30.02  ? 61  TYR   A CD1 1 
ATOM   487  C CD2 . TYR   A 1 62 ? 7.183   -11.823 6.140   1.00 29.16  ? 61  TYR   A CD2 1 
ATOM   488  C CE1 . TYR   A 1 62 ? 6.634   -14.505 6.591   1.00 26.80  ? 61  TYR   A CE1 1 
ATOM   489  C CE2 . TYR   A 1 62 ? 7.887   -12.527 7.110   1.00 27.80  ? 61  TYR   A CE2 1 
ATOM   490  C CZ  . TYR   A 1 62 ? 7.590   -13.853 7.352   1.00 28.88  ? 61  TYR   A CZ  1 
ATOM   491  O OH  . TYR   A 1 62 ? 8.272   -14.540 8.321   1.00 31.73  ? 61  TYR   A OH  1 
ATOM   492  N N   . ASP   A 1 63 ? 4.370   -9.455  6.213   1.00 29.32  ? 62  ASP   A N   1 
ATOM   493  C CA  . ASP   A 1 63 ? 4.587   -8.777  7.480   1.00 39.70  ? 62  ASP   A CA  1 
ATOM   494  C C   . ASP   A 1 63 ? 3.281   -8.766  8.280   1.00 39.61  ? 62  ASP   A C   1 
ATOM   495  O O   . ASP   A 1 63 ? 3.205   -9.355  9.360   1.00 39.98  ? 62  ASP   A O   1 
ATOM   496  C CB  . ASP   A 1 63 ? 5.261   -7.439  7.234   1.00 46.22  ? 62  ASP   A CB  1 
ATOM   497  C CG  . ASP   A 1 63 ? 6.374   -7.139  8.221   1.00 74.01  ? 62  ASP   A CG  1 
ATOM   498  O OD1 . ASP   A 1 63 ? 6.048   -6.875  9.403   1.00 81.41  ? 62  ASP   A OD1 1 
ATOM   499  O OD2 . ASP   A 1 63 ? 7.556   -7.235  7.809   1.00 81.57  ? 62  ASP   A OD2 1 
ATOM   500  N N   . LYS   A 1 64 ? 2.230   -8.198  7.673   1.00 36.74  ? 63  LYS   A N   1 
ATOM   501  C CA  . LYS   A 1 64 ? 0.891   -8.140  8.256   1.00 35.13  ? 63  LYS   A CA  1 
ATOM   502  C C   . LYS   A 1 64 ? 0.347   -9.511  8.676   1.00 33.76  ? 63  LYS   A C   1 
ATOM   503  O O   . LYS   A 1 64 ? -0.427  -9.573  9.635   1.00 32.02  ? 63  LYS   A O   1 
ATOM   504  C CB  . LYS   A 1 64 ? -0.044  -7.527  7.208   1.00 36.32  ? 63  LYS   A CB  1 
ATOM   505  C CG  . LYS   A 1 64 ? -1.492  -7.288  7.674   1.00 38.97  ? 63  LYS   A CG  1 
ATOM   506  C CD  . LYS   A 1 64 ? -2.306  -6.727  6.519   1.00 38.33  ? 63  LYS   A CD  1 
ATOM   507  C CE  . LYS   A 1 64 ? -3.424  -5.840  7.003   1.00 43.76  ? 63  LYS   A CE  1 
ATOM   508  N NZ  . LYS   A 1 64 ? -4.392  -6.389  7.944   1.00 41.83  ? 63  LYS   A NZ  1 
ATOM   509  N N   . SER   A 1 65 ? 0.708   -10.593 7.951   1.00 29.11  ? 64  SER   A N   1 
ATOM   510  C CA  . SER   A 1 65 ? -0.003  -11.867 7.985   1.00 29.84  ? 64  SER   A CA  1 
ATOM   511  C C   . SER   A 1 65 ? 0.747   -12.940 8.769   1.00 28.96  ? 64  SER   A C   1 
ATOM   512  O O   . SER   A 1 65 ? 0.206   -14.026 8.974   1.00 30.22  ? 64  SER   A O   1 
ATOM   513  C CB  . SER   A 1 65 ? -0.247  -12.415 6.573   1.00 29.98  ? 64  SER   A CB  1 
ATOM   514  O OG  . SER   A 1 65 ? -1.246  -11.658 5.906   1.00 40.56  ? 64  SER   A OG  1 
ATOM   515  N N   . LYS   A 1 66 ? 2.014   -12.691 9.117   1.00 31.99  ? 65  LYS   A N   1 
ATOM   516  C CA  . LYS   A 1 66 ? 2.855   -13.776 9.620   1.00 34.16  ? 65  LYS   A CA  1 
ATOM   517  C C   . LYS   A 1 66 ? 2.354   -14.313 10.960  1.00 35.14  ? 65  LYS   A C   1 
ATOM   518  O O   . LYS   A 1 66 ? 2.497   -15.514 11.235  1.00 35.78  ? 65  LYS   A O   1 
ATOM   519  C CB  . LYS   A 1 66 ? 4.341   -13.415 9.693   1.00 38.37  ? 65  LYS   A CB  1 
ATOM   520  C CG  . LYS   A 1 66 ? 4.645   -12.109 10.366  1.00 42.25  ? 65  LYS   A CG  1 
ATOM   521  C CD  . LYS   A 1 66 ? 6.142   -11.951 10.607  1.00 54.35  ? 65  LYS   A CD  1 
ATOM   522  C CE  . LYS   A 1 66 ? 6.496   -10.625 11.220  1.00 48.37  ? 65  LYS   A CE  1 
ATOM   523  N NZ  . LYS   A 1 66 ? 6.740   -9.597  10.199  1.00 61.45  ? 65  LYS   A NZ  1 
ATOM   524  N N   A ASP   A 1 67 ? 1.773   -13.424 11.781  0.50 35.71  ? 66  ASP   A N   1 
ATOM   525  N N   B ASP   A 1 67 ? 1.777   -13.428 11.787  0.50 35.82  ? 66  ASP   A N   1 
ATOM   526  C CA  A ASP   A 1 67 ? 1.285   -13.807 13.103  0.50 37.79  ? 66  ASP   A CA  1 
ATOM   527  C CA  B ASP   A 1 67 ? 1.284   -13.844 13.095  0.50 37.92  ? 66  ASP   A CA  1 
ATOM   528  C C   A ASP   A 1 67 ? 0.221   -14.898 12.955  0.50 37.71  ? 66  ASP   A C   1 
ATOM   529  C C   B ASP   A 1 67 ? 0.271   -14.969 12.900  0.50 37.86  ? 66  ASP   A C   1 
ATOM   530  O O   A ASP   A 1 67 ? 0.208   -15.863 13.711  0.50 39.10  ? 66  ASP   A O   1 
ATOM   531  O O   B ASP   A 1 67 ? 0.337   -16.001 13.564  0.50 38.72  ? 66  ASP   A O   1 
ATOM   532  C CB  A ASP   A 1 67 ? 0.897   -12.601 13.949  0.50 36.52  ? 66  ASP   A CB  1 
ATOM   533  C CB  B ASP   A 1 67 ? 0.700   -12.690 13.892  0.50 36.76  ? 66  ASP   A CB  1 
ATOM   534  C CG  A ASP   A 1 67 ? 2.040   -11.796 14.563  0.50 41.74  ? 66  ASP   A CG  1 
ATOM   535  C CG  B ASP   A 1 67 ? 0.301   -13.025 15.323  0.50 41.76  ? 66  ASP   A CG  1 
ATOM   536  O OD1 A ASP   A 1 67 ? 3.180   -12.299 14.601  0.50 38.90  ? 66  ASP   A OD1 1 
ATOM   537  O OD1 B ASP   A 1 67 ? 1.209   -13.120 16.179  0.50 42.38  ? 66  ASP   A OD1 1 
ATOM   538  O OD2 A ASP   A 1 67 ? 1.797   -10.650 14.991  0.50 46.57  ? 66  ASP   A OD2 1 
ATOM   539  O OD2 B ASP   A 1 67 ? -0.915  -13.215 15.567  0.50 45.09  ? 66  ASP   A OD2 1 
ATOM   540  N N   . LYS   A 1 68 ? -0.617  -14.780 11.920  1.00 37.29  ? 67  LYS   A N   1 
ATOM   541  C CA  . LYS   A 1 68 ? -1.705  -15.706 11.676  1.00 33.91  ? 67  LYS   A CA  1 
ATOM   542  C C   . LYS   A 1 68 ? -1.220  -16.954 10.942  1.00 37.47  ? 67  LYS   A C   1 
ATOM   543  O O   . LYS   A 1 68 ? -1.661  -18.070 11.236  1.00 40.85  ? 67  LYS   A O   1 
ATOM   544  C CB  . LYS   A 1 68 ? -2.765  -14.925 10.886  1.00 33.51  ? 67  LYS   A CB  1 
ATOM   545  C CG  . LYS   A 1 68 ? -4.025  -15.685 10.576  1.00 35.45  ? 67  LYS   A CG  1 
ATOM   546  C CD  . LYS   A 1 68 ? -5.065  -14.755 9.955   1.00 38.47  ? 67  LYS   A CD  1 
ATOM   547  C CE  . LYS   A 1 68 ? -6.444  -15.347 9.968   1.00 42.93  ? 67  LYS   A CE  1 
ATOM   548  N NZ  . LYS   A 1 68 ? -7.414  -14.476 9.289   1.00 45.16  ? 67  LYS   A NZ  1 
ATOM   549  N N   . TYR   A 1 69 ? -0.346  -16.773 9.950   1.00 34.48  ? 68  TYR   A N   1 
ATOM   550  C CA  . TYR   A 1 69 ? -0.142  -17.842 8.986   1.00 30.19  ? 68  TYR   A CA  1 
ATOM   551  C C   . TYR   A 1 69 ? 1.220   -18.520 9.147   1.00 28.77  ? 68  TYR   A C   1 
ATOM   552  O O   . TYR   A 1 69 ? 1.427   -19.564 8.548   1.00 31.10  ? 68  TYR   A O   1 
ATOM   553  C CB  . TYR   A 1 69 ? -0.327  -17.388 7.531   1.00 28.81  ? 68  TYR   A CB  1 
ATOM   554  C CG  . TYR   A 1 69 ? -1.729  -16.904 7.169   1.00 27.82  ? 68  TYR   A CG  1 
ATOM   555  C CD1 . TYR   A 1 69 ? -2.870  -17.648 7.511   1.00 32.10  ? 68  TYR   A CD1 1 
ATOM   556  C CD2 . TYR   A 1 69 ? -1.910  -15.729 6.441   1.00 28.45  ? 68  TYR   A CD2 1 
ATOM   557  C CE1 . TYR   A 1 69 ? -4.146  -17.235 7.139   1.00 32.63  ? 68  TYR   A CE1 1 
ATOM   558  C CE2 . TYR   A 1 69 ? -3.177  -15.301 6.055   1.00 28.15  ? 68  TYR   A CE2 1 
ATOM   559  C CZ  . TYR   A 1 69 ? -4.293  -16.055 6.419   1.00 31.98  ? 68  TYR   A CZ  1 
ATOM   560  O OH  . TYR   A 1 69 ? -5.551  -15.656 6.074   1.00 34.19  ? 68  TYR   A OH  1 
ATOM   561  N N   . GLY   A 1 70 ? 2.148   -17.900 9.874   1.00 31.77  ? 69  GLY   A N   1 
ATOM   562  C CA  . GLY   A 1 70 ? 3.517   -18.382 9.879   1.00 34.52  ? 69  GLY   A CA  1 
ATOM   563  C C   . GLY   A 1 70 ? 3.769   -19.284 11.090  1.00 35.89  ? 69  GLY   A C   1 
ATOM   564  O O   . GLY   A 1 70 ? 4.630   -19.008 11.890  1.00 41.24  ? 69  GLY   A O   1 
ATOM   565  N N   . LYS   A 1 71 ? 2.987   -20.351 11.215  1.00 40.42  ? 70  LYS   A N   1 
ATOM   566  C CA  . LYS   A 1 71 ? 3.196   -21.353 12.243  1.00 44.60  ? 70  LYS   A CA  1 
ATOM   567  C C   . LYS   A 1 71 ? 3.408   -22.692 11.539  1.00 41.21  ? 70  LYS   A C   1 
ATOM   568  O O   . LYS   A 1 71 ? 3.032   -22.847 10.378  1.00 36.93  ? 70  LYS   A O   1 
ATOM   569  C CB  . LYS   A 1 71 ? 2.063   -21.273 13.276  1.00 50.58  ? 70  LYS   A CB  1 
ATOM   570  C CG  . LYS   A 1 71 ? 2.141   -20.018 14.144  1.00 55.57  ? 70  LYS   A CG  1 
ATOM   571  C CD  . LYS   A 1 71 ? 0.871   -19.692 14.924  1.00 66.88  ? 70  LYS   A CD  1 
ATOM   572  C CE  . LYS   A 1 71 ? -0.259  -19.279 14.026  1.00 69.96  ? 70  LYS   A CE  1 
ATOM   573  N NZ  . LYS   A 1 71 ? -1.499  -18.870 14.697  1.00 62.84  ? 70  LYS   A NZ  1 
ATOM   574  N N   . PRO   A 1 72 ? 4.120   -23.652 12.172  1.00 41.16  ? 71  PRO   A N   1 
ATOM   575  C CA  . PRO   A 1 72 ? 4.446   -24.930 11.526  1.00 36.61  ? 71  PRO   A CA  1 
ATOM   576  C C   . PRO   A 1 72 ? 3.233   -25.710 11.056  1.00 38.02  ? 71  PRO   A C   1 
ATOM   577  O O   . PRO   A 1 72 ? 2.188   -25.661 11.686  1.00 46.16  ? 71  PRO   A O   1 
ATOM   578  C CB  . PRO   A 1 72 ? 5.227   -25.684 12.620  1.00 37.65  ? 71  PRO   A CB  1 
ATOM   579  C CG  . PRO   A 1 72 ? 5.864   -24.580 13.414  1.00 42.48  ? 71  PRO   A CG  1 
ATOM   580  C CD  . PRO   A 1 72 ? 4.781   -23.485 13.477  1.00 41.76  ? 71  PRO   A CD  1 
ATOM   581  N N   . ASN   A 1 73 ? 3.412   -26.454 9.968   1.00 42.59  ? 72  ASN   A N   1 
ATOM   582  C CA  . ASN   A 1 73 ? 2.338   -27.151 9.299   1.00 48.01  ? 72  ASN   A CA  1 
ATOM   583  C C   . ASN   A 1 73 ? 2.872   -28.536 8.981   1.00 49.92  ? 72  ASN   A C   1 
ATOM   584  O O   . ASN   A 1 73 ? 4.070   -28.702 8.801   1.00 49.75  ? 72  ASN   A O   1 
ATOM   585  C CB  . ASN   A 1 73 ? 1.948   -26.394 8.036   1.00 49.93  ? 72  ASN   A CB  1 
ATOM   586  C CG  . ASN   A 1 73 ? 0.735   -26.976 7.352   1.00 67.57  ? 72  ASN   A CG  1 
ATOM   587  O OD1 . ASN   A 1 73 ? 0.855   -27.961 6.622   1.00 77.34  ? 72  ASN   A OD1 1 
ATOM   588  N ND2 . ASN   A 1 73 ? -0.433  -26.375 7.537   1.00 71.19  ? 72  ASN   A ND2 1 
ATOM   589  N N   . LYS   A 1 74 ? 1.970   -29.513 8.918   1.00 51.36  ? 73  LYS   A N   1 
ATOM   590  C CA  . LYS   A 1 74 ? 2.312   -30.888 8.612   1.00 48.91  ? 73  LYS   A CA  1 
ATOM   591  C C   . LYS   A 1 74 ? 2.723   -31.024 7.145   1.00 46.54  ? 73  LYS   A C   1 
ATOM   592  O O   . LYS   A 1 74 ? 3.407   -31.974 6.784   1.00 53.50  ? 73  LYS   A O   1 
ATOM   593  C CB  . LYS   A 1 74 ? 1.122   -31.779 9.021   1.00 54.45  ? 73  LYS   A CB  1 
ATOM   594  C CG  . LYS   A 1 74 ? 0.096   -32.190 7.939   1.00 53.40  ? 73  LYS   A CG  1 
ATOM   595  N N   . ARG   A 1 75 ? 2.327   -30.078 6.287   1.00 44.33  ? 74  ARG   A N   1 
ATOM   596  C CA  . ARG   A 1 75 ? 2.383   -30.329 4.852   1.00 40.06  ? 74  ARG   A CA  1 
ATOM   597  C C   . ARG   A 1 75 ? 3.820   -30.246 4.351   1.00 38.91  ? 74  ARG   A C   1 
ATOM   598  O O   . ARG   A 1 75 ? 4.625   -29.492 4.890   1.00 35.61  ? 74  ARG   A O   1 
ATOM   599  C CB  . ARG   A 1 75 ? 1.437   -29.427 4.043   1.00 45.37  ? 74  ARG   A CB  1 
ATOM   600  C CG  . ARG   A 1 75 ? -0.023  -29.710 4.360   1.00 47.61  ? 74  ARG   A CG  1 
ATOM   601  C CD  . ARG   A 1 75 ? -0.691  -30.690 3.419   1.00 41.03  ? 74  ARG   A CD  1 
ATOM   602  N NE  . ARG   A 1 75 ? -1.726  -29.971 2.667   1.00 59.27  ? 74  ARG   A NE  1 
ATOM   603  C CZ  . ARG   A 1 75 ? -2.743  -29.300 3.238   1.00 71.41  ? 74  ARG   A CZ  1 
ATOM   604  N NH1 . ARG   A 1 75 ? -3.703  -28.800 2.479   1.00 73.37  ? 74  ARG   A NH1 1 
ATOM   605  N NH2 . ARG   A 1 75 ? -2.827  -29.145 4.560   1.00 71.34  ? 74  ARG   A NH2 1 
ATOM   606  N N   . LYS   A 1 76 ? 4.107   -31.019 3.298   1.00 36.39  ? 75  LYS   A N   1 
ATOM   607  C CA  . LYS   A 1 76 ? 5.452   -31.216 2.796   1.00 38.08  ? 75  LYS   A CA  1 
ATOM   608  C C   . LYS   A 1 76 ? 6.004   -29.888 2.284   1.00 35.68  ? 75  LYS   A C   1 
ATOM   609  O O   . LYS   A 1 76 ? 5.415   -29.267 1.403   1.00 32.60  ? 75  LYS   A O   1 
ATOM   610  C CB  . LYS   A 1 76 ? 5.354   -32.192 1.626   1.00 37.97  ? 75  LYS   A CB  1 
ATOM   611  C CG  . LYS   A 1 76 ? 6.614   -32.555 0.848   1.00 43.47  ? 75  LYS   A CG  1 
ATOM   612  C CD  . LYS   A 1 76 ? 6.315   -33.798 0.004   1.00 50.64  ? 75  LYS   A CD  1 
ATOM   613  C CE  . LYS   A 1 76 ? 7.134   -33.971 -1.243  1.00 59.12  ? 75  LYS   A CE  1 
ATOM   614  N NZ  . LYS   A 1 76 ? 8.534   -34.272 -0.941  1.00 60.74  ? 75  LYS   A NZ  1 
ATOM   615  N N   . GLY   A 1 77 ? 7.157   -29.480 2.813   1.00 33.77  ? 76  GLY   A N   1 
ATOM   616  C CA  . GLY   A 1 77 ? 7.809   -28.298 2.271   1.00 33.88  ? 76  GLY   A CA  1 
ATOM   617  C C   . GLY   A 1 77 ? 7.538   -27.066 3.131   1.00 35.13  ? 76  GLY   A C   1 
ATOM   618  O O   . GLY   A 1 77 ? 8.292   -26.099 3.074   1.00 35.99  ? 76  GLY   A O   1 
ATOM   619  N N   . PHE   A 1 78 ? 6.520   -27.139 3.994   1.00 32.20  ? 77  PHE   A N   1 
ATOM   620  C CA  . PHE   A 1 78 ? 6.000   -25.934 4.614   1.00 33.96  ? 77  PHE   A CA  1 
ATOM   621  C C   . PHE   A 1 78 ? 6.992   -25.323 5.613   1.00 37.71  ? 77  PHE   A C   1 
ATOM   622  O O   . PHE   A 1 78 ? 7.223   -24.110 5.648   1.00 31.45  ? 77  PHE   A O   1 
ATOM   623  C CB  . PHE   A 1 78 ? 4.625   -26.237 5.212   1.00 32.80  ? 77  PHE   A CB  1 
ATOM   624  C CG  . PHE   A 1 78 ? 3.911   -24.959 5.627   1.00 31.82  ? 77  PHE   A CG  1 
ATOM   625  C CD1 . PHE   A 1 78 ? 4.270   -24.292 6.796   1.00 30.74  ? 77  PHE   A CD1 1 
ATOM   626  C CD2 . PHE   A 1 78 ? 2.882   -24.428 4.851   1.00 35.15  ? 77  PHE   A CD2 1 
ATOM   627  C CE1 . PHE   A 1 78 ? 3.638   -23.114 7.165   1.00 30.66  ? 77  PHE   A CE1 1 
ATOM   628  C CE2 . PHE   A 1 78 ? 2.242   -23.251 5.220   1.00 29.53  ? 77  PHE   A CE2 1 
ATOM   629  C CZ  . PHE   A 1 78 ? 2.617   -22.598 6.381   1.00 28.82  ? 77  PHE   A CZ  1 
ATOM   630  N N   . ASN   A 1 79 ? 7.545   -26.163 6.481   1.00 36.04  ? 78  ASN   A N   1 
ATOM   631  C CA  . ASN   A 1 79 ? 8.401   -25.645 7.542   1.00 33.93  ? 78  ASN   A CA  1 
ATOM   632  C C   . ASN   A 1 79 ? 9.744   -25.198 6.959   1.00 28.77  ? 78  ASN   A C   1 
ATOM   633  O O   . ASN   A 1 79 ? 10.350  -24.250 7.469   1.00 31.12  ? 78  ASN   A O   1 
ATOM   634  C CB  . ASN   A 1 79 ? 8.525   -26.667 8.666   1.00 36.18  ? 78  ASN   A CB  1 
ATOM   635  C CG  . ASN   A 1 79 ? 7.171   -26.965 9.267   1.00 44.19  ? 78  ASN   A CG  1 
ATOM   636  O OD1 . ASN   A 1 79 ? 6.240   -26.153 9.154   1.00 37.15  ? 78  ASN   A OD1 1 
ATOM   637  N ND2 . ASN   A 1 79 ? 7.064   -28.087 9.963   1.00 39.92  ? 78  ASN   A ND2 1 
ATOM   638  N N   . GLU   A 1 80 ? 10.211  -25.908 5.918   1.00 29.04  ? 79  GLU   A N   1 
ATOM   639  C CA  . GLU   A 1 80 ? 11.354  -25.445 5.148   1.00 29.33  ? 79  GLU   A CA  1 
ATOM   640  C C   . GLU   A 1 80 ? 11.023  -24.075 4.561   1.00 29.34  ? 79  GLU   A C   1 
ATOM   641  O O   . GLU   A 1 80 ? 11.867  -23.169 4.560   1.00 29.40  ? 79  GLU   A O   1 
ATOM   642  C CB  . GLU   A 1 80 ? 11.836  -26.391 4.045   1.00 28.75  ? 79  GLU   A CB  1 
ATOM   643  C CG  . GLU   A 1 80 ? 13.125  -25.917 3.363   1.00 28.85  ? 79  GLU   A CG  1 
ATOM   644  C CD  . GLU   A 1 80 ? 13.723  -26.932 2.365   1.00 39.56  ? 79  GLU   A CD  1 
ATOM   645  O OE1 . GLU   A 1 80 ? 13.089  -27.949 2.066   1.00 42.68  ? 79  GLU   A OE1 1 
ATOM   646  O OE2 . GLU   A 1 80 ? 14.836  -26.725 1.859   1.00 37.76  ? 79  GLU   A OE2 1 
ATOM   647  N N   . GLY   A 1 81 ? 9.797   -23.935 4.039   1.00 29.22  ? 80  GLY   A N   1 
ATOM   648  C CA  . GLY   A 1 81 ? 9.374   -22.658 3.478   1.00 27.08  ? 80  GLY   A CA  1 
ATOM   649  C C   . GLY   A 1 81 ? 9.407   -21.531 4.518   1.00 27.50  ? 80  GLY   A C   1 
ATOM   650  O O   . GLY   A 1 81 ? 9.732   -20.384 4.190   1.00 24.95  ? 80  GLY   A O   1 
ATOM   651  N N   . LEU   A 1 82 ? 8.958   -21.837 5.746   1.00 24.91  ? 81  LEU   A N   1 
ATOM   652  C CA  . LEU   A 1 82 ? 8.979   -20.845 6.813   1.00 29.19  ? 81  LEU   A CA  1 
ATOM   653  C C   . LEU   A 1 82 ? 10.417  -20.393 7.059   1.00 29.10  ? 81  LEU   A C   1 
ATOM   654  O O   . LEU   A 1 82 ? 10.651  -19.202 7.323   1.00 25.41  ? 81  LEU   A O   1 
ATOM   655  C CB  . LEU   A 1 82 ? 8.314   -21.341 8.106   1.00 30.26  ? 81  LEU   A CB  1 
ATOM   656  C CG  . LEU   A 1 82 ? 6.824   -21.701 8.002   1.00 30.51  ? 81  LEU   A CG  1 
ATOM   657  C CD1 . LEU   A 1 82 ? 6.390   -22.493 9.246   1.00 35.37  ? 81  LEU   A CD1 1 
ATOM   658  C CD2 . LEU   A 1 82 ? 5.856   -20.545 7.768   1.00 28.89  ? 81  LEU   A CD2 1 
ATOM   659  N N   . TRP   A 1 83 ? 11.367  -21.345 7.006   1.00 27.29  ? 82  TRP   A N   1 
ATOM   660  C CA  . TRP   A 1 83 ? 12.755  -20.977 7.310   1.00 29.76  ? 82  TRP   A CA  1 
ATOM   661  C C   . TRP   A 1 83 ? 13.228  -20.029 6.213   1.00 30.99  ? 82  TRP   A C   1 
ATOM   662  O O   . TRP   A 1 83 ? 13.804  -18.985 6.487   1.00 27.13  ? 82  TRP   A O   1 
ATOM   663  C CB  . TRP   A 1 83 ? 13.702  -22.197 7.456   1.00 29.07  ? 82  TRP   A CB  1 
ATOM   664  C CG  . TRP   A 1 83 ? 15.155  -21.848 7.712   1.00 28.81  ? 82  TRP   A CG  1 
ATOM   665  C CD1 . TRP   A 1 83 ? 15.788  -21.748 8.921   1.00 27.49  ? 82  TRP   A CD1 1 
ATOM   666  C CD2 . TRP   A 1 83 ? 16.143  -21.506 6.723   1.00 26.63  ? 82  TRP   A CD2 1 
ATOM   667  N NE1 . TRP   A 1 83 ? 17.101  -21.401 8.753   1.00 33.77  ? 82  TRP   A NE1 1 
ATOM   668  C CE2 . TRP   A 1 83 ? 17.349  -21.236 7.413   1.00 32.61  ? 82  TRP   A CE2 1 
ATOM   669  C CE3 . TRP   A 1 83 ? 16.122  -21.419 5.326   1.00 31.16  ? 82  TRP   A CE3 1 
ATOM   670  C CZ2 . TRP   A 1 83 ? 18.525  -20.883 6.756   1.00 28.49  ? 82  TRP   A CZ2 1 
ATOM   671  C CZ3 . TRP   A 1 83 ? 17.277  -21.047 4.675   1.00 32.70  ? 82  TRP   A CZ3 1 
ATOM   672  C CH2 . TRP   A 1 83 ? 18.475  -20.814 5.383   1.00 30.72  ? 82  TRP   A CH2 1 
ATOM   673  N N   . GLU   A 1 84 ? 12.930  -20.391 4.960   1.00 29.15  ? 83  GLU   A N   1 
ATOM   674  C CA  . GLU   A 1 84 ? 13.416  -19.628 3.823   1.00 27.28  ? 83  GLU   A CA  1 
ATOM   675  C C   . GLU   A 1 84 ? 12.879  -18.195 3.866   1.00 25.62  ? 83  GLU   A C   1 
ATOM   676  O O   . GLU   A 1 84 ? 13.630  -17.246 3.682   1.00 22.52  ? 83  GLU   A O   1 
ATOM   677  C CB  . GLU   A 1 84 ? 12.997  -20.345 2.533   1.00 27.74  ? 83  GLU   A CB  1 
ATOM   678  C CG  . GLU   A 1 84 ? 13.660  -21.713 2.368   1.00 29.85  ? 83  GLU   A CG  1 
ATOM   679  C CD  . GLU   A 1 84 ? 13.300  -22.410 1.060   1.00 30.51  ? 83  GLU   A CD  1 
ATOM   680  O OE1 . GLU   A 1 84 ? 12.359  -21.951 0.385   1.00 28.60  ? 83  GLU   A OE1 1 
ATOM   681  O OE2 . GLU   A 1 84 ? 13.963  -23.392 0.679   1.00 31.56  ? 83  GLU   A OE2 1 
ATOM   682  N N   . ILE   A 1 85 ? 11.565  -18.030 4.063   1.00 24.11  ? 84  ILE   A N   1 
ATOM   683  C CA  . ILE   A 1 85 ? 11.005  -16.695 3.942   1.00 24.20  ? 84  ILE   A CA  1 
ATOM   684  C C   . ILE   A 1 85 ? 11.578  -15.812 5.066   1.00 25.15  ? 84  ILE   A C   1 
ATOM   685  O O   . ILE   A 1 85 ? 11.736  -14.590 4.927   1.00 24.54  ? 84  ILE   A O   1 
ATOM   686  C CB  . ILE   A 1 85 ? 9.467   -16.722 3.942   1.00 21.43  ? 84  ILE   A CB  1 
ATOM   687  C CG1 . ILE   A 1 85 ? 8.904   -15.306 3.523   1.00 22.88  ? 84  ILE   A CG1 1 
ATOM   688  C CG2 . ILE   A 1 85 ? 8.933   -17.143 5.324   1.00 20.52  ? 84  ILE   A CG2 1 
ATOM   689  C CD1 . ILE   A 1 85 ? 7.439   -15.301 3.056   1.00 20.41  ? 84  ILE   A CD1 1 
ATOM   690  N N   . GLN   A 1 86 ? 11.900  -16.440 6.201   1.00 24.03  ? 85  GLN   A N   1 
ATOM   691  C CA  . GLN   A 1 86 ? 12.365  -15.650 7.345   1.00 26.69  ? 85  GLN   A CA  1 
ATOM   692  C C   . GLN   A 1 86 ? 13.868  -15.375 7.248   1.00 26.37  ? 85  GLN   A C   1 
ATOM   693  O O   . GLN   A 1 86 ? 14.317  -14.317 7.691   1.00 30.15  ? 85  GLN   A O   1 
ATOM   694  C CB  . GLN   A 1 86 ? 11.952  -16.355 8.647   1.00 28.22  ? 85  GLN   A CB  1 
ATOM   695  C CG  . GLN   A 1 86 ? 12.509  -15.705 9.912   1.00 36.15  ? 85  GLN   A CG  1 
ATOM   696  C CD  . GLN   A 1 86 ? 11.901  -16.256 11.192  1.00 48.56  ? 85  GLN   A CD  1 
ATOM   697  O OE1 . GLN   A 1 86 ? 11.745  -17.474 11.386  1.00 41.18  ? 85  GLN   A OE1 1 
ATOM   698  N NE2 . GLN   A 1 86 ? 11.544  -15.342 12.086  1.00 47.55  ? 85  GLN   A NE2 1 
ATOM   699  N N   . ASN   A 1 87 ? 14.641  -16.297 6.649   1.00 23.46  ? 86  ASN   A N   1 
ATOM   700  C CA  . ASN   A 1 87 ? 16.099  -16.298 6.771   1.00 25.22  ? 86  ASN   A CA  1 
ATOM   701  C C   . ASN   A 1 87 ? 16.834  -15.936 5.476   1.00 25.19  ? 86  ASN   A C   1 
ATOM   702  O O   . ASN   A 1 87 ? 17.927  -15.370 5.543   1.00 26.77  ? 86  ASN   A O   1 
ATOM   703  C CB  . ASN   A 1 87 ? 16.615  -17.593 7.408   1.00 24.76  ? 86  ASN   A CB  1 
ATOM   704  C CG  . ASN   A 1 87 ? 16.154  -17.689 8.848   1.00 28.84  ? 86  ASN   A CG  1 
ATOM   705  O OD1 . ASN   A 1 87 ? 16.551  -16.867 9.685   1.00 32.12  ? 86  ASN   A OD1 1 
ATOM   706  N ND2 . ASN   A 1 87 ? 15.246  -18.597 9.164   1.00 27.33  ? 86  ASN   A ND2 1 
ATOM   707  N N   . ASN   A 1 88 ? 16.291  -16.309 4.304   1.00 25.65  ? 87  ASN   A N   1 
ATOM   708  C CA  . ASN   A 1 88 ? 16.919  -15.936 3.046   1.00 24.30  ? 87  ASN   A CA  1 
ATOM   709  C C   . ASN   A 1 88 ? 15.853  -15.869 1.949   1.00 24.76  ? 87  ASN   A C   1 
ATOM   710  O O   . ASN   A 1 88 ? 15.874  -16.645 0.988   1.00 24.96  ? 87  ASN   A O   1 
ATOM   711  C CB  . ASN   A 1 88 ? 18.094  -16.864 2.709   1.00 26.69  ? 87  ASN   A CB  1 
ATOM   712  C CG  . ASN   A 1 88 ? 19.148  -16.224 1.835   1.00 27.92  ? 87  ASN   A CG  1 
ATOM   713  O OD1 . ASN   A 1 88 ? 18.896  -15.218 1.147   1.00 25.47  ? 87  ASN   A OD1 1 
ATOM   714  N ND2 . ASN   A 1 88 ? 20.323  -16.846 1.796   1.00 25.88  ? 87  ASN   A ND2 1 
ATOM   715  N N   . PRO   A 1 89 ? 14.896  -14.910 2.047   1.00 24.18  ? 88  PRO   A N   1 
ATOM   716  C CA  . PRO   A 1 89 ? 13.783  -14.853 1.105   1.00 22.26  ? 88  PRO   A CA  1 
ATOM   717  C C   . PRO   A 1 89 ? 14.159  -14.425 -0.313  1.00 23.28  ? 88  PRO   A C   1 
ATOM   718  O O   . PRO   A 1 89 ? 13.379  -14.668 -1.203  1.00 22.39  ? 88  PRO   A O   1 
ATOM   719  C CB  . PRO   A 1 89 ? 12.822  -13.873 1.796   1.00 20.34  ? 88  PRO   A CB  1 
ATOM   720  C CG  . PRO   A 1 89 ? 13.744  -12.908 2.554   1.00 21.29  ? 88  PRO   A CG  1 
ATOM   721  C CD  . PRO   A 1 89 ? 14.851  -13.833 3.063   1.00 21.14  ? 88  PRO   A CD  1 
ATOM   722  N N   . HIS   A 1 90 ? 15.342  -13.825 -0.517  1.00 22.10  ? 89  HIS   A N   1 
ATOM   723  C CA  . HIS   A 1 90 ? 15.733  -13.273 -1.804  1.00 22.84  ? 89  HIS   A CA  1 
ATOM   724  C C   . HIS   A 1 90 ? 16.808  -14.122 -2.483  1.00 23.92  ? 89  HIS   A C   1 
ATOM   725  O O   . HIS   A 1 90 ? 17.308  -13.725 -3.536  1.00 22.21  ? 89  HIS   A O   1 
ATOM   726  C CB  . HIS   A 1 90 ? 16.155  -11.802 -1.664  1.00 22.43  ? 89  HIS   A CB  1 
ATOM   727  C CG  . HIS   A 1 90 ? 15.067  -10.968 -1.094  1.00 24.23  ? 89  HIS   A CG  1 
ATOM   728  N ND1 . HIS   A 1 90 ? 13.811  -10.892 -1.675  1.00 24.20  ? 89  HIS   A ND1 1 
ATOM   729  C CD2 . HIS   A 1 90 ? 14.994  -10.273 0.043   1.00 25.65  ? 89  HIS   A CD2 1 
ATOM   730  C CE1 . HIS   A 1 90 ? 13.055  -10.064 -0.964  1.00 22.77  ? 89  HIS   A CE1 1 
ATOM   731  N NE2 . HIS   A 1 90 ? 13.751  -9.695  0.091   1.00 25.35  ? 89  HIS   A NE2 1 
ATOM   732  N N   . ALA   A 1 91 ? 17.084  -15.308 -1.917  1.00 24.66  ? 90  ALA   A N   1 
