data_7HH9
# 
_entry.id   7HH9 
# 
_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   7HH9         pdb_00007hh9 10.2210/pdb7hh9/pdb 
WWPDB D_1001407471 ?            ?                   
# 
_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                        7HH9 
_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    1   ? ?    ? ? 
4 non-polymer syn '(1R)-N-methyl-1-(pyridin-4-yl)propan-1-amine'     150.221   2   ? ?    ? ? 
5 water       nat water                                              18.015    233 ? ?    ? ? 
# 
_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 '(1R)-N-methyl-1-(pyridin-4-yl)propan-1-amine' A1A3W 
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 
A1A3W non-polymer         . '(1R)-N-methyl-1-(pyridin-4-yl)propan-1-amine' ?                 'C9 H14 N2'      150.221 
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 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 33 VAL VAL B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 27 ASP ASP C . n 
C 1 29 ILE 29 28 28 ILE ILE C . n 
C 1 30 ALA 30 29 29 ALA ALA C . n 
C 1 31 ASP 31 30 30 ASP ASP C . n 
C 1 32 GLY 32 31 31 GLY GLY C . n 
C 1 33 ALA 33 32 32 ALA ALA C . n 
C 1 34 VAL 34 33 33 VAL VAL C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A3W 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A3W 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 SO4   1   101 95  SO4   SO4 A . 
E 2 SO4   1   102 96  SO4   SO4 A . 
F 3 EDO   1   103 97  EDO   EDO A . 
G 2 SO4   1   104 4   SO4   SO4 A . 
H 2 SO4   1   101 1   SO4   SO4 B . 
I 2 SO4   1   102 3   SO4   SO4 B . 
J 4 A1A3W 1   103 102 A1A3W LIG B . 
K 2 SO4   1   101 5   SO4   SO4 C . 
L 4 A1A3W 1   102 101 A1A3W LIG C . 
M 5 HOH   1   201 307 HOH   HOH A . 
M 5 HOH   2   202 202 HOH   HOH A . 
M 5 HOH   3   203 84  HOH   HOH A . 
M 5 HOH   4   204 304 HOH   HOH A . 
M 5 HOH   5   205 66  HOH   HOH A . 
M 5 HOH   6   206 71  HOH   HOH A . 
M 5 HOH   7   207 55  HOH   HOH A . 
M 5 HOH   8   208 278 HOH   HOH A . 
M 5 HOH   9   209 293 HOH   HOH A . 
M 5 HOH   10  210 299 HOH   HOH A . 
M 5 HOH   11  211 289 HOH   HOH A . 
M 5 HOH   12  212 208 HOH   HOH A . 
M 5 HOH   13  213 95  HOH   HOH A . 
M 5 HOH   14  214 287 HOH   HOH A . 
M 5 HOH   15  215 139 HOH   HOH A . 
M 5 HOH   16  216 91  HOH   HOH A . 
M 5 HOH   17  217 86  HOH   HOH A . 
M 5 HOH   18  218 26  HOH   HOH A . 
M 5 HOH   19  219 188 HOH   HOH A . 
M 5 HOH   20  220 203 HOH   HOH A . 
M 5 HOH   21  221 8   HOH   HOH A . 
M 5 HOH   22  222 85  HOH   HOH A . 
M 5 HOH   23  223 28  HOH   HOH A . 
M 5 HOH   24  224 87  HOH   HOH A . 
M 5 HOH   25  225 41  HOH   HOH A . 
M 5 HOH   26  226 37  HOH   HOH A . 
M 5 HOH   27  227 260 HOH   HOH A . 
M 5 HOH   28  228 1   HOH   HOH A . 
M 5 HOH   29  229 211 HOH   HOH A . 
M 5 HOH   30  230 2   HOH   HOH A . 
M 5 HOH   31  231 34  HOH   HOH A . 
M 5 HOH   32  232 259 HOH   HOH A . 
M 5 HOH   33  233 32  HOH   HOH A . 
M 5 HOH   34  234 179 HOH   HOH A . 
M 5 HOH   35  235 167 HOH   HOH A . 
M 5 HOH   36  236 97  HOH   HOH A . 
M 5 HOH   37  237 42  HOH   HOH A . 
M 5 HOH   38  238 23  HOH   HOH A . 
M 5 HOH   39  239 7   HOH   HOH A . 
M 5 HOH   40  240 12  HOH   HOH A . 
M 5 HOH   41  241 290 HOH   HOH A . 
M 5 HOH   42  242 288 HOH   HOH A . 
M 5 HOH   43  243 99  HOH   HOH A . 
M 5 HOH   44  244 292 HOH   HOH A . 
M 5 HOH   45  245 78  HOH   HOH A . 
M 5 HOH   46  246 190 HOH   HOH A . 
M 5 HOH   47  247 297 HOH   HOH A . 
M 5 HOH   48  248 267 HOH   HOH A . 
M 5 HOH   49  249 301 HOH   HOH A . 
M 5 HOH   50  250 94  HOH   HOH A . 
M 5 HOH   51  251 60  HOH   HOH A . 
M 5 HOH   52  252 274 HOH   HOH A . 
M 5 HOH   53  253 111 HOH   HOH A . 
M 5 HOH   54  254 185 HOH   HOH A . 
M 5 HOH   55  255 145 HOH   HOH A . 
M 5 HOH   56  256 164 HOH   HOH A . 
M 5 HOH   57  257 20  HOH   HOH A . 
M 5 HOH   58  258 27  HOH   HOH A . 
M 5 HOH   59  259 38  HOH   HOH A . 
M 5 HOH   60  260 199 HOH   HOH A . 
M 5 HOH   61  261 115 HOH   HOH A . 
M 5 HOH   62  262 300 HOH   HOH A . 
M 5 HOH   63  263 93  HOH   HOH A . 
M 5 HOH   64  264 18  HOH   HOH A . 
M 5 HOH   65  265 116 HOH   HOH A . 
M 5 HOH   66  266 77  HOH   HOH A . 
M 5 HOH   67  267 152 HOH   HOH A . 
M 5 HOH   68  268 218 HOH   HOH A . 
M 5 HOH   69  269 109 HOH   HOH A . 
M 5 HOH   70  270 58  HOH   HOH A . 
M 5 HOH   71  271 318 HOH   HOH A . 
M 5 HOH   72  272 14  HOH   HOH A . 
M 5 HOH   73  273 222 HOH   HOH A . 
M 5 HOH   74  274 21  HOH   HOH A . 
M 5 HOH   75  275 31  HOH   HOH A . 
M 5 HOH   76  276 73  HOH   HOH A . 
M 5 HOH   77  277 16  HOH   HOH A . 
M 5 HOH   78  278 131 HOH   HOH A . 
M 5 HOH   79  279 165 HOH   HOH A . 
M 5 HOH   80  280 19  HOH   HOH A . 
M 5 HOH   81  281 9   HOH   HOH A . 
M 5 HOH   82  282 281 HOH   HOH A . 
M 5 HOH   83  283 64  HOH   HOH A . 
M 5 HOH   84  284 143 HOH   HOH A . 
M 5 HOH   85  285 75  HOH   HOH A . 
M 5 HOH   86  286 113 HOH   HOH A . 
M 5 HOH   87  287 47  HOH   HOH A . 
M 5 HOH   88  288 22  HOH   HOH A . 
M 5 HOH   89  289 296 HOH   HOH A . 
M 5 HOH   90  290 63  HOH   HOH A . 
M 5 HOH   91  291 108 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 83  HOH   HOH A . 
M 5 HOH   95  295 219 HOH   HOH A . 
M 5 HOH   96  296 283 HOH   HOH A . 
M 5 HOH   97  297 205 HOH   HOH A . 
M 5 HOH   98  298 156 HOH   HOH A . 
M 5 HOH   99  299 35  HOH   HOH A . 
M 5 HOH   100 300 57  HOH   HOH A . 
M 5 HOH   101 301 206 HOH   HOH A . 
M 5 HOH   102 302 125 HOH   HOH A . 
M 5 HOH   103 303 332 HOH   HOH A . 
N 5 HOH   1   201 329 HOH   HOH B . 
N 5 HOH   2   202 184 HOH   HOH B . 
N 5 HOH   3   203 331 HOH   HOH B . 
N 5 HOH   4   204 123 HOH   HOH B . 
N 5 HOH   5   205 272 HOH   HOH B . 
N 5 HOH   6   206 258 HOH   HOH B . 
N 5 HOH   7   207 98  HOH   HOH B . 
N 5 HOH   8   208 89  HOH   HOH B . 
N 5 HOH   9   209 279 HOH   HOH B . 
N 5 HOH   10  210 172 HOH   HOH B . 
N 5 HOH   11  211 247 HOH   HOH B . 
N 5 HOH   12  212 69  HOH   HOH B . 
N 5 HOH   13  213 249 HOH   HOH B . 
N 5 HOH   14  214 54  HOH   HOH B . 
N 5 HOH   15  215 153 HOH   HOH B . 
N 5 HOH   16  216 280 HOH   HOH B . 
N 5 HOH   17  217 17  HOH   HOH B . 
N 5 HOH   18  218 6   HOH   HOH B . 
N 5 HOH   19  219 215 HOH   HOH B . 
N 5 HOH   20  220 137 HOH   HOH B . 
N 5 HOH   21  221 10  HOH   HOH B . 
N 5 HOH   22  222 117 HOH   HOH B . 
N 5 HOH   23  223 261 HOH   HOH B . 
N 5 HOH   24  224 5   HOH   HOH B . 
N 5 HOH   25  225 119 HOH   HOH B . 
N 5 HOH   26  226 25  HOH   HOH B . 
N 5 HOH   27  227 170 HOH   HOH B . 
N 5 HOH   28  228 224 HOH   HOH B . 
N 5 HOH   29  229 150 HOH   HOH B . 
N 5 HOH   30  230 61  HOH   HOH B . 
N 5 HOH   31  231 120 HOH   HOH B . 
N 5 HOH   32  232 320 HOH   HOH B . 
N 5 HOH   33  233 101 HOH   HOH B . 
N 5 HOH   34  234 79  HOH   HOH B . 
N 5 HOH   35  235 59  HOH   HOH B . 
N 5 HOH   36  236 24  HOH   HOH B . 
N 5 HOH   37  237 315 HOH   HOH B . 
N 5 HOH   38  238 217 HOH   HOH B . 
N 5 HOH   39  239 96  HOH   HOH B . 
N 5 HOH   40  240 13  HOH   HOH B . 
N 5 HOH   41  241 169 HOH   HOH B . 
N 5 HOH   42  242 68  HOH   HOH B . 
N 5 HOH   43  243 74  HOH   HOH B . 
N 5 HOH   44  244 157 HOH   HOH B . 
N 5 HOH   45  245 223 HOH   HOH B . 
N 5 HOH   46  246 175 HOH   HOH B . 
N 5 HOH   47  247 168 HOH   HOH B . 
N 5 HOH   48  248 214 HOH   HOH B . 
N 5 HOH   49  249 36  HOH   HOH B . 
N 5 HOH   50  250 160 HOH   HOH B . 
N 5 HOH   51  251 104 HOH   HOH B . 
N 5 HOH   52  252 72  HOH   HOH B . 
N 5 HOH   53  253 197 HOH   HOH B . 
N 5 HOH   54  254 76  HOH   HOH B . 
N 5 HOH   55  255 44  HOH   HOH B . 
N 5 HOH   56  256 322 HOH   HOH B . 
N 5 HOH   57  257 316 HOH   HOH B . 
N 5 HOH   58  258 163 HOH   HOH B . 
N 5 HOH   59  259 46  HOH   HOH B . 
N 5 HOH   60  260 303 HOH   HOH B . 
N 5 HOH   61  261 177 HOH   HOH B . 
N 5 HOH   62  262 201 HOH   HOH B . 
N 5 HOH   63  263 291 HOH   HOH B . 
N 5 HOH   64  264 182 HOH   HOH B . 
N 5 HOH   65  265 314 HOH   HOH B . 
N 5 HOH   66  266 107 HOH   HOH B . 
N 5 HOH   67  267 312 HOH   HOH B . 
N 5 HOH   68  268 310 HOH   HOH B . 
O 5 HOH   1   201 321 HOH   HOH C . 
O 5 HOH   2   202 254 HOH   HOH C . 
O 5 HOH   3   203 323 HOH   HOH C . 
O 5 HOH   4   204 173 HOH   HOH C . 
O 5 HOH   5   205 134 HOH   HOH C . 
O 5 HOH   6   206 284 HOH   HOH C . 
O 5 HOH   7   207 226 HOH   HOH C . 
O 5 HOH   8   208 90  HOH   HOH C . 
O 5 HOH   9   209 271 HOH   HOH C . 
O 5 HOH   10  210 53  HOH   HOH C . 
O 5 HOH   11  211 49  HOH   HOH C . 
O 5 HOH   12  212 317 HOH   HOH C . 
O 5 HOH   13  213 151 HOH   HOH C . 
O 5 HOH   14  214 189 HOH   HOH C . 
O 5 HOH   15  215 118 HOH   HOH C . 
O 5 HOH   16  216 142 HOH   HOH C . 
O 5 HOH   17  217 161 HOH   HOH C . 
O 5 HOH   18  218 333 HOH   HOH C . 
O 5 HOH   19  219 56  HOH   HOH C . 
O 5 HOH   20  220 82  HOH   HOH C . 
O 5 HOH   21  221 269 HOH   HOH C . 
O 5 HOH   22  222 302 HOH   HOH C . 
O 5 HOH   23  223 209 HOH   HOH C . 
O 5 HOH   24  224 15  HOH   HOH C . 
O 5 HOH   25  225 294 HOH   HOH C . 
O 5 HOH   26  226 102 HOH   HOH C . 
O 5 HOH   27  227 45  HOH   HOH C . 
O 5 HOH   28  228 4   HOH   HOH C . 
O 5 HOH   29  229 40  HOH   HOH C . 
O 5 HOH   30  230 48  HOH   HOH C . 
O 5 HOH   31  231 126 HOH   HOH C . 
O 5 HOH   32  232 275 HOH   HOH C . 
O 5 HOH   33  233 43  HOH   HOH C . 
O 5 HOH   34  234 122 HOH   HOH C . 
O 5 HOH   35  235 171 HOH   HOH C . 
O 5 HOH   36  236 130 HOH   HOH C . 
O 5 HOH   37  237 242 HOH   HOH C . 
O 5 HOH   38  238 132 HOH   HOH C . 
O 5 HOH   39  239 148 HOH   HOH C . 
O 5 HOH   40  240 309 HOH   HOH C . 
O 5 HOH   41  241 67  HOH   HOH C . 
O 5 HOH   42  242 135 HOH   HOH C . 
O 5 HOH   43  243 334 HOH   HOH C . 
O 5 HOH   44  244 62  HOH   HOH C . 
O 5 HOH   45  245 328 HOH   HOH C . 
O 5 HOH   46  246 149 HOH   HOH C . 
O 5 HOH   47  247 298 HOH   HOH C . 
O 5 HOH   48  248 198 HOH   HOH C . 
O 5 HOH   49  249 65  HOH   HOH C . 
O 5 HOH   50  250 330 HOH   HOH C . 
O 5 HOH   51  251 305 HOH   HOH C . 
O 5 HOH   52  252 146 HOH   HOH C . 
O 5 HOH   53  253 241 HOH   HOH C . 
O 5 HOH   54  254 270 HOH   HOH C . 
O 5 HOH   55  255 319 HOH   HOH C . 
O 5 HOH   56  256 70  HOH   HOH C . 
O 5 HOH   57  257 246 HOH   HOH C . 
O 5 HOH   58  258 295 HOH   HOH C . 
O 5 HOH   59  259 324 HOH   HOH C . 
O 5 HOH   60  260 103 HOH   HOH C . 
O 5 HOH   61  261 92  HOH   HOH C . 
O 5 HOH   62  262 313 HOH   HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 16 ? CE  ? A LYS 17 CE  
2  1 Y 1 A LYS 16 ? NZ  ? A LYS 17 NZ  
3  1 Y 1 A ASP 62 ? CG  ? A ASP 63 CG  
4  1 Y 1 A ASP 62 ? OD1 ? A ASP 63 OD1 
5  1 Y 1 A ASP 62 ? OD2 ? A ASP 63 OD2 
6  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
7  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
8  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
9  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
10 1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
11 1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
12 1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
13 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
14 1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
15 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
16 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
17 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
18 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
19 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
20 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
21 1 Y 1 B LYS 65 ? CD  ? B LYS 66 CD  
22 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
23 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
24 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
25 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
26 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
27 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
28 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
29 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
30 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
31 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
32 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
33 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
34 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
35 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
36 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
37 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
38 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
39 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
40 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
41 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
42 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
43 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
44 1 Y 1 C ASP 27 ? CG  ? C ASP 28 CG  
45 1 Y 1 C ASP 27 ? OD1 ? C ASP 28 OD1 
46 1 Y 1 C ASP 27 ? OD2 ? C ASP 28 OD2 
47 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
48 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
49 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
50 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
51 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
52 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
53 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
54 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
55 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
56 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
57 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
58 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
59 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
60 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
61 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
62 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
63 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
64 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
65 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
66 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
67 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
68 1 Y 1 C LYS 75 ? NZ  ? C LYS 76 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HH9 
_cell.length_a           41.780 
_cell.length_b           42.080 
_cell.length_c           159.160 
_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                         7HH9 
_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          7HH9 
_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                     7HH9 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             79.58 
_reflns.d_resolution_high            1.54 
_reflns.number_obs                   42643 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.075 
_reflns.pdbx_netI_over_sigmaI        10.5 
_reflns.pdbx_redundancy              6.1 
_reflns.pdbx_Rrim_I_all              0.083 
_reflns.pdbx_Rpim_I_all              0.033 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     261938 
_reflns.pdbx_chi_squared             0.97 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.54 
_reflns_shell.d_res_low                   1.58 
_reflns_shell.number_measured_all         15875 
_reflns_shell.number_unique_obs           3083 
_reflns_shell.Rmerge_I_obs                1.780 
_reflns_shell.pdbx_chi_squared            0.76 
_reflns_shell.pdbx_redundancy             5.1 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             1.984 
_reflns_shell.pdbx_Rpim_I_all             0.868 
_reflns_shell.pdbx_CC_half                0.341 
_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                                 7HH9 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     40309 
_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                             79.58 
_refine.ls_d_res_high                            1.54 
_refine.ls_percent_reflns_obs                    99.93 
_refine.ls_R_factor_obs                          0.21071 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20846 
_refine.ls_R_factor_R_free                       0.25135 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.3 
_refine.ls_number_reflns_R_free                  2256 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.955 
_refine.B_iso_mean                               36.160 
_refine.aniso_B[1][1]                            0.32 
_refine.aniso_B[2][2]                            -0.07 
_refine.aniso_B[3][3]                            -0.24 
_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                       0.093 
_refine.pdbx_overall_ESU_R_Free                  0.097 
_refine.overall_SU_ML                            0.084 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.416 
_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        2156 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         56 
_refine_hist.number_atoms_solvent             233 
_refine_hist.number_atoms_total               2445 
_refine_hist.d_res_high                       1.54 
_refine_hist.d_res_low                        79.58 
# 
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             0.009  0.012  ? 2307 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.905  1.829  ? 3140 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.047  5.000  ? 270  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       8.259  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.301 10.000 ? 297  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.123  0.200  ? 292  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.010  0.020  ? 1934 '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                  3.266  3.409  ? 1089 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.427  6.096  ? 1356 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.560  3.688  ? 1218 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       8.631  50.89  ? 3563 '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                       1.540 
_refine_ls_shell.d_res_low                        1.580 
_refine_ls_shell.number_reflns_R_work             2909 
_refine_ls_shell.R_factor_R_work                  0.345 
_refine_ls_shell.percent_reflns_obs               99.71 
_refine_ls_shell.R_factor_R_free                  0.368 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             169 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HH9 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z1250132788' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HH9 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 2 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HH9 A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HH9 B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HH9 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 7HH9 GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HH9 SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HH9 GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HH9 SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HH9 GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HH9 SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O ALA A 24 ? O ALA A 23 N VAL A 12 ? N VAL A 11 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O ALA B 24 ? O ALA B 23 N VAL B 12 ? N VAL B 11 
AA2 4 5 N PHE B 13 ? N PHE B 12 O PHE B 60 ? O PHE B 59 
AA3 1 2 O LEU C 54 ? O LEU C 53 N TYR C 41 ? N TYR C 40 
AA3 2 3 O PHE C 44 ? O PHE C 43 N ARG C 25 ? N ARG C 24 
AA3 3 4 O ALA C 24 ? O ALA C 23 N VAL C 12 ? N VAL C 11 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HH9 
_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 210 ? ? O C HOH 218 ? ? 1.23 
2 1 O  B HOH 216 ? ? O B HOH 256 ? ? 1.53 
3 1 O2 C SO4 101 ? ? O C HOH 201 ? ? 2.00 
4 1 O2 A SO4 104 ? ? O A HOH 201 ? ? 2.05 
5 1 O  C HOH 225 ? ? O C HOH 255 ? ? 2.15 
6 1 O  B HOH 241 ? ? O B HOH 258 ? ? 2.18 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_1             C 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              74 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CZ 
_pdbx_validate_rmsd_angle.auth_asym_id_2             C 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              74 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH1 
_pdbx_validate_rmsd_angle.auth_asym_id_3             C 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              74 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                116.18 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -4.12 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.50 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -156.15 69.64   
2 1 ASN B 38 ? ? 80.56   -5.13   
3 1 ASN B 87 ? ? -162.15 59.08   
4 1 ASN C 87 ? ? -158.47 50.65   
5 1 ALA C 90 ? ? -63.55  -177.74 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_1   A 
_pdbx_validate_peptide_omega.auth_seq_id_1    11 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PHE 
_pdbx_validate_peptide_omega.auth_asym_id_2   A 
_pdbx_validate_peptide_omega.auth_seq_id_2    12 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            148.84 
# 
_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                       303 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.95 
_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 ALA 29 ? B ALA 30 
4  1 Y 1 B ASP 30 ? B ASP 31 
5  1 Y 1 B GLY 31 ? B GLY 32 
6  1 Y 1 B ALA 32 ? B ALA 33 
7  1 Y 1 C GLY 0  ? C GLY 1  
8  1 Y 1 C MET 1  ? C MET 2  
9  1 Y 1 C PRO 2  ? C PRO 3  
10 1 Y 1 C 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 
A1A3W N1   N Y N 1   
A1A3W C4   C Y N 2   
A1A3W C5   C Y N 3   
A1A3W C6   C Y N 4   
A1A3W C7   C Y N 5   
A1A3W C8   C Y N 6   
A1A3W C3   C N N 7   
A1A3W N    N N N 8   
A1A3W C2   C N S 9   
A1A3W C1   C N N 10  
A1A3W C    C N N 11  
A1A3W H10  H N N 12  
A1A3W H11  H N N 13  
A1A3W H12  H N N 14  
A1A3W H13  H N N 15  
A1A3W H7   H N N 16  
A1A3W H9   H N N 17  
A1A3W H8   H N N 18  
A1A3W H6   H N N 19  
A1A3W H5   H N N 20  
A1A3W H4   H N N 21  
A1A3W H3   H N N 22  
A1A3W H2   H N N 23  
A1A3W H1   H N N 24  
A1A3W H    H N N 25  
ALA   N    N N N 26  
ALA   CA   C N S 27  
ALA   C    C N N 28  
ALA   O    O N N 29  
ALA   CB   C N N 30  
ALA   OXT  O N N 31  
ALA   H    H N N 32  
ALA   H2   H N N 33  
ALA   HA   H N N 34  
ALA   HB1  H N N 35  
ALA   HB2  H N N 36  
ALA   HB3  H N N 37  
ALA   HXT  H N N 38  
ARG   N    N N N 39  
ARG   CA   C N S 40  
ARG   C    C N N 41  
ARG   O    O N N 42  
ARG   CB   C N N 43  
ARG   CG   C N N 44  
ARG   CD   C N N 45  
ARG   NE   N N N 46  
ARG   CZ   C N N 47  
ARG   NH1  N N N 48  
ARG   NH2  N N N 49  
ARG   OXT  O N N 50  
ARG   H    H N N 51  
ARG   H2   H N N 52  
ARG   HA   H N N 53  
ARG   HB2  H N N 54  
ARG   HB3  H N N 55  
ARG   HG2  H N N 56  
ARG   HG3  H N N 57  
ARG   HD2  H N N 58  
ARG   HD3  H N N 59  
ARG   HE   H N N 60  
ARG   HH11 H N N 61  
ARG   HH12 H N N 62  
ARG   HH21 H N N 63  
ARG   HH22 H N N 64  
ARG   HXT  H N N 65  
ASN   N    N N N 66  
ASN   CA   C N S 67  
ASN   C    C N N 68  
ASN   O    O N N 69  
ASN   CB   C N N 70  
ASN   CG   C N N 71  
ASN   OD1  O N N 72  
ASN   ND2  N N N 73  
ASN   OXT  O N N 74  
ASN   H    H N N 75  
ASN   H2   H N N 76  
ASN   HA   H N N 77  
ASN   HB2  H N N 78  
ASN   HB3  H N N 79  
ASN   HD21 H N N 80  
ASN   HD22 H N N 81  
ASN   HXT  H N N 82  
ASP   N    N N N 83  
ASP   CA   C N S 84  
ASP   C    C N N 85  
ASP   O    O N N 86  
ASP   CB   C N N 87  
ASP   CG   C N N 88  
ASP   OD1  O N N 89  
ASP   OD2  O N N 90  
ASP   OXT  O N N 91  
ASP   H    H N N 92  
ASP   H2   H N N 93  
ASP   HA   H N N 94  
ASP   HB2  H N N 95  
ASP   HB3  H N N 96  
ASP   HD2  H N N 97  
ASP   HXT  H N N 98  
CYS   N    N N N 99  
CYS   CA   C N R 100 
CYS   C    C N N 101 
CYS   O    O N N 102 
CYS   CB   C N N 103 
CYS   SG   S N N 104 
CYS   OXT  O N N 105 
CYS   H    H N N 106 
CYS   H2   H N N 107 
CYS   HA   H N N 108 
CYS   HB2  H N N 109 
CYS   HB3  H N N 110 
CYS   HG   H N N 111 
CYS   HXT  H N N 112 
EDO   C1   C N N 113 
EDO   O1   O N N 114 
EDO   C2   C N N 115 
EDO   O2   O N N 116 
EDO   H11  H N N 117 
EDO   H12  H N N 118 
EDO   HO1  H N N 119 
EDO   H21  H N N 120 
EDO   H22  H N N 121 
EDO   HO2  H N N 122 
GLN   N    N N N 123 
GLN   CA   C N S 124 
GLN   C    C N N 125 
GLN   O    O N N 126 
GLN   CB   C N N 127 
GLN   CG   C N N 128 
GLN   CD   C N N 129 
GLN   OE1  O N N 130 
GLN   NE2  N N N 131 
GLN   OXT  O N N 132 
GLN   H    H N N 133 
GLN   H2   H N N 134 
GLN   HA   H N N 135 
GLN   HB2  H N N 136 
GLN   HB3  H N N 137 
GLN   HG2  H N N 138 
GLN   HG3  H N N 139 
GLN   HE21 H N N 140 
GLN   HE22 H N N 141 
GLN   HXT  H N N 142 
GLU   N    N N N 143 
GLU   CA   C N S 144 
GLU   C    C N N 145 
GLU   O    O N N 146 
GLU   CB   C N N 147 
GLU   CG   C N N 148 
GLU   CD   C N N 149 
GLU   OE1  O N N 150 
GLU   OE2  O N N 151 
GLU   OXT  O N N 152 
GLU   H    H N N 153 
GLU   H2   H N N 154 
GLU   HA   H N N 155 
GLU   HB2  H N N 156 
GLU   HB3  H N N 157 
GLU   HG2  H N N 158 
GLU   HG3  H N N 159 
GLU   HE2  H N N 160 
GLU   HXT  H N N 161 
GLY   N    N N N 162 
GLY   CA   C N N 163 
GLY   C    C N N 164 
GLY   O    O N N 165 
GLY   OXT  O N N 166 
GLY   H    H N N 167 
GLY   H2   H N N 168 
GLY   HA2  H N N 169 
GLY   HA3  H N N 170 
GLY   HXT  H N N 171 
HIS   N    N N N 172 
HIS   CA   C N S 173 
HIS   C    C N N 174 
HIS   O    O N N 175 
HIS   CB   C N N 176 
HIS   CG   C Y N 177 
HIS   ND1  N Y N 178 
HIS   CD2  C Y N 179 
HIS   CE1  C Y N 180 
HIS   NE2  N Y N 181 
HIS   OXT  O N N 182 
HIS   H    H N N 183 
HIS   H2   H N N 184 
HIS   HA   H N N 185 
HIS   HB2  H N N 186 
HIS   HB3  H N N 187 
HIS   HD1  H N N 188 
HIS   HD2  H N N 189 
HIS   HE1  H N N 190 
HIS   HE2  H N N 191 
HIS   HXT  H N N 192 
HOH   O    O N N 193 
HOH   H1   H N N 194 
HOH   H2   H N N 195 
ILE   N    N N N 196 
ILE   CA   C N S 197 
ILE   C    C N N 198 
ILE   O    O N N 199 
ILE   CB   C N S 200 
ILE   CG1  C N N 201 
ILE   CG2  C N N 202 
ILE   CD1  C N N 203 
ILE   OXT  O N N 204 
ILE   H    H N N 205 
ILE   H2   H N N 206 
ILE   HA   H N N 207 
ILE   HB   H N N 208 
ILE   HG12 H N N 209 
ILE   HG13 H N N 210 
ILE   HG21 H N N 211 
ILE   HG22 H N N 212 
ILE   HG23 H N N 213 
ILE   HD11 H N N 214 
ILE   HD12 H N N 215 
ILE   HD13 H N N 216 
ILE   HXT  H N N 217 
LEU   N    N N N 218 
LEU   CA   C N S 219 
LEU   C    C N N 220 
LEU   O    O N N 221 
LEU   CB   C N N 222 
LEU   CG   C N N 223 
LEU   CD1  C N N 224 
LEU   CD2  C N N 225 
LEU   OXT  O N N 226 
LEU   H    H N N 227 
LEU   H2   H N N 228 
LEU   HA   H N N 229 
LEU   HB2  H N N 230 
LEU   HB3  H N N 231 
LEU   HG   H N N 232 
LEU   HD11 H N N 233 
LEU   HD12 H N N 234 
LEU   HD13 H N N 235 
LEU   HD21 H N N 236 
LEU   HD22 H N N 237 
LEU   HD23 H N N 238 
LEU   HXT  H N N 239 
LYS   N    N N N 240 
LYS   CA   C N S 241 
LYS   C    C N N 242 
LYS   O    O N N 243 
LYS   CB   C N N 244 
LYS   CG   C N N 245 
LYS   CD   C N N 246 
LYS   CE   C N N 247 
LYS   NZ   N N N 248 
LYS   OXT  O N N 249 
LYS   H    H N N 250 
LYS   H2   H N N 251 
LYS   HA   H N N 252 
LYS   HB2  H N N 253 
LYS   HB3  H N N 254 
LYS   HG2  H N N 255 
LYS   HG3  H N N 256 
LYS   HD2  H N N 257 
LYS   HD3  H N N 258 
LYS   HE2  H N N 259 
LYS   HE3  H N N 260 
LYS   HZ1  H N N 261 
LYS   HZ2  H N N 262 
LYS   HZ3  H N N 263 
LYS   HXT  H N N 264 
MET   N    N N N 265 
MET   CA   C N S 266 
MET   C    C N N 267 
MET   O    O N N 268 
MET   CB   C N N 269 
MET   CG   C N N 270 
MET   SD   S N N 271 
MET   CE   C N N 272 
MET   OXT  O N N 273 