ATOM   733  C CA  . ALA   A 1 91 ? 18.113  -16.194 -2.453  1.00 23.38  ? 90  ALA   A CA  1 
ATOM   734  C C   . ALA   A 1 91 ? 17.619  -16.882 -3.724  1.00 32.24  ? 90  ALA   A C   1 
ATOM   735  O O   . ALA   A 1 91 ? 16.392  -16.982 -3.980  1.00 26.01  ? 90  ALA   A O   1 
ATOM   736  C CB  . ALA   A 1 91 ? 18.485  -17.223 -1.413  1.00 24.74  ? 90  ALA   A CB  1 
ATOM   737  N N   . SER   A 1 92 ? 18.609  -17.378 -4.485  1.00 30.84  ? 91  SER   A N   1 
ATOM   738  C CA  . SER   A 1 92 ? 18.350  -18.266 -5.608  1.00 35.13  ? 91  SER   A CA  1 
ATOM   739  C C   . SER   A 1 92 ? 18.032  -19.643 -5.054  1.00 35.80  ? 91  SER   A C   1 
ATOM   740  O O   . SER   A 1 92 ? 18.836  -20.185 -4.293  1.00 35.75  ? 91  SER   A O   1 
ATOM   741  C CB  . SER   A 1 92 ? 19.542  -18.346 -6.514  1.00 34.83  ? 91  SER   A CB  1 
ATOM   742  O OG  . SER   A 1 92 ? 19.222  -19.223 -7.582  1.00 42.61  ? 91  SER   A OG  1 
ATOM   743  N N   . TYR   A 1 93 ? 16.882  -20.209 -5.450  1.00 32.15  ? 92  TYR   A N   1 
ATOM   744  C CA  . TYR   A 1 93 ? 16.613  -21.570 -5.028  1.00 36.01  ? 92  TYR   A CA  1 
ATOM   745  C C   . TYR   A 1 93 ? 16.576  -22.510 -6.238  1.00 42.35  ? 92  TYR   A C   1 
ATOM   746  O O   . TYR   A 1 93 ? 15.981  -23.575 -6.149  1.00 50.77  ? 92  TYR   A O   1 
ATOM   747  C CB  . TYR   A 1 93 ? 15.332  -21.648 -4.192  1.00 28.89  ? 92  TYR   A CB  1 
ATOM   748  C CG  . TYR   A 1 93 ? 15.451  -21.023 -2.815  1.00 31.33  ? 92  TYR   A CG  1 
ATOM   749  C CD1 . TYR   A 1 93 ? 15.884  -21.782 -1.728  1.00 32.70  ? 92  TYR   A CD1 1 
ATOM   750  C CD2 . TYR   A 1 93 ? 15.125  -19.686 -2.605  1.00 28.96  ? 92  TYR   A CD2 1 
ATOM   751  C CE1 . TYR   A 1 93 ? 16.003  -21.212 -0.466  1.00 33.28  ? 92  TYR   A CE1 1 
ATOM   752  C CE2 . TYR   A 1 93 ? 15.217  -19.119 -1.346  1.00 28.10  ? 92  TYR   A CE2 1 
ATOM   753  C CZ  . TYR   A 1 93 ? 15.650  -19.888 -0.274  1.00 29.02  ? 92  TYR   A CZ  1 
ATOM   754  O OH  . TYR   A 1 93 ? 15.832  -19.351 0.972   1.00 31.07  ? 92  TYR   A OH  1 
ATOM   755  N N   . SER   A 1 94 ? 17.218  -22.124 -7.347  1.00 54.53  ? 93  SER   A N   1 
ATOM   756  C CA  . SER   A 1 94 ? 17.388  -23.011 -8.494  1.00 69.21  ? 93  SER   A CA  1 
ATOM   757  C C   . SER   A 1 94 ? 18.108  -24.286 -8.027  1.00 79.34  ? 93  SER   A C   1 
ATOM   758  O O   . SER   A 1 94 ? 19.297  -24.158 -7.642  1.00 73.51  ? 93  SER   A O   1 
ATOM   759  C CB  . SER   A 1 94 ? 18.180  -22.360 -9.612  1.00 66.95  ? 93  SER   A CB  1 
ATOM   760  O OG  . SER   A 1 94 ? 18.064  -20.947 -9.610  1.00 71.51  ? 93  SER   A OG  1 
ATOM   761  O OXT . SER   A 1 94 ? 17.458  -25.358 -8.055  1.00 89.61  ? 93  SER   A OXT 1 
ATOM   762  N N   . MET   B 1 2  ? 38.768  -11.042 -42.594 1.00 69.38  ? 1   MET   B N   1 
ATOM   763  C CA  . MET   B 1 2  ? 38.391  -12.114 -43.553 1.00 75.83  ? 1   MET   B CA  1 
ATOM   764  C C   . MET   B 1 2  ? 36.875  -12.303 -43.489 1.00 70.74  ? 1   MET   B C   1 
ATOM   765  O O   . MET   B 1 2  ? 36.371  -12.691 -42.434 1.00 68.17  ? 1   MET   B O   1 
ATOM   766  C CB  . MET   B 1 2  ? 39.135  -13.416 -43.220 1.00 77.29  ? 1   MET   B CB  1 
ATOM   767  C CG  . MET   B 1 2  ? 39.085  -14.503 -44.297 1.00 87.07  ? 1   MET   B CG  1 
ATOM   768  S SD  . MET   B 1 2  ? 39.854  -14.157 -45.896 1.00 89.99  ? 1   MET   B SD  1 
ATOM   769  C CE  . MET   B 1 2  ? 41.412  -13.360 -45.479 1.00 81.22  ? 1   MET   B CE  1 
ATOM   770  N N   . PRO   B 1 3  ? 36.116  -12.002 -44.585 1.00 66.35  ? 2   PRO   B N   1 
ATOM   771  C CA  . PRO   B 1 3  ? 34.662  -12.217 -44.626 1.00 60.45  ? 2   PRO   B CA  1 
ATOM   772  C C   . PRO   B 1 3  ? 34.310  -13.660 -44.268 1.00 54.49  ? 2   PRO   B C   1 
ATOM   773  O O   . PRO   B 1 3  ? 35.038  -14.570 -44.647 1.00 53.71  ? 2   PRO   B O   1 
ATOM   774  C CB  . PRO   B 1 3  ? 34.250  -11.859 -46.073 1.00 62.45  ? 2   PRO   B CB  1 
ATOM   775  C CG  . PRO   B 1 3  ? 35.371  -10.976 -46.581 1.00 57.87  ? 2   PRO   B CG  1 
ATOM   776  C CD  . PRO   B 1 3  ? 36.622  -11.412 -45.837 1.00 59.60  ? 2   PRO   B CD  1 
ATOM   777  N N   . HIS   B 1 4  ? 33.237  -13.855 -43.485 1.00 50.30  ? 3   HIS   B N   1 
ATOM   778  C CA  . HIS   B 1 4  ? 32.797  -15.203 -43.144 1.00 50.96  ? 3   HIS   B CA  1 
ATOM   779  C C   . HIS   B 1 4  ? 31.402  -15.460 -43.716 1.00 46.79  ? 3   HIS   B C   1 
ATOM   780  O O   . HIS   B 1 4  ? 30.833  -14.596 -44.387 1.00 43.81  ? 3   HIS   B O   1 
ATOM   781  C CB  . HIS   B 1 4  ? 32.976  -15.495 -41.652 1.00 56.88  ? 3   HIS   B CB  1 
ATOM   782  C CG  . HIS   B 1 4  ? 34.395  -15.406 -41.196 1.00 73.53  ? 3   HIS   B CG  1 
ATOM   783  N ND1 . HIS   B 1 4  ? 35.392  -16.213 -41.706 1.00 80.32  ? 3   HIS   B ND1 1 
ATOM   784  C CD2 . HIS   B 1 4  ? 34.991  -14.594 -40.308 1.00 69.80  ? 3   HIS   B CD2 1 
ATOM   785  C CE1 . HIS   B 1 4  ? 36.545  -15.902 -41.128 1.00 75.23  ? 3   HIS   B CE1 1 
ATOM   786  N NE2 . HIS   B 1 4  ? 36.325  -14.920 -40.276 1.00 72.63  ? 3   HIS   B NE2 1 
ATOM   787  N N   . ALA   B 1 5  ? 30.867  -16.664 -43.471 1.00 42.15  ? 4   ALA   B N   1 
ATOM   788  C CA  . ALA   B 1 5  ? 29.584  -17.055 -44.038 1.00 41.47  ? 4   ALA   B CA  1 
ATOM   789  C C   . ALA   B 1 5  ? 28.548  -16.029 -43.599 1.00 41.20  ? 4   ALA   B C   1 
ATOM   790  O O   . ALA   B 1 5  ? 27.677  -15.623 -44.373 1.00 40.24  ? 4   ALA   B O   1 
ATOM   791  C CB  . ALA   B 1 5  ? 29.217  -18.427 -43.529 1.00 39.67  ? 4   ALA   B CB  1 
ATOM   792  N N   . PHE   B 1 6  ? 28.669  -15.642 -42.323 1.00 40.57  ? 5   PHE   B N   1 
ATOM   793  C CA  . PHE   B 1 6  ? 27.844  -14.610 -41.710 1.00 45.20  ? 5   PHE   B CA  1 
ATOM   794  C C   . PHE   B 1 6  ? 28.742  -13.403 -41.455 1.00 44.43  ? 5   PHE   B C   1 
ATOM   795  O O   . PHE   B 1 6  ? 29.868  -13.584 -41.002 1.00 42.16  ? 5   PHE   B O   1 
ATOM   796  C CB  . PHE   B 1 6  ? 27.271  -15.068 -40.360 1.00 42.65  ? 5   PHE   B CB  1 
ATOM   797  C CG  . PHE   B 1 6  ? 26.254  -16.197 -40.444 1.00 42.39  ? 5   PHE   B CG  1 
ATOM   798  C CD1 . PHE   B 1 6  ? 24.912  -15.920 -40.695 1.00 39.82  ? 5   PHE   B CD1 1 
ATOM   799  C CD2 . PHE   B 1 6  ? 26.639  -17.522 -40.263 1.00 42.82  ? 5   PHE   B CD2 1 
ATOM   800  C CE1 . PHE   B 1 6  ? 23.979  -16.938 -40.801 1.00 43.66  ? 5   PHE   B CE1 1 
ATOM   801  C CE2 . PHE   B 1 6  ? 25.700  -18.541 -40.368 1.00 41.68  ? 5   PHE   B CE2 1 
ATOM   802  C CZ  . PHE   B 1 6  ? 24.371  -18.248 -40.621 1.00 41.48  ? 5   PHE   B CZ  1 
ATOM   803  N N   . LYS   B 1 7  ? 28.237  -12.201 -41.772 1.00 45.26  ? 6   LYS   B N   1 
ATOM   804  C CA  . LYS   B 1 7  ? 28.968  -10.957 -41.582 1.00 46.12  ? 6   LYS   B CA  1 
ATOM   805  C C   . LYS   B 1 7  ? 28.188  -10.089 -40.589 1.00 48.11  ? 6   LYS   B C   1 
ATOM   806  O O   . LYS   B 1 7  ? 26.965  -10.236 -40.498 1.00 44.25  ? 6   LYS   B O   1 
ATOM   807  C CB  . LYS   B 1 7  ? 29.059  -10.276 -42.951 1.00 48.71  ? 6   LYS   B CB  1 
ATOM   808  C CG  . LYS   B 1 7  ? 27.716  -9.965  -43.603 1.00 54.64  ? 6   LYS   B CG  1 
ATOM   809  C CD  . LYS   B 1 7  ? 27.797  -9.274  -44.966 1.00 60.28  ? 6   LYS   B CD  1 
ATOM   810  C CE  . LYS   B 1 7  ? 26.474  -8.827  -45.516 1.00 57.83  ? 6   LYS   B CE  1 
ATOM   811  N NZ  . LYS   B 1 7  ? 25.599  -9.970  -45.791 1.00 58.02  ? 6   LYS   B NZ  1 
ATOM   812  N N   . PRO   B 1 8  ? 28.841  -9.131  -39.871 1.00 45.01  ? 7   PRO   B N   1 
ATOM   813  C CA  . PRO   B 1 8  ? 28.151  -8.244  -38.924 1.00 36.52  ? 7   PRO   B CA  1 
ATOM   814  C C   . PRO   B 1 8  ? 26.974  -7.539  -39.578 1.00 38.14  ? 7   PRO   B C   1 
ATOM   815  O O   . PRO   B 1 8  ? 27.065  -7.096  -40.729 1.00 40.54  ? 7   PRO   B O   1 
ATOM   816  C CB  . PRO   B 1 8  ? 29.295  -7.303  -38.558 1.00 41.93  ? 7   PRO   B CB  1 
ATOM   817  C CG  . PRO   B 1 8  ? 30.513  -8.231  -38.576 1.00 42.38  ? 7   PRO   B CG  1 
ATOM   818  C CD  . PRO   B 1 8  ? 30.281  -8.826  -39.949 1.00 46.62  ? 7   PRO   B CD  1 
ATOM   819  N N   . GLY   B 1 9  ? 25.833  -7.553  -38.884 1.00 31.49  ? 8   GLY   B N   1 
ATOM   820  C CA  . GLY   B 1 9  ? 24.625  -6.904  -39.369 1.00 30.50  ? 8   GLY   B CA  1 
ATOM   821  C C   . GLY   B 1 9  ? 23.670  -7.862  -40.077 1.00 31.34  ? 8   GLY   B C   1 
ATOM   822  O O   . GLY   B 1 9  ? 22.536  -7.483  -40.420 1.00 33.15  ? 8   GLY   B O   1 
ATOM   823  N N   . ASP   B 1 10 ? 24.149  -9.088  -40.359 1.00 30.47  ? 9   ASP   B N   1 
ATOM   824  C CA  . ASP   B 1 10 ? 23.265  -10.128 -40.890 1.00 31.79  ? 9   ASP   B CA  1 
ATOM   825  C C   . ASP   B 1 10 ? 22.181  -10.409 -39.839 1.00 29.92  ? 9   ASP   B C   1 
ATOM   826  O O   . ASP   B 1 10 ? 22.464  -10.432 -38.645 1.00 30.66  ? 9   ASP   B O   1 
ATOM   827  C CB  . ASP   B 1 10 ? 24.028  -11.415 -41.186 1.00 34.64  ? 9   ASP   B CB  1 
ATOM   828  C CG  . ASP   B 1 10 ? 24.746  -11.499 -42.527 1.00 42.30  ? 9   ASP   B CG  1 
ATOM   829  O OD1 . ASP   B 1 10 ? 24.465  -10.656 -43.386 1.00 39.36  ? 9   ASP   B OD1 1 
ATOM   830  O OD2 . ASP   B 1 10 ? 25.610  -12.395 -42.680 1.00 47.20  ? 9   ASP   B OD2 1 
ATOM   831  N N   . LEU   B 1 11 ? 20.934  -10.537 -40.272 1.00 32.19  ? 10  LEU   B N   1 
ATOM   832  C CA  . LEU   B 1 11 ? 19.837  -10.795 -39.348 1.00 34.98  ? 10  LEU   B CA  1 
ATOM   833  C C   . LEU   B 1 11 ? 19.545  -12.293 -39.334 1.00 32.68  ? 10  LEU   B C   1 
ATOM   834  O O   . LEU   B 1 11 ? 19.532  -12.911 -40.398 1.00 33.94  ? 10  LEU   B O   1 
ATOM   835  C CB  . LEU   B 1 11 ? 18.619  -9.987  -39.807 1.00 29.20  ? 10  LEU   B CB  1 
ATOM   836  C CG  . LEU   B 1 11 ? 18.876  -8.484  -39.975 1.00 27.03  ? 10  LEU   B CG  1 
ATOM   837  C CD1 . LEU   B 1 11 ? 17.559  -7.719  -40.253 1.00 27.81  ? 10  LEU   B CD1 1 
ATOM   838  C CD2 . LEU   B 1 11 ? 19.609  -7.969  -38.735 1.00 24.67  ? 10  LEU   B CD2 1 
ATOM   839  N N   . VAL   B 1 12 ? 19.259  -12.856 -38.147 1.00 28.92  ? 11  VAL   B N   1 
ATOM   840  C CA  . VAL   B 1 12 ? 19.064  -14.304 -38.020 1.00 28.81  ? 11  VAL   B CA  1 
ATOM   841  C C   . VAL   B 1 12 ? 17.941  -14.610 -37.033 1.00 30.32  ? 11  VAL   B C   1 
ATOM   842  O O   . VAL   B 1 12 ? 17.487  -13.723 -36.315 1.00 27.13  ? 11  VAL   B O   1 
ATOM   843  C CB  . VAL   B 1 12 ? 20.372  -14.981 -37.569 1.00 30.26  ? 11  VAL   B CB  1 
ATOM   844  C CG1 . VAL   B 1 12 ? 21.513  -14.847 -38.605 1.00 28.25  ? 11  VAL   B CG1 1 
ATOM   845  C CG2 . VAL   B 1 12 ? 20.796  -14.559 -36.166 1.00 28.56  ? 11  VAL   B CG2 1 
ATOM   846  N N   . PHE   B 1 13 ? 17.457  -15.863 -37.022 1.00 30.56  ? 12  PHE   B N   1 
ATOM   847  C CA  . PHE   B 1 13 ? 16.947  -16.419 -35.772 1.00 28.56  ? 12  PHE   B CA  1 
ATOM   848  C C   . PHE   B 1 13 ? 18.060  -17.264 -35.171 1.00 29.37  ? 12  PHE   B C   1 
ATOM   849  O O   . PHE   B 1 13 ? 18.704  -18.025 -35.916 1.00 28.15  ? 12  PHE   B O   1 
ATOM   850  C CB  . PHE   B 1 13 ? 15.689  -17.269 -35.952 1.00 28.35  ? 12  PHE   B CB  1 
ATOM   851  C CG  . PHE   B 1 13 ? 14.508  -16.413 -36.351 1.00 30.72  ? 12  PHE   B CG  1 
ATOM   852  C CD1 . PHE   B 1 13 ? 14.279  -16.109 -37.694 1.00 33.10  ? 12  PHE   B CD1 1 
ATOM   853  C CD2 . PHE   B 1 13 ? 13.622  -15.930 -35.394 1.00 31.44  ? 12  PHE   B CD2 1 
ATOM   854  C CE1 . PHE   B 1 13 ? 13.199  -15.325 -38.076 1.00 34.71  ? 12  PHE   B CE1 1 
ATOM   855  C CE2 . PHE   B 1 13 ? 12.536  -15.138 -35.779 1.00 33.83  ? 12  PHE   B CE2 1 
ATOM   856  C CZ  . PHE   B 1 13 ? 12.329  -14.838 -37.124 1.00 33.59  ? 12  PHE   B CZ  1 
ATOM   857  N N   . ALA   B 1 14 ? 18.289  -17.101 -33.848 1.00 25.48  ? 13  ALA   B N   1 
ATOM   858  C CA  . ALA   B 1 14 ? 19.325  -17.835 -33.150 1.00 30.37  ? 13  ALA   B CA  1 
ATOM   859  C C   . ALA   B 1 14 ? 18.700  -18.752 -32.104 1.00 27.56  ? 13  ALA   B C   1 
ATOM   860  O O   . ALA   B 1 14 ? 17.754  -18.380 -31.394 1.00 29.20  ? 13  ALA   B O   1 
ATOM   861  C CB  . ALA   B 1 14 ? 20.371  -16.921 -32.536 1.00 27.91  ? 13  ALA   B CB  1 
ATOM   862  N N   . LYS   B 1 15 ? 19.259  -19.956 -32.027 1.00 25.31  ? 14  LYS   B N   1 
ATOM   863  C CA  . LYS   B 1 15 ? 18.635  -21.026 -31.265 1.00 28.13  ? 14  LYS   B CA  1 
ATOM   864  C C   . LYS   B 1 15 ? 19.522  -21.319 -30.067 1.00 32.01  ? 14  LYS   B C   1 
ATOM   865  O O   . LYS   B 1 15 ? 20.705  -21.591 -30.239 1.00 32.01  ? 14  LYS   B O   1 
ATOM   866  C CB  . LYS   B 1 15 ? 18.442  -22.303 -32.106 1.00 30.63  ? 14  LYS   B CB  1 
ATOM   867  C CG  . LYS   B 1 15 ? 17.703  -23.422 -31.314 1.00 29.95  ? 14  LYS   B CG  1 
ATOM   868  C CD  . LYS   B 1 15 ? 16.246  -23.078 -31.010 1.00 34.63  ? 14  LYS   B CD  1 
ATOM   869  C CE  . LYS   B 1 15 ? 15.366  -24.156 -30.326 1.00 35.24  ? 14  LYS   B CE  1 
ATOM   870  N NZ  . LYS   B 1 15 ? 15.907  -24.460 -29.001 1.00 33.49  ? 14  LYS   B NZ  1 
ATOM   871  N N   . MET   B 1 16 ? 18.926  -21.259 -28.872 1.00 31.18  ? 15  MET   B N   1 
ATOM   872  C CA  . MET   B 1 16 ? 19.573  -21.679 -27.641 1.00 36.65  ? 15  MET   B CA  1 
ATOM   873  C C   . MET   B 1 16 ? 18.686  -22.697 -26.928 1.00 33.53  ? 15  MET   B C   1 
ATOM   874  O O   . MET   B 1 16 ? 17.453  -22.604 -26.970 1.00 31.61  ? 15  MET   B O   1 
ATOM   875  C CB  . MET   B 1 16 ? 19.877  -20.486 -26.728 1.00 37.08  ? 15  MET   B CB  1 
ATOM   876  C CG  . MET   B 1 16 ? 20.614  -19.403 -27.463 1.00 44.79  ? 15  MET   B CG  1 
ATOM   877  S SD  . MET   B 1 16 ? 21.961  -18.660 -26.539 1.00 53.63  ? 15  MET   B SD  1 
ATOM   878  C CE  . MET   B 1 16 ? 21.159  -18.004 -25.066 1.00 65.26  ? 15  MET   B CE  1 
ATOM   879  N N   . LYS   B 1 17 ? 19.324  -23.700 -26.315 1.00 35.93  ? 16  LYS   B N   1 
ATOM   880  C CA  . LYS   B 1 17 ? 18.582  -24.695 -25.548 1.00 36.84  ? 16  LYS   B CA  1 
ATOM   881  C C   . LYS   B 1 17 ? 17.644  -23.974 -24.566 1.00 32.10  ? 16  LYS   B C   1 
ATOM   882  O O   . LYS   B 1 17 ? 18.047  -23.022 -23.902 1.00 34.27  ? 16  LYS   B O   1 
ATOM   883  C CB  . LYS   B 1 17 ? 19.598  -25.683 -24.942 1.00 42.68  ? 16  LYS   B CB  1 
ATOM   884  C CG  . LYS   B 1 17 ? 19.032  -26.857 -24.113 1.00 46.67  ? 16  LYS   B CG  1 
ATOM   885  C CD  . LYS   B 1 17 ? 20.025  -27.554 -23.180 1.00 46.09  ? 16  LYS   B CD  1 
ATOM   886  N N   . GLY   B 1 18 ? 16.373  -24.391 -24.527 1.00 34.39  ? 17  GLY   B N   1 
ATOM   887  C CA  . GLY   B 1 18 ? 15.402  -23.856 -23.578 1.00 37.57  ? 17  GLY   B CA  1 
ATOM   888  C C   . GLY   B 1 18 ? 14.538  -22.734 -24.156 1.00 36.60  ? 17  GLY   B C   1 
ATOM   889  O O   . GLY   B 1 18 ? 13.620  -22.280 -23.484 1.00 41.28  ? 17  GLY   B O   1 
ATOM   890  N N   . TYR   B 1 19 ? 14.883  -22.231 -25.359 1.00 33.67  ? 18  TYR   B N   1 
ATOM   891  C CA  . TYR   B 1 19 ? 14.232  -21.047 -25.914 1.00 34.11  ? 18  TYR   B CA  1 
ATOM   892  C C   . TYR   B 1 19 ? 13.823  -21.275 -27.373 1.00 30.70  ? 18  TYR   B C   1 
ATOM   893  O O   . TYR   B 1 19 ? 14.488  -22.004 -28.103 1.00 34.72  ? 18  TYR   B O   1 
ATOM   894  C CB  . TYR   B 1 19 ? 15.185  -19.842 -25.883 1.00 35.28  ? 18  TYR   B CB  1 
ATOM   895  C CG  . TYR   B 1 19 ? 15.716  -19.480 -24.500 1.00 39.54  ? 18  TYR   B CG  1 
ATOM   896  C CD1 . TYR   B 1 19 ? 15.057  -18.560 -23.686 1.00 38.77  ? 18  TYR   B CD1 1 
ATOM   897  C CD2 . TYR   B 1 19 ? 16.864  -20.085 -23.995 1.00 42.51  ? 18  TYR   B CD2 1 
ATOM   898  C CE1 . TYR   B 1 19 ? 15.536  -18.249 -22.419 1.00 39.73  ? 18  TYR   B CE1 1 
ATOM   899  C CE2 . TYR   B 1 19 ? 17.363  -19.765 -22.739 1.00 44.54  ? 18  TYR   B CE2 1 
ATOM   900  C CZ  . TYR   B 1 19 ? 16.688  -18.860 -21.941 1.00 41.64  ? 18  TYR   B CZ  1 
ATOM   901  O OH  . TYR   B 1 19 ? 17.212  -18.558 -20.715 1.00 44.24  ? 18  TYR   B OH  1 
ATOM   902  N N   . PRO   B 1 20 ? 12.764  -20.624 -27.891 1.00 28.30  ? 19  PRO   B N   1 
ATOM   903  C CA  . PRO   B 1 20 ? 12.446  -20.740 -29.317 1.00 28.68  ? 19  PRO   B CA  1 
ATOM   904  C C   . PRO   B 1 20 ? 13.521  -20.013 -30.133 1.00 29.33  ? 19  PRO   B C   1 
ATOM   905  O O   . PRO   B 1 20 ? 14.217  -19.141 -29.609 1.00 29.98  ? 19  PRO   B O   1 
ATOM   906  C CB  . PRO   B 1 20 ? 11.080  -20.060 -29.423 1.00 28.15  ? 19  PRO   B CB  1 
ATOM   907  C CG  . PRO   B 1 20 ? 11.117  -19.014 -28.327 1.00 29.62  ? 19  PRO   B CG  1 
ATOM   908  C CD  . PRO   B 1 20 ? 11.862  -19.708 -27.166 1.00 30.61  ? 19  PRO   B CD  1 
ATOM   909  N N   . HIS   B 1 21 ? 13.711  -20.428 -31.388 1.00 27.61  ? 20  HIS   B N   1 
ATOM   910  C CA  . HIS   B 1 21 ? 14.510  -19.649 -32.349 1.00 29.27  ? 20  HIS   B CA  1 
ATOM   911  C C   . HIS   B 1 21 ? 14.251  -18.153 -32.179 1.00 28.27  ? 20  HIS   B C   1 
ATOM   912  O O   . HIS   B 1 21 ? 13.104  -17.717 -32.258 1.00 28.85  ? 20  HIS   B O   1 
ATOM   913  C CB  . HIS   B 1 21 ? 14.143  -20.083 -33.770 1.00 27.70  ? 20  HIS   B CB  1 
ATOM   914  C CG  . HIS   B 1 21 ? 14.319  -21.563 -33.963 1.00 31.03  ? 20  HIS   B CG  1 
ATOM   915  N ND1 . HIS   B 1 21 ? 13.442  -22.515 -33.462 1.00 31.09  ? 20  HIS   B ND1 1 
ATOM   916  C CD2 . HIS   B 1 21 ? 15.346  -22.249 -34.528 1.00 31.43  ? 20  HIS   B CD2 1 
ATOM   917  C CE1 . HIS   B 1 21 ? 13.905  -23.732 -33.779 1.00 33.61  ? 20  HIS   B CE1 1 
ATOM   918  N NE2 . HIS   B 1 21 ? 15.053  -23.588 -34.433 1.00 31.09  ? 20  HIS   B NE2 1 
ATOM   919  N N   . TRP   B 1 22 ? 15.302  -17.362 -31.930 1.00 29.33  ? 21  TRP   B N   1 
ATOM   920  C CA  . TRP   B 1 22 ? 15.060  -16.025 -31.393 1.00 29.40  ? 21  TRP   B CA  1 
ATOM   921  C C   . TRP   B 1 22 ? 15.562  -14.943 -32.357 1.00 28.33  ? 21  TRP   B C   1 
ATOM   922  O O   . TRP   B 1 22 ? 16.671  -15.058 -32.869 1.00 29.31  ? 21  TRP   B O   1 
ATOM   923  C CB  . TRP   B 1 22 ? 15.765  -15.903 -30.038 1.00 28.30  ? 21  TRP   B CB  1 
ATOM   924  C CG  . TRP   B 1 22 ? 15.244  -14.740 -29.221 1.00 31.53  ? 21  TRP   B CG  1 
ATOM   925  C CD1 . TRP   B 1 22 ? 15.553  -13.405 -29.341 1.00 27.51  ? 21  TRP   B CD1 1 
ATOM   926  C CD2 . TRP   B 1 22 ? 14.294  -14.843 -28.134 1.00 29.69  ? 21  TRP   B CD2 1 
ATOM   927  N NE1 . TRP   B 1 22 ? 14.841  -12.683 -28.408 1.00 30.10  ? 21  TRP   B NE1 1 
ATOM   928  C CE2 . TRP   B 1 22 ? 14.088  -13.538 -27.638 1.00 29.03  ? 21  TRP   B CE2 1 
ATOM   929  C CE3 . TRP   B 1 22 ? 13.633  -15.923 -27.527 1.00 31.92  ? 21  TRP   B CE3 1 
ATOM   930  C CZ2 . TRP   B 1 22 ? 13.224  -13.283 -26.574 1.00 30.13  ? 21  TRP   B CZ2 1 
ATOM   931  C CZ3 . TRP   B 1 22 ? 12.813  -15.681 -26.446 1.00 29.66  ? 21  TRP   B CZ3 1 
ATOM   932  C CH2 . TRP   B 1 22 ? 12.593  -14.372 -26.004 1.00 30.91  ? 21  TRP   B CH2 1 
ATOM   933  N N   . PRO   B 1 23 ? 14.790  -13.867 -32.652 1.00 29.92  ? 22  PRO   B N   1 
ATOM   934  C CA  . PRO   B 1 23 ? 15.255  -12.814 -33.574 1.00 28.56  ? 22  PRO   B CA  1 
ATOM   935  C C   . PRO   B 1 23 ? 16.545  -12.220 -33.031 1.00 27.91  ? 22  PRO   B C   1 
ATOM   936  O O   . PRO   B 1 23 ? 16.654  -11.897 -31.857 1.00 30.32  ? 22  PRO   B O   1 
ATOM   937  C CB  . PRO   B 1 23 ? 14.089  -11.781 -33.608 1.00 30.76  ? 22  PRO   B CB  1 
ATOM   938  C CG  . PRO   B 1 23 ? 13.298  -12.110 -32.331 1.00 32.14  ? 22  PRO   B CG  1 
ATOM   939  C CD  . PRO   B 1 23 ? 13.424  -13.629 -32.180 1.00 28.21  ? 22  PRO   B CD  1 
ATOM   940  N N   . ALA   B 1 24 ? 17.578  -12.177 -33.871 1.00 26.11  ? 23  ALA   B N   1 
ATOM   941  C CA  . ALA   B 1 24 ? 18.889  -11.775 -33.399 1.00 24.27  ? 23  ALA   B CA  1 
ATOM   942  C C   . ALA   B 1 24 ? 19.681  -11.229 -34.593 1.00 27.12  ? 23  ALA   B C   1 
ATOM   943  O O   . ALA   B 1 24 ? 19.220  -11.292 -35.744 1.00 31.18  ? 23  ALA   B O   1 
ATOM   944  C CB  . ALA   B 1 24 ? 19.605  -12.955 -32.782 1.00 25.88  ? 23  ALA   B CB  1 
ATOM   945  N N   . ARG   B 1 25 ? 20.873  -10.709 -34.293 1.00 27.78  ? 24  ARG   B N   1 
ATOM   946  C CA  . ARG   B 1 25 ? 21.768  -10.204 -35.323 1.00 33.50  ? 24  ARG   B CA  1 
ATOM   947  C C   . ARG   B 1 25 ? 23.187  -10.636 -34.982 1.00 33.81  ? 24  ARG   B C   1 
ATOM   948  O O   . ARG   B 1 25 ? 23.484  -10.934 -33.831 1.00 33.40  ? 24  ARG   B O   1 
ATOM   949  C CB  . ARG   B 1 25 ? 21.722  -8.685  -35.474 1.00 33.72  ? 24  ARG   B CB  1 
ATOM   950  C CG  . ARG   B 1 25 ? 22.472  -7.960  -34.364 1.00 35.81  ? 24  ARG   B CG  1 
ATOM   951  C CD  . ARG   B 1 25 ? 22.152  -6.486  -34.380 1.00 32.42  ? 24  ARG   B CD  1 
ATOM   952  N NE  . ARG   B 1 25 ? 22.867  -5.756  -33.332 1.00 32.53  ? 24  ARG   B NE  1 
ATOM   953  C CZ  . ARG   B 1 25 ? 22.528  -4.526  -32.935 1.00 35.14  ? 24  ARG   B CZ  1 
ATOM   954  N NH1 . ARG   B 1 25 ? 21.591  -3.865  -33.589 1.00 31.71  ? 24  ARG   B NH1 1 
ATOM   955  N NH2 . ARG   B 1 25 ? 23.138  -3.969  -31.902 1.00 30.44  ? 24  ARG   B NH2 1 
ATOM   956  N N   . ILE   B 1 26 ? 24.037  -10.707 -36.020 1.00 34.38  ? 25  ILE   B N   1 
ATOM   957  C CA  . ILE   B 1 26 ? 25.462  -10.873 -35.835 1.00 34.31  ? 25  ILE   B CA  1 
ATOM   958  C C   . ILE   B 1 26 ? 26.007  -9.485  -35.509 1.00 36.55  ? 25  ILE   B C   1 
ATOM   959  O O   . ILE   B 1 26 ? 25.761  -8.551  -36.272 1.00 35.27  ? 25  ILE   B O   1 
ATOM   960  C CB  . ILE   B 1 26 ? 26.118  -11.379 -37.135 1.00 34.81  ? 25  ILE   B CB  1 
ATOM   961  C CG1 . ILE   B 1 26 ? 25.417  -12.607 -37.700 1.00 29.80  ? 25  ILE   B CG1 1 
ATOM   962  C CG2 . ILE   B 1 26 ? 27.623  -11.581 -36.937 1.00 38.75  ? 25  ILE   B CG2 1 
ATOM   963  C CD1 . ILE   B 1 26 ? 25.579  -13.848 -36.829 1.00 28.53  ? 25  ILE   B CD1 1 
ATOM   964  N N   . ASP   B 1 27 ? 26.793  -9.393  -34.431 1.00 37.45  ? 26  ASP   B N   1 
ATOM   965  C CA  . ASP   B 1 27 ? 27.453  -8.148  -34.038 1.00 46.16  ? 26  ASP   B CA  1 
ATOM   966  C C   . ASP   B 1 27 ? 28.888  -8.085  -34.557 1.00 47.25  ? 26  ASP   B C   1 
ATOM   967  O O   . ASP   B 1 27 ? 29.459  -9.111  -34.920 1.00 44.09  ? 26  ASP   B O   1 
ATOM   968  C CB  . ASP   B 1 27 ? 27.473  -7.987  -32.525 1.00 39.82  ? 26  ASP   B CB  1 
ATOM   969  C CG  . ASP   B 1 27 ? 26.244  -7.300  -31.960 1.00 42.93  ? 26  ASP   B CG  1 
ATOM   970  O OD1 . ASP   B 1 27 ? 25.405  -6.854  -32.778 1.00 44.79  ? 26  ASP   B OD1 1 
ATOM   971  O OD2 . ASP   B 1 27 ? 26.152  -7.198  -30.720 1.00 37.73  ? 26  ASP   B OD2 1 
ATOM   972  N N   A ASP   B 1 28 ? 29.441  -6.861  -34.563 0.50 53.20  ? 27  ASP   B N   1 
ATOM   973  N N   B ASP   B 1 28 ? 29.458  -6.874  -34.596 0.50 52.78  ? 27  ASP   B N   1 
ATOM   974  C CA  A ASP   B 1 28 ? 30.854  -6.588  -34.788 0.50 59.69  ? 27  ASP   B CA  1 
ATOM   975  C CA  B ASP   B 1 28 ? 30.881  -6.738  -34.865 0.50 58.93  ? 27  ASP   B CA  1 
ATOM   976  C C   A ASP   B 1 28 ? 31.623  -7.005  -33.531 0.50 65.90  ? 27  ASP   B C   1 
ATOM   977  C C   B ASP   B 1 28 ? 31.631  -6.984  -33.557 0.50 65.73  ? 27  ASP   B C   1 
ATOM   978  O O   A ASP   B 1 28 ? 31.030  -7.085  -32.455 0.50 69.28  ? 27  ASP   B O   1 
ATOM   979  O O   B ASP   B 1 28 ? 31.037  -6.909  -32.481 0.50 70.09  ? 27  ASP   B O   1 