MET   H    H N N 274 
MET   H2   H N N 275 
MET   HA   H N N 276 
MET   HB2  H N N 277 
MET   HB3  H N N 278 
MET   HG2  H N N 279 
MET   HG3  H N N 280 
MET   HE1  H N N 281 
MET   HE2  H N N 282 
MET   HE3  H N N 283 
MET   HXT  H N N 284 
PHE   N    N N N 285 
PHE   CA   C N S 286 
PHE   C    C N N 287 
PHE   O    O N N 288 
PHE   CB   C N N 289 
PHE   CG   C Y N 290 
PHE   CD1  C Y N 291 
PHE   CD2  C Y N 292 
PHE   CE1  C Y N 293 
PHE   CE2  C Y N 294 
PHE   CZ   C Y N 295 
PHE   OXT  O N N 296 
PHE   H    H N N 297 
PHE   H2   H N N 298 
PHE   HA   H N N 299 
PHE   HB2  H N N 300 
PHE   HB3  H N N 301 
PHE   HD1  H N N 302 
PHE   HD2  H N N 303 
PHE   HE1  H N N 304 
PHE   HE2  H N N 305 
PHE   HZ   H N N 306 
PHE   HXT  H N N 307 
PRO   N    N N N 308 
PRO   CA   C N S 309 
PRO   C    C N N 310 
PRO   O    O N N 311 
PRO   CB   C N N 312 
PRO   CG   C N N 313 
PRO   CD   C N N 314 
PRO   OXT  O N N 315 
PRO   H    H N N 316 
PRO   HA   H N N 317 
PRO   HB2  H N N 318 
PRO   HB3  H N N 319 
PRO   HG2  H N N 320 
PRO   HG3  H N N 321 
PRO   HD2  H N N 322 
PRO   HD3  H N N 323 
PRO   HXT  H N N 324 
SER   N    N N N 325 
SER   CA   C N S 326 
SER   C    C N N 327 
SER   O    O N N 328 
SER   CB   C N N 329 
SER   OG   O N N 330 
SER   OXT  O N N 331 
SER   H    H N N 332 
SER   H2   H N N 333 
SER   HA   H N N 334 
SER   HB2  H N N 335 
SER   HB3  H N N 336 
SER   HG   H N N 337 
SER   HXT  H N N 338 
SO4   S    S N N 339 
SO4   O1   O N N 340 
SO4   O2   O N N 341 
SO4   O3   O N N 342 
SO4   O4   O N N 343 
THR   N    N N N 344 
THR   CA   C N S 345 
THR   C    C N N 346 
THR   O    O N N 347 
THR   CB   C N R 348 
THR   OG1  O N N 349 
THR   CG2  C N N 350 
THR   OXT  O N N 351 
THR   H    H N N 352 
THR   H2   H N N 353 
THR   HA   H N N 354 
THR   HB   H N N 355 
THR   HG1  H N N 356 
THR   HG21 H N N 357 
THR   HG22 H N N 358 
THR   HG23 H N N 359 
THR   HXT  H N N 360 
TRP   N    N N N 361 
TRP   CA   C N S 362 
TRP   C    C N N 363 
TRP   O    O N N 364 
TRP   CB   C N N 365 
TRP   CG   C Y N 366 
TRP   CD1  C Y N 367 
TRP   CD2  C Y N 368 
TRP   NE1  N Y N 369 
TRP   CE2  C Y N 370 
TRP   CE3  C Y N 371 
TRP   CZ2  C Y N 372 
TRP   CZ3  C Y N 373 
TRP   CH2  C Y N 374 
TRP   OXT  O N N 375 
TRP   H    H N N 376 
TRP   H2   H N N 377 
TRP   HA   H N N 378 
TRP   HB2  H N N 379 
TRP   HB3  H N N 380 
TRP   HD1  H N N 381 
TRP   HE1  H N N 382 
TRP   HE3  H N N 383 
TRP   HZ2  H N N 384 
TRP   HZ3  H N N 385 
TRP   HH2  H N N 386 
TRP   HXT  H N N 387 
TYR   N    N N N 388 
TYR   CA   C N S 389 
TYR   C    C N N 390 
TYR   O    O N N 391 
TYR   CB   C N N 392 
TYR   CG   C Y N 393 
TYR   CD1  C Y N 394 
TYR   CD2  C Y N 395 
TYR   CE1  C Y N 396 
TYR   CE2  C Y N 397 
TYR   CZ   C Y N 398 
TYR   OH   O N N 399 
TYR   OXT  O N N 400 
TYR   H    H N N 401 
TYR   H2   H N N 402 
TYR   HA   H N N 403 
TYR   HB2  H N N 404 
TYR   HB3  H N N 405 
TYR   HD1  H N N 406 
TYR   HD2  H N N 407 
TYR   HE1  H N N 408 
TYR   HE2  H N N 409 
TYR   HH   H N N 410 
TYR   HXT  H N N 411 
VAL   N    N N N 412 
VAL   CA   C N S 413 
VAL   C    C N N 414 
VAL   O    O N N 415 
VAL   CB   C N N 416 
VAL   CG1  C N N 417 
VAL   CG2  C N N 418 
VAL   OXT  O N N 419 
VAL   H    H N N 420 
VAL   H2   H N N 421 
VAL   HA   H N N 422 
VAL   HB   H N N 423 
VAL   HG11 H N N 424 
VAL   HG12 H N N 425 
VAL   HG13 H N N 426 
VAL   HG21 H N N 427 
VAL   HG22 H N N 428 
VAL   HG23 H N N 429 
VAL   HXT  H N N 430 
# 
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 
A1A3W C   C1   sing N N 1   
A1A3W C1  C2   sing N N 2   
A1A3W C2  N    sing N N 3   
A1A3W N   C3   sing N N 4   
A1A3W C4  C2   sing N N 5   
A1A3W C4  C5   sing Y N 6   
A1A3W C5  C6   doub Y N 7   
A1A3W C6  N1   sing Y N 8   
A1A3W N1  C7   doub Y N 9   
A1A3W C7  C8   sing Y N 10  
A1A3W C8  C4   doub Y N 11  
A1A3W C5  H10  sing N N 12  
A1A3W C6  H11  sing N N 13  
A1A3W C7  H12  sing N N 14  
A1A3W C8  H13  sing N N 15  
A1A3W C3  H7   sing N N 16  
A1A3W C3  H9   sing N N 17  
A1A3W C3  H8   sing N N 18  
A1A3W N   H6   sing N N 19  
A1A3W C2  H5   sing N N 20  
A1A3W C1  H4   sing N N 21  
A1A3W C1  H3   sing N N 22  
A1A3W C   H2   sing N N 23  
A1A3W C   H1   sing N N 24  
A1A3W C   H    sing N N 25  
ALA   N   CA   sing N N 26  
ALA   N   H    sing N N 27  
ALA   N   H2   sing N N 28  
ALA   CA  C    sing N N 29  
ALA   CA  CB   sing N N 30  
ALA   CA  HA   sing N N 31  
ALA   C   O    doub N N 32  
ALA   C   OXT  sing N N 33  
ALA   CB  HB1  sing N N 34  
ALA   CB  HB2  sing N N 35  
ALA   CB  HB3  sing N N 36  
ALA   OXT HXT  sing N N 37  
ARG   N   CA   sing N N 38  
ARG   N   H    sing N N 39  
ARG   N   H2   sing N N 40  
ARG   CA  C    sing N N 41  
ARG   CA  CB   sing N N 42  
ARG   CA  HA   sing N N 43  
ARG   C   O    doub N N 44  
ARG   C   OXT  sing N N 45  
ARG   CB  CG   sing N N 46  
ARG   CB  HB2  sing N N 47  
ARG   CB  HB3  sing N N 48  
ARG   CG  CD   sing N N 49  
ARG   CG  HG2  sing N N 50  
ARG   CG  HG3  sing N N 51  
ARG   CD  NE   sing N N 52  
ARG   CD  HD2  sing N N 53  
ARG   CD  HD3  sing N N 54  
ARG   NE  CZ   sing N N 55  
ARG   NE  HE   sing N N 56  
ARG   CZ  NH1  sing N N 57  
ARG   CZ  NH2  doub N N 58  
ARG   NH1 HH11 sing N N 59  
ARG   NH1 HH12 sing N N 60  
ARG   NH2 HH21 sing N N 61  
ARG   NH2 HH22 sing N N 62  
ARG   OXT HXT  sing N N 63  
ASN   N   CA   sing N N 64  
ASN   N   H    sing N N 65  
ASN   N   H2   sing N N 66  
ASN   CA  C    sing N N 67  
ASN   CA  CB   sing N N 68  
ASN   CA  HA   sing N N 69  
ASN   C   O    doub N N 70  
ASN   C   OXT  sing N N 71  
ASN   CB  CG   sing N N 72  
ASN   CB  HB2  sing N N 73  
ASN   CB  HB3  sing N N 74  
ASN   CG  OD1  doub N N 75  
ASN   CG  ND2  sing N N 76  
ASN   ND2 HD21 sing N N 77  
ASN   ND2 HD22 sing N N 78  
ASN   OXT HXT  sing N N 79  
ASP   N   CA   sing N N 80  
ASP   N   H    sing N N 81  
ASP   N   H2   sing N N 82  
ASP   CA  C    sing N N 83  
ASP   CA  CB   sing N N 84  
ASP   CA  HA   sing N N 85  
ASP   C   O    doub N N 86  
ASP   C   OXT  sing N N 87  
ASP   CB  CG   sing N N 88  
ASP   CB  HB2  sing N N 89  
ASP   CB  HB3  sing N N 90  
ASP   CG  OD1  doub N N 91  
ASP   CG  OD2  sing N N 92  
ASP   OD2 HD2  sing N N 93  
ASP   OXT HXT  sing N N 94  
CYS   N   CA   sing N N 95  
CYS   N   H    sing N N 96  
CYS   N   H2   sing N N 97  
CYS   CA  C    sing N N 98  
CYS   CA  CB   sing N N 99  
CYS   CA  HA   sing N N 100 
CYS   C   O    doub N N 101 
CYS   C   OXT  sing N N 102 
CYS   CB  SG   sing N N 103 
CYS   CB  HB2  sing N N 104 
CYS   CB  HB3  sing N N 105 
CYS   SG  HG   sing N N 106 
CYS   OXT HXT  sing N N 107 
EDO   C1  O1   sing N N 108 
EDO   C1  C2   sing N N 109 
EDO   C1  H11  sing N N 110 
EDO   C1  H12  sing N N 111 
EDO   O1  HO1  sing N N 112 
EDO   C2  O2   sing N N 113 
EDO   C2  H21  sing N N 114 
EDO   C2  H22  sing N N 115 
EDO   O2  HO2  sing N N 116 
GLN   N   CA   sing N N 117 
GLN   N   H    sing N N 118 
GLN   N   H2   sing N N 119 
GLN   CA  C    sing N N 120 
GLN   CA  CB   sing N N 121 
GLN   CA  HA   sing N N 122 
GLN   C   O    doub N N 123 
GLN   C   OXT  sing N N 124 
GLN   CB  CG   sing N N 125 
GLN   CB  HB2  sing N N 126 
GLN   CB  HB3  sing N N 127 
GLN   CG  CD   sing N N 128 
GLN   CG  HG2  sing N N 129 
GLN   CG  HG3  sing N N 130 
GLN   CD  OE1  doub N N 131 
GLN   CD  NE2  sing N N 132 
GLN   NE2 HE21 sing N N 133 
GLN   NE2 HE22 sing N N 134 
GLN   OXT HXT  sing N N 135 
GLU   N   CA   sing N N 136 
GLU   N   H    sing N N 137 
GLU   N   H2   sing N N 138 
GLU   CA  C    sing N N 139 
GLU   CA  CB   sing N N 140 
GLU   CA  HA   sing N N 141 
GLU   C   O    doub N N 142 
GLU   C   OXT  sing N N 143 
GLU   CB  CG   sing N N 144 
GLU   CB  HB2  sing N N 145 
GLU   CB  HB3  sing N N 146 
GLU   CG  CD   sing N N 147 
GLU   CG  HG2  sing N N 148 
GLU   CG  HG3  sing N N 149 
GLU   CD  OE1  doub N N 150 
GLU   CD  OE2  sing N N 151 
GLU   OE2 HE2  sing N N 152 
GLU   OXT HXT  sing N N 153 
GLY   N   CA   sing N N 154 
GLY   N   H    sing N N 155 
GLY   N   H2   sing N N 156 
GLY   CA  C    sing N N 157 
GLY   CA  HA2  sing N N 158 
GLY   CA  HA3  sing N N 159 
GLY   C   O    doub N N 160 
GLY   C   OXT  sing N N 161 
GLY   OXT HXT  sing N N 162 
HIS   N   CA   sing N N 163 
HIS   N   H    sing N N 164 
HIS   N   H2   sing N N 165 
HIS   CA  C    sing N N 166 
HIS   CA  CB   sing N N 167 
HIS   CA  HA   sing N N 168 
HIS   C   O    doub N N 169 
HIS   C   OXT  sing N N 170 
HIS   CB  CG   sing N N 171 
HIS   CB  HB2  sing N N 172 
HIS   CB  HB3  sing N N 173 
HIS   CG  ND1  sing Y N 174 
HIS   CG  CD2  doub Y N 175 
HIS   ND1 CE1  doub Y N 176 
HIS   ND1 HD1  sing N N 177 
HIS   CD2 NE2  sing Y N 178 
HIS   CD2 HD2  sing N N 179 
HIS   CE1 NE2  sing Y N 180 
HIS   CE1 HE1  sing N N 181 
HIS   NE2 HE2  sing N N 182 
HIS   OXT HXT  sing N N 183 
HOH   O   H1   sing N N 184 
HOH   O   H2   sing N N 185 
ILE   N   CA   sing N N 186 
ILE   N   H    sing N N 187 
ILE   N   H2   sing N N 188 
ILE   CA  C    sing N N 189 
ILE   CA  CB   sing N N 190 
ILE   CA  HA   sing N N 191 
ILE   C   O    doub N N 192 
ILE   C   OXT  sing N N 193 
ILE   CB  CG1  sing N N 194 
ILE   CB  CG2  sing N N 195 
ILE   CB  HB   sing N N 196 
ILE   CG1 CD1  sing N N 197 
ILE   CG1 HG12 sing N N 198 
ILE   CG1 HG13 sing N N 199 
ILE   CG2 HG21 sing N N 200 
ILE   CG2 HG22 sing N N 201 
ILE   CG2 HG23 sing N N 202 
ILE   CD1 HD11 sing N N 203 
ILE   CD1 HD12 sing N N 204 
ILE   CD1 HD13 sing N N 205 
ILE   OXT HXT  sing N N 206 
LEU   N   CA   sing N N 207 
LEU   N   H    sing N N 208 
LEU   N   H2   sing N N 209 
LEU   CA  C    sing N N 210 
LEU   CA  CB   sing N N 211 
LEU   CA  HA   sing N N 212 
LEU   C   O    doub N N 213 
LEU   C   OXT  sing N N 214 
LEU   CB  CG   sing N N 215 
LEU   CB  HB2  sing N N 216 
LEU   CB  HB3  sing N N 217 
LEU   CG  CD1  sing N N 218 
LEU   CG  CD2  sing N N 219 
LEU   CG  HG   sing N N 220 
LEU   CD1 HD11 sing N N 221 
LEU   CD1 HD12 sing N N 222 
LEU   CD1 HD13 sing N N 223 
LEU   CD2 HD21 sing N N 224 
LEU   CD2 HD22 sing N N 225 
LEU   CD2 HD23 sing N N 226 
LEU   OXT HXT  sing N N 227 
LYS   N   CA   sing N N 228 
LYS   N   H    sing N N 229 
LYS   N   H2   sing N N 230 
LYS   CA  C    sing N N 231 
LYS   CA  CB   sing N N 232 
LYS   CA  HA   sing N N 233 
LYS   C   O    doub N N 234 
LYS   C   OXT  sing N N 235 
LYS   CB  CG   sing N N 236 
LYS   CB  HB2  sing N N 237 
LYS   CB  HB3  sing N N 238 
LYS   CG  CD   sing N N 239 
LYS   CG  HG2  sing N N 240 
LYS   CG  HG3  sing N N 241 
LYS   CD  CE   sing N N 242 
LYS   CD  HD2  sing N N 243 
LYS   CD  HD3  sing N N 244 
LYS   CE  NZ   sing N N 245 
LYS   CE  HE2  sing N N 246 
LYS   CE  HE3  sing N N 247 
LYS   NZ  HZ1  sing N N 248 
LYS   NZ  HZ2  sing N N 249 
LYS   NZ  HZ3  sing N N 250 
LYS   OXT HXT  sing N N 251 
MET   N   CA   sing N N 252 
MET   N   H    sing N N 253 
MET   N   H2   sing N N 254 
MET   CA  C    sing N N 255 
MET   CA  CB   sing N N 256 
MET   CA  HA   sing N N 257 
MET   C   O    doub N N 258 
MET   C   OXT  sing N N 259 
MET   CB  CG   sing N N 260 
MET   CB  HB2  sing N N 261 
MET   CB  HB3  sing N N 262 
MET   CG  SD   sing N N 263 
MET   CG  HG2  sing N N 264 
MET   CG  HG3  sing N N 265 
MET   SD  CE   sing N N 266 
MET   CE  HE1  sing N N 267 
MET   CE  HE2  sing N N 268 
MET   CE  HE3  sing N N 269 
MET   OXT HXT  sing N N 270 
PHE   N   CA   sing N N 271 
PHE   N   H    sing N N 272 
PHE   N   H2   sing N N 273 
PHE   CA  C    sing N N 274 
PHE   CA  CB   sing N N 275 
PHE   CA  HA   sing N N 276 
PHE   C   O    doub N N 277 
PHE   C   OXT  sing N N 278 
PHE   CB  CG   sing N N 279 
PHE   CB  HB2  sing N N 280 
PHE   CB  HB3  sing N N 281 
PHE   CG  CD1  doub Y N 282 
PHE   CG  CD2  sing Y N 283 
PHE   CD1 CE1  sing Y N 284 
PHE   CD1 HD1  sing N N 285 
PHE   CD2 CE2  doub Y N 286 
PHE   CD2 HD2  sing N N 287 
PHE   CE1 CZ   doub Y N 288 
PHE   CE1 HE1  sing N N 289 
PHE   CE2 CZ   sing Y N 290 
PHE   CE2 HE2  sing N N 291 
PHE   CZ  HZ   sing N N 292 
PHE   OXT HXT  sing N N 293 
PRO   N   CA   sing N N 294 
PRO   N   CD   sing N N 295 
PRO   N   H    sing N N 296 
PRO   CA  C    sing N N 297 
PRO   CA  CB   sing N N 298 
PRO   CA  HA   sing N N 299 
PRO   C   O    doub N N 300 
PRO   C   OXT  sing N N 301 
PRO   CB  CG   sing N N 302 
PRO   CB  HB2  sing N N 303 
PRO   CB  HB3  sing N N 304 
PRO   CG  CD   sing N N 305 
PRO   CG  HG2  sing N N 306 
PRO   CG  HG3  sing N N 307 
PRO   CD  HD2  sing N N 308 
PRO   CD  HD3  sing N N 309 
PRO   OXT HXT  sing N N 310 
SER   N   CA   sing N N 311 
SER   N   H    sing N N 312 
SER   N   H2   sing N N 313 
SER   CA  C    sing N N 314 
SER   CA  CB   sing N N 315 
SER   CA  HA   sing N N 316 
SER   C   O    doub N N 317 
SER   C   OXT  sing N N 318 
SER   CB  OG   sing N N 319 
SER   CB  HB2  sing N N 320 
SER   CB  HB3  sing N N 321 
SER   OG  HG   sing N N 322 
SER   OXT HXT  sing N N 323 
SO4   S   O1   doub N N 324 
SO4   S   O2   doub N N 325 
SO4   S   O3   sing N N 326 
SO4   S   O4   sing N N 327 
THR   N   CA   sing N N 328 
THR   N   H    sing N N 329 
THR   N   H2   sing N N 330 
THR   CA  C    sing N N 331 
THR   CA  CB   sing N N 332 
THR   CA  HA   sing N N 333 
THR   C   O    doub N N 334 
THR   C   OXT  sing N N 335 
THR   CB  OG1  sing N N 336 
THR   CB  CG2  sing N N 337 
THR   CB  HB   sing N N 338 
THR   OG1 HG1  sing N N 339 
THR   CG2 HG21 sing N N 340 
THR   CG2 HG22 sing N N 341 
THR   CG2 HG23 sing N N 342 
THR   OXT HXT  sing N N 343 
TRP   N   CA   sing N N 344 
TRP   N   H    sing N N 345 
TRP   N   H2   sing N N 346 
TRP   CA  C    sing N N 347 
TRP   CA  CB   sing N N 348 
TRP   CA  HA   sing N N 349 
TRP   C   O    doub N N 350 
TRP   C   OXT  sing N N 351 
TRP   CB  CG   sing N N 352 
TRP   CB  HB2  sing N N 353 
TRP   CB  HB3  sing N N 354 
TRP   CG  CD1  doub Y N 355 
TRP   CG  CD2  sing Y N 356 
TRP   CD1 NE1  sing Y N 357 
TRP   CD1 HD1  sing N N 358 
TRP   CD2 CE2  doub Y N 359 
TRP   CD2 CE3  sing Y N 360 
TRP   NE1 CE2  sing Y N 361 
TRP   NE1 HE1  sing N N 362 
TRP   CE2 CZ2  sing Y N 363 
TRP   CE3 CZ3  doub Y N 364 
TRP   CE3 HE3  sing N N 365 
TRP   CZ2 CH2  doub Y N 366 
TRP   CZ2 HZ2  sing N N 367 
TRP   CZ3 CH2  sing Y N 368 
TRP   CZ3 HZ3  sing N N 369 
TRP   CH2 HH2  sing N N 370 
TRP   OXT HXT  sing N N 371 
TYR   N   CA   sing N N 372 
TYR   N   H    sing N N 373 
TYR   N   H2   sing N N 374 
TYR   CA  C    sing N N 375 
TYR   CA  CB   sing N N 376 
TYR   CA  HA   sing N N 377 
TYR   C   O    doub N N 378 
TYR   C   OXT  sing N N 379 
TYR   CB  CG   sing N N 380 
TYR   CB  HB2  sing N N 381 
TYR   CB  HB3  sing N N 382 
TYR   CG  CD1  doub Y N 383 
TYR   CG  CD2  sing Y N 384 
TYR   CD1 CE1  sing Y N 385 
TYR   CD1 HD1  sing N N 386 
TYR   CD2 CE2  doub Y N 387 
TYR   CD2 HD2  sing N N 388 
TYR   CE1 CZ   doub Y N 389 
TYR   CE1 HE1  sing N N 390 
TYR   CE2 CZ   sing Y N 391 
TYR   CE2 HE2  sing N N 392 
TYR   CZ  OH   sing N N 393 
TYR   OH  HH   sing N N 394 
TYR   OXT HXT  sing N N 395 
VAL   N   CA   sing N N 396 
VAL   N   H    sing N N 397 
VAL   N   H2   sing N N 398 
VAL   CA  C    sing N N 399 
VAL   CA  CB   sing N N 400 
VAL   CA  HA   sing N N 401 
VAL   C   O    doub N N 402 
VAL   C   OXT  sing N N 403 
VAL   CB  CG1  sing N N 404 
VAL   CB  CG2  sing N N 405 
VAL   CB  HB   sing N N 406 
VAL   CG1 HG11 sing N N 407 
VAL   CG1 HG12 sing N N 408 
VAL   CG1 HG13 sing N N 409 
VAL   CG2 HG21 sing N N 410 
VAL   CG2 HG22 sing N N 411 
VAL   CG2 HG23 sing N N 412 
VAL   OXT HXT  sing N N 413 
# 
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                    7HH9 
_atom_sites.fract_transf_matrix[1][1]   0.023935 
_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]   0.023764 
_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]   0.006283 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET   A 1 2  ? 0.549   4.320   2.346   1.00 51.87  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? -0.556  3.572   1.687   1.00 59.99  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? 0.010   2.560   0.693   1.00 50.80  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 1.053   2.790   0.097   1.00 51.27  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -1.561  4.518   1.021   1.00 63.32  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -2.487  5.218   2.009   1.00 73.37  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -3.766  4.215   2.803   1.00 66.74  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -4.737  5.450   3.682   1.00 69.12  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? -0.631  1.371   0.560   1.00 45.70  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? -0.158  0.283   -0.313  1.00 42.32  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? 0.071   0.613   -1.791  1.00 39.25  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? -0.684  1.369   -2.407  1.00 39.63  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -1.324  -0.754  -0.161  1.00 42.30  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -1.809  -0.517  1.256   1.00 45.04  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -1.839  1.001   1.321   1.00 44.10  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 1.080   -0.044  -2.376  1.00 36.99  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 1.312   0.041   -3.798  1.00 38.90  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 0.720   -1.232  -4.394  1.00 36.62  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? 0.229   -2.090  -3.651  1.00 34.45  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 2.829   0.152   -4.031  1.00 41.86  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 3.410   1.480   -3.643  1.00 53.57  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 2.807   2.366   -2.773  1.00 61.54  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 4.530   2.090   -4.058  1.00 61.01  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 3.547   3.458   -2.657  1.00 59.47  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 4.605   3.309   -3.424  1.00 54.52  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 0.808   -1.395  -5.722  1.00 28.82  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? 0.551   -2.709  -6.277  1.00 27.20  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 1.680   -3.661  -5.889  1.00 28.72  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 2.778   -3.226  -5.495  1.00 30.60  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? 0.387   -2.613  -7.785  1.00 32.89  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 1.395   -4.953  -6.014  1.00 26.89  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 2.424   -5.958  -5.819  1.00 27.42  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 3.550   -5.745  -6.832  1.00 27.20  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 3.317   -5.362  -7.983  1.00 29.89  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 1.896   -7.388  -5.952  1.00 28.07  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 1.106   -7.724  -4.693  1.00 30.60  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 1.763   -7.949  -3.492  1.00 26.36  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? -0.281  -7.876  -4.725  1.00 25.69  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 1.084   -8.290  -2.330  1.00 24.86  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -0.955  -8.259  -3.567  1.00 24.70  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? -0.299  -8.446  -2.373  1.00 24.71  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 4.787   -6.004  -6.373  1.00 25.34  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 5.924   -5.961  -7.282  1.00 24.92  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 6.825   -7.156  -6.987  1.00 23.41  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 6.823   -7.697  -5.880  1.00 23.49  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 6.714   -4.665  -7.018  1.00 29.57  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 7.280   -4.543  -5.620  1.00 30.32  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 7.959   -3.190  -5.335  1.00 34.91  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 8.615   -3.214  -3.971  1.00 31.20  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 7.700   -3.203  -2.828  1.00 33.49  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 7.734   -7.533  -7.902  1.00 25.48  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 8.669   -8.629  -7.645  1.00 24.39  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 9.478   -8.365  -6.374  1.00 22.16  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 9.997   -7.273  -6.123  1.00 24.73  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 9.580   -8.673  -8.904  1.00 26.31  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 8.669   -8.067  -9.962  1.00 28.79  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 7.887   -6.946  -9.255  1.00 27.53  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 9.652   -9.438  -5.614  1.00 21.43  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 10.409  -9.392  -4.372  1.00 22.20  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 9.498   -9.215  -3.160  1.00 23.70  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 9.882   -9.446  -2.007  1.00 23.75  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 8.243   -8.771  -3.393  1.00 20.72  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 7.347   -8.760  -2.237  1.00 20.79  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 7.091   -10.151 -1.624  1.00 18.49  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 6.906   -11.121 -2.323  1.00 20.17  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 5.987   -8.160  -2.623  1.00 21.24  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 5.976   -6.660  -2.862  1.00 25.27  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 6.920   -5.949  -2.419  1.00 24.64  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 4.991   -6.170  -3.448  1.00 24.74  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 6.951   -10.184 -0.286  1.00 20.11  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 6.788   -11.419 0.467   1.00 19.54  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 5.305   -11.519 0.869   1.00 18.50  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 4.721   -10.508 1.327   1.00 21.92  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 7.756   -11.506 1.664   1.00 20.60  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 9.230   -11.187 1.360   1.00 23.06  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 10.032  -11.344 2.667   1.00 21.77  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 9.629   -12.176 0.311   1.00 21.88  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 4.742   -12.726 0.710   1.00 19.19  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 3.303   -12.895 0.948   1.00 20.21  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 3.064   -14.251 1.611   1.00 21.64  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 3.925   -15.129 1.651   1.00 20.76  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 2.494   -12.826 -0.374  1.00 18.31  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 2.697   -11.446 -1.001  1.00 22.24  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 2.930   -13.935 -1.325  1.00 21.13  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 1.833   -14.456 2.118   1.00 20.89  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 1.274   -15.791 2.141   1.00 23.06  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? 0.319   -15.876 0.954   1.00 22.52  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? -0.499  -14.944 0.760   1.00 22.30  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? 0.512   -16.145 3.444   1.00 21.96  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 1.439   -16.173 4.652   1.00 22.19  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 1.737   -15.004 5.321   1.00 23.10  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 1.976   -17.390 5.090   1.00 25.71  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 2.630   -15.030 6.394   1.00 27.18  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 2.888   -17.419 6.152   1.00 26.70  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 3.204   -16.244 6.789   1.00 29.57  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? 0.435   -16.972 0.174   1.00 22.10  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? -0.365  -17.128 -1.034  1.00 22.68  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -1.354  -18.284 -0.829  1.00 24.10  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -0.999  -19.315 -0.261  1.00 24.62  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? 0.519   -17.344 -2.260  1.00 21.59  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -2.624  -18.095 -1.260  1.00 21.93  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -3.617  -19.123 -0.987  1.00 24.73  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -3.945  -19.881 -2.275  1.00 27.33  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -4.299  -19.264 -3.268  1.00 26.85  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -4.872  -18.422 -0.427  1.00 26.09  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -5.965  -19.500 -0.067  1.00 28.92  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -5.542  -20.287 1.186   1.00 33.39  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -6.638  -21.148 1.782   1.00 35.35  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -6.941  -22.294 0.917   1.00 34.56  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -3.853  -21.219 -2.213  1.00 25.89  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -4.289  -22.144 -3.249  1.00 29.98  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -5.389  -22.992 -2.613  1.00 29.40  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -5.280  -23.330 -1.445  1.00 27.87  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -3.108  -23.079 -3.542  1.00 30.13  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -1.878  -22.334 -4.035  1.00 30.70  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -2.093  -21.686 -5.706  1.00 34.37  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -1.552  -23.169 -6.523  1.00 30.92  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -6.419  -23.322 -3.408  1.00 38.42  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -7.432  -24.313 -3.049  1.00 41.73  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -6.795  -25.553 -2.425  1.00 36.11  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -5.839  -26.123 -2.943  1.00 34.11  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -8.156  -24.717 -4.334  1.00 41.34  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -9.366  -25.629 -4.126  1.00 40.51  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -10.542 -25.019 -4.884  1.00 54.54  ? 16  LYS   A CD  1 
ATOM   125  N N   . GLY   A 1 18 ? -7.295  -25.961 -1.254  1.00 35.60  ? 17  GLY   A N   1 
ATOM   126  C CA  . GLY   A 1 18 ? -6.843  -27.210 -0.672  1.00 34.80  ? 17  GLY   A CA  1 
ATOM   127  C C   . GLY   A 1 18 ? -5.526  -27.099 0.085   1.00 39.12  ? 17  GLY   A C   1 
ATOM   128  O O   . GLY   A 1 18 ? -5.041  -28.078 0.651   1.00 38.63  ? 17  GLY   A O   1 
ATOM   129  N N   . TYR   A 1 19 ? -4.936  -25.902 0.094   1.00 34.01  ? 18  TYR   A N   1 
ATOM   130  C CA  . TYR   A 1 19 ? -3.742  -25.727 0.890   1.00 34.74  ? 18  TYR   A CA  1 