ATOM   980  C CB  A ASP   B 1 28 ? 31.061  -5.121  -35.143 0.50 53.96  ? 27  ASP   B CB  1 
ATOM   981  C CB  B ASP   B 1 28 ? 31.221  -5.414  -35.530 0.50 53.43  ? 27  ASP   B CB  1 
ATOM   982  C CG  A ASP   B 1 28 ? 29.864  -4.423  -35.782 0.50 51.37  ? 27  ASP   B CG  1 
ATOM   983  C CG  B ASP   B 1 28 ? 32.053  -5.538  -36.798 0.50 49.44  ? 27  ASP   B CG  1 
ATOM   984  O OD1 A ASP   B 1 28 ? 29.898  -4.171  -37.015 0.50 49.32  ? 27  ASP   B OD1 1 
ATOM   985  O OD1 B ASP   B 1 28 ? 33.000  -6.355  -36.808 0.50 49.59  ? 27  ASP   B OD1 1 
ATOM   986  O OD2 A ASP   B 1 28 ? 28.905  -4.120  -35.041 0.50 42.38  ? 27  ASP   B OD2 1 
ATOM   987  O OD2 B ASP   B 1 28 ? 31.736  -4.827  -37.771 0.50 45.78  ? 27  ASP   B OD2 1 
ATOM   988  N N   . ILE   B 1 29 ? 32.930  -7.288  -33.668 1.00 67.51  ? 28  ILE   B N   1 
ATOM   989  C CA  . ILE   B 1 29 ? 33.738  -7.732  -32.537 1.00 74.54  ? 28  ILE   B CA  1 
ATOM   990  C C   . ILE   B 1 29 ? 34.037  -6.547  -31.621 1.00 89.73  ? 28  ILE   B C   1 
ATOM   991  O O   . ILE   B 1 29 ? 34.202  -6.726  -30.417 1.00 102.65 ? 28  ILE   B O   1 
ATOM   992  C CB  . ILE   B 1 29 ? 35.018  -8.470  -32.977 1.00 64.45  ? 28  ILE   B CB  1 
ATOM   993  N N   . ALA   B 1 30 ? 34.075  -5.340  -32.207 1.00 92.67  ? 29  ALA   B N   1 
ATOM   994  C CA  . ALA   B 1 30 ? 34.345  -4.096  -31.500 1.00 94.46  ? 29  ALA   B CA  1 
ATOM   995  C C   . ALA   B 1 30 ? 35.720  -4.160  -30.825 1.00 93.55  ? 29  ALA   B C   1 
ATOM   996  O O   . ALA   B 1 30 ? 36.509  -3.213  -31.051 1.00 97.20  ? 29  ALA   B O   1 
ATOM   997  C CB  . ALA   B 1 30 ? 33.234  -3.768  -30.517 1.00 92.65  ? 29  ALA   B CB  1 
ATOM   998  N N   . LYS   B 1 35 ? 36.905  -11.945 -27.583 1.00 87.65  ? 34  LYS   B N   1 
ATOM   999  C CA  . LYS   B 1 35 ? 36.765  -12.435 -28.987 1.00 80.60  ? 34  LYS   B CA  1 
ATOM   1000 C C   . LYS   B 1 35 ? 36.050  -13.792 -28.994 1.00 77.44  ? 34  LYS   B C   1 
ATOM   1001 O O   . LYS   B 1 35 ? 36.222  -14.589 -28.071 1.00 74.80  ? 34  LYS   B O   1 
ATOM   1002 C CB  . LYS   B 1 35 ? 38.125  -12.435 -29.699 1.00 69.40  ? 34  LYS   B CB  1 
ATOM   1003 N N   . PRO   B 1 36 ? 35.197  -14.105 -30.009 1.00 76.19  ? 35  PRO   B N   1 
ATOM   1004 C CA  . PRO   B 1 36 ? 34.473  -15.386 -30.040 1.00 60.85  ? 35  PRO   B CA  1 
ATOM   1005 C C   . PRO   B 1 36 ? 35.350  -16.626 -29.871 1.00 55.13  ? 35  PRO   B C   1 
ATOM   1006 O O   . PRO   B 1 36 ? 36.530  -16.582 -30.204 1.00 63.25  ? 35  PRO   B O   1 
ATOM   1007 C CB  . PRO   B 1 36 ? 33.742  -15.366 -31.400 1.00 64.89  ? 35  PRO   B CB  1 
ATOM   1008 C CG  . PRO   B 1 36 ? 34.378  -14.227 -32.185 1.00 65.73  ? 35  PRO   B CG  1 
ATOM   1009 C CD  . PRO   B 1 36 ? 34.860  -13.230 -31.148 1.00 69.26  ? 35  PRO   B CD  1 
ATOM   1010 N N   . PRO   B 1 37 ? 34.838  -17.764 -29.330 1.00 53.84  ? 36  PRO   B N   1 
ATOM   1011 C CA  . PRO   B 1 37 ? 35.574  -19.028 -29.386 1.00 54.93  ? 36  PRO   B CA  1 
ATOM   1012 C C   . PRO   B 1 37 ? 35.652  -19.394 -30.868 1.00 65.29  ? 36  PRO   B C   1 
ATOM   1013 O O   . PRO   B 1 37 ? 34.910  -18.826 -31.672 1.00 65.45  ? 36  PRO   B O   1 
ATOM   1014 C CB  . PRO   B 1 37 ? 34.743  -20.037 -28.568 1.00 53.22  ? 36  PRO   B CB  1 
ATOM   1015 C CG  . PRO   B 1 37 ? 33.651  -19.219 -27.898 1.00 54.51  ? 36  PRO   B CG  1 
ATOM   1016 C CD  . PRO   B 1 37 ? 33.542  -17.897 -28.647 1.00 53.79  ? 36  PRO   B CD  1 
ATOM   1017 N N   . PRO   B 1 38 ? 36.550  -20.316 -31.304 1.00 69.94  ? 37  PRO   B N   1 
ATOM   1018 C CA  . PRO   B 1 38 ? 36.640  -20.672 -32.729 1.00 70.86  ? 37  PRO   B CA  1 
ATOM   1019 C C   . PRO   B 1 38 ? 35.303  -21.119 -33.343 1.00 61.57  ? 37  PRO   B C   1 
ATOM   1020 O O   . PRO   B 1 38 ? 34.534  -21.841 -32.701 1.00 59.16  ? 37  PRO   B O   1 
ATOM   1021 C CB  . PRO   B 1 38 ? 37.716  -21.793 -32.759 1.00 68.91  ? 37  PRO   B CB  1 
ATOM   1022 C CG  . PRO   B 1 38 ? 38.509  -21.607 -31.480 1.00 65.49  ? 37  PRO   B CG  1 
ATOM   1023 C CD  . PRO   B 1 38 ? 37.514  -21.052 -30.464 1.00 71.57  ? 37  PRO   B CD  1 
ATOM   1024 N N   . ASN   B 1 39 ? 35.020  -20.659 -34.575 1.00 53.99  ? 38  ASN   B N   1 
ATOM   1025 C CA  . ASN   B 1 39 ? 33.846  -21.082 -35.340 1.00 57.21  ? 38  ASN   B CA  1 
ATOM   1026 C C   . ASN   B 1 39 ? 32.539  -20.412 -34.885 1.00 52.58  ? 38  ASN   B C   1 
ATOM   1027 O O   . ASN   B 1 39 ? 31.496  -20.661 -35.464 1.00 51.13  ? 38  ASN   B O   1 
ATOM   1028 C CB  . ASN   B 1 39 ? 33.596  -22.585 -35.216 1.00 61.76  ? 38  ASN   B CB  1 
ATOM   1029 C CG  . ASN   B 1 39 ? 34.821  -23.418 -35.520 1.00 66.69  ? 38  ASN   B CG  1 
ATOM   1030 O OD1 . ASN   B 1 39 ? 35.193  -24.276 -34.713 1.00 69.37  ? 38  ASN   B OD1 1 
ATOM   1031 N ND2 . ASN   B 1 39 ? 35.457  -23.184 -36.663 1.00 59.04  ? 38  ASN   B ND2 1 
ATOM   1032 N N   . LYS   B 1 40 ? 32.568  -19.570 -33.845 1.00 53.43  ? 39  LYS   B N   1 
ATOM   1033 C CA  . LYS   B 1 40 ? 31.345  -19.036 -33.270 1.00 44.73  ? 39  LYS   B CA  1 
ATOM   1034 C C   . LYS   B 1 40 ? 31.261  -17.544 -33.547 1.00 44.17  ? 39  LYS   B C   1 
ATOM   1035 O O   . LYS   B 1 40 ? 32.246  -16.936 -33.917 1.00 43.31  ? 39  LYS   B O   1 
ATOM   1036 C CB  . LYS   B 1 40 ? 31.345  -19.348 -31.777 1.00 43.10  ? 39  LYS   B CB  1 
ATOM   1037 C CG  . LYS   B 1 40 ? 31.265  -20.830 -31.472 1.00 42.36  ? 39  LYS   B CG  1 
ATOM   1038 C CD  . LYS   B 1 40 ? 30.862  -21.004 -30.015 1.00 47.86  ? 39  LYS   B CD  1 
ATOM   1039 C CE  . LYS   B 1 40 ? 29.865  -22.096 -29.734 1.00 63.00  ? 39  LYS   B CE  1 
ATOM   1040 N NZ  . LYS   B 1 40 ? 30.381  -23.383 -29.260 1.00 68.11  ? 39  LYS   B NZ  1 
ATOM   1041 N N   . TYR   B 1 41 ? 30.066  -16.966 -33.421 1.00 43.28  ? 40  TYR   B N   1 
ATOM   1042 C CA  . TYR   B 1 41 ? 29.888  -15.558 -33.744 1.00 41.50  ? 40  TYR   B CA  1 
ATOM   1043 C C   . TYR   B 1 41 ? 29.248  -14.846 -32.555 1.00 39.69  ? 40  TYR   B C   1 
ATOM   1044 O O   . TYR   B 1 41 ? 28.488  -15.462 -31.797 1.00 34.50  ? 40  TYR   B O   1 
ATOM   1045 C CB  . TYR   B 1 41 ? 28.932  -15.339 -34.920 1.00 40.55  ? 40  TYR   B CB  1 
ATOM   1046 C CG  . TYR   B 1 41 ? 29.368  -15.843 -36.290 1.00 40.69  ? 40  TYR   B CG  1 
ATOM   1047 C CD1 . TYR   B 1 41 ? 30.049  -15.010 -37.175 1.00 39.10  ? 40  TYR   B CD1 1 
ATOM   1048 C CD2 . TYR   B 1 41 ? 29.049  -17.130 -36.712 1.00 36.11  ? 40  TYR   B CD2 1 
ATOM   1049 C CE1 . TYR   B 1 41 ? 30.443  -15.461 -38.425 1.00 43.00  ? 40  TYR   B CE1 1 
ATOM   1050 C CE2 . TYR   B 1 41 ? 29.433  -17.591 -37.959 1.00 38.88  ? 40  TYR   B CE2 1 
ATOM   1051 C CZ  . TYR   B 1 41 ? 30.122  -16.751 -38.824 1.00 43.84  ? 40  TYR   B CZ  1 
ATOM   1052 O OH  . TYR   B 1 41 ? 30.483  -17.198 -40.065 1.00 42.12  ? 40  TYR   B OH  1 
ATOM   1053 N N   . PRO   B 1 42 ? 29.515  -13.529 -32.384 1.00 44.30  ? 41  PRO   B N   1 
ATOM   1054 C CA  . PRO   B 1 42 ? 28.829  -12.740 -31.371 1.00 36.29  ? 41  PRO   B CA  1 
ATOM   1055 C C   . PRO   B 1 42 ? 27.399  -12.544 -31.845 1.00 36.31  ? 41  PRO   B C   1 
ATOM   1056 O O   . PRO   B 1 42 ? 27.146  -11.968 -32.913 1.00 37.20  ? 41  PRO   B O   1 
ATOM   1057 C CB  . PRO   B 1 42 ? 29.617  -11.425 -31.280 1.00 40.45  ? 41  PRO   B CB  1 
ATOM   1058 C CG  . PRO   B 1 42 ? 30.387  -11.321 -32.582 1.00 38.82  ? 41  PRO   B CG  1 
ATOM   1059 C CD  . PRO   B 1 42 ? 30.521  -12.739 -33.120 1.00 44.64  ? 41  PRO   B CD  1 
ATOM   1060 N N   . ILE   B 1 43 ? 26.471  -13.018 -31.007 1.00 32.46  ? 42  ILE   B N   1 
ATOM   1061 C CA  . ILE   B 1 43 ? 25.050  -12.857 -31.283 1.00 33.02  ? 42  ILE   B CA  1 
ATOM   1062 C C   . ILE   B 1 43 ? 24.436  -11.821 -30.341 1.00 30.91  ? 42  ILE   B C   1 
ATOM   1063 O O   . ILE   B 1 43 ? 24.784  -11.809 -29.173 1.00 32.94  ? 42  ILE   B O   1 
ATOM   1064 C CB  . ILE   B 1 43 ? 24.364  -14.211 -31.102 1.00 28.22  ? 42  ILE   B CB  1 
ATOM   1065 C CG1 . ILE   B 1 43 ? 25.091  -15.266 -31.964 1.00 28.39  ? 42  ILE   B CG1 1 
ATOM   1066 C CG2 . ILE   B 1 43 ? 22.887  -14.054 -31.475 1.00 25.14  ? 42  ILE   B CG2 1 
ATOM   1067 C CD1 . ILE   B 1 43 ? 25.228  -14.900 -33.432 1.00 28.38  ? 42  ILE   B CD1 1 
ATOM   1068 N N   . PHE   B 1 44 ? 23.572  -10.944 -30.882 1.00 34.59  ? 43  PHE   B N   1 
ATOM   1069 C CA  . PHE   B 1 44 ? 22.810  -9.965  -30.114 1.00 32.67  ? 43  PHE   B CA  1 
ATOM   1070 C C   . PHE   B 1 44 ? 21.340  -10.329 -30.291 1.00 33.63  ? 43  PHE   B C   1 
ATOM   1071 O O   . PHE   B 1 44 ? 20.831  -10.328 -31.409 1.00 31.43  ? 43  PHE   B O   1 
ATOM   1072 C CB  . PHE   B 1 44 ? 23.080  -8.516  -30.528 1.00 32.89  ? 43  PHE   B CB  1 
ATOM   1073 C CG  . PHE   B 1 44 ? 22.161  -7.489  -29.868 1.00 32.69  ? 43  PHE   B CG  1 
ATOM   1074 C CD1 . PHE   B 1 44 ? 20.974  -7.084  -30.484 1.00 34.47  ? 43  PHE   B CD1 1 
ATOM   1075 C CD2 . PHE   B 1 44 ? 22.473  -6.946  -28.627 1.00 36.39  ? 43  PHE   B CD2 1 
ATOM   1076 C CE1 . PHE   B 1 44 ? 20.129  -6.160  -29.883 1.00 32.48  ? 43  PHE   B CE1 1 
ATOM   1077 C CE2 . PHE   B 1 44 ? 21.619  -6.027  -28.017 1.00 34.35  ? 43  PHE   B CE2 1 
ATOM   1078 C CZ  . PHE   B 1 44 ? 20.465  -5.629  -28.645 1.00 34.00  ? 43  PHE   B CZ  1 
ATOM   1079 N N   . PHE   B 1 45 ? 20.669  -10.653 -29.177 1.00 31.94  ? 44  PHE   B N   1 
ATOM   1080 C CA  . PHE   B 1 45 ? 19.256  -10.995 -29.185 1.00 28.73  ? 44  PHE   B CA  1 
ATOM   1081 C C   . PHE   B 1 45 ? 18.405  -9.735  -29.054 1.00 31.70  ? 44  PHE   B C   1 
ATOM   1082 O O   . PHE   B 1 45 ? 18.451  -9.065  -28.022 1.00 30.38  ? 44  PHE   B O   1 
ATOM   1083 C CB  . PHE   B 1 45 ? 18.930  -11.960 -28.039 1.00 29.77  ? 44  PHE   B CB  1 
ATOM   1084 C CG  . PHE   B 1 45 ? 19.626  -13.300 -28.216 1.00 29.55  ? 44  PHE   B CG  1 
ATOM   1085 C CD1 . PHE   B 1 45 ? 20.902  -13.511 -27.719 1.00 32.89  ? 44  PHE   B CD1 1 
ATOM   1086 C CD2 . PHE   B 1 45 ? 19.007  -14.334 -28.919 1.00 31.11  ? 44  PHE   B CD2 1 
ATOM   1087 C CE1 . PHE   B 1 45 ? 21.549  -14.714 -27.931 1.00 32.49  ? 44  PHE   B CE1 1 
ATOM   1088 C CE2 . PHE   B 1 45 ? 19.640  -15.554 -29.090 1.00 31.24  ? 44  PHE   B CE2 1 
ATOM   1089 C CZ  . PHE   B 1 45 ? 20.910  -15.736 -28.598 1.00 33.46  ? 44  PHE   B CZ  1 
ATOM   1090 N N   . PHE   B 1 46 ? 17.587  -9.474  -30.090 1.00 26.68  ? 45  PHE   B N   1 
ATOM   1091 C CA  . PHE   B 1 46 ? 16.586  -8.425  -30.042 1.00 28.70  ? 45  PHE   B CA  1 
ATOM   1092 C C   . PHE   B 1 46 ? 15.623  -8.681  -28.873 1.00 33.03  ? 45  PHE   B C   1 
ATOM   1093 O O   . PHE   B 1 46 ? 15.375  -9.838  -28.480 1.00 28.65  ? 45  PHE   B O   1 
ATOM   1094 C CB  . PHE   B 1 46 ? 15.858  -8.288  -31.381 1.00 25.12  ? 45  PHE   B CB  1 
ATOM   1095 C CG  . PHE   B 1 46 ? 16.758  -7.816  -32.525 1.00 31.40  ? 45  PHE   B CG  1 
ATOM   1096 C CD1 . PHE   B 1 46 ? 17.244  -6.500  -32.568 1.00 34.90  ? 45  PHE   B CD1 1 
ATOM   1097 C CD2 . PHE   B 1 46 ? 17.134  -8.693  -33.547 1.00 30.19  ? 45  PHE   B CD2 1 
ATOM   1098 C CE1 . PHE   B 1 46 ? 18.083  -6.071  -33.592 1.00 31.15  ? 45  PHE   B CE1 1 
ATOM   1099 C CE2 . PHE   B 1 46 ? 17.968  -8.259  -34.583 1.00 32.06  ? 45  PHE   B CE2 1 
ATOM   1100 C CZ  . PHE   B 1 46 ? 18.434  -6.957  -34.601 1.00 30.31  ? 45  PHE   B CZ  1 
ATOM   1101 N N   . GLY   B 1 47 ? 15.036  -7.588  -28.350 1.00 33.65  ? 46  GLY   B N   1 
ATOM   1102 C CA  . GLY   B 1 47 ? 14.049  -7.702  -27.283 1.00 33.85  ? 46  GLY   B CA  1 
ATOM   1103 C C   . GLY   B 1 47 ? 14.738  -7.804  -25.923 1.00 36.05  ? 46  GLY   B C   1 
ATOM   1104 O O   . GLY   B 1 47 ? 14.672  -6.889  -25.127 1.00 36.92  ? 46  GLY   B O   1 
ATOM   1105 N N   . THR   B 1 48 ? 15.435  -8.904  -25.668 1.00 35.67  ? 47  THR   B N   1 
ATOM   1106 C CA  . THR   B 1 48 ? 16.141  -9.049  -24.412 1.00 34.96  ? 47  THR   B CA  1 
ATOM   1107 C C   . THR   B 1 48 ? 17.437  -8.257  -24.438 1.00 35.98  ? 47  THR   B C   1 
ATOM   1108 O O   . THR   B 1 48 ? 17.973  -7.934  -23.386 1.00 34.71  ? 47  THR   B O   1 
ATOM   1109 C CB  . THR   B 1 48 ? 16.389  -10.525 -24.092 1.00 35.31  ? 47  THR   B CB  1 
ATOM   1110 O OG1 . THR   B 1 48 ? 17.394  -11.005 -24.982 1.00 34.70  ? 47  THR   B OG1 1 
ATOM   1111 C CG2 . THR   B 1 48 ? 15.104  -11.342 -24.114 1.00 32.82  ? 47  THR   B CG2 1 
ATOM   1112 N N   . HIS   B 1 49 ? 17.988  -8.024  -25.632 1.00 31.00  ? 48  HIS   B N   1 
ATOM   1113 C CA  . HIS   B 1 49 ? 19.228  -7.272  -25.750 1.00 36.25  ? 48  HIS   B CA  1 
ATOM   1114 C C   . HIS   B 1 49 ? 20.360  -7.982  -25.020 1.00 36.98  ? 48  HIS   B C   1 
ATOM   1115 O O   . HIS   B 1 49 ? 21.311  -7.318  -24.632 1.00 41.64  ? 48  HIS   B O   1 
ATOM   1116 C CB  . HIS   B 1 49 ? 19.123  -5.808  -25.273 1.00 33.88  ? 48  HIS   B CB  1 
ATOM   1117 C CG  . HIS   B 1 49 ? 17.926  -5.086  -25.779 1.00 34.90  ? 48  HIS   B CG  1 
ATOM   1118 N ND1 . HIS   B 1 49 ? 17.175  -4.286  -24.945 1.00 37.89  ? 48  HIS   B ND1 1 
ATOM   1119 C CD2 . HIS   B 1 49 ? 17.306  -5.056  -26.985 1.00 33.76  ? 48  HIS   B CD2 1 
ATOM   1120 C CE1 . HIS   B 1 49 ? 16.146  -3.776  -25.632 1.00 41.84  ? 48  HIS   B CE1 1 
ATOM   1121 N NE2 . HIS   B 1 49 ? 16.197  -4.237  -26.878 1.00 40.75  ? 48  HIS   B NE2 1 
ATOM   1122 N N   . GLU   B 1 50 ? 20.296  -9.313  -24.895 1.00 32.52  ? 49  GLU   B N   1 
ATOM   1123 C CA  . GLU   B 1 50 ? 21.414  -10.062 -24.316 1.00 37.30  ? 49  GLU   B CA  1 
ATOM   1124 C C   . GLU   B 1 50 ? 22.321  -10.550 -25.455 1.00 37.08  ? 49  GLU   B C   1 
ATOM   1125 O O   . GLU   B 1 50 ? 21.981  -10.403 -26.637 1.00 32.52  ? 49  GLU   B O   1 
ATOM   1126 C CB  . GLU   B 1 50 ? 20.941  -11.315 -23.579 1.00 41.95  ? 49  GLU   B CB  1 
ATOM   1127 C CG  . GLU   B 1 50 ? 20.034  -11.038 -22.385 1.00 51.68  ? 49  GLU   B CG  1 
ATOM   1128 C CD  . GLU   B 1 50 ? 19.285  -12.321 -22.035 1.00 65.09  ? 49  GLU   B CD  1 
ATOM   1129 O OE1 . GLU   B 1 50 ? 18.590  -12.838 -22.939 1.00 77.82  ? 49  GLU   B OE1 1 
ATOM   1130 O OE2 . GLU   B 1 50 ? 19.369  -12.814 -20.891 1.00 65.43  ? 49  GLU   B OE2 1 
ATOM   1131 N N   . THR   B 1 51 ? 23.461  -11.150 -25.098 1.00 34.49  ? 50  THR   B N   1 
ATOM   1132 C CA  . THR   B 1 51 ? 24.411  -11.629 -26.092 1.00 36.34  ? 50  THR   B CA  1 
ATOM   1133 C C   . THR   B 1 51 ? 24.786  -13.067 -25.763 1.00 42.31  ? 50  THR   B C   1 
ATOM   1134 O O   . THR   B 1 51 ? 24.589  -13.518 -24.639 1.00 42.85  ? 50  THR   B O   1 
ATOM   1135 C CB  . THR   B 1 51 ? 25.627  -10.703 -26.247 1.00 36.96  ? 50  THR   B CB  1 
ATOM   1136 O OG1 . THR   B 1 51 ? 26.146  -10.514 -24.942 1.00 40.36  ? 50  THR   B OG1 1 
ATOM   1137 C CG2 . THR   B 1 51 ? 25.281  -9.291  -26.671 1.00 37.51  ? 50  THR   B CG2 1 
ATOM   1138 N N   . ALA   B 1 52 ? 25.248  -13.798 -26.787 1.00 41.83  ? 51  ALA   B N   1 
ATOM   1139 C CA  . ALA   B 1 52 ? 25.943  -15.061 -26.615 1.00 39.91  ? 51  ALA   B CA  1 
ATOM   1140 C C   . ALA   B 1 52 ? 26.856  -15.292 -27.815 1.00 35.96  ? 51  ALA   B C   1 
ATOM   1141 O O   . ALA   B 1 52 ? 26.833  -14.528 -28.791 1.00 37.00  ? 51  ALA   B O   1 
ATOM   1142 C CB  . ALA   B 1 52 ? 24.988  -16.220 -26.366 1.00 39.14  ? 51  ALA   B CB  1 
ATOM   1143 N N   . PHE   B 1 53 ? 27.734  -16.290 -27.679 1.00 34.88  ? 52  PHE   B N   1 
ATOM   1144 C CA  . PHE   B 1 53 ? 28.494  -16.793 -28.814 1.00 39.39  ? 52  PHE   B CA  1 
ATOM   1145 C C   . PHE   B 1 53 ? 27.819  -18.079 -29.307 1.00 41.04  ? 52  PHE   B C   1 
ATOM   1146 O O   . PHE   B 1 53 ? 27.512  -18.976 -28.510 1.00 49.56  ? 52  PHE   B O   1 
ATOM   1147 C CB  . PHE   B 1 53 ? 29.951  -17.040 -28.396 1.00 41.35  ? 52  PHE   B CB  1 
ATOM   1148 C CG  . PHE   B 1 53 ? 30.756  -15.800 -28.037 1.00 44.63  ? 52  PHE   B CG  1 
ATOM   1149 C CD1 . PHE   B 1 53 ? 31.068  -14.845 -29.003 1.00 49.94  ? 52  PHE   B CD1 1 
ATOM   1150 C CD2 . PHE   B 1 53 ? 31.213  -15.604 -26.739 1.00 49.92  ? 52  PHE   B CD2 1 
ATOM   1151 C CE1 . PHE   B 1 53 ? 31.798  -13.709 -28.678 1.00 47.02  ? 52  PHE   B CE1 1 
ATOM   1152 C CE2 . PHE   B 1 53 ? 31.945  -14.473 -26.415 1.00 49.41  ? 52  PHE   B CE2 1 
ATOM   1153 C CZ  . PHE   B 1 53 ? 32.244  -13.535 -27.382 1.00 49.94  ? 52  PHE   B CZ  1 
ATOM   1154 N N   . LEU   B 1 54 ? 27.531  -18.140 -30.614 1.00 36.51  ? 53  LEU   B N   1 
ATOM   1155 C CA  . LEU   B 1 54 ? 26.847  -19.279 -31.212 1.00 36.94  ? 53  LEU   B CA  1 
ATOM   1156 C C   . LEU   B 1 54 ? 27.567  -19.634 -32.513 1.00 36.25  ? 53  LEU   B C   1 
ATOM   1157 O O   . LEU   B 1 54 ? 28.094  -18.732 -33.172 1.00 34.25  ? 53  LEU   B O   1 
ATOM   1158 C CB  . LEU   B 1 54 ? 25.355  -19.037 -31.490 1.00 36.05  ? 53  LEU   B CB  1 
ATOM   1159 C CG  . LEU   B 1 54 ? 24.423  -18.916 -30.280 1.00 37.08  ? 53  LEU   B CG  1 
ATOM   1160 C CD1 . LEU   B 1 54 ? 23.028  -18.587 -30.771 1.00 33.12  ? 53  LEU   B CD1 1 
ATOM   1161 C CD2 . LEU   B 1 54 ? 24.461  -20.249 -29.546 1.00 40.84  ? 53  LEU   B CD2 1 
ATOM   1162 N N   . GLY   B 1 55 ? 27.523  -20.932 -32.856 1.00 34.98  ? 54  GLY   B N   1 
ATOM   1163 C CA  . GLY   B 1 55 ? 27.993  -21.504 -34.110 1.00 33.29  ? 54  GLY   B CA  1 
ATOM   1164 C C   . GLY   B 1 55 ? 26.890  -21.522 -35.168 1.00 33.58  ? 54  GLY   B C   1 
ATOM   1165 O O   . GLY   B 1 55 ? 25.709  -21.388 -34.842 1.00 34.07  ? 54  GLY   B O   1 
ATOM   1166 N N   . PRO   B 1 56 ? 27.233  -21.705 -36.463 1.00 33.88  ? 55  PRO   B N   1 
ATOM   1167 C CA  . PRO   B 1 56 ? 26.247  -21.673 -37.543 1.00 34.61  ? 55  PRO   B CA  1 
ATOM   1168 C C   . PRO   B 1 56 ? 25.089  -22.657 -37.436 1.00 31.48  ? 55  PRO   B C   1 
ATOM   1169 O O   . PRO   B 1 56 ? 24.027  -22.366 -37.958 1.00 32.13  ? 55  PRO   B O   1 
ATOM   1170 C CB  . PRO   B 1 56 ? 27.034  -21.895 -38.848 1.00 36.79  ? 55  PRO   B CB  1 
ATOM   1171 C CG  . PRO   B 1 56 ? 28.485  -21.890 -38.447 1.00 36.53  ? 55  PRO   B CG  1 
ATOM   1172 C CD  . PRO   B 1 56 ? 28.595  -21.950 -36.950 1.00 37.77  ? 55  PRO   B CD  1 
ATOM   1173 N N   . LYS   B 1 57 ? 25.293  -23.799 -36.747 1.00 34.94  ? 56  LYS   B N   1 
ATOM   1174 C CA  . LYS   B 1 57 ? 24.261  -24.822 -36.638 1.00 34.90  ? 56  LYS   B CA  1 
ATOM   1175 C C   . LYS   B 1 57 ? 23.038  -24.221 -35.951 1.00 32.17  ? 56  LYS   B C   1 
ATOM   1176 O O   . LYS   B 1 57 ? 21.924  -24.697 -36.156 1.00 33.60  ? 56  LYS   B O   1 
ATOM   1177 C CB  . LYS   B 1 57 ? 24.722  -26.090 -35.904 1.00 37.12  ? 56  LYS   B CB  1 
ATOM   1178 C CG  . LYS   B 1 57 ? 24.751  -26.011 -34.369 1.00 42.46  ? 56  LYS   B CG  1 
ATOM   1179 C CD  . LYS   B 1 57 ? 24.963  -27.389 -33.732 1.00 45.55  ? 56  LYS   B CD  1 
ATOM   1180 C CE  . LYS   B 1 57 ? 25.133  -27.460 -32.212 1.00 48.61  ? 56  LYS   B CE  1 
ATOM   1181 N NZ  . LYS   B 1 57 ? 23.950  -27.008 -31.465 1.00 49.58  ? 56  LYS   B NZ  1 
ATOM   1182 N N   . ASP   B 1 58 ? 23.264  -23.149 -35.180 1.00 32.08  ? 57  ASP   B N   1 
ATOM   1183 C CA  . ASP   B 1 58 ? 22.218  -22.546 -34.368 1.00 33.83  ? 57  ASP   B CA  1 
ATOM   1184 C C   . ASP   B 1 58 ? 21.723  -21.225 -34.958 1.00 33.09  ? 57  ASP   B C   1 
ATOM   1185 O O   . ASP   B 1 58 ? 20.916  -20.548 -34.301 1.00 34.15  ? 57  ASP   B O   1 
ATOM   1186 C CB  . ASP   B 1 58 ? 22.681  -22.374 -32.933 1.00 37.90  ? 57  ASP   B CB  1 
ATOM   1187 C CG  . ASP   B 1 58 ? 22.902  -23.672 -32.169 1.00 39.08  ? 57  ASP   B CG  1 
ATOM   1188 O OD1 . ASP   B 1 58 ? 22.022  -24.556 -32.265 1.00 34.68  ? 57  ASP   B OD1 1 
ATOM   1189 O OD2 . ASP   B 1 58 ? 23.935  -23.752 -31.458 1.00 42.95  ? 57  ASP   B OD2 1 
ATOM   1190 N N   . LEU   B 1 59 ? 22.182  -20.903 -36.187 1.00 31.34  ? 58  LEU   B N   1 
ATOM   1191 C CA  . LEU   B 1 59 ? 21.919  -19.626 -36.847 1.00 28.59  ? 58  LEU   B CA  1 
ATOM   1192 C C   . LEU   B 1 59 ? 21.139  -19.820 -38.146 1.00 27.15  ? 58  LEU   B C   1 
ATOM   1193 O O   . LEU   B 1 59 ? 21.568  -20.508 -39.072 1.00 30.21  ? 58  LEU   B O   1 
ATOM   1194 C CB  . LEU   B 1 59 ? 23.246  -18.907 -37.076 1.00 30.95  ? 58  LEU   B CB  1 
ATOM   1195 C CG  . LEU   B 1 59 ? 24.050  -18.587 -35.810 1.00 30.02  ? 58  LEU   B CG  1 
ATOM   1196 C CD1 . LEU   B 1 59 ? 25.268  -17.773 -36.210 1.00 32.64  ? 58  LEU   B CD1 1 
ATOM   1197 C CD2 . LEU   B 1 59 ? 23.179  -17.757 -34.854 1.00 31.03  ? 58  LEU   B CD2 1 
ATOM   1198 N N   . PHE   B 1 60 ? 19.969  -19.183 -38.197 1.00 27.35  ? 59  PHE   B N   1 
ATOM   1199 C CA  . PHE   B 1 60 ? 19.004  -19.331 -39.274 1.00 30.29  ? 59  PHE   B CA  1 
ATOM   1200 C C   . PHE   B 1 60 ? 18.855  -17.963 -39.953 1.00 30.68  ? 59  PHE   B C   1 
ATOM   1201 O O   . PHE   B 1 60 ? 18.311  -17.033 -39.358 1.00 28.13  ? 59  PHE   B O   1 
ATOM   1202 C CB  . PHE   B 1 60 ? 17.670  -19.906 -38.773 1.00 27.05  ? 59  PHE   B CB  1 
ATOM   1203 C CG  . PHE   B 1 60 ? 17.800  -21.311 -38.182 1.00 30.94  ? 59  PHE   B CG  1 
ATOM   1204 C CD1 . PHE   B 1 60 ? 18.369  -21.502 -36.929 1.00 29.23  ? 59  PHE   B CD1 1 
ATOM   1205 C CD2 . PHE   B 1 60 ? 17.369  -22.433 -38.889 1.00 30.71  ? 59  PHE   B CD2 1 
ATOM   1206 C CE1 . PHE   B 1 60 ? 18.507  -22.778 -36.383 1.00 35.44  ? 59  PHE   B CE1 1 
ATOM   1207 C CE2 . PHE   B 1 60 ? 17.475  -23.707 -38.340 1.00 33.38  ? 59  PHE   B CE2 1 
ATOM   1208 C CZ  . PHE   B 1 60 ? 18.065  -23.882 -37.098 1.00 32.78  ? 59  PHE   B CZ  1 
ATOM   1209 N N   . PRO   B 1 61 ? 19.379  -17.770 -41.189 1.00 33.24  ? 60  PRO   B N   1 
ATOM   1210 C CA  . PRO   B 1 61 ? 19.117  -16.530 -41.941 1.00 33.53  ? 60  PRO   B CA  1 
ATOM   1211 C C   . PRO   B 1 61 ? 17.661  -16.061 -41.886 1.00 35.77  ? 60  PRO   B C   1 
ATOM   1212 O O   . PRO   B 1 61 ? 16.732  -16.834 -42.119 1.00 35.59  ? 60  PRO   B O   1 
ATOM   1213 C CB  . PRO   B 1 61 ? 19.661  -16.789 -43.365 1.00 29.00  ? 60  PRO   B CB  1 
ATOM   1214 C CG  . PRO   B 1 61 ? 20.789  -17.791 -43.101 1.00 36.52  ? 60  PRO   B CG  1 
ATOM   1215 C CD  . PRO   B 1 61 ? 20.316  -18.669 -41.892 1.00 33.51  ? 60  PRO   B CD  1 
ATOM   1216 N N   . TYR   B 1 62 ? 17.481  -14.778 -41.527 1.00 34.68  ? 61  TYR   B N   1 
ATOM   1217 C CA  . TYR   B 1 62 ? 16.187  -14.256 -41.132 1.00 34.84  ? 61  TYR   B CA  1 
ATOM   1218 C C   . TYR   B 1 62 ? 15.181  -14.308 -42.269 1.00 35.88  ? 61  TYR   B C   1 
ATOM   1219 O O   . TYR   B 1 62 ? 14.022  -14.654 -42.054 1.00 32.88  ? 61  TYR   B O   1 
ATOM   1220 C CB  . TYR   B 1 62 ? 16.378  -12.805 -40.683 1.00 38.49  ? 61  TYR   B CB  1 
ATOM   1221 C CG  . TYR   B 1 62 ? 15.085  -12.049 -40.421 1.00 40.76  ? 61  TYR   B CG  1 
ATOM   1222 C CD1 . TYR   B 1 62 ? 14.312  -12.312 -39.294 1.00 40.68  ? 61  TYR   B CD1 1 
ATOM   1223 C CD2 . TYR   B 1 62 ? 14.674  -11.024 -41.271 1.00 45.94  ? 61  TYR   B CD2 1 
ATOM   1224 C CE1 . TYR   B 1 62 ? 13.153  -11.596 -39.037 1.00 38.96  ? 61  TYR   B CE1 1 
ATOM   1225 C CE2 . TYR   B 1 62 ? 13.517  -10.302 -41.025 1.00 49.12  ? 61  TYR   B CE2 1 
ATOM   1226 C CZ  . TYR   B 1 62 ? 12.758  -10.591 -39.901 1.00 45.86  ? 61  TYR   B CZ  1 
ATOM   1227 O OH  . TYR   B 1 62 ? 11.608  -9.906  -39.650 1.00 45.06  ? 61  TYR   B OH  1 
ATOM   1228 N N   . ASP   B 1 63 ? 15.619  -13.905 -43.465 1.00 45.30  ? 62  ASP   B N   1 
ATOM   1229 C CA  . ASP   B 1 63 ? 14.702  -13.757 -44.589 1.00 45.93  ? 62  ASP   B CA  1 
ATOM   1230 C C   . ASP   B 1 63 ? 14.102  -15.119 -44.890 1.00 42.92  ? 62  ASP   B C   1 
ATOM   1231 O O   . ASP   B 1 63 ? 12.882  -15.271 -44.835 1.00 48.68  ? 62  ASP   B O   1 
ATOM   1232 C CB  . ASP   B 1 63 ? 15.374  -13.164 -45.815 1.00 52.30  ? 62  ASP   B CB  1 
ATOM   1233 C CG  . ASP   B 1 63 ? 15.134  -11.680 -46.047 1.00 63.56  ? 62  ASP   B CG  1 
ATOM   1234 O OD1 . ASP   B 1 63 ? 14.554  -11.010 -45.146 1.00 63.84  ? 62  ASP   B OD1 1 
ATOM   1235 O OD2 . ASP   B 1 63 ? 15.515  -11.207 -47.141 1.00 75.51  ? 62  ASP   B OD2 1 
ATOM   1236 N N   . LYS   B 1 64 ? 14.992  -16.095 -45.101 1.00 42.23  ? 63  LYS   B N   1 
ATOM   1237 C CA  . LYS   B 1 64 ? 14.614  -17.473 -45.376 1.00 43.52  ? 63  LYS   B CA  1 
ATOM   1238 C C   . LYS   B 1 64 ? 13.703  -18.022 -44.281 1.00 40.95  ? 63  LYS   B C   1 
ATOM   1239 O O   . LYS   B 1 64 ? 12.805  -18.813 -44.569 1.00 46.72  ? 63  LYS   B O   1 
ATOM   1240 C CB  . LYS   B 1 64 ? 15.840  -18.393 -45.465 1.00 48.50  ? 63  LYS   B CB  1 
ATOM   1241 C CG  . LYS   B 1 64 ? 15.527  -19.838 -45.867 1.00 43.33  ? 63  LYS   B CG  1 
ATOM   1242 C CD  . LYS   B 1 64 ? 16.572  -20.908 -45.568 1.00 49.41  ? 63  LYS   B CD  1 
ATOM   1243 C CE  . LYS   B 1 64 ? 16.459  -22.207 -46.352 1.00 48.48  ? 63  LYS   B CE  1 
ATOM   1244 N NZ  . LYS   B 1 64 ? 15.122  -22.780 -46.549 1.00 52.72  ? 63  LYS   B NZ  1 
ATOM   1245 N N   . SER   B 1 65 ? 13.932  -17.631 -43.024 1.00 38.80  ? 64  SER   B N   1 
ATOM   1246 C CA  . SER   B 1 65 ? 13.299  -18.380 -41.938 1.00 45.68  ? 64  SER   B CA  1 
ATOM   1247 C C   . SER   B 1 65 ? 12.171  -17.617 -41.244 1.00 41.24  ? 64  SER   B C   1 
ATOM   1248 O O   . SER   B 1 65 ? 11.516  -18.179 -40.365 1.00 44.54  ? 64  SER   B O   1 
ATOM   1249 C CB  . SER   B 1 65 ? 14.323  -18.914 -40.963 1.00 41.41  ? 64  SER   B CB  1 
ATOM   1250 O OG  . SER   B 1 65 ? 15.085  -17.815 -40.492 1.00 53.11  ? 64  SER   B OG  1 
ATOM   1251 N N   . LYS   B 1 66 ? 11.874  -16.389 -41.699 1.00 39.27  ? 65  LYS   B N   1 
ATOM   1252 C CA  . LYS   B 1 66 ? 11.017  -15.483 -40.932 1.00 37.68  ? 65  LYS   B CA  1 
ATOM   1253 C C   . LYS   B 1 66 ? 9.577   -15.978 -40.778 1.00 42.47  ? 65  LYS   B C   1 
ATOM   1254 O O   . LYS   B 1 66 ? 8.957   -15.714 -39.754 1.00 46.33  ? 65  LYS   B O   1 
ATOM   1255 C CB  . LYS   B 1 66 ? 11.108  -14.003 -41.333 1.00 39.87  ? 65  LYS   B CB  1 
ATOM   1256 C CG  . LYS   B 1 66 ? 10.351  -13.569 -42.595 1.00 44.42  ? 65  LYS   B CG  1 
ATOM   1257 N N   . ASP   B 1 67 ? 9.013   -16.690 -41.761 1.00 43.00  ? 66  ASP   B N   1 
ATOM   1258 C CA  . ASP   B 1 67 ? 7.601   -17.024 -41.610 1.00 51.36  ? 66  ASP   B CA  1 
ATOM   1259 C C   . ASP   B 1 67 ? 7.413   -18.282 -40.749 1.00 48.54  ? 66  ASP   B C   1 
ATOM   1260 O O   . ASP   B 1 67 ? 6.353   -18.482 -40.138 1.00 49.31  ? 66  ASP   B O   1 
ATOM   1261 C CB  . ASP   B 1 67 ? 6.818   -16.837 -42.903 1.00 65.53  ? 66  ASP   B CB  1 
ATOM   1262 C CG  . ASP   B 1 67 ? 7.356   -17.587 -44.110 1.00 78.46  ? 66  ASP   B CG  1 
ATOM   1263 O OD1 . ASP   B 1 67 ? 6.985   -17.218 -45.255 1.00 83.55  ? 66  ASP   B OD1 1 
ATOM   1264 O OD2 . ASP   B 1 67 ? 8.135   -18.537 -43.891 1.00 75.80  ? 66  ASP   B OD2 1 
ATOM   1265 N N   . LYS   B 1 68 ? 8.471   -19.098 -40.671 1.00 42.01  ? 67  LYS   B N   1 
ATOM   1266 C CA  . LYS   B 1 68 ? 8.516   -20.282 -39.826 1.00 41.42  ? 67  LYS   B CA  1 
ATOM   1267 C C   . LYS   B 1 68 ? 8.766   -19.916 -38.361 1.00 38.97  ? 67  LYS   B C   1 
ATOM   1268 O O   . LYS   B 1 68 ? 8.033   -20.385 -37.484 1.00 40.45  ? 67  LYS   B O   1 
ATOM   1269 C CB  . LYS   B 1 68 ? 9.627   -21.209 -40.312 1.00 42.63  ? 67  LYS   B CB  1 
ATOM   1270 C CG  . LYS   B 1 68 ? 9.773   -22.450 -39.473 1.00 53.19  ? 67  LYS   B CG  1 
ATOM   1271 C CD  . LYS   B 1 68 ? 10.828  -23.348 -40.104 1.00 65.39  ? 67  LYS   B CD  1 
ATOM   1272 C CE  . LYS   B 1 68 ? 10.995  -24.609 -39.326 1.00 66.10  ? 67  LYS   B CE  1 
ATOM   1273 N NZ  . LYS   B 1 68 ? 9.714   -25.317 -39.273 1.00 67.79  ? 67  LYS   B NZ  1 
ATOM   1274 N N   . TYR   B 1 69 ? 9.791   -19.091 -38.088 1.00 32.21  ? 68  TYR   B N   1 
ATOM   1275 C CA  . TYR   B 1 69 ? 10.179  -18.790 -36.710 1.00 34.04  ? 68  TYR   B CA  1 
ATOM   1276 C C   . TYR   B 1 69 ? 9.636   -17.451 -36.218 1.00 38.75  ? 68  TYR   B C   1 
ATOM   1277 O O   . TYR   B 1 69 ? 9.726   -17.169 -35.021 1.00 40.70  ? 68  TYR   B O   1 
ATOM   1278 C CB  . TYR   B 1 69 ? 11.687  -18.868 -36.455 1.00 33.25  ? 68  TYR   B CB  1 
ATOM   1279 C CG  . TYR   B 1 69 ? 12.264  -20.245 -36.755 1.00 36.59  ? 68  TYR   B CG  1 
ATOM   1280 C CD1 . TYR   B 1 69 ? 11.689  -21.402 -36.226 1.00 37.97  ? 68  TYR   B CD1 1 
ATOM   1281 C CD2 . TYR   B 1 69 ? 13.358  -20.384 -37.603 1.00 39.33  ? 68  TYR   B CD2 1 
ATOM   1282 C CE1 . TYR   B 1 69 ? 12.211  -22.658 -36.505 1.00 40.26  ? 68  TYR   B CE1 1 
ATOM   1283 C CE2 . TYR   B 1 69 ? 13.879  -21.629 -37.907 1.00 42.37  ? 68  TYR   B CE2 1 
ATOM   1284 C CZ  . TYR   B 1 69 ? 13.304  -22.762 -37.351 1.00 41.24  ? 68  TYR   B CZ  1 
ATOM   1285 O OH  . TYR   B 1 69 ? 13.829  -23.968 -37.662 1.00 39.48  ? 68  TYR   B OH  1 
ATOM   1286 N N   . GLY   B 1 70 ? 9.086   -16.631 -37.121 1.00 37.39  ? 69  GLY   B N   1 
ATOM   1287 C CA  . GLY   B 1 70 ? 8.816   -15.247 -36.769 1.00 42.66  ? 69  GLY   B CA  1 
ATOM   1288 C C   . GLY   B 1 70 ? 7.424   -14.994 -36.178 1.00 48.67  ? 69  GLY   B C   1 
ATOM   1289 O O   . GLY   B 1 70 ? 6.886   -13.894 -36.319 1.00 47.30  ? 69  GLY   B O   1 
ATOM   1290 N N   . LYS   B 1 71 ? 6.833   -15.990 -35.508 1.00 50.59  ? 70  LYS   B N   1 
ATOM   1291 C CA  . LYS   B 1 71 ? 5.489   -15.810 -34.987 1.00 47.37  ? 70  LYS   B CA  1 
ATOM   1292 C C   . LYS   B 1 71 ? 5.557   -15.364 -33.536 1.00 51.01  ? 70  LYS   B C   1 
ATOM   1293 O O   . LYS   B 1 71 ? 6.374   -15.877 -32.773 1.00 49.09  ? 70  LYS   B O   1 
ATOM   1294 C CB  . LYS   B 1 71 ? 4.657   -17.091 -34.939 1.00 52.05  ? 70  LYS   B CB  1 
ATOM   1295 C CG  . LYS   B 1 71 ? 3.734   -17.359 -36.117 1.00 62.74  ? 70  LYS   B CG  1 
ATOM   1296 C CD  . LYS   B 1 71 ? 4.365   -18.150 -37.256 1.00 62.33  ? 70  LYS   B CD  1 
ATOM   1297 C CE  . LYS   B 1 71 ? 3.282   -18.775 -38.095 1.00 65.87  ? 70  LYS   B CE  1 
ATOM   1298 N NZ  . LYS   B 1 71 ? 3.825   -19.688 -39.103 1.00 65.07  ? 70  LYS   B NZ  1 
ATOM   1299 N N   . PRO   B 1 72 ? 4.654   -14.459 -33.092 1.00 48.94  ? 71  PRO   B N   1 
ATOM   1300 C CA  . PRO   B 1 72 ? 4.617   -14.067 -31.678 1.00 47.47  ? 71  PRO   B CA  1 
ATOM   1301 C C   . PRO   B 1 72 ? 4.382   -15.262 -30.751 1.00 47.91  ? 71  PRO   B C   1 
ATOM   1302 O O   . PRO   B 1 72 ? 3.795   -16.273 -31.154 1.00 46.53  ? 71  PRO   B O   1 
ATOM   1303 C CB  . PRO   B 1 72 ? 3.531   -12.955 -31.592 1.00 47.47  ? 71  PRO   B CB  1 
ATOM   1304 C CG  . PRO   B 1 72 ? 3.329   -12.542 -33.030 1.00 47.47  ? 71  PRO   B CG  1 
ATOM   1305 C CD  . PRO   B 1 72 ? 3.641   -13.764 -33.910 1.00 49.79  ? 71  PRO   B CD  1 
ATOM   1306 N N   . ASN   B 1 73 ? 4.928   -15.166 -29.529 1.00 43.53  ? 72  ASN   B N   1 
ATOM   1307 C CA  . ASN   B 1 73 ? 4.678   -16.127 -28.464 1.00 43.08  ? 72  ASN   B CA  1 
ATOM   1308 C C   . ASN   B 1 73 ? 4.654   -15.359 -27.136 1.00 50.71  ? 72  ASN   B C   1 
ATOM   1309 O O   . ASN   B 1 73 ? 4.689   -14.123 -27.130 1.00 47.26  ? 72  ASN   B O   1 
ATOM   1310 C CB  . ASN   B 1 73 ? 5.672   -17.288 -28.480 1.00 41.07  ? 72  ASN   B CB  1 
ATOM   1311 C CG  . ASN   B 1 73 ? 7.091   -16.834 -28.220 1.00 43.23  ? 72  ASN   B CG  1 
ATOM   1312 O OD1 . ASN   B 1 73 ? 7.337   -16.088 -27.257 1.00 38.47  ? 72  ASN   B OD1 1 
ATOM   1313 N ND2 . ASN   B 1 73 ? 8.028   -17.218 -29.087 1.00 35.98  ? 72  ASN   B ND2 1 
ATOM   1314 N N   . LYS   B 1 74 ? 4.645   -16.090 -26.012 1.00 46.76  ? 73  LYS   B N   1 
ATOM   1315 C CA  . LYS   B 1 74 ? 4.535   -15.465 -24.699 1.00 51.48  ? 73  LYS   B CA  1 
ATOM   1316 C C   . LYS   B 1 74 ? 5.876   -15.491 -23.948 1.00 47.70  ? 73  LYS   B C   1 
ATOM   1317 O O   . LYS   B 1 74 ? 5.899   -15.383 -22.727 1.00 48.19  ? 73  LYS   B O   1 
ATOM   1318 C CB  . LYS   B 1 74 ? 3.349   -16.086 -23.938 1.00 45.15  ? 73  LYS   B CB  1 
ATOM   1319 N N   . ARG   B 1 75 ? 7.008   -15.659 -24.646 1.00 38.36  ? 74  ARG   B N   1 
ATOM   1320 C CA  . ARG   B 1 75 ? 8.272   -15.524 -23.932 1.00 36.05  ? 74  ARG   B CA  1 
ATOM   1321 C C   . ARG   B 1 75 ? 8.563   -14.028 -23.761 1.00 38.92  ? 74  ARG   B C   1 
ATOM   1322 O O   . ARG   B 1 75 ? 8.285   -13.226 -24.664 1.00 37.95  ? 74  ARG   B O   1 
ATOM   1323 C CB  . ARG   B 1 75 ? 9.418   -16.347 -24.526 1.00 37.81  ? 74  ARG   B CB  1 
ATOM   1324 C CG  . ARG   B 1 75 ? 9.232   -17.839 -24.776 1.00 39.89  ? 74  ARG   B CG  1 
ATOM   1325 C CD  . ARG   B 1 75 ? 9.071   -18.644 -23.498 1.00 41.89  ? 74  ARG   B CD  1 
ATOM   1326 N NE  . ARG   B 1 75 ? 9.316   -20.068 -23.752 1.00 41.21  ? 74  ARG   B NE  1 
ATOM   1327 C CZ  . ARG   B 1 75 ? 10.452  -20.675 -23.463 1.00 41.63  ? 74  ARG   B CZ  1 
ATOM   1328 N NH1 . ARG   B 1 75 ? 11.443  -20.010 -22.886 1.00 42.97  ? 74  ARG   B NH1 1 
ATOM   1329 N NH2 . ARG   B 1 75 ? 10.603  -21.946 -23.787 1.00 40.43  ? 74  ARG   B NH2 1 
ATOM   1330 N N   . LYS   B 1 76 ? 9.063   -13.652 -22.571 1.00 35.12  ? 75  LYS   B N   1 
ATOM   1331 C CA  . LYS   B 1 76 ? 9.410   -12.271 -22.261 1.00 35.06  ? 75  LYS   B CA  1 
ATOM   1332 C C   . LYS   B 1 76 ? 10.518  -11.757 -23.191 1.00 32.56  ? 75  LYS   B C   1 
ATOM   1333 O O   . LYS   B 1 76 ? 11.614  -12.350 -23.253 1.00 27.79  ? 75  LYS   B O   1 
ATOM   1334 C CB  . LYS   B 1 76 ? 9.917   -12.158 -20.815 1.00 35.74  ? 75  LYS   B CB  1 
ATOM   1335 C CG  . LYS   B 1 76 ? 10.339  -10.730 -20.441 1.00 35.62  ? 75  LYS   B CG  1 
ATOM   1336 C CD  . LYS   B 1 76 ? 10.836  -10.566 -19.003 1.00 35.73  ? 75  LYS   B CD  1 
ATOM   1337 C CE  . LYS   B 1 76 ? 10.985  -9.133  -18.568 1.00 42.36  ? 75  LYS   B CE  1 
ATOM   1338 N NZ  . LYS   B 1 76 ? 11.486  -9.075  -17.185 1.00 53.32  ? 75  LYS   B NZ  1 
ATOM   1339 N N   . GLY   B 1 77 ? 10.213  -10.649 -23.880 1.00 33.40  ? 76  GLY   B N   1 
ATOM   1340 C CA  . GLY   B 1 77 ? 11.168  -9.969  -24.757 1.00 36.39  ? 76  GLY   B CA  1 
ATOM   1341 C C   . GLY   B 1 77 ? 11.025  -10.374 -26.231 1.00 33.33  ? 76  GLY   B C   1 
ATOM   1342 O O   . GLY   B 1 77 ? 11.498  -9.662  -27.105 1.00 37.28  ? 76  GLY   B O   1 
ATOM   1343 N N   . PHE   B 1 78 ? 10.364  -11.512 -26.509 1.00 32.13  ? 77  PHE   B N   1 
ATOM   1344 C CA  . PHE   B 1 78 ? 10.205  -12.067 -27.855 1.00 31.15  ? 77  PHE   B CA  1 
ATOM   1345 C C   . PHE   B 1 78 ? 9.460   -11.121 -28.794 1.00 33.25  ? 77  PHE   B C   1 
ATOM   1346 O O   . PHE   B 1 78 ? 9.968   -10.816 -29.875 1.00 30.29  ? 77  PHE   B O   1 
ATOM   1347 C CB  . PHE   B 1 78 ? 9.466   -13.408 -27.885 1.00 29.51  ? 77  PHE   B CB  1 
ATOM   1348 C CG  . PHE   B 1 78 ? 9.695   -14.158 -29.191 1.00 30.98  ? 77  PHE   B CG  1 
ATOM   1349 C CD1 . PHE   B 1 78 ? 10.803  -14.996 -29.332 1.00 28.60  ? 77  PHE   B CD1 1 
ATOM   1350 C CD2 . PHE   B 1 78 ? 8.803   -14.016 -30.255 1.00 32.76  ? 77  PHE   B CD2 1 
ATOM   1351 C CE1 . PHE   B 1 78 ? 11.035  -15.683 -30.516 1.00 27.07  ? 77  PHE   B CE1 1 
ATOM   1352 C CE2 . PHE   B 1 78 ? 9.029   -14.697 -31.452 1.00 36.23  ? 77  PHE   B CE2 1 
ATOM   1353 C CZ  . PHE   B 1 78 ? 10.132  -15.541 -31.565 1.00 31.32  ? 77  PHE   B CZ  1 
ATOM   1354 N N   . ASN   B 1 79 ? 8.250   -10.683 -28.422 1.00 33.26  ? 78  ASN   B N   1 
ATOM   1355 C CA  . ASN   B 1 79 ? 7.505   -9.797  -29.314 1.00 35.39  ? 78  ASN   B CA  1 
ATOM   1356 C C   . ASN   B 1 79 ? 8.242   -8.462  -29.511 1.00 36.63  ? 78  ASN   B C   1 
ATOM   1357 O O   . ASN   B 1 79 ? 8.228   -7.894  -30.601 1.00 37.00  ? 78  ASN   B O   1 
ATOM   1358 C CB  . ASN   B 1 79 ? 6.005   -9.705  -29.012 1.00 38.67  ? 78  ASN   B CB  1 
ATOM   1359 C CG  . ASN   B 1 79 ? 5.292   -11.044 -29.034 1.00 45.07  ? 78  ASN   B CG  1 
ATOM   1360 O OD1 . ASN   B 1 79 ? 5.791   -12.031 -29.591 1.00 43.27  ? 78  ASN   B OD1 1 
ATOM   1361 N ND2 . ASN   B 1 79 ? 4.120   -11.117 -28.414 1.00 42.00  ? 78  ASN   B ND2 1 
ATOM   1362 N N   . GLU   B 1 80 ? 8.926   -7.973  -28.482 1.00 34.62  ? 79  GLU   B N   1 
ATOM   1363 C CA  . GLU   B 1 80 ? 9.729   -6.773  -28.647 1.00 36.76  ? 79  GLU   B CA  1 
ATOM   1364 C C   . GLU   B 1 80 ? 10.855  -7.019  -29.655 1.00 37.85  ? 79  GLU   B C   1 
ATOM   1365 O O   . GLU   B 1 80 ? 11.130  -6.142  -30.470 1.00 38.06  ? 79  GLU   B O   1 
ATOM   1366 C CB  . GLU   B 1 80 ? 10.278  -6.203  -27.343 1.00 33.11  ? 79  GLU   B CB  1 
ATOM   1367 C CG  . GLU   B 1 80 ? 9.217   -5.401  -26.594 1.00 42.64  ? 79  GLU   B CG  1 
ATOM   1368 N N   . GLY   B 1 81 ? 11.494  -8.198  -29.572 1.00 37.07  ? 80  GLY   B N   1 
ATOM   1369 C CA  . GLY   B 1 81 ? 12.534  -8.645  -30.489 1.00 33.89  ? 80  GLY   B CA  1 
ATOM   1370 C C   . GLY   B 1 81 ? 12.031  -8.655  -31.928 1.00 35.34  ? 80  GLY   B C   1 
ATOM   1371 O O   . GLY   B 1 81 ? 12.718  -8.179  -32.836 1.00 36.16  ? 80  GLY   B O   1 
ATOM   1372 N N   . LEU   B 1 82 ? 10.817  -9.184  -32.122 1.00 29.41  ? 81  LEU   B N   1 
ATOM   1373 C CA  . LEU   B 1 82 ? 10.199  -9.201  -33.435 1.00 32.88  ? 81  LEU   B CA  1 
ATOM   1374 C C   . LEU   B 1 82 ? 10.091  -7.767  -33.965 1.00 34.35  ? 81  LEU   B C   1 
ATOM   1375 O O   . LEU   B 1 82 ? 10.403  -7.515  -35.124 1.00 35.48  ? 81  LEU   B O   1 
ATOM   1376 C CB  . LEU   B 1 82 ? 8.858   -9.926  -33.452 1.00 34.20  ? 81  LEU   B CB  1 
ATOM   1377 C CG  . LEU   B 1 82 ? 8.881   -11.435 -33.205 1.00 32.20  ? 81  LEU   B CG  1 
ATOM   1378 C CD1 . LEU   B 1 82 ? 7.490   -12.047 -33.292 1.00 31.33  ? 81  LEU   B CD1 1 
ATOM   1379 C CD2 . LEU   B 1 82 ? 9.831   -12.110 -34.190 1.00 32.30  ? 81  LEU   B CD2 1 
ATOM   1380 N N   . TRP   B 1 83 ? 9.676   -6.834  -33.103 1.00 33.74  ? 82  TRP   B N   1 
ATOM   1381 C CA  . TRP   B 1 83 ? 9.533   -5.429  -33.459 1.00 36.25  ? 82  TRP   B CA  1 
ATOM   1382 C C   . TRP   B 1 83 ? 10.864  -4.824  -33.913 1.00 33.33  ? 82  TRP   B C   1 
ATOM   1383 O O   . TRP   B 1 83 ? 10.898  -4.092  -34.903 1.00 35.08  ? 82  TRP   B O   1 
ATOM   1384 C CB  . TRP   B 1 83 ? 8.892   -4.590  -32.342 1.00 35.34  ? 82  TRP   B CB  1 
ATOM   1385 C CG  . TRP   B 1 83 ? 8.625   -3.182  -32.813 1.00 37.24  ? 82  TRP   B CG  1 
ATOM   1386 C CD1 . TRP   B 1 83 ? 7.475   -2.693  -33.359 1.00 43.22  ? 82  TRP   B CD1 1 
ATOM   1387 C CD2 . TRP   B 1 83 ? 9.580   -2.095  -32.849 1.00 37.36  ? 82  TRP   B CD2 1 
ATOM   1388 N NE1 . TRP   B 1 83 ? 7.649   -1.383  -33.729 1.00 45.64  ? 82  TRP   B NE1 1 
ATOM   1389 C CE2 . TRP   B 1 83 ? 8.926   -0.988  -33.427 1.00 39.11  ? 82  TRP   B CE2 1 
ATOM   1390 C CE3 . TRP   B 1 83 ? 10.919  -1.954  -32.444 1.00 37.87  ? 82  TRP   B CE3 1 
ATOM   1391 C CZ2 . TRP   B 1 83 ? 9.560   0.249   -33.595 1.00 40.32  ? 82  TRP   B CZ2 1 
ATOM   1392 C CZ3 . TRP   B 1 83 ? 11.540  -0.731  -32.589 1.00 40.45  ? 82  TRP   B CZ3 1 
ATOM   1393 C CH2 . TRP   B 1 83 ? 10.867  0.353   -33.170 1.00 39.99  ? 82  TRP   B CH2 1 
ATOM   1394 N N   . GLU   B 1 84 ? 11.936  -5.119  -33.167 1.00 31.69  ? 83  GLU   B N   1 
ATOM   1395 C CA  . GLU   B 1 84 ? 13.244  -4.546  -33.413 1.00 34.22  ? 83  GLU   B CA  1 
ATOM   1396 C C   . GLU   B 1 84 ? 13.819  -5.072  -34.731 1.00 36.64  ? 83  GLU   B C   1 
ATOM   1397 O O   . GLU   B 1 84 ? 14.345  -4.280  -35.520 1.00 40.68  ? 83  GLU   B O   1 
ATOM   1398 C CB  . GLU   B 1 84 ? 14.177  -4.811  -32.237 1.00 31.45  ? 83  GLU   B CB  1 
ATOM   1399 C CG  . GLU   B 1 84 ? 13.672  -4.154  -30.953 1.00 33.45  ? 83  GLU   B CG  1 
ATOM   1400 C CD  . GLU   B 1 84 ? 14.510  -4.463  -29.729 1.00 35.18  ? 83  GLU   B CD  1 
ATOM   1401 O OE1 . GLU   B 1 84 ? 15.455  -5.299  -29.831 1.00 35.32  ? 83  GLU   B OE1 1 
ATOM   1402 O OE2 . GLU   B 1 84 ? 14.245  -3.827  -28.659 1.00 36.96  ? 83  GLU   B OE2 1 
ATOM   1403 N N   . ILE   B 1 85 ? 13.725  -6.389  -34.964 1.00 33.82  ? 84  ILE   B N   1 
ATOM   1404 C CA  . ILE   B 1 85 ? 14.380  -6.966  -36.139 1.00 34.52  ? 84  ILE   B CA  1 
ATOM   1405 C C   . ILE   B 1 85 ? 13.703  -6.411  -37.394 1.00 31.87  ? 84  ILE   B C   1 
ATOM   1406 O O   . ILE   B 1 85 ? 14.360  -6.187  -38.420 1.00 30.94  ? 84  ILE   B O   1 
ATOM   1407 C CB  . ILE   B 1 85 ? 14.425  -8.501  -36.089 1.00 31.39  ? 84  ILE   B CB  1 
ATOM   1408 C CG1 . ILE   B 1 85 ? 15.430  -9.089  -37.102 1.00 33.92  ? 84  ILE   B CG1 1 
ATOM   1409 C CG2 . ILE   B 1 85 ? 13.027  -9.104  -36.267 1.00 29.41  ? 84  ILE   B CG2 1 
ATOM   1410 C CD1 . ILE   B 1 85 ? 16.029  -10.447 -36.702 1.00 32.59  ? 84  ILE   B CD1 1 
ATOM   1411 N N   . GLN   B 1 86 ? 12.405  -6.138  -37.267 1.00 34.02  ? 85  GLN   B N   1 
ATOM   1412 C CA  . GLN   B 1 86 ? 11.561  -5.563  -38.312 1.00 37.67  ? 85  GLN   B CA  1 
ATOM   1413 C C   . GLN   B 1 86 ? 11.850  -4.068  -38.531 1.00 37.91  ? 85  GLN   B C   1 
ATOM   1414 O O   . GLN   B 1 86 ? 11.894  -3.622  -39.677 1.00 37.24  ? 85  GLN   B O   1 
ATOM   1415 C CB  . GLN   B 1 86 ? 10.090  -5.855  -37.991 1.00 44.36  ? 85  GLN   B CB  1 
ATOM   1416 C CG  . GLN   B 1 86 ? 9.599   -7.246  -38.405 1.00 53.57  ? 85  GLN   B CG  1 
ATOM   1417 C CD  . GLN   B 1 86 ? 8.448   -7.837  -37.599 1.00 58.81  ? 85  GLN   B CD  1 
ATOM   1418 O OE1 . GLN   B 1 86 ? 7.282   -7.407  -37.648 1.00 57.65  ? 85  GLN   B OE1 1 
ATOM   1419 N NE2 . GLN   B 1 86 ? 8.766   -8.910  -36.887 1.00 54.69  ? 85  GLN   B NE2 1 
ATOM   1420 N N   . ASN   B 1 87 ? 12.046  -3.276  -37.463 1.00 33.29  ? 86  ASN   B N   1 
ATOM   1421 C CA  . ASN   B 1 87 ? 11.879  -1.832  -37.633 1.00 37.67  ? 86  ASN   B CA  1 
ATOM   1422 C C   . ASN   B 1 87 ? 13.179  -1.061  -37.469 1.00 36.62  ? 86  ASN   B C   1 
ATOM   1423 O O   . ASN   B 1 87 ? 13.304  0.033   -38.013 1.00 40.65  ? 86  ASN   B O   1 
ATOM   1424 C CB  . ASN   B 1 87 ? 10.855  -1.228  -36.671 1.00 35.63  ? 86  ASN   B CB  1 
ATOM   1425 C CG  . ASN   B 1 87 ? 9.497   -1.777  -36.990 1.00 39.28  ? 86  ASN   B CG  1 
ATOM   1426 O OD1 . ASN   B 1 87 ? 8.922   -1.409  -38.017 1.00 47.73  ? 86  ASN   B OD1 1 
ATOM   1427 N ND2 . ASN   B 1 87 ? 9.043   -2.745  -36.209 1.00 42.36  ? 86  ASN   B ND2 1 
ATOM   1428 N N   . ASN   B 1 88 ? 14.116  -1.604  -36.684 1.00 35.10  ? 87  ASN   B N   1 
ATOM   1429 C CA  . ASN   B 1 88 ? 15.386  -0.941  -36.470 1.00 32.29  ? 87  ASN   B CA  1 
ATOM   1430 C C   . ASN   B 1 88 ? 16.450  -1.974  -36.105 1.00 32.27  ? 87  ASN   B C   1 
ATOM   1431 O O   . ASN   B 1 88 ? 17.065  -1.894  -35.036 1.00 30.04  ? 87  ASN   B O   1 
ATOM   1432 C CB  . ASN   B 1 88 ? 15.254  0.196   -35.459 1.00 38.08  ? 87  ASN   B CB  1 
ATOM   1433 C CG  . ASN   B 1 88 ? 16.340  1.233   -35.654 1.00 39.86  ? 87  ASN   B CG  1 
ATOM   1434 O OD1 . ASN   B 1 88 ? 17.358  0.992   -36.318 1.00 35.47  ? 87  ASN   B OD1 1 
ATOM   1435 N ND2 . ASN   B 1 88 ? 16.153  2.396   -35.066 1.00 40.44  ? 87  ASN   B ND2 1 
ATOM   1436 N N   . PRO   B 1 89 ? 16.711  -2.966  -37.000 1.00 31.06  ? 88  PRO   B N   1 
ATOM   1437 C CA  . PRO   B 1 89 ? 17.647  -4.061  -36.701 1.00 28.77  ? 88  PRO   B CA  1 
ATOM   1438 C C   . PRO   B 1 89 ? 19.064  -3.619  -36.363 1.00 28.58  ? 88  PRO   B C   1 
ATOM   1439 O O   . PRO   B 1 89 ? 19.827  -4.378  -35.755 1.00 29.95  ? 88  PRO   B O   1 
ATOM   1440 C CB  . PRO   B 1 89 ? 17.637  -4.944  -37.982 1.00 26.43  ? 88  PRO   B CB  1 
ATOM   1441 C CG  . PRO   B 1 89 ? 17.055  -4.013  -39.073 1.00 26.25  ? 88  PRO   B CG  1 
ATOM   1442 C CD  . PRO   B 1 89 ? 16.058  -3.111  -38.311 1.00 26.54  ? 88  PRO   B CD  1 
ATOM   1443 N N   . HIS   B 1 90 ? 19.443  -2.410  -36.819 1.00 30.21  ? 89  HIS   B N   1 
ATOM   1444 C CA  . HIS   B 1 90 ? 20.847  -2.030  -36.789 1.00 30.30  ? 89  HIS   B CA  1 
ATOM   1445 C C   . HIS   B 1 90 ? 21.127  -0.961  -35.721 1.00 32.92  ? 89  HIS   B C   1 
ATOM   1446 O O   . HIS   B 1 90 ? 22.243  -0.411  -35.665 1.00 31.38  ? 89  HIS   B O   1 
ATOM   1447 C CB  . HIS   B 1 90 ? 21.322  -1.617  -38.190 1.00 30.65  ? 89  HIS   B CB  1 
ATOM   1448 C CG  . HIS   B 1 90 ? 21.185  -2.707  -39.217 1.00 28.88  ? 89  HIS   B CG  1 
ATOM   1449 N ND1 . HIS   B 1 90 ? 21.866  -3.900  -39.116 1.00 26.57  ? 89  HIS   B ND1 1 
ATOM   1450 C CD2 . HIS   B 1 90 ? 20.500  -2.761  -40.358 1.00 27.24  ? 89  HIS   B CD2 1 
ATOM   1451 C CE1 . HIS   B 1 90 ? 21.565  -4.659  -40.153 1.00 26.47  ? 89  HIS   B CE1 1 
ATOM   1452 N NE2 . HIS   B 1 90 ? 20.729  -3.984  -40.912 1.00 26.83  ? 89  HIS   B NE2 1 
ATOM   1453 N N   . ALA   B 1 91 ? 20.122  -0.662  -34.882 1.00 31.65  ? 90  ALA   B N   1 
ATOM   1454 C CA  . ALA   B 1 91 ? 20.266  0.395   -33.884 1.00 29.72  ? 90  ALA   B CA  1 
ATOM   1455 C C   . ALA   B 1 91 ? 21.231  -0.031  -32.780 1.00 35.36  ? 90  ALA   B C   1 
ATOM   1456 O O   . ALA   B 1 91 ? 21.510  -1.218  -32.603 1.00 34.92  ? 90  ALA   B O   1 
ATOM   1457 C CB  . ALA   B 1 91 ? 18.915  0.777   -33.311 1.00 28.96  ? 90  ALA   B CB  1 
ATOM   1458 N N   . SER   B 1 92 ? 21.757  0.972   -32.060 1.00 32.73  ? 91  SER   B N   1 
ATOM   1459 C CA  . SER   B 1 92 ? 22.416  0.793   -30.782 1.00 40.11  ? 91  SER   B CA  1 
ATOM   1460 C C   . SER   B 1 92 ? 21.337  0.526   -29.736 1.00 44.92  ? 91  SER   B C   1 
ATOM   1461 O O   . SER   B 1 92 ? 20.372  1.296   -29.648 1.00 43.85  ? 91  SER   B O   1 
ATOM   1462 C CB  . SER   B 1 92 ? 23.217  2.047   -30.438 1.00 41.04  ? 91  SER   B CB  1 
ATOM   1463 O OG  . SER   B 1 92 ? 23.827  1.906   -29.169 1.00 49.82  ? 91  SER   B OG  1 
ATOM   1464 N N   . TYR   B 1 93 ? 21.505  -0.563  -28.964 1.00 45.54  ? 92  TYR   B N   1 
ATOM   1465 C CA  . TYR   B 1 93 ? 20.545  -0.958  -27.940 1.00 51.59  ? 92  TYR   B CA  1 
ATOM   1466 C C   . TYR   B 1 93 ? 21.172  -0.831  -26.557 1.00 59.80  ? 92  TYR   B C   1 
ATOM   1467 O O   . TYR   B 1 93 ? 20.544  -1.191  -25.559 1.00 65.58  ? 92  TYR   B O   1 
ATOM   1468 C CB  . TYR   B 1 93 ? 19.896  -2.328  -28.165 1.00 43.48  ? 92  TYR   B CB  1 
ATOM   1469 C CG  . TYR   B 1 93 ? 18.899  -2.242  -29.302 1.00 37.49  ? 92  TYR   B CG  1 
ATOM   1470 C CD1 . TYR   B 1 93 ? 17.620  -1.755  -29.080 1.00 33.40  ? 92  TYR   B CD1 1 
ATOM   1471 C CD2 . TYR   B 1 93 ? 19.253  -2.629  -30.594 1.00 37.62  ? 92  TYR   B CD2 1 
ATOM   1472 C CE1 . TYR   B 1 93 ? 16.718  -1.617  -30.117 1.00 36.80  ? 92  TYR   B CE1 1 