ATOM   131  C C   . TYR   A 1 19 ? -3.874  -24.548 1.836   1.00 30.82  ? 18  TYR   A C   1 
ATOM   132  O O   . TYR   A 1 19 ? -4.598  -23.587 1.543   1.00 30.43  ? 18  TYR   A O   1 
ATOM   133  C CB  . TYR   A 1 19 ? -2.584  -25.323 -0.009  1.00 34.34  ? 18  TYR   A CB  1 
ATOM   134  C CG  . TYR   A 1 19 ? -2.078  -26.417 -0.929  1.00 37.88  ? 18  TYR   A CG  1 
ATOM   135  C CD1 . TYR   A 1 19 ? -1.017  -27.226 -0.548  1.00 45.87  ? 18  TYR   A CD1 1 
ATOM   136  C CD2 . TYR   A 1 19 ? -2.639  -26.585 -2.186  1.00 40.61  ? 18  TYR   A CD2 1 
ATOM   137  C CE1 . TYR   A 1 19 ? -0.522  -28.188 -1.409  1.00 53.65  ? 18  TYR   A CE1 1 
ATOM   138  C CE2 . TYR   A 1 19 ? -2.156  -27.545 -3.058  1.00 50.59  ? 18  TYR   A CE2 1 
ATOM   139  C CZ  . TYR   A 1 19 ? -1.096  -28.346 -2.662  1.00 57.58  ? 18  TYR   A CZ  1 
ATOM   140  O OH  . TYR   A 1 19 ? -0.612  -29.302 -3.513  1.00 66.27  ? 18  TYR   A OH  1 
ATOM   141  N N   . PRO   A 1 20 ? -3.127  -24.573 2.967   1.00 31.47  ? 19  PRO   A N   1 
ATOM   142  C CA  . PRO   A 1 20 ? -3.108  -23.469 3.926   1.00 31.05  ? 19  PRO   A CA  1 
ATOM   143  C C   . PRO   A 1 20 ? -2.406  -22.280 3.249   1.00 28.80  ? 19  PRO   A C   1 
ATOM   144  O O   . PRO   A 1 20 ? -1.654  -22.490 2.308   1.00 29.00  ? 19  PRO   A O   1 
ATOM   145  C CB  . PRO   A 1 20 ? -2.323  -24.030 5.122   1.00 34.35  ? 19  PRO   A CB  1 
ATOM   146  C CG  . PRO   A 1 20 ? -1.407  -25.068 4.500   1.00 33.05  ? 19  PRO   A CG  1 
ATOM   147  C CD  . PRO   A 1 20 ? -2.184  -25.654 3.344   1.00 33.22  ? 19  PRO   A CD  1 
ATOM   148  N N   . HIS   A 1 21 ? -2.711  -21.083 3.713   1.00 27.68  ? 20  HIS   A N   1 
ATOM   149  C CA  . HIS   A 1 21 ? -1.978  -19.888 3.269   1.00 24.08  ? 20  HIS   A CA  1 
ATOM   150  C C   . HIS   A 1 21 ? -0.486  -20.195 3.374   1.00 29.06  ? 20  HIS   A C   1 
ATOM   151  O O   . HIS   A 1 21 ? -0.036  -20.599 4.449   1.00 26.67  ? 20  HIS   A O   1 
ATOM   152  C CB  . HIS   A 1 21 ? -2.419  -18.696 4.113   1.00 25.40  ? 20  HIS   A CB  1 
ATOM   153  C CG  . HIS   A 1 21 ? -3.880  -18.325 3.936   1.00 25.67  ? 20  HIS   A CG  1 
ATOM   154  N ND1 . HIS   A 1 21 ? -4.938  -18.953 4.593   1.00 30.37  ? 20  HIS   A ND1 1 
ATOM   155  C CD2 . HIS   A 1 21 ? -4.417  -17.347 3.166   1.00 26.35  ? 20  HIS   A CD2 1 
ATOM   156  C CE1 . HIS   A 1 21 ? -6.075  -18.361 4.228   1.00 30.09  ? 20  HIS   A CE1 1 
ATOM   157  N NE2 . HIS   A 1 21 ? -5.808  -17.385 3.358   1.00 30.03  ? 20  HIS   A NE2 1 
ATOM   158  N N   . TRP   A 1 22 ? 0.264   -19.965 2.274   1.00 25.64  ? 21  TRP   A N   1 
ATOM   159  C CA  . TRP   A 1 22 ? 1.582   -20.588 2.127   1.00 23.16  ? 21  TRP   A CA  1 
ATOM   160  C C   . TRP   A 1 22 ? 2.645   -19.484 2.007   1.00 22.90  ? 21  TRP   A C   1 
ATOM   161  O O   . TRP   A 1 22 ? 2.497   -18.579 1.191   1.00 23.29  ? 21  TRP   A O   1 
ATOM   162  C CB  . TRP   A 1 22 ? 1.617   -21.483 0.892   1.00 24.52  ? 21  TRP   A CB  1 
ATOM   163  C CG  . TRP   A 1 22 ? 2.703   -22.523 0.971   1.00 24.43  ? 21  TRP   A CG  1 
ATOM   164  C CD1 . TRP   A 1 22 ? 4.045   -22.310 0.791   1.00 25.12  ? 21  TRP   A CD1 1 
ATOM   165  C CD2 . TRP   A 1 22 ? 2.527   -23.895 1.359   1.00 26.33  ? 21  TRP   A CD2 1 
ATOM   166  N NE1 . TRP   A 1 22 ? 4.698   -23.509 0.900   1.00 24.45  ? 21  TRP   A NE1 1 
ATOM   167  C CE2 . TRP   A 1 22 ? 3.806   -24.491 1.300   1.00 28.16  ? 21  TRP   A CE2 1 
ATOM   168  C CE3 . TRP   A 1 22 ? 1.422   -24.681 1.712   1.00 29.30  ? 21  TRP   A CE3 1 
ATOM   169  C CZ2 . TRP   A 1 22 ? 4.020   -25.834 1.612   1.00 30.86  ? 21  TRP   A CZ2 1 
ATOM   170  C CZ3 . TRP   A 1 22 ? 1.639   -26.016 2.023   1.00 31.77  ? 21  TRP   A CZ3 1 
ATOM   171  C CH2 . TRP   A 1 22 ? 2.921   -26.580 1.989   1.00 34.59  ? 21  TRP   A CH2 1 
ATOM   172  N N   . PRO   A 1 23 ? 3.788   -19.553 2.733   1.00 21.39  ? 22  PRO   A N   1 
ATOM   173  C CA  . PRO   A 1 23 ? 4.824   -18.529 2.554   1.00 21.25  ? 22  PRO   A CA  1 
ATOM   174  C C   . PRO   A 1 23 ? 5.345   -18.514 1.109   1.00 20.70  ? 22  PRO   A C   1 
ATOM   175  O O   . PRO   A 1 23 ? 5.707   -19.558 0.528   1.00 22.46  ? 22  PRO   A O   1 
ATOM   176  C CB  . PRO   A 1 23 ? 5.915   -18.952 3.560   1.00 21.28  ? 22  PRO   A CB  1 
ATOM   177  C CG  . PRO   A 1 23 ? 5.710   -20.447 3.716   1.00 20.45  ? 22  PRO   A CG  1 
ATOM   178  C CD  . PRO   A 1 23 ? 4.160   -20.625 3.661   1.00 20.96  ? 22  PRO   A CD  1 
ATOM   179  N N   . ALA   A 1 24 ? 5.408   -17.319 0.520   1.00 19.25  ? 23  ALA   A N   1 
ATOM   180  C CA  . ALA   A 1 24 ? 5.721   -17.199 -0.891  1.00 19.95  ? 23  ALA   A CA  1 
ATOM   181  C C   . ALA   A 1 24 ? 6.294   -15.802 -1.205  1.00 19.62  ? 23  ALA   A C   1 
ATOM   182  O O   . ALA   A 1 24 ? 6.311   -14.896 -0.372  1.00 20.40  ? 23  ALA   A O   1 
ATOM   183  C CB  . ALA   A 1 24 ? 4.408   -17.491 -1.699  1.00 22.18  ? 23  ALA   A CB  1 
ATOM   184  N N   . ARG   A 1 25 ? 6.791   -15.643 -2.444  1.00 20.27  ? 24  ARG   A N   1 
ATOM   185  C CA  . ARG   A 1 25 ? 7.183   -14.337 -2.925  1.00 19.35  ? 24  ARG   A CA  1 
ATOM   186  C C   . ARG   A 1 25 ? 6.649   -14.090 -4.322  1.00 18.38  ? 24  ARG   A C   1 
ATOM   187  O O   . ARG   A 1 25 ? 6.344   -15.053 -5.031  1.00 21.06  ? 24  ARG   A O   1 
ATOM   188  C CB  . ARG   A 1 25 ? 8.703   -14.169 -2.878  1.00 20.35  ? 24  ARG   A CB  1 
ATOM   189  C CG  . ARG   A 1 25 ? 9.421   -15.106 -3.834  1.00 20.72  ? 24  ARG   A CG  1 
ATOM   190  C CD  . ARG   A 1 25 ? 10.968  -14.876 -3.747  1.00 21.28  ? 24  ARG   A CD  1 
ATOM   191  N NE  . ARG   A 1 25 ? 11.627  -15.717 -4.791  1.00 23.57  ? 24  ARG   A NE  1 
ATOM   192  C CZ  . ARG   A 1 25 ? 12.900  -16.148 -4.683  1.00 24.20  ? 24  ARG   A CZ  1 
ATOM   193  N NH1 . ARG   A 1 25 ? 13.575  -15.937 -3.569  1.00 23.65  ? 24  ARG   A NH1 1 
ATOM   194  N NH2 . ARG   A 1 25 ? 13.475  -16.754 -5.711  1.00 27.92  ? 24  ARG   A NH2 1 
ATOM   195  N N   . ILE   A 1 26 ? 6.526   -12.811 -4.669  1.00 20.57  ? 25  ILE   A N   1 
ATOM   196  C CA  . ILE   A 1 26 ? 6.318   -12.429 -6.061  1.00 20.31  ? 25  ILE   A CA  1 
ATOM   197  C C   . ILE   A 1 26 ? 7.654   -12.561 -6.769  1.00 22.95  ? 25  ILE   A C   1 
ATOM   198  O O   . ILE   A 1 26 ? 8.621   -11.897 -6.400  1.00 22.20  ? 25  ILE   A O   1 
ATOM   199  C CB  . ILE   A 1 26 ? 5.815   -10.978 -6.165  1.00 22.72  ? 25  ILE   A CB  1 
ATOM   200  C CG1 . ILE   A 1 26 ? 4.600   -10.649 -5.224  1.00 28.47  ? 25  ILE   A CG1 1 
ATOM   201  C CG2 . ILE   A 1 26 ? 5.525   -10.634 -7.635  1.00 23.47  ? 25  ILE   A CG2 1 
ATOM   202  C CD1 . ILE   A 1 26 ? 3.300   -11.309 -5.607  1.00 34.99  ? 25  ILE   A CD1 1 
ATOM   203  N N   . ASP   A 1 27 ? 7.674   -13.373 -7.816  1.00 23.58  ? 26  ASP   A N   1 
ATOM   204  C CA  . ASP   A 1 27 ? 8.934   -13.607 -8.545  1.00 24.29  ? 26  ASP   A CA  1 
ATOM   205  C C   . ASP   A 1 27 ? 9.095   -12.614 -9.699  1.00 28.04  ? 26  ASP   A C   1 
ATOM   206  O O   . ASP   A 1 27 ? 8.160   -11.962 -10.128 1.00 27.47  ? 26  ASP   A O   1 
ATOM   207  C CB  . ASP   A 1 27 ? 9.015   -14.999 -9.127  1.00 23.71  ? 26  ASP   A CB  1 
ATOM   208  C CG  . ASP   A 1 27 ? 10.019  -15.923 -8.469  1.00 24.95  ? 26  ASP   A CG  1 
ATOM   209  O OD1 . ASP   A 1 27 ? 10.637  -15.471 -7.480  1.00 29.96  ? 26  ASP   A OD1 1 
ATOM   210  O OD2 . ASP   A 1 27 ? 10.134  -17.059 -8.901  1.00 29.66  ? 26  ASP   A OD2 1 
ATOM   211  N N   . ASP   A 1 28 ? 10.352  -12.435 -10.166 1.00 30.36  ? 27  ASP   A N   1 
ATOM   212  C CA  . ASP   A 1 28 ? 10.552  -11.721 -11.417 1.00 35.65  ? 27  ASP   A CA  1 
ATOM   213  C C   . ASP   A 1 28 ? 10.268  -12.715 -12.535 1.00 34.55  ? 27  ASP   A C   1 
ATOM   214  O O   . ASP   A 1 28 ? 10.126  -13.899 -12.288 1.00 36.23  ? 27  ASP   A O   1 
ATOM   215  C CB  . ASP   A 1 28 ? 12.000  -11.278 -11.575 1.00 39.81  ? 27  ASP   A CB  1 
ATOM   216  C CG  . ASP   A 1 28 ? 12.440  -10.036 -10.802 1.00 48.44  ? 27  ASP   A CG  1 
ATOM   217  O OD1 . ASP   A 1 28 ? 12.117  -8.918  -11.241 1.00 49.28  ? 27  ASP   A OD1 1 
ATOM   218  O OD2 . ASP   A 1 28 ? 13.147  -10.202 -9.783  1.00 56.56  ? 27  ASP   A OD2 1 
ATOM   219  N N   . ILE   A 1 29 ? 10.141  -12.232 -13.764 1.00 38.59  ? 28  ILE   A N   1 
ATOM   220  C CA  . ILE   A 1 29 ? 10.043  -13.155 -14.894 1.00 35.46  ? 28  ILE   A CA  1 
ATOM   221  C C   . ILE   A 1 29 ? 11.367  -13.013 -15.626 1.00 34.56  ? 28  ILE   A C   1 
ATOM   222  O O   . ILE   A 1 29 ? 11.755  -11.877 -15.861 1.00 36.08  ? 28  ILE   A O   1 
ATOM   223  C CB  . ILE   A 1 29 ? 8.920   -12.680 -15.812 1.00 35.74  ? 28  ILE   A CB  1 
ATOM   224  C CG1 . ILE   A 1 29 ? 7.560   -12.684 -15.107 1.00 38.91  ? 28  ILE   A CG1 1 
ATOM   225  C CG2 . ILE   A 1 29 ? 8.908   -13.493 -17.119 1.00 36.97  ? 28  ILE   A CG2 1 
ATOM   226  C CD1 . ILE   A 1 29 ? 6.631   -11.603 -15.623 1.00 38.15  ? 28  ILE   A CD1 1 
ATOM   227  N N   . ALA   A 1 30 ? 12.067  -14.124 -15.866 1.00 35.09  ? 29  ALA   A N   1 
ATOM   228  C CA  . ALA   A 1 30 ? 13.401  -14.054 -16.464 1.00 33.63  ? 29  ALA   A CA  1 
ATOM   229  C C   . ALA   A 1 30 ? 13.235  -13.748 -17.957 1.00 31.97  ? 29  ALA   A C   1 
ATOM   230  O O   . ALA   A 1 30 ? 12.216  -14.103 -18.557 1.00 34.10  ? 29  ALA   A O   1 
ATOM   231  C CB  . ALA   A 1 30 ? 14.150  -15.351 -16.229 1.00 35.55  ? 29  ALA   A CB  1 
ATOM   232  N N   . ASP   A 1 31 ? 14.204  -13.010 -18.503 1.00 32.65  ? 30  ASP   A N   1 
ATOM   233  C CA  . ASP   A 1 31 ? 14.310  -12.927 -19.960 1.00 34.41  ? 30  ASP   A CA  1 
ATOM   234  C C   . ASP   A 1 31 ? 14.058  -14.302 -20.565 1.00 31.91  ? 30  ASP   A C   1 
ATOM   235  O O   . ASP   A 1 31 ? 14.667  -15.283 -20.149 1.00 36.05  ? 30  ASP   A O   1 
ATOM   236  C CB  . ASP   A 1 31 ? 15.688  -12.408 -20.338 1.00 34.37  ? 30  ASP   A CB  1 
ATOM   237  C CG  . ASP   A 1 31 ? 15.873  -10.917 -20.129 1.00 40.35  ? 30  ASP   A CG  1 
ATOM   238  O OD1 . ASP   A 1 31 ? 14.858  -10.234 -19.952 1.00 38.26  ? 30  ASP   A OD1 1 
ATOM   239  O OD2 . ASP   A 1 31 ? 17.041  -10.461 -20.136 1.00 42.50  ? 30  ASP   A OD2 1 
ATOM   240  N N   . GLY   A 1 32 ? 13.148  -14.352 -21.556 1.00 31.37  ? 31  GLY   A N   1 
ATOM   241  C CA  . GLY   A 1 32 ? 12.899  -15.575 -22.310 1.00 32.98  ? 31  GLY   A CA  1 
ATOM   242  C C   . GLY   A 1 32 ? 11.939  -16.554 -21.646 1.00 36.42  ? 31  GLY   A C   1 
ATOM   243  O O   . GLY   A 1 32 ? 11.553  -17.563 -22.246 1.00 38.35  ? 31  GLY   A O   1 
ATOM   244  N N   . ALA   A 1 33 ? 11.576  -16.278 -20.390 1.00 35.00  ? 32  ALA   A N   1 
ATOM   245  C CA  . ALA   A 1 33 ? 10.697  -17.178 -19.651 1.00 38.51  ? 32  ALA   A CA  1 
ATOM   246  C C   . ALA   A 1 33 ? 9.232   -16.896 -19.979 1.00 35.52  ? 32  ALA   A C   1 
ATOM   247  O O   . ALA   A 1 33 ? 8.859   -15.825 -20.440 1.00 35.33  ? 32  ALA   A O   1 
ATOM   248  C CB  . ALA   A 1 33 ? 10.969  -17.003 -18.161 1.00 37.77  ? 32  ALA   A CB  1 
ATOM   249  N N   . VAL   A 1 34 ? 8.353   -17.855 -19.676 1.00 38.23  ? 33  VAL   A N   1 
ATOM   250  C CA  . VAL   A 1 34 ? 6.939   -17.722 -20.005 1.00 37.81  ? 33  VAL   A CA  1 
ATOM   251  C C   . VAL   A 1 34 ? 6.283   -16.692 -19.086 1.00 35.28  ? 33  VAL   A C   1 
ATOM   252  O O   . VAL   A 1 34 ? 6.464   -16.759 -17.885 1.00 38.87  ? 33  VAL   A O   1 
ATOM   253  C CB  . VAL   A 1 34 ? 6.349   -19.124 -19.757 1.00 41.19  ? 33  VAL   A CB  1 
ATOM   254  C CG1 . VAL   A 1 34 ? 4.827   -19.110 -19.869 1.00 44.29  ? 33  VAL   A CG1 1 
ATOM   255  C CG2 . VAL   A 1 34 ? 6.989   -20.148 -20.693 1.00 40.81  ? 33  VAL   A CG2 1 
ATOM   256  N N   . LYS   A 1 35 ? 5.551   -15.738 -19.672 1.00 38.51  ? 34  LYS   A N   1 
ATOM   257  C CA  . LYS   A 1 35 ? 4.874   -14.665 -18.953 1.00 35.80  ? 34  LYS   A CA  1 
ATOM   258  C C   . LYS   A 1 35 ? 3.585   -15.177 -18.317 1.00 38.36  ? 34  LYS   A C   1 
ATOM   259  O O   . LYS   A 1 35 ? 2.932   -16.078 -18.838 1.00 36.93  ? 34  LYS   A O   1 
ATOM   260  C CB  . LYS   A 1 35 ? 4.603   -13.449 -19.842 1.00 38.73  ? 34  LYS   A CB  1 
ATOM   261  C CG  . LYS   A 1 35 ? 5.903   -12.728 -20.251 1.00 37.24  ? 34  LYS   A CG  1 
ATOM   262  C CD  . LYS   A 1 35 ? 5.659   -11.559 -21.203 1.00 42.94  ? 34  LYS   A CD  1 
ATOM   263  C CE  . LYS   A 1 35 ? 5.242   -11.890 -22.609 1.00 43.08  ? 34  LYS   A CE  1 
ATOM   264  N NZ  . LYS   A 1 35 ? 4.982   -10.633 -23.310 1.00 48.02  ? 34  LYS   A NZ  1 
ATOM   265  N N   . PRO   A 1 36 ? 3.173   -14.612 -17.163 1.00 37.55  ? 35  PRO   A N   1 
ATOM   266  C CA  . PRO   A 1 36 ? 1.914   -15.026 -16.549 1.00 35.86  ? 35  PRO   A CA  1 
ATOM   267  C C   . PRO   A 1 36 ? 0.759   -14.570 -17.431 1.00 34.39  ? 35  PRO   A C   1 
ATOM   268  O O   . PRO   A 1 36 ? 0.882   -13.627 -18.202 1.00 39.57  ? 35  PRO   A O   1 
ATOM   269  C CB  . PRO   A 1 36 ? 1.839   -14.290 -15.195 1.00 36.61  ? 35  PRO   A CB  1 
ATOM   270  C CG  . PRO   A 1 36 ? 2.944   -13.239 -15.218 1.00 39.94  ? 35  PRO   A CG  1 
ATOM   271  C CD  . PRO   A 1 36 ? 3.852   -13.537 -16.423 1.00 38.26  ? 35  PRO   A CD  1 
ATOM   272  N N   . PRO   A 1 37 ? -0.459  -15.089 -17.194 1.00 38.10  ? 36  PRO   A N   1 
ATOM   273  C CA  . PRO   A 1 37 ? -1.658  -14.515 -17.817 1.00 41.68  ? 36  PRO   A CA  1 
ATOM   274  C C   . PRO   A 1 37 ? -1.901  -13.089 -17.347 1.00 44.13  ? 36  PRO   A C   1 
ATOM   275  O O   . PRO   A 1 37 ? -1.431  -12.687 -16.284 1.00 34.14  ? 36  PRO   A O   1 
ATOM   276  C CB  . PRO   A 1 37 ? -2.807  -15.440 -17.390 1.00 41.40  ? 36  PRO   A CB  1 
ATOM   277  C CG  . PRO   A 1 37 ? -2.130  -16.648 -16.803 1.00 39.42  ? 36  PRO   A CG  1 
ATOM   278  C CD  . PRO   A 1 37 ? -0.737  -16.250 -16.340 1.00 39.27  ? 36  PRO   A CD  1 
ATOM   279  N N   . PRO   A 1 38 ? -2.625  -12.252 -18.114 1.00 40.31  ? 37  PRO   A N   1 
ATOM   280  C CA  . PRO   A 1 38 ? -3.043  -10.935 -17.619 1.00 43.19  ? 37  PRO   A CA  1 
ATOM   281  C C   . PRO   A 1 38 ? -3.613  -10.954 -16.199 1.00 35.41  ? 37  PRO   A C   1 
ATOM   282  O O   . PRO   A 1 38 ? -4.331  -11.878 -15.838 1.00 40.59  ? 37  PRO   A O   1 
ATOM   283  C CB  . PRO   A 1 38 ? -4.088  -10.440 -18.653 1.00 42.24  ? 37  PRO   A CB  1 
ATOM   284  C CG  . PRO   A 1 38 ? -4.267  -11.605 -19.588 1.00 40.35  ? 37  PRO   A CG  1 
ATOM   285  C CD  . PRO   A 1 38 ? -3.048  -12.507 -19.508 1.00 44.30  ? 37  PRO   A CD  1 
ATOM   286  N N   . ASN   A 1 39 ? -3.243  -9.926  -15.424 1.00 40.89  ? 38  ASN   A N   1 
ATOM   287  C CA  . ASN   A 1 39 ? -3.666  -9.662  -14.060 1.00 41.15  ? 38  ASN   A CA  1 
ATOM   288  C C   . ASN   A 1 39 ? -3.189  -10.743 -13.095 1.00 35.10  ? 38  ASN   A C   1 
ATOM   289  O O   . ASN   A 1 39 ? -3.689  -10.776 -11.969 1.00 35.05  ? 38  ASN   A O   1 
ATOM   290  C CB  . ASN   A 1 39 ? -5.177  -9.501  -13.950 1.00 45.69  ? 38  ASN   A CB  1 
ATOM   291  C CG  . ASN   A 1 39 ? -5.638  -8.420  -14.894 1.00 50.14  ? 38  ASN   A CG  1 
ATOM   292  O OD1 . ASN   A 1 39 ? -5.451  -7.233  -14.601 1.00 53.90  ? 38  ASN   A OD1 1 
ATOM   293  N ND2 . ASN   A 1 39 ? -6.171  -8.817  -16.037 1.00 49.09  ? 38  ASN   A ND2 1 
ATOM   294  N N   . LYS   A 1 40 ? -2.232  -11.594 -13.513 1.00 32.14  ? 39  LYS   A N   1 
ATOM   295  C CA  . LYS   A 1 40 ? -1.718  -12.656 -12.645 1.00 25.91  ? 39  LYS   A CA  1 
ATOM   296  C C   . LYS   A 1 40 ? -0.232  -12.382 -12.406 1.00 23.97  ? 39  LYS   A C   1 
ATOM   297  O O   . LYS   A 1 40 ? 0.417   -11.667 -13.175 1.00 29.06  ? 39  LYS   A O   1 
ATOM   298  C CB  . LYS   A 1 40 ? -1.882  -14.119 -13.070 1.00 28.56  ? 39  LYS   A CB  1 
ATOM   299  C CG  . LYS   A 1 40 ? -3.292  -14.577 -13.481 1.00 32.65  ? 39  LYS   A CG  1 
ATOM   300  C CD  . LYS   A 1 40 ? -4.147  -14.325 -12.256 1.00 35.19  ? 39  LYS   A CD  1 
ATOM   301  C CE  . LYS   A 1 40 ? -5.629  -14.623 -12.424 1.00 48.74  ? 39  LYS   A CE  1 
ATOM   302  N NZ  . LYS   A 1 40 ? -5.888  -16.059 -12.559 1.00 53.72  ? 39  LYS   A NZ  1 
ATOM   303  N N   . TYR   A 1 41 ? 0.238   -12.792 -11.221 1.00 22.87  ? 40  TYR   A N   1 
ATOM   304  C CA  . TYR   A 1 41 ? 1.641   -12.671 -10.847 1.00 23.33  ? 40  TYR   A CA  1 
ATOM   305  C C   . TYR   A 1 41 ? 2.244   -14.049 -10.770 1.00 23.54  ? 40  TYR   A C   1 
ATOM   306  O O   . TYR   A 1 41 ? 1.635   -15.013 -10.352 1.00 23.11  ? 40  TYR   A O   1 
ATOM   307  C CB  . TYR   A 1 41 ? 1.761   -12.017 -9.442  1.00 22.60  ? 40  TYR   A CB  1 
ATOM   308  C CG  . TYR   A 1 41 ? 1.281   -10.570 -9.435  1.00 25.14  ? 40  TYR   A CG  1 
ATOM   309  C CD1 . TYR   A 1 41 ? -0.087  -10.269 -9.304  1.00 28.64  ? 40  TYR   A CD1 1 
ATOM   310  C CD2 . TYR   A 1 41 ? 2.157   -9.524  -9.628  1.00 27.71  ? 40  TYR   A CD2 1 
ATOM   311  C CE1 . TYR   A 1 41 ? -0.524  -8.952  -9.361  1.00 30.79  ? 40  TYR   A CE1 1 
ATOM   312  C CE2 . TYR   A 1 41 ? 1.727   -8.199  -9.656  1.00 30.27  ? 40  TYR   A CE2 1 
ATOM   313  C CZ  . TYR   A 1 41 ? 0.380   -7.926  -9.521  1.00 35.22  ? 40  TYR   A CZ  1 
ATOM   314  O OH  . TYR   A 1 41 ? -0.107  -6.651  -9.607  1.00 38.06  ? 40  TYR   A OH  1 
ATOM   315  N N   . PRO   A 1 42 ? 3.554   -14.176 -11.056 1.00 22.03  ? 41  PRO   A N   1 
ATOM   316  C CA  . PRO   A 1 42 ? 4.241   -15.436 -10.793 1.00 22.08  ? 41  PRO   A CA  1 
ATOM   317  C C   . PRO   A 1 42 ? 4.577   -15.547 -9.311  1.00 22.40  ? 41  PRO   A C   1 
ATOM   318  O O   . PRO   A 1 42 ? 5.268   -14.664 -8.804  1.00 24.11  ? 41  PRO   A O   1 
ATOM   319  C CB  . PRO   A 1 42 ? 5.549   -15.266 -11.623 1.00 22.62  ? 41  PRO   A CB  1 
ATOM   320  C CG  . PRO   A 1 42 ? 5.688   -13.825 -11.852 1.00 24.15  ? 41  PRO   A CG  1 
ATOM   321  C CD  . PRO   A 1 42 ? 4.388   -13.075 -11.549 1.00 25.56  ? 41  PRO   A CD  1 
ATOM   322  N N   . ILE   A 1 43 ? 4.038   -16.577 -8.655  1.00 21.91  ? 42  ILE   A N   1 
ATOM   323  C CA  . ILE   A 1 43 ? 4.252   -16.750 -7.226  1.00 20.28  ? 42  ILE   A CA  1 
ATOM   324  C C   . ILE   A 1 43 ? 5.242   -17.904 -7.052  1.00 23.05  ? 42  ILE   A C   1 
ATOM   325  O O   . ILE   A 1 43 ? 4.984   -19.035 -7.527  1.00 25.30  ? 42  ILE   A O   1 
ATOM   326  C CB  . ILE   A 1 43 ? 2.913   -17.028 -6.548  1.00 20.09  ? 42  ILE   A CB  1 
ATOM   327  C CG1 . ILE   A 1 43 ? 1.930   -15.898 -6.877  1.00 23.00  ? 42  ILE   A CG1 1 
ATOM   328  C CG2 . ILE   A 1 43 ? 3.179   -17.205 -5.042  1.00 20.67  ? 42  ILE   A CG2 1 
ATOM   329  C CD1 . ILE   A 1 43 ? 2.442   -14.517 -6.489  1.00 22.38  ? 42  ILE   A CD1 1 
ATOM   330  N N   . PHE   A 1 44 ? 6.320   -17.628 -6.283  1.00 21.57  ? 43  PHE   A N   1 
ATOM   331  C CA  . PHE   A 1 44 ? 7.235   -18.702 -5.939  1.00 22.90  ? 43  PHE   A CA  1 
ATOM   332  C C   . PHE   A 1 44 ? 6.923   -19.123 -4.511  1.00 20.83  ? 43  PHE   A C   1 
ATOM   333  O O   . PHE   A 1 44 ? 6.928   -18.308 -3.591  1.00 22.30  ? 43  PHE   A O   1 
ATOM   334  C CB  . PHE   A 1 44 ? 8.692   -18.199 -6.035  1.00 21.29  ? 43  PHE   A CB  1 
ATOM   335  C CG  . PHE   A 1 44 ? 9.697   -19.255 -5.580  1.00 23.41  ? 43  PHE   A CG  1 
ATOM   336  C CD1 . PHE   A 1 44 ? 10.037  -20.272 -6.470  1.00 26.21  ? 43  PHE   A CD1 1 
ATOM   337  C CD2 . PHE   A 1 44 ? 10.287  -19.229 -4.308  1.00 27.09  ? 43  PHE   A CD2 1 
ATOM   338  C CE1 . PHE   A 1 44 ? 10.971  -21.237 -6.112  1.00 28.86  ? 43  PHE   A CE1 1 
ATOM   339  C CE2 . PHE   A 1 44 ? 11.233  -20.200 -3.956  1.00 28.02  ? 43  PHE   A CE2 1 
ATOM   340  C CZ  . PHE   A 1 44 ? 11.569  -21.184 -4.858  1.00 27.88  ? 43  PHE   A CZ  1 
ATOM   341  N N   . PHE   A 1 45 ? 6.631   -20.415 -4.312  1.00 21.52  ? 44  PHE   A N   1 
ATOM   342  C CA  . PHE   A 1 45 ? 6.257   -20.920 -3.003  1.00 21.58  ? 44  PHE   A CA  1 
ATOM   343  C C   . PHE   A 1 45 ? 7.484   -21.438 -2.274  1.00 24.26  ? 44  PHE   A C   1 
ATOM   344  O O   . PHE   A 1 45 ? 8.206   -22.321 -2.798  1.00 25.69  ? 44  PHE   A O   1 
ATOM   345  C CB  . PHE   A 1 45 ? 5.249   -22.080 -3.178  1.00 25.67  ? 44  PHE   A CB  1 
ATOM   346  C CG  . PHE   A 1 45 ? 3.865   -21.598 -3.600  1.00 23.37  ? 44  PHE   A CG  1 
ATOM   347  C CD1 . PHE   A 1 45 ? 3.534   -21.451 -4.934  1.00 25.94  ? 44  PHE   A CD1 1 
ATOM   348  C CD2 . PHE   A 1 45 ? 2.894   -21.309 -2.646  1.00 25.85  ? 44  PHE   A CD2 1 
ATOM   349  C CE1 . PHE   A 1 45 ? 2.289   -20.955 -5.315  1.00 29.99  ? 44  PHE   A CE1 1 
ATOM   350  C CE2 . PHE   A 1 45 ? 1.629   -20.818 -3.022  1.00 25.34  ? 44  PHE   A CE2 1 
ATOM   351  C CZ  . PHE   A 1 45 ? 1.355   -20.633 -4.351  1.00 28.45  ? 44  PHE   A CZ  1 
ATOM   352  N N   . PHE   A 1 46 ? 7.737   -20.868 -1.093  1.00 21.83  ? 45  PHE   A N   1 
ATOM   353  C CA  . PHE   A 1 46 ? 8.915   -21.321 -0.338  1.00 23.58  ? 45  PHE   A CA  1 
ATOM   354  C C   . PHE   A 1 46 ? 8.711   -22.757 0.129   1.00 26.30  ? 45  PHE   A C   1 
ATOM   355  O O   . PHE   A 1 46 ? 7.576   -23.218 0.275   1.00 25.29  ? 45  PHE   A O   1 
ATOM   356  C CB  . PHE   A 1 46 ? 9.190   -20.410 0.874   1.00 22.44  ? 45  PHE   A CB  1 
ATOM   357  C CG  . PHE   A 1 46 ? 9.649   -19.031 0.450   1.00 21.00  ? 45  PHE   A CG  1 
ATOM   358  C CD1 . PHE   A 1 46 ? 10.903  -18.853 -0.121  1.00 21.58  ? 45  PHE   A CD1 1 
ATOM   359  C CD2 . PHE   A 1 46 ? 8.896   -17.862 0.697   1.00 22.70  ? 45  PHE   A CD2 1 
ATOM   360  C CE1 . PHE   A 1 46 ? 11.342  -17.594 -0.537  1.00 20.74  ? 45  PHE   A CE1 1 
ATOM   361  C CE2 . PHE   A 1 46 ? 9.343   -16.596 0.306   1.00 22.09  ? 45  PHE   A CE2 1 
ATOM   362  C CZ  . PHE   A 1 46 ? 10.595  -16.451 -0.303  1.00 21.76  ? 45  PHE   A CZ  1 
ATOM   363  N N   . GLY   A 1 47 ? 9.828   -23.467 0.343   1.00 24.35  ? 46  GLY   A N   1 
ATOM   364  C CA  . GLY   A 1 47 ? 9.781   -24.823 0.878   1.00 24.07  ? 46  GLY   A CA  1 
ATOM   365  C C   . GLY   A 1 47 ? 9.536   -25.843 -0.248  1.00 32.72  ? 46  GLY   A C   1 
ATOM   366  O O   . GLY   A 1 47 ? 10.392  -26.669 -0.566  1.00 33.01  ? 46  GLY   A O   1 
ATOM   367  N N   . THR   A 1 48 ? 8.384   -25.755 -0.935  1.00 28.88  ? 47  THR   A N   1 
ATOM   368  C CA  . THR   A 1 48 ? 8.112   -26.605 -2.092  1.00 30.57  ? 47  THR   A CA  1 
ATOM   369  C C   . THR   A 1 48 ? 8.911   -26.181 -3.322  1.00 32.19  ? 47  THR   A C   1 
ATOM   370  O O   . THR   A 1 48 ? 9.200   -26.996 -4.195  1.00 32.76  ? 47  THR   A O   1 
ATOM   371  C CB  . THR   A 1 48 ? 6.623   -26.691 -2.429  1.00 30.20  ? 47  THR   A CB  1 
ATOM   372  O OG1 . THR   A 1 48 ? 6.254   -25.403 -2.932  1.00 30.66  ? 47  THR   A OG1 1 
ATOM   373  C CG2 . THR   A 1 48 ? 5.807   -27.174 -1.256  1.00 34.22  ? 47  THR   A CG2 1 
ATOM   374  N N   . HIS   A 1 49 ? 9.206   -24.881 -3.440  1.00 26.59  ? 48  HIS   A N   1 
ATOM   375  C CA  . HIS   A 1 49 ? 9.875   -24.274 -4.579  1.00 27.12  ? 48  HIS   A CA  1 
ATOM   376  C C   . HIS   A 1 49 ? 9.089   -24.436 -5.875  1.00 29.34  ? 48  HIS   A C   1 
ATOM   377  O O   . HIS   A 1 49 ? 9.682   -24.359 -6.950  1.00 31.20  ? 48  HIS   A O   1 
ATOM   378  C CB  . HIS   A 1 49 ? 11.322  -24.763 -4.748  1.00 27.26  ? 48  HIS   A CB  1 
ATOM   379  C CG  . HIS   A 1 49 ? 12.062  -24.746 -3.465  1.00 29.02  ? 48  HIS   A CG  1 
ATOM   380  N ND1 . HIS   A 1 49 ? 12.894  -25.779 -3.095  1.00 31.50  ? 48  HIS   A ND1 1 
ATOM   381  C CD2 . HIS   A 1 49 ? 12.057  -23.873 -2.423  1.00 28.77  ? 48  HIS   A CD2 1 
ATOM   382  C CE1 . HIS   A 1 49 ? 13.368  -25.544 -1.876  1.00 36.42  ? 48  HIS   A CE1 1 
ATOM   383  N NE2 . HIS   A 1 49 ? 12.905  -24.372 -1.469  1.00 30.12  ? 48  HIS   A NE2 1 
ATOM   384  N N   . GLU   A 1 50 ? 7.752   -24.537 -5.761  1.00 29.47  ? 49  GLU   A N   1 
ATOM   385  C CA  . GLU   A 1 50 ? 6.842   -24.552 -6.898  1.00 29.29  ? 49  GLU   A CA  1 
ATOM   386  C C   . GLU   A 1 50 ? 6.419   -23.128 -7.295  1.00 28.11  ? 49  GLU   A C   1 
ATOM   387  O O   . GLU   A 1 50 ? 6.658   -22.166 -6.552  1.00 27.18  ? 49  GLU   A O   1 
ATOM   388  C CB  . GLU   A 1 50 ? 5.620   -25.360 -6.493  1.00 30.46  ? 49  GLU   A CB  1 
ATOM   389  C CG  . GLU   A 1 50 ? 5.935   -26.840 -6.262  1.00 42.00  ? 49  GLU   A CG  1 
ATOM   390  C CD  . GLU   A 1 50 ? 4.723   -27.632 -5.801  1.00 51.29  ? 49  GLU   A CD  1 
ATOM   391  O OE1 . GLU   A 1 50 ? 3.585   -27.123 -5.907  1.00 54.31  ? 49  GLU   A OE1 1 
ATOM   392  O OE2 . GLU   A 1 50 ? 4.926   -28.752 -5.289  1.00 50.97  ? 49  GLU   A OE2 1 
ATOM   393  N N   . THR   A 1 51 ? 5.966   -22.982 -8.548  1.00 27.79  ? 50  THR   A N   1 
ATOM   394  C CA  . THR   A 1 51 ? 5.509   -21.692 -9.047  1.00 26.53  ? 50  THR   A CA  1 
ATOM   395  C C   . THR   A 1 51 ? 4.057   -21.855 -9.472  1.00 31.18  ? 50  THR   A C   1 
ATOM   396  O O   . THR   A 1 51 ? 3.728   -22.865 -10.099 1.00 35.04  ? 50  THR   A O   1 
ATOM   397  C CB  . THR   A 1 51 ? 6.315   -21.163 -10.231 1.00 32.43  ? 50  THR   A CB  1 
ATOM   398  O OG1 . THR   A 1 51 ? 7.615   -20.793 -9.768  1.00 31.82  ? 50  THR   A OG1 1 
ATOM   399  C CG2 . THR   A 1 51 ? 5.713   -19.914 -10.866 1.00 36.10  ? 50  THR   A CG2 1 
ATOM   400  N N   . ALA   A 1 52 ? 3.221   -20.856 -9.184  1.00 25.36  ? 51  ALA   A N   1 
ATOM   401  C CA  . ALA   A 1 52 ? 1.871   -20.836 -9.716  1.00 25.95  ? 51  ALA   A CA  1 
ATOM   402  C C   . ALA   A 1 52 ? 1.545   -19.389 -10.053 1.00 26.71  ? 51  ALA   A C   1 
ATOM   403  O O   . ALA   A 1 52 ? 2.241   -18.467 -9.601  1.00 27.26  ? 51  ALA   A O   1 
ATOM   404  C CB  . ALA   A 1 52 ? 0.864   -21.404 -8.736  1.00 28.65  ? 51  ALA   A CB  1 
ATOM   405  N N   . PHE   A 1 53 ? 0.477   -19.161 -10.846 1.00 24.31  ? 52  PHE   A N   1 
ATOM   406  C CA  . PHE   A 1 53 ? 0.097   -17.804 -11.171 1.00 25.86  ? 52  PHE   A CA  1 
ATOM   407  C C   . PHE   A 1 53 ? -1.151  -17.448 -10.381 1.00 28.43  ? 52  PHE   A C   1 
ATOM   408  O O   . PHE   A 1 53 ? -2.139  -18.187 -10.396 1.00 31.41  ? 52  PHE   A O   1 
ATOM   409  C CB  . PHE   A 1 53 ? -0.232  -17.701 -12.665 1.00 27.42  ? 52  PHE   A CB  1 
ATOM   410  C CG  . PHE   A 1 53 ? 0.950   -18.117 -13.520 1.00 27.20  ? 52  PHE   A CG  1 
ATOM   411  C CD1 . PHE   A 1 53 ? 2.105   -17.345 -13.524 1.00 32.99  ? 52  PHE   A CD1 1 
ATOM   412  C CD2 . PHE   A 1 53 ? 0.836   -19.175 -14.412 1.00 33.16  ? 52  PHE   A CD2 1 
ATOM   413  C CE1 . PHE   A 1 53 ? 3.200   -17.705 -14.300 1.00 42.93  ? 52  PHE   A CE1 1 
ATOM   414  C CE2 . PHE   A 1 53 ? 1.921   -19.500 -15.218 1.00 38.83  ? 52  PHE   A CE2 1 
ATOM   415  C CZ  . PHE   A 1 53 ? 3.100   -18.777 -15.159 1.00 33.69  ? 52  PHE   A CZ  1 
ATOM   416  N N   . LEU   A 1 54 ? -1.067  -16.339 -9.662  1.00 25.79  ? 53  LEU   A N   1 
ATOM   417  C CA  . LEU   A 1 54 ? -2.154  -15.962 -8.779  1.00 24.12  ? 53  LEU   A CA  1 
ATOM   418  C C   . LEU   A 1 54 ? -2.453  -14.482 -8.955  1.00 23.84  ? 53  LEU   A C   1 
ATOM   419  O O   . LEU   A 1 54 ? -1.623  -13.651 -9.307  1.00 23.93  ? 53  LEU   A O   1 
ATOM   420  C CB  . LEU   A 1 54 ? -1.862  -16.275 -7.306  1.00 24.58  ? 53  LEU   A CB  1 
ATOM   421  C CG  . LEU   A 1 54 ? -1.784  -17.749 -6.948  1.00 25.02  ? 53  LEU   A CG  1 
ATOM   422  C CD1 . LEU   A 1 54 ? -1.401  -17.800 -5.475  1.00 26.23  ? 53  LEU   A CD1 1 
ATOM   423  C CD2 . LEU   A 1 54 ? -3.206  -18.352 -7.094  1.00 31.26  ? 53  LEU   A CD2 1 
ATOM   424  N N   . GLY   A 1 55 ? -3.743  -14.156 -8.687  1.00 22.54  ? 54  GLY   A N   1 
ATOM   425  C CA  . GLY   A 1 55 ? -4.116  -12.753 -8.610  1.00 24.46  ? 54  GLY   A CA  1 
ATOM   426  C C   . GLY   A 1 55 ? -4.084  -12.234 -7.162  1.00 20.84  ? 54  GLY   A C   1 
ATOM   427  O O   . GLY   A 1 55 ? -4.048  -13.041 -6.230  1.00 21.74  ? 54  GLY   A O   1 
ATOM   428  N N   . PRO   A 1 56 ? -4.207  -10.900 -6.964  1.00 23.44  ? 55  PRO   A N   1 
ATOM   429  C CA  . PRO   A 1 56 ? -4.171  -10.281 -5.621  1.00 21.40  ? 55  PRO   A CA  1 
ATOM   430  C C   . PRO   A 1 56 ? -5.148  -10.803 -4.577  1.00 21.82  ? 55  PRO   A C   1 
ATOM   431  O O   . PRO   A 1 56 ? -4.881  -10.735 -3.382  1.00 21.10  ? 55  PRO   A O   1 
ATOM   432  C CB  . PRO   A 1 56 ? -4.370  -8.789  -5.882  1.00 23.60  ? 55  PRO   A CB  1 
ATOM   433  C CG  . PRO   A 1 56 ? -3.834  -8.608  -7.289  1.00 26.36  ? 55  PRO   A CG  1 
ATOM   434  C CD  . PRO   A 1 56 ? -4.199  -9.886  -8.036  1.00 25.37  ? 55  PRO   A CD  1 
ATOM   435  N N   . LYS   A 1 57 ? -6.288  -11.349 -5.066  1.00 23.92  ? 56  LYS   A N   1 
ATOM   436  C CA  . LYS   A 1 57 ? -7.282  -11.863 -4.111  1.00 24.90  ? 56  LYS   A CA  1 
ATOM   437  C C   . LYS   A 1 57 ? -6.755  -13.016 -3.246  1.00 22.42  ? 56  LYS   A C   1 
ATOM   438  O O   . LYS   A 1 57 ? -7.188  -13.234 -2.112  1.00 22.34  ? 56  LYS   A O   1 
ATOM   439  C CB  . LYS   A 1 57 ? -8.619  -12.376 -4.701  1.00 25.33  ? 56  LYS   A CB  1 
ATOM   440  C CG  . LYS   A 1 57 ? -8.429  -13.647 -5.495  1.00 31.19  ? 56  LYS   A CG  1 
ATOM   441  C CD  . LYS   A 1 57 ? -9.717  -14.039 -6.224  1.00 40.14  ? 56  LYS   A CD  1 
ATOM   442  C CE  . LYS   A 1 57 ? -9.522  -15.329 -6.970  1.00 37.51  ? 56  LYS   A CE  1 
ATOM   443  N NZ  . LYS   A 1 57 ? -9.375  -16.454 -6.038  1.00 46.57  ? 56  LYS   A NZ  1 
ATOM   444  N N   . ASP   A 1 58 ? -5.689  -13.702 -3.733  1.00 22.95  ? 57  ASP   A N   1 
ATOM   445  C CA  . ASP   A 1 58 ? -5.076  -14.819 -3.052  1.00 22.36  ? 57  ASP   A CA  1 
ATOM   446  C C   . ASP   A 1 58 ? -3.703  -14.443 -2.451  1.00 23.14  ? 57  ASP   A C   1 
ATOM   447  O O   . ASP   A 1 58 ? -3.032  -15.346 -1.987  1.00 23.35  ? 57  ASP   A O   1 
ATOM   448  C CB  . ASP   A 1 58 ? -4.984  -15.991 -4.031  1.00 23.13  ? 57  ASP   A CB  1 
ATOM   449  C CG  . ASP   A 1 58 ? -6.367  -16.569 -4.327  1.00 28.09  ? 57  ASP   A CG  1 
ATOM   450  O OD1 . ASP   A 1 58 ? -7.127  -16.611 -3.372  1.00 27.99  ? 57  ASP   A OD1 1 
ATOM   451  O OD2 . ASP   A 1 58 ? -6.661  -16.973 -5.476  1.00 29.73  ? 57  ASP   A OD2 1 
ATOM   452  N N   . LEU   A 1 59 ? -3.348  -13.151 -2.405  1.00 20.59  ? 58  LEU   A N   1 
ATOM   453  C CA  . LEU   A 1 59 ? -2.015  -12.726 -1.936  1.00 20.71  ? 58  LEU   A CA  1 
ATOM   454  C C   . LEU   A 1 59 ? -2.178  -11.863 -0.688  1.00 19.34  ? 58  LEU   A C   1 
ATOM   455  O O   . LEU   A 1 59 ? -2.816  -10.784 -0.695  1.00 21.33  ? 58  LEU   A O   1 
ATOM   456  C CB  . LEU   A 1 59 ? -1.308  -11.948 -3.051  1.00 18.67  ? 58  LEU   A CB  1 
ATOM   457  C CG  . LEU   A 1 59 ? -1.174  -12.724 -4.353  1.00 21.83  ? 58  LEU   A CG  1 
ATOM   458  C CD1 . LEU   A 1 59 ? -0.517  -11.872 -5.412  1.00 21.77  ? 58  LEU   A CD1 1 
ATOM   459  C CD2 . LEU   A 1 59 ? -0.386  -14.021 -4.186  1.00 23.32  ? 58  LEU   A CD2 1 
ATOM   460  N N   . PHE   A 1 60 ? -1.607  -12.333 0.418   1.00 18.43  ? 59  PHE   A N   1 
ATOM   461  C CA  . PHE   A 1 60 ? -1.681  -11.615 1.702   1.00 20.34  ? 59  PHE   A CA  1 
ATOM   462  C C   . PHE   A 1 60 ? -0.297  -11.119 2.112   1.00 22.44  ? 59  PHE   A C   1 
ATOM   463  O O   . PHE   A 1 60 ? 0.614   -11.913 2.275   1.00 22.90  ? 59  PHE   A O   1 
ATOM   464  C CB  . PHE   A 1 60 ? -2.188  -12.614 2.739   1.00 21.32  ? 59  PHE   A CB  1 
ATOM   465  C CG  . PHE   A 1 60 ? -3.632  -13.076 2.484   1.00 20.57  ? 59  PHE   A CG  1 
ATOM   466  C CD1 . PHE   A 1 60 ? -3.901  -14.005 1.480   1.00 23.38  ? 59  PHE   A CD1 1 
ATOM   467  C CD2 . PHE   A 1 60 ? -4.662  -12.565 3.250   1.00 26.69  ? 59  PHE   A CD2 1 
ATOM   468  C CE1 . PHE   A 1 60 ? -5.200  -14.404 1.181   1.00 25.05  ? 59  PHE   A CE1 1 
ATOM   469  C CE2 . PHE   A 1 60 ? -5.953  -12.989 2.952   1.00 23.59  ? 59  PHE   A CE2 1 
ATOM   470  C CZ  . PHE   A 1 60 ? -6.209  -13.903 1.967   1.00 26.42  ? 59  PHE   A CZ  1 
ATOM   471  N N   . PRO   A 1 61 ? -0.077  -9.813  2.274   1.00 23.22  ? 60  PRO   A N   1 
ATOM   472  C CA  . PRO   A 1 61 ? 1.286   -9.317  2.584   1.00 22.48  ? 60  PRO   A CA  1 
ATOM   473  C C   . PRO   A 1 61 ? 1.813   -9.984  3.842   1.00 21.76  ? 60  PRO   A C   1 
ATOM   474  O O   . PRO   A 1 61 ? 1.132   -10.174 4.844   1.00 25.65  ? 60  PRO   A O   1 
ATOM   475  C CB  . PRO   A 1 61 ? 1.098   -7.792  2.688   1.00 24.61  ? 60  PRO   A CB  1 
ATOM   476  C CG  . PRO   A 1 61 ? -0.060  -7.515  1.660   1.00 27.07  ? 60  PRO   A CG  1 
ATOM   477  C CD  . PRO   A 1 61 ? -1.005  -8.691  2.015   1.00 27.12  ? 60  PRO   A CD  1 
ATOM   478  N N   . TYR   A 1 62 ? 3.107   -10.422 3.807   1.00 22.61  ? 61  TYR   A N   1 
ATOM   479  C CA  . TYR   A 1 62 ? 3.644   -11.269 4.861   1.00 22.53  ? 61  TYR   A CA  1 
ATOM   480  C C   . TYR   A 1 62 ? 3.699   -10.604 6.249   1.00 22.45  ? 61  TYR   A C   1 
ATOM   481  O O   . TYR   A 1 62 ? 3.344   -11.293 7.191   1.00 27.19  ? 61  TYR   A O   1 
ATOM   482  C CB  . TYR   A 1 62 ? 5.074   -11.609 4.403   1.00 24.43  ? 61  TYR   A CB  1 
ATOM   483  C CG  . TYR   A 1 62 ? 5.860   -12.410 5.448   1.00 22.06  ? 61  TYR   A CG  1 
ATOM   484  C CD1 . TYR   A 1 62 ? 5.581   -13.738 5.714   1.00 24.43  ? 61  TYR   A CD1 1 
ATOM   485  C CD2 . TYR   A 1 62 ? 6.918   -11.791 6.117   1.00 28.74  ? 61  TYR   A CD2 1 
ATOM   486  C CE1 . TYR   A 1 62 ? 6.299   -14.472 6.666   1.00 27.81  ? 61  TYR   A CE1 1 
ATOM   487  C CE2 . TYR   A 1 62 ? 7.634   -12.522 7.051   1.00 27.53  ? 61  TYR   A CE2 1 
ATOM   488  C CZ  . TYR   A 1 62 ? 7.322   -13.829 7.333   1.00 27.94  ? 61  TYR   A CZ  1 
ATOM   489  O OH  . TYR   A 1 62 ? 8.059   -14.549 8.261   1.00 30.26  ? 61  TYR   A OH  1 
ATOM   490  N N   . ASP   A 1 63 ? 4.172   -9.347  6.315   1.00 28.60  ? 62  ASP   A N   1 
ATOM   491  C CA  . ASP   A 1 63 ? 4.299   -8.634  7.585   1.00 33.18  ? 62  ASP   A CA  1 
ATOM   492  C C   . ASP   A 1 63 ? 2.949   -8.608  8.325   1.00 30.33  ? 62  ASP   A C   1 
ATOM   493  O O   . ASP   A 1 63 ? 2.865   -9.130  9.441   1.00 39.64  ? 62  ASP   A O   1 
ATOM   494  C CB  . ASP   A 1 63 ? 5.087   -7.344  7.411   1.00 31.06  ? 62  ASP   A CB  1 
ATOM   495  N N   . LYS   A 1 64 ? 1.891   -8.152  7.637   1.00 33.65  ? 63  LYS   A N   1 
ATOM   496  C CA  . LYS   A 1 64 ? 0.542   -8.051  8.201   1.00 32.62  ? 63  LYS   A CA  1 
ATOM   497  C C   . LYS   A 1 64 ? 0.027   -9.408  8.685   1.00 32.73  ? 63  LYS   A C   1 
ATOM   498  O O   . LYS   A 1 64 ? -0.693  -9.464  9.690   1.00 32.21  ? 63  LYS   A O   1 
ATOM   499  C CB  . LYS   A 1 64 ? -0.433  -7.425  7.180   1.00 33.24  ? 63  LYS   A CB  1 
ATOM   500  C CG  . LYS   A 1 64 ? -1.912  -7.268  7.642   1.00 34.50  ? 63  LYS   A CG  1 
ATOM   501  C CD  . LYS   A 1 64 ? -2.815  -6.668  6.564   1.00 36.50  ? 63  LYS   A CD  1 
ATOM   502  C CE  . LYS   A 1 64 ? -3.837  -5.734  7.138   1.00 44.68  ? 63  LYS   A CE  1 
ATOM   503  N NZ  . LYS   A 1 64 ? -4.786  -6.400  8.026   1.00 45.16  ? 63  LYS   A NZ  1 
ATOM   504  N N   . SER   A 1 65 ? 0.349   -10.497 7.951   1.00 28.62  ? 64  SER   A N   1 
ATOM   505  C CA  . SER   A 1 65 ? -0.351  -11.777 8.044   1.00 28.47  ? 64  SER   A CA  1 
ATOM   506  C C   . SER   A 1 65 ? 0.407   -12.854 8.825   1.00 28.21  ? 64  SER   A C   1 
ATOM   507  O O   . SER   A 1 65 ? -0.111  -13.956 8.985   1.00 28.29  ? 64  SER   A O   1 
ATOM   508  C CB  . SER   A 1 65 ? -0.621  -12.315 6.658   1.00 29.06  ? 64  SER   A CB  1 
ATOM   509  O OG  . SER   A 1 65 ? -1.444  -11.348 6.023   1.00 37.99  ? 64  SER   A OG  1 
ATOM   510  N N   . LYS   A 1 66 ? 1.661   -12.598 9.206   1.00 27.87  ? 65  LYS   A N   1 
ATOM   511  C CA  . LYS   A 1 66 ? 2.479   -13.700 9.709   1.00 32.02  ? 65  LYS   A CA  1 
ATOM   512  C C   . LYS   A 1 66 ? 2.061   -14.214 11.093  1.00 27.20  ? 65  LYS   A C   1 
ATOM   513  O O   . LYS   A 1 66 ? 2.236   -15.399 11.416  1.00 32.76  ? 65  LYS   A O   1 
ATOM   514  C CB  . LYS   A 1 66 ? 3.968   -13.367 9.609   1.00 31.39  ? 65  LYS   A CB  1 
ATOM   515  C CG  . LYS   A 1 66 ? 4.396   -12.199 10.430  1.00 32.10  ? 65  LYS   A CG  1 
ATOM   516  C CD  . LYS   A 1 66 ? 5.919   -12.124 10.379  1.00 44.30  ? 65  LYS   A CD  1 
ATOM   517  C CE  . LYS   A 1 66 ? 6.487   -11.074 11.303  1.00 50.07  ? 65  LYS   A CE  1 
ATOM   518  N NZ  . LYS   A 1 66 ? 6.292   -9.710  10.785  1.00 57.00  ? 65  LYS   A NZ  1 
ATOM   519  N N   A ASP   A 1 67 ? 1.459   -13.332 11.897  0.50 32.47  ? 66  ASP   A N   1 
ATOM   520  N N   B ASP   A 1 67 ? 1.473   -13.329 11.904  0.50 31.17  ? 66  ASP   A N   1 
ATOM   521  C CA  A ASP   A 1 67 ? 0.991   -13.754 13.210  0.50 36.62  ? 66  ASP   A CA  1 
ATOM   522  C CA  B ASP   A 1 67 ? 0.985   -13.779 13.200  0.50 33.81  ? 66  ASP   A CA  1 
ATOM   523  C C   A ASP   A 1 67 ? -0.120  -14.794 13.042  0.50 37.12  ? 66  ASP   A C   1 
ATOM   524  C C   B ASP   A 1 67 ? -0.048  -14.879 12.970  0.50 34.58  ? 66  ASP   A C   1 
ATOM   525  O O   A ASP   A 1 67 ? -0.233  -15.723 13.829  0.50 41.72  ? 66  ASP   A O   1 
ATOM   526  O O   B ASP   A 1 67 ? -0.027  -15.916 13.623  0.50 36.37  ? 66  ASP   A O   1 
ATOM   527  C CB  A ASP   A 1 67 ? 0.676   -12.563 14.106  0.50 39.38  ? 66  ASP   A CB  1 
ATOM   528  C CB  B ASP   A 1 67 ? 0.452   -12.631 14.042  0.50 34.87  ? 66  ASP   A CB  1 
ATOM   529  C CG  A ASP   A 1 67 ? 1.872   -11.753 14.595  0.50 42.82  ? 66  ASP   A CG  1 
ATOM   530  C CG  B ASP   A 1 67 ? -0.007  -13.022 15.440  0.50 35.19  ? 66  ASP   A CG  1 
ATOM   531  O OD1 A ASP   A 1 67 ? 3.023   -12.215 14.424  0.50 45.14  ? 66  ASP   A OD1 1 
ATOM   532  O OD1 B ASP   A 1 67 ? 0.856   -13.122 16.352  0.50 38.66  ? 66  ASP   A OD1 1 
ATOM   533  O OD2 A ASP   A 1 67 ? 1.653   -10.649 15.132  0.50 46.38  ? 66  ASP   A OD2 1 
ATOM   534  O OD2 B ASP   A 1 67 ? -1.216  -13.257 15.600  0.50 41.97  ? 66  ASP   A OD2 1 
ATOM   535  N N   . LYS   A 1 68 ? -0.909  -14.671 11.970  1.00 33.10  ? 67  LYS   A N   1 
ATOM   536  C CA  . LYS   A 1 68 ? -2.026  -15.559 11.727  1.00 29.13  ? 67  LYS   A CA  1 
ATOM   537  C C   . LYS   A 1 68 ? -1.566  -16.815 11.005  1.00 31.79  ? 67  LYS   A C   1 
ATOM   538  O O   . LYS   A 1 68 ? -2.058  -17.905 11.287  1.00 34.62  ? 67  LYS   A O   1 
ATOM   539  C CB  . LYS   A 1 68 ? -3.085  -14.780 10.940  1.00 30.82  ? 67  LYS   A CB  1 
ATOM   540  C CG  . LYS   A 1 68 ? -4.352  -15.557 10.666  1.00 35.57  ? 67  LYS   A CG  1 
ATOM   541  C CD  . LYS   A 1 68 ? -5.338  -14.651 9.922   1.00 39.34  ? 67  LYS   A CD  1 
ATOM   542  C CE  . LYS   A 1 68 ? -6.687  -15.280 9.714   1.00 40.78  ? 67  LYS   A CE  1 
ATOM   543  N NZ  . LYS   A 1 68 ? -7.613  -14.304 9.099   1.00 42.53  ? 67  LYS   A NZ  1 
ATOM   544  N N   . TYR   A 1 69 ? -0.690  -16.647 9.993   1.00 30.93  ? 68  TYR   A N   1 
ATOM   545  C CA  . TYR   A 1 69 ? -0.460  -17.735 9.057   1.00 30.04  ? 68  TYR   A CA  1 
ATOM   546  C C   . TYR   A 1 69 ? 0.915   -18.388 9.214   1.00 29.30  ? 68  TYR   A C   1 
ATOM   547  O O   . TYR   A 1 69 ? 1.122   -19.456 8.635   1.00 30.45  ? 68  TYR   A O   1 
ATOM   548  C CB  . TYR   A 1 69 ? -0.582  -17.247 7.604   1.00 28.23  ? 68  TYR   A CB  1 
ATOM   549  C CG  . TYR   A 1 69 ? -1.995  -16.835 7.197   1.00 27.99  ? 68  TYR   A CG  1 
ATOM   550  C CD1 . TYR   A 1 69 ? -3.108  -17.582 7.580   1.00 31.57  ? 68  TYR   A CD1 1 
ATOM   551  C CD2 . TYR   A 1 69 ? -2.183  -15.677 6.431   1.00 26.49  ? 68  TYR   A CD2 1 
ATOM   552  C CE1 . TYR   A 1 69 ? -4.381  -17.178 7.200   1.00 28.61  ? 68  TYR   A CE1 1 
ATOM   553  C CE2 . TYR   A 1 69 ? -3.457  -15.260 6.070   1.00 28.71  ? 68  TYR   A CE2 1 
ATOM   554  C CZ  . TYR   A 1 69 ? -4.552  -16.021 6.451   1.00 30.69  ? 68  TYR   A CZ  1 
ATOM   555  O OH  . TYR   A 1 69 ? -5.798  -15.611 6.046   1.00 30.70  ? 68  TYR   A OH  1 
ATOM   556  N N   . GLY   A 1 70 ? 1.803   -17.782 9.995   1.00 29.81  ? 69  GLY   A N   1 
ATOM   557  C CA  . GLY   A 1 70 ? 3.199   -18.223 10.027  1.00 27.94  ? 69  GLY   A CA  1 
ATOM   558  C C   . GLY   A 1 70 ? 3.487   -19.195 11.186  1.00 31.94  ? 69  GLY   A C   1 
ATOM   559  O O   . GLY   A 1 70 ? 4.466   -19.054 11.876  1.00 37.77  ? 69  GLY   A O   1 
ATOM   560  N N   . LYS   A 1 71 ? 2.631   -20.198 11.345  1.00 36.87  ? 70  LYS   A N   1 
ATOM   561  C CA  . LYS   A 1 71 ? 2.831   -21.203 12.372  1.00 41.01  ? 70  LYS   A CA  1 
ATOM   562  C C   . LYS   A 1 71 ? 3.118   -22.528 11.676  1.00 36.96  ? 70  LYS   A C   1 
ATOM   563  O O   . LYS   A 1 71 ? 2.676   -22.803 10.555  1.00 35.62  ? 70  LYS   A O   1 
ATOM   564  C CB  . LYS   A 1 71 ? 1.628   -21.242 13.326  1.00 41.69  ? 70  LYS   A CB  1 
ATOM   565  C CG  . LYS   A 1 71 ? 1.516   -20.022 14.244  1.00 47.39  ? 70  LYS   A CG  1 
ATOM   566  C CD  . LYS   A 1 71 ? 0.085   -19.580 14.548  1.00 55.83  ? 70  LYS   A CD  1 
ATOM   567  N N   . PRO   A 1 72 ? 3.878   -23.436 12.320  1.00 34.83  ? 71  PRO   A N   1 
ATOM   568  C CA  . PRO   A 1 72 ? 4.109   -24.736 11.698  1.00 34.03  ? 71  PRO   A CA  1 
ATOM   569  C C   . PRO   A 1 72 ? 2.860   -25.467 11.236  1.00 36.60  ? 71  PRO   A C   1 
ATOM   570  O O   . PRO   A 1 72 ? 1.789   -25.312 11.814  1.00 46.55  ? 71  PRO   A O   1 
ATOM   571  C CB  . PRO   A 1 72 ? 4.887   -25.515 12.776  1.00 38.70  ? 71  PRO   A CB  1 
ATOM   572  C CG  . PRO   A 1 72 ? 5.538   -24.410 13.598  1.00 39.53  ? 71  PRO   A CG  1 
ATOM   573  C CD  . PRO   A 1 72 ? 4.564   -23.227 13.606  1.00 40.59  ? 71  PRO   A CD  1 
ATOM   574  N N   . ASN   A 1 73 ? 3.043   -26.254 10.186  1.00 37.64  ? 72  ASN   A N   1 
ATOM   575  C CA  . ASN   A 1 73 ? 2.001   -26.998 9.520   1.00 41.82  ? 72  ASN   A CA  1 
ATOM   576  C C   . ASN   A 1 73 ? 2.584   -28.344 9.129   1.00 47.06  ? 72  ASN   A C   1 
ATOM   577  O O   . ASN   A 1 73 ? 3.757   -28.434 8.769   1.00 44.65  ? 72  ASN   A O   1 
ATOM   578  C CB  . ASN   A 1 73 ? 1.621   -26.318 8.210   1.00 42.00  ? 72  ASN   A CB  1 
ATOM   579  C CG  . ASN   A 1 73 ? 0.203   -26.631 7.822   1.00 52.91  ? 72  ASN   A CG  1 
ATOM   580  O OD1 . ASN   A 1 73 ? -0.031  -27.431 6.908   1.00 52.28  ? 72  ASN   A OD1 1 
ATOM   581  N ND2 . ASN   A 1 73 ? -0.747  -26.012 8.508   1.00 60.46  ? 72  ASN   A ND2 1 
ATOM   582  N N   . LYS   A 1 74 ? 1.742   -29.375 9.188   1.00 46.79  ? 73  LYS   A N   1 
ATOM   583  C CA  . LYS   A 1 74 ? 2.126   -30.728 8.830   1.00 48.89  ? 73  LYS   A CA  1 
ATOM   584  C C   . LYS   A 1 74 ? 2.427   -30.834 7.336   1.00 40.93  ? 73  LYS   A C   1 
ATOM   585  O O   . LYS   A 1 74 ? 3.088   -31.777 6.902   1.00 43.30  ? 73  LYS   A O   1 
ATOM   586  C CB  . LYS   A 1 74 ? 1.014   -31.688 9.292   1.00 51.95  ? 73  LYS   A CB  1 
ATOM   587  C CG  . LYS   A 1 74 ? -0.273  -31.685 8.466   1.00 56.89  ? 73  LYS   A CG  1 
ATOM   588  N N   . ARG   A 1 75 ? 1.938   -29.885 6.522   1.00 38.58  ? 74  ARG   A N   1 
ATOM   589  C CA  . ARG   A 1 75 ? 2.053   -30.050 5.085   1.00 34.57  ? 74  ARG   A CA  1 
ATOM   590  C C   . ARG   A 1 75 ? 3.508   -30.044 4.612   1.00 36.55  ? 74  ARG   A C   1 
ATOM   591  O O   . ARG   A 1 75 ? 4.350   -29.306 5.136   1.00 34.96  ? 74  ARG   A O   1 
ATOM   592  C CB  . ARG   A 1 75 ? 1.155   -29.086 4.292   1.00 38.48  ? 74  ARG   A CB  1 
ATOM   593  C CG  . ARG   A 1 75 ? -0.323  -29.274 4.611   1.00 45.52  ? 74  ARG   A CG  1 
ATOM   594  C CD  . ARG   A 1 75 ? -0.884  -30.503 3.912   1.00 43.82  ? 74  ARG   A CD  1 
ATOM   595  N NE  . ARG   A 1 75 ? -1.643  -30.186 2.702   1.00 54.54  ? 74  ARG   A NE  1 
ATOM   596  C CZ  . ARG   A 1 75 ? -2.815  -29.547 2.775   1.00 54.14  ? 74  ARG   A CZ  1 
ATOM   597  N NH1 . ARG   A 1 75 ? -3.433  -29.189 1.670   1.00 59.87  ? 74  ARG   A NH1 1 
ATOM   598  N NH2 . ARG   A 1 75 ? -3.365  -29.270 3.953   1.00 55.45  ? 74  ARG   A NH2 1 
ATOM   599  N N   . LYS   A 1 76 ? 3.751   -30.874 3.595   1.00 34.70  ? 75  LYS   A N   1 
ATOM   600  C CA  . LYS   A 1 76 ? 5.056   -31.102 2.999   1.00 38.45  ? 75  LYS   A CA  1 
ATOM   601  C C   . LYS   A 1 76 ? 5.645   -29.778 2.521   1.00 35.95  ? 75  LYS   A C   1 
ATOM   602  O O   . LYS   A 1 76 ? 5.101   -29.128 1.625   1.00 34.40  ? 75  LYS   A O   1 
ATOM   603  C CB  . LYS   A 1 76 ? 4.988   -32.017 1.772   1.00 40.91  ? 75  LYS   A CB  1 
ATOM   604  C CG  . LYS   A 1 76 ? 6.334   -32.410 1.175   1.00 43.49  ? 75  LYS   A CG  1 
ATOM   605  C CD  . LYS   A 1 76 ? 6.285   -33.350 -0.034  1.00 42.76  ? 75  LYS   A CD  1 
ATOM   606  C CE  . LYS   A 1 76 ? 7.594   -33.846 -0.575  1.00 48.60  ? 75  LYS   A CE  1 
ATOM   607  N N   . GLY   A 1 77 ? 6.794   -29.435 3.109   1.00 36.99  ? 76  GLY   A N   1 
ATOM   608  C CA  . GLY   A 1 77 ? 7.558   -28.307 2.602   1.00 30.45  ? 76  GLY   A CA  1 
ATOM   609  C C   . GLY   A 1 77 ? 7.211   -27.041 3.379   1.00 32.09  ? 76  GLY   A C   1 
ATOM   610  O O   . GLY   A 1 77 ? 7.914   -26.055 3.273   1.00 29.41  ? 76  GLY   A O   1 
ATOM   611  N N   . PHE   A 1 78 ? 6.158   -27.060 4.185   1.00 28.44  ? 77  PHE   A N   1 
ATOM   612  C CA  . PHE   A 1 78 ? 5.681   -25.824 4.788   1.00 30.76  ? 77  PHE   A CA  1 
ATOM   613  C C   . PHE   A 1 78 ? 6.686   -25.231 5.786   1.00 31.76  ? 77  PHE   A C   1 
ATOM   614  O O   . PHE   A 1 78 ? 6.973   -24.029 5.803   1.00 29.63  ? 77  PHE   A O   1 
ATOM   615  C CB  . PHE   A 1 78 ? 4.311   -26.056 5.441   1.00 30.78  ? 77  PHE   A CB  1 
ATOM   616  C CG  . PHE   A 1 78 ? 3.594   -24.767 5.856   1.00 29.64  ? 77  PHE   A CG  1 
ATOM   617  C CD1 . PHE   A 1 78 ? 3.887   -24.128 7.056   1.00 31.00  ? 77  PHE   A CD1 1 
ATOM   618  C CD2 . PHE   A 1 78 ? 2.627   -24.195 5.008   1.00 31.44  ? 77  PHE   A CD2 1 
ATOM   619  C CE1 . PHE   A 1 78 ? 3.275   -22.927 7.412   1.00 31.76  ? 77  PHE   A CE1 1 
ATOM   620  C CE2 . PHE   A 1 78 ? 1.961   -23.025 5.395   1.00 28.48  ? 77  PHE   A CE2 1 
ATOM   621  C CZ  . PHE   A 1 78 ? 2.317   -22.369 6.558   1.00 28.54  ? 77  PHE   A CZ  1 
ATOM   622  N N   . ASN   A 1 79 ? 7.206   -26.066 6.688   1.00 27.18  ? 78  ASN   A N   1 
ATOM   623  C CA  . ASN   A 1 79 ? 8.120   -25.565 7.704   1.00 27.06  ? 78  ASN   A CA  1 
ATOM   624  C C   . ASN   A 1 79 ? 9.458   -25.109 7.089   1.00 27.49  ? 78  ASN   A C   1 
ATOM   625  O O   . ASN   A 1 79 ? 10.032  -24.119 7.560   1.00 26.57  ? 78  ASN   A O   1 
ATOM   626  C CB  . ASN   A 1 79 ? 8.294   -26.621 8.801   1.00 29.04  ? 78  ASN   A CB  1 
ATOM   627  C CG  . ASN   A 1 79 ? 6.980   -26.884 9.506   1.00 39.85  ? 78  ASN   A CG  1 
ATOM   628  O OD1 . ASN   A 1 79 ? 6.086   -26.029 9.502   1.00 31.44  ? 78  ASN   A OD1 1 
ATOM   629  N ND2 . ASN   A 1 79 ? 6.845   -28.039 10.150  1.00 33.58  ? 78  ASN   A ND2 1 
ATOM   630  N N   . GLU   A 1 80 ? 9.960   -25.826 6.069   1.00 26.52  ? 79  GLU   A N   1 
ATOM   631  C CA  . GLU   A 1 80 ? 11.110  -25.331 5.325   1.00 27.02  ? 79  GLU   A CA  1 
ATOM   632  C C   . GLU   A 1 80 ? 10.769  -23.965 4.736   1.00 25.31  ? 79  GLU   A C   1 
ATOM   633  O O   . GLU   A 1 80 ? 11.570  -23.019 4.788   1.00 24.07  ? 79  GLU   A O   1 
ATOM   634  C CB  . GLU   A 1 80 ? 11.498  -26.282 4.191   1.00 27.97  ? 79  GLU   A CB  1 
ATOM   635  C CG  . GLU   A 1 80 ? 12.778  -25.848 3.486   1.00 31.57  ? 79  GLU   A CG  1 
ATOM   636  C CD  . GLU   A 1 80 ? 13.308  -26.978 2.608   1.00 41.09  ? 79  GLU   A CD  1 
ATOM   637  O OE1 . GLU   A 1 80 ? 12.707  -28.064 2.640   1.00 49.83  ? 79  GLU   A OE1 1 
ATOM   638  O OE2 . GLU   A 1 80 ? 14.308  -26.817 1.907   1.00 38.50  ? 79  GLU   A OE2 1 
ATOM   639  N N   . GLY   A 1 81 ? 9.522   -23.862 4.253   1.00 25.14  ? 80  GLY   A N   1 
ATOM   640  C CA  . GLY   A 1 81 ? 9.079   -22.593 3.681   1.00 27.53  ? 80  GLY   A CA  1 
ATOM   641  C C   . GLY   A 1 81 ? 9.103   -21.437 4.694   1.00 23.08  ? 80  GLY   A C   1 
ATOM   642  O O   . GLY   A 1 81 ? 9.461   -20.290 4.349   1.00 22.88  ? 80  GLY   A O   1 
ATOM   643  N N   . LEU   A 1 82 ? 8.677   -21.697 5.943   1.00 22.80  ? 81  LEU   A N   1 
ATOM   644  C CA  . LEU   A 1 82 ? 8.710   -20.648 6.946   1.00 24.65  ? 81  LEU   A CA  1 
ATOM   645  C C   . LEU   A 1 82 ? 10.161  -20.223 7.218   1.00 24.19  ? 81  LEU   A C   1 
ATOM   646  O O   . LEU   A 1 82 ? 10.415  -19.047 7.467   1.00 23.68  ? 81  LEU   A O   1 
ATOM   647  C CB  . LEU   A 1 82 ? 8.047   -21.095 8.257   1.00 27.35  ? 81  LEU   A CB  1 
ATOM   648  C CG  . LEU   A 1 82 ? 6.572   -21.513 8.148   1.00 28.20  ? 81  LEU   A CG  1 
ATOM   649  C CD1 . LEU   A 1 82 ? 6.234   -22.150 9.486   1.00 30.98  ? 81  LEU   A CD1 1 
ATOM   650  C CD2 . LEU   A 1 82 ? 5.715   -20.295 7.952   1.00 29.37  ? 81  LEU   A CD2 1 
ATOM   651  N N   . TRP   A 1 83 ? 11.108  -21.183 7.192   1.00 24.53  ? 82  TRP   A N   1 
ATOM   652  C CA  . TRP   A 1 83 ? 12.493  -20.785 7.442   1.00 24.55  ? 82  TRP   A CA  1 
ATOM   653  C C   . TRP   A 1 83 ? 12.943  -19.877 6.315   1.00 22.05  ? 82  TRP   A C   1 
ATOM   654  O O   . TRP   A 1 83 ? 13.634  -18.911 6.561   1.00 23.65  ? 82  TRP   A O   1 
ATOM   655  C CB  . TRP   A 1 83 ? 13.443  -22.004 7.585   1.00 22.82  ? 82  TRP   A CB  1 
ATOM   656  C CG  . TRP   A 1 83 ? 14.896  -21.661 7.825   1.00 24.17  ? 82  TRP   A CG  1 
ATOM   657  C CD1 . TRP   A 1 83 ? 15.536  -21.542 9.026   1.00 26.97  ? 82  TRP   A CD1 1 
ATOM   658  C CD2 . TRP   A 1 83 ? 15.858  -21.371 6.803   1.00 24.12  ? 82  TRP   A CD2 1 
ATOM   659  N NE1 . TRP   A 1 83 ? 16.843  -21.210 8.810   1.00 28.34  ? 82  TRP   A NE1 1 
ATOM   660  C CE2 . TRP   A 1 83 ? 17.061  -21.074 7.455   1.00 25.81  ? 82  TRP   A CE2 1 
ATOM   661  C CE3 . TRP   A 1 83 ? 15.795  -21.335 5.407   1.00 25.05  ? 82  TRP   A CE3 1 
ATOM   662  C CZ2 . TRP   A 1 83 ? 18.216  -20.740 6.735   1.00 24.98  ? 82  TRP   A CZ2 1 
ATOM   663  C CZ3 . TRP   A 1 83 ? 16.912  -20.975 4.682   1.00 27.92  ? 82  TRP   A CZ3 1 
ATOM   664  C CH2 . TRP   A 1 83 ? 18.116  -20.685 5.358   1.00 26.26  ? 82  TRP   A CH2 1 
ATOM   665  N N   . GLU   A 1 84 ? 12.645  -20.258 5.071   1.00 22.64  ? 83  GLU   A N   1 
ATOM   666  C CA  . GLU   A 1 84 ? 13.156  -19.509 3.942   1.00 20.25  ? 83  GLU   A CA  1 
ATOM   667  C C   . GLU   A 1 84 ? 12.657  -18.063 3.956   1.00 23.68  ? 83  GLU   A C   1 
ATOM   668  O O   . GLU   A 1 84 ? 13.400  -17.135 3.714   1.00 21.86  ? 83  GLU   A O   1 
ATOM   669  C CB  . GLU   A 1 84 ? 12.745  -20.168 2.640   1.00 21.64  ? 83  GLU   A CB  1 
ATOM   670  C CG  . GLU   A 1 84 ? 13.431  -21.524 2.454   1.00 21.56  ? 83  GLU   A CG  1 
ATOM   671  C CD  . GLU   A 1 84 ? 13.000  -22.281 1.204   1.00 25.12  ? 83  GLU   A CD  1 
ATOM   672  O OE1 . GLU   A 1 84 ? 12.071  -21.856 0.494   1.00 26.97  ? 83  GLU   A OE1 1 
ATOM   673  O OE2 . GLU   A 1 84 ? 13.593  -23.388 0.918   1.00 27.78  ? 83  GLU   A OE2 1 
ATOM   674  N N   . ILE   A 1 85 ? 11.352  -17.879 4.163   1.00 20.45  ? 84  ILE   A N   1 
ATOM   675  C CA  . ILE   A 1 85 ? 10.774  -16.550 4.049   1.00 20.92  ? 84  ILE   A CA  1 
ATOM   676  C C   . ILE   A 1 85 ? 11.321  -15.656 5.172   1.00 21.71  ? 84  ILE   A C   1 
ATOM   677  O O   . ILE   A 1 85 ? 11.489  -14.462 4.957   1.00 22.27  ? 84  ILE   A O   1 
ATOM   678  C CB  . ILE   A 1 85 ? 9.215   -16.600 4.064   1.00 20.72  ? 84  ILE   A CB  1 
ATOM   679  C CG1 . ILE   A 1 85 ? 8.627   -15.239 3.614   1.00 21.27  ? 84  ILE   A CG1 1 
ATOM   680  C CG2 . ILE   A 1 85 ? 8.657   -16.952 5.445   1.00 22.90  ? 84  ILE   A CG2 1 
ATOM   681  C CD1 . ILE   A 1 85 ? 7.183   -15.373 3.100   1.00 20.93  ? 84  ILE   A CD1 1 
ATOM   682  N N   . GLN   A 1 86 ? 11.654  -16.238 6.347   1.00 24.03  ? 85  GLN   A N   1 
ATOM   683  C CA  . GLN   A 1 86 ? 12.190  -15.440 7.452   1.00 22.98  ? 85  GLN   A CA  1 
ATOM   684  C C   . GLN   A 1 86 ? 13.683  -15.187 7.277   1.00 23.65  ? 85  GLN   A C   1 
ATOM   685  O O   . GLN   A 1 86 ? 14.139  -14.085 7.673   1.00 25.73  ? 85  GLN   A O   1 
ATOM   686  C CB  . GLN   A 1 86 ? 11.823  -16.159 8.753   1.00 27.93  ? 85  GLN   A CB  1 
ATOM   687  C CG  . GLN   A 1 86 ? 12.378  -15.498 10.010  1.00 34.87  ? 85  GLN   A CG  1 
ATOM   688  C CD  . GLN   A 1 86 ? 11.701  -16.052 11.251  1.00 41.38  ? 85  GLN   A CD  1 
ATOM   689  O OE1 . GLN   A 1 86 ? 11.412  -17.259 11.349  1.00 39.82  ? 85  GLN   A OE1 1 
ATOM   690  N NE2 . GLN   A 1 86 ? 11.414  -15.167 12.197  1.00 46.33  ? 85  GLN   A NE2 1 
ATOM   691  N N   . ASN   A 1 87 ? 14.421  -16.197 6.756   1.00 21.09  ? 86  ASN   A N   1 
ATOM   692  C CA  . ASN   A 1 87 ? 15.887  -16.214 6.850   1.00 23.34  ? 86  ASN   A CA  1 
ATOM   693  C C   . ASN   A 1 87 ? 16.613  -15.888 5.546   1.00 25.07  ? 86  ASN   A C   1 
ATOM   694  O O   . ASN   A 1 87 ? 17.706  -15.324 5.590   1.00 26.32  ? 86  ASN   A O   1 
ATOM   695  C CB  . ASN   A 1 87 ? 16.390  -17.501 7.500   1.00 25.92  ? 86  ASN   A CB  1 
ATOM   696  C CG  . ASN   A 1 87 ? 15.938  -17.562 8.938   1.00 28.68  ? 86  ASN   A CG  1 
ATOM   697  O OD1 . ASN   A 1 87 ? 16.315  -16.676 9.720   1.00 30.85  ? 86  ASN   A OD1 1 
ATOM   698  N ND2 . ASN   A 1 87 ? 14.987  -18.429 9.265   1.00 26.66  ? 86  ASN   A ND2 1 
ATOM   699  N N   . ASN   A 1 88 ? 16.073  -16.227 4.373   1.00 22.81  ? 87  ASN   A N   1 
ATOM   700  C CA  . ASN   A 1 88 ? 16.691  -15.831 3.111   1.00 21.12  ? 87  ASN   A CA  1 
ATOM   701  C C   . ASN   A 1 88 ? 15.622  -15.814 2.020   1.00 22.21  ? 87  ASN   A C   1 
ATOM   702  O O   . ASN   A 1 88 ? 15.642  -16.562 1.035   1.00 22.49  ? 87  ASN   A O   1 
ATOM   703  C CB  . ASN   A 1 88 ? 17.843  -16.784 2.737   1.00 24.91  ? 87  ASN   A CB  1 
ATOM   704  C CG  . ASN   A 1 88 ? 18.909  -16.133 1.879   1.00 25.12  ? 87  ASN   A CG  1 
ATOM   705  O OD1 . ASN   A 1 88 ? 18.687  -15.149 1.181   1.00 23.20  ? 87  ASN   A OD1 1 
ATOM   706  N ND2 . ASN   A 1 88 ? 20.128  -16.701 1.864   1.00 28.47  ? 87  ASN   A ND2 1 
ATOM   707  N N   . PRO   A 1 89 ? 14.698  -14.839 2.112   1.00 21.66  ? 88  PRO   A N   1 
ATOM   708  C CA  . PRO   A 1 89 ? 13.547  -14.819 1.202   1.00 19.96  ? 88  PRO   A CA  1 
ATOM   709  C C   . PRO   A 1 89 ? 13.897  -14.371 -0.205  1.00 22.89  ? 88  PRO   A C   1 
ATOM   710  O O   . PRO   A 1 89 ? 13.088  -14.602 -1.095  1.00 22.39  ? 88  PRO   A O   1 
ATOM   711  C CB  . PRO   A 1 89 ? 12.617  -13.844 1.844   1.00 20.52  ? 88  PRO   A CB  1 
ATOM   712  C CG  . PRO   A 1 89 ? 13.523  -12.896 2.585   1.00 20.48  ? 88  PRO   A CG  1 
ATOM   713  C CD  . PRO   A 1 89 ? 14.670  -13.795 3.125   1.00 21.48  ? 88  PRO   A CD  1 
ATOM   714  N N   . HIS   A 1 90 ? 15.135  -13.826 -0.430  1.00 19.82  ? 89  HIS   A N   1 
ATOM   715  C CA  . HIS   A 1 90 ? 15.447  -13.318 -1.754  1.00 20.34  ? 89  HIS   A CA  1 
ATOM   716  C C   . HIS   A 1 90 ? 16.573  -14.117 -2.439  1.00 20.20  ? 89  HIS   A C   1 
ATOM   717  O O   . HIS   A 1 90 ? 17.046  -13.719 -3.500  1.00 23.24  ? 89  HIS   A O   1 
ATOM   718  C CB  . HIS   A 1 90 ? 15.839  -11.838 -1.656  1.00 20.31  ? 89  HIS   A CB  1 
ATOM   719  C CG  . HIS   A 1 90 ? 14.795  -10.953 -1.068  1.00 19.65  ? 89  HIS   A CG  1 
ATOM   720  N ND1 . HIS   A 1 90 ? 13.532  -10.906 -1.640  1.00 21.72  ? 89  HIS   A ND1 1 
ATOM   721  C CD2 . HIS   A 1 90 ? 14.771  -10.198 0.023   1.00 21.89  ? 89  HIS   A CD2 1 
ATOM   722  C CE1 . HIS   A 1 90 ? 12.765  -10.086 -0.928  1.00 21.34  ? 89  HIS   A CE1 1 
ATOM   723  N NE2 . HIS   A 1 90 ? 13.490  -9.638  0.107   1.00 22.61  ? 89  HIS   A NE2 1 
ATOM   724  N N   . ALA   A 1 91 ? 16.815  -15.313 -1.912  1.00 21.64  ? 90  ALA   A N   1 
ATOM   725  C CA  . ALA   A 1 91 ? 17.867  -16.180 -2.448  1.00 23.03  ? 90  ALA   A CA  1 
ATOM   726  C C   . ALA   A 1 91 ? 17.398  -16.894 -3.704  1.00 27.96  ? 90  ALA   A C   1 
ATOM   727  O O   . ALA   A 1 91 ? 16.217  -17.006 -4.002  1.00 25.51  ? 90  ALA   A O   1 