ATOM   1473 C CE2 . TYR   B 1 93 ? 18.348  -2.511  -31.638 1.00 35.26  ? 92  TYR   B CE2 1 
ATOM   1474 C CZ  . TYR   B 1 93 ? 17.084  -2.005  -31.394 1.00 37.26  ? 92  TYR   B CZ  1 
ATOM   1475 O OH  . TYR   B 1 93 ? 16.152  -1.903  -32.392 1.00 40.25  ? 92  TYR   B OH  1 
ATOM   1476 N N   . SER   B 1 94 ? 22.398  -0.296  -26.536 1.00 75.81  ? 93  SER   B N   1 
ATOM   1477 C CA  . SER   B 1 94 ? 23.068  0.183   -25.337 1.00 89.12  ? 93  SER   B CA  1 
ATOM   1478 C C   . SER   B 1 94 ? 22.068  0.919   -24.429 1.00 102.40 ? 93  SER   B C   1 
ATOM   1479 O O   . SER   B 1 94 ? 21.186  1.622   -24.983 1.00 106.68 ? 93  SER   B O   1 
ATOM   1480 C CB  . SER   B 1 94 ? 24.235  1.075   -25.698 1.00 82.71  ? 93  SER   B CB  1 
ATOM   1481 O OG  . SER   B 1 94 ? 25.245  0.336   -26.370 1.00 72.56  ? 93  SER   B OG  1 
ATOM   1482 O OXT . SER   B 1 94 ? 22.192  0.755   -23.196 1.00 116.91 ? 93  SER   B OXT 1 
ATOM   1483 N N   . HIS   C 1 4  ? 33.067  -24.170 27.084  1.00 71.41  ? 3   HIS   C N   1 
ATOM   1484 C CA  . HIS   C 1 4  ? 32.015  -23.132 27.275  1.00 83.67  ? 3   HIS   C CA  1 
ATOM   1485 C C   . HIS   C 1 4  ? 31.273  -23.407 28.592  1.00 89.97  ? 3   HIS   C C   1 
ATOM   1486 O O   . HIS   C 1 4  ? 31.788  -24.099 29.471  1.00 88.90  ? 3   HIS   C O   1 
ATOM   1487 C CB  . HIS   C 1 4  ? 31.178  -23.035 25.990  1.00 88.43  ? 3   HIS   C CB  1 
ATOM   1488 C CG  . HIS   C 1 4  ? 30.393  -21.771 25.797  1.00 101.28 ? 3   HIS   C CG  1 
ATOM   1489 N ND1 . HIS   C 1 4  ? 29.155  -21.547 26.365  1.00 105.99 ? 3   HIS   C ND1 1 
ATOM   1490 C CD2 . HIS   C 1 4  ? 30.667  -20.673 25.080  1.00 100.35 ? 3   HIS   C CD2 1 
ATOM   1491 C CE1 . HIS   C 1 4  ? 28.708  -20.352 26.005  1.00 103.47 ? 3   HIS   C CE1 1 
ATOM   1492 N NE2 . HIS   C 1 4  ? 29.611  -19.804 25.224  1.00 102.60 ? 3   HIS   C NE2 1 
ATOM   1493 N N   . ALA   C 1 5  ? 30.062  -22.851 28.732  1.00 83.96  ? 4   ALA   C N   1 
ATOM   1494 C CA  . ALA   C 1 5  ? 29.250  -22.974 29.933  1.00 77.46  ? 4   ALA   C CA  1 
ATOM   1495 C C   . ALA   C 1 5  ? 27.772  -22.993 29.555  1.00 78.05  ? 4   ALA   C C   1 
ATOM   1496 O O   . ALA   C 1 5  ? 27.311  -22.117 28.823  1.00 81.43  ? 4   ALA   C O   1 
ATOM   1497 C CB  . ALA   C 1 5  ? 29.515  -21.775 30.794  1.00 82.40  ? 4   ALA   C CB  1 
ATOM   1498 N N   . PHE   C 1 6  ? 27.032  -23.971 30.089  1.00 64.69  ? 5   PHE   C N   1 
ATOM   1499 C CA  . PHE   C 1 6  ? 25.648  -24.165 29.686  1.00 60.59  ? 5   PHE   C CA  1 
ATOM   1500 C C   . PHE   C 1 6  ? 24.798  -24.335 30.939  1.00 65.74  ? 5   PHE   C C   1 
ATOM   1501 O O   . PHE   C 1 6  ? 25.084  -25.215 31.746  1.00 80.71  ? 5   PHE   C O   1 
ATOM   1502 C CB  . PHE   C 1 6  ? 25.451  -25.374 28.752  1.00 53.00  ? 5   PHE   C CB  1 
ATOM   1503 C CG  . PHE   C 1 6  ? 26.229  -25.354 27.438  1.00 48.07  ? 5   PHE   C CG  1 
ATOM   1504 C CD1 . PHE   C 1 6  ? 27.334  -26.172 27.244  1.00 45.60  ? 5   PHE   C CD1 1 
ATOM   1505 C CD2 . PHE   C 1 6  ? 25.860  -24.509 26.391  1.00 48.97  ? 5   PHE   C CD2 1 
ATOM   1506 C CE1 . PHE   C 1 6  ? 28.063  -26.147 26.052  1.00 47.34  ? 5   PHE   C CE1 1 
ATOM   1507 C CE2 . PHE   C 1 6  ? 26.581  -24.497 25.198  1.00 48.07  ? 5   PHE   C CE2 1 
ATOM   1508 C CZ  . PHE   C 1 6  ? 27.680  -25.305 25.025  1.00 44.20  ? 5   PHE   C CZ  1 
ATOM   1509 N N   . LYS   C 1 7  ? 23.769  -23.488 31.084  1.00 60.77  ? 6   LYS   C N   1 
ATOM   1510 C CA  . LYS   C 1 7  ? 22.788  -23.585 32.159  1.00 60.27  ? 6   LYS   C CA  1 
ATOM   1511 C C   . LYS   C 1 7  ? 21.465  -23.910 31.487  1.00 62.20  ? 6   LYS   C C   1 
ATOM   1512 O O   . LYS   C 1 7  ? 21.385  -23.789 30.269  1.00 67.86  ? 6   LYS   C O   1 
ATOM   1513 C CB  . LYS   C 1 7  ? 22.653  -22.285 32.968  1.00 54.35  ? 6   LYS   C CB  1 
ATOM   1514 N N   . PRO   C 1 8  ? 20.411  -24.355 32.213  1.00 66.68  ? 7   PRO   C N   1 
ATOM   1515 C CA  . PRO   C 1 8  ? 19.116  -24.611 31.574  1.00 66.42  ? 7   PRO   C CA  1 
ATOM   1516 C C   . PRO   C 1 8  ? 18.643  -23.385 30.794  1.00 70.34  ? 7   PRO   C C   1 
ATOM   1517 O O   . PRO   C 1 8  ? 18.909  -22.248 31.194  1.00 66.38  ? 7   PRO   C O   1 
ATOM   1518 C CB  . PRO   C 1 8  ? 18.175  -24.995 32.732  1.00 68.24  ? 7   PRO   C CB  1 
ATOM   1519 C CG  . PRO   C 1 8  ? 19.117  -25.489 33.813  1.00 69.36  ? 7   PRO   C CG  1 
ATOM   1520 C CD  . PRO   C 1 8  ? 20.410  -24.683 33.650  1.00 63.32  ? 7   PRO   C CD  1 
ATOM   1521 N N   . GLY   C 1 9  ? 17.979  -23.635 29.657  1.00 69.34  ? 8   GLY   C N   1 
ATOM   1522 C CA  . GLY   C 1 9  ? 17.431  -22.573 28.831  1.00 63.13  ? 8   GLY   C CA  1 
ATOM   1523 C C   . GLY   C 1 9  ? 18.324  -22.206 27.644  1.00 61.27  ? 8   GLY   C C   1 
ATOM   1524 O O   . GLY   C 1 9  ? 17.797  -21.802 26.611  1.00 74.85  ? 8   GLY   C O   1 
ATOM   1525 N N   . ASP   C 1 10 ? 19.655  -22.333 27.803  1.00 50.67  ? 9   ASP   C N   1 
ATOM   1526 C CA  . ASP   C 1 10 ? 20.627  -22.008 26.767  1.00 49.44  ? 9   ASP   C CA  1 
ATOM   1527 C C   . ASP   C 1 10 ? 20.296  -22.754 25.467  1.00 48.39  ? 9   ASP   C C   1 
ATOM   1528 O O   . ASP   C 1 10 ? 20.088  -23.967 25.463  1.00 40.54  ? 9   ASP   C O   1 
ATOM   1529 C CB  . ASP   C 1 10 ? 22.058  -22.308 27.197  1.00 52.08  ? 9   ASP   C CB  1 
ATOM   1530 C CG  . ASP   C 1 10 ? 22.654  -21.454 28.312  1.00 56.00  ? 9   ASP   C CG  1 
ATOM   1531 O OD1 . ASP   C 1 10 ? 21.947  -20.573 28.821  1.00 52.10  ? 9   ASP   C OD1 1 
ATOM   1532 O OD2 . ASP   C 1 10 ? 23.831  -21.679 28.666  1.00 58.65  ? 9   ASP   C OD2 1 
ATOM   1533 N N   . LEU   C 1 11 ? 20.257  -22.012 24.358  1.00 45.81  ? 10  LEU   C N   1 
ATOM   1534 C CA  . LEU   C 1 11 ? 19.926  -22.582 23.059  1.00 46.18  ? 10  LEU   C CA  1 
ATOM   1535 C C   . LEU   C 1 11 ? 21.189  -23.105 22.386  1.00 42.12  ? 10  LEU   C C   1 
ATOM   1536 O O   . LEU   C 1 11 ? 22.208  -22.421 22.355  1.00 42.33  ? 10  LEU   C O   1 
ATOM   1537 C CB  . LEU   C 1 11 ? 19.233  -21.516 22.206  1.00 45.04  ? 10  LEU   C CB  1 
ATOM   1538 C CG  . LEU   C 1 11 ? 17.968  -20.903 22.812  1.00 43.98  ? 10  LEU   C CG  1 
ATOM   1539 C CD1 . LEU   C 1 11 ? 17.303  -19.990 21.801  1.00 50.03  ? 10  LEU   C CD1 1 
ATOM   1540 C CD2 . LEU   C 1 11 ? 17.014  -22.004 23.247  1.00 47.15  ? 10  LEU   C CD2 1 
ATOM   1541 N N   . VAL   C 1 12 ? 21.100  -24.305 21.794  1.00 39.01  ? 11  VAL   C N   1 
ATOM   1542 C CA  . VAL   C 1 12 ? 22.275  -24.907 21.183  1.00 35.18  ? 11  VAL   C CA  1 
ATOM   1543 C C   . VAL   C 1 12 ? 21.857  -25.672 19.916  1.00 35.25  ? 11  VAL   C C   1 
ATOM   1544 O O   . VAL   C 1 12 ? 20.661  -25.891 19.700  1.00 33.82  ? 11  VAL   C O   1 
ATOM   1545 C CB  . VAL   C 1 12 ? 22.910  -25.879 22.203  1.00 37.73  ? 11  VAL   C CB  1 
ATOM   1546 C CG1 . VAL   C 1 12 ? 23.286  -25.176 23.512  1.00 37.72  ? 11  VAL   C CG1 1 
ATOM   1547 C CG2 . VAL   C 1 12 ? 22.011  -27.087 22.474  1.00 30.90  ? 11  VAL   C CG2 1 
ATOM   1548 N N   . PHE   C 1 13 ? 22.873  -26.076 19.126  1.00 34.65  ? 12  PHE   C N   1 
ATOM   1549 C CA  . PHE   C 1 13 ? 22.856  -27.251 18.269  1.00 33.98  ? 12  PHE   C CA  1 
ATOM   1550 C C   . PHE   C 1 13 ? 23.562  -28.393 19.000  1.00 33.51  ? 12  PHE   C C   1 
ATOM   1551 O O   . PHE   C 1 13 ? 24.630  -28.225 19.579  1.00 33.60  ? 12  PHE   C O   1 
ATOM   1552 C CB  . PHE   C 1 13 ? 23.482  -27.034 16.882  1.00 35.24  ? 12  PHE   C CB  1 
ATOM   1553 C CG  . PHE   C 1 13 ? 22.743  -26.004 16.042  1.00 37.95  ? 12  PHE   C CG  1 
ATOM   1554 C CD1 . PHE   C 1 13 ? 21.696  -26.386 15.204  1.00 33.38  ? 12  PHE   C CD1 1 
ATOM   1555 C CD2 . PHE   C 1 13 ? 23.083  -24.651 16.112  1.00 36.64  ? 12  PHE   C CD2 1 
ATOM   1556 C CE1 . PHE   C 1 13 ? 21.030  -25.433 14.447  1.00 34.92  ? 12  PHE   C CE1 1 
ATOM   1557 C CE2 . PHE   C 1 13 ? 22.401  -23.704 15.370  1.00 38.56  ? 12  PHE   C CE2 1 
ATOM   1558 C CZ  . PHE   C 1 13 ? 21.376  -24.097 14.533  1.00 41.88  ? 12  PHE   C CZ  1 
ATOM   1559 N N   . ALA   C 1 14 ? 22.935  -29.562 18.962  1.00 30.33  ? 13  ALA   C N   1 
ATOM   1560 C CA  . ALA   C 1 14 ? 23.335  -30.715 19.748  1.00 31.51  ? 13  ALA   C CA  1 
ATOM   1561 C C   . ALA   C 1 14 ? 23.612  -31.854 18.778  1.00 32.95  ? 13  ALA   C C   1 
ATOM   1562 O O   . ALA   C 1 14 ? 22.731  -32.187 17.979  1.00 28.75  ? 13  ALA   C O   1 
ATOM   1563 C CB  . ALA   C 1 14 ? 22.183  -31.107 20.648  1.00 31.17  ? 13  ALA   C CB  1 
ATOM   1564 N N   . LYS   C 1 15 ? 24.830  -32.412 18.832  1.00 34.08  ? 14  LYS   C N   1 
ATOM   1565 C CA  . LYS   C 1 15 ? 25.233  -33.399 17.842  1.00 32.78  ? 14  LYS   C CA  1 
ATOM   1566 C C   . LYS   C 1 15 ? 25.203  -34.777 18.483  1.00 33.73  ? 14  LYS   C C   1 
ATOM   1567 O O   . LYS   C 1 15 ? 25.876  -34.997 19.479  1.00 36.02  ? 14  LYS   C O   1 
ATOM   1568 C CB  . LYS   C 1 15 ? 26.648  -33.194 17.264  1.00 36.83  ? 14  LYS   C CB  1 
ATOM   1569 C CG  . LYS   C 1 15 ? 27.126  -34.216 16.212  1.00 32.70  ? 14  LYS   C CG  1 
ATOM   1570 C CD  . LYS   C 1 15 ? 26.373  -34.151 14.880  1.00 34.77  ? 14  LYS   C CD  1 
ATOM   1571 C CE  . LYS   C 1 15 ? 26.913  -35.037 13.768  1.00 35.47  ? 14  LYS   C CE  1 
ATOM   1572 N NZ  . LYS   C 1 15 ? 26.543  -36.446 13.996  1.00 31.57  ? 14  LYS   C NZ  1 
ATOM   1573 N N   . MET   C 1 16 ? 24.447  -35.696 17.876  1.00 33.32  ? 15  MET   C N   1 
ATOM   1574 C CA  . MET   C 1 16 ? 24.480  -37.107 18.227  1.00 31.60  ? 15  MET   C CA  1 
ATOM   1575 C C   . MET   C 1 16 ? 24.897  -37.919 17.000  1.00 36.14  ? 15  MET   C C   1 
ATOM   1576 O O   . MET   C 1 16 ? 24.607  -37.532 15.865  1.00 29.54  ? 15  MET   C O   1 
ATOM   1577 C CB  . MET   C 1 16 ? 23.075  -37.587 18.614  1.00 31.92  ? 15  MET   C CB  1 
ATOM   1578 C CG  . MET   C 1 16 ? 22.475  -36.827 19.779  1.00 41.55  ? 15  MET   C CG  1 
ATOM   1579 S SD  . MET   C 1 16 ? 21.030  -37.609 20.525  1.00 47.18  ? 15  MET   C SD  1 
ATOM   1580 C CE  . MET   C 1 16 ? 21.764  -39.050 21.321  1.00 49.63  ? 15  MET   C CE  1 
ATOM   1581 N N   . LYS   C 1 17 ? 25.536  -39.067 17.237  1.00 35.94  ? 16  LYS   C N   1 
ATOM   1582 C CA  . LYS   C 1 17 ? 25.927  -39.958 16.154  1.00 39.76  ? 16  LYS   C CA  1 
ATOM   1583 C C   . LYS   C 1 17 ? 24.670  -40.366 15.378  1.00 34.23  ? 16  LYS   C C   1 
ATOM   1584 O O   . LYS   C 1 17 ? 23.693  -40.797 15.961  1.00 33.76  ? 16  LYS   C O   1 
ATOM   1585 C CB  . LYS   C 1 17 ? 26.570  -41.207 16.782  1.00 38.87  ? 16  LYS   C CB  1 
ATOM   1586 C CG  . LYS   C 1 17 ? 27.183  -42.216 15.833  1.00 43.79  ? 16  LYS   C CG  1 
ATOM   1587 C CD  . LYS   C 1 17 ? 28.388  -41.584 15.148  1.00 50.10  ? 16  LYS   C CD  1 
ATOM   1588 C CE  . LYS   C 1 17 ? 29.130  -42.556 14.277  1.00 58.67  ? 16  LYS   C CE  1 
ATOM   1589 N NZ  . LYS   C 1 17 ? 30.279  -41.872 13.677  1.00 54.05  ? 16  LYS   C NZ  1 
ATOM   1590 N N   . GLY   C 1 18 ? 24.707  -40.240 14.062  1.00 38.97  ? 17  GLY   C N   1 
ATOM   1591 C CA  . GLY   C 1 18 ? 23.582  -40.695 13.266  1.00 38.83  ? 17  GLY   C CA  1 
ATOM   1592 C C   . GLY   C 1 18 ? 22.656  -39.539 12.885  1.00 39.64  ? 17  GLY   C C   1 
ATOM   1593 O O   . GLY   C 1 18 ? 21.634  -39.750 12.233  1.00 39.60  ? 17  GLY   C O   1 
ATOM   1594 N N   . TYR   C 1 19 ? 22.994  -38.321 13.329  1.00 38.76  ? 18  TYR   C N   1 
ATOM   1595 C CA  . TYR   C 1 19 ? 22.073  -37.194 13.190  1.00 37.89  ? 18  TYR   C CA  1 
ATOM   1596 C C   . TYR   C 1 19 ? 22.862  -35.929 12.899  1.00 34.62  ? 18  TYR   C C   1 
ATOM   1597 O O   . TYR   C 1 19 ? 23.982  -35.760 13.392  1.00 33.24  ? 18  TYR   C O   1 
ATOM   1598 C CB  . TYR   C 1 19 ? 21.165  -36.859 14.376  1.00 33.00  ? 18  TYR   C CB  1 
ATOM   1599 C CG  . TYR   C 1 19 ? 20.333  -38.038 14.841  1.00 35.39  ? 18  TYR   C CG  1 
ATOM   1600 C CD1 . TYR   C 1 19 ? 20.898  -39.098 15.563  1.00 31.15  ? 18  TYR   C CD1 1 
ATOM   1601 C CD2 . TYR   C 1 19 ? 18.982  -38.083 14.559  1.00 35.16  ? 18  TYR   C CD2 1 
ATOM   1602 C CE1 . TYR   C 1 19 ? 20.118  -40.163 15.987  1.00 34.98  ? 18  TYR   C CE1 1 
ATOM   1603 C CE2 . TYR   C 1 19 ? 18.203  -39.148 14.978  1.00 38.79  ? 18  TYR   C CE2 1 
ATOM   1604 C CZ  . TYR   C 1 19 ? 18.771  -40.194 15.682  1.00 38.08  ? 18  TYR   C CZ  1 
ATOM   1605 O OH  . TYR   C 1 19 ? 17.946  -41.218 16.065  1.00 48.01  ? 18  TYR   C OH  1 
ATOM   1606 N N   . PRO   C 1 20 ? 22.266  -35.030 12.084  1.00 34.37  ? 19  PRO   C N   1 
ATOM   1607 C CA  . PRO   C 1 20 ? 22.844  -33.709 11.840  1.00 33.00  ? 19  PRO   C CA  1 
ATOM   1608 C C   . PRO   C 1 20 ? 22.805  -32.905 13.146  1.00 33.71  ? 19  PRO   C C   1 
ATOM   1609 O O   . PRO   C 1 20 ? 22.035  -33.226 14.069  1.00 28.78  ? 19  PRO   C O   1 
ATOM   1610 C CB  . PRO   C 1 20 ? 21.908  -33.142 10.758  1.00 34.94  ? 19  PRO   C CB  1 
ATOM   1611 C CG  . PRO   C 1 20 ? 20.575  -33.819 11.040  1.00 39.62  ? 19  PRO   C CG  1 
ATOM   1612 C CD  . PRO   C 1 20 ? 20.959  -35.237 11.433  1.00 31.99  ? 19  PRO   C CD  1 
ATOM   1613 N N   . HIS   C 1 21 ? 23.675  -31.892 13.240  1.00 32.72  ? 20  HIS   C N   1 
ATOM   1614 C CA  . HIS   C 1 21 ? 23.611  -30.942 14.352  1.00 32.08  ? 20  HIS   C CA  1 
ATOM   1615 C C   . HIS   C 1 21 ? 22.181  -30.411 14.474  1.00 35.30  ? 20  HIS   C C   1 
ATOM   1616 O O   . HIS   C 1 21 ? 21.617  -29.895 13.502  1.00 32.89  ? 20  HIS   C O   1 
ATOM   1617 C CB  . HIS   C 1 21 ? 24.582  -29.783 14.121  1.00 34.49  ? 20  HIS   C CB  1 
ATOM   1618 C CG  . HIS   C 1 21 ? 26.010  -30.221 14.127  1.00 35.38  ? 20  HIS   C CG  1 
ATOM   1619 N ND1 . HIS   C 1 21 ? 26.655  -30.770 13.039  1.00 35.49  ? 20  HIS   C ND1 1 
ATOM   1620 C CD2 . HIS   C 1 21 ? 26.909  -30.212 15.140  1.00 38.65  ? 20  HIS   C CD2 1 
ATOM   1621 C CE1 . HIS   C 1 21 ? 27.902  -31.077 13.393  1.00 38.86  ? 20  HIS   C CE1 1 
ATOM   1622 N NE2 . HIS   C 1 21 ? 28.078  -30.712 14.654  1.00 35.94  ? 20  HIS   C NE2 1 
ATOM   1623 N N   . TRP   C 1 22 ? 21.589  -30.560 15.674  1.00 31.69  ? 21  TRP   C N   1 
ATOM   1624 C CA  . TRP   C 1 22 ? 20.146  -30.445 15.797  1.00 29.75  ? 21  TRP   C CA  1 
ATOM   1625 C C   . TRP   C 1 22 ? 19.795  -29.300 16.740  1.00 30.72  ? 21  TRP   C C   1 
ATOM   1626 O O   . TRP   C 1 22 ? 20.384  -29.187 17.810  1.00 30.66  ? 21  TRP   C O   1 
ATOM   1627 C CB  . TRP   C 1 22 ? 19.559  -31.759 16.320  1.00 31.12  ? 21  TRP   C CB  1 
ATOM   1628 C CG  . TRP   C 1 22 ? 18.103  -31.935 15.985  1.00 31.55  ? 21  TRP   C CG  1 
ATOM   1629 C CD1 . TRP   C 1 22 ? 16.997  -31.368 16.561  1.00 33.69  ? 21  TRP   C CD1 1 
ATOM   1630 C CD2 . TRP   C 1 22 ? 17.613  -32.825 14.953  1.00 31.18  ? 21  TRP   C CD2 1 
ATOM   1631 N NE1 . TRP   C 1 22 ? 15.853  -31.837 15.943  1.00 31.96  ? 21  TRP   C NE1 1 
ATOM   1632 C CE2 . TRP   C 1 22 ? 16.203  -32.735 14.966  1.00 30.14  ? 21  TRP   C CE2 1 
ATOM   1633 C CE3 . TRP   C 1 22 ? 18.235  -33.699 14.046  1.00 29.04  ? 21  TRP   C CE3 1 
ATOM   1634 C CZ2 . TRP   C 1 22 ? 15.416  -33.481 14.088  1.00 31.29  ? 21  TRP   C CZ2 1 
ATOM   1635 C CZ3 . TRP   C 1 22 ? 17.444  -34.444 13.187  1.00 32.60  ? 21  TRP   C CZ3 1 
ATOM   1636 C CH2 . TRP   C 1 22 ? 16.056  -34.357 13.237  1.00 28.99  ? 21  TRP   C CH2 1 
ATOM   1637 N N   . PRO   C 1 23 ? 18.826  -28.427 16.376  1.00 35.89  ? 22  PRO   C N   1 
ATOM   1638 C CA  . PRO   C 1 23 ? 18.415  -27.319 17.238  1.00 31.66  ? 22  PRO   C CA  1 
ATOM   1639 C C   . PRO   C 1 23 ? 17.851  -27.874 18.534  1.00 28.91  ? 22  PRO   C C   1 
ATOM   1640 O O   . PRO   C 1 23 ? 16.893  -28.650 18.517  1.00 29.48  ? 22  PRO   C O   1 
ATOM   1641 C CB  . PRO   C 1 23 ? 17.311  -26.655 16.409  1.00 31.74  ? 22  PRO   C CB  1 
ATOM   1642 C CG  . PRO   C 1 23 ? 16.742  -27.802 15.578  1.00 30.49  ? 22  PRO   C CG  1 
ATOM   1643 C CD  . PRO   C 1 23 ? 18.045  -28.482 15.124  1.00 31.93  ? 22  PRO   C CD  1 
ATOM   1644 N N   . ALA   C 1 24 ? 18.409  -27.404 19.658  1.00 29.67  ? 23  ALA   C N   1 
ATOM   1645 C CA  . ALA   C 1 24 ? 18.056  -27.953 20.964  1.00 35.26  ? 23  ALA   C CA  1 
ATOM   1646 C C   . ALA   C 1 24 ? 18.186  -26.884 22.052  1.00 35.81  ? 23  ALA   C C   1 
ATOM   1647 O O   . ALA   C 1 24 ? 18.609  -25.753 21.795  1.00 33.81  ? 23  ALA   C O   1 
ATOM   1648 C CB  . ALA   C 1 24 ? 18.959  -29.140 21.254  1.00 30.38  ? 23  ALA   C CB  1 
ATOM   1649 N N   . ARG   C 1 25 ? 17.836  -27.255 23.289  1.00 40.60  ? 24  ARG   C N   1 
ATOM   1650 C CA  . ARG   C 1 25 ? 18.207  -26.443 24.441  1.00 40.40  ? 24  ARG   C CA  1 
ATOM   1651 C C   . ARG   C 1 25 ? 18.620  -27.347 25.611  1.00 38.80  ? 24  ARG   C C   1 
ATOM   1652 O O   . ARG   C 1 25 ? 18.202  -28.507 25.668  1.00 35.58  ? 24  ARG   C O   1 
ATOM   1653 C CB  . ARG   C 1 25 ? 17.018  -25.565 24.838  1.00 37.06  ? 24  ARG   C CB  1 
ATOM   1654 C CG  . ARG   C 1 25 ? 15.779  -26.344 25.243  1.00 39.38  ? 24  ARG   C CG  1 
ATOM   1655 C CD  . ARG   C 1 25 ? 14.778  -25.513 26.048  1.00 47.64  ? 24  ARG   C CD  1 
ATOM   1656 N NE  . ARG   C 1 25 ? 13.560  -26.310 26.249  1.00 52.78  ? 24  ARG   C NE  1 
ATOM   1657 C CZ  . ARG   C 1 25 ? 12.302  -25.986 25.944  1.00 57.52  ? 24  ARG   C CZ  1 
ATOM   1658 N NH1 . ARG   C 1 25 ? 12.000  -24.794 25.463  1.00 54.32  ? 24  ARG   C NH1 1 
ATOM   1659 N NH2 . ARG   C 1 25 ? 11.328  -26.855 26.153  1.00 60.62  ? 24  ARG   C NH2 1 
ATOM   1660 N N   . ILE   C 1 26 ? 19.399  -26.773 26.545  1.00 39.94  ? 25  ILE   C N   1 
ATOM   1661 C CA  . ILE   C 1 26 ? 19.680  -27.340 27.858  1.00 42.58  ? 25  ILE   C CA  1 
ATOM   1662 C C   . ILE   C 1 26 ? 18.411  -27.323 28.712  1.00 50.29  ? 25  ILE   C C   1 
ATOM   1663 O O   . ILE   C 1 26 ? 17.832  -26.266 28.951  1.00 52.19  ? 25  ILE   C O   1 
ATOM   1664 C CB  . ILE   C 1 26 ? 20.783  -26.523 28.561  1.00 42.73  ? 25  ILE   C CB  1 
ATOM   1665 C CG1 . ILE   C 1 26 ? 21.941  -26.173 27.634  1.00 43.87  ? 25  ILE   C CG1 1 
ATOM   1666 C CG2 . ILE   C 1 26 ? 21.260  -27.207 29.850  1.00 40.31  ? 25  ILE   C CG2 1 
ATOM   1667 C CD1 . ILE   C 1 26 ? 22.845  -27.332 27.264  1.00 44.63  ? 25  ILE   C CD1 1 
ATOM   1668 N N   . ASP   C 1 27 ? 17.999  -28.497 29.198  1.00 51.82  ? 26  ASP   C N   1 
ATOM   1669 C CA  . ASP   C 1 27 ? 16.896  -28.595 30.141  1.00 56.30  ? 26  ASP   C CA  1 
ATOM   1670 C C   . ASP   C 1 27 ? 17.354  -28.223 31.558  1.00 59.21  ? 26  ASP   C C   1 
ATOM   1671 O O   . ASP   C 1 27 ? 18.008  -29.071 32.198  1.00 67.72  ? 26  ASP   C O   1 
ATOM   1672 C CB  . ASP   C 1 27 ? 16.229  -29.958 30.099  1.00 56.04  ? 26  ASP   C CB  1 
ATOM   1673 C CG  . ASP   C 1 27 ? 15.007  -30.036 29.201  1.00 64.23  ? 26  ASP   C CG  1 
ATOM   1674 O OD1 . ASP   C 1 27 ? 14.767  -29.046 28.469  1.00 62.89  ? 26  ASP   C OD1 1 
ATOM   1675 O OD2 . ASP   C 1 27 ? 14.288  -31.061 29.288  1.00 61.66  ? 26  ASP   C OD2 1 
ATOM   1676 N N   . LYS   C 1 35 ? 19.548  -38.910 37.668  1.00 67.65  ? 34  LYS   C N   1 
ATOM   1677 C CA  . LYS   C 1 35 ? 20.693  -37.959 37.571  1.00 66.37  ? 34  LYS   C CA  1 
ATOM   1678 C C   . LYS   C 1 35 ? 21.415  -38.201 36.245  1.00 61.59  ? 34  LYS   C C   1 
ATOM   1679 O O   . LYS   C 1 35 ? 21.484  -39.330 35.761  1.00 52.55  ? 34  LYS   C O   1 
ATOM   1680 C CB  . LYS   C 1 35 ? 21.634  -38.047 38.782  1.00 62.71  ? 34  LYS   C CB  1 
ATOM   1681 N N   . PRO   C 1 36 ? 21.977  -37.159 35.595  1.00 63.12  ? 35  PRO   C N   1 
ATOM   1682 C CA  . PRO   C 1 36 ? 22.659  -37.370 34.318  1.00 64.04  ? 35  PRO   C CA  1 
ATOM   1683 C C   . PRO   C 1 36 ? 23.832  -38.335 34.516  1.00 63.71  ? 35  PRO   C C   1 
ATOM   1684 O O   . PRO   C 1 36 ? 24.333  -38.506 35.633  1.00 57.15  ? 35  PRO   C O   1 
ATOM   1685 C CB  . PRO   C 1 36 ? 23.121  -35.962 33.867  1.00 64.51  ? 35  PRO   C CB  1 
ATOM   1686 C CG  . PRO   C 1 36 ? 22.454  -34.992 34.824  1.00 64.60  ? 35  PRO   C CG  1 
ATOM   1687 C CD  . PRO   C 1 36 ? 22.031  -35.765 36.069  1.00 65.35  ? 35  PRO   C CD  1 
ATOM   1688 N N   . PRO   C 1 37 ? 24.311  -39.016 33.450  1.00 58.20  ? 36  PRO   C N   1 
ATOM   1689 C CA  . PRO   C 1 37 ? 25.634  -39.636 33.505  1.00 55.00  ? 36  PRO   C CA  1 
ATOM   1690 C C   . PRO   C 1 37 ? 26.646  -38.536 33.834  1.00 51.50  ? 36  PRO   C C   1 
ATOM   1691 O O   . PRO   C 1 37 ? 26.360  -37.342 33.667  1.00 43.86  ? 36  PRO   C O   1 
ATOM   1692 C CB  . PRO   C 1 37 ? 25.815  -40.255 32.110  1.00 52.26  ? 36  PRO   C CB  1 
ATOM   1693 C CG  . PRO   C 1 37 ? 24.391  -40.410 31.621  1.00 52.02  ? 36  PRO   C CG  1 
ATOM   1694 C CD  . PRO   C 1 37 ? 23.625  -39.222 32.162  1.00 55.01  ? 36  PRO   C CD  1 
ATOM   1695 N N   . PRO   C 1 38 ? 27.826  -38.903 34.393  1.00 48.00  ? 37  PRO   C N   1 
ATOM   1696 C CA  . PRO   C 1 38 ? 28.846  -37.919 34.760  1.00 45.56  ? 37  PRO   C CA  1 
ATOM   1697 C C   . PRO   C 1 38 ? 29.154  -36.998 33.590  1.00 45.39  ? 37  PRO   C C   1 
ATOM   1698 O O   . PRO   C 1 38 ? 29.373  -37.475 32.477  1.00 46.58  ? 37  PRO   C O   1 
ATOM   1699 C CB  . PRO   C 1 38 ? 30.052  -38.818 35.093  1.00 49.47  ? 37  PRO   C CB  1 
ATOM   1700 C CG  . PRO   C 1 38 ? 29.423  -40.107 35.598  1.00 48.52  ? 37  PRO   C CG  1 
ATOM   1701 C CD  . PRO   C 1 38 ? 28.215  -40.290 34.710  1.00 47.88  ? 37  PRO   C CD  1 
ATOM   1702 N N   . ASN   C 1 39 ? 29.112  -35.685 33.855  1.00 46.89  ? 38  ASN   C N   1 
ATOM   1703 C CA  . ASN   C 1 39 ? 29.565  -34.655 32.935  1.00 43.69  ? 38  ASN   C CA  1 
ATOM   1704 C C   . ASN   C 1 39 ? 28.624  -34.517 31.732  1.00 48.63  ? 38  ASN   C C   1 
ATOM   1705 O O   . ASN   C 1 39 ? 29.026  -33.978 30.694  1.00 52.62  ? 38  ASN   C O   1 
ATOM   1706 C CB  . ASN   C 1 39 ? 31.020  -34.862 32.520  1.00 46.24  ? 38  ASN   C CB  1 
ATOM   1707 C CG  . ASN   C 1 39 ? 31.606  -33.662 31.808  1.00 59.38  ? 38  ASN   C CG  1 
ATOM   1708 O OD1 . ASN   C 1 39 ? 31.184  -32.519 32.047  1.00 63.79  ? 38  ASN   C OD1 1 
ATOM   1709 N ND2 . ASN   C 1 39 ? 32.574  -33.893 30.927  1.00 54.75  ? 38  ASN   C ND2 1 
ATOM   1710 N N   . LYS   C 1 40 ? 27.367  -34.956 31.867  1.00 40.11  ? 39  LYS   C N   1 
ATOM   1711 C CA  . LYS   C 1 40 ? 26.445  -34.896 30.744  1.00 37.78  ? 39  LYS   C CA  1 
ATOM   1712 C C   . LYS   C 1 40 ? 25.339  -33.896 31.037  1.00 42.90  ? 39  LYS   C C   1 
ATOM   1713 O O   . LYS   C 1 40 ? 24.909  -33.786 32.178  1.00 42.78  ? 39  LYS   C O   1 
ATOM   1714 C CB  . LYS   C 1 40 ? 25.753  -36.244 30.516  1.00 33.38  ? 39  LYS   C CB  1 
ATOM   1715 C CG  . LYS   C 1 40 ? 26.648  -37.405 30.165  1.00 35.85  ? 39  LYS   C CG  1 
ATOM   1716 C CD  . LYS   C 1 40 ? 27.262  -37.382 28.779  1.00 41.56  ? 39  LYS   C CD  1 
ATOM   1717 C CE  . LYS   C 1 40 ? 28.191  -38.543 28.549  1.00 43.76  ? 39  LYS   C CE  1 
ATOM   1718 N NZ  . LYS   C 1 40 ? 29.204  -38.221 27.537  1.00 52.00  ? 39  LYS   C NZ  1 