ATOM   728  C CB  . ALA   A 1 91 ? 18.323  -17.155 -1.411  1.00 25.68  ? 90  ALA   A CB  1 
ATOM   729  N N   . SER   A 1 92 ? 18.389  -17.367 -4.448  1.00 27.55  ? 91  SER   A N   1 
ATOM   730  C CA  . SER   A 1 92 ? 18.137  -18.310 -5.508  1.00 31.69  ? 91  SER   A CA  1 
ATOM   731  C C   . SER   A 1 92 ? 17.887  -19.700 -4.928  1.00 31.50  ? 91  SER   A C   1 
ATOM   732  O O   . SER   A 1 92 ? 18.743  -20.250 -4.213  1.00 34.61  ? 91  SER   A O   1 
ATOM   733  C CB  . SER   A 1 92 ? 19.309  -18.324 -6.428  1.00 33.99  ? 91  SER   A CB  1 
ATOM   734  O OG  . SER   A 1 92 ? 19.032  -19.316 -7.396  1.00 40.63  ? 91  SER   A OG  1 
ATOM   735  N N   . TYR   A 1 93 ? 16.736  -20.284 -5.294  1.00 27.82  ? 92  TYR   A N   1 
ATOM   736  C CA  . TYR   A 1 93 ? 16.349  -21.612 -4.859  1.00 33.07  ? 92  TYR   A CA  1 
ATOM   737  C C   . TYR   A 1 93 ? 16.244  -22.540 -6.067  1.00 38.66  ? 92  TYR   A C   1 
ATOM   738  O O   . TYR   A 1 93 ? 15.690  -23.630 -5.946  1.00 40.71  ? 92  TYR   A O   1 
ATOM   739  C CB  . TYR   A 1 93 ? 15.015  -21.589 -4.098  1.00 29.20  ? 92  TYR   A CB  1 
ATOM   740  C CG  . TYR   A 1 93 ? 15.144  -20.986 -2.714  1.00 28.68  ? 92  TYR   A CG  1 
ATOM   741  C CD1 . TYR   A 1 93 ? 15.557  -21.750 -1.616  1.00 26.87  ? 92  TYR   A CD1 1 
ATOM   742  C CD2 . TYR   A 1 93 ? 14.856  -19.638 -2.507  1.00 27.19  ? 92  TYR   A CD2 1 
ATOM   743  C CE1 . TYR   A 1 93 ? 15.727  -21.175 -0.361  1.00 30.75  ? 92  TYR   A CE1 1 
ATOM   744  C CE2 . TYR   A 1 93 ? 14.974  -19.082 -1.251  1.00 27.42  ? 92  TYR   A CE2 1 
ATOM   745  C CZ  . TYR   A 1 93 ? 15.387  -19.842 -0.177  1.00 27.53  ? 92  TYR   A CZ  1 
ATOM   746  O OH  . TYR   A 1 93 ? 15.614  -19.286 1.042   1.00 30.06  ? 92  TYR   A OH  1 
ATOM   747  N N   . SER   A 1 94 ? 16.736  -22.086 -7.219  1.00 43.50  ? 93  SER   A N   1 
ATOM   748  C CA  . SER   A 1 94 ? 16.989  -22.987 -8.336  1.00 59.85  ? 93  SER   A CA  1 
ATOM   749  C C   . SER   A 1 94 ? 17.977  -24.078 -7.884  1.00 66.01  ? 93  SER   A C   1 
ATOM   750  O O   . SER   A 1 94 ? 19.138  -23.709 -7.595  1.00 70.41  ? 93  SER   A O   1 
ATOM   751  C CB  . SER   A 1 94 ? 17.512  -22.222 -9.527  1.00 57.96  ? 93  SER   A CB  1 
ATOM   752  O OG  . SER   A 1 94 ? 16.730  -21.056 -9.746  1.00 66.44  ? 93  SER   A OG  1 
ATOM   753  O OXT . SER   A 1 94 ? 17.550  -25.258 -7.799  1.00 73.22  ? 93  SER   A OXT 1 
ATOM   754  N N   . MET   B 1 2  ? 38.835  -11.507 -42.028 1.00 48.16  ? 1   MET   B N   1 
ATOM   755  C CA  . MET   B 1 2  ? 38.463  -12.232 -43.273 1.00 51.81  ? 1   MET   B CA  1 
ATOM   756  C C   . MET   B 1 2  ? 36.942  -12.336 -43.312 1.00 47.04  ? 1   MET   B C   1 
ATOM   757  O O   . MET   B 1 2  ? 36.320  -12.492 -42.259 1.00 50.02  ? 1   MET   B O   1 
ATOM   758  C CB  . MET   B 1 2  ? 39.086  -13.637 -43.325 1.00 53.21  ? 1   MET   B CB  1 
ATOM   759  C CG  . MET   B 1 2  ? 39.078  -14.285 -44.717 1.00 64.25  ? 1   MET   B CG  1 
ATOM   760  S SD  . MET   B 1 2  ? 40.478  -13.956 -45.820 1.00 66.74  ? 1   MET   B SD  1 
ATOM   761  C CE  . MET   B 1 2  ? 41.153  -12.488 -45.030 1.00 37.63  ? 1   MET   B CE  1 
ATOM   762  N N   . PRO   B 1 3  ? 36.290  -12.191 -44.495 1.00 42.71  ? 2   PRO   B N   1 
ATOM   763  C CA  . PRO   B 1 3  ? 34.845  -12.433 -44.600 1.00 41.52  ? 2   PRO   B CA  1 
ATOM   764  C C   . PRO   B 1 3  ? 34.529  -13.882 -44.231 1.00 44.85  ? 2   PRO   B C   1 
ATOM   765  O O   . PRO   B 1 3  ? 35.288  -14.780 -44.566 1.00 42.35  ? 2   PRO   B O   1 
ATOM   766  C CB  . PRO   B 1 3  ? 34.497  -12.112 -46.057 1.00 44.39  ? 2   PRO   B CB  1 
ATOM   767  C CG  . PRO   B 1 3  ? 35.649  -11.218 -46.503 1.00 39.03  ? 2   PRO   B CG  1 
ATOM   768  C CD  . PRO   B 1 3  ? 36.881  -11.731 -45.761 1.00 39.93  ? 2   PRO   B CD  1 
ATOM   769  N N   . HIS   B 1 4  ? 33.415  -14.087 -43.514 1.00 39.36  ? 3   HIS   B N   1 
ATOM   770  C CA  . HIS   B 1 4  ? 32.983  -15.426 -43.136 1.00 40.57  ? 3   HIS   B CA  1 
ATOM   771  C C   . HIS   B 1 4  ? 31.606  -15.680 -43.736 1.00 39.26  ? 3   HIS   B C   1 
ATOM   772  O O   . HIS   B 1 4  ? 31.026  -14.789 -44.366 1.00 36.61  ? 3   HIS   B O   1 
ATOM   773  C CB  . HIS   B 1 4  ? 33.085  -15.615 -41.621 1.00 48.94  ? 3   HIS   B CB  1 
ATOM   774  C CG  . HIS   B 1 4  ? 34.500  -15.695 -41.153 1.00 59.78  ? 3   HIS   B CG  1 
ATOM   775  N ND1 . HIS   B 1 4  ? 35.419  -16.547 -41.734 1.00 58.76  ? 3   HIS   B ND1 1 
ATOM   776  C CD2 . HIS   B 1 4  ? 35.151  -15.057 -40.163 1.00 59.98  ? 3   HIS   B CD2 1 
ATOM   777  C CE1 . HIS   B 1 4  ? 36.586  -16.418 -41.112 1.00 60.19  ? 3   HIS   B CE1 1 
ATOM   778  N NE2 . HIS   B 1 4  ? 36.449  -15.512 -40.162 1.00 61.25  ? 3   HIS   B NE2 1 
ATOM   779  N N   . ALA   B 1 5  ? 31.082  -16.903 -43.564 1.00 35.42  ? 4   ALA   B N   1 
ATOM   780  C CA  . ALA   B 1 5  ? 29.784  -17.205 -44.144 1.00 37.40  ? 4   ALA   B CA  1 
ATOM   781  C C   . ALA   B 1 5  ? 28.767  -16.194 -43.627 1.00 37.53  ? 4   ALA   B C   1 
ATOM   782  O O   . ALA   B 1 5  ? 27.877  -15.769 -44.361 1.00 39.05  ? 4   ALA   B O   1 
ATOM   783  C CB  . ALA   B 1 5  ? 29.357  -18.603 -43.769 1.00 35.67  ? 4   ALA   B CB  1 
ATOM   784  N N   . PHE   B 1 6  ? 28.883  -15.869 -42.338 1.00 38.59  ? 5   PHE   B N   1 
ATOM   785  C CA  . PHE   B 1 6  ? 28.047  -14.854 -41.708 1.00 38.18  ? 5   PHE   B CA  1 
ATOM   786  C C   . PHE   B 1 6  ? 28.836  -13.558 -41.483 1.00 33.98  ? 5   PHE   B C   1 
ATOM   787  O O   . PHE   B 1 6  ? 29.967  -13.574 -40.999 1.00 37.25  ? 5   PHE   B O   1 
ATOM   788  C CB  . PHE   B 1 6  ? 27.465  -15.304 -40.358 1.00 36.08  ? 5   PHE   B CB  1 
ATOM   789  C CG  . PHE   B 1 6  ? 26.357  -16.348 -40.420 1.00 34.38  ? 5   PHE   B CG  1 
ATOM   790  C CD1 . PHE   B 1 6  ? 25.027  -15.977 -40.601 1.00 34.54  ? 5   PHE   B CD1 1 
ATOM   791  C CD2 . PHE   B 1 6  ? 26.650  -17.705 -40.326 1.00 39.39  ? 5   PHE   B CD2 1 
ATOM   792  C CE1 . PHE   B 1 6  ? 24.026  -16.942 -40.682 1.00 34.89  ? 5   PHE   B CE1 1 
ATOM   793  C CE2 . PHE   B 1 6  ? 25.636  -18.655 -40.394 1.00 30.61  ? 5   PHE   B CE2 1 
ATOM   794  C CZ  . PHE   B 1 6  ? 24.327  -18.277 -40.546 1.00 33.62  ? 5   PHE   B CZ  1 
ATOM   795  N N   . LYS   B 1 7  ? 28.222  -12.435 -41.838 1.00 38.17  ? 6   LYS   B N   1 
ATOM   796  C CA  . LYS   B 1 7  ? 28.919  -11.167 -41.664 1.00 34.41  ? 6   LYS   B CA  1 
ATOM   797  C C   . LYS   B 1 7  ? 28.188  -10.323 -40.616 1.00 36.39  ? 6   LYS   B C   1 
ATOM   798  O O   . LYS   B 1 7  ? 26.977  -10.459 -40.421 1.00 31.25  ? 6   LYS   B O   1 
ATOM   799  C CB  . LYS   B 1 7  ? 29.020  -10.458 -43.014 1.00 41.46  ? 6   LYS   B CB  1 
ATOM   800  C CG  . LYS   B 1 7  ? 27.727  -9.973  -43.621 1.00 44.50  ? 6   LYS   B CG  1 
ATOM   801  C CD  . LYS   B 1 7  ? 27.930  -9.633  -45.100 1.00 45.18  ? 6   LYS   B CD  1 
ATOM   802  C CE  . LYS   B 1 7  ? 26.655  -9.281  -45.788 1.00 48.62  ? 6   LYS   B CE  1 
ATOM   803  N NZ  . LYS   B 1 7  ? 25.773  -10.453 -45.870 1.00 49.49  ? 6   LYS   B NZ  1 
ATOM   804  N N   . PRO   B 1 8  ? 28.888  -9.370  -39.961 1.00 39.08  ? 7   PRO   B N   1 
ATOM   805  C CA  . PRO   B 1 8  ? 28.258  -8.457  -38.995 1.00 31.87  ? 7   PRO   B CA  1 
ATOM   806  C C   . PRO   B 1 8  ? 27.089  -7.720  -39.625 1.00 36.64  ? 7   PRO   B C   1 
ATOM   807  O O   . PRO   B 1 8  ? 27.197  -7.221  -40.757 1.00 38.24  ? 7   PRO   B O   1 
ATOM   808  C CB  . PRO   B 1 8  ? 29.435  -7.506  -38.719 1.00 39.16  ? 7   PRO   B CB  1 
ATOM   809  C CG  . PRO   B 1 8  ? 30.644  -8.389  -38.874 1.00 37.91  ? 7   PRO   B CG  1 
ATOM   810  C CD  . PRO   B 1 8  ? 30.321  -9.071  -40.177 1.00 39.72  ? 7   PRO   B CD  1 
ATOM   811  N N   . GLY   B 1 9  ? 25.958  -7.710  -38.907 1.00 29.64  ? 8   GLY   B N   1 
ATOM   812  C CA  . GLY   B 1 9  ? 24.743  -7.101  -39.394 1.00 30.26  ? 8   GLY   B CA  1 
ATOM   813  C C   . GLY   B 1 9  ? 23.809  -8.105  -40.058 1.00 28.32  ? 8   GLY   B C   1 
ATOM   814  O O   . GLY   B 1 9  ? 22.671  -7.755  -40.342 1.00 30.42  ? 8   GLY   B O   1 
ATOM   815  N N   . ASP   B 1 10 ? 24.278  -9.339  -40.343 1.00 30.54  ? 9   ASP   B N   1 
ATOM   816  C CA  . ASP   B 1 10 ? 23.340  -10.331 -40.856 1.00 32.05  ? 9   ASP   B CA  1 
ATOM   817  C C   . ASP   B 1 10 ? 22.265  -10.625 -39.797 1.00 25.82  ? 9   ASP   B C   1 
ATOM   818  O O   . ASP   B 1 10 ? 22.557  -10.662 -38.597 1.00 29.23  ? 9   ASP   B O   1 
ATOM   819  C CB  . ASP   B 1 10 ? 24.020  -11.633 -41.232 1.00 33.32  ? 9   ASP   B CB  1 
ATOM   820  C CG  . ASP   B 1 10 ? 24.760  -11.684 -42.562 1.00 36.33  ? 9   ASP   B CG  1 
ATOM   821  O OD1 . ASP   B 1 10 ? 24.437  -10.855 -43.427 1.00 35.05  ? 9   ASP   B OD1 1 
ATOM   822  O OD2 . ASP   B 1 10 ? 25.624  -12.583 -42.705 1.00 36.60  ? 9   ASP   B OD2 1 
ATOM   823  N N   . LEU   B 1 11 ? 21.043  -10.813 -40.263 1.00 27.18  ? 10  LEU   B N   1 
ATOM   824  C CA  . LEU   B 1 11 ? 19.946  -11.024 -39.335 1.00 27.60  ? 10  LEU   B CA  1 
ATOM   825  C C   . LEU   B 1 11 ? 19.637  -12.515 -39.330 1.00 26.38  ? 10  LEU   B C   1 
ATOM   826  O O   . LEU   B 1 11 ? 19.668  -13.140 -40.396 1.00 30.04  ? 10  LEU   B O   1 
ATOM   827  C CB  . LEU   B 1 11 ? 18.741  -10.198 -39.759 1.00 27.80  ? 10  LEU   B CB  1 
ATOM   828  C CG  . LEU   B 1 11 ? 19.038  -8.695  -39.878 1.00 26.25  ? 10  LEU   B CG  1 
ATOM   829  C CD1 . LEU   B 1 11 ? 17.712  -8.029  -40.237 1.00 30.63  ? 10  LEU   B CD1 1 
ATOM   830  C CD2 . LEU   B 1 11 ? 19.717  -8.199  -38.609 1.00 27.02  ? 10  LEU   B CD2 1 
ATOM   831  N N   . VAL   B 1 12 ? 19.309  -13.056 -38.144 1.00 24.51  ? 11  VAL   B N   1 
ATOM   832  C CA  . VAL   B 1 12 ? 19.118  -14.504 -38.034 1.00 25.24  ? 11  VAL   B CA  1 
ATOM   833  C C   . VAL   B 1 12 ? 18.029  -14.768 -37.004 1.00 26.07  ? 11  VAL   B C   1 
ATOM   834  O O   . VAL   B 1 12 ? 17.597  -13.863 -36.289 1.00 24.96  ? 11  VAL   B O   1 
ATOM   835  C CB  . VAL   B 1 12 ? 20.401  -15.222 -37.575 1.00 24.03  ? 11  VAL   B CB  1 
ATOM   836  C CG1 . VAL   B 1 12 ? 21.550  -15.035 -38.594 1.00 28.51  ? 11  VAL   B CG1 1 
ATOM   837  C CG2 . VAL   B 1 12 ? 20.858  -14.822 -36.153 1.00 26.14  ? 11  VAL   B CG2 1 
ATOM   838  N N   . PHE   B 1 13 ? 17.597  -16.046 -36.950 1.00 25.68  ? 12  PHE   B N   1 
ATOM   839  C CA  . PHE   B 1 13 ? 17.101  -16.585 -35.693 1.00 24.34  ? 12  PHE   B CA  1 
ATOM   840  C C   . PHE   B 1 13 ? 18.186  -17.476 -35.120 1.00 24.77  ? 12  PHE   B C   1 
ATOM   841  O O   . PHE   B 1 13 ? 18.814  -18.252 -35.877 1.00 27.17  ? 12  PHE   B O   1 
ATOM   842  C CB  . PHE   B 1 13 ? 15.831  -17.414 -35.917 1.00 22.54  ? 12  PHE   B CB  1 
ATOM   843  C CG  . PHE   B 1 13 ? 14.631  -16.579 -36.339 1.00 25.09  ? 12  PHE   B CG  1 
ATOM   844  C CD1 . PHE   B 1 13 ? 14.421  -16.256 -37.676 1.00 27.63  ? 12  PHE   B CD1 1 
ATOM   845  C CD2 . PHE   B 1 13 ? 13.727  -16.097 -35.393 1.00 28.38  ? 12  PHE   B CD2 1 
ATOM   846  C CE1 . PHE   B 1 13 ? 13.330  -15.490 -38.059 1.00 31.14  ? 12  PHE   B CE1 1 
ATOM   847  C CE2 . PHE   B 1 13 ? 12.641  -15.322 -35.780 1.00 28.18  ? 12  PHE   B CE2 1 
ATOM   848  C CZ  . PHE   B 1 13 ? 12.443  -15.025 -37.122 1.00 32.30  ? 12  PHE   B CZ  1 
ATOM   849  N N   . ALA   B 1 14 ? 18.372  -17.345 -33.787 1.00 24.30  ? 13  ALA   B N   1 
ATOM   850  C CA  . ALA   B 1 14 ? 19.441  -18.019 -33.088 1.00 25.11  ? 13  ALA   B CA  1 
ATOM   851  C C   . ALA   B 1 14 ? 18.820  -18.963 -32.059 1.00 24.77  ? 13  ALA   B C   1 
ATOM   852  O O   . ALA   B 1 14 ? 17.931  -18.582 -31.310 1.00 25.35  ? 13  ALA   B O   1 
ATOM   853  C CB  . ALA   B 1 14 ? 20.334  -16.994 -32.423 1.00 26.23  ? 13  ALA   B CB  1 
ATOM   854  N N   . LYS   B 1 15 ? 19.286  -20.208 -32.054 1.00 25.06  ? 14  LYS   B N   1 
ATOM   855  C CA  . LYS   B 1 15 ? 18.689  -21.249 -31.222 1.00 28.06  ? 14  LYS   B CA  1 
ATOM   856  C C   . LYS   B 1 15 ? 19.570  -21.558 -30.018 1.00 29.06  ? 14  LYS   B C   1 
ATOM   857  O O   . LYS   B 1 15 ? 20.752  -21.873 -30.137 1.00 31.62  ? 14  LYS   B O   1 
ATOM   858  C CB  . LYS   B 1 15 ? 18.434  -22.502 -32.071 1.00 28.98  ? 14  LYS   B CB  1 
ATOM   859  C CG  . LYS   B 1 15 ? 17.736  -23.650 -31.287 1.00 26.40  ? 14  LYS   B CG  1 
ATOM   860  C CD  . LYS   B 1 15 ? 16.268  -23.306 -31.064 1.00 28.68  ? 14  LYS   B CD  1 
ATOM   861  C CE  . LYS   B 1 15 ? 15.476  -24.419 -30.332 1.00 30.94  ? 14  LYS   B CE  1 
ATOM   862  N NZ  . LYS   B 1 15 ? 15.961  -24.630 -28.974 1.00 30.46  ? 14  LYS   B NZ  1 
ATOM   863  N N   . MET   B 1 16 ? 18.950  -21.475 -28.840 1.00 29.76  ? 15  MET   B N   1 
ATOM   864  C CA  . MET   B 1 16 ? 19.543  -21.822 -27.547 1.00 30.63  ? 15  MET   B CA  1 
ATOM   865  C C   . MET   B 1 16 ? 18.668  -22.895 -26.897 1.00 29.19  ? 15  MET   B C   1 
ATOM   866  O O   . MET   B 1 16 ? 17.427  -22.873 -26.998 1.00 29.50  ? 15  MET   B O   1 
ATOM   867  C CB  . MET   B 1 16 ? 19.589  -20.606 -26.618 1.00 35.40  ? 15  MET   B CB  1 
ATOM   868  C CG  . MET   B 1 16 ? 20.367  -19.400 -27.116 1.00 40.09  ? 15  MET   B CG  1 
ATOM   869  S SD  . MET   B 1 16 ? 22.156  -19.356 -26.891 1.00 48.71  ? 15  MET   B SD  1 
ATOM   870  C CE  . MET   B 1 16 ? 22.560  -19.756 -25.189 1.00 50.59  ? 15  MET   B CE  1 
ATOM   871  N N   . LYS   B 1 17 ? 19.321  -23.840 -26.217 1.00 31.00  ? 16  LYS   B N   1 
ATOM   872  C CA  . LYS   B 1 17 ? 18.593  -24.845 -25.455 1.00 33.32  ? 16  LYS   B CA  1 
ATOM   873  C C   . LYS   B 1 17 ? 17.614  -24.171 -24.487 1.00 32.85  ? 16  LYS   B C   1 
ATOM   874  O O   . LYS   B 1 17 ? 17.951  -23.216 -23.788 1.00 33.83  ? 16  LYS   B O   1 
ATOM   875  C CB  . LYS   B 1 17 ? 19.620  -25.687 -24.683 1.00 41.56  ? 16  LYS   B CB  1 
ATOM   876  C CG  . LYS   B 1 17 ? 19.126  -27.044 -24.176 1.00 49.16  ? 16  LYS   B CG  1 
ATOM   877  C CD  . LYS   B 1 17 ? 20.140  -27.756 -23.284 1.00 51.34  ? 16  LYS   B CD  1 
ATOM   878  N N   . GLY   B 1 18 ? 16.367  -24.638 -24.540 1.00 35.00  ? 17  GLY   B N   1 
ATOM   879  C CA  . GLY   B 1 18 ? 15.337  -24.150 -23.636 1.00 35.08  ? 17  GLY   B CA  1 
ATOM   880  C C   . GLY   B 1 18 ? 14.481  -23.034 -24.229 1.00 36.60  ? 17  GLY   B C   1 
ATOM   881  O O   . GLY   B 1 18 ? 13.498  -22.629 -23.610 1.00 35.25  ? 17  GLY   B O   1 
ATOM   882  N N   . TYR   B 1 19 ? 14.855  -22.521 -25.411 1.00 32.64  ? 18  TYR   B N   1 
ATOM   883  C CA  . TYR   B 1 19 ? 14.152  -21.362 -25.941 1.00 31.02  ? 18  TYR   B CA  1 
ATOM   884  C C   . TYR   B 1 19 ? 13.827  -21.568 -27.413 1.00 28.10  ? 18  TYR   B C   1 
ATOM   885  O O   . TYR   B 1 19 ? 14.551  -22.257 -28.141 1.00 31.25  ? 18  TYR   B O   1 
ATOM   886  C CB  . TYR   B 1 19 ? 15.094  -20.159 -25.833 1.00 27.76  ? 18  TYR   B CB  1 
ATOM   887  C CG  . TYR   B 1 19 ? 15.467  -19.852 -24.390 1.00 30.07  ? 18  TYR   B CG  1 
ATOM   888  C CD1 . TYR   B 1 19 ? 14.575  -19.125 -23.600 1.00 36.15  ? 18  TYR   B CD1 1 
ATOM   889  C CD2 . TYR   B 1 19 ? 16.650  -20.331 -23.821 1.00 30.35  ? 18  TYR   B CD2 1 
ATOM   890  C CE1 . TYR   B 1 19 ? 14.866  -18.849 -22.276 1.00 34.31  ? 18  TYR   B CE1 1 
ATOM   891  C CE2 . TYR   B 1 19 ? 16.942  -20.052 -22.490 1.00 34.39  ? 18  TYR   B CE2 1 
ATOM   892  C CZ  . TYR   B 1 19 ? 16.049  -19.310 -21.735 1.00 35.55  ? 18  TYR   B CZ  1 
ATOM   893  O OH  . TYR   B 1 19 ? 16.347  -19.040 -20.427 1.00 40.58  ? 18  TYR   B OH  1 
ATOM   894  N N   . PRO   B 1 20 ? 12.751  -20.924 -27.904 1.00 26.88  ? 19  PRO   B N   1 
ATOM   895  C CA  . PRO   B 1 20 ? 12.420  -20.955 -29.325 1.00 27.28  ? 19  PRO   B CA  1 
ATOM   896  C C   . PRO   B 1 20 ? 13.524  -20.225 -30.092 1.00 26.08  ? 19  PRO   B C   1 
ATOM   897  O O   . PRO   B 1 20 ? 14.152  -19.322 -29.555 1.00 26.63  ? 19  PRO   B O   1 
ATOM   898  C CB  . PRO   B 1 20 ? 11.091  -20.234 -29.406 1.00 27.43  ? 19  PRO   B CB  1 
ATOM   899  C CG  . PRO   B 1 20 ? 11.128  -19.282 -28.216 1.00 27.47  ? 19  PRO   B CG  1 
ATOM   900  C CD  . PRO   B 1 20 ? 11.916  -19.987 -27.128 1.00 26.95  ? 19  PRO   B CD  1 
ATOM   901  N N   . HIS   B 1 21 ? 13.654  -20.579 -31.383 1.00 25.39  ? 20  HIS   B N   1 
ATOM   902  C CA  . HIS   B 1 21 ? 14.519  -19.827 -32.294 1.00 25.72  ? 20  HIS   B CA  1 
ATOM   903  C C   . HIS   B 1 21 ? 14.258  -18.330 -32.113 1.00 25.46  ? 20  HIS   B C   1 
ATOM   904  O O   . HIS   B 1 21 ? 13.116  -17.879 -32.210 1.00 26.23  ? 20  HIS   B O   1 
ATOM   905  C CB  . HIS   B 1 21 ? 14.267  -20.302 -33.733 1.00 25.43  ? 20  HIS   B CB  1 
ATOM   906  C CG  . HIS   B 1 21 ? 14.493  -21.783 -33.933 1.00 27.14  ? 20  HIS   B CG  1 
ATOM   907  N ND1 . HIS   B 1 21 ? 13.519  -22.701 -33.541 1.00 29.40  ? 20  HIS   B ND1 1 
ATOM   908  C CD2 . HIS   B 1 21 ? 15.494  -22.498 -34.467 1.00 27.16  ? 20  HIS   B CD2 1 
ATOM   909  C CE1 . HIS   B 1 21 ? 13.952  -23.932 -33.827 1.00 29.97  ? 20  HIS   B CE1 1 
ATOM   910  N NE2 . HIS   B 1 21 ? 15.144  -23.845 -34.410 1.00 28.21  ? 20  HIS   B NE2 1 
ATOM   911  N N   . TRP   B 1 22 ? 15.326  -17.556 -31.934 1.00 25.11  ? 21  TRP   B N   1 
ATOM   912  C CA  . TRP   B 1 22 ? 15.130  -16.223 -31.350 1.00 22.95  ? 21  TRP   B CA  1 
ATOM   913  C C   . TRP   B 1 22 ? 15.652  -15.146 -32.302 1.00 23.31  ? 21  TRP   B C   1 
ATOM   914  O O   . TRP   B 1 22 ? 16.784  -15.267 -32.752 1.00 24.33  ? 21  TRP   B O   1 
ATOM   915  C CB  . TRP   B 1 22 ? 15.859  -16.147 -29.998 1.00 24.68  ? 21  TRP   B CB  1 
ATOM   916  C CG  . TRP   B 1 22 ? 15.374  -15.004 -29.127 1.00 25.90  ? 21  TRP   B CG  1 
ATOM   917  C CD1 . TRP   B 1 22 ? 15.642  -13.666 -29.261 1.00 26.31  ? 21  TRP   B CD1 1 
ATOM   918  C CD2 . TRP   B 1 22 ? 14.465  -15.099 -27.988 1.00 27.65  ? 21  TRP   B CD2 1 
ATOM   919  N NE1 . TRP   B 1 22 ? 14.966  -12.930 -28.307 1.00 28.07  ? 21  TRP   B NE1 1 
ATOM   920  C CE2 . TRP   B 1 22 ? 14.234  -13.785 -27.518 1.00 27.04  ? 21  TRP   B CE2 1 
ATOM   921  C CE3 . TRP   B 1 22 ? 13.824  -16.177 -27.343 1.00 27.79  ? 21  TRP   B CE3 1 
ATOM   922  C CZ2 . TRP   B 1 22 ? 13.392  -13.477 -26.439 1.00 26.69  ? 21  TRP   B CZ2 1 
ATOM   923  C CZ3 . TRP   B 1 22 ? 13.017  -15.879 -26.255 1.00 28.88  ? 21  TRP   B CZ3 1 
ATOM   924  C CH2 . TRP   B 1 22 ? 12.778  -14.557 -25.835 1.00 30.20  ? 21  TRP   B CH2 1 
ATOM   925  N N   . PRO   B 1 23 ? 14.901  -14.054 -32.570 1.00 25.56  ? 22  PRO   B N   1 
ATOM   926  C CA  . PRO   B 1 23 ? 15.354  -13.018 -33.521 1.00 24.71  ? 22  PRO   B CA  1 
ATOM   927  C C   . PRO   B 1 23 ? 16.651  -12.400 -33.013 1.00 24.64  ? 22  PRO   B C   1 
ATOM   928  O O   . PRO   B 1 23 ? 16.789  -12.050 -31.848 1.00 25.01  ? 22  PRO   B O   1 
ATOM   929  C CB  . PRO   B 1 23 ? 14.181  -12.025 -33.515 1.00 24.51  ? 22  PRO   B CB  1 
ATOM   930  C CG  . PRO   B 1 23 ? 13.558  -12.239 -32.139 1.00 25.51  ? 22  PRO   B CG  1 
ATOM   931  C CD  . PRO   B 1 23 ? 13.556  -13.768 -32.049 1.00 25.13  ? 22  PRO   B CD  1 
ATOM   932  N N   . ALA   B 1 24 ? 17.654  -12.288 -33.886 1.00 25.55  ? 23  ALA   B N   1 
ATOM   933  C CA  . ALA   B 1 24 ? 18.978  -11.936 -33.416 1.00 24.79  ? 23  ALA   B CA  1 
ATOM   934  C C   . ALA   B 1 24 ? 19.783  -11.374 -34.601 1.00 22.59  ? 23  ALA   B C   1 
ATOM   935  O O   . ALA   B 1 24 ? 19.318  -11.412 -35.753 1.00 24.24  ? 23  ALA   B O   1 
ATOM   936  C CB  . ALA   B 1 24 ? 19.666  -13.145 -32.770 1.00 25.77  ? 23  ALA   B CB  1 
ATOM   937  N N   . ARG   B 1 25 ? 20.980  -10.881 -34.274 1.00 26.66  ? 24  ARG   B N   1 
ATOM   938  C CA  . ARG   B 1 25 ? 21.886  -10.423 -35.327 1.00 25.65  ? 24  ARG   B CA  1 
ATOM   939  C C   . ARG   B 1 25 ? 23.302  -10.870 -35.007 1.00 26.13  ? 24  ARG   B C   1 
ATOM   940  O O   . ARG   B 1 25 ? 23.634  -11.131 -33.854 1.00 27.29  ? 24  ARG   B O   1 
ATOM   941  C CB  . ARG   B 1 25 ? 21.890  -8.900  -35.441 1.00 24.46  ? 24  ARG   B CB  1 
ATOM   942  C CG  . ARG   B 1 25 ? 22.482  -8.200  -34.236 1.00 24.26  ? 24  ARG   B CG  1 
ATOM   943  C CD  . ARG   B 1 25 ? 22.399  -6.679  -34.474 1.00 26.33  ? 24  ARG   B CD  1 
ATOM   944  N NE  . ARG   B 1 25 ? 22.930  -6.017  -33.282 1.00 27.89  ? 24  ARG   B NE  1 
ATOM   945  C CZ  . ARG   B 1 25 ? 22.663  -4.740  -32.924 1.00 30.78  ? 24  ARG   B CZ  1 
ATOM   946  N NH1 . ARG   B 1 25 ? 21.679  -4.073  -33.534 1.00 28.24  ? 24  ARG   B NH1 1 
ATOM   947  N NH2 . ARG   B 1 25 ? 23.339  -4.200  -31.894 1.00 30.04  ? 24  ARG   B NH2 1 
ATOM   948  N N   . ILE   B 1 26 ? 24.140  -10.937 -36.074 1.00 26.39  ? 25  ILE   B N   1 
ATOM   949  C CA  . ILE   B 1 26 ? 25.567  -11.145 -35.906 1.00 28.91  ? 25  ILE   B CA  1 
ATOM   950  C C   . ILE   B 1 26 ? 26.146  -9.780  -35.559 1.00 31.24  ? 25  ILE   B C   1 
ATOM   951  O O   . ILE   B 1 26 ? 25.845  -8.786  -36.219 1.00 31.27  ? 25  ILE   B O   1 
ATOM   952  C CB  . ILE   B 1 26 ? 26.193  -11.610 -37.239 1.00 32.38  ? 25  ILE   B CB  1 
ATOM   953  C CG1 . ILE   B 1 26 ? 25.470  -12.808 -37.812 1.00 32.26  ? 25  ILE   B CG1 1 
ATOM   954  C CG2 . ILE   B 1 26 ? 27.681  -11.900 -37.041 1.00 33.37  ? 25  ILE   B CG2 1 
ATOM   955  C CD1 . ILE   B 1 26 ? 25.485  -14.021 -36.891 1.00 31.99  ? 25  ILE   B CD1 1 
ATOM   956  N N   . ASP   B 1 27 ? 26.927  -9.745  -34.489 1.00 31.48  ? 26  ASP   B N   1 
ATOM   957  C CA  . ASP   B 1 27 ? 27.513  -8.474  -34.093 1.00 36.01  ? 26  ASP   B CA  1 
ATOM   958  C C   . ASP   B 1 27 ? 28.954  -8.404  -34.591 1.00 39.16  ? 26  ASP   B C   1 
ATOM   959  O O   . ASP   B 1 27 ? 29.526  -9.429  -34.943 1.00 45.10  ? 26  ASP   B O   1 
ATOM   960  C CB  . ASP   B 1 27 ? 27.503  -8.339  -32.587 1.00 31.39  ? 26  ASP   B CB  1 
ATOM   961  C CG  . ASP   B 1 27 ? 26.332  -7.598  -31.963 1.00 39.56  ? 26  ASP   B CG  1 
ATOM   962  O OD1 . ASP   B 1 27 ? 25.490  -7.050  -32.713 1.00 38.09  ? 26  ASP   B OD1 1 
ATOM   963  O OD2 . ASP   B 1 27 ? 26.305  -7.542  -30.713 1.00 36.92  ? 26  ASP   B OD2 1 
ATOM   964  N N   . ASP   B 1 28 ? 29.537  -7.193  -34.566 1.00 50.25  ? 27  ASP   B N   1 
ATOM   965  C CA  . ASP   B 1 28 ? 30.959  -6.993  -34.821 1.00 58.01  ? 27  ASP   B CA  1 
ATOM   966  C C   . ASP   B 1 28 ? 31.729  -7.310  -33.531 1.00 63.37  ? 27  ASP   B C   1 
ATOM   967  O O   . ASP   B 1 28 ? 31.164  -7.210  -32.445 1.00 72.00  ? 27  ASP   B O   1 
ATOM   968  C CB  . ASP   B 1 28 ? 31.211  -5.604  -35.396 1.00 58.79  ? 27  ASP   B CB  1 
ATOM   969  C CG  . ASP   B 1 28 ? 31.995  -5.549  -36.709 1.00 61.85  ? 27  ASP   B CG  1 
ATOM   970  O OD1 . ASP   B 1 28 ? 33.022  -6.259  -36.843 1.00 61.97  ? 27  ASP   B OD1 1 
ATOM   971  O OD2 . ASP   B 1 28 ? 31.586  -4.780  -37.602 1.00 65.14  ? 27  ASP   B OD2 1 
ATOM   972  N N   . ILE   B 1 29 ? 33.008  -7.704  -33.642 1.00 69.44  ? 28  ILE   B N   1 
ATOM   973  C CA  . ILE   B 1 29 ? 33.760  -8.241  -32.511 1.00 70.45  ? 28  ILE   B CA  1 
ATOM   974  C C   . ILE   B 1 29 ? 34.386  -7.102  -31.684 1.00 73.62  ? 28  ILE   B C   1 
ATOM   975  O O   . ILE   B 1 29 ? 34.660  -6.031  -32.278 1.00 75.62  ? 28  ILE   B O   1 
ATOM   976  C CB  . ILE   B 1 29 ? 34.819  -9.263  -32.966 1.00 61.71  ? 28  ILE   B CB  1 
ATOM   977  N N   . VAL   B 1 34 ? 37.207  -9.956  -25.753 1.00 62.10  ? 33  VAL   B N   1 
ATOM   978  C CA  . VAL   B 1 34 ? 36.963  -11.429 -25.707 1.00 62.79  ? 33  VAL   B CA  1 
ATOM   979  C C   . VAL   B 1 34 ? 36.549  -11.850 -27.111 1.00 73.61  ? 33  VAL   B C   1 
ATOM   980  O O   . VAL   B 1 34 ? 35.413  -11.612 -27.513 1.00 85.08  ? 33  VAL   B O   1 
ATOM   981  C CB  . VAL   B 1 34 ? 35.917  -11.827 -24.638 1.00 64.66  ? 33  VAL   B CB  1 
ATOM   982  C CG1 . VAL   B 1 34 ? 34.682  -10.926 -24.647 1.00 62.62  ? 33  VAL   B CG1 1 
ATOM   983  C CG2 . VAL   B 1 34 ? 35.516  -13.299 -24.711 1.00 58.29  ? 33  VAL   B CG2 1 
ATOM   984  N N   . LYS   B 1 35 ? 37.490  -12.426 -27.868 1.00 72.48  ? 34  LYS   B N   1 
ATOM   985  C CA  . LYS   B 1 35 ? 37.190  -12.921 -29.205 1.00 65.07  ? 34  LYS   B CA  1 
ATOM   986  C C   . LYS   B 1 35 ? 36.282  -14.154 -29.089 1.00 63.86  ? 34  LYS   B C   1 
ATOM   987  O O   . LYS   B 1 35 ? 36.348  -14.880 -28.093 1.00 58.60  ? 34  LYS   B O   1 
ATOM   988  C CB  . LYS   B 1 35 ? 38.506  -13.134 -29.964 1.00 62.95  ? 34  LYS   B CB  1 
ATOM   989  N N   . PRO   B 1 36 ? 35.379  -14.433 -30.069 1.00 61.22  ? 35  PRO   B N   1 
ATOM   990  C CA  . PRO   B 1 36 ? 34.478  -15.584 -29.960 1.00 51.37  ? 35  PRO   B CA  1 
ATOM   991  C C   . PRO   B 1 36 ? 35.335  -16.839 -29.916 1.00 46.86  ? 35  PRO   B C   1 
ATOM   992  O O   . PRO   B 1 36 ? 36.436  -16.837 -30.447 1.00 48.80  ? 35  PRO   B O   1 
ATOM   993  C CB  . PRO   B 1 36 ? 33.615  -15.528 -31.234 1.00 49.40  ? 35  PRO   B CB  1 
ATOM   994  C CG  . PRO   B 1 36 ? 34.413  -14.652 -32.191 1.00 56.61  ? 35  PRO   B CG  1 
ATOM   995  C CD  . PRO   B 1 36 ? 35.190  -13.677 -31.320 1.00 56.10  ? 35  PRO   B CD  1 
ATOM   996  N N   . PRO   B 1 37 ? 34.873  -17.946 -29.292 1.00 46.57  ? 36  PRO   B N   1 
ATOM   997  C CA  . PRO   B 1 37 ? 35.580  -19.221 -29.393 1.00 42.83  ? 36  PRO   B CA  1 
ATOM   998  C C   . PRO   B 1 37 ? 35.643  -19.614 -30.863 1.00 47.50  ? 36  PRO   B C   1 
ATOM   999  O O   . PRO   B 1 37 ? 34.892  -19.082 -31.691 1.00 44.79  ? 36  PRO   B O   1 
ATOM   1000 C CB  . PRO   B 1 37 ? 34.762  -20.233 -28.558 1.00 49.63  ? 36  PRO   B CB  1 
ATOM   1001 C CG  . PRO   B 1 37 ? 33.814  -19.383 -27.741 1.00 46.29  ? 36  PRO   B CG  1 
ATOM   1002 C CD  . PRO   B 1 37 ? 33.670  -18.029 -28.446 1.00 48.45  ? 36  PRO   B CD  1 
ATOM   1003 N N   . PRO   B 1 38 ? 36.540  -20.561 -31.229 1.00 46.74  ? 37  PRO   B N   1 
ATOM   1004 C CA  . PRO   B 1 38 ? 36.653  -21.038 -32.617 1.00 46.79  ? 37  PRO   B CA  1 
ATOM   1005 C C   . PRO   B 1 38 ? 35.312  -21.452 -33.231 1.00 45.27  ? 37  PRO   B C   1 
ATOM   1006 O O   . PRO   B 1 38 ? 34.525  -22.142 -32.581 1.00 44.32  ? 37  PRO   B O   1 
ATOM   1007 C CB  . PRO   B 1 38 ? 37.612  -22.259 -32.474 1.00 42.34  ? 37  PRO   B CB  1 
ATOM   1008 C CG  . PRO   B 1 38 ? 38.476  -21.919 -31.260 1.00 48.39  ? 37  PRO   B CG  1 
ATOM   1009 C CD  . PRO   B 1 38 ? 37.509  -21.201 -30.318 1.00 54.14  ? 37  PRO   B CD  1 
ATOM   1010 N N   . ASN   B 1 39 ? 35.069  -21.027 -34.479 1.00 42.68  ? 38  ASN   B N   1 
ATOM   1011 C CA  . ASN   B 1 39 ? 33.911  -21.468 -35.249 1.00 45.89  ? 38  ASN   B CA  1 
ATOM   1012 C C   . ASN   B 1 39 ? 32.645  -20.703 -34.861 1.00 40.32  ? 38  ASN   B C   1 
ATOM   1013 O O   . ASN   B 1 39 ? 31.605  -20.922 -35.461 1.00 42.03  ? 38  ASN   B O   1 
ATOM   1014 C CB  . ASN   B 1 39 ? 33.597  -22.955 -35.081 1.00 44.06  ? 38  ASN   B CB  1 
ATOM   1015 C CG  . ASN   B 1 39 ? 34.767  -23.837 -35.456 1.00 54.06  ? 38  ASN   B CG  1 
ATOM   1016 O OD1 . ASN   B 1 39 ? 35.091  -24.789 -34.734 1.00 58.31  ? 38  ASN   B OD1 1 
ATOM   1017 N ND2 . ASN   B 1 39 ? 35.411  -23.538 -36.574 1.00 45.29  ? 38  ASN   B ND2 1 
ATOM   1018 N N   . LYS   B 1 40 ? 32.704  -19.837 -33.839 1.00 39.69  ? 39  LYS   B N   1 
ATOM   1019 C CA  . LYS   B 1 40 ? 31.491  -19.205 -33.332 1.00 36.74  ? 39  LYS   B CA  1 
ATOM   1020 C C   . LYS   B 1 40 ? 31.436  -17.717 -33.680 1.00 32.19  ? 39  LYS   B C   1 
ATOM   1021 O O   . LYS   B 1 40 ? 32.447  -17.124 -34.027 1.00 36.98  ? 39  LYS   B O   1 
ATOM   1022 C CB  . LYS   B 1 40 ? 31.444  -19.469 -31.829 1.00 34.99  ? 39  LYS   B CB  1 
ATOM   1023 C CG  . LYS   B 1 40 ? 31.172  -20.932 -31.522 1.00 39.11  ? 39  LYS   B CG  1 
ATOM   1024 C CD  . LYS   B 1 40 ? 30.958  -21.005 -30.016 1.00 46.81  ? 39  LYS   B CD  1 
ATOM   1025 C CE  . LYS   B 1 40 ? 29.978  -22.013 -29.512 1.00 61.36  ? 39  LYS   B CE  1 
ATOM   1026 N NZ  . LYS   B 1 40 ? 30.441  -23.358 -29.837 1.00 66.08  ? 39  LYS   B NZ  1 
ATOM   1027 N N   . TYR   B 1 41 ? 30.244  -17.115 -33.561 1.00 32.09  ? 40  TYR   B N   1 
ATOM   1028 C CA  . TYR   B 1 41 ? 29.992  -15.710 -33.851 1.00 31.29  ? 40  TYR   B CA  1 
ATOM   1029 C C   . TYR   B 1 41 ? 29.411  -15.011 -32.624 1.00 36.81  ? 40  TYR   B C   1 
ATOM   1030 O O   . TYR   B 1 41 ? 28.657  -15.618 -31.843 1.00 31.15  ? 40  TYR   B O   1 
ATOM   1031 C CB  . TYR   B 1 41 ? 28.938  -15.573 -34.957 1.00 31.03  ? 40  TYR   B CB  1 
ATOM   1032 C CG  . TYR   B 1 41 ? 29.391  -16.046 -36.333 1.00 32.89  ? 40  TYR   B CG  1 
ATOM   1033 C CD1 . TYR   B 1 41 ? 30.002  -15.174 -37.230 1.00 32.77  ? 40  TYR   B CD1 1 
ATOM   1034 C CD2 . TYR   B 1 41 ? 29.178  -17.361 -36.738 1.00 31.46  ? 40  TYR   B CD2 1 
ATOM   1035 C CE1 . TYR   B 1 41 ? 30.405  -15.607 -38.489 1.00 33.84  ? 40  TYR   B CE1 1 
ATOM   1036 C CE2 . TYR   B 1 41 ? 29.594  -17.817 -37.981 1.00 35.79  ? 40  TYR   B CE2 1 
ATOM   1037 C CZ  . TYR   B 1 41 ? 30.210  -16.927 -38.859 1.00 35.74  ? 40  TYR   B CZ  1 
ATOM   1038 O OH  . TYR   B 1 41 ? 30.593  -17.321 -40.112 1.00 33.93  ? 40  TYR   B OH  1 
ATOM   1039 N N   . PRO   B 1 42 ? 29.676  -13.690 -32.458 1.00 36.30  ? 41  PRO   B N   1 
ATOM   1040 C CA  . PRO   B 1 42 ? 28.980  -12.918 -31.427 1.00 31.71  ? 41  PRO   B CA  1 
ATOM   1041 C C   . PRO   B 1 42 ? 27.553  -12.627 -31.863 1.00 30.02  ? 41  PRO   B C   1 
ATOM   1042 O O   . PRO   B 1 42 ? 27.340  -11.995 -32.910 1.00 33.29  ? 41  PRO   B O   1 
ATOM   1043 C CB  . PRO   B 1 42 ? 29.847  -11.656 -31.275 1.00 33.45  ? 41  PRO   B CB  1 
ATOM   1044 C CG  . PRO   B 1 42 ? 30.585  -11.508 -32.591 1.00 35.88  ? 41  PRO   B CG  1 
ATOM   1045 C CD  . PRO   B 1 42 ? 30.668  -12.896 -33.221 1.00 35.52  ? 41  PRO   B CD  1 
ATOM   1046 N N   . ILE   B 1 43 ? 26.586  -13.105 -31.043 1.00 28.55  ? 42  ILE   B N   1 
ATOM   1047 C CA  . ILE   B 1 43 ? 25.164  -12.931 -31.319 1.00 28.08  ? 42  ILE   B CA  1 
ATOM   1048 C C   . ILE   B 1 43 ? 24.565  -11.903 -30.359 1.00 28.72  ? 42  ILE   B C   1 
ATOM   1049 O O   . ILE   B 1 43 ? 24.875  -11.936 -29.178 1.00 33.02  ? 42  ILE   B O   1 
ATOM   1050 C CB  . ILE   B 1 43 ? 24.450  -14.285 -31.162 1.00 29.90  ? 42  ILE   B CB  1 
ATOM   1051 C CG1 . ILE   B 1 43 ? 25.217  -15.383 -31.960 1.00 31.15  ? 42  ILE   B CG1 1 
ATOM   1052 C CG2 . ILE   B 1 43 ? 22.975  -14.172 -31.567 1.00 31.79  ? 42  ILE   B CG2 1 
ATOM   1053 C CD1 . ILE   B 1 43 ? 25.342  -15.112 -33.449 1.00 29.97  ? 42  ILE   B CD1 1 
ATOM   1054 N N   . PHE   B 1 44 ? 23.676  -11.065 -30.894 1.00 26.88  ? 43  PHE   B N   1 
ATOM   1055 C CA  . PHE   B 1 44 ? 22.884  -10.146 -30.093 1.00 26.89  ? 43  PHE   B CA  1 
ATOM   1056 C C   . PHE   B 1 44 ? 21.434  -10.564 -30.286 1.00 25.76  ? 43  PHE   B C   1 
ATOM   1057 O O   . PHE   B 1 44 ? 20.951  -10.644 -31.413 1.00 27.38  ? 43  PHE   B O   1 
ATOM   1058 C CB  . PHE   B 1 44 ? 23.179  -8.688  -30.502 1.00 28.19  ? 43  PHE   B CB  1 
ATOM   1059 C CG  . PHE   B 1 44 ? 22.230  -7.663  -29.879 1.00 30.06  ? 43  PHE   B CG  1 
ATOM   1060 C CD1 . PHE   B 1 44 ? 21.029  -7.295  -30.498 1.00 26.27  ? 43  PHE   B CD1 1 
ATOM   1061 C CD2 . PHE   B 1 44 ? 22.537  -7.086  -28.658 1.00 33.81  ? 43  PHE   B CD2 1 
ATOM   1062 C CE1 . PHE   B 1 44 ? 20.157  -6.371  -29.926 1.00 28.31  ? 43  PHE   B CE1 1 
ATOM   1063 C CE2 . PHE   B 1 44 ? 21.667  -6.160  -28.071 1.00 30.20  ? 43  PHE   B CE2 1 
ATOM   1064 C CZ  . PHE   B 1 44 ? 20.469  -5.838  -28.686 1.00 33.37  ? 43  PHE   B CZ  1 
ATOM   1065 N N   . PHE   B 1 45 ? 20.750  -10.834 -29.172 1.00 26.80  ? 44  PHE   B N   1 
ATOM   1066 C CA  . PHE   B 1 45 ? 19.367  -11.256 -29.199 1.00 27.52  ? 44  PHE   B CA  1 
ATOM   1067 C C   . PHE   B 1 45 ? 18.497  -10.025 -29.073 1.00 25.11  ? 44  PHE   B C   1 
ATOM   1068 O O   . PHE   B 1 45 ? 18.616  -9.273  -28.084 1.00 28.59  ? 44  PHE   B O   1 
ATOM   1069 C CB  . PHE   B 1 45 ? 19.163  -12.204 -28.008 1.00 27.17  ? 44  PHE   B CB  1 
ATOM   1070 C CG  . PHE   B 1 45 ? 19.881  -13.533 -28.161 1.00 27.41  ? 44  PHE   B CG  1 
ATOM   1071 C CD1 . PHE   B 1 45 ? 21.214  -13.648 -27.815 1.00 29.50  ? 44  PHE   B CD1 1 
ATOM   1072 C CD2 . PHE   B 1 45 ? 19.260  -14.620 -28.771 1.00 26.49  ? 44  PHE   B CD2 1 
ATOM   1073 C CE1 . PHE   B 1 45 ? 21.910  -14.837 -28.017 1.00 33.68  ? 44  PHE   B CE1 1 
ATOM   1074 C CE2 . PHE   B 1 45 ? 19.959  -15.825 -28.911 1.00 29.05  ? 44  PHE   B CE2 1 
ATOM   1075 C CZ  . PHE   B 1 45 ? 21.288  -15.928 -28.585 1.00 27.44  ? 44  PHE   B CZ  1 
ATOM   1076 N N   . PHE   B 1 46 ? 17.624  -9.834  -30.056 1.00 26.24  ? 45  PHE   B N   1 
ATOM   1077 C CA  . PHE   B 1 46 ? 16.691  -8.730  -30.010 1.00 24.81  ? 45  PHE   B CA  1 
ATOM   1078 C C   . PHE   B 1 46 ? 15.667  -8.913  -28.874 1.00 29.71  ? 45  PHE   B C   1 
ATOM   1079 O O   . PHE   B 1 46 ? 15.356  -10.025 -28.465 1.00 29.32  ? 45  PHE   B O   1 
ATOM   1080 C CB  . PHE   B 1 46 ? 15.977  -8.500  -31.335 1.00 25.70  ? 45  PHE   B CB  1 
ATOM   1081 C CG  . PHE   B 1 46 ? 16.928  -8.081  -32.446 1.00 27.52  ? 45  PHE   B CG  1 
ATOM   1082 C CD1 . PHE   B 1 46 ? 17.424  -6.770  -32.468 1.00 30.85  ? 45  PHE   B CD1 1 
ATOM   1083 C CD2 . PHE   B 1 46 ? 17.238  -8.948  -33.510 1.00 25.94  ? 45  PHE   B CD2 1 
ATOM   1084 C CE1 . PHE   B 1 46 ? 18.220  -6.333  -33.534 1.00 27.79  ? 45  PHE   B CE1 1 
ATOM   1085 C CE2 . PHE   B 1 46 ? 18.070  -8.514  -34.558 1.00 25.23  ? 45  PHE   B CE2 1 
ATOM   1086 C CZ  . PHE   B 1 46 ? 18.557  -7.205  -34.551 1.00 26.21  ? 45  PHE   B CZ  1 
ATOM   1087 N N   . GLY   B 1 47 ? 15.133  -7.797  -28.372 1.00 29.36  ? 46  GLY   B N   1 
ATOM   1088 C CA  . GLY   B 1 47 ? 14.127  -7.875  -27.310 1.00 27.06  ? 46  GLY   B CA  1 
ATOM   1089 C C   . GLY   B 1 47 ? 14.762  -7.950  -25.923 1.00 31.27  ? 46  GLY   B C   1 
ATOM   1090 O O   . GLY   B 1 47 ? 14.600  -7.034  -25.114 1.00 33.98  ? 46  GLY   B O   1 
ATOM   1091 N N   . THR   B 1 48 ? 15.517  -9.025  -25.644 1.00 31.26  ? 47  THR   B N   1 
ATOM   1092 C CA  . THR   B 1 48 ? 16.161  -9.234  -24.360 1.00 32.16  ? 47  THR   B CA  1 
ATOM   1093 C C   . THR   B 1 48 ? 17.468  -8.450  -24.326 1.00 34.08  ? 47  THR   B C   1 
ATOM   1094 O O   . THR   B 1 48 ? 17.963  -8.110  -23.256 1.00 35.31  ? 47  THR   B O   1 
ATOM   1095 C CB  . THR   B 1 48 ? 16.428  -10.716 -24.080 1.00 33.82  ? 47  THR   B CB  1 
ATOM   1096 O OG1 . THR   B 1 48 ? 17.389  -11.187 -25.038 1.00 29.27  ? 47  THR   B OG1 1 
ATOM   1097 C CG2 . THR   B 1 48 ? 15.140  -11.518 -24.014 1.00 28.07  ? 47  THR   B CG2 1 
ATOM   1098 N N   . HIS   B 1 49 ? 18.026  -8.195  -25.516 1.00 30.73  ? 48  HIS   B N   1 
ATOM   1099 C CA  . HIS   B 1 49 ? 19.302  -7.513  -25.668 1.00 33.61  ? 48  HIS   B CA  1 
ATOM   1100 C C   . HIS   B 1 49 ? 20.417  -8.311  -25.011 1.00 34.81  ? 48  HIS   B C   1 
ATOM   1101 O O   . HIS   B 1 49 ? 21.429  -7.729  -24.654 1.00 38.32  ? 48  HIS   B O   1 
ATOM   1102 C CB  . HIS   B 1 49 ? 19.244  -6.042  -25.216 1.00 30.22  ? 48  HIS   B CB  1 
ATOM   1103 C CG  . HIS   B 1 49 ? 18.071  -5.321  -25.775 1.00 33.70  ? 48  HIS   B CG  1 
ATOM   1104 N ND1 . HIS   B 1 49 ? 17.371  -4.406  -25.020 1.00 36.77  ? 48  HIS   B ND1 1 
ATOM   1105 C CD2 . HIS   B 1 49 ? 17.443  -5.359  -26.966 1.00 29.39  ? 48  HIS   B CD2 1 
ATOM   1106 C CE1 . HIS   B 1 49 ? 16.339  -3.949  -25.731 1.00 44.00  ? 48  HIS   B CE1 1 
ATOM   1107 N NE2 . HIS   B 1 49 ? 16.376  -4.504  -26.937 1.00 37.08  ? 48  HIS   B NE2 1 
ATOM   1108 N N   . GLU   B 1 50 ? 20.263  -9.637  -24.898 1.00 32.84  ? 49  GLU   B N   1 
ATOM   1109 C CA  . GLU   B 1 50 ? 21.338  -10.487 -24.415 1.00 35.10  ? 49  GLU   B CA  1 
ATOM   1110 C C   . GLU   B 1 50 ? 22.346  -10.763 -25.540 1.00 34.71  ? 49  GLU   B C   1 
ATOM   1111 O O   . GLU   B 1 50 ? 22.096  -10.484 -26.723 1.00 31.85  ? 49  GLU   B O   1 
ATOM   1112 C CB  . GLU   B 1 50 ? 20.807  -11.817 -23.875 1.00 37.86  ? 49  GLU   B CB  1 
ATOM   1113 C CG  . GLU   B 1 50 ? 19.892  -11.609 -22.666 1.00 38.70  ? 49  GLU   B CG  1 
ATOM   1114 C CD  . GLU   B 1 50 ? 19.172  -12.893 -22.290 1.00 46.04  ? 49  GLU   B CD  1 
ATOM   1115 O OE1 . GLU   B 1 50 ? 18.359  -13.364 -23.119 1.00 53.87  ? 49  GLU   B OE1 1 
ATOM   1116 O OE2 . GLU   B 1 50 ? 19.416  -13.415 -21.194 1.00 50.68  ? 49  GLU   B OE2 1 
ATOM   1117 N N   . THR   B 1 51 ? 23.495  -11.288 -25.133 1.00 31.12  ? 50  THR   B N   1 
ATOM   1118 C CA  . THR   B 1 51 ? 24.539  -11.676 -26.062 1.00 31.62  ? 50  THR   B CA  1 
ATOM   1119 C C   . THR   B 1 51 ? 24.968  -13.101 -25.719 1.00 32.85  ? 50  THR   B C   1 
ATOM   1120 O O   . THR   B 1 51 ? 24.811  -13.556 -24.574 1.00 36.05  ? 50  THR   B O   1 
ATOM   1121 C CB  . THR   B 1 51 ? 25.699  -10.678 -26.099 1.00 37.47  ? 50  THR   B CB  1 
ATOM   1122 O OG1 . THR   B 1 51 ? 26.148  -10.597 -24.757 1.00 38.59  ? 50  THR   B OG1 1 
ATOM   1123 C CG2 . THR   B 1 51 ? 25.284  -9.265  -26.466 1.00 35.53  ? 50  THR   B CG2 1 
ATOM   1124 N N   . ALA   B 1 52 ? 25.466  -13.833 -26.729 1.00 31.78  ? 51  ALA   B N   1 
ATOM   1125 C CA  . ALA   B 1 52 ? 26.116  -15.120 -26.534 1.00 34.99  ? 51  ALA   B CA  1 
ATOM   1126 C C   . ALA   B 1 52 ? 27.006  -15.428 -27.740 1.00 34.08  ? 51  ALA   B C   1 
ATOM   1127 O O   . ALA   B 1 52 ? 26.977  -14.694 -28.743 1.00 36.60  ? 51  ALA   B O   1 
ATOM   1128 C CB  . ALA   B 1 52 ? 25.091  -16.208 -26.273 1.00 32.07  ? 51  ALA   B CB  1 
ATOM   1129 N N   . PHE   B 1 53 ? 27.811  -16.492 -27.629 1.00 33.57  ? 52  PHE   B N   1 
ATOM   1130 C CA  . PHE   B 1 53 ? 28.557  -16.972 -28.779 1.00 35.28  ? 52  PHE   B CA  1 
ATOM   1131 C C   . PHE   B 1 53 ? 27.852  -18.212 -29.325 1.00 33.43  ? 52  PHE   B C   1 
ATOM   1132 O O   . PHE   B 1 53 ? 27.557  -19.138 -28.574 1.00 34.18  ? 52  PHE   B O   1 
ATOM   1133 C CB  . PHE   B 1 53 ? 30.041  -17.237 -28.489 1.00 30.91  ? 52  PHE   B CB  1 
ATOM   1134 C CG  . PHE   B 1 53 ? 30.817  -15.995 -28.073 1.00 36.57  ? 52  PHE   B CG  1 
ATOM   1135 C CD1 . PHE   B 1 53 ? 31.079  -14.981 -28.980 1.00 39.86  ? 52  PHE   B CD1 1 
ATOM   1136 C CD2 . PHE   B 1 53 ? 31.288  -15.862 -26.774 1.00 41.38  ? 52  PHE   B CD2 1 
ATOM   1137 C CE1 . PHE   B 1 53 ? 31.780  -13.844 -28.597 1.00 40.76  ? 52  PHE   B CE1 1 
ATOM   1138 C CE2 . PHE   B 1 53 ? 31.975  -14.725 -26.381 1.00 41.98  ? 52  PHE   B CE2 1 
ATOM   1139 C CZ  . PHE   B 1 53 ? 32.230  -13.726 -27.294 1.00 38.46  ? 52  PHE   B CZ  1 
ATOM   1140 N N   . LEU   B 1 54 ? 27.651  -18.274 -30.651 1.00 29.49  ? 53  LEU   B N   1 
ATOM   1141 C CA  . LEU   B 1 54 ? 27.026  -19.467 -31.223 1.00 29.60  ? 53  LEU   B CA  1 
ATOM   1142 C C   . LEU   B 1 54 ? 27.733  -19.839 -32.529 1.00 29.91  ? 53  LEU   B C   1 
ATOM   1143 O O   . LEU   B 1 54 ? 28.229  -18.959 -33.250 1.00 30.71  ? 53  LEU   B O   1 
ATOM   1144 C CB  . LEU   B 1 54 ? 25.541  -19.257 -31.521 1.00 29.65  ? 53  LEU   B CB  1 
ATOM   1145 C CG  . LEU   B 1 54 ? 24.534  -19.234 -30.370 1.00 30.54  ? 53  LEU   B CG  1 
ATOM   1146 C CD1 . LEU   B 1 54 ? 23.153  -18.894 -30.903 1.00 30.83  ? 53  LEU   B CD1 1 
ATOM   1147 C CD2 . LEU   B 1 54 ? 24.555  -20.557 -29.623 1.00 30.00  ? 53  LEU   B CD2 1 
ATOM   1148 N N   . GLY   B 1 55 ? 27.626  -21.133 -32.870 1.00 33.24  ? 54  GLY   B N   1 
ATOM   1149 C CA  . GLY   B 1 55 ? 28.122  -21.680 -34.129 1.00 28.99  ? 54  GLY   B CA  1 
ATOM   1150 C C   . GLY   B 1 55 ? 27.004  -21.764 -35.165 1.00 30.91  ? 54  GLY   B C   1 
ATOM   1151 O O   . GLY   B 1 55 ? 25.821  -21.668 -34.811 1.00 29.62  ? 54  GLY   B O   1 
ATOM   1152 N N   . PRO   B 1 56 ? 27.347  -21.967 -36.464 1.00 28.62  ? 55  PRO   B N   1 
ATOM   1153 C CA  . PRO   B 1 56 ? 26.367  -21.991 -37.543 1.00 28.26  ? 55  PRO   B CA  1 
ATOM   1154 C C   . PRO   B 1 56 ? 25.200  -22.958 -37.414 1.00 26.02  ? 55  PRO   B C   1 
ATOM   1155 O O   . PRO   B 1 56 ? 24.129  -22.696 -37.952 1.00 28.94  ? 55  PRO   B O   1 
ATOM   1156 C CB  . PRO   B 1 56 ? 27.186  -22.256 -38.805 1.00 32.74  ? 55  PRO   B CB  1 
ATOM   1157 C CG  . PRO   B 1 56 ? 28.606  -21.956 -38.425 1.00 29.70  ? 55  PRO   B CG  1 
ATOM   1158 C CD  . PRO   B 1 56 ? 28.739  -22.109 -36.936 1.00 27.92  ? 55  PRO   B CD  1 
ATOM   1159 N N   . LYS   B 1 57 ? 25.401  -24.068 -36.688 1.00 30.72  ? 56  LYS   B N   1 
ATOM   1160 C CA  . LYS   B 1 57 ? 24.340  -25.062 -36.608 1.00 28.30  ? 56  LYS   B CA  1 
ATOM   1161 C C   . LYS   B 1 57 ? 23.131  -24.454 -35.901 1.00 28.62  ? 56  LYS   B C   1 
ATOM   1162 O O   . LYS   B 1 57 ? 22.004  -24.901 -36.104 1.00 27.98  ? 56  LYS   B O   1 
ATOM   1163 C CB  . LYS   B 1 57 ? 24.767  -26.326 -35.842 1.00 32.63  ? 56  LYS   B CB  1 
ATOM   1164 C CG  . LYS   B 1 57 ? 24.852  -26.163 -34.328 1.00 35.70  ? 56  LYS   B CG  1 
ATOM   1165 C CD  . LYS   B 1 57 ? 25.149  -27.532 -33.704 1.00 39.39  ? 56  LYS   B CD  1 
ATOM   1166 C CE  . LYS   B 1 57 ? 25.434  -27.569 -32.223 1.00 41.88  ? 56  LYS   B CE  1 
ATOM   1167 N NZ  . LYS   B 1 57 ? 24.332  -27.023 -31.420 1.00 45.58  ? 56  LYS   B NZ  1 
ATOM   1168 N N   . ASP   B 1 58 ? 23.366  -23.377 -35.122 1.00 27.39  ? 57  ASP   B N   1 
ATOM   1169 C CA  . ASP   B 1 58 ? 22.304  -22.754 -34.346 1.00 27.85  ? 57  ASP   B CA  1 
ATOM   1170 C C   . ASP   B 1 58 ? 21.871  -21.406 -34.918 1.00 27.20  ? 57  ASP   B C   1 
ATOM   1171 O O   . ASP   B 1 58 ? 21.087  -20.672 -34.271 1.00 26.40  ? 57  ASP   B O   1 
ATOM   1172 C CB  . ASP   B 1 58 ? 22.758  -22.624 -32.907 1.00 28.35  ? 57  ASP   B CB  1 
ATOM   1173 C CG  . ASP   B 1 58 ? 22.850  -23.971 -32.186 1.00 33.22  ? 57  ASP   B CG  1 
ATOM   1174 O OD1 . ASP   B 1 58 ? 21.906  -24.768 -32.358 1.00 35.08  ? 57  ASP   B OD1 1 
ATOM   1175 O OD2 . ASP   B 1 58 ? 23.825  -24.168 -31.444 1.00 38.35  ? 57  ASP   B OD2 1 
ATOM   1176 N N   . LEU   B 1 59 ? 22.313  -21.115 -36.153 1.00 27.40  ? 58  LEU   B N   1 
ATOM   1177 C CA  . LEU   B 1 59 ? 22.041  -19.820 -36.766 1.00 25.98  ? 58  LEU   B CA  1 
ATOM   1178 C C   . LEU   B 1 59 ? 21.304  -20.007 -38.086 1.00 27.46  ? 58  LEU   B C   1 
ATOM   1179 O O   . LEU   B 1 59 ? 21.800  -20.655 -39.022 1.00 27.30  ? 58  LEU   B O   1 
ATOM   1180 C CB  . LEU   B 1 59 ? 23.367  -19.097 -36.990 1.00 27.01  ? 58  LEU   B CB  1 
ATOM   1181 C CG  . LEU   B 1 59 ? 24.164  -18.780 -35.728 1.00 26.54  ? 58  LEU   B CG  1 
ATOM   1182 C CD1 . LEU   B 1 59 ? 25.451  -18.112 -36.172 1.00 28.26  ? 58  LEU   B CD1 1 
ATOM   1183 C CD2 . LEU   B 1 59 ? 23.413  -17.850 -34.790 1.00 27.38  ? 58  LEU   B CD2 1 
ATOM   1184 N N   . PHE   B 1 60 ? 20.121  -19.412 -38.157 1.00 23.70  ? 59  PHE   B N   1 
ATOM   1185 C CA  . PHE   B 1 60 ? 19.211  -19.598 -39.270 1.00 24.93  ? 59  PHE   B CA  1 
ATOM   1186 C C   . PHE   B 1 60 ? 18.990  -18.237 -39.936 1.00 26.52  ? 59  PHE   B C   1 
ATOM   1187 O O   . PHE   B 1 60 ? 18.378  -17.328 -39.368 1.00 27.08  ? 59  PHE   B O   1 
ATOM   1188 C CB  . PHE   B 1 60 ? 17.893  -20.111 -38.674 1.00 25.32  ? 59  PHE   B CB  1 
ATOM   1189 C CG  . PHE   B 1 60 ? 17.973  -21.516 -38.091 1.00 22.68  ? 59  PHE   B CG  1 
ATOM   1190 C CD1 . PHE   B 1 60 ? 18.490  -21.734 -36.813 1.00 25.11  ? 59  PHE   B CD1 1 
ATOM   1191 C CD2 . PHE   B 1 60 ? 17.539  -22.606 -38.835 1.00 28.42  ? 59  PHE   B CD2 1 
ATOM   1192 C CE1 . PHE   B 1 60 ? 18.599  -23.018 -36.274 1.00 27.74  ? 59  PHE   B CE1 1 
ATOM   1193 C CE2 . PHE   B 1 60 ? 17.647  -23.893 -38.304 1.00 28.89  ? 59  PHE   B CE2 1 
ATOM   1194 C CZ  . PHE   B 1 60 ? 18.191  -24.103 -37.058 1.00 28.24  ? 59  PHE   B CZ  1 
ATOM   1195 N N   . PRO   B 1 61 ? 19.498  -18.032 -41.173 1.00 29.29  ? 60  PRO   B N   1 
ATOM   1196 C CA  . PRO   B 1 61 ? 19.257  -16.754 -41.854 1.00 28.83  ? 60  PRO   B CA  1 
ATOM   1197 C C   . PRO   B 1 61 ? 17.799  -16.283 -41.820 1.00 26.02  ? 60  PRO   B C   1 
ATOM   1198 O O   . PRO   B 1 61 ? 16.856  -17.045 -42.090 1.00 28.30  ? 60  PRO   B O   1 
ATOM   1199 C CB  . PRO   B 1 61 ? 19.831  -17.038 -43.267 1.00 27.30  ? 60  PRO   B CB  1 
ATOM   1200 C CG  . PRO   B 1 61 ? 20.902  -18.098 -43.047 1.00 32.60  ? 60  PRO   B CG  1 
ATOM   1201 C CD  . PRO   B 1 61 ? 20.283  -19.010 -41.951 1.00 30.47  ? 60  PRO   B CD  1 
ATOM   1202 N N   . TYR   B 1 62 ? 17.601  -14.989 -41.464 1.00 28.87  ? 61  TYR   B N   1 
ATOM   1203 C CA  . TYR   B 1 62 ? 16.290  -14.440 -41.167 1.00 29.02  ? 61  TYR   B CA  1 
ATOM   1204 C C   . TYR   B 1 62 ? 15.293  -14.494 -42.318 1.00 32.00  ? 61  TYR   B C   1 
ATOM   1205 O O   . TYR   B 1 62 ? 14.143  -14.897 -42.103 1.00 34.23  ? 61  TYR   B O   1 
ATOM   1206 C CB  . TYR   B 1 62 ? 16.496  -12.992 -40.704 1.00 32.57  ? 61  TYR   B CB  1 
ATOM   1207 C CG  . TYR   B 1 62 ? 15.168  -12.309 -40.423 1.00 33.61  ? 61  TYR   B CG  1 
ATOM   1208 C CD1 . TYR   B 1 62 ? 14.473  -12.543 -39.246 1.00 33.08  ? 61  TYR   B CD1 1 
ATOM   1209 C CD2 . TYR   B 1 62 ? 14.650  -11.398 -41.329 1.00 36.89  ? 61  TYR   B CD2 1 
ATOM   1210 C CE1 . TYR   B 1 62 ? 13.264  -11.912 -39.000 1.00 35.64  ? 61  TYR   B CE1 1 
ATOM   1211 C CE2 . TYR   B 1 62 ? 13.450  -10.749 -41.100 1.00 38.42  ? 61  TYR   B CE2 1 
ATOM   1212 C CZ  . TYR   B 1 62 ? 12.757  -11.021 -39.935 1.00 36.71  ? 61  TYR   B CZ  1 
ATOM   1213 O OH  . TYR   B 1 62 ? 11.585  -10.362 -39.745 1.00 39.01  ? 61  TYR   B OH  1 
ATOM   1214 N N   . ASP   B 1 63 ? 15.762  -14.113 -43.523 1.00 35.14  ? 62  ASP   B N   1 
ATOM   1215 C CA  . ASP   B 1 63 ? 14.919  -14.088 -44.720 1.00 37.76  ? 62  ASP   B CA  1 
ATOM   1216 C C   . ASP   B 1 63 ? 14.332  -15.466 -45.019 1.00 34.21  ? 62  ASP   B C   1 
ATOM   1217 O O   . ASP   B 1 63 ? 13.132  -15.593 -45.221 1.00 39.90  ? 62  ASP   B O   1 
ATOM   1218 C CB  . ASP   B 1 63 ? 15.634  -13.464 -45.908 1.00 44.37  ? 62  ASP   B CB  1 
ATOM   1219 C CG  . ASP   B 1 63 ? 15.323  -11.994 -46.137 1.00 57.83  ? 62  ASP   B CG  1 
ATOM   1220 O OD1 . ASP   B 1 63 ? 14.792  -11.358 -45.198 1.00 56.60  ? 62  ASP   B OD1 1 
ATOM   1221 O OD2 . ASP   B 1 63 ? 15.571  -11.513 -47.267 1.00 63.98  ? 62  ASP   B OD2 1 
ATOM   1222 N N   . LYS   B 1 64 ? 15.187  -16.479 -44.990 1.00 36.42  ? 63  LYS   B N   1 
ATOM   1223 C CA  . LYS   B 1 64 ? 14.792  -17.839 -45.281 1.00 37.27  ? 63  LYS   B CA  1 
ATOM   1224 C C   . LYS   B 1 64 ? 13.814  -18.356 -44.229 1.00 35.04  ? 63  LYS   B C   1 
ATOM   1225 O O   . LYS   B 1 64 ? 12.893  -19.098 -44.553 1.00 38.24  ? 63  LYS   B O   1 
ATOM   1226 C CB  . LYS   B 1 64 ? 16.007  -18.770 -45.272 1.00 39.05  ? 63  LYS   B CB  1 
ATOM   1227 C CG  . LYS   B 1 64 ? 15.680  -20.172 -45.754 1.00 41.48  ? 63  LYS   B CG  1 
ATOM   1228 C CD  . LYS   B 1 64 ? 16.873  -21.099 -45.582 1.00 47.51  ? 63  LYS   B CD  1 
ATOM   1229 C CE  . LYS   B 1 64 ? 16.753  -22.425 -46.281 1.00 42.30  ? 63  LYS   B CE  1 
ATOM   1230 N NZ  . LYS   B 1 64 ? 15.427  -23.020 -46.142 1.00 42.46  ? 63  LYS   B NZ  1 
ATOM   1231 N N   . SER   B 1 65 ? 13.998  -17.950 -42.973 1.00 34.81  ? 64  SER   B N   1 
ATOM   1232 C CA  . SER   B 1 65 ? 13.321  -18.674 -41.894 1.00 33.27  ? 64  SER   B CA  1 
ATOM   1233 C C   . SER   B 1 65 ? 12.231  -17.860 -41.165 1.00 35.80  ? 64  SER   B C   1 
ATOM   1234 O O   . SER   B 1 65 ? 11.588  -18.370 -40.254 1.00 35.01  ? 64  SER   B O   1 
ATOM   1235 C CB  . SER   B 1 65 ? 14.380  -19.199 -40.975 1.00 34.22  ? 64  SER   B CB  1 
ATOM   1236 O OG  . SER   B 1 65 ? 15.090  -18.122 -40.398 1.00 48.18  ? 64  SER   B OG  1 
ATOM   1237 N N   . LYS   B 1 66 ? 11.932  -16.635 -41.602 1.00 33.78  ? 65  LYS   B N   1 
ATOM   1238 C CA  . LYS   B 1 66 ? 11.028  -15.785 -40.819 1.00 35.47  ? 65  LYS   B CA  1 
ATOM   1239 C C   . LYS   B 1 66 ? 9.583   -16.288 -40.772 1.00 38.59  ? 65  LYS   B C   1 
ATOM   1240 O O   . LYS   B 1 66 ? 8.862   -16.015 -39.815 1.00 38.34  ? 65  LYS   B O   1 
ATOM   1241 C CB  . LYS   B 1 66 ? 11.015  -14.295 -41.194 1.00 38.75  ? 65  LYS   B CB  1 
ATOM   1242 C CG  . LYS   B 1 66 ? 10.740  -13.980 -42.671 1.00 39.75  ? 65  LYS   B CG  1 
ATOM   1243 N N   . ASP   B 1 67 ? 9.095   -16.958 -41.806 1.00 36.87  ? 66  ASP   B N   1 
ATOM   1244 C CA  . ASP   B 1 67 ? 7.692   -17.304 -41.675 1.00 43.05  ? 66  ASP   B CA  1 
ATOM   1245 C C   . ASP   B 1 67 ? 7.538   -18.567 -40.828 1.00 42.37  ? 66  ASP   B C   1 
ATOM   1246 O O   . ASP   B 1 67 ? 6.458   -18.809 -40.294 1.00 46.32  ? 66  ASP   B O   1 
ATOM   1247 C CB  . ASP   B 1 67 ? 6.911   -17.135 -42.967 1.00 57.23  ? 66  ASP   B CB  1 
ATOM   1248 C CG  . ASP   B 1 67 ? 7.492   -17.865 -44.159 1.00 71.40  ? 66  ASP   B CG  1 
ATOM   1249 O OD1 . ASP   B 1 67 ? 7.141   -17.497 -45.303 1.00 80.37  ? 66  ASP   B OD1 1 
ATOM   1250 O OD2 . ASP   B 1 67 ? 8.275   -18.801 -43.922 1.00 77.41  ? 66  ASP   B OD2 1 
ATOM   1251 N N   . LYS   B 1 68 ? 8.634   -19.316 -40.664 1.00 37.02  ? 67  LYS   B N   1 
ATOM   1252 C CA  . LYS   B 1 68 ? 8.614   -20.470 -39.781 1.00 32.32  ? 67  LYS   B CA  1 
ATOM   1253 C C   . LYS   B 1 68 ? 8.802   -20.039 -38.328 1.00 36.12  ? 67  LYS   B C   1 
ATOM   1254 O O   . LYS   B 1 68 ? 8.083   -20.513 -37.448 1.00 35.48  ? 67  LYS   B O   1 
ATOM   1255 C CB  . LYS   B 1 68 ? 9.703   -21.477 -40.165 1.00 34.69  ? 67  LYS   B CB  1 
ATOM   1256 C CG  . LYS   B 1 68 ? 9.747   -22.746 -39.337 1.00 40.26  ? 67  LYS   B CG  1 
ATOM   1257 C CD  . LYS   B 1 68 ? 10.966  -23.572 -39.773 1.00 42.44  ? 67  LYS   B CD  1 
ATOM   1258 C CE  . LYS   B 1 68 ? 11.120  -24.918 -39.112 1.00 56.11  ? 67  LYS   B CE  1 
ATOM   1259 N NZ  . LYS   B 1 68 ? 9.953   -25.772 -39.342 1.00 60.90  ? 67  LYS   B NZ  1 
ATOM   1260 N N   . TYR   B 1 69 ? 9.793   -19.173 -38.068 1.00 31.36  ? 68  TYR   B N   1 
ATOM   1261 C CA  . TYR   B 1 69 ? 10.193  -18.863 -36.697 1.00 27.70  ? 68  TYR   B CA  1 
ATOM   1262 C C   . TYR   B 1 69 ? 9.729   -17.504 -36.185 1.00 30.01  ? 68  TYR   B C   1 
ATOM   1263 O O   . TYR   B 1 69 ? 9.880   -17.220 -34.991 1.00 30.95  ? 68  TYR   B O   1 
ATOM   1264 C CB  . TYR   B 1 69 ? 11.716  -18.913 -36.594 1.00 28.08  ? 68  TYR   B CB  1 
ATOM   1265 C CG  . TYR   B 1 69 ? 12.338  -20.280 -36.872 1.00 29.92  ? 68  TYR   B CG  1 
ATOM   1266 C CD1 . TYR   B 1 69 ? 11.790  -21.431 -36.313 1.00 30.82  ? 68  TYR   B CD1 1 
ATOM   1267 C CD2 . TYR   B 1 69 ? 13.482  -20.413 -37.657 1.00 30.37  ? 68  TYR   B CD2 1 
ATOM   1268 C CE1 . TYR   B 1 69 ? 12.354  -22.679 -36.554 1.00 31.96  ? 68  TYR   B CE1 1 
ATOM   1269 C CE2 . TYR   B 1 69 ? 14.059  -21.650 -37.897 1.00 35.62  ? 68  TYR   B CE2 1 
ATOM   1270 C CZ  . TYR   B 1 69 ? 13.480  -22.787 -37.355 1.00 37.04  ? 68  TYR   B CZ  1 
ATOM   1271 O OH  . TYR   B 1 69 ? 14.050  -23.996 -37.643 1.00 34.95  ? 68  TYR   B OH  1 
ATOM   1272 N N   . GLY   B 1 70 ? 9.234   -16.641 -37.083 1.00 31.56  ? 69  GLY   B N   1 
ATOM   1273 C CA  . GLY   B 1 70 ? 8.934   -15.264 -36.729 1.00 35.76  ? 69  GLY   B CA  1 
ATOM   1274 C C   . GLY   B 1 70 ? 7.515   -15.062 -36.205 1.00 36.08  ? 69  GLY   B C   1 
ATOM   1275 O O   . GLY   B 1 70 ? 6.948   -14.011 -36.434 1.00 37.10  ? 69  GLY   B O   1 
ATOM   1276 N N   . LYS   B 1 71 ? 6.949   -16.051 -35.507 1.00 40.85  ? 70  LYS   B N   1 
ATOM   1277 C CA  . LYS   B 1 71 ? 5.605   -15.914 -34.971 1.00 38.38  ? 70  LYS   B CA  1 
ATOM   1278 C C   . LYS   B 1 71 ? 5.682   -15.476 -33.518 1.00 36.97  ? 70  LYS   B C   1 
ATOM   1279 O O   . LYS   B 1 71 ? 6.550   -15.904 -32.762 1.00 36.17  ? 70  LYS   B O   1 
ATOM   1280 C CB  . LYS   B 1 71 ? 4.831   -17.236 -34.941 1.00 44.25  ? 70  LYS   B CB  1 
ATOM   1281 C CG  . LYS   B 1 71 ? 3.925   -17.547 -36.136 1.00 56.62  ? 70  LYS   B CG  1 
ATOM   1282 C CD  . LYS   B 1 71 ? 4.621   -17.590 -37.486 1.00 55.43  ? 70  LYS   B CD  1 
ATOM   1283 C CE  . LYS   B 1 71 ? 3.685   -18.016 -38.579 1.00 59.65  ? 70  LYS   B CE  1 
ATOM   1284 N NZ  . LYS   B 1 71 ? 4.199   -17.572 -39.880 1.00 64.68  ? 70  LYS   B NZ  1 
ATOM   1285 N N   . PRO   B 1 72 ? 4.743   -14.624 -33.068 1.00 39.56  ? 71  PRO   B N   1 
ATOM   1286 C CA  . PRO   B 1 72 ? 4.751   -14.177 -31.680 1.00 37.78  ? 71  PRO   B CA  1 
ATOM   1287 C C   . PRO   B 1 72 ? 4.435   -15.312 -30.709 1.00 39.43  ? 71  PRO   B C   1 
ATOM   1288 O O   . PRO   B 1 72 ? 3.775   -16.299 -31.064 1.00 38.32  ? 71  PRO   B O   1 
ATOM   1289 C CB  . PRO   B 1 72 ? 3.695   -13.077 -31.686 1.00 36.54  ? 71  PRO   B CB  1 
ATOM   1290 C CG  . PRO   B 1 72 ? 2.748   -13.559 -32.742 1.00 40.58  ? 71  PRO   B CG  1 
ATOM   1291 C CD  . PRO   B 1 72 ? 3.665   -14.038 -33.875 1.00 39.01  ? 71  PRO   B CD  1 
ATOM   1292 N N   . ASN   B 1 73 ? 4.981   -15.183 -29.495 1.00 35.52  ? 72  ASN   B N   1 
ATOM   1293 C CA  . ASN   B 1 73 ? 4.737   -16.144 -28.434 1.00 35.29  ? 72  ASN   B CA  1 
ATOM   1294 C C   . ASN   B 1 73 ? 4.679   -15.379 -27.110 1.00 36.56  ? 72  ASN   B C   1 
ATOM   1295 O O   . ASN   B 1 73 ? 4.692   -14.144 -27.095 1.00 39.20  ? 72  ASN   B O   1 
ATOM   1296 C CB  . ASN   B 1 73 ? 5.745   -17.296 -28.476 1.00 36.02  ? 72  ASN   B CB  1 
ATOM   1297 C CG  . ASN   B 1 73 ? 7.156   -16.840 -28.212 1.00 36.00  ? 72  ASN   B CG  1 
ATOM   1298 O OD1 . ASN   B 1 73 ? 7.388   -16.059 -27.276 1.00 34.13  ? 72  ASN   B OD1 1 
ATOM   1299 N ND2 . ASN   B 1 73 ? 8.104   -17.287 -29.033 1.00 34.83  ? 72  ASN   B ND2 1 
ATOM   1300 N N   . LYS   B 1 74 ? 4.630   -16.122 -26.006 1.00 38.88  ? 73  LYS   B N   1 
ATOM   1301 C CA  . LYS   B 1 74 ? 4.455   -15.524 -24.685 1.00 40.74  ? 73  LYS   B CA  1 
ATOM   1302 C C   . LYS   B 1 74 ? 5.773   -15.497 -23.881 1.00 41.98  ? 73  LYS   B C   1 
ATOM   1303 O O   . LYS   B 1 74 ? 5.753   -15.261 -22.670 1.00 41.84  ? 73  LYS   B O   1 
ATOM   1304 C CB  . LYS   B 1 74 ? 3.306   -16.303 -24.015 1.00 43.96  ? 73  LYS   B CB  1 
ATOM   1305 N N   . ARG   B 1 75 ? 6.933   -15.727 -24.521 1.00 31.44  ? 74  ARG   B N   1 
ATOM   1306 C CA  . ARG   B 1 75 ? 8.214   -15.609 -23.828 1.00 33.33  ? 74  ARG   B CA  1 
ATOM   1307 C C   . ARG   B 1 75 ? 8.584   -14.127 -23.661 1.00 33.13  ? 74  ARG   B C   1 
ATOM   1308 O O   . ARG   B 1 75 ? 8.498   -13.316 -24.589 1.00 35.47  ? 74  ARG   B O   1 
ATOM   1309 C CB  . ARG   B 1 75 ? 9.353   -16.421 -24.475 1.00 33.47  ? 74  ARG   B CB  1 
ATOM   1310 C CG  . ARG   B 1 75 ? 9.126   -17.887 -24.819 1.00 36.63  ? 74  ARG   B CG  1 
ATOM   1311 C CD  . ARG   B 1 75 ? 9.068   -18.639 -23.531 1.00 39.82  ? 74  ARG   B CD  1 
ATOM   1312 N NE  . ARG   B 1 75 ? 9.297   -20.058 -23.810 1.00 40.44  ? 74  ARG   B NE  1 
ATOM   1313 C CZ  . ARG   B 1 75 ? 10.366  -20.714 -23.419 1.00 40.47  ? 74  ARG   B CZ  1 
ATOM   1314 N NH1 . ARG   B 1 75 ? 11.389  -20.087 -22.859 1.00 49.16  ? 74  ARG   B NH1 1 
ATOM   1315 N NH2 . ARG   B 1 75 ? 10.420  -22.009 -23.648 1.00 47.01  ? 74  ARG   B NH2 1 
ATOM   1316 N N   . LYS   B 1 76 ? 8.982   -13.747 -22.447 1.00 32.02  ? 75  LYS   B N   1 
ATOM   1317 C CA  . LYS   B 1 76 ? 9.367   -12.382 -22.164 1.00 30.54  ? 75  LYS   B CA  1 
ATOM   1318 C C   . LYS   B 1 76 ? 10.493  -11.920 -23.112 1.00 27.20  ? 75  LYS   B C   1 
ATOM   1319 O O   . LYS   B 1 76 ? 11.569  -12.531 -23.119 1.00 30.92  ? 75  LYS   B O   1 
ATOM   1320 C CB  . LYS   B 1 76 ? 9.949   -12.331 -20.739 1.00 31.87  ? 75  LYS   B CB  1 
ATOM   1321 C CG  . LYS   B 1 76 ? 10.226  -10.908 -20.239 1.00 32.43  ? 75  LYS   B CG  1 
ATOM   1322 C CD  . LYS   B 1 76 ? 10.726  -10.806 -18.807 1.00 36.87  ? 75  LYS   B CD  1 
ATOM   1323 C CE  . LYS   B 1 76 ? 11.197  -9.399  -18.510 1.00 38.19  ? 75  LYS   B CE  1 
ATOM   1324 N NZ  . LYS   B 1 76 ? 11.465  -9.265  -17.068 1.00 46.31  ? 75  LYS   B NZ  1 
ATOM   1325 N N   . GLY   B 1 77 ? 10.191  -10.836 -23.831 1.00 28.38  ? 76  GLY   B N   1 