ATOM   1719 N N   . TYR   C 1 41 ? 24.873  -33.188 29.999  1.00 40.15  ? 40  TYR   C N   1 
ATOM   1720 C CA  . TYR   C 1 41 ? 23.773  -32.235 30.130  1.00 38.56  ? 40  TYR   C CA  1 
ATOM   1721 C C   . TYR   C 1 41 ? 22.495  -32.881 29.618  1.00 38.13  ? 40  TYR   C C   1 
ATOM   1722 O O   . TYR   C 1 41 ? 22.538  -33.699 28.691  1.00 37.07  ? 40  TYR   C O   1 
ATOM   1723 C CB  . TYR   C 1 41 ? 23.894  -30.935 29.320  1.00 34.08  ? 40  TYR   C CB  1 
ATOM   1724 C CG  . TYR   C 1 41 ? 25.084  -30.076 29.704  1.00 39.83  ? 40  TYR   C CG  1 
ATOM   1725 C CD1 . TYR   C 1 41 ? 26.364  -30.363 29.222  1.00 39.22  ? 40  TYR   C CD1 1 
ATOM   1726 C CD2 . TYR   C 1 41 ? 24.932  -28.989 30.573  1.00 40.73  ? 40  TYR   C CD2 1 
ATOM   1727 C CE1 . TYR   C 1 41 ? 27.456  -29.596 29.597  1.00 48.24  ? 40  TYR   C CE1 1 
ATOM   1728 C CE2 . TYR   C 1 41 ? 26.019  -28.200 30.925  1.00 41.16  ? 40  TYR   C CE2 1 
ATOM   1729 C CZ  . TYR   C 1 41 ? 27.281  -28.520 30.457  1.00 50.66  ? 40  TYR   C CZ  1 
ATOM   1730 O OH  . TYR   C 1 41 ? 28.349  -27.758 30.831  1.00 60.85  ? 40  TYR   C OH  1 
ATOM   1731 N N   . PRO   C 1 42 ? 21.329  -32.512 30.207  1.00 39.08  ? 41  PRO   C N   1 
ATOM   1732 C CA  . PRO   C 1 42 ? 20.029  -33.006 29.745  1.00 35.70  ? 41  PRO   C CA  1 
ATOM   1733 C C   . PRO   C 1 42 ? 19.612  -32.110 28.581  1.00 41.04  ? 41  PRO   C C   1 
ATOM   1734 O O   . PRO   C 1 42 ? 19.540  -30.888 28.728  1.00 39.64  ? 41  PRO   C O   1 
ATOM   1735 C CB  . PRO   C 1 42 ? 19.114  -32.840 30.956  1.00 34.96  ? 41  PRO   C CB  1 
ATOM   1736 C CG  . PRO   C 1 42 ? 19.780  -31.753 31.766  1.00 38.48  ? 41  PRO   C CG  1 
ATOM   1737 C CD  . PRO   C 1 42 ? 21.234  -31.628 31.384  1.00 38.10  ? 41  PRO   C CD  1 
ATOM   1738 N N   . ILE   C 1 43 ? 19.362  -32.739 27.425  1.00 37.81  ? 42  ILE   C N   1 
ATOM   1739 C CA  . ILE   C 1 43 ? 19.107  -31.986 26.200  1.00 36.71  ? 42  ILE   C CA  1 
ATOM   1740 C C   . ILE   C 1 43 ? 17.670  -32.242 25.765  1.00 40.92  ? 42  ILE   C C   1 
ATOM   1741 O O   . ILE   C 1 43 ? 17.190  -33.383 25.792  1.00 45.48  ? 42  ILE   C O   1 
ATOM   1742 C CB  . ILE   C 1 43 ? 20.118  -32.360 25.093  1.00 34.19  ? 42  ILE   C CB  1 
ATOM   1743 C CG1 . ILE   C 1 43 ? 21.581  -32.074 25.510  1.00 32.03  ? 42  ILE   C CG1 1 
ATOM   1744 C CG2 . ILE   C 1 43 ? 19.763  -31.733 23.736  1.00 33.37  ? 42  ILE   C CG2 1 
ATOM   1745 C CD1 . ILE   C 1 43 ? 21.902  -30.636 25.877  1.00 32.70  ? 42  ILE   C CD1 1 
ATOM   1746 N N   . PHE   C 1 44 ? 16.995  -31.167 25.347  1.00 41.32  ? 43  PHE   C N   1 
ATOM   1747 C CA  . PHE   C 1 44 ? 15.714  -31.301 24.681  1.00 34.86  ? 43  PHE   C CA  1 
ATOM   1748 C C   . PHE   C 1 44 ? 15.863  -30.858 23.228  1.00 35.25  ? 43  PHE   C C   1 
ATOM   1749 O O   . PHE   C 1 44 ? 16.396  -29.783 22.967  1.00 36.86  ? 43  PHE   C O   1 
ATOM   1750 C CB  . PHE   C 1 44 ? 14.782  -30.299 25.362  1.00 40.24  ? 43  PHE   C CB  1 
ATOM   1751 C CG  . PHE   C 1 44 ? 13.408  -30.229 24.713  1.00 42.61  ? 43  PHE   C CG  1 
ATOM   1752 C CD1 . PHE   C 1 44 ? 12.507  -31.286 24.856  1.00 40.24  ? 43  PHE   C CD1 1 
ATOM   1753 C CD2 . PHE   C 1 44 ? 13.016  -29.099 23.984  1.00 47.56  ? 43  PHE   C CD2 1 
ATOM   1754 C CE1 . PHE   C 1 44 ? 11.249  -31.228 24.268  1.00 46.67  ? 43  PHE   C CE1 1 
ATOM   1755 C CE2 . PHE   C 1 44 ? 11.761  -29.046 23.387  1.00 46.76  ? 43  PHE   C CE2 1 
ATOM   1756 C CZ  . PHE   C 1 44 ? 10.882  -30.109 23.530  1.00 46.89  ? 43  PHE   C CZ  1 
ATOM   1757 N N   . PHE   C 1 45 ? 15.384  -31.700 22.316  1.00 34.73  ? 44  PHE   C N   1 
ATOM   1758 C CA  . PHE   C 1 45 ? 15.528  -31.503 20.884  1.00 37.67  ? 44  PHE   C CA  1 
ATOM   1759 C C   . PHE   C 1 45 ? 14.262  -30.830 20.357  1.00 35.32  ? 44  PHE   C C   1 
ATOM   1760 O O   . PHE   C 1 45 ? 13.164  -31.357 20.531  1.00 36.88  ? 44  PHE   C O   1 
ATOM   1761 C CB  . PHE   C 1 45 ? 15.818  -32.830 20.176  1.00 30.92  ? 44  PHE   C CB  1 
ATOM   1762 C CG  . PHE   C 1 45 ? 17.210  -33.395 20.435  1.00 33.29  ? 44  PHE   C CG  1 
ATOM   1763 C CD1 . PHE   C 1 45 ? 18.308  -32.987 19.674  1.00 32.07  ? 44  PHE   C CD1 1 
ATOM   1764 C CD2 . PHE   C 1 45 ? 17.427  -34.321 21.467  1.00 31.04  ? 44  PHE   C CD2 1 
ATOM   1765 C CE1 . PHE   C 1 45 ? 19.589  -33.480 19.933  1.00 31.28  ? 44  PHE   C CE1 1 
ATOM   1766 C CE2 . PHE   C 1 45 ? 18.696  -34.838 21.704  1.00 31.11  ? 44  PHE   C CE2 1 
ATOM   1767 C CZ  . PHE   C 1 45 ? 19.772  -34.402 20.952  1.00 32.15  ? 44  PHE   C CZ  1 
ATOM   1768 N N   . PHE   C 1 46 ? 14.426  -29.679 19.683  1.00 34.32  ? 45  PHE   C N   1 
ATOM   1769 C CA  . PHE   C 1 46 ? 13.277  -29.045 19.053  1.00 32.25  ? 45  PHE   C CA  1 
ATOM   1770 C C   . PHE   C 1 46 ? 12.788  -29.900 17.887  1.00 31.78  ? 45  PHE   C C   1 
ATOM   1771 O O   . PHE   C 1 46 ? 13.558  -30.650 17.283  1.00 35.17  ? 45  PHE   C O   1 
ATOM   1772 C CB  . PHE   C 1 46 ? 13.566  -27.610 18.604  1.00 33.06  ? 45  PHE   C CB  1 
ATOM   1773 C CG  . PHE   C 1 46 ? 13.892  -26.632 19.722  1.00 35.08  ? 45  PHE   C CG  1 
ATOM   1774 C CD1 . PHE   C 1 46 ? 12.891  -26.164 20.570  1.00 37.65  ? 45  PHE   C CD1 1 
ATOM   1775 C CD2 . PHE   C 1 46 ? 15.189  -26.163 19.894  1.00 33.81  ? 45  PHE   C CD2 1 
ATOM   1776 C CE1 . PHE   C 1 46 ? 13.193  -25.252 21.577  1.00 37.74  ? 45  PHE   C CE1 1 
ATOM   1777 C CE2 . PHE   C 1 46 ? 15.474  -25.244 20.889  1.00 36.66  ? 45  PHE   C CE2 1 
ATOM   1778 C CZ  . PHE   C 1 46 ? 14.484  -24.806 21.734  1.00 35.73  ? 45  PHE   C CZ  1 
ATOM   1779 N N   . GLY   C 1 47 ? 11.505  -29.760 17.553  1.00 32.26  ? 46  GLY   C N   1 
ATOM   1780 C CA  . GLY   C 1 47 ? 10.996  -30.478 16.402  1.00 36.10  ? 46  GLY   C CA  1 
ATOM   1781 C C   . GLY   C 1 47 ? 10.536  -31.880 16.788  1.00 41.34  ? 46  GLY   C C   1 
ATOM   1782 O O   . GLY   C 1 47 ? 9.341   -32.138 16.767  1.00 42.68  ? 46  GLY   C O   1 
ATOM   1783 N N   . THR   C 1 48 ? 11.483  -32.769 17.122  1.00 42.28  ? 47  THR   C N   1 
ATOM   1784 C CA  . THR   C 1 48 ? 11.142  -34.123 17.541  1.00 38.34  ? 47  THR   C CA  1 
ATOM   1785 C C   . THR   C 1 48 ? 10.572  -34.086 18.950  1.00 36.22  ? 47  THR   C C   1 
ATOM   1786 O O   . THR   C 1 48 ? 9.765   -34.951 19.294  1.00 41.82  ? 47  THR   C O   1 
ATOM   1787 C CB  . THR   C 1 48 ? 12.349  -35.053 17.532  1.00 40.29  ? 47  THR   C CB  1 
ATOM   1788 O OG1 . THR   C 1 48 ? 13.214  -34.558 18.551  1.00 40.66  ? 47  THR   C OG1 1 
ATOM   1789 C CG2 . THR   C 1 48 ? 12.974  -35.217 16.161  1.00 39.37  ? 47  THR   C CG2 1 
ATOM   1790 N N   . HIS   C 1 49 ? 11.066  -33.149 19.764  1.00 34.03  ? 48  HIS   C N   1 
ATOM   1791 C CA  . HIS   C 1 49 ? 10.620  -32.958 21.139  1.00 41.92  ? 48  HIS   C CA  1 
ATOM   1792 C C   . HIS   C 1 49 ? 11.099  -34.101 22.042  1.00 37.09  ? 48  HIS   C C   1 
ATOM   1793 O O   . HIS   C 1 49 ? 10.456  -34.397 23.044  1.00 39.11  ? 48  HIS   C O   1 
ATOM   1794 C CB  . HIS   C 1 49 ? 9.093   -32.780 21.186  1.00 41.06  ? 48  HIS   C CB  1 
ATOM   1795 C CG  . HIS   C 1 49 ? 8.612   -31.607 20.399  1.00 50.53  ? 48  HIS   C CG  1 
ATOM   1796 N ND1 . HIS   C 1 49 ? 7.542   -31.680 19.534  1.00 53.73  ? 48  HIS   C ND1 1 
ATOM   1797 C CD2 . HIS   C 1 49 ? 9.070   -30.348 20.318  1.00 49.20  ? 48  HIS   C CD2 1 
ATOM   1798 C CE1 . HIS   C 1 49 ? 7.368   -30.495 18.957  1.00 52.65  ? 48  HIS   C CE1 1 
ATOM   1799 N NE2 . HIS   C 1 49 ? 8.272   -29.671 19.433  1.00 53.50  ? 48  HIS   C NE2 1 
ATOM   1800 N N   . GLU   C 1 50 ? 12.224  -34.734 21.702  1.00 34.57  ? 49  GLU   C N   1 
ATOM   1801 C CA  . GLU   C 1 50 ? 12.749  -35.828 22.512  1.00 37.39  ? 49  GLU   C CA  1 
ATOM   1802 C C   . GLU   C 1 50 ? 13.957  -35.372 23.327  1.00 37.78  ? 49  GLU   C C   1 
ATOM   1803 O O   . GLU   C 1 50 ? 14.372  -34.220 23.232  1.00 38.18  ? 49  GLU   C O   1 
ATOM   1804 C CB  . GLU   C 1 50 ? 12.976  -37.025 21.608  1.00 39.13  ? 49  GLU   C CB  1 
ATOM   1805 C CG  . GLU   C 1 50 ? 11.657  -37.442 20.968  1.00 52.41  ? 49  GLU   C CG  1 
ATOM   1806 C CD  . GLU   C 1 50 ? 11.790  -38.646 20.071  1.00 61.68  ? 49  GLU   C CD  1 
ATOM   1807 O OE1 . GLU   C 1 50 ? 12.820  -38.780 19.365  1.00 67.89  ? 49  GLU   C OE1 1 
ATOM   1808 O OE2 . GLU   C 1 50 ? 10.830  -39.446 20.115  1.00 75.22  ? 49  GLU   C OE2 1 
ATOM   1809 N N   . THR   C 1 51 ? 14.444  -36.242 24.226  1.00 41.47  ? 50  THR   C N   1 
ATOM   1810 C CA  . THR   C 1 51 ? 15.518  -35.853 25.143  1.00 43.08  ? 50  THR   C CA  1 
ATOM   1811 C C   . THR   C 1 51 ? 16.668  -36.853 25.076  1.00 35.20  ? 50  THR   C C   1 
ATOM   1812 O O   . THR   C 1 51 ? 16.521  -37.967 24.595  1.00 39.94  ? 50  THR   C O   1 
ATOM   1813 C CB  . THR   C 1 51 ? 15.048  -35.728 26.594  1.00 47.74  ? 50  THR   C CB  1 
ATOM   1814 O OG1 . THR   C 1 51 ? 14.478  -37.002 26.876  1.00 48.32  ? 50  THR   C OG1 1 
ATOM   1815 C CG2 . THR   C 1 51 ? 14.100  -34.572 26.849  1.00 47.12  ? 50  THR   C CG2 1 
ATOM   1816 N N   . ALA   C 1 52 ? 17.835  -36.417 25.536  1.00 37.63  ? 51  ALA   C N   1 
ATOM   1817 C CA  . ALA   C 1 52 ? 18.996  -37.279 25.647  1.00 42.38  ? 51  ALA   C CA  1 
ATOM   1818 C C   . ALA   C 1 52 ? 20.029  -36.550 26.497  1.00 43.75  ? 51  ALA   C C   1 
ATOM   1819 O O   . ALA   C 1 52 ? 19.830  -35.385 26.832  1.00 41.70  ? 51  ALA   C O   1 
ATOM   1820 C CB  . ALA   C 1 52 ? 19.524  -37.652 24.277  1.00 43.61  ? 51  ALA   C CB  1 
ATOM   1821 N N   . PHE   C 1 53 ? 21.091  -37.275 26.875  1.00 48.25  ? 52  PHE   C N   1 
ATOM   1822 C CA  . PHE   C 1 53 ? 22.201  -36.755 27.659  1.00 45.77  ? 52  PHE   C CA  1 
ATOM   1823 C C   . PHE   C 1 53 ? 23.375  -36.565 26.717  1.00 39.60  ? 52  PHE   C C   1 
ATOM   1824 O O   . PHE   C 1 53 ? 23.755  -37.489 26.010  1.00 42.22  ? 52  PHE   C O   1 
ATOM   1825 C CB  . PHE   C 1 53 ? 22.554  -37.757 28.766  1.00 44.19  ? 52  PHE   C CB  1 
ATOM   1826 C CG  . PHE   C 1 53 ? 21.541  -37.709 29.901  1.00 43.15  ? 52  PHE   C CG  1 
ATOM   1827 C CD1 . PHE   C 1 53 ? 21.184  -36.497 30.487  1.00 43.14  ? 52  PHE   C CD1 1 
ATOM   1828 C CD2 . PHE   C 1 53 ? 20.911  -38.866 30.348  1.00 51.92  ? 52  PHE   C CD2 1 
ATOM   1829 C CE1 . PHE   C 1 53 ? 20.246  -36.444 31.510  1.00 47.66  ? 52  PHE   C CE1 1 
ATOM   1830 C CE2 . PHE   C 1 53 ? 19.972  -38.813 31.373  1.00 55.65  ? 52  PHE   C CE2 1 
ATOM   1831 C CZ  . PHE   C 1 53 ? 19.635  -37.599 31.945  1.00 49.61  ? 52  PHE   C CZ  1 
ATOM   1832 N N   . LEU   C 1 54 ? 23.936  -35.355 26.716  1.00 32.05  ? 53  LEU   C N   1 
ATOM   1833 C CA  . LEU   C 1 54 ? 25.057  -35.077 25.842  1.00 33.82  ? 53  LEU   C CA  1 
ATOM   1834 C C   . LEU   C 1 54 ? 26.149  -34.407 26.660  1.00 35.34  ? 53  LEU   C C   1 
ATOM   1835 O O   . LEU   C 1 54 ? 25.855  -33.726 27.630  1.00 34.15  ? 53  LEU   C O   1 
ATOM   1836 C CB  . LEU   C 1 54 ? 24.635  -34.229 24.641  1.00 36.81  ? 53  LEU   C CB  1 
ATOM   1837 C CG  . LEU   C 1 54 ? 23.714  -34.939 23.637  1.00 39.31  ? 53  LEU   C CG  1 
ATOM   1838 C CD1 . LEU   C 1 54 ? 23.331  -34.002 22.511  1.00 36.15  ? 53  LEU   C CD1 1 
ATOM   1839 C CD2 . LEU   C 1 54 ? 24.412  -36.165 23.065  1.00 42.07  ? 53  LEU   C CD2 1 
ATOM   1840 N N   . GLY   C 1 55 ? 27.397  -34.640 26.260  1.00 38.47  ? 54  GLY   C N   1 
ATOM   1841 C CA  . GLY   C 1 55 ? 28.543  -33.966 26.840  1.00 39.53  ? 54  GLY   C CA  1 
ATOM   1842 C C   . GLY   C 1 55 ? 28.847  -32.653 26.118  1.00 45.04  ? 54  GLY   C C   1 
ATOM   1843 O O   . GLY   C 1 55 ? 28.337  -32.384 25.008  1.00 39.37  ? 54  GLY   C O   1 
ATOM   1844 N N   . PRO   C 1 56 ? 29.679  -31.791 26.745  1.00 45.79  ? 55  PRO   C N   1 
ATOM   1845 C CA  . PRO   C 1 56 ? 29.917  -30.448 26.233  1.00 49.04  ? 55  PRO   C CA  1 
ATOM   1846 C C   . PRO   C 1 56 ? 30.470  -30.429 24.810  1.00 44.69  ? 55  PRO   C C   1 
ATOM   1847 O O   . PRO   C 1 56 ? 30.160  -29.514 24.051  1.00 56.97  ? 55  PRO   C O   1 
ATOM   1848 C CB  . PRO   C 1 56 ? 30.862  -29.794 27.281  1.00 50.67  ? 55  PRO   C CB  1 
ATOM   1849 C CG  . PRO   C 1 56 ? 31.476  -30.958 28.021  1.00 41.35  ? 55  PRO   C CG  1 
ATOM   1850 C CD  . PRO   C 1 56 ? 30.444  -32.072 27.972  1.00 48.55  ? 55  PRO   C CD  1 
ATOM   1851 N N   . LYS   C 1 57 ? 31.242  -31.459 24.439  1.00 43.50  ? 56  LYS   C N   1 
ATOM   1852 C CA  . LYS   C 1 57 ? 31.868  -31.499 23.126  1.00 45.73  ? 56  LYS   C CA  1 
ATOM   1853 C C   . LYS   C 1 57 ? 30.814  -31.623 22.024  1.00 50.32  ? 56  LYS   C C   1 
ATOM   1854 O O   . LYS   C 1 57 ? 31.152  -31.541 20.839  1.00 45.07  ? 56  LYS   C O   1 
ATOM   1855 C CB  . LYS   C 1 57 ? 32.779  -32.720 22.937  1.00 43.62  ? 56  LYS   C CB  1 
ATOM   1856 N N   . ASP   C 1 58 ? 29.561  -31.890 22.417  1.00 43.11  ? 57  ASP   C N   1 
ATOM   1857 C CA  . ASP   C 1 58 ? 28.536  -32.244 21.448  1.00 45.11  ? 57  ASP   C CA  1 
ATOM   1858 C C   . ASP   C 1 58 ? 27.584  -31.079 21.282  1.00 38.02  ? 57  ASP   C C   1 
ATOM   1859 O O   . ASP   C 1 58 ? 26.552  -31.213 20.631  1.00 44.70  ? 57  ASP   C O   1 
ATOM   1860 C CB  . ASP   C 1 58 ? 27.769  -33.487 21.875  1.00 40.26  ? 57  ASP   C CB  1 
ATOM   1861 C CG  . ASP   C 1 58 ? 28.586  -34.762 21.794  1.00 42.33  ? 57  ASP   C CG  1 
ATOM   1862 O OD1 . ASP   C 1 58 ? 29.540  -34.785 20.992  1.00 47.66  ? 57  ASP   C OD1 1 
ATOM   1863 O OD2 . ASP   C 1 58 ? 28.279  -35.686 22.557  1.00 46.53  ? 57  ASP   C OD2 1 
ATOM   1864 N N   . LEU   C 1 59 ? 27.909  -29.965 21.933  1.00 38.96  ? 58  LEU   C N   1 
ATOM   1865 C CA  . LEU   C 1 59 ? 26.973  -28.858 22.079  1.00 37.13  ? 58  LEU   C CA  1 
ATOM   1866 C C   . LEU   C 1 59 ? 27.573  -27.568 21.530  1.00 42.60  ? 58  LEU   C C   1 
ATOM   1867 O O   . LEU   C 1 59 ? 28.733  -27.262 21.770  1.00 45.41  ? 58  LEU   C O   1 
ATOM   1868 C CB  . LEU   C 1 59 ? 26.572  -28.695 23.546  1.00 40.68  ? 58  LEU   C CB  1 
ATOM   1869 C CG  . LEU   C 1 59 ? 25.971  -29.932 24.220  1.00 39.93  ? 58  LEU   C CG  1 
ATOM   1870 C CD1 . LEU   C 1 59 ? 25.711  -29.697 25.686  1.00 35.73  ? 58  LEU   C CD1 1 
ATOM   1871 C CD2 . LEU   C 1 59 ? 24.682  -30.342 23.517  1.00 32.81  ? 58  LEU   C CD2 1 
ATOM   1872 N N   . PHE   C 1 60 ? 26.753  -26.814 20.797  1.00 43.70  ? 59  PHE   C N   1 
ATOM   1873 C CA  . PHE   C 1 60 ? 27.222  -25.629 20.096  1.00 47.55  ? 59  PHE   C CA  1 
ATOM   1874 C C   . PHE   C 1 60 ? 26.243  -24.504 20.399  1.00 46.21  ? 59  PHE   C C   1 
ATOM   1875 O O   . PHE   C 1 60 ? 25.049  -24.640 20.128  1.00 47.96  ? 59  PHE   C O   1 
ATOM   1876 C CB  . PHE   C 1 60 ? 27.465  -25.888 18.604  1.00 41.72  ? 59  PHE   C CB  1 
ATOM   1877 C CG  . PHE   C 1 60 ? 28.466  -27.002 18.330  1.00 47.02  ? 59  PHE   C CG  1 
ATOM   1878 C CD1 . PHE   C 1 60 ? 28.083  -28.344 18.369  1.00 44.20  ? 59  PHE   C CD1 1 
ATOM   1879 C CD2 . PHE   C 1 60 ? 29.795  -26.710 18.031  1.00 50.05  ? 59  PHE   C CD2 1 
ATOM   1880 C CE1 . PHE   C 1 60 ? 28.998  -29.358 18.153  1.00 43.87  ? 59  PHE   C CE1 1 
ATOM   1881 C CE2 . PHE   C 1 60 ? 30.707  -27.733 17.792  1.00 50.85  ? 59  PHE   C CE2 1 
ATOM   1882 C CZ  . PHE   C 1 60 ? 30.312  -29.050 17.854  1.00 47.55  ? 59  PHE   C CZ  1 
ATOM   1883 N N   . PRO   C 1 61 ? 26.710  -23.370 20.986  1.00 48.09  ? 60  PRO   C N   1 
ATOM   1884 C CA  . PRO   C 1 61 ? 25.810  -22.275 21.354  1.00 48.08  ? 60  PRO   C CA  1 
ATOM   1885 C C   . PRO   C 1 61 ? 25.138  -21.803 20.066  1.00 48.27  ? 60  PRO   C C   1 
ATOM   1886 O O   . PRO   C 1 61 ? 25.801  -21.644 19.040  1.00 46.88  ? 60  PRO   C O   1 
ATOM   1887 C CB  . PRO   C 1 61 ? 26.721  -21.200 21.988  1.00 46.92  ? 60  PRO   C CB  1 
ATOM   1888 C CG  . PRO   C 1 61 ? 28.045  -21.906 22.206  1.00 45.59  ? 60  PRO   C CG  1 
ATOM   1889 C CD  . PRO   C 1 61 ? 28.131  -23.048 21.217  1.00 49.33  ? 60  PRO   C CD  1 
ATOM   1890 N N   . TYR   C 1 62 ? 23.807  -21.638 20.141  1.00 54.17  ? 61  TYR   C N   1 
ATOM   1891 C CA  . TYR   C 1 62 ? 22.949  -21.365 19.000  1.00 56.83  ? 61  TYR   C CA  1 
ATOM   1892 C C   . TYR   C 1 62 ? 23.440  -20.141 18.232  1.00 64.41  ? 61  TYR   C C   1 
ATOM   1893 O O   . TYR   C 1 62 ? 23.837  -20.270 17.072  1.00 62.80  ? 61  TYR   C O   1 
ATOM   1894 C CB  . TYR   C 1 62 ? 21.524  -21.093 19.480  1.00 51.39  ? 61  TYR   C CB  1 
ATOM   1895 C CG  . TYR   C 1 62 ? 20.530  -20.756 18.379  1.00 55.18  ? 61  TYR   C CG  1 
ATOM   1896 C CD1 . TYR   C 1 62 ? 20.435  -21.525 17.219  1.00 58.40  ? 61  TYR   C CD1 1 
ATOM   1897 C CD2 . TYR   C 1 62 ? 19.684  -19.659 18.507  1.00 55.57  ? 61  TYR   C CD2 1 
ATOM   1898 C CE1 . TYR   C 1 62 ? 19.517  -21.208 16.225  1.00 58.14  ? 61  TYR   C CE1 1 
ATOM   1899 C CE2 . TYR   C 1 62 ? 18.763  -19.334 17.525  1.00 56.93  ? 61  TYR   C CE2 1 
ATOM   1900 C CZ  . TYR   C 1 62 ? 18.679  -20.111 16.380  1.00 55.73  ? 61  TYR   C CZ  1 
ATOM   1901 O OH  . TYR   C 1 62 ? 17.747  -19.778 15.436  1.00 48.09  ? 61  TYR   C OH  1 
ATOM   1902 N N   . ASP   C 1 63 ? 23.404  -18.969 18.890  1.00 59.69  ? 62  ASP   C N   1 
ATOM   1903 C CA  . ASP   C 1 63 ? 23.842  -17.717 18.284  1.00 56.76  ? 62  ASP   C CA  1 
ATOM   1904 C C   . ASP   C 1 63 ? 25.185  -17.864 17.579  1.00 56.41  ? 62  ASP   C C   1 
ATOM   1905 O O   . ASP   C 1 63 ? 25.328  -17.426 16.437  1.00 66.61  ? 62  ASP   C O   1 
ATOM   1906 C CB  . ASP   C 1 63 ? 23.768  -16.540 19.242  1.00 58.98  ? 62  ASP   C CB  1 
ATOM   1907 C CG  . ASP   C 1 63 ? 22.430  -15.816 19.204  1.00 73.63  ? 62  ASP   C CG  1 
ATOM   1908 O OD1 . ASP   C 1 63 ? 21.728  -15.823 20.245  1.00 68.38  ? 62  ASP   C OD1 1 
ATOM   1909 O OD2 . ASP   C 1 63 ? 22.090  -15.269 18.120  1.00 77.00  ? 62  ASP   C OD2 1 
ATOM   1910 N N   . LYS   C 1 64 ? 26.163  -18.483 18.246  1.00 48.17  ? 63  LYS   C N   1 
ATOM   1911 C CA  . LYS   C 1 64 ? 27.502  -18.578 17.675  1.00 48.29  ? 63  LYS   C CA  1 
ATOM   1912 C C   . LYS   C 1 64 ? 27.486  -19.397 16.383  1.00 47.88  ? 63  LYS   C C   1 
ATOM   1913 O O   . LYS   C 1 64 ? 28.211  -19.063 15.455  1.00 44.22  ? 63  LYS   C O   1 
ATOM   1914 C CB  . LYS   C 1 64 ? 28.540  -19.111 18.672  1.00 54.38  ? 63  LYS   C CB  1 
ATOM   1915 N N   . SER   C 1 65 ? 26.623  -20.434 16.300  1.00 46.31  ? 64  SER   C N   1 
ATOM   1916 C CA  . SER   C 1 65 ? 26.770  -21.450 15.260  1.00 43.76  ? 64  SER   C CA  1 
ATOM   1917 C C   . SER   C 1 65 ? 25.578  -21.533 14.289  1.00 41.87  ? 64  SER   C C   1 
ATOM   1918 O O   . SER   C 1 65 ? 25.586  -22.355 13.378  1.00 41.09  ? 64  SER   C O   1 
ATOM   1919 C CB  . SER   C 1 65 ? 27.105  -22.786 15.875  1.00 39.65  ? 64  SER   C CB  1 
ATOM   1920 O OG  . SER   C 1 65 ? 25.995  -23.243 16.636  1.00 41.14  ? 64  SER   C OG  1 
ATOM   1921 N N   . LYS   C 1 66 ? 24.556  -20.685 14.455  1.00 43.51  ? 65  LYS   C N   1 
ATOM   1922 C CA  . LYS   C 1 66 ? 23.350  -20.806 13.641  1.00 42.69  ? 65  LYS   C CA  1 
ATOM   1923 C C   . LYS   C 1 66 ? 23.654  -20.604 12.161  1.00 48.05  ? 65  LYS   C C   1 
ATOM   1924 O O   . LYS   C 1 66 ? 23.060  -21.283 11.320  1.00 46.98  ? 65  LYS   C O   1 
ATOM   1925 C CB  . LYS   C 1 66 ? 22.182  -19.906 14.053  1.00 42.74  ? 65  LYS   C CB  1 
ATOM   1926 C CG  . LYS   C 1 66 ? 22.480  -18.420 14.163  1.00 43.49  ? 65  LYS   C CG  1 
ATOM   1927 C CD  . LYS   C 1 66 ? 21.163  -17.665 14.323  1.00 53.53  ? 65  LYS   C CD  1 
ATOM   1928 C CE  . LYS   C 1 66 ? 21.376  -16.237 14.708  1.00 56.33  ? 65  LYS   C CE  1 
ATOM   1929 N NZ  . LYS   C 1 66 ? 20.121  -15.664 15.192  1.00 63.70  ? 65  LYS   C NZ  1 
ATOM   1930 N N   . ASP   C 1 67 ? 24.580  -19.683 11.860  1.00 45.78  ? 66  ASP   C N   1 
ATOM   1931 C CA  . ASP   C 1 67 ? 24.966  -19.383 10.486  1.00 50.88  ? 66  ASP   C CA  1 
ATOM   1932 C C   . ASP   C 1 67 ? 25.405  -20.666 9.773   1.00 47.20  ? 66  ASP   C C   1 
ATOM   1933 O O   . ASP   C 1 67 ? 25.105  -20.834 8.603   1.00 42.76  ? 66  ASP   C O   1 
ATOM   1934 C CB  . ASP   C 1 67 ? 25.895  -18.174 10.381  1.00 52.62  ? 66  ASP   C CB  1 
ATOM   1935 C CG  . ASP   C 1 67 ? 27.268  -18.305 11.025  1.00 65.36  ? 66  ASP   C CG  1 
ATOM   1936 O OD1 . ASP   C 1 67 ? 27.505  -19.325 11.716  1.00 64.66  ? 66  ASP   C OD1 1 
ATOM   1937 O OD2 . ASP   C 1 67 ? 28.090  -17.372 10.845  1.00 68.92  ? 66  ASP   C OD2 1 
ATOM   1938 N N   . LYS   C 1 68 ? 26.031  -21.601 10.510  1.00 42.55  ? 67  LYS   C N   1 
ATOM   1939 C CA  . LYS   C 1 68 ? 26.558  -22.855 9.986   1.00 39.83  ? 67  LYS   C CA  1 
ATOM   1940 C C   . LYS   C 1 68 ? 25.542  -24.017 10.083  1.00 41.19  ? 67  LYS   C C   1 
ATOM   1941 O O   . LYS   C 1 68 ? 25.395  -24.793 9.140   1.00 42.84  ? 67  LYS   C O   1 
ATOM   1942 C CB  . LYS   C 1 68 ? 27.822  -23.095 10.820  1.00 38.70  ? 67  LYS   C CB  1 
ATOM   1943 C CG  . LYS   C 1 68 ? 28.657  -24.308 10.510  1.00 40.08  ? 67  LYS   C CG  1 
ATOM   1944 C CD  . LYS   C 1 68 ? 29.896  -24.289 11.414  1.00 46.10  ? 67  LYS   C CD  1 
ATOM   1945 C CE  . LYS   C 1 68 ? 30.669  -25.568 11.467  1.00 53.23  ? 67  LYS   C CE  1 
ATOM   1946 N NZ  . LYS   C 1 68 ? 30.887  -26.154 10.138  1.00 61.77  ? 67  LYS   C NZ  1 
ATOM   1947 N N   . TYR   C 1 69 ? 24.832  -24.160 11.211  1.00 36.36  ? 68  TYR   C N   1 
ATOM   1948 C CA  . TYR   C 1 69 ? 23.999  -25.347 11.369  1.00 39.13  ? 68  TYR   C CA  1 
ATOM   1949 C C   . TYR   C 1 69 ? 22.518  -25.044 11.147  1.00 35.76  ? 68  TYR   C C   1 
ATOM   1950 O O   . TYR   C 1 69 ? 21.737  -25.973 10.974  1.00 33.86  ? 68  TYR   C O   1 
ATOM   1951 C CB  . TYR   C 1 69 ? 24.167  -25.959 12.765  1.00 36.62  ? 68  TYR   C CB  1 
ATOM   1952 C CG  . TYR   C 1 69 ? 25.590  -26.397 13.059  1.00 36.62  ? 68  TYR   C CG  1 
ATOM   1953 C CD1 . TYR   C 1 69 ? 26.297  -27.229 12.179  1.00 37.10  ? 68  TYR   C CD1 1 
ATOM   1954 C CD2 . TYR   C 1 69 ? 26.209  -25.990 14.238  1.00 39.82  ? 68  TYR   C CD2 1 
ATOM   1955 C CE1 . TYR   C 1 69 ? 27.581  -27.658 12.472  1.00 36.58  ? 68  TYR   C CE1 1 
ATOM   1956 C CE2 . TYR   C 1 69 ? 27.494  -26.411 14.539  1.00 38.28  ? 68  TYR   C CE2 1 
ATOM   1957 C CZ  . TYR   C 1 69 ? 28.181  -27.211 13.641  1.00 39.83  ? 68  TYR   C CZ  1 
ATOM   1958 O OH  . TYR   C 1 69 ? 29.429  -27.579 14.024  1.00 39.50  ? 68  TYR   C OH  1 
ATOM   1959 N N   . GLY   C 1 70 ? 22.125  -23.769 11.266  1.00 30.53  ? 69  GLY   C N   1 
ATOM   1960 C CA  . GLY   C 1 70 ? 20.714  -23.414 11.161  1.00 34.79  ? 69  GLY   C CA  1 
ATOM   1961 C C   . GLY   C 1 70 ? 20.342  -23.247 9.694   1.00 37.48  ? 69  GLY   C C   1 
ATOM   1962 O O   . GLY   C 1 70 ? 20.372  -22.131 9.166   1.00 37.38  ? 69  GLY   C O   1 
ATOM   1963 N N   . LYS   C 1 71 ? 20.133  -24.388 9.026   1.00 34.18  ? 70  LYS   C N   1 
ATOM   1964 C CA  . LYS   C 1 71 ? 19.828  -24.446 7.604   1.00 37.61  ? 70  LYS   C CA  1 
ATOM   1965 C C   . LYS   C 1 71 ? 18.955  -25.682 7.418   1.00 39.13  ? 70  LYS   C C   1 