ATOM   1326 C CA  . GLY   B 1 77 ? 11.139  -10.160 -24.726 1.00 29.90  ? 76  GLY   B CA  1 
ATOM   1327 C C   . GLY   B 1 77 ? 11.041  -10.637 -26.183 1.00 30.57  ? 76  GLY   B C   1 
ATOM   1328 O O   . GLY   B 1 77 ? 11.600  -10.027 -27.101 1.00 27.73  ? 76  GLY   B O   1 
ATOM   1329 N N   . PHE   B 1 78 ? 10.329  -11.731 -26.431 1.00 27.88  ? 77  PHE   B N   1 
ATOM   1330 C CA  . PHE   B 1 78 ? 10.277  -12.264 -27.794 1.00 26.29  ? 77  PHE   B CA  1 
ATOM   1331 C C   . PHE   B 1 78 ? 9.555   -11.322 -28.764 1.00 28.89  ? 77  PHE   B C   1 
ATOM   1332 O O   . PHE   B 1 78 ? 10.071  -11.014 -29.848 1.00 27.53  ? 77  PHE   B O   1 
ATOM   1333 C CB  . PHE   B 1 78 ? 9.605   -13.631 -27.824 1.00 28.23  ? 77  PHE   B CB  1 
ATOM   1334 C CG  . PHE   B 1 78 ? 9.897   -14.379 -29.118 1.00 27.57  ? 77  PHE   B CG  1 
ATOM   1335 C CD1 . PHE   B 1 78 ? 10.987  -15.237 -29.175 1.00 27.33  ? 77  PHE   B CD1 1 
ATOM   1336 C CD2 . PHE   B 1 78 ? 9.051   -14.256 -30.209 1.00 30.56  ? 77  PHE   B CD2 1 
ATOM   1337 C CE1 . PHE   B 1 78 ? 11.255  -15.939 -30.341 1.00 27.61  ? 77  PHE   B CE1 1 
ATOM   1338 C CE2 . PHE   B 1 78 ? 9.317   -14.980 -31.371 1.00 31.05  ? 77  PHE   B CE2 1 
ATOM   1339 C CZ  . PHE   B 1 78 ? 10.411  -15.836 -31.419 1.00 29.26  ? 77  PHE   B CZ  1 
ATOM   1340 N N   . ASN   B 1 79 ? 8.322   -10.886 -28.454 1.00 27.03  ? 78  ASN   B N   1 
ATOM   1341 C CA  . ASN   B 1 79 ? 7.609   -10.037 -29.399 1.00 30.13  ? 78  ASN   B CA  1 
ATOM   1342 C C   . ASN   B 1 79 ? 8.327   -8.695  -29.593 1.00 31.41  ? 78  ASN   B C   1 
ATOM   1343 O O   . ASN   B 1 79 ? 8.293   -8.131  -30.698 1.00 31.87  ? 78  ASN   B O   1 
ATOM   1344 C CB  . ASN   B 1 79 ? 6.129   -9.895  -29.035 1.00 33.12  ? 78  ASN   B CB  1 
ATOM   1345 C CG  . ASN   B 1 79 ? 5.411   -11.227 -28.952 1.00 40.03  ? 78  ASN   B CG  1 
ATOM   1346 O OD1 . ASN   B 1 79 ? 5.928   -12.244 -29.442 1.00 34.32  ? 78  ASN   B OD1 1 
ATOM   1347 N ND2 . ASN   B 1 79 ? 4.237   -11.251 -28.323 1.00 35.96  ? 78  ASN   B ND2 1 
ATOM   1348 N N   . GLU   B 1 80 ? 8.954   -8.197  -28.524 1.00 30.00  ? 79  GLU   B N   1 
ATOM   1349 C CA  . GLU   B 1 80 ? 9.734   -6.974  -28.623 1.00 32.75  ? 79  GLU   B CA  1 
ATOM   1350 C C   . GLU   B 1 80 ? 10.874  -7.226  -29.606 1.00 30.77  ? 79  GLU   B C   1 
ATOM   1351 O O   . GLU   B 1 80 ? 11.172  -6.366  -30.437 1.00 32.21  ? 79  GLU   B O   1 
ATOM   1352 C CB  . GLU   B 1 80 ? 10.313  -6.523  -27.289 1.00 31.93  ? 79  GLU   B CB  1 
ATOM   1353 C CG  . GLU   B 1 80 ? 9.242   -5.967  -26.348 1.00 39.61  ? 79  GLU   B CG  1 
ATOM   1354 N N   . GLY   B 1 81 ? 11.473  -8.429  -29.499 1.00 28.86  ? 80  GLY   B N   1 
ATOM   1355 C CA  . GLY   B 1 81 ? 12.551  -8.833  -30.399 1.00 28.59  ? 80  GLY   B CA  1 
ATOM   1356 C C   . GLY   B 1 81 ? 12.083  -8.922  -31.848 1.00 28.32  ? 80  GLY   B C   1 
ATOM   1357 O O   . GLY   B 1 81 ? 12.841  -8.519  -32.749 1.00 28.75  ? 80  GLY   B O   1 
ATOM   1358 N N   . LEU   B 1 82 ? 10.852  -9.411  -32.080 1.00 26.09  ? 81  LEU   B N   1 
ATOM   1359 C CA  . LEU   B 1 82 ? 10.292  -9.422  -33.417 1.00 29.43  ? 81  LEU   B CA  1 
ATOM   1360 C C   . LEU   B 1 82 ? 10.129  -7.986  -33.911 1.00 28.95  ? 81  LEU   B C   1 
ATOM   1361 O O   . LEU   B 1 82 ? 10.320  -7.746  -35.099 1.00 30.34  ? 81  LEU   B O   1 
ATOM   1362 C CB  . LEU   B 1 82 ? 8.953   -10.166 -33.410 1.00 29.70  ? 81  LEU   B CB  1 
ATOM   1363 C CG  . LEU   B 1 82 ? 9.062   -11.683 -33.219 1.00 28.29  ? 81  LEU   B CG  1 
ATOM   1364 C CD1 . LEU   B 1 82 ? 7.636   -12.247 -33.242 1.00 28.51  ? 81  LEU   B CD1 1 
ATOM   1365 C CD2 . LEU   B 1 82 ? 9.921   -12.350 -34.291 1.00 29.19  ? 81  LEU   B CD2 1 
ATOM   1366 N N   . TRP   B 1 83 ? 9.746   -7.055  -33.013 1.00 29.53  ? 82  TRP   B N   1 
ATOM   1367 C CA  . TRP   B 1 83 ? 9.587   -5.652  -33.385 1.00 31.19  ? 82  TRP   B CA  1 
ATOM   1368 C C   . TRP   B 1 83 ? 10.915  -5.058  -33.833 1.00 29.17  ? 82  TRP   B C   1 
ATOM   1369 O O   . TRP   B 1 83 ? 10.982  -4.434  -34.903 1.00 30.31  ? 82  TRP   B O   1 
ATOM   1370 C CB  . TRP   B 1 83 ? 8.971   -4.806  -32.262 1.00 33.90  ? 82  TRP   B CB  1 
ATOM   1371 C CG  . TRP   B 1 83 ? 8.669   -3.415  -32.758 1.00 37.68  ? 82  TRP   B CG  1 
ATOM   1372 C CD1 . TRP   B 1 83 ? 7.533   -2.981  -33.376 1.00 40.39  ? 82  TRP   B CD1 1 
ATOM   1373 C CD2 . TRP   B 1 83 ? 9.596   -2.308  -32.779 1.00 38.47  ? 82  TRP   B CD2 1 
ATOM   1374 N NE1 . TRP   B 1 83 ? 7.674   -1.667  -33.743 1.00 42.61  ? 82  TRP   B NE1 1 
ATOM   1375 C CE2 . TRP   B 1 83 ? 8.926   -1.232  -33.398 1.00 38.16  ? 82  TRP   B CE2 1 
ATOM   1376 C CE3 . TRP   B 1 83 ? 10.917  -2.128  -32.331 1.00 38.22  ? 82  TRP   B CE3 1 
ATOM   1377 C CZ2 . TRP   B 1 83 ? 9.542   0.010   -33.572 1.00 35.67  ? 82  TRP   B CZ2 1 
ATOM   1378 C CZ3 . TRP   B 1 83 ? 11.521  -0.898  -32.502 1.00 39.23  ? 82  TRP   B CZ3 1 
ATOM   1379 C CH2 . TRP   B 1 83 ? 10.840  0.152   -33.118 1.00 37.11  ? 82  TRP   B CH2 1 
ATOM   1380 N N   . GLU   B 1 84 ? 11.967  -5.356  -33.073 1.00 26.57  ? 83  GLU   B N   1 
ATOM   1381 C CA  . GLU   B 1 84 ? 13.289  -4.794  -33.299 1.00 28.15  ? 83  GLU   B CA  1 
ATOM   1382 C C   . GLU   B 1 84 ? 13.873  -5.311  -34.611 1.00 28.60  ? 83  GLU   B C   1 
ATOM   1383 O O   . GLU   B 1 84 ? 14.492  -4.545  -35.358 1.00 28.33  ? 83  GLU   B O   1 
ATOM   1384 C CB  . GLU   B 1 84 ? 14.245  -5.047  -32.153 1.00 27.92  ? 83  GLU   B CB  1 
ATOM   1385 C CG  . GLU   B 1 84 ? 13.850  -4.237  -30.917 1.00 31.13  ? 83  GLU   B CG  1 
ATOM   1386 C CD  . GLU   B 1 84 ? 14.678  -4.613  -29.725 1.00 31.39  ? 83  GLU   B CD  1 
ATOM   1387 O OE1 . GLU   B 1 84 ? 15.563  -5.500  -29.812 1.00 30.38  ? 83  GLU   B OE1 1 
ATOM   1388 O OE2 . GLU   B 1 84 ? 14.422  -4.023  -28.636 1.00 32.22  ? 83  GLU   B OE2 1 
ATOM   1389 N N   . ILE   B 1 85 ? 13.747  -6.618  -34.885 1.00 28.36  ? 84  ILE   B N   1 
ATOM   1390 C CA  . ILE   B 1 85 ? 14.471  -7.138  -36.044 1.00 25.38  ? 84  ILE   B CA  1 
ATOM   1391 C C   . ILE   B 1 85 ? 13.815  -6.594  -37.312 1.00 28.67  ? 84  ILE   B C   1 
ATOM   1392 O O   . ILE   B 1 85 ? 14.474  -6.420  -38.327 1.00 27.14  ? 84  ILE   B O   1 
ATOM   1393 C CB  . ILE   B 1 85 ? 14.525  -8.686  -36.031 1.00 25.40  ? 84  ILE   B CB  1 
ATOM   1394 C CG1 . ILE   B 1 85 ? 15.569  -9.276  -37.019 1.00 26.95  ? 84  ILE   B CG1 1 
ATOM   1395 C CG2 . ILE   B 1 85 ? 13.147  -9.289  -36.284 1.00 26.03  ? 84  ILE   B CG2 1 
ATOM   1396 C CD1 . ILE   B 1 85 ? 15.976  -10.706 -36.696 1.00 25.87  ? 84  ILE   B CD1 1 
ATOM   1397 N N   . GLN   B 1 86 ? 12.510  -6.287  -37.234 1.00 28.29  ? 85  GLN   B N   1 
ATOM   1398 C CA  . GLN   B 1 86 ? 11.722  -5.771  -38.336 1.00 30.81  ? 85  GLN   B CA  1 
ATOM   1399 C C   . GLN   B 1 86 ? 11.991  -4.279  -38.529 1.00 32.69  ? 85  GLN   B C   1 
ATOM   1400 O O   . GLN   B 1 86 ? 12.189  -3.825  -39.660 1.00 34.01  ? 85  GLN   B O   1 
ATOM   1401 C CB  . GLN   B 1 86 ? 10.241  -6.064  -38.072 1.00 35.19  ? 85  GLN   B CB  1 
ATOM   1402 N N   . ASN   B 1 87 ? 11.994  -3.514  -37.426 1.00 29.04  ? 86  ASN   B N   1 
ATOM   1403 C CA  . ASN   B 1 87 ? 11.892  -2.056  -37.516 1.00 30.71  ? 86  ASN   B CA  1 
ATOM   1404 C C   . ASN   B 1 87 ? 13.231  -1.336  -37.362 1.00 28.00  ? 86  ASN   B C   1 
ATOM   1405 O O   . ASN   B 1 87 ? 13.372  -0.219  -37.890 1.00 31.61  ? 86  ASN   B O   1 
ATOM   1406 C CB  . ASN   B 1 87 ? 10.849  -1.527  -36.525 1.00 31.70  ? 86  ASN   B CB  1 
ATOM   1407 C CG  . ASN   B 1 87 ? 9.473   -1.962  -36.967 1.00 40.49  ? 86  ASN   B CG  1 
ATOM   1408 O OD1 . ASN   B 1 87 ? 8.936   -1.394  -37.914 1.00 45.11  ? 86  ASN   B OD1 1 
ATOM   1409 N ND2 . ASN   B 1 87 ? 8.917   -3.005  -36.365 1.00 40.39  ? 86  ASN   B ND2 1 
ATOM   1410 N N   . ASN   B 1 88 ? 14.214  -1.925  -36.662 1.00 27.92  ? 87  ASN   B N   1 
ATOM   1411 C CA  . ASN   B 1 88 ? 15.482  -1.233  -36.418 1.00 29.70  ? 87  ASN   B CA  1 
ATOM   1412 C C   . ASN   B 1 88 ? 16.564  -2.224  -36.009 1.00 27.14  ? 87  ASN   B C   1 
ATOM   1413 O O   . ASN   B 1 88 ? 17.152  -2.140  -34.927 1.00 28.39  ? 87  ASN   B O   1 
ATOM   1414 C CB  . ASN   B 1 88 ? 15.327  -0.048  -35.463 1.00 31.84  ? 87  ASN   B CB  1 
ATOM   1415 C CG  . ASN   B 1 88 ? 16.415  0.992   -35.647 1.00 33.01  ? 87  ASN   B CG  1 
ATOM   1416 O OD1 . ASN   B 1 88 ? 17.446  0.775   -36.301 1.00 31.25  ? 87  ASN   B OD1 1 
ATOM   1417 N ND2 . ASN   B 1 88 ? 16.191  2.170   -35.077 1.00 35.51  ? 87  ASN   B ND2 1 
ATOM   1418 N N   . PRO   B 1 89 ? 16.834  -3.201  -36.898 1.00 26.24  ? 88  PRO   B N   1 
ATOM   1419 C CA  . PRO   B 1 89 ? 17.764  -4.289  -36.592 1.00 25.88  ? 88  PRO   B CA  1 
ATOM   1420 C C   . PRO   B 1 89 ? 19.205  -3.857  -36.366 1.00 24.07  ? 88  PRO   B C   1 
ATOM   1421 O O   . PRO   B 1 89 ? 19.982  -4.581  -35.756 1.00 27.11  ? 88  PRO   B O   1 
ATOM   1422 C CB  . PRO   B 1 89 ? 17.634  -5.187  -37.865 1.00 26.13  ? 88  PRO   B CB  1 
ATOM   1423 C CG  . PRO   B 1 89 ? 17.207  -4.252  -38.990 1.00 25.31  ? 88  PRO   B CG  1 
ATOM   1424 C CD  . PRO   B 1 89 ? 16.274  -3.266  -38.267 1.00 25.64  ? 88  PRO   B CD  1 
ATOM   1425 N N   . HIS   B 1 90 ? 19.569  -2.659  -36.895 1.00 26.66  ? 89  HIS   B N   1 
ATOM   1426 C CA  . HIS   B 1 90 ? 20.964  -2.236  -36.827 1.00 25.62  ? 89  HIS   B CA  1 
ATOM   1427 C C   . HIS   B 1 90 ? 21.240  -1.156  -35.776 1.00 29.77  ? 89  HIS   B C   1 
ATOM   1428 O O   . HIS   B 1 90 ? 22.345  -0.629  -35.723 1.00 30.14  ? 89  HIS   B O   1 
ATOM   1429 C CB  . HIS   B 1 90 ? 21.486  -1.831  -38.221 1.00 26.18  ? 89  HIS   B CB  1 
ATOM   1430 C CG  . HIS   B 1 90 ? 21.295  -2.922  -39.216 1.00 27.60  ? 89  HIS   B CG  1 
ATOM   1431 N ND1 . HIS   B 1 90 ? 21.942  -4.138  -39.099 1.00 28.28  ? 89  HIS   B ND1 1 
ATOM   1432 C CD2 . HIS   B 1 90 ? 20.620  -2.948  -40.390 1.00 25.26  ? 89  HIS   B CD2 1 
ATOM   1433 C CE1 . HIS   B 1 90 ? 21.618  -4.885  -40.145 1.00 25.55  ? 89  HIS   B CE1 1 
ATOM   1434 N NE2 . HIS   B 1 90 ? 20.853  -4.186  -40.936 1.00 26.53  ? 89  HIS   B NE2 1 
ATOM   1435 N N   . ALA   B 1 91 ? 20.298  -0.917  -34.872 1.00 27.54  ? 90  ALA   B N   1 
ATOM   1436 C CA  . ALA   B 1 91 ? 20.434  0.138   -33.877 1.00 29.63  ? 90  ALA   B CA  1 
ATOM   1437 C C   . ALA   B 1 91 ? 21.390  -0.243  -32.741 1.00 32.72  ? 90  ALA   B C   1 
ATOM   1438 O O   . ALA   B 1 91 ? 21.711  -1.410  -32.494 1.00 30.39  ? 90  ALA   B O   1 
ATOM   1439 C CB  . ALA   B 1 91 ? 19.056  0.512   -33.353 1.00 27.70  ? 90  ALA   B CB  1 
ATOM   1440 N N   . SER   B 1 92 ? 21.830  0.786   -31.993 1.00 33.18  ? 91  SER   B N   1 
ATOM   1441 C CA  . SER   B 1 92 ? 22.495  0.617   -30.721 1.00 39.08  ? 91  SER   B CA  1 
ATOM   1442 C C   . SER   B 1 92 ? 21.410  0.414   -29.667 1.00 41.26  ? 91  SER   B C   1 
ATOM   1443 O O   . SER   B 1 92 ? 20.517  1.259   -29.545 1.00 41.79  ? 91  SER   B O   1 
ATOM   1444 C CB  . SER   B 1 92 ? 23.322  1.871   -30.415 1.00 36.44  ? 91  SER   B CB  1 
ATOM   1445 O OG  . SER   B 1 92 ? 23.937  1.735   -29.148 1.00 44.18  ? 91  SER   B OG  1 
ATOM   1446 N N   . TYR   B 1 93 ? 21.473  -0.745  -28.987 1.00 37.25  ? 92  TYR   B N   1 
ATOM   1447 C CA  . TYR   B 1 93 ? 20.620  -1.134  -27.877 1.00 36.48  ? 92  TYR   B CA  1 
ATOM   1448 C C   . TYR   B 1 93 ? 21.483  -1.115  -26.617 1.00 46.14  ? 92  TYR   B C   1 
ATOM   1449 O O   . TYR   B 1 93 ? 21.100  -1.659  -25.590 1.00 50.18  ? 92  TYR   B O   1 
ATOM   1450 C CB  . TYR   B 1 93 ? 20.033  -2.518  -28.199 1.00 33.17  ? 92  TYR   B CB  1 
ATOM   1451 C CG  . TYR   B 1 93 ? 19.029  -2.443  -29.332 1.00 31.69  ? 92  TYR   B CG  1 
ATOM   1452 C CD1 . TYR   B 1 93 ? 17.746  -1.956  -29.098 1.00 33.98  ? 92  TYR   B CD1 1 
ATOM   1453 C CD2 . TYR   B 1 93 ? 19.348  -2.834  -30.648 1.00 29.88  ? 92  TYR   B CD2 1 
ATOM   1454 C CE1 . TYR   B 1 93 ? 16.812  -1.820  -30.110 1.00 33.33  ? 92  TYR   B CE1 1 
ATOM   1455 C CE2 . TYR   B 1 93 ? 18.407  -2.713  -31.655 1.00 31.29  ? 92  TYR   B CE2 1 
ATOM   1456 C CZ  . TYR   B 1 93 ? 17.143  -2.221  -31.399 1.00 33.09  ? 92  TYR   B CZ  1 
ATOM   1457 O OH  . TYR   B 1 93 ? 16.202  -2.116  -32.387 1.00 32.56  ? 92  TYR   B OH  1 
ATOM   1458 N N   . SER   B 1 94 ? 22.649  -0.461  -26.734 1.00 56.81  ? 93  SER   B N   1 
ATOM   1459 C CA  . SER   B 1 94 ? 23.588  -0.181  -25.655 1.00 68.46  ? 93  SER   B CA  1 
ATOM   1460 C C   . SER   B 1 94 ? 22.862  0.319   -24.398 1.00 79.05  ? 93  SER   B C   1 
ATOM   1461 O O   . SER   B 1 94 ? 21.872  1.081   -24.552 1.00 76.34  ? 93  SER   B O   1 
ATOM   1462 C CB  . SER   B 1 94 ? 24.624  0.835   -26.080 1.00 68.90  ? 93  SER   B CB  1 
ATOM   1463 O OG  . SER   B 1 94 ? 25.663  0.232   -26.835 1.00 68.92  ? 93  SER   B OG  1 
ATOM   1464 O OXT . SER   B 1 94 ? 23.343  -0.038  -23.300 1.00 93.81  ? 93  SER   B OXT 1 
ATOM   1465 N N   . HIS   C 1 4  ? 32.745  -23.106 26.204  1.00 80.52  ? 3   HIS   C N   1 
ATOM   1466 C CA  . HIS   C 1 4  ? 31.933  -22.171 27.031  1.00 82.76  ? 3   HIS   C CA  1 
ATOM   1467 C C   . HIS   C 1 4  ? 31.565  -22.878 28.335  1.00 81.09  ? 3   HIS   C C   1 
ATOM   1468 O O   . HIS   C 1 4  ? 32.374  -23.619 28.896  1.00 78.03  ? 3   HIS   C O   1 
ATOM   1469 C CB  . HIS   C 1 4  ? 30.732  -21.656 26.222  1.00 85.87  ? 3   HIS   C CB  1 
ATOM   1470 N N   . ALA   C 1 5  ? 30.343  -22.620 28.813  1.00 76.81  ? 4   ALA   C N   1 
ATOM   1471 C CA  . ALA   C 1 5  ? 29.701  -23.445 29.823  1.00 68.70  ? 4   ALA   C CA  1 
ATOM   1472 C C   . ALA   C 1 5  ? 28.229  -23.061 29.938  1.00 68.23  ? 4   ALA   C C   1 
ATOM   1473 O O   . ALA   C 1 5  ? 27.899  -21.883 30.043  1.00 79.29  ? 4   ALA   C O   1 
ATOM   1474 C CB  . ALA   C 1 5  ? 30.420  -23.314 31.131  1.00 73.20  ? 4   ALA   C CB  1 
ATOM   1475 N N   . PHE   C 1 6  ? 27.363  -24.080 29.920  1.00 59.13  ? 5   PHE   C N   1 
ATOM   1476 C CA  . PHE   C 1 6  ? 25.953  -23.925 29.603  1.00 51.36  ? 5   PHE   C CA  1 
ATOM   1477 C C   . PHE   C 1 6  ? 25.141  -23.944 30.888  1.00 57.05  ? 5   PHE   C C   1 
ATOM   1478 O O   . PHE   C 1 6  ? 25.519  -24.628 31.836  1.00 62.57  ? 5   PHE   C O   1 
ATOM   1479 C CB  . PHE   C 1 6  ? 25.517  -25.071 28.673  1.00 44.81  ? 5   PHE   C CB  1 
ATOM   1480 C CG  . PHE   C 1 6  ? 26.315  -25.113 27.374  1.00 41.45  ? 5   PHE   C CG  1 
ATOM   1481 C CD1 . PHE   C 1 6  ? 27.414  -25.955 27.223  1.00 41.18  ? 5   PHE   C CD1 1 
ATOM   1482 C CD2 . PHE   C 1 6  ? 26.005  -24.258 26.316  1.00 46.10  ? 5   PHE   C CD2 1 
ATOM   1483 C CE1 . PHE   C 1 6  ? 28.140  -25.991 26.030  1.00 45.26  ? 5   PHE   C CE1 1 
ATOM   1484 C CE2 . PHE   C 1 6  ? 26.727  -24.293 25.128  1.00 47.09  ? 5   PHE   C CE2 1 
ATOM   1485 C CZ  . PHE   C 1 6  ? 27.803  -25.146 24.985  1.00 45.41  ? 5   PHE   C CZ  1 
ATOM   1486 N N   . LYS   C 1 7  ? 24.028  -23.199 30.894  1.00 48.26  ? 6   LYS   C N   1 
ATOM   1487 C CA  . LYS   C 1 7  ? 23.095  -23.172 32.010  1.00 49.35  ? 6   LYS   C CA  1 
ATOM   1488 C C   . LYS   C 1 7  ? 21.718  -23.527 31.458  1.00 41.94  ? 6   LYS   C C   1 
ATOM   1489 O O   . LYS   C 1 7  ? 21.499  -23.426 30.251  1.00 51.54  ? 6   LYS   C O   1 
ATOM   1490 C CB  . LYS   C 1 7  ? 23.052  -21.820 32.747  1.00 46.61  ? 6   LYS   C CB  1 
ATOM   1491 N N   . PRO   C 1 8  ? 20.741  -23.935 32.298  1.00 45.85  ? 7   PRO   C N   1 
ATOM   1492 C CA  . PRO   C 1 8  ? 19.399  -24.240 31.797  1.00 45.70  ? 7   PRO   C CA  1 
ATOM   1493 C C   . PRO   C 1 8  ? 18.918  -23.051 30.961  1.00 53.41  ? 7   PRO   C C   1 
ATOM   1494 O O   . PRO   C 1 8  ? 19.235  -21.894 31.270  1.00 54.29  ? 7   PRO   C O   1 
ATOM   1495 C CB  . PRO   C 1 8  ? 18.612  -24.439 33.096  1.00 49.03  ? 7   PRO   C CB  1 
ATOM   1496 C CG  . PRO   C 1 8  ? 19.648  -24.980 34.053  1.00 47.58  ? 7   PRO   C CG  1 
ATOM   1497 C CD  . PRO   C 1 8  ? 20.875  -24.125 33.754  1.00 46.70  ? 7   PRO   C CD  1 
ATOM   1498 N N   . GLY   C 1 9  ? 18.228  -23.352 29.852  1.00 48.14  ? 8   GLY   C N   1 
ATOM   1499 C CA  . GLY   C 1 9  ? 17.611  -22.333 29.015  1.00 46.76  ? 8   GLY   C CA  1 
ATOM   1500 C C   . GLY   C 1 9  ? 18.484  -21.869 27.847  1.00 47.70  ? 8   GLY   C C   1 
ATOM   1501 O O   . GLY   C 1 9  ? 17.945  -21.297 26.899  1.00 56.00  ? 8   GLY   C O   1 
ATOM   1502 N N   . ASP   C 1 10 ? 19.804  -22.133 27.901  1.00 42.00  ? 9   ASP   C N   1 
ATOM   1503 C CA  . ASP   C 1 10 ? 20.715  -21.839 26.810  1.00 40.47  ? 9   ASP   C CA  1 
ATOM   1504 C C   . ASP   C 1 10 ? 20.314  -22.602 25.555  1.00 38.00  ? 9   ASP   C C   1 
ATOM   1505 O O   . ASP   C 1 10 ? 19.926  -23.773 25.614  1.00 36.70  ? 9   ASP   C O   1 
ATOM   1506 C CB  . ASP   C 1 10 ? 22.175  -22.102 27.141  1.00 42.98  ? 9   ASP   C CB  1 
ATOM   1507 C CG  . ASP   C 1 10 ? 22.769  -21.204 28.221  1.00 52.10  ? 9   ASP   C CG  1 
ATOM   1508 O OD1 . ASP   C 1 10 ? 22.208  -20.120 28.434  1.00 52.89  ? 9   ASP   C OD1 1 
ATOM   1509 O OD2 . ASP   C 1 10 ? 23.766  -21.612 28.860  1.00 58.05  ? 9   ASP   C OD2 1 
ATOM   1510 N N   . LEU   C 1 11 ? 20.317  -21.860 24.448  1.00 38.54  ? 10  LEU   C N   1 
ATOM   1511 C CA  . LEU   C 1 11 ? 19.889  -22.366 23.155  1.00 35.97  ? 10  LEU   C CA  1 
ATOM   1512 C C   . LEU   C 1 11 ? 21.117  -22.856 22.425  1.00 35.54  ? 10  LEU   C C   1 
ATOM   1513 O O   . LEU   C 1 11 ? 22.131  -22.173 22.415  1.00 34.94  ? 10  LEU   C O   1 
ATOM   1514 C CB  . LEU   C 1 11 ? 19.216  -21.248 22.358  1.00 39.54  ? 10  LEU   C CB  1 
ATOM   1515 C CG  . LEU   C 1 11 ? 17.874  -20.778 22.909  1.00 35.28  ? 10  LEU   C CG  1 
ATOM   1516 C CD1 . LEU   C 1 11 ? 17.287  -19.780 21.917  1.00 36.86  ? 10  LEU   C CD1 1 
ATOM   1517 C CD2 . LEU   C 1 11 ? 16.902  -21.903 23.247  1.00 36.50  ? 10  LEU   C CD2 1 
ATOM   1518 N N   . VAL   C 1 12 ? 21.018  -24.059 21.817  1.00 30.72  ? 11  VAL   C N   1 
ATOM   1519 C CA  . VAL   C 1 12 ? 22.193  -24.663 21.228  1.00 31.35  ? 11  VAL   C CA  1 
ATOM   1520 C C   . VAL   C 1 12 ? 21.767  -25.410 19.957  1.00 29.36  ? 11  VAL   C C   1 
ATOM   1521 O O   . VAL   C 1 12 ? 20.571  -25.585 19.699  1.00 30.24  ? 11  VAL   C O   1 
ATOM   1522 C CB  . VAL   C 1 12 ? 22.876  -25.639 22.211  1.00 33.24  ? 11  VAL   C CB  1 
ATOM   1523 C CG1 . VAL   C 1 12 ? 23.220  -24.964 23.543  1.00 34.14  ? 11  VAL   C CG1 1 
ATOM   1524 C CG2 . VAL   C 1 12 ? 22.041  -26.889 22.478  1.00 32.32  ? 11  VAL   C CG2 1 
ATOM   1525 N N   . PHE   C 1 13 ? 22.788  -25.809 19.204  1.00 31.53  ? 12  PHE   C N   1 
ATOM   1526 C CA  . PHE   C 1 13 ? 22.724  -26.977 18.329  1.00 28.62  ? 12  PHE   C CA  1 
ATOM   1527 C C   . PHE   C 1 13 ? 23.408  -28.147 19.028  1.00 30.17  ? 12  PHE   C C   1 
ATOM   1528 O O   . PHE   C 1 13 ? 24.525  -28.033 19.563  1.00 31.34  ? 12  PHE   C O   1 
ATOM   1529 C CB  . PHE   C 1 13 ? 23.393  -26.712 16.963  1.00 35.31  ? 12  PHE   C CB  1 
ATOM   1530 C CG  . PHE   C 1 13 ? 22.582  -25.730 16.129  1.00 36.76  ? 12  PHE   C CG  1 
ATOM   1531 C CD1 . PHE   C 1 13 ? 21.519  -26.174 15.339  1.00 32.48  ? 12  PHE   C CD1 1 
ATOM   1532 C CD2 . PHE   C 1 13 ? 22.882  -24.368 16.131  1.00 34.68  ? 12  PHE   C CD2 1 
ATOM   1533 C CE1 . PHE   C 1 13 ? 20.751  -25.280 14.601  1.00 36.59  ? 12  PHE   C CE1 1 
ATOM   1534 C CE2 . PHE   C 1 13 ? 22.093  -23.482 15.416  1.00 34.67  ? 12  PHE   C CE2 1 
ATOM   1535 C CZ  . PHE   C 1 13 ? 21.044  -23.941 14.645  1.00 38.28  ? 12  PHE   C CZ  1 
ATOM   1536 N N   . ALA   C 1 14 ? 22.714  -29.296 19.012  1.00 28.63  ? 13  ALA   C N   1 
ATOM   1537 C CA  . ALA   C 1 14 ? 23.192  -30.477 19.717  1.00 26.37  ? 13  ALA   C CA  1 
ATOM   1538 C C   . ALA   C 1 14 ? 23.480  -31.583 18.718  1.00 29.59  ? 13  ALA   C C   1 
ATOM   1539 O O   . ALA   C 1 14 ? 22.626  -31.888 17.892  1.00 28.12  ? 13  ALA   C O   1 
ATOM   1540 C CB  . ALA   C 1 14 ? 22.141  -30.925 20.708  1.00 24.33  ? 13  ALA   C CB  1 
ATOM   1541 N N   . LYS   C 1 15 ? 24.664  -32.184 18.831  1.00 28.30  ? 14  LYS   C N   1 
ATOM   1542 C CA  . LYS   C 1 15 ? 25.076  -33.161 17.828  1.00 26.65  ? 14  LYS   C CA  1 
ATOM   1543 C C   . LYS   C 1 15 ? 25.093  -34.548 18.440  1.00 27.99  ? 14  LYS   C C   1 
ATOM   1544 O O   . LYS   C 1 15 ? 25.776  -34.799 19.417  1.00 32.00  ? 14  LYS   C O   1 
ATOM   1545 C CB  . LYS   C 1 15 ? 26.509  -32.840 17.376  1.00 28.25  ? 14  LYS   C CB  1 
ATOM   1546 C CG  . LYS   C 1 15 ? 26.974  -33.740 16.236  1.00 31.77  ? 14  LYS   C CG  1 
ATOM   1547 C CD  . LYS   C 1 15 ? 26.162  -33.628 14.934  1.00 29.80  ? 14  LYS   C CD  1 
ATOM   1548 C CE  . LYS   C 1 15 ? 26.652  -34.489 13.771  1.00 31.91  ? 14  LYS   C CE  1 
ATOM   1549 N NZ  . LYS   C 1 15 ? 26.419  -35.927 13.980  1.00 32.62  ? 14  LYS   C NZ  1 
ATOM   1550 N N   . MET   C 1 16 ? 24.312  -35.462 17.866  1.00 27.11  ? 15  MET   C N   1 
ATOM   1551 C CA  . MET   C 1 16 ? 24.392  -36.882 18.185  1.00 26.77  ? 15  MET   C CA  1 
ATOM   1552 C C   . MET   C 1 16 ? 24.809  -37.662 16.953  1.00 31.29  ? 15  MET   C C   1 
ATOM   1553 O O   . MET   C 1 16 ? 24.460  -37.288 15.841  1.00 27.46  ? 15  MET   C O   1 
ATOM   1554 C CB  . MET   C 1 16 ? 23.024  -37.406 18.637  1.00 26.84  ? 15  MET   C CB  1 
ATOM   1555 C CG  . MET   C 1 16 ? 22.594  -36.653 19.894  1.00 34.71  ? 15  MET   C CG  1 
ATOM   1556 S SD  . MET   C 1 16 ? 21.068  -37.311 20.569  1.00 41.63  ? 15  MET   C SD  1 
ATOM   1557 C CE  . MET   C 1 16 ? 20.046  -36.816 19.173  1.00 48.35  ? 15  MET   C CE  1 
ATOM   1558 N N   . LYS   C 1 17 ? 25.523  -38.775 17.180  1.00 31.81  ? 16  LYS   C N   1 
ATOM   1559 C CA  . LYS   C 1 17 ? 25.862  -39.689 16.100  1.00 33.57  ? 16  LYS   C CA  1 
ATOM   1560 C C   . LYS   C 1 17 ? 24.590  -40.107 15.353  1.00 28.55  ? 16  LYS   C C   1 
ATOM   1561 O O   . LYS   C 1 17 ? 23.614  -40.553 15.962  1.00 31.79  ? 16  LYS   C O   1 
ATOM   1562 C CB  . LYS   C 1 17 ? 26.554  -40.895 16.751  1.00 31.64  ? 16  LYS   C CB  1 
ATOM   1563 C CG  . LYS   C 1 17 ? 27.215  -41.842 15.750  1.00 39.37  ? 16  LYS   C CG  1 
ATOM   1564 C CD  . LYS   C 1 17 ? 28.325  -41.102 15.023  1.00 38.82  ? 16  LYS   C CD  1 
ATOM   1565 C CE  . LYS   C 1 17 ? 29.125  -42.044 14.175  1.00 54.61  ? 16  LYS   C CE  1 
ATOM   1566 N NZ  . LYS   C 1 17 ? 30.362  -41.409 13.728  1.00 54.24  ? 16  LYS   C NZ  1 
ATOM   1567 N N   . GLY   C 1 18 ? 24.638  -39.938 14.027  1.00 32.57  ? 17  GLY   C N   1 
ATOM   1568 C CA  . GLY   C 1 18 ? 23.608  -40.430 13.130  1.00 30.85  ? 17  GLY   C CA  1 
ATOM   1569 C C   . GLY   C 1 18 ? 22.602  -39.327 12.777  1.00 33.26  ? 17  GLY   C C   1 
ATOM   1570 O O   . GLY   C 1 18 ? 21.596  -39.606 12.118  1.00 32.95  ? 17  GLY   C O   1 
ATOM   1571 N N   . TYR   C 1 19 ? 22.849  -38.088 13.236  1.00 30.18  ? 18  TYR   C N   1 
ATOM   1572 C CA  . TYR   C 1 19 ? 21.861  -37.014 13.068  1.00 28.79  ? 18  TYR   C CA  1 
ATOM   1573 C C   . TYR   C 1 19 ? 22.594  -35.714 12.829  1.00 28.10  ? 18  TYR   C C   1 
ATOM   1574 O O   . TYR   C 1 19 ? 23.716  -35.530 13.339  1.00 28.67  ? 18  TYR   C O   1 
ATOM   1575 C CB  . TYR   C 1 19 ? 21.024  -36.687 14.307  1.00 26.51  ? 18  TYR   C CB  1 
ATOM   1576 C CG  . TYR   C 1 19 ? 20.330  -37.954 14.757  1.00 28.60  ? 18  TYR   C CG  1 
ATOM   1577 C CD1 . TYR   C 1 19 ? 21.000  -38.867 15.569  1.00 30.18  ? 18  TYR   C CD1 1 
ATOM   1578 C CD2 . TYR   C 1 19 ? 19.079  -38.271 14.270  1.00 29.50  ? 18  TYR   C CD2 1 
ATOM   1579 C CE1 . TYR   C 1 19 ? 20.402  -40.051 15.944  1.00 32.67  ? 18  TYR   C CE1 1 
ATOM   1580 C CE2 . TYR   C 1 19 ? 18.477  -39.470 14.625  1.00 36.70  ? 18  TYR   C CE2 1 
ATOM   1581 C CZ  . TYR   C 1 19 ? 19.141  -40.340 15.471  1.00 34.99  ? 18  TYR   C CZ  1 
ATOM   1582 O OH  . TYR   C 1 19 ? 18.539  -41.501 15.847  1.00 45.64  ? 18  TYR   C OH  1 
ATOM   1583 N N   . PRO   C 1 20 ? 21.989  -34.771 12.059  1.00 27.04  ? 19  PRO   C N   1 
ATOM   1584 C CA  . PRO   C 1 20 ? 22.599  -33.452 11.860  1.00 24.43  ? 19  PRO   C CA  1 
ATOM   1585 C C   . PRO   C 1 20 ? 22.618  -32.662 13.163  1.00 24.81  ? 19  PRO   C C   1 
ATOM   1586 O O   . PRO   C 1 20 ? 21.837  -32.941 14.060  1.00 25.24  ? 19  PRO   C O   1 
ATOM   1587 C CB  . PRO   C 1 20 ? 21.660  -32.768 10.806  1.00 28.06  ? 19  PRO   C CB  1 
ATOM   1588 C CG  . PRO   C 1 20 ? 20.339  -33.461 11.042  1.00 28.98  ? 19  PRO   C CG  1 
ATOM   1589 C CD  . PRO   C 1 20 ? 20.677  -34.914 11.377  1.00 25.91  ? 19  PRO   C CD  1 
ATOM   1590 N N   . HIS   C 1 21 ? 23.445  -31.622 13.202  1.00 26.50  ? 20  HIS   C N   1 
ATOM   1591 C CA  . HIS   C 1 21 ? 23.396  -30.711 14.340  1.00 26.93  ? 20  HIS   C CA  1 
ATOM   1592 C C   . HIS   C 1 21 ? 21.972  -30.191 14.499  1.00 28.18  ? 20  HIS   C C   1 
ATOM   1593 O O   . HIS   C 1 21 ? 21.394  -29.648 13.565  1.00 29.94  ? 20  HIS   C O   1 
ATOM   1594 C CB  . HIS   C 1 21 ? 24.365  -29.540 14.177  1.00 29.72  ? 20  HIS   C CB  1 
ATOM   1595 C CG  . HIS   C 1 21 ? 25.790  -29.996 14.139  1.00 32.12  ? 20  HIS   C CG  1 
ATOM   1596 N ND1 . HIS   C 1 21 ? 26.442  -30.615 13.092  1.00 36.91  ? 20  HIS   C ND1 1 
ATOM   1597 C CD2 . HIS   C 1 21 ? 26.704  -29.865 15.129  1.00 34.12  ? 20  HIS   C CD2 1 
ATOM   1598 C CE1 . HIS   C 1 21 ? 27.702  -30.848 13.450  1.00 36.22  ? 20  HIS   C CE1 1 
ATOM   1599 N NE2 . HIS   C 1 21 ? 27.885  -30.400 14.685  1.00 33.24  ? 20  HIS   C NE2 1 
ATOM   1600 N N   . TRP   C 1 22 ? 21.422  -30.359 15.707  1.00 24.26  ? 21  TRP   C N   1 
ATOM   1601 C CA  . TRP   C 1 22 ? 19.976  -30.260 15.865  1.00 23.97  ? 21  TRP   C CA  1 
ATOM   1602 C C   . TRP   C 1 22 ? 19.606  -29.080 16.772  1.00 26.65  ? 21  TRP   C C   1 
ATOM   1603 O O   . TRP   C 1 22 ? 20.165  -28.908 17.862  1.00 26.13  ? 21  TRP   C O   1 
ATOM   1604 C CB  . TRP   C 1 22 ? 19.448  -31.575 16.470  1.00 23.61  ? 21  TRP   C CB  1 
ATOM   1605 C CG  . TRP   C 1 22 ? 17.977  -31.747 16.174  1.00 26.05  ? 21  TRP   C CG  1 
ATOM   1606 C CD1 . TRP   C 1 22 ? 16.906  -31.128 16.765  1.00 28.39  ? 21  TRP   C CD1 1 
ATOM   1607 C CD2 . TRP   C 1 22 ? 17.439  -32.638 15.179  1.00 26.02  ? 21  TRP   C CD2 1 
ATOM   1608 N NE1 . TRP   C 1 22 ? 15.733  -31.574 16.196  1.00 28.00  ? 21  TRP   C NE1 1 
ATOM   1609 C CE2 . TRP   C 1 22 ? 16.030  -32.503 15.231  1.00 25.19  ? 21  TRP   C CE2 1 
ATOM   1610 C CE3 . TRP   C 1 22 ? 18.019  -33.538 14.275  1.00 25.71  ? 21  TRP   C CE3 1 
ATOM   1611 C CZ2 . TRP   C 1 22 ? 15.202  -33.232 14.367  1.00 26.13  ? 21  TRP   C CZ2 1 
ATOM   1612 C CZ3 . TRP   C 1 22 ? 17.203  -34.256 13.412  1.00 26.94  ? 21  TRP   C CZ3 1 
ATOM   1613 C CH2 . TRP   C 1 22 ? 15.814  -34.079 13.472  1.00 25.94  ? 21  TRP   C CH2 1 
ATOM   1614 N N   . PRO   C 1 23 ? 18.589  -28.247 16.447  1.00 27.35  ? 22  PRO   C N   1 
ATOM   1615 C CA  . PRO   C 1 23 ? 18.230  -27.136 17.339  1.00 26.29  ? 22  PRO   C CA  1 
ATOM   1616 C C   . PRO   C 1 23 ? 17.662  -27.673 18.652  1.00 23.86  ? 22  PRO   C C   1 
ATOM   1617 O O   . PRO   C 1 23 ? 16.794  -28.558 18.688  1.00 26.42  ? 22  PRO   C O   1 
ATOM   1618 C CB  . PRO   C 1 23 ? 17.176  -26.374 16.480  1.00 30.68  ? 22  PRO   C CB  1 
ATOM   1619 C CG  . PRO   C 1 23 ? 16.572  -27.465 15.611  1.00 26.82  ? 22  PRO   C CG  1 
ATOM   1620 C CD  . PRO   C 1 23 ? 17.809  -28.250 15.183  1.00 26.09  ? 22  PRO   C CD  1 
ATOM   1621 N N   . ALA   C 1 24 ? 18.198  -27.151 19.757  1.00 28.16  ? 23  ALA   C N   1 
ATOM   1622 C CA  . ALA   C 1 24 ? 17.878  -27.695 21.069  1.00 31.43  ? 23  ALA   C CA  1 
ATOM   1623 C C   . ALA   C 1 24 ? 18.075  -26.634 22.145  1.00 33.93  ? 23  ALA   C C   1 
ATOM   1624 O O   . ALA   C 1 24 ? 18.566  -25.533 21.875  1.00 32.92  ? 23  ALA   C O   1 