ATOM   1966 O O   . LYS   C 1 71 ? 19.155  -26.686 8.098   1.00 39.39  ? 70  LYS   C O   1 
ATOM   1967 C CB  . LYS   C 1 71 ? 21.095  -24.545 6.735   1.00 42.95  ? 70  LYS   C CB  1 
ATOM   1968 C CG  . LYS   C 1 71 ? 22.092  -25.619 7.155   1.00 40.92  ? 70  LYS   C CG  1 
ATOM   1969 C CD  . LYS   C 1 71 ? 23.155  -26.140 6.192   1.00 47.86  ? 70  LYS   C CD  1 
ATOM   1970 C CE  . LYS   C 1 71 ? 23.991  -27.236 6.814   1.00 44.56  ? 70  LYS   C CE  1 
ATOM   1971 N N   . PRO   C 1 72 ? 17.911  -25.641 6.565   1.00 35.51  ? 71  PRO   C N   1 
ATOM   1972 C CA  . PRO   C 1 72 ? 16.955  -26.742 6.531   1.00 29.73  ? 71  PRO   C CA  1 
ATOM   1973 C C   . PRO   C 1 72 ? 17.645  -28.061 6.209   1.00 33.05  ? 71  PRO   C C   1 
ATOM   1974 O O   . PRO   C 1 72 ? 18.687  -28.116 5.557   1.00 32.45  ? 71  PRO   C O   1 
ATOM   1975 C CB  . PRO   C 1 72 ? 16.011  -26.303 5.416   1.00 33.47  ? 71  PRO   C CB  1 
ATOM   1976 C CG  . PRO   C 1 72 ? 16.108  -24.810 5.476   1.00 34.54  ? 71  PRO   C CG  1 
ATOM   1977 C CD  . PRO   C 1 72 ? 17.583  -24.550 5.636   1.00 34.45  ? 71  PRO   C CD  1 
ATOM   1978 N N   . ASN   C 1 73 ? 17.026  -29.135 6.664   1.00 32.62  ? 72  ASN   C N   1 
ATOM   1979 C CA  . ASN   C 1 73 ? 17.317  -30.398 6.029   1.00 41.84  ? 72  ASN   C CA  1 
ATOM   1980 C C   . ASN   C 1 73 ? 16.111  -31.307 6.179   1.00 32.53  ? 72  ASN   C C   1 
ATOM   1981 O O   . ASN   C 1 73 ? 15.140  -30.967 6.856   1.00 32.44  ? 72  ASN   C O   1 
ATOM   1982 C CB  . ASN   C 1 73 ? 18.664  -30.992 6.432   1.00 44.92  ? 72  ASN   C CB  1 
ATOM   1983 C CG  . ASN   C 1 73 ? 18.629  -31.666 7.776   1.00 45.97  ? 72  ASN   C CG  1 
ATOM   1984 O OD1 . ASN   C 1 73 ? 17.776  -32.527 8.031   1.00 48.73  ? 72  ASN   C OD1 1 
ATOM   1985 N ND2 . ASN   C 1 73 ? 19.575  -31.304 8.625   1.00 47.30  ? 72  ASN   C ND2 1 
ATOM   1986 N N   . LYS   C 1 74 ? 16.256  -32.482 5.580   1.00 37.62  ? 73  LYS   C N   1 
ATOM   1987 C CA  . LYS   C 1 74 ? 15.140  -33.340 5.250   1.00 39.95  ? 73  LYS   C CA  1 
ATOM   1988 C C   . LYS   C 1 74 ? 14.773  -34.242 6.414   1.00 39.09  ? 73  LYS   C C   1 
ATOM   1989 O O   . LYS   C 1 74 ? 13.698  -34.825 6.384   1.00 39.23  ? 73  LYS   C O   1 
ATOM   1990 C CB  . LYS   C 1 74 ? 15.590  -34.126 4.014   1.00 42.90  ? 73  LYS   C CB  1 
ATOM   1991 C CG  . LYS   C 1 74 ? 14.931  -33.610 2.736   1.00 60.16  ? 73  LYS   C CG  1 
ATOM   1992 C CD  . LYS   C 1 74 ? 15.261  -32.175 2.339   1.00 54.84  ? 73  LYS   C CD  1 
ATOM   1993 N N   . ARG   C 1 75 ? 15.665  -34.380 7.405   1.00 34.95  ? 74  ARG   C N   1 
ATOM   1994 C CA  . ARG   C 1 75 ? 15.431  -35.338 8.486   1.00 36.95  ? 74  ARG   C CA  1 
ATOM   1995 C C   . ARG   C 1 75 ? 14.147  -34.978 9.227   1.00 38.39  ? 74  ARG   C C   1 
ATOM   1996 O O   . ARG   C 1 75 ? 13.815  -33.797 9.351   1.00 39.14  ? 74  ARG   C O   1 
ATOM   1997 C CB  . ARG   C 1 75 ? 16.603  -35.429 9.483   1.00 35.73  ? 74  ARG   C CB  1 
ATOM   1998 C CG  . ARG   C 1 75 ? 17.994  -35.615 8.890   1.00 43.08  ? 74  ARG   C CG  1 
ATOM   1999 C CD  . ARG   C 1 75 ? 18.371  -36.925 8.198   1.00 44.10  ? 74  ARG   C CD  1 
ATOM   2000 N NE  . ARG   C 1 75 ? 18.233  -37.976 9.208   1.00 40.96  ? 74  ARG   C NE  1 
ATOM   2001 C CZ  . ARG   C 1 75 ? 19.232  -38.486 9.930   1.00 36.28  ? 74  ARG   C CZ  1 
ATOM   2002 N NH1 . ARG   C 1 75 ? 18.941  -39.078 11.080  1.00 34.08  ? 74  ARG   C NH1 1 
ATOM   2003 N NH2 . ARG   C 1 75 ? 20.482  -38.269 9.545   1.00 38.31  ? 74  ARG   C NH2 1 
ATOM   2004 N N   . LYS   C 1 76 ? 13.436  -36.007 9.726   1.00 40.08  ? 75  LYS   C N   1 
ATOM   2005 C CA  . LYS   C 1 76 ? 12.122  -35.837 10.339  1.00 44.34  ? 75  LYS   C CA  1 
ATOM   2006 C C   . LYS   C 1 76 ? 12.163  -34.852 11.506  1.00 43.49  ? 75  LYS   C C   1 
ATOM   2007 O O   . LYS   C 1 76 ? 12.885  -35.072 12.480  1.00 39.42  ? 75  LYS   C O   1 
ATOM   2008 C CB  . LYS   C 1 76 ? 11.507  -37.146 10.857  1.00 43.74  ? 75  LYS   C CB  1 
ATOM   2009 C CG  . LYS   C 1 76 ? 9.995   -37.217 10.681  1.00 49.91  ? 75  LYS   C CG  1 
ATOM   2010 C CD  . LYS   C 1 76 ? 9.335   -38.416 11.356  1.00 57.97  ? 75  LYS   C CD  1 
ATOM   2011 N N   . GLY   C 1 77 ? 11.320  -33.807 11.436  1.00 40.74  ? 76  GLY   C N   1 
ATOM   2012 C CA  . GLY   C 1 77 ? 11.145  -32.904 12.568  1.00 35.84  ? 76  GLY   C CA  1 
ATOM   2013 C C   . GLY   C 1 77 ? 12.186  -31.779 12.612  1.00 31.89  ? 76  GLY   C C   1 
ATOM   2014 O O   . GLY   C 1 77 ? 12.147  -30.888 13.472  1.00 35.17  ? 76  GLY   C O   1 
ATOM   2015 N N   . PHE   C 1 78 ? 13.137  -31.801 11.686  1.00 30.92  ? 77  PHE   C N   1 
ATOM   2016 C CA  . PHE   C 1 78 ? 14.244  -30.862 11.802  1.00 31.05  ? 77  PHE   C CA  1 
ATOM   2017 C C   . PHE   C 1 78 ? 13.764  -29.436 11.510  1.00 37.02  ? 77  PHE   C C   1 
ATOM   2018 O O   . PHE   C 1 78 ? 14.209  -28.478 12.144  1.00 34.60  ? 77  PHE   C O   1 
ATOM   2019 C CB  . PHE   C 1 78 ? 15.364  -31.243 10.835  1.00 34.24  ? 77  PHE   C CB  1 
ATOM   2020 C CG  . PHE   C 1 78 ? 16.651  -30.464 11.078  1.00 33.09  ? 77  PHE   C CG  1 
ATOM   2021 C CD1 . PHE   C 1 78 ? 16.832  -29.178 10.560  1.00 33.95  ? 77  PHE   C CD1 1 
ATOM   2022 C CD2 . PHE   C 1 78 ? 17.679  -31.005 11.831  1.00 28.79  ? 77  PHE   C CD2 1 
ATOM   2023 C CE1 . PHE   C 1 78 ? 17.998  -28.458 10.799  1.00 34.42  ? 77  PHE   C CE1 1 
ATOM   2024 C CE2 . PHE   C 1 78 ? 18.852  -30.278 12.058  1.00 30.44  ? 77  PHE   C CE2 1 
ATOM   2025 C CZ  . PHE   C 1 78 ? 19.022  -29.018 11.536  1.00 33.41  ? 77  PHE   C CZ  1 
ATOM   2026 N N   . ASN   C 1 79 ? 12.910  -29.290 10.492  1.00 33.26  ? 78  ASN   C N   1 
ATOM   2027 C CA  . ASN   C 1 79 ? 12.575  -27.951 10.014  1.00 37.78  ? 78  ASN   C CA  1 
ATOM   2028 C C   . ASN   C 1 79 ? 11.605  -27.298 10.997  1.00 34.06  ? 78  ASN   C C   1 
ATOM   2029 O O   . ASN   C 1 79 ? 11.689  -26.102 11.266  1.00 32.94  ? 78  ASN   C O   1 
ATOM   2030 C CB  . ASN   C 1 79 ? 12.133  -27.946 8.553   1.00 34.62  ? 78  ASN   C CB  1 
ATOM   2031 C CG  . ASN   C 1 79 ? 13.276  -28.308 7.631   1.00 33.22  ? 78  ASN   C CG  1 
ATOM   2032 O OD1 . ASN   C 1 79 ? 14.436  -28.016 7.930   1.00 33.04  ? 78  ASN   C OD1 1 
ATOM   2033 N ND2 . ASN   C 1 79 ? 12.964  -28.891 6.482   1.00 34.21  ? 78  ASN   C ND2 1 
ATOM   2034 N N   . GLU   C 1 80 ? 10.721  -28.105 11.589  1.00 36.55  ? 79  GLU   C N   1 
ATOM   2035 C CA  . GLU   C 1 80 ? 9.899   -27.561 12.661  1.00 36.94  ? 79  GLU   C CA  1 
ATOM   2036 C C   . GLU   C 1 80 ? 10.814  -27.151 13.818  1.00 39.43  ? 79  GLU   C C   1 
ATOM   2037 O O   . GLU   C 1 80 ? 10.574  -26.134 14.468  1.00 38.06  ? 79  GLU   C O   1 
ATOM   2038 C CB  . GLU   C 1 80 ? 8.789   -28.542 13.034  1.00 36.41  ? 79  GLU   C CB  1 
ATOM   2039 C CG  . GLU   C 1 80 ? 7.964   -28.058 14.217  1.00 39.83  ? 79  GLU   C CG  1 
ATOM   2040 C CD  . GLU   C 1 80 ? 6.681   -28.843 14.397  1.00 52.13  ? 79  GLU   C CD  1 
ATOM   2041 O OE1 . GLU   C 1 80 ? 6.578   -29.959 13.869  1.00 58.23  ? 79  GLU   C OE1 1 
ATOM   2042 O OE2 . GLU   C 1 80 ? 5.769   -28.328 15.065  1.00 54.07  ? 79  GLU   C OE2 1 
ATOM   2043 N N   . GLY   C 1 81 ? 11.873  -27.949 14.063  1.00 36.62  ? 80  GLY   C N   1 
ATOM   2044 C CA  . GLY   C 1 81 ? 12.802  -27.614 15.135  1.00 35.76  ? 80  GLY   C CA  1 
ATOM   2045 C C   . GLY   C 1 81 ? 13.470  -26.255 14.932  1.00 38.90  ? 80  GLY   C C   1 
ATOM   2046 O O   . GLY   C 1 81 ? 13.615  -25.499 15.885  1.00 36.67  ? 80  GLY   C O   1 
ATOM   2047 N N   . LEU   C 1 82 ? 13.909  -25.968 13.691  1.00 38.70  ? 81  LEU   C N   1 
ATOM   2048 C CA  . LEU   C 1 82 ? 14.484  -24.669 13.338  1.00 38.36  ? 81  LEU   C CA  1 
ATOM   2049 C C   . LEU   C 1 82 ? 13.469  -23.559 13.603  1.00 35.26  ? 81  LEU   C C   1 
ATOM   2050 O O   . LEU   C 1 82 ? 13.815  -22.495 14.100  1.00 36.00  ? 81  LEU   C O   1 
ATOM   2051 C CB  . LEU   C 1 82 ? 14.888  -24.618 11.867  1.00 37.42  ? 81  LEU   C CB  1 
ATOM   2052 C CG  . LEU   C 1 82 ? 16.090  -25.458 11.435  1.00 32.94  ? 81  LEU   C CG  1 
ATOM   2053 C CD1 . LEU   C 1 82 ? 16.342  -25.149 9.967   1.00 29.89  ? 81  LEU   C CD1 1 
ATOM   2054 C CD2 . LEU   C 1 82 ? 17.265  -25.009 12.241  1.00 28.67  ? 81  LEU   C CD2 1 
ATOM   2055 N N   . TRP   C 1 83 ? 12.213  -23.794 13.234  1.00 35.41  ? 82  TRP   C N   1 
ATOM   2056 C CA  . TRP   C 1 83 ? 11.203  -22.783 13.492  1.00 42.11  ? 82  TRP   C CA  1 
ATOM   2057 C C   . TRP   C 1 83 ? 11.136  -22.492 14.999  1.00 41.23  ? 82  TRP   C C   1 
ATOM   2058 O O   . TRP   C 1 83 ? 11.130  -21.331 15.417  1.00 39.22  ? 82  TRP   C O   1 
ATOM   2059 C CB  . TRP   C 1 83 ? 9.832   -23.195 12.927  1.00 40.21  ? 82  TRP   C CB  1 
ATOM   2060 C CG  . TRP   C 1 83 ? 8.854   -22.057 13.025  1.00 47.01  ? 82  TRP   C CG  1 
ATOM   2061 C CD1 . TRP   C 1 83 ? 8.632   -21.081 12.096  1.00 46.48  ? 82  TRP   C CD1 1 
ATOM   2062 C CD2 . TRP   C 1 83 ? 8.029   -21.722 14.161  1.00 47.39  ? 82  TRP   C CD2 1 
ATOM   2063 N NE1 . TRP   C 1 83 ? 7.699   -20.187 12.552  1.00 42.09  ? 82  TRP   C NE1 1 
ATOM   2064 C CE2 . TRP   C 1 83 ? 7.307   -20.555 13.809  1.00 43.86  ? 82  TRP   C CE2 1 
ATOM   2065 C CE3 . TRP   C 1 83 ? 7.815   -22.306 15.417  1.00 43.02  ? 82  TRP   C CE3 1 
ATOM   2066 C CZ2 . TRP   C 1 83 ? 6.391   -19.963 14.673  1.00 43.09  ? 82  TRP   C CZ2 1 
ATOM   2067 C CZ3 . TRP   C 1 83 ? 6.923   -21.703 16.276  1.00 45.82  ? 82  TRP   C CZ3 1 
ATOM   2068 C CH2 . TRP   C 1 83 ? 6.235   -20.547 15.912  1.00 50.59  ? 82  TRP   C CH2 1 
ATOM   2069 N N   . GLU   C 1 84 ? 11.128  -23.560 15.809  1.00 36.39  ? 83  GLU   C N   1 
ATOM   2070 C CA  . GLU   C 1 84 ? 10.982  -23.419 17.251  1.00 38.52  ? 83  GLU   C CA  1 
ATOM   2071 C C   . GLU   C 1 84 ? 12.166  -22.689 17.885  1.00 38.98  ? 83  GLU   C C   1 
ATOM   2072 O O   . GLU   C 1 84 ? 11.979  -21.846 18.764  1.00 41.93  ? 83  GLU   C O   1 
ATOM   2073 C CB  . GLU   C 1 84 ? 10.740  -24.754 17.946  1.00 34.76  ? 83  GLU   C CB  1 
ATOM   2074 C CG  . GLU   C 1 84 ? 9.397   -25.370 17.571  1.00 39.74  ? 83  GLU   C CG  1 
ATOM   2075 C CD  . GLU   C 1 84 ? 9.305   -26.797 18.049  1.00 46.42  ? 83  GLU   C CD  1 
ATOM   2076 O OE1 . GLU   C 1 84 ? 10.327  -27.311 18.563  1.00 45.38  ? 83  GLU   C OE1 1 
ATOM   2077 O OE2 . GLU   C 1 84 ? 8.224   -27.397 17.883  1.00 46.31  ? 83  GLU   C OE2 1 
ATOM   2078 N N   . ILE   C 1 85 ? 13.387  -23.002 17.452  1.00 39.77  ? 84  ILE   C N   1 
ATOM   2079 C CA  . ILE   C 1 85 ? 14.535  -22.419 18.121  1.00 40.66  ? 84  ILE   C CA  1 
ATOM   2080 C C   . ILE   C 1 85 ? 14.612  -20.921 17.839  1.00 41.22  ? 84  ILE   C C   1 
ATOM   2081 O O   . ILE   C 1 85 ? 15.154  -20.174 18.641  1.00 35.45  ? 84  ILE   C O   1 
ATOM   2082 C CB  . ILE   C 1 85 ? 15.831  -23.154 17.756  1.00 37.52  ? 84  ILE   C CB  1 
ATOM   2083 C CG1 . ILE   C 1 85 ? 16.892  -22.844 18.791  1.00 37.99  ? 84  ILE   C CG1 1 
ATOM   2084 C CG2 . ILE   C 1 85 ? 16.287  -22.842 16.318  1.00 34.05  ? 84  ILE   C CG2 1 
ATOM   2085 C CD1 . ILE   C 1 85 ? 18.135  -23.707 18.715  1.00 38.12  ? 84  ILE   C CD1 1 
ATOM   2086 N N   . GLN   C 1 86 ? 14.065  -20.487 16.701  1.00 41.38  ? 85  GLN   C N   1 
ATOM   2087 C CA  . GLN   C 1 86 ? 14.103  -19.078 16.323  1.00 42.38  ? 85  GLN   C CA  1 
ATOM   2088 C C   . GLN   C 1 86 ? 12.874  -18.313 16.830  1.00 40.57  ? 85  GLN   C C   1 
ATOM   2089 O O   . GLN   C 1 86 ? 12.985  -17.158 17.211  1.00 41.73  ? 85  GLN   C O   1 
ATOM   2090 C CB  . GLN   C 1 86 ? 14.236  -19.006 14.798  1.00 39.23  ? 85  GLN   C CB  1 
ATOM   2091 C CG  . GLN   C 1 86 ? 14.536  -17.614 14.255  1.00 43.39  ? 85  GLN   C CG  1 
ATOM   2092 C CD  . GLN   C 1 86 ? 14.779  -17.618 12.755  1.00 45.69  ? 85  GLN   C CD  1 
ATOM   2093 O OE1 . GLN   C 1 86 ? 14.556  -18.616 12.046  1.00 42.00  ? 85  GLN   C OE1 1 
ATOM   2094 N NE2 . GLN   C 1 86 ? 15.282  -16.493 12.265  1.00 45.66  ? 85  GLN   C NE2 1 
ATOM   2095 N N   . ASN   C 1 87 ? 11.709  -18.960 16.848  1.00 44.32  ? 86  ASN   C N   1 
ATOM   2096 C CA  . ASN   C 1 87 ? 10.439  -18.282 17.047  1.00 48.69  ? 86  ASN   C CA  1 
ATOM   2097 C C   . ASN   C 1 87 ? 9.841   -18.520 18.443  1.00 55.81  ? 86  ASN   C C   1 
ATOM   2098 O O   . ASN   C 1 87 ? 9.235   -17.612 19.017  1.00 53.82  ? 86  ASN   C O   1 
ATOM   2099 C CB  . ASN   C 1 87 ? 9.496   -18.560 15.879  1.00 43.64  ? 86  ASN   C CB  1 
ATOM   2100 C CG  . ASN   C 1 87 ? 10.061  -17.943 14.624  1.00 47.57  ? 86  ASN   C CG  1 
ATOM   2101 O OD1 . ASN   C 1 87 ? 10.093  -16.715 14.512  1.00 47.82  ? 86  ASN   C OD1 1 
ATOM   2102 N ND2 . ASN   C 1 87 ? 10.562  -18.751 13.701  1.00 40.95  ? 86  ASN   C ND2 1 
ATOM   2103 N N   . ASN   C 1 88 ? 9.986   -19.733 18.995  1.00 54.75  ? 87  ASN   C N   1 
ATOM   2104 C CA  . ASN   C 1 88 ? 9.312   -20.046 20.249  1.00 51.45  ? 87  ASN   C CA  1 
ATOM   2105 C C   . ASN   C 1 88 ? 10.198  -20.903 21.150  1.00 49.91  ? 87  ASN   C C   1 
ATOM   2106 O O   . ASN   C 1 88 ? 9.790   -21.997 21.546  1.00 51.08  ? 87  ASN   C O   1 
ATOM   2107 C CB  . ASN   C 1 88 ? 7.986   -20.764 19.998  1.00 50.46  ? 87  ASN   C CB  1 
ATOM   2108 C CG  . ASN   C 1 88 ? 7.051   -20.607 21.175  1.00 54.48  ? 87  ASN   C CG  1 
ATOM   2109 O OD1 . ASN   C 1 88 ? 7.378   -19.894 22.133  1.00 51.50  ? 87  ASN   C OD1 1 
ATOM   2110 N ND2 . ASN   C 1 88 ? 5.891   -21.243 21.125  1.00 47.00  ? 87  ASN   C ND2 1 
ATOM   2111 N N   . PRO   C 1 89 ? 11.428  -20.455 21.491  1.00 52.49  ? 88  PRO   C N   1 
ATOM   2112 C CA  . PRO   C 1 89 ? 12.417  -21.349 22.106  1.00 56.24  ? 88  PRO   C CA  1 
ATOM   2113 C C   . PRO   C 1 89 ? 12.176  -21.842 23.534  1.00 60.55  ? 88  PRO   C C   1 
ATOM   2114 O O   . PRO   C 1 89 ? 12.814  -22.811 23.947  1.00 52.81  ? 88  PRO   C O   1 
ATOM   2115 C CB  . PRO   C 1 89 ? 13.769  -20.609 21.955  1.00 50.00  ? 88  PRO   C CB  1 
ATOM   2116 C CG  . PRO   C 1 89 ? 13.369  -19.147 21.847  1.00 52.77  ? 88  PRO   C CG  1 
ATOM   2117 C CD  . PRO   C 1 89 ? 11.953  -19.097 21.258  1.00 47.82  ? 88  PRO   C CD  1 
ATOM   2118 N N   . HIS   C 1 90 ? 11.236  -21.203 24.254  1.00 62.43  ? 89  HIS   C N   1 
ATOM   2119 C CA  . HIS   C 1 90 ? 10.995  -21.506 25.661  1.00 51.62  ? 89  HIS   C CA  1 
ATOM   2120 C C   . HIS   C 1 90 ? 9.536   -21.873 25.918  1.00 54.95  ? 89  HIS   C C   1 
ATOM   2121 O O   . HIS   C 1 90 ? 9.071   -21.768 27.042  1.00 62.58  ? 89  HIS   C O   1 
ATOM   2122 C CB  . HIS   C 1 90 ? 11.540  -20.399 26.561  1.00 41.15  ? 89  HIS   C CB  1 
ATOM   2123 C CG  . HIS   C 1 90 ? 12.966  -20.013 26.283  1.00 39.28  ? 89  HIS   C CG  1 
ATOM   2124 N ND1 . HIS   C 1 90 ? 13.322  -18.826 25.685  1.00 43.33  ? 89  HIS   C ND1 1 
ATOM   2125 C CD2 . HIS   C 1 90 ? 14.128  -20.619 26.568  1.00 39.57  ? 89  HIS   C CD2 1 
ATOM   2126 C CE1 . HIS   C 1 90 ? 14.658  -18.728 25.598  1.00 40.83  ? 89  HIS   C CE1 1 
ATOM   2127 N NE2 . HIS   C 1 90 ? 15.169  -19.815 26.134  1.00 40.87  ? 89  HIS   C NE2 1 
ATOM   2128 N N   . ALA   C 1 91 ? 8.822   -22.339 24.887  1.00 62.41  ? 90  ALA   C N   1 
ATOM   2129 C CA  . ALA   C 1 91 ? 7.525   -22.976 25.080  1.00 62.42  ? 90  ALA   C CA  1 
ATOM   2130 C C   . ALA   C 1 91 ? 7.694   -24.378 25.675  1.00 72.75  ? 90  ALA   C C   1 
ATOM   2131 O O   . ALA   C 1 91 ? 8.805   -24.908 25.743  1.00 70.12  ? 90  ALA   C O   1 
ATOM   2132 C CB  . ALA   C 1 91 ? 6.728   -23.002 23.787  1.00 61.53  ? 90  ALA   C CB  1 
ATOM   2133 N N   . SER   C 1 92 ? 6.561   -24.981 26.070  1.00 80.28  ? 91  SER   C N   1 
ATOM   2134 C CA  . SER   C 1 92 ? 6.513   -26.177 26.901  1.00 78.22  ? 91  SER   C CA  1 
ATOM   2135 C C   . SER   C 1 92 ? 6.780   -27.448 26.105  1.00 72.70  ? 91  SER   C C   1 
ATOM   2136 O O   . SER   C 1 92 ? 7.534   -28.307 26.551  1.00 73.10  ? 91  SER   C O   1 
ATOM   2137 C CB  . SER   C 1 92 ? 5.190   -26.289 27.603  1.00 76.40  ? 91  SER   C CB  1 
ATOM   2138 O OG  . SER   C 1 92 ? 5.115   -25.304 28.618  1.00 79.22  ? 91  SER   C OG  1 
ATOM   2139 N N   . TYR   C 1 93 ? 6.088   -27.591 24.974  1.00 69.11  ? 92  TYR   C N   1 
ATOM   2140 C CA  . TYR   C 1 93 ? 6.132   -28.814 24.188  1.00 84.38  ? 92  TYR   C CA  1 
ATOM   2141 C C   . TYR   C 1 93 ? 5.889   -30.016 25.117  1.00 90.55  ? 92  TYR   C C   1 
ATOM   2142 O O   . TYR   C 1 93 ? 5.517   -31.097 24.613  1.00 96.81  ? 92  TYR   C O   1 
ATOM   2143 C CB  . TYR   C 1 93 ? 7.452   -28.865 23.406  1.00 82.03  ? 92  TYR   C CB  1 
ATOM   2144 C CG  . TYR   C 1 93 ? 7.745   -27.603 22.599  1.00 69.43  ? 92  TYR   C CG  1 
ATOM   2145 C CD1 . TYR   C 1 93 ? 7.024   -27.311 21.443  1.00 58.09  ? 92  TYR   C CD1 1 
ATOM   2146 C CD2 . TYR   C 1 93 ? 8.736   -26.705 22.994  1.00 66.63  ? 92  TYR   C CD2 1 
ATOM   2147 C CE1 . TYR   C 1 93 ? 7.267   -26.160 20.711  1.00 61.68  ? 92  TYR   C CE1 1 
ATOM   2148 C CE2 . TYR   C 1 93 ? 8.999   -25.557 22.258  1.00 60.12  ? 92  TYR   C CE2 1 
ATOM   2149 C CZ  . TYR   C 1 93 ? 8.261   -25.285 21.115  1.00 62.58  ? 92  TYR   C CZ  1 
ATOM   2150 O OH  . TYR   C 1 93 ? 8.490   -24.152 20.381  1.00 66.80  ? 92  TYR   C OH  1 
HETATM 2151 S S   . SO4   D 2 .  ? 1.506   -33.783 1.731   1.00 118.52 ? 101 SO4   A S   1 
HETATM 2152 O O1  . SO4   D 2 .  ? 2.423   -34.254 0.725   1.00 115.11 ? 101 SO4   A O1  1 
HETATM 2153 O O2  . SO4   D 2 .  ? 1.313   -32.361 1.588   1.00 109.52 ? 101 SO4   A O2  1 
HETATM 2154 O O3  . SO4   D 2 .  ? 0.243   -34.457 1.570   1.00 131.19 ? 101 SO4   A O3  1 
HETATM 2155 O O4  . SO4   D 2 .  ? 2.040   -34.067 3.036   1.00 109.27 ? 101 SO4   A O4  1 
HETATM 2156 S S   . SO4   E 2 .  ? -8.870  -24.789 1.469   1.00 92.74  ? 102 SO4   A S   1 
HETATM 2157 O O1  . SO4   E 2 .  ? -9.334  -24.385 0.160   1.00 77.02  ? 102 SO4   A O1  1 
HETATM 2158 O O2  . SO4   E 2 .  ? -9.253  -23.784 2.437   1.00 81.98  ? 102 SO4   A O2  1 
HETATM 2159 O O3  . SO4   E 2 .  ? -9.432  -26.072 1.827   1.00 82.32  ? 102 SO4   A O3  1 
HETATM 2160 O O4  . SO4   E 2 .  ? -7.439  -24.908 1.453   1.00 106.76 ? 102 SO4   A O4  1 
HETATM 2161 C C1  . EDO   F 3 .  ? 13.992  -19.529 -7.506  1.00 39.66  ? 103 EDO   A C1  1 
HETATM 2162 O O1  . EDO   F 3 .  ? 15.286  -18.972 -7.259  1.00 34.51  ? 103 EDO   A O1  1 
HETATM 2163 C C2  . EDO   F 3 .  ? 13.171  -18.855 -8.561  1.00 39.14  ? 103 EDO   A C2  1 
HETATM 2164 O O2  . EDO   F 3 .  ? 12.780  -17.556 -8.187  1.00 37.71  ? 103 EDO   A O2  1 
HETATM 2165 S S   . SO4   G 2 .  ? 9.238   -29.442 5.883   1.00 62.49  ? 104 SO4   A S   1 
HETATM 2166 O O1  . SO4   G 2 .  ? 10.061  -28.536 5.157   1.00 64.20  ? 104 SO4   A O1  1 
HETATM 2167 O O2  . SO4   G 2 .  ? 8.858   -30.528 5.013   1.00 76.08  ? 104 SO4   A O2  1 
HETATM 2168 O O3  . SO4   G 2 .  ? 9.976   -29.973 7.018   1.00 64.33  ? 104 SO4   A O3  1 
HETATM 2169 O O4  . SO4   G 2 .  ? 8.046   -28.756 6.328   1.00 71.49  ? 104 SO4   A O4  1 
HETATM 2170 C C1  . EDO   H 3 .  ? 17.091  -15.843 -25.084 1.00 49.71  ? 101 EDO   B C1  1 
HETATM 2171 O O1  . EDO   H 3 .  ? 18.095  -16.561 -25.761 1.00 58.74  ? 101 EDO   B O1  1 
HETATM 2172 C C2  . EDO   H 3 .  ? 17.181  -14.421 -25.435 1.00 44.22  ? 101 EDO   B C2  1 
HETATM 2173 O O2  . EDO   H 3 .  ? 18.384  -13.926 -24.852 1.00 48.18  ? 101 EDO   B O2  1 
HETATM 2174 S S   . SO4   I 2 .  ? 7.535   -8.339  -24.987 1.00 89.50  ? 102 SO4   B S   1 
HETATM 2175 O O1  . SO4   I 2 .  ? 8.680   -8.424  -25.860 1.00 50.49  ? 102 SO4   B O1  1 
HETATM 2176 O O2  . SO4   I 2 .  ? 6.394   -8.998  -25.600 1.00 65.37  ? 102 SO4   B O2  1 
HETATM 2177 O O3  . SO4   I 2 .  ? 7.799   -8.988  -23.714 1.00 69.74  ? 102 SO4   B O3  1 
HETATM 2178 O O4  . SO4   I 2 .  ? 7.268   -6.933  -24.771 1.00 76.57  ? 102 SO4   B O4  1 
HETATM 2179 S S   . SO4   J 2 .  ? 14.575  -27.041 -26.507 1.00 62.25  ? 103 SO4   B S   1 
HETATM 2180 O O1  . SO4   J 2 .  ? 15.749  -26.436 -25.937 1.00 59.57  ? 103 SO4   B O1  1 
HETATM 2181 O O2  . SO4   J 2 .  ? 14.969  -28.216 -27.250 1.00 69.37  ? 103 SO4   B O2  1 
HETATM 2182 O O3  . SO4   J 2 .  ? 13.661  -27.441 -25.472 1.00 66.65  ? 103 SO4   B O3  1 
HETATM 2183 O O4  . SO4   J 2 .  ? 13.929  -26.092 -27.385 1.00 61.40  ? 103 SO4   B O4  1 
HETATM 2184 S S   . SO4   K 2 .  ? 29.445  -38.861 12.165  1.00 100.41 ? 101 SO4   C S   1 
HETATM 2185 O O1  . SO4   K 2 .  ? 30.354  -37.772 11.904  1.00 97.98  ? 101 SO4   C O1  1 
HETATM 2186 O O2  . SO4   K 2 .  ? 28.308  -38.753 11.293  1.00 85.08  ? 101 SO4   C O2  1 
HETATM 2187 O O3  . SO4   K 2 .  ? 30.107  -40.114 11.934  1.00 91.26  ? 101 SO4   C O3  1 
HETATM 2188 O O4  . SO4   K 2 .  ? 29.014  -38.810 13.537  1.00 103.30 ? 101 SO4   C O4  1 
HETATM 2189 N N1  . A1AKB L 4 .  ? 16.626  -37.733 19.350  0.66 45.82  ? 102 A1AKB C N1  1 
HETATM 2190 C C4  . A1AKB L 4 .  ? 17.021  -40.130 19.642  0.66 43.72  ? 102 A1AKB C C4  1 
HETATM 2191 C C5  . A1AKB L 4 .  ? 17.454  -38.612 21.465  0.66 45.73  ? 102 A1AKB C C5  1 
HETATM 2192 C C6  . A1AKB L 4 .  ? 16.480  -37.654 20.807  0.66 37.70  ? 102 A1AKB C C6  1 
HETATM 2193 O O   . A1AKB L 4 .  ? 15.180  -36.070 18.697  0.66 40.66  ? 102 A1AKB C O   1 
HETATM 2194 C C2  . A1AKB L 4 .  ? 16.241  -36.640 18.569  0.66 42.92  ? 102 A1AKB C C2  1 
HETATM 2195 N N   . A1AKB L 4 .  ? 17.114  -36.206 17.655  0.66 40.62  ? 102 A1AKB C N   1 
HETATM 2196 C C1  . A1AKB L 4 .  ? 18.557  -36.115 17.866  0.66 43.26  ? 102 A1AKB C C1  1 
HETATM 2197 C C   . A1AKB L 4 .  ? 16.632  -35.847 16.336  0.66 41.36  ? 102 A1AKB C C   1 
HETATM 2198 N N2  . A1AKB L 4 .  ? 17.177  -39.995 21.087  0.66 39.38  ? 102 A1AKB C N2  1 
HETATM 2199 C C3  . A1AKB L 4 .  ? 17.458  -38.870 18.932  0.66 43.50  ? 102 A1AKB C C3  1 
HETATM 2200 O O   . HOH   M 5 .  ? 4.139   -10.588 13.643  1.00 52.65  ? 201 HOH   A O   1 
HETATM 2201 O O   . HOH   M 5 .  ? 11.025  -9.259  -13.097 1.00 60.55  ? 202 HOH   A O   1 
HETATM 2202 O O   . HOH   M 5 .  ? 8.617   -32.649 4.240   1.00 51.71  ? 203 HOH   A O   1 
HETATM 2203 O O   . HOH   M 5 .  ? -5.485  -13.331 -16.468 1.00 46.72  ? 204 HOH   A O   1 
HETATM 2204 O O   . HOH   M 5 .  ? 5.530   -29.162 7.039   1.00 56.47  ? 205 HOH   A O   1 
HETATM 2205 O O   . HOH   M 5 .  ? -1.048  -30.832 0.554   1.00 58.19  ? 206 HOH   A O   1 
HETATM 2206 O O   . HOH   M 5 .  ? 10.304  -18.978 10.215  1.00 66.37  ? 207 HOH   A O   1 
HETATM 2207 O O   . HOH   M 5 .  ? 7.137   -10.694 -11.939 1.00 44.17  ? 208 HOH   A O   1 
HETATM 2208 O O   . HOH   M 5 .  ? 0.887   -9.178  -13.320 1.00 66.67  ? 209 HOH   A O   1 
HETATM 2209 O O   . HOH   M 5 .  ? 11.420  -23.881 9.684   1.00 42.68  ? 210 HOH   A O   1 
HETATM 2210 O O   . HOH   M 5 .  ? 9.242   -18.200 -10.909 1.00 34.71  ? 211 HOH   A O   1 
HETATM 2211 O O   . HOH   M 5 .  ? 14.095  -15.656 -9.148  1.00 34.24  ? 212 HOH   A O   1 
HETATM 2212 O O   . HOH   M 5 .  ? 10.912  -5.383  -7.757  1.00 32.83  ? 213 HOH   A O   1 
HETATM 2213 O O   . HOH   M 5 .  ? 13.100  -12.081 7.998   1.00 56.84  ? 214 HOH   A O   1 
HETATM 2214 O O   . HOH   M 5 .  ? 9.799   -30.612 9.497   1.00 38.01  ? 215 HOH   A O   1 
HETATM 2215 O O   . HOH   M 5 .  ? -7.066  -21.328 -4.730  1.00 71.02  ? 216 HOH   A O   1 
HETATM 2216 O O   . HOH   M 5 .  ? 4.742   -8.005  1.081   1.00 34.91  ? 217 HOH   A O   1 
HETATM 2217 O O   . HOH   M 5 .  ? -2.204  3.159   -2.361  1.00 40.02  ? 218 HOH   A O   1 
HETATM 2218 O O   . HOH   M 5 .  ? -2.049  -30.870 -3.860  1.00 48.75  ? 219 HOH   A O   1 
HETATM 2219 O O   . HOH   M 5 .  ? 10.156  -13.312 9.606   1.00 40.76  ? 220 HOH   A O   1 
HETATM 2220 O O   . HOH   M 5 .  ? 0.571   -10.564 -15.555 1.00 49.81  ? 221 HOH   A O   1 
HETATM 2221 O O   . HOH   M 5 .  ? -4.211  -21.180 6.177   1.00 42.75  ? 222 HOH   A O   1 
HETATM 2222 O O   . HOH   M 5 .  ? 11.031  -29.782 3.088   1.00 49.24  ? 223 HOH   A O   1 
HETATM 2223 O O   . HOH   M 5 .  ? -1.883  2.789   -0.829  1.00 70.45  ? 224 HOH   A O   1 
HETATM 2224 O O   . HOH   M 5 .  ? 0.339   -33.715 4.995   1.00 49.33  ? 225 HOH   A O   1 
HETATM 2225 O O   . HOH   M 5 .  ? 11.515  -12.135 5.821   1.00 34.74  ? 226 HOH   A O   1 
HETATM 2226 O O   . HOH   M 5 .  ? 16.109  -24.433 1.797   1.00 41.16  ? 227 HOH   A O   1 
HETATM 2227 O O   . HOH   M 5 .  ? 11.475  -12.413 -6.207  1.00 28.27  ? 228 HOH   A O   1 
HETATM 2228 O O   . HOH   M 5 .  ? -7.651  -17.136 6.699   1.00 47.26  ? 229 HOH   A O   1 
HETATM 2229 O O   . HOH   M 5 .  ? 3.504   -29.496 -0.433  1.00 44.89  ? 230 HOH   A O   1 
HETATM 2230 O O   . HOH   M 5 .  ? 19.971  -15.631 7.229   1.00 34.70  ? 231 HOH   A O   1 
HETATM 2231 O O   . HOH   M 5 .  ? -3.594  -10.648 6.678   1.00 34.75  ? 232 HOH   A O   1 
HETATM 2232 O O   . HOH   M 5 .  ? 1.781   0.456   -7.533  1.00 44.71  ? 233 HOH   A O   1 
HETATM 2233 O O   . HOH   M 5 .  ? -0.358  -20.922 7.038   1.00 36.74  ? 234 HOH   A O   1 
HETATM 2234 O O   . HOH   M 5 .  ? 12.544  -15.397 -11.809 1.00 68.39  ? 235 HOH   A O   1 
HETATM 2235 O O   . HOH   M 5 .  ? 4.563   -3.594  -3.297  1.00 34.92  ? 236 HOH   A O   1 
HETATM 2236 O O   . HOH   M 5 .  ? -7.777  -15.884 -0.972  1.00 30.93  ? 237 HOH   A O   1 
HETATM 2237 O O   . HOH   M 5 .  ? -1.579  -22.047 -0.666  1.00 29.74  ? 238 HOH   A O   1 
HETATM 2238 O O   . HOH   M 5 .  ? 8.301   -17.860 -15.923 1.00 60.18  ? 239 HOH   A O   1 
HETATM 2239 O O   . HOH   M 5 .  ? -5.436  -15.887 -7.911  1.00 30.36  ? 240 HOH   A O   1 
HETATM 2240 O O   . HOH   M 5 .  ? 1.997   -10.684 11.582  1.00 38.61  ? 241 HOH   A O   1 
HETATM 2241 O O   . HOH   M 5 .  ? -0.548  -29.508 10.044  1.00 73.43  ? 242 HOH   A O   1 
HETATM 2242 O O   . HOH   M 5 .  ? 1.264   -18.012 -18.534 1.00 54.66  ? 243 HOH   A O   1 
HETATM 2243 O O   . HOH   M 5 .  ? 8.299   -34.673 1.783   1.00 59.44  ? 244 HOH   A O   1 
HETATM 2244 O O   . HOH   M 5 .  ? 17.039  -18.382 -9.701  1.00 49.73  ? 245 HOH   A O   1 
HETATM 2245 O O   . HOH   M 5 .  ? 9.797   -6.159  -1.726  1.00 42.96  ? 246 HOH   A O   1 
HETATM 2246 O O   . HOH   M 5 .  ? -8.245  -21.251 -1.288  1.00 44.52  ? 247 HOH   A O   1 
HETATM 2247 O O   . HOH   M 5 .  ? 17.320  -12.932 1.428   1.00 23.02  ? 248 HOH   A O   1 
HETATM 2248 O O   . HOH   M 5 .  ? 8.998   -16.312 -13.162 1.00 40.29  ? 249 HOH   A O   1 
HETATM 2249 O O   . HOH   M 5 .  ? 2.533   -25.240 -10.190 1.00 47.78  ? 250 HOH   A O   1 
HETATM 2250 O O   . HOH   M 5 .  ? 15.892  -12.113 -5.347  1.00 39.89  ? 251 HOH   A O   1 
HETATM 2251 O O   . HOH   M 5 .  ? -1.698  -29.010 -6.194  1.00 98.83  ? 252 HOH   A O   1 
HETATM 2252 O O   . HOH   M 5 .  ? 0.427   -23.374 9.390   1.00 45.72  ? 253 HOH   A O   1 
HETATM 2253 O O   . HOH   M 5 .  ? 13.373  -12.018 -4.246  1.00 20.16  ? 254 HOH   A O   1 
HETATM 2254 O O   . HOH   M 5 .  ? 2.429   -24.731 -6.512  1.00 49.13  ? 255 HOH   A O   1 
HETATM 2255 O O   . HOH   M 5 .  ? 13.145  -9.176  -7.263  1.00 48.87  ? 256 HOH   A O   1 
HETATM 2256 O O   . HOH   M 5 .  ? 3.061   -10.091 -13.068 1.00 49.90  ? 257 HOH   A O   1 
HETATM 2257 O O   . HOH   M 5 .  ? 2.285   -4.616  -10.381 1.00 46.66  ? 258 HOH   A O   1 
HETATM 2258 O O   . HOH   M 5 .  ? -3.533  -7.613  10.405  1.00 49.66  ? 259 HOH   A O   1 
HETATM 2259 O O   . HOH   M 5 .  ? 6.787   -5.900  0.402   1.00 50.71  ? 260 HOH   A O   1 
HETATM 2260 O O   . HOH   M 5 .  ? -4.260  -25.835 -5.638  1.00 54.39  ? 261 HOH   A O   1 
HETATM 2261 O O   . HOH   M 5 .  ? 16.794  -12.388 -17.093 1.00 47.57  ? 262 HOH   A O   1 
HETATM 2262 O O   . HOH   M 5 .  ? 14.483  -29.542 4.069   1.00 42.46  ? 263 HOH   A O   1 
HETATM 2263 O O   . HOH   M 5 .  ? -1.496  -11.826 11.179  1.00 37.83  ? 264 HOH   A O   1 
HETATM 2264 O O   . HOH   M 5 .  ? -5.584  -19.828 -5.700  1.00 43.23  ? 265 HOH   A O   1 
HETATM 2265 O O   . HOH   M 5 .  ? -1.384  -7.428  11.416  1.00 51.73  ? 266 HOH   A O   1 
HETATM 2266 O O   . HOH   M 5 .  ? 8.025   -7.803  1.209   1.00 30.31  ? 267 HOH   A O   1 
HETATM 2267 O O   . HOH   M 5 .  ? 5.211   -7.567  4.099   1.00 36.07  ? 268 HOH   A O   1 
HETATM 2268 O O   . HOH   M 5 .  ? 21.387  -16.846 -3.554  1.00 32.69  ? 269 HOH   A O   1 
HETATM 2269 O O   . HOH   M 5 .  ? -6.038  -12.742 6.629   1.00 42.43  ? 270 HOH   A O   1 
HETATM 2270 O O   . HOH   M 5 .  ? 13.396  -28.290 -4.892  1.00 61.36  ? 271 HOH   A O   1 
HETATM 2271 O O   . HOH   M 5 .  ? 12.900  -13.255 -8.482  1.00 43.34  ? 272 HOH   A O   1 
HETATM 2272 O O   . HOH   M 5 .  ? 11.147  -7.861  0.342   1.00 27.28  ? 273 HOH   A O   1 
HETATM 2273 O O   . HOH   M 5 .  ? 6.490   -16.094 -14.894 1.00 48.12  ? 274 HOH   A O   1 
HETATM 2274 O O   . HOH   M 5 .  ? -8.763  -15.835 -12.760 1.00 54.47  ? 275 HOH   A O   1 
HETATM 2275 O O   . HOH   M 5 .  ? -7.947  -16.619 1.821   1.00 42.96  ? 276 HOH   A O   1 
HETATM 2276 O O   . HOH   M 5 .  ? -5.836  -26.640 3.424   1.00 54.60  ? 277 HOH   A O   1 
HETATM 2277 O O   . HOH   M 5 .  ? -9.601  -16.190 10.608  1.00 63.41  ? 278 HOH   A O   1 
HETATM 2278 O O   . HOH   M 5 .  ? 9.409   -20.400 -18.539 1.00 52.32  ? 279 HOH   A O   1 
HETATM 2279 O O   . HOH   M 5 .  ? 11.636  -5.676  -3.886  1.00 49.64  ? 280 HOH   A O   1 
HETATM 2280 O O   . HOH   M 5 .  ? 15.073  -13.365 10.586  1.00 48.28  ? 281 HOH   A O   1 
HETATM 2281 O O   . HOH   M 5 .  ? 8.245   -17.650 8.802   1.00 49.56  ? 282 HOH   A O   1 
HETATM 2282 O O   . HOH   M 5 .  ? -7.104  -11.567 -8.035  1.00 29.79  ? 283 HOH   A O   1 
HETATM 2283 O O   . HOH   M 5 .  ? -6.198  -11.827 -11.410 1.00 44.51  ? 284 HOH   A O   1 
HETATM 2284 O O   . HOH   M 5 .  ? 10.951  -27.854 -7.140  1.00 50.54  ? 285 HOH   A O   1 
HETATM 2285 O O   . HOH   M 5 .  ? -0.156  -21.067 11.174  1.00 69.13  ? 286 HOH   A O   1 
HETATM 2286 O O   . HOH   M 5 .  ? -7.956  -19.681 -3.435  1.00 46.81  ? 287 HOH   A O   1 
HETATM 2287 O O   . HOH   M 5 .  ? 22.548  -16.845 -0.631  1.00 45.86  ? 288 HOH   A O   1 
HETATM 2288 O O   . HOH   M 5 .  ? 8.804   -9.268  -13.831 1.00 38.15  ? 289 HOH   A O   1 
HETATM 2289 O O   . HOH   M 5 .  ? -5.518  -23.679 -6.773  1.00 51.78  ? 290 HOH   A O   1 
HETATM 2290 O O   . HOH   M 5 .  ? 17.444  -13.782 10.686  1.00 46.28  ? 291 HOH   A O   1 
HETATM 2291 O O   . HOH   M 5 .  ? -3.575  -10.847 9.665   1.00 58.16  ? 292 HOH   A O   1 
HETATM 2292 O O   . HOH   M 5 .  ? -3.842  -26.781 7.411   1.00 59.45  ? 293 HOH   A O   1 
HETATM 2293 O O   . HOH   M 5 .  ? 8.253   -8.336  4.580   1.00 38.37  ? 294 HOH   A O   1 
HETATM 2294 O O   . HOH   M 5 .  ? 15.117  -28.648 -1.044  1.00 65.30  ? 295 HOH   A O   1 
HETATM 2295 O O   . HOH   M 5 .  ? 2.719   -24.842 15.149  1.00 70.51  ? 296 HOH   A O   1 
HETATM 2296 O O   . HOH   M 5 .  ? -1.341  -9.115  14.031  1.00 47.93  ? 297 HOH   A O   1 
HETATM 2297 O O   . HOH   M 5 .  ? -11.249 -16.437 -3.691  1.00 60.97  ? 298 HOH   A O   1 
HETATM 2298 O O   . HOH   M 5 .  ? -7.120  -14.159 -9.260  1.00 45.83  ? 299 HOH   A O   1 
HETATM 2299 O O   . HOH   M 5 .  ? 10.733  -35.256 1.847   1.00 53.88  ? 300 HOH   A O   1 
HETATM 2300 O O   . HOH   M 5 .  ? 10.090  -2.296  -0.334  1.00 72.69  ? 301 HOH   A O   1 
HETATM 2301 O O   . HOH   M 5 .  ? 5.070   -7.020  -11.044 1.00 48.90  ? 302 HOH   A O   1 
HETATM 2302 O O   . HOH   M 5 .  ? 12.352  -29.434 -2.856  1.00 61.46  ? 303 HOH   A O   1 
HETATM 2303 O O   . HOH   M 5 .  ? 5.502   -34.507 4.553   1.00 83.95  ? 304 HOH   A O   1 
HETATM 2304 O O   . HOH   M 5 .  ? 10.875  -11.786 10.461  1.00 52.34  ? 305 HOH   A O   1 
HETATM 2305 O O   . HOH   M 5 .  ? 7.194   -30.870 -2.711  1.00 53.10  ? 306 HOH   A O   1 
HETATM 2306 O O   . HOH   M 5 .  ? -9.183  -19.096 1.827   1.00 43.34  ? 307 HOH   A O   1 
HETATM 2307 O O   . HOH   M 5 .  ? -5.705  -23.000 5.864   1.00 60.24  ? 308 HOH   A O   1 
HETATM 2308 O O   . HOH   M 5 .  ? 4.969   -9.621  -11.334 1.00 47.67  ? 309 HOH   A O   1 
HETATM 2309 O O   . HOH   M 5 .  ? -6.964  -19.266 8.213   1.00 51.03  ? 310 HOH   A O   1 
HETATM 2310 O O   . HOH   M 5 .  ? -11.158 -13.427 -3.085  1.00 47.26  ? 311 HOH   A O   1 
HETATM 2311 O O   . HOH   M 5 .  ? 12.941  -18.547 -15.422 1.00 40.78  ? 312 HOH   A O   1 
HETATM 2312 O O   . HOH   M 5 .  ? -4.866  -21.180 -8.088  1.00 57.11  ? 313 HOH   A O   1 
HETATM 2313 O O   . HOH   M 5 .  ? 4.712   -3.261  2.225   1.00 72.75  ? 314 HOH   A O   1 
HETATM 2314 O O   . HOH   N 5 .  ? 6.759   -12.475 -26.097 1.00 37.18  ? 201 HOH   B O   1 
HETATM 2315 O O   . HOH   N 5 .  ? 20.038  -22.139 -23.346 1.00 54.69  ? 202 HOH   B O   1 
HETATM 2316 O O   . HOH   N 5 .  ? 6.540   -7.613  -32.219 1.00 69.27  ? 203 HOH   B O   1 
HETATM 2317 O O   . HOH   N 5 .  ? 10.145  -19.630 -43.208 1.00 50.24  ? 204 HOH   B O   1 
HETATM 2318 O O   . HOH   N 5 .  ? 27.892  -7.994  -29.168 1.00 48.82  ? 205 HOH   B O   1 
HETATM 2319 O O   . HOH   N 5 .  ? 29.660  -12.603 -45.245 1.00 68.37  ? 206 HOH   B O   1 
HETATM 2320 O O   . HOH   N 5 .  ? 10.086  -11.102 -38.117 1.00 54.29  ? 207 HOH   B O   1 
HETATM 2321 O O   . HOH   N 5 .  ? 26.433  -12.844 -44.976 1.00 44.66  ? 208 HOH   B O   1 
HETATM 2322 O O   . HOH   N 5 .  ? 26.283  -22.963 -31.314 1.00 42.32  ? 209 HOH   B O   1 
HETATM 2323 O O   . HOH   N 5 .  ? 25.050  -5.061  -29.915 1.00 45.14  ? 210 HOH   B O   1 
HETATM 2324 O O   . HOH   N 5 .  ? 25.735  -4.547  -33.893 1.00 52.97  ? 211 HOH   B O   1 
HETATM 2325 O O   . HOH   N 5 .  ? 27.492  -17.843 -25.584 1.00 68.14  ? 212 HOH   B O   1 
HETATM 2326 O O   . HOH   N 5 .  ? 24.462  -1.584  -36.441 1.00 57.91  ? 213 HOH   B O   1 
HETATM 2327 O O   . HOH   N 5 .  ? 17.694  -19.492 -42.251 1.00 64.29  ? 214 HOH   B O   1 
HETATM 2328 O O   . HOH   N 5 .  ? 30.876  -8.060  -30.014 1.00 52.78  ? 215 HOH   B O   1 
HETATM 2329 O O   . HOH   N 5 .  ? 11.300  1.311   -39.168 1.00 40.98  ? 216 HOH   B O   1 
HETATM 2330 O O   . HOH   N 5 .  ? 20.634  -15.078 -24.052 1.00 54.41  ? 217 HOH   B O   1 
HETATM 2331 O O   . HOH   N 5 .  ? 6.908   -20.516 -24.848 1.00 55.83  ? 218 HOH   B O   1 
HETATM 2332 O O   . HOH   N 5 .  ? 10.639  -18.783 -33.076 1.00 31.01  ? 219 HOH   B O   1 
HETATM 2333 O O   . HOH   N 5 .  ? 20.763  -13.467 -42.730 1.00 42.20  ? 220 HOH   B O   1 
HETATM 2334 O O   . HOH   N 5 .  ? 25.302  -5.885  -36.099 1.00 64.43  ? 221 HOH   B O   1 
HETATM 2335 O O   . HOH   N 5 .  ? 8.864   -8.684  -16.549 1.00 46.05  ? 222 HOH   B O   1 
HETATM 2336 O O   . HOH   N 5 .  ? 18.176  -0.399  -38.543 1.00 34.33  ? 223 HOH   B O   1 
HETATM 2337 O O   . HOH   N 5 .  ? 16.895  -19.173 -28.894 1.00 25.84  ? 224 HOH   B O   1 
HETATM 2338 O O   . HOH   N 5 .  ? 34.958  -22.979 -30.220 1.00 65.86  ? 225 HOH   B O   1 
HETATM 2339 O O   . HOH   N 5 .  ? 13.127  -22.496 -20.759 1.00 52.33  ? 226 HOH   B O   1 
HETATM 2340 O O   . HOH   N 5 .  ? 22.245  3.637   -32.720 1.00 53.63  ? 227 HOH   B O   1 
HETATM 2341 O O   . HOH   N 5 .  ? 23.715  -4.121  -37.038 1.00 34.69  ? 228 HOH   B O   1 
HETATM 2342 O O   . HOH   N 5 .  ? 10.252  -16.520 -44.257 1.00 49.83  ? 229 HOH   B O   1 
HETATM 2343 O O   . HOH   N 5 .  ? 3.498   -8.551  -27.487 1.00 61.44  ? 230 HOH   B O   1 
HETATM 2344 O O   . HOH   N 5 .  ? 22.839  -23.018 -28.978 1.00 46.73  ? 231 HOH   B O   1 
HETATM 2345 O O   . HOH   N 5 .  ? 27.341  -10.614 -28.993 1.00 53.88  ? 232 HOH   B O   1 
HETATM 2346 O O   . HOH   N 5 .  ? 17.796  -0.515  -25.597 1.00 61.76  ? 233 HOH   B O   1 
HETATM 2347 O O   . HOH   N 5 .  ? 23.743  -2.274  -29.299 1.00 45.15  ? 234 HOH   B O   1 
HETATM 2348 O O   . HOH   N 5 .  ? 19.878  -2.624  -23.191 1.00 69.09  ? 235 HOH   B O   1 
HETATM 2349 O O   . HOH   N 5 .  ? 13.055  -4.602  -42.086 1.00 48.68  ? 236 HOH   B O   1 
HETATM 2350 O O   . HOH   N 5 .  ? 8.359   -23.615 -24.364 1.00 65.48  ? 237 HOH   B O   1 
HETATM 2351 O O   . HOH   N 5 .  ? 3.884   -19.148 -31.070 1.00 60.34  ? 238 HOH   B O   1 
HETATM 2352 O O   . HOH   N 5 .  ? 32.513  -18.824 -42.414 1.00 50.39  ? 239 HOH   B O   1 
HETATM 2353 O O   . HOH   N 5 .  ? 14.288  -6.279  -41.333 1.00 49.21  ? 240 HOH   B O   1 
HETATM 2354 O O   . HOH   N 5 .  ? 21.058  -6.337  -42.674 1.00 39.71  ? 241 HOH   B O   1 
HETATM 2355 O O   . HOH   N 5 .  ? 10.691  -21.817 -32.733 1.00 38.83  ? 242 HOH   B O   1 
HETATM 2356 O O   . HOH   N 5 .  ? 32.034  -21.402 -38.254 1.00 54.84  ? 243 HOH   B O   1 
HETATM 2357 O O   . HOH   N 5 .  ? 14.488  -24.577 -40.484 1.00 45.63  ? 244 HOH   B O   1 
HETATM 2358 O O   . HOH   N 5 .  ? 8.530   -27.840 -38.240 1.00 55.44  ? 245 HOH   B O   1 
HETATM 2359 O O   . HOH   N 5 .  ? 7.336   -12.539 -38.948 1.00 66.17  ? 246 HOH   B O   1 
HETATM 2360 O O   . HOH   N 5 .  ? 4.537   -19.076 -25.715 1.00 47.77  ? 247 HOH   B O   1 
HETATM 2361 O O   . HOH   N 5 .  ? 20.332  -9.980  -43.164 1.00 42.66  ? 248 HOH   B O   1 
HETATM 2362 O O   . HOH   N 5 .  ? 24.833  -6.889  -42.747 1.00 60.92  ? 249 HOH   B O   1 
HETATM 2363 O O   . HOH   N 5 .  ? 1.528   -12.665 -28.537 1.00 47.82  ? 250 HOH   B O   1 
HETATM 2364 O O   . HOH   N 5 .  ? 17.677  -3.121  -22.201 1.00 59.82  ? 251 HOH   B O   1 
HETATM 2365 O O   . HOH   N 5 .  ? 20.813  -26.579 -30.365 1.00 57.95  ? 252 HOH   B O   1 
HETATM 2366 O O   . HOH   N 5 .  ? 31.584  -12.414 -38.797 1.00 64.26  ? 253 HOH   B O   1 
HETATM 2367 O O   . HOH   N 5 .  ? 23.864  -10.714 -22.121 1.00 54.90  ? 254 HOH   B O   1 
HETATM 2368 O O   . HOH   N 5 .  ? 18.578  -25.912 -29.071 1.00 40.46  ? 255 HOH   B O   1 
HETATM 2369 O O   . HOH   N 5 .  ? 7.374   -8.197  -20.805 1.00 55.26  ? 256 HOH   B O   1 
HETATM 2370 O O   . HOH   N 5 .  ? 17.009  -9.774  -43.814 1.00 56.72  ? 257 HOH   B O   1 
HETATM 2371 O O   . HOH   N 5 .  ? 17.932  -15.854 -45.897 1.00 47.22  ? 258 HOH   B O   1 
HETATM 2372 O O   . HOH   N 5 .  ? 7.418   -18.669 -31.839 1.00 76.17  ? 259 HOH   B O   1 
HETATM 2373 O O   . HOH   N 5 .  ? 19.690  -25.784 -34.261 1.00 52.74  ? 260 HOH   B O   1 
HETATM 2374 O O   . HOH   N 5 .  ? 7.298   -19.194 -34.687 1.00 60.40  ? 261 HOH   B O   1 
HETATM 2375 O O   . HOH   N 5 .  ? 18.305  4.637   -34.465 1.00 41.54  ? 262 HOH   B O   1 
HETATM 2376 O O   . HOH   N 5 .  ? 27.908  -24.816 -35.107 1.00 36.25  ? 263 HOH   B O   1 
HETATM 2377 O O   . HOH   N 5 .  ? 38.890  -13.170 -39.315 1.00 62.06  ? 264 HOH   B O   1 
HETATM 2378 O O   . HOH   N 5 .  ? 13.265  -20.210 -19.974 1.00 54.27  ? 265 HOH   B O   1 
HETATM 2379 O O   . HOH   N 5 .  ? 26.431  -0.366  -29.541 1.00 50.28  ? 266 HOH   B O   1 
HETATM 2380 O O   . HOH   N 5 .  ? 20.493  3.995   -33.214 1.00 37.79  ? 267 HOH   B O   1 
HETATM 2381 O O   . HOH   N 5 .  ? 9.938   -6.229  -41.115 1.00 51.79  ? 268 HOH   B O   1 
HETATM 2382 O O   . HOH   N 5 .  ? 15.108  -7.990  -43.162 1.00 44.58  ? 269 HOH   B O   1 
HETATM 2383 O O   . HOH   N 5 .  ? 34.073  -17.130 -38.412 1.00 65.11  ? 270 HOH   B O   1 
HETATM 2384 O O   . HOH   N 5 .  ? 1.037   -22.141 -39.917 1.00 89.42  ? 271 HOH   B O   1 
HETATM 2385 O O   . HOH   N 5 .  ? 17.278  -25.767 -21.055 1.00 56.43  ? 272 HOH   B O   1 
HETATM 2386 O O   . HOH   N 5 .  ? 15.222  -21.908 -41.890 1.00 47.27  ? 273 HOH   B O   1 
HETATM 2387 O O   . HOH   N 5 .  ? 7.423   -10.025 -18.416 1.00 50.23  ? 274 HOH   B O   1 
HETATM 2388 O O   . HOH   N 5 .  ? 22.948  -29.311 -35.657 1.00 45.03  ? 275 HOH   B O   1 
HETATM 2389 O O   . HOH   O 5 .  ? 20.117  -20.290 29.738  1.00 53.30  ? 201 HOH   C O   1 
HETATM 2390 O O   . HOH   O 5 .  ? 26.854  -37.795 10.081  1.00 44.49  ? 202 HOH   C O   1 
HETATM 2391 O O   . HOH   O 5 .  ? 26.681  -39.170 12.680  1.00 41.33  ? 203 HOH   C O   1 
HETATM 2392 O O   . HOH   O 5 .  ? 8.546   -36.751 18.477  1.00 59.69  ? 204 HOH   C O   1 
HETATM 2393 O O   . HOH   O 5 .  ? 15.682  -41.141 15.336  1.00 60.67  ? 205 HOH   C O   1 
HETATM 2394 O O   . HOH   O 5 .  ? 30.501  -27.477 29.824  1.00 79.70  ? 206 HOH   C O   1 
HETATM 2395 O O   . HOH   O 5 .  ? 7.808   -31.724 12.697  1.00 47.35  ? 207 HOH   C O   1 
HETATM 2396 O O   . HOH   O 5 .  ? 9.281   -18.922 23.411  1.00 50.19  ? 208 HOH   C O   1 
HETATM 2397 O O   . HOH   O 5 .  ? 28.008  -37.488 15.737  1.00 44.05  ? 209 HOH   C O   1 
HETATM 2398 O O   . HOH   O 5 .  ? 19.565  -20.239 10.602  1.00 44.98  ? 210 HOH   C O   1 
HETATM 2399 O O   . HOH   O 5 .  ? 23.166  -41.511 18.308  1.00 47.15  ? 211 HOH   C O   1 
HETATM 2400 O O   . HOH   O 5 .  ? 5.622   -33.311 23.431  1.00 60.71  ? 212 HOH   C O   1 
HETATM 2401 O O   . HOH   O 5 .  ? 15.590  -21.365 12.703  1.00 41.56  ? 213 HOH   C O   1 
HETATM 2402 O O   . HOH   O 5 .  ? 30.358  -40.432 9.429   1.00 48.69  ? 214 HOH   C O   1 
HETATM 2403 O O   . HOH   O 5 .  ? 12.356  -28.258 28.353  1.00 52.12  ? 215 HOH   C O   1 
HETATM 2404 O O   . HOH   O 5 .  ? 23.464  -18.611 21.413  1.00 56.58  ? 216 HOH   C O   1 
HETATM 2405 O O   . HOH   O 5 .  ? 13.580  -37.254 13.603  1.00 57.04  ? 217 HOH   C O   1 
HETATM 2406 O O   . HOH   O 5 .  ? 12.995  -31.584 8.097   1.00 40.36  ? 218 HOH   C O   1 
HETATM 2407 O O   . HOH   O 5 .  ? 5.834   -26.554 16.927  1.00 48.70  ? 219 HOH   C O   1 
HETATM 2408 O O   . HOH   O 5 .  ? 17.796  -17.207 15.296  1.00 51.76  ? 220 HOH   C O   1 
HETATM 2409 O O   . HOH   O 5 .  ? 29.957  -39.810 31.476  1.00 48.20  ? 221 HOH   C O   1 
HETATM 2410 O O   . HOH   O 5 .  ? 25.733  -19.620 6.383   1.00 43.03  ? 222 HOH   C O   1 
HETATM 2411 O O   . HOH   O 5 .  ? 9.606   -30.430 11.132  1.00 56.96  ? 223 HOH   C O   1 
HETATM 2412 O O   . HOH   O 5 .  ? 22.002  -20.054 24.206  1.00 62.67  ? 224 HOH   C O   1 
HETATM 2413 O O   . HOH   O 5 .  ? 30.339  -36.128 28.675  1.00 59.73  ? 225 HOH   C O   1 
HETATM 2414 O O   . HOH   O 5 .  ? 31.940  -33.675 25.730  1.00 45.30  ? 226 HOH   C O   1 
HETATM 2415 O O   . HOH   O 5 .  ? 26.055  -17.713 13.887  1.00 46.03  ? 227 HOH   C O   1 
HETATM 2416 O O   . HOH   O 5 .  ? 20.262  -42.051 12.204  1.00 31.64  ? 228 HOH   C O   1 
HETATM 2417 O O   . HOH   O 5 .  ? 25.364  -31.439 10.770  1.00 35.50  ? 229 HOH   C O   1 
HETATM 2418 O O   . HOH   O 5 .  ? 33.293  -24.635 31.650  1.00 57.56  ? 230 HOH   C O   1 
HETATM 2419 O O   . HOH   O 5 .  ? 21.054  -39.930 26.356  1.00 39.64  ? 231 HOH   C O   1 
HETATM 2420 O O   . HOH   O 5 .  ? 19.784  -27.041 3.323   1.00 53.39  ? 232 HOH   C O   1 
HETATM 2421 O O   . HOH   O 5 .  ? 7.185   -18.059 10.874  1.00 42.86  ? 233 HOH   C O   1 
HETATM 2422 O O   . HOH   O 5 .  ? 22.457  -28.672 11.066  1.00 34.70  ? 234 HOH   C O   1 
HETATM 2423 O O   . HOH   O 5 .  ? 22.222  -34.589 16.591  1.00 28.32  ? 235 HOH   C O   1 
HETATM 2424 O O   . HOH   O 5 .  ? 14.013  -38.689 9.133   1.00 73.50  ? 236 HOH   C O   1 
HETATM 2425 O O   . HOH   O 5 .  ? 19.937  -13.302 13.649  1.00 45.34  ? 237 HOH   C O   1 
HETATM 2426 O O   . HOH   O 5 .  ? 30.609  -32.636 18.267  1.00 44.43  ? 238 HOH   C O   1 
HETATM 2427 O O   . HOH   O 5 .  ? 21.015  -29.565 4.708   1.00 66.93  ? 239 HOH   C O   1 
HETATM 2428 O O   . HOH   O 5 .  ? 16.438  -17.651 19.239  1.00 56.83  ? 240 HOH   C O   1 
HETATM 2429 O O   . HOH   O 5 .  ? 25.610  -34.140 34.963  1.00 57.69  ? 241 HOH   C O   1 
HETATM 2430 O O   . HOH   O 5 .  ? 31.776  -43.143 11.540  1.00 51.33  ? 242 HOH   C O   1 
HETATM 2431 O O   . HOH   O 5 .  ? 21.170  -28.869 8.386   1.00 37.50  ? 243 HOH   C O   1 
HETATM 2432 O O   . HOH   O 5 .  ? 31.530  -39.964 27.207  1.00 47.72  ? 244 HOH   C O   1 
HETATM 2433 O O   . HOH   O 5 .  ? 30.561  -32.107 15.464  1.00 60.32  ? 245 HOH   C O   1 
HETATM 2434 O O   . HOH   O 5 .  ? 2.888   -27.623 15.034  1.00 67.01  ? 246 HOH   C O   1 
HETATM 2435 O O   . HOH   O 5 .  ? 31.338  -34.415 35.437  1.00 60.15  ? 247 HOH   C O   1 
HETATM 2436 O O   . HOH   O 5 .  ? 30.299  -25.418 31.744  1.00 78.19  ? 248 HOH   C O   1 
HETATM 2437 O O   . HOH   O 5 .  ? 27.533  -38.071 24.989  1.00 59.22  ? 249 HOH   C O   1 
HETATM 2438 O O   . HOH   O 5 .  ? 25.903  -17.924 21.239  1.00 53.18  ? 250 HOH   C O   1 
HETATM 2439 O O   . HOH   O 5 .  ? 31.348  -43.920 15.740  1.00 64.73  ? 251 HOH   C O   1 
HETATM 2440 O O   . HOH   O 5 .  ? 16.818  -38.207 28.555  1.00 49.63  ? 252 HOH   C O   1 
HETATM 2441 O O   . HOH   O 5 .  ? 25.545  -39.891 20.288  1.00 45.24  ? 253 HOH   C O   1 
HETATM 2442 O O   . HOH   O 5 .  ? 4.088   -25.446 23.792  1.00 60.93  ? 254 HOH   C O   1 
HETATM 2443 O O   . HOH   O 5 .  ? 6.272   -34.585 19.269  1.00 70.48  ? 255 HOH   C O   1 
HETATM 2444 O O   . HOH   O 5 .  ? 15.017  -38.867 16.737  1.00 59.50  ? 256 HOH   C O   1 
HETATM 2445 O O   . HOH   O 5 .  ? 21.944  -13.889 13.072  1.00 51.75  ? 257 HOH   C O   1 
HETATM 2446 O O   . HOH   O 5 .  ? 12.494  -20.878 10.649  1.00 46.15  ? 258 HOH   C O   1 
HETATM 2447 O O   . HOH   O 5 .  ? 27.930  -14.759 12.961  1.00 64.60  ? 259 HOH   C O   1 
HETATM 2448 O O   . HOH   O 5 .  ? 29.363  -41.631 27.310  1.00 41.73  ? 260 HOH   C O   1 
HETATM 2449 O O   . HOH   O 5 .  ? 14.460  -22.781 27.879  1.00 67.75  ? 261 HOH   C O   1 
HETATM 2450 O O   . HOH   O 5 .  ? 4.344   -18.199 22.863  1.00 64.17  ? 262 HOH   C O   1 
HETATM 2451 O O   . HOH   O 5 .  ? 25.247  -36.402 9.993   1.00 48.20  ? 263 HOH   C O   1 
HETATM 2452 O O   . HOH   O 5 .  ? 32.044  -39.347 29.905  1.00 55.14  ? 264 HOH   C O   1 
HETATM 2453 O O   . HOH   O 5 .  ? 14.622  -42.302 19.262  1.00 66.46  ? 265 HOH   C O   1 
HETATM 2454 O O   . HOH   O 5 .  ? 4.968   -24.072 18.487  1.00 47.87  ? 266 HOH   C O   1 
HETATM 2455 O O   . HOH   O 5 .  ? 37.344  -24.450 27.020  1.00 72.13  ? 267 HOH   C O   1 
HETATM 2456 O O   . HOH   O 5 .  ? 28.690  -41.887 29.842  1.00 50.78  ? 268 HOH   C O   1 
HETATM 2457 O O   . HOH   O 5 .  ? 17.745  -27.308 36.218  1.00 83.69  ? 269 HOH   C O   1 
HETATM 2458 O O   . HOH   O 5 .  ? 28.899  -40.839 19.584  1.00 65.43  ? 270 HOH   C O   1 
# 