ATOM   1625 C CB  . ALA   C 1 24 ? 18.762  -28.915 21.357  1.00 28.82  ? 23  ALA   C CB  1 
ATOM   1626 N N   . ARG   C 1 25 ? 17.775  -27.022 23.396  1.00 31.87  ? 24  ARG   C N   1 
ATOM   1627 C CA  . ARG   C 1 25 ? 18.195  -26.189 24.509  1.00 31.81  ? 24  ARG   C CA  1 
ATOM   1628 C C   . ARG   C 1 25 ? 18.630  -27.059 25.686  1.00 30.15  ? 24  ARG   C C   1 
ATOM   1629 O O   . ARG   C 1 25 ? 18.269  -28.231 25.744  1.00 32.43  ? 24  ARG   C O   1 
ATOM   1630 C CB  . ARG   C 1 25 ? 17.010  -25.330 24.947  1.00 32.93  ? 24  ARG   C CB  1 
ATOM   1631 C CG  . ARG   C 1 25 ? 15.706  -26.059 25.249  1.00 41.79  ? 24  ARG   C CG  1 
ATOM   1632 C CD  . ARG   C 1 25 ? 14.710  -25.147 25.979  1.00 40.94  ? 24  ARG   C CD  1 
ATOM   1633 N NE  . ARG   C 1 25 ? 13.566  -25.955 26.409  1.00 48.11  ? 24  ARG   C NE  1 
ATOM   1634 C CZ  . ARG   C 1 25 ? 12.271  -25.711 26.208  1.00 53.32  ? 24  ARG   C CZ  1 
ATOM   1635 N NH1 . ARG   C 1 25 ? 11.880  -24.603 25.602  1.00 52.42  ? 24  ARG   C NH1 1 
ATOM   1636 N NH2 . ARG   C 1 25 ? 11.365  -26.582 26.635  1.00 56.01  ? 24  ARG   C NH2 1 
ATOM   1637 N N   . ILE   C 1 26 ? 19.317  -26.406 26.623  1.00 33.87  ? 25  ILE   C N   1 
ATOM   1638 C CA  . ILE   C 1 26 ? 19.726  -26.982 27.897  1.00 33.60  ? 25  ILE   C CA  1 
ATOM   1639 C C   . ILE   C 1 26 ? 18.521  -26.952 28.818  1.00 41.65  ? 25  ILE   C C   1 
ATOM   1640 O O   . ILE   C 1 26 ? 17.935  -25.892 29.034  1.00 43.05  ? 25  ILE   C O   1 
ATOM   1641 C CB  . ILE   C 1 26 ? 20.901  -26.181 28.491  1.00 36.69  ? 25  ILE   C CB  1 
ATOM   1642 C CG1 . ILE   C 1 26 ? 22.025  -25.916 27.492  1.00 41.45  ? 25  ILE   C CG1 1 
ATOM   1643 C CG2 . ILE   C 1 26 ? 21.435  -26.834 29.770  1.00 37.15  ? 25  ILE   C CG2 1 
ATOM   1644 C CD1 . ILE   C 1 26 ? 22.823  -27.123 27.044  1.00 42.98  ? 25  ILE   C CD1 1 
ATOM   1645 N N   . ASP   C 1 27 ? 18.182  -28.117 29.372  1.00 37.74  ? 26  ASP   C N   1 
ATOM   1646 C CA  . ASP   C 1 27 ? 17.138  -28.207 30.383  1.00 47.29  ? 26  ASP   C CA  1 
ATOM   1647 C C   . ASP   C 1 27 ? 17.764  -28.211 31.778  1.00 54.26  ? 26  ASP   C C   1 
ATOM   1648 O O   . ASP   C 1 27 ? 18.968  -28.419 31.909  1.00 57.08  ? 26  ASP   C O   1 
ATOM   1649 C CB  . ASP   C 1 27 ? 16.273  -29.433 30.143  1.00 47.75  ? 26  ASP   C CB  1 
ATOM   1650 C CG  . ASP   C 1 27 ? 15.046  -29.192 29.279  1.00 53.47  ? 26  ASP   C CG  1 
ATOM   1651 O OD1 . ASP   C 1 27 ? 14.914  -28.061 28.752  1.00 50.29  ? 26  ASP   C OD1 1 
ATOM   1652 O OD2 . ASP   C 1 27 ? 14.217  -30.125 29.192  1.00 60.70  ? 26  ASP   C OD2 1 
ATOM   1653 N N   . ASP   C 1 28 ? 16.955  -27.948 32.817  1.00 64.51  ? 27  ASP   C N   1 
ATOM   1654 C CA  . ASP   C 1 28 ? 17.358  -28.215 34.195  1.00 64.96  ? 27  ASP   C CA  1 
ATOM   1655 C C   . ASP   C 1 28 ? 16.944  -29.646 34.535  1.00 63.00  ? 27  ASP   C C   1 
ATOM   1656 O O   . ASP   C 1 28 ? 16.182  -30.252 33.785  1.00 59.13  ? 27  ASP   C O   1 
ATOM   1657 C CB  . ASP   C 1 28 ? 16.859  -27.148 35.164  1.00 66.10  ? 27  ASP   C CB  1 
ATOM   1658 N N   . ILE   C 1 29 ? 17.499  -30.199 35.623  1.00 58.54  ? 28  ILE   C N   1 
ATOM   1659 C CA  . ILE   C 1 29 ? 17.099  -31.510 36.111  1.00 58.21  ? 28  ILE   C CA  1 
ATOM   1660 C C   . ILE   C 1 29 ? 16.212  -31.297 37.334  1.00 58.22  ? 28  ILE   C C   1 
ATOM   1661 O O   . ILE   C 1 29 ? 16.554  -30.476 38.185  1.00 54.64  ? 28  ILE   C O   1 
ATOM   1662 C CB  . ILE   C 1 29 ? 18.331  -32.364 36.463  1.00 55.55  ? 28  ILE   C CB  1 
ATOM   1663 N N   . ALA   C 1 30 ? 15.083  -32.023 37.417  1.00 55.36  ? 29  ALA   C N   1 
ATOM   1664 C CA  . ALA   C 1 30 ? 14.243  -31.985 38.613  1.00 54.85  ? 29  ALA   C CA  1 
ATOM   1665 C C   . ALA   C 1 30 ? 15.021  -32.551 39.805  1.00 57.35  ? 29  ALA   C C   1 
ATOM   1666 O O   . ALA   C 1 30 ? 15.754  -33.539 39.664  1.00 49.19  ? 29  ALA   C O   1 
ATOM   1667 C CB  . ALA   C 1 30 ? 12.937  -32.739 38.395  1.00 50.30  ? 29  ALA   C CB  1 
ATOM   1668 N N   . ASP   C 1 31 ? 14.883  -31.904 40.975  1.00 49.82  ? 30  ASP   C N   1 
ATOM   1669 C CA  . ASP   C 1 31 ? 15.412  -32.499 42.192  1.00 52.32  ? 30  ASP   C CA  1 
ATOM   1670 C C   . ASP   C 1 31 ? 14.746  -33.861 42.425  1.00 58.69  ? 30  ASP   C C   1 
ATOM   1671 O O   . ASP   C 1 31 ? 13.510  -33.994 42.400  1.00 54.39  ? 30  ASP   C O   1 
ATOM   1672 C CB  . ASP   C 1 31 ? 15.331  -31.581 43.400  1.00 53.60  ? 30  ASP   C CB  1 
ATOM   1673 C CG  . ASP   C 1 31 ? 16.228  -32.009 44.555  1.00 55.66  ? 30  ASP   C CG  1 
ATOM   1674 O OD1 . ASP   C 1 31 ? 17.270  -31.363 44.757  1.00 57.09  ? 30  ASP   C OD1 1 
ATOM   1675 O OD2 . ASP   C 1 31 ? 15.889  -32.991 45.239  1.00 64.56  ? 30  ASP   C OD2 1 
ATOM   1676 N N   . GLY   C 1 32 ? 15.608  -34.868 42.621  1.00 55.67  ? 31  GLY   C N   1 
ATOM   1677 C CA  . GLY   C 1 32 ? 15.174  -36.225 42.919  1.00 59.99  ? 31  GLY   C CA  1 
ATOM   1678 C C   . GLY   C 1 32 ? 14.959  -37.065 41.663  1.00 54.25  ? 31  GLY   C C   1 
ATOM   1679 O O   . GLY   C 1 32 ? 14.533  -38.213 41.775  1.00 51.78  ? 31  GLY   C O   1 
ATOM   1680 N N   . ALA   C 1 33 ? 15.234  -36.463 40.491  1.00 47.94  ? 32  ALA   C N   1 
ATOM   1681 C CA  . ALA   C 1 33 ? 15.237  -37.143 39.208  1.00 46.31  ? 32  ALA   C CA  1 
ATOM   1682 C C   . ALA   C 1 33 ? 16.596  -37.809 38.985  1.00 51.80  ? 32  ALA   C C   1 
ATOM   1683 O O   . ALA   C 1 33 ? 17.544  -37.550 39.730  1.00 51.76  ? 32  ALA   C O   1 
ATOM   1684 C CB  . ALA   C 1 33 ? 14.953  -36.155 38.100  1.00 41.69  ? 32  ALA   C CB  1 
ATOM   1685 N N   . VAL   C 1 34 ? 16.675  -38.646 37.937  1.00 48.90  ? 33  VAL   C N   1 
ATOM   1686 C CA  . VAL   C 1 34 ? 17.899  -39.344 37.561  1.00 57.56  ? 33  VAL   C CA  1 
ATOM   1687 C C   . VAL   C 1 34 ? 18.939  -38.304 37.141  1.00 57.37  ? 33  VAL   C C   1 
ATOM   1688 O O   . VAL   C 1 34 ? 18.677  -37.484 36.257  1.00 49.84  ? 33  VAL   C O   1 
ATOM   1689 C CB  . VAL   C 1 34 ? 17.740  -40.415 36.462  1.00 65.05  ? 33  VAL   C CB  1 
ATOM   1690 C CG1 . VAL   C 1 34 ? 19.083  -41.009 36.034  1.00 65.80  ? 33  VAL   C CG1 1 
ATOM   1691 C CG2 . VAL   C 1 34 ? 16.763  -41.512 36.866  1.00 63.34  ? 33  VAL   C CG2 1 
ATOM   1692 N N   . LYS   C 1 35 ? 20.116  -38.387 37.789  1.00 55.76  ? 34  LYS   C N   1 
ATOM   1693 C CA  . LYS   C 1 35 ? 21.265  -37.539 37.520  1.00 52.29  ? 34  LYS   C CA  1 
ATOM   1694 C C   . LYS   C 1 35 ? 21.786  -37.846 36.115  1.00 48.06  ? 34  LYS   C C   1 
ATOM   1695 O O   . LYS   C 1 35 ? 21.727  -38.988 35.643  1.00 49.05  ? 34  LYS   C O   1 
ATOM   1696 C CB  . LYS   C 1 35 ? 22.313  -37.764 38.618  1.00 53.09  ? 34  LYS   C CB  1 
ATOM   1697 N N   . PRO   C 1 36 ? 22.268  -36.824 35.374  1.00 43.56  ? 35  PRO   C N   1 
ATOM   1698 C CA  . PRO   C 1 36 ? 22.914  -37.080 34.090  1.00 43.56  ? 35  PRO   C CA  1 
ATOM   1699 C C   . PRO   C 1 36 ? 24.055  -38.046 34.392  1.00 47.55  ? 35  PRO   C C   1 
ATOM   1700 O O   . PRO   C 1 36 ? 24.491  -38.152 35.545  1.00 45.49  ? 35  PRO   C O   1 
ATOM   1701 C CB  . PRO   C 1 36 ? 23.447  -35.678 33.676  1.00 49.42  ? 35  PRO   C CB  1 
ATOM   1702 C CG  . PRO   C 1 36 ? 22.589  -34.682 34.443  1.00 50.08  ? 35  PRO   C CG  1 
ATOM   1703 C CD  . PRO   C 1 36 ? 22.216  -35.397 35.737  1.00 45.58  ? 35  PRO   C CD  1 
ATOM   1704 N N   . PRO   C 1 37 ? 24.608  -38.757 33.388  1.00 42.90  ? 36  PRO   C N   1 
ATOM   1705 C CA  . PRO   C 1 37 ? 25.954  -39.294 33.537  1.00 42.84  ? 36  PRO   C CA  1 
ATOM   1706 C C   . PRO   C 1 37 ? 26.897  -38.148 33.891  1.00 44.19  ? 36  PRO   C C   1 
ATOM   1707 O O   . PRO   C 1 37 ? 26.597  -36.975 33.648  1.00 38.97  ? 36  PRO   C O   1 
ATOM   1708 C CB  . PRO   C 1 37 ? 26.211  -39.855 32.133  1.00 40.53  ? 36  PRO   C CB  1 
ATOM   1709 C CG  . PRO   C 1 37 ? 24.840  -40.324 31.706  1.00 42.71  ? 36  PRO   C CG  1 
ATOM   1710 C CD  . PRO   C 1 37 ? 23.984  -39.140 32.107  1.00 37.92  ? 36  PRO   C CD  1 
ATOM   1711 N N   . PRO   C 1 38 ? 28.082  -38.471 34.451  1.00 40.84  ? 37  PRO   C N   1 
ATOM   1712 C CA  . PRO   C 1 38 ? 29.081  -37.460 34.774  1.00 40.54  ? 37  PRO   C CA  1 
ATOM   1713 C C   . PRO   C 1 38 ? 29.340  -36.532 33.599  1.00 41.21  ? 37  PRO   C C   1 
ATOM   1714 O O   . PRO   C 1 38 ? 29.659  -36.983 32.493  1.00 37.49  ? 37  PRO   C O   1 
ATOM   1715 C CB  . PRO   C 1 38 ? 30.344  -38.314 35.122  1.00 39.06  ? 37  PRO   C CB  1 
ATOM   1716 C CG  . PRO   C 1 38 ? 29.781  -39.648 35.543  1.00 39.34  ? 37  PRO   C CG  1 
ATOM   1717 C CD  . PRO   C 1 38 ? 28.526  -39.843 34.740  1.00 42.36  ? 37  PRO   C CD  1 
ATOM   1718 N N   . ASN   C 1 39 ? 29.174  -35.233 33.879  1.00 38.75  ? 38  ASN   C N   1 
ATOM   1719 C CA  . ASN   C 1 39 ? 29.584  -34.155 33.006  1.00 38.93  ? 38  ASN   C CA  1 
ATOM   1720 C C   . ASN   C 1 39 ? 28.657  -34.074 31.788  1.00 36.01  ? 38  ASN   C C   1 
ATOM   1721 O O   . ASN   C 1 39 ? 29.094  -33.623 30.732  1.00 42.96  ? 38  ASN   C O   1 
ATOM   1722 C CB  . ASN   C 1 39 ? 31.060  -34.232 32.613  1.00 38.59  ? 38  ASN   C CB  1 
ATOM   1723 C CG  . ASN   C 1 39 ? 31.548  -32.928 32.017  1.00 47.18  ? 38  ASN   C CG  1 
ATOM   1724 O OD1 . ASN   C 1 39 ? 31.028  -31.853 32.346  1.00 65.00  ? 38  ASN   C OD1 1 
ATOM   1725 N ND2 . ASN   C 1 39 ? 32.525  -32.982 31.122  1.00 47.26  ? 38  ASN   C ND2 1 
ATOM   1726 N N   . LYS   C 1 40 ? 27.407  -34.544 31.918  1.00 35.49  ? 39  LYS   C N   1 
ATOM   1727 C CA  . LYS   C 1 40 ? 26.495  -34.424 30.790  1.00 29.61  ? 39  LYS   C CA  1 
ATOM   1728 C C   . LYS   C 1 40 ? 25.346  -33.490 31.156  1.00 33.54  ? 39  LYS   C C   1 
ATOM   1729 O O   . LYS   C 1 40 ? 24.983  -33.336 32.317  1.00 36.40  ? 39  LYS   C O   1 
ATOM   1730 C CB  . LYS   C 1 40 ? 25.820  -35.726 30.345  1.00 30.11  ? 39  LYS   C CB  1 
ATOM   1731 C CG  . LYS   C 1 40 ? 26.696  -36.867 29.896  1.00 38.77  ? 39  LYS   C CG  1 
ATOM   1732 C CD  . LYS   C 1 40 ? 27.843  -36.619 28.939  1.00 42.38  ? 39  LYS   C CD  1 
ATOM   1733 C CE  . LYS   C 1 40 ? 28.468  -37.965 28.622  1.00 43.96  ? 39  LYS   C CE  1 
ATOM   1734 N NZ  . LYS   C 1 40 ? 29.497  -37.808 27.591  1.00 52.94  ? 39  LYS   C NZ  1 
ATOM   1735 N N   . TYR   C 1 41 ? 24.776  -32.862 30.129  1.00 30.16  ? 40  TYR   C N   1 
ATOM   1736 C CA  . TYR   C 1 41 ? 23.662  -31.940 30.293  1.00 30.31  ? 40  TYR   C CA  1 
ATOM   1737 C C   . TYR   C 1 41 ? 22.384  -32.575 29.768  1.00 32.55  ? 40  TYR   C C   1 
ATOM   1738 O O   . TYR   C 1 41 ? 22.426  -33.315 28.780  1.00 31.05  ? 40  TYR   C O   1 
ATOM   1739 C CB  . TYR   C 1 41 ? 23.828  -30.733 29.375  1.00 32.10  ? 40  TYR   C CB  1 
ATOM   1740 C CG  . TYR   C 1 41 ? 25.002  -29.854 29.768  1.00 30.64  ? 40  TYR   C CG  1 
ATOM   1741 C CD1 . TYR   C 1 41 ? 26.289  -30.074 29.266  1.00 33.96  ? 40  TYR   C CD1 1 
ATOM   1742 C CD2 . TYR   C 1 41 ? 24.820  -28.796 30.662  1.00 33.88  ? 40  TYR   C CD2 1 
ATOM   1743 C CE1 . TYR   C 1 41 ? 27.354  -29.264 29.622  1.00 43.08  ? 40  TYR   C CE1 1 
ATOM   1744 C CE2 . TYR   C 1 41 ? 25.877  -27.962 30.988  1.00 35.58  ? 40  TYR   C CE2 1 
ATOM   1745 C CZ  . TYR   C 1 41 ? 27.143  -28.209 30.497  1.00 42.82  ? 40  TYR   C CZ  1 
ATOM   1746 O OH  . TYR   C 1 41 ? 28.177  -27.379 30.839  1.00 54.48  ? 40  TYR   C OH  1 
ATOM   1747 N N   . PRO   C 1 42 ? 21.216  -32.261 30.377  1.00 34.35  ? 41  PRO   C N   1 
ATOM   1748 C CA  . PRO   C 1 42 ? 19.919  -32.677 29.829  1.00 30.75  ? 41  PRO   C CA  1 
ATOM   1749 C C   . PRO   C 1 42 ? 19.629  -31.713 28.689  1.00 31.20  ? 41  PRO   C C   1 
ATOM   1750 O O   . PRO   C 1 42 ? 19.685  -30.483 28.878  1.00 30.89  ? 41  PRO   C O   1 
ATOM   1751 C CB  . PRO   C 1 42 ? 18.891  -32.518 30.949  1.00 34.34  ? 41  PRO   C CB  1 
ATOM   1752 C CG  . PRO   C 1 42 ? 19.605  -31.663 31.954  1.00 39.10  ? 41  PRO   C CG  1 
ATOM   1753 C CD  . PRO   C 1 42 ? 21.081  -31.454 31.602  1.00 37.07  ? 41  PRO   C CD  1 
ATOM   1754 N N   . ILE   C 1 43 ? 19.367  -32.315 27.530  1.00 31.67  ? 42  ILE   C N   1 
ATOM   1755 C CA  . ILE   C 1 43 ? 19.061  -31.560 26.317  1.00 29.70  ? 42  ILE   C CA  1 
ATOM   1756 C C   . ILE   C 1 43 ? 17.613  -31.803 25.955  1.00 30.37  ? 42  ILE   C C   1 
ATOM   1757 O O   . ILE   C 1 43 ? 17.136  -32.934 25.987  1.00 29.73  ? 42  ILE   C O   1 
ATOM   1758 C CB  . ILE   C 1 43 ? 19.961  -32.021 25.167  1.00 28.51  ? 42  ILE   C CB  1 
ATOM   1759 C CG1 . ILE   C 1 43 ? 21.461  -31.846 25.503  1.00 29.62  ? 42  ILE   C CG1 1 
ATOM   1760 C CG2 . ILE   C 1 43 ? 19.548  -31.320 23.864  1.00 29.56  ? 42  ILE   C CG2 1 
ATOM   1761 C CD1 . ILE   C 1 43 ? 21.813  -30.452 25.986  1.00 33.18  ? 42  ILE   C CD1 1 
ATOM   1762 N N   . PHE   C 1 44 ? 16.939  -30.745 25.473  1.00 32.29  ? 43  PHE   C N   1 
ATOM   1763 C CA  . PHE   C 1 44 ? 15.635  -30.961 24.879  1.00 32.49  ? 43  PHE   C CA  1 
ATOM   1764 C C   . PHE   C 1 44 ? 15.767  -30.601 23.404  1.00 28.84  ? 43  PHE   C C   1 
ATOM   1765 O O   . PHE   C 1 44 ? 16.326  -29.547 23.107  1.00 30.86  ? 43  PHE   C O   1 
ATOM   1766 C CB  . PHE   C 1 44 ? 14.648  -29.973 25.518  1.00 35.24  ? 43  PHE   C CB  1 
ATOM   1767 C CG  . PHE   C 1 44 ? 13.268  -29.904 24.878  1.00 36.45  ? 43  PHE   C CG  1 
ATOM   1768 C CD1 . PHE   C 1 44 ? 12.303  -30.886 25.133  1.00 39.17  ? 43  PHE   C CD1 1 
ATOM   1769 C CD2 . PHE   C 1 44 ? 12.953  -28.865 23.996  1.00 39.09  ? 43  PHE   C CD2 1 
ATOM   1770 C CE1 . PHE   C 1 44 ? 11.043  -30.834 24.537  1.00 41.39  ? 43  PHE   C CE1 1 
ATOM   1771 C CE2 . PHE   C 1 44 ? 11.700  -28.823 23.389  1.00 37.51  ? 43  PHE   C CE2 1 
ATOM   1772 C CZ  . PHE   C 1 44 ? 10.745  -29.785 23.671  1.00 40.20  ? 43  PHE   C CZ  1 
ATOM   1773 N N   . PHE   C 1 45 ? 15.232  -31.465 22.533  1.00 27.72  ? 44  PHE   C N   1 
ATOM   1774 C CA  . PHE   C 1 45 ? 15.389  -31.255 21.100  1.00 31.49  ? 44  PHE   C CA  1 
ATOM   1775 C C   . PHE   C 1 45 ? 14.131  -30.585 20.564  1.00 29.51  ? 44  PHE   C C   1 
ATOM   1776 O O   . PHE   C 1 45 ? 13.030  -31.133 20.696  1.00 31.16  ? 44  PHE   C O   1 
ATOM   1777 C CB  . PHE   C 1 45 ? 15.649  -32.556 20.341  1.00 28.27  ? 44  PHE   C CB  1 
ATOM   1778 C CG  . PHE   C 1 45 ? 17.011  -33.142 20.670  1.00 28.90  ? 44  PHE   C CG  1 
ATOM   1779 C CD1 . PHE   C 1 45 ? 18.132  -32.799 19.924  1.00 29.34  ? 44  PHE   C CD1 1 
ATOM   1780 C CD2 . PHE   C 1 45 ? 17.158  -33.988 21.764  1.00 29.52  ? 44  PHE   C CD2 1 
ATOM   1781 C CE1 . PHE   C 1 45 ? 19.374  -33.351 20.234  1.00 29.79  ? 44  PHE   C CE1 1 
ATOM   1782 C CE2 . PHE   C 1 45 ? 18.400  -34.530 22.074  1.00 29.91  ? 44  PHE   C CE2 1 
ATOM   1783 C CZ  . PHE   C 1 45 ? 19.497  -34.203 21.313  1.00 29.80  ? 44  PHE   C CZ  1 
ATOM   1784 N N   . PHE   C 1 46 ? 14.317  -29.433 19.901  1.00 29.03  ? 45  PHE   C N   1 
ATOM   1785 C CA  . PHE   C 1 46 ? 13.166  -28.819 19.261  1.00 29.77  ? 45  PHE   C CA  1 
ATOM   1786 C C   . PHE   C 1 46 ? 12.658  -29.647 18.082  1.00 31.63  ? 45  PHE   C C   1 
ATOM   1787 O O   . PHE   C 1 46 ? 13.368  -30.431 17.457  1.00 29.93  ? 45  PHE   C O   1 
ATOM   1788 C CB  . PHE   C 1 46 ? 13.474  -27.381 18.838  1.00 27.22  ? 45  PHE   C CB  1 
ATOM   1789 C CG  . PHE   C 1 46 ? 13.742  -26.384 19.958  1.00 29.03  ? 45  PHE   C CG  1 
ATOM   1790 C CD1 . PHE   C 1 46 ? 12.685  -25.924 20.739  1.00 33.89  ? 45  PHE   C CD1 1 
ATOM   1791 C CD2 . PHE   C 1 46 ? 15.020  -25.850 20.155  1.00 30.53  ? 45  PHE   C CD2 1 
ATOM   1792 C CE1 . PHE   C 1 46 ? 12.933  -25.005 21.750  1.00 33.65  ? 45  PHE   C CE1 1 
ATOM   1793 C CE2 . PHE   C 1 46 ? 15.262  -24.942 21.177  1.00 34.14  ? 45  PHE   C CE2 1 
ATOM   1794 C CZ  . PHE   C 1 46 ? 14.213  -24.508 21.959  1.00 33.34  ? 45  PHE   C CZ  1 
ATOM   1795 N N   . GLY   C 1 47 ? 11.359  -29.492 17.793  1.00 28.00  ? 46  GLY   C N   1 
ATOM   1796 C CA  . GLY   C 1 47 ? 10.770  -30.176 16.666  1.00 32.45  ? 46  GLY   C CA  1 
ATOM   1797 C C   . GLY   C 1 47 ? 10.289  -31.559 17.081  1.00 39.88  ? 46  GLY   C C   1 
ATOM   1798 O O   . GLY   C 1 47 ? 9.081   -31.789 17.178  1.00 45.77  ? 46  GLY   C O   1 
ATOM   1799 N N   . THR   C 1 48 ? 11.251  -32.457 17.365  1.00 33.37  ? 47  THR   C N   1 
ATOM   1800 C CA  . THR   C 1 48 ? 10.912  -33.800 17.820  1.00 32.45  ? 47  THR   C CA  1 
ATOM   1801 C C   . THR   C 1 48 ? 10.460  -33.788 19.283  1.00 34.17  ? 47  THR   C C   1 
ATOM   1802 O O   . THR   C 1 48 ? 9.737   -34.702 19.705  1.00 39.86  ? 47  THR   C O   1 
ATOM   1803 C CB  . THR   C 1 48 ? 12.073  -34.777 17.612  1.00 31.37  ? 47  THR   C CB  1 
ATOM   1804 O OG1 . THR   C 1 48 ? 12.951  -34.235 18.610  1.00 31.04  ? 47  THR   C OG1 1 
ATOM   1805 C CG2 . THR   C 1 48 ? 12.510  -34.901 16.156  1.00 31.86  ? 47  THR   C CG2 1 
ATOM   1806 N N   . HIS   C 1 49 ? 10.890  -32.789 20.061  1.00 32.25  ? 48  HIS   C N   1 
ATOM   1807 C CA  . HIS   C 1 49 ? 10.643  -32.655 21.491  1.00 36.17  ? 48  HIS   C CA  1 
ATOM   1808 C C   . HIS   C 1 49 ? 11.139  -33.870 22.282  1.00 35.00  ? 48  HIS   C C   1 
ATOM   1809 O O   . HIS   C 1 49 ? 10.562  -34.206 23.319  1.00 42.65  ? 48  HIS   C O   1 
ATOM   1810 C CB  . HIS   C 1 49 ? 9.164   -32.378 21.796  1.00 36.97  ? 48  HIS   C CB  1 
ATOM   1811 C CG  . HIS   C 1 49 ? 8.607   -31.314 20.912  1.00 40.91  ? 48  HIS   C CG  1 
ATOM   1812 N ND1 . HIS   C 1 49 ? 7.523   -31.530 20.083  1.00 47.77  ? 48  HIS   C ND1 1 
ATOM   1813 C CD2 . HIS   C 1 49 ? 9.048   -30.082 20.647  1.00 39.31  ? 48  HIS   C CD2 1 
ATOM   1814 C CE1 . HIS   C 1 49 ? 7.291   -30.430 19.377  1.00 47.02  ? 48  HIS   C CE1 1 
ATOM   1815 N NE2 . HIS   C 1 49 ? 8.200   -29.538 19.714  1.00 46.25  ? 48  HIS   C NE2 1 
ATOM   1816 N N   . GLU   C 1 50 ? 12.211  -34.508 21.815  1.00 36.87  ? 49  GLU   C N   1 
ATOM   1817 C CA  . GLU   C 1 50 ? 12.864  -35.577 22.556  1.00 34.35  ? 49  GLU   C CA  1 
ATOM   1818 C C   . GLU   C 1 50 ? 13.878  -35.019 23.556  1.00 34.93  ? 49  GLU   C C   1 
ATOM   1819 O O   . GLU   C 1 50 ? 14.185  -33.831 23.571  1.00 33.24  ? 49  GLU   C O   1 
ATOM   1820 C CB  . GLU   C 1 50 ? 13.528  -36.512 21.551  1.00 37.59  ? 49  GLU   C CB  1 
ATOM   1821 C CG  . GLU   C 1 50 ? 12.560  -37.215 20.605  1.00 40.51  ? 49  GLU   C CG  1 
ATOM   1822 C CD  . GLU   C 1 50 ? 13.371  -37.768 19.442  1.00 48.92  ? 49  GLU   C CD  1 
ATOM   1823 O OE1 . GLU   C 1 50 ? 13.408  -38.990 19.252  1.00 56.71  ? 49  GLU   C OE1 1 
ATOM   1824 O OE2 . GLU   C 1 50 ? 14.005  -36.954 18.737  1.00 51.36  ? 49  GLU   C OE2 1 
ATOM   1825 N N   . THR   C 1 51 ? 14.377  -35.914 24.430  1.00 34.19  ? 50  THR   C N   1 
ATOM   1826 C CA  . THR   C 1 51 ? 15.440  -35.587 25.378  1.00 33.95  ? 50  THR   C CA  1 
ATOM   1827 C C   . THR   C 1 51 ? 16.586  -36.595 25.277  1.00 30.34  ? 50  THR   C C   1 
ATOM   1828 O O   . THR   C 1 51 ? 16.441  -37.717 24.800  1.00 32.99  ? 50  THR   C O   1 
ATOM   1829 C CB  . THR   C 1 51 ? 14.924  -35.461 26.813  1.00 36.58  ? 50  THR   C CB  1 
ATOM   1830 O OG1 . THR   C 1 51 ? 14.298  -36.723 27.058  1.00 39.08  ? 50  THR   C OG1 1 
ATOM   1831 C CG2 . THR   C 1 51 ? 13.968  -34.296 27.011  1.00 37.67  ? 50  THR   C CG2 1 
ATOM   1832 N N   . ALA   C 1 52 ? 17.774  -36.123 25.664  1.00 31.77  ? 51  ALA   C N   1 
ATOM   1833 C CA  . ALA   C 1 52 ? 18.963  -36.955 25.811  1.00 32.22  ? 51  ALA   C CA  1 
ATOM   1834 C C   . ALA   C 1 52 ? 19.925  -36.256 26.771  1.00 34.67  ? 51  ALA   C C   1 
ATOM   1835 O O   . ALA   C 1 52 ? 19.705  -35.114 27.183  1.00 36.33  ? 51  ALA   C O   1 
ATOM   1836 C CB  . ALA   C 1 52 ? 19.600  -37.207 24.468  1.00 31.89  ? 51  ALA   C CB  1 
ATOM   1837 N N   . PHE   C 1 53 ? 21.002  -36.961 27.169  1.00 33.01  ? 52  PHE   C N   1 
ATOM   1838 C CA  . PHE   C 1 53 ? 22.106  -36.340 27.891  1.00 33.69  ? 52  PHE   C CA  1 
ATOM   1839 C C   . PHE   C 1 53 ? 23.297  -36.250 26.949  1.00 31.54  ? 52  PHE   C C   1 
ATOM   1840 O O   . PHE   C 1 53 ? 23.664  -37.228 26.306  1.00 32.47  ? 52  PHE   C O   1 
ATOM   1841 C CB  . PHE   C 1 53 ? 22.466  -37.276 29.060  1.00 31.99  ? 52  PHE   C CB  1 
ATOM   1842 C CG  . PHE   C 1 53 ? 21.462  -37.258 30.193  1.00 32.00  ? 52  PHE   C CG  1 
ATOM   1843 C CD1 . PHE   C 1 53 ? 21.071  -36.069 30.800  1.00 35.35  ? 52  PHE   C CD1 1 
ATOM   1844 C CD2 . PHE   C 1 53 ? 20.898  -38.450 30.641  1.00 40.65  ? 52  PHE   C CD2 1 
ATOM   1845 C CE1 . PHE   C 1 53 ? 20.145  -36.069 31.842  1.00 38.22  ? 52  PHE   C CE1 1 
ATOM   1846 C CE2 . PHE   C 1 53 ? 19.965  -38.443 31.681  1.00 42.64  ? 52  PHE   C CE2 1 
ATOM   1847 C CZ  . PHE   C 1 53 ? 19.586  -37.253 32.273  1.00 39.38  ? 52  PHE   C CZ  1 
ATOM   1848 N N   . LEU   C 1 54 ? 23.940  -35.085 26.908  1.00 28.72  ? 53  LEU   C N   1 
ATOM   1849 C CA  . LEU   C 1 54 ? 25.063  -34.877 26.008  1.00 28.20  ? 53  LEU   C CA  1 
ATOM   1850 C C   . LEU   C 1 54 ? 26.146  -34.103 26.740  1.00 31.53  ? 53  LEU   C C   1 
ATOM   1851 O O   . LEU   C 1 54 ? 25.839  -33.291 27.599  1.00 31.35  ? 53  LEU   C O   1 
ATOM   1852 C CB  . LEU   C 1 54 ? 24.645  -34.094 24.768  1.00 27.98  ? 53  LEU   C CB  1 
ATOM   1853 C CG  . LEU   C 1 54 ? 23.775  -34.863 23.770  1.00 31.27  ? 53  LEU   C CG  1 
ATOM   1854 C CD1 . LEU   C 1 54 ? 23.457  -33.969 22.597  1.00 29.83  ? 53  LEU   C CD1 1 
ATOM   1855 C CD2 . LEU   C 1 54 ? 24.523  -36.106 23.288  1.00 37.92  ? 53  LEU   C CD2 1 
ATOM   1856 N N   . GLY   C 1 55 ? 27.391  -34.345 26.329  1.00 33.64  ? 54  GLY   C N   1 
ATOM   1857 C CA  . GLY   C 1 55 ? 28.542  -33.615 26.836  1.00 32.94  ? 54  GLY   C CA  1 
ATOM   1858 C C   . GLY   C 1 55 ? 28.825  -32.337 26.054  1.00 36.53  ? 54  GLY   C C   1 
ATOM   1859 O O   . GLY   C 1 55 ? 28.283  -32.096 24.960  1.00 33.91  ? 54  GLY   C O   1 
ATOM   1860 N N   . PRO   C 1 56 ? 29.651  -31.440 26.635  1.00 38.34  ? 55  PRO   C N   1 
ATOM   1861 C CA  . PRO   C 1 56 ? 29.868  -30.109 26.077  1.00 40.34  ? 55  PRO   C CA  1 
ATOM   1862 C C   . PRO   C 1 56 ? 30.497  -30.135 24.685  1.00 38.03  ? 55  PRO   C C   1 
ATOM   1863 O O   . PRO   C 1 56 ? 30.309  -29.207 23.898  1.00 47.77  ? 55  PRO   C O   1 
ATOM   1864 C CB  . PRO   C 1 56 ? 30.741  -29.384 27.149  1.00 46.87  ? 55  PRO   C CB  1 
ATOM   1865 C CG  . PRO   C 1 56 ? 31.383  -30.505 27.931  1.00 40.36  ? 55  PRO   C CG  1 
ATOM   1866 C CD  . PRO   C 1 56 ? 30.421  -31.679 27.878  1.00 38.78  ? 55  PRO   C CD  1 
ATOM   1867 N N   . LYS   C 1 57 ? 31.192  -31.231 24.376  1.00 41.47  ? 56  LYS   C N   1 
ATOM   1868 C CA  . LYS   C 1 57 ? 31.825  -31.419 23.082  1.00 41.27  ? 56  LYS   C CA  1 
ATOM   1869 C C   . LYS   C 1 57 ? 30.745  -31.434 21.999  1.00 44.15  ? 56  LYS   C C   1 
ATOM   1870 O O   . LYS   C 1 57 ? 31.042  -31.182 20.827  1.00 43.65  ? 56  LYS   C O   1 
ATOM   1871 C CB  . LYS   C 1 57 ? 32.563  -32.767 23.012  1.00 44.20  ? 56  LYS   C CB  1 
ATOM   1872 N N   . ASP   C 1 58 ? 29.503  -31.756 22.395  1.00 39.17  ? 57  ASP   C N   1 
ATOM   1873 C CA  . ASP   C 1 58 ? 28.471  -32.040 21.402  1.00 36.02  ? 57  ASP   C CA  1 
ATOM   1874 C C   . ASP   C 1 58 ? 27.498  -30.875 21.261  1.00 36.81  ? 57  ASP   C C   1 
ATOM   1875 O O   . ASP   C 1 58 ? 26.452  -31.034 20.630  1.00 32.95  ? 57  ASP   C O   1 
ATOM   1876 C CB  . ASP   C 1 58 ? 27.687  -33.288 21.765  1.00 38.63  ? 57  ASP   C CB  1 
ATOM   1877 C CG  . ASP   C 1 58 ? 28.487  -34.580 21.809  1.00 43.65  ? 57  ASP   C CG  1 
ATOM   1878 O OD1 . ASP   C 1 58 ? 29.330  -34.755 20.929  1.00 45.48  ? 57  ASP   C OD1 1 
ATOM   1879 O OD2 . ASP   C 1 58 ? 28.188  -35.428 22.666  1.00 51.17  ? 57  ASP   C OD2 1 
ATOM   1880 N N   . LEU   C 1 59 ? 27.812  -29.719 21.860  1.00 29.82  ? 58  LEU   C N   1 
ATOM   1881 C CA  . LEU   C 1 59 ? 26.862  -28.633 22.050  1.00 34.19  ? 58  LEU   C CA  1 
ATOM   1882 C C   . LEU   C 1 59 ? 27.478  -27.353 21.492  1.00 38.21  ? 58  LEU   C C   1 
ATOM   1883 O O   . LEU   C 1 59 ? 28.657  -27.112 21.739  1.00 44.66  ? 58  LEU   C O   1 
ATOM   1884 C CB  . LEU   C 1 59 ? 26.553  -28.458 23.538  1.00 31.70  ? 58  LEU   C CB  1 
ATOM   1885 C CG  . LEU   C 1 59 ? 25.963  -29.695 24.211  1.00 30.51  ? 58  LEU   C CG  1 
ATOM   1886 C CD1 . LEU   C 1 59 ? 25.844  -29.513 25.710  1.00 32.58  ? 58  LEU   C CD1 1 
ATOM   1887 C CD2 . LEU   C 1 59 ? 24.601  -30.061 23.596  1.00 25.40  ? 58  LEU   C CD2 1 
ATOM   1888 N N   . PHE   C 1 60 ? 26.687  -26.564 20.745  1.00 36.77  ? 59  PHE   C N   1 
ATOM   1889 C CA  . PHE   C 1 60 ? 27.182  -25.321 20.145  1.00 36.43  ? 59  PHE   C CA  1 
ATOM   1890 C C   . PHE   C 1 60 ? 26.211  -24.180 20.419  1.00 40.62  ? 59  PHE   C C   1 
ATOM   1891 O O   . PHE   C 1 60 ? 25.021  -24.315 20.210  1.00 35.53  ? 59  PHE   C O   1 
ATOM   1892 C CB  . PHE   C 1 60 ? 27.331  -25.564 18.641  1.00 36.13  ? 59  PHE   C CB  1 
ATOM   1893 C CG  . PHE   C 1 60 ? 28.248  -26.739 18.337  1.00 32.28  ? 59  PHE   C CG  1 
ATOM   1894 C CD1 . PHE   C 1 60 ? 27.780  -28.049 18.365  1.00 35.01  ? 59  PHE   C CD1 1 
ATOM   1895 C CD2 . PHE   C 1 60 ? 29.605  -26.539 18.075  1.00 37.51  ? 59  PHE   C CD2 1 
ATOM   1896 C CE1 . PHE   C 1 60 ? 28.618  -29.124 18.108  1.00 33.77  ? 59  PHE   C CE1 1 
ATOM   1897 C CE2 . PHE   C 1 60 ? 30.437  -27.613 17.795  1.00 37.54  ? 59  PHE   C CE2 1 
ATOM   1898 C CZ  . PHE   C 1 60 ? 29.949  -28.901 17.813  1.00 40.03  ? 59  PHE   C CZ  1 
ATOM   1899 N N   . PRO   C 1 61 ? 26.634  -23.004 20.946  1.00 38.01  ? 60  PRO   C N   1 
ATOM   1900 C CA  . PRO   C 1 61 ? 25.647  -21.972 21.286  1.00 39.74  ? 60  PRO   C CA  1 
ATOM   1901 C C   . PRO   C 1 61 ? 24.952  -21.498 20.013  1.00 35.01  ? 60  PRO   C C   1 
ATOM   1902 O O   . PRO   C 1 61 ? 25.580  -21.413 18.962  1.00 40.07  ? 60  PRO   C O   1 
ATOM   1903 C CB  . PRO   C 1 61 ? 26.431  -20.852 21.997  1.00 43.03  ? 60  PRO   C CB  1 
ATOM   1904 C CG  . PRO   C 1 61 ? 27.823  -21.435 22.179  1.00 40.45  ? 60  PRO   C CG  1 
ATOM   1905 C CD  . PRO   C 1 61 ? 28.022  -22.651 21.293  1.00 46.47  ? 60  PRO   C CD  1 
ATOM   1906 N N   . TYR   C 1 62 ? 23.632  -21.306 20.129  1.00 38.56  ? 61  TYR   C N   1 
ATOM   1907 C CA  . TYR   C 1 62 ? 22.722  -21.051 19.022  1.00 41.97  ? 61  TYR   C CA  1 
ATOM   1908 C C   . TYR   C 1 62 ? 23.109  -19.780 18.269  1.00 46.25  ? 61  TYR   C C   1 
ATOM   1909 O O   . TYR   C 1 62 ? 23.206  -19.795 17.041  1.00 45.02  ? 61  TYR   C O   1 
ATOM   1910 C CB  . TYR   C 1 62 ? 21.297  -20.900 19.552  1.00 44.60  ? 61  TYR   C CB  1 
ATOM   1911 C CG  . TYR   C 1 62 ? 20.324  -20.547 18.438  1.00 44.47  ? 61  TYR   C CG  1 
ATOM   1912 C CD1 . TYR   C 1 62 ? 20.121  -21.423 17.370  1.00 44.72  ? 61  TYR   C CD1 1 
ATOM   1913 C CD2 . TYR   C 1 62 ? 19.614  -19.347 18.466  1.00 44.86  ? 61  TYR   C CD2 1 
ATOM   1914 C CE1 . TYR   C 1 62 ? 19.235  -21.099 16.348  1.00 43.66  ? 61  TYR   C CE1 1 
ATOM   1915 C CE2 . TYR   C 1 62 ? 18.716  -19.026 17.461  1.00 43.88  ? 61  TYR   C CE2 1 
ATOM   1916 C CZ  . TYR   C 1 62 ? 18.542  -19.895 16.394  1.00 46.56  ? 61  TYR   C CZ  1 
ATOM   1917 O OH  . TYR   C 1 62 ? 17.669  -19.554 15.394  1.00 42.90  ? 61  TYR   C OH  1 
ATOM   1918 N N   . ASP   C 1 63 ? 23.344  -18.681 19.000  1.00 48.57  ? 62  ASP   C N   1 
ATOM   1919 C CA  . ASP   C 1 63 ? 23.647  -17.425 18.332  1.00 51.05  ? 62  ASP   C CA  1 
ATOM   1920 C C   . ASP   C 1 63 ? 24.951  -17.520 17.559  1.00 45.30  ? 62  ASP   C C   1 
ATOM   1921 O O   . ASP   C 1 63 ? 25.024  -17.010 16.439  1.00 56.99  ? 62  ASP   C O   1 
ATOM   1922 C CB  . ASP   C 1 63 ? 23.531  -16.218 19.245  1.00 57.42  ? 62  ASP   C CB  1 
ATOM   1923 C CG  . ASP   C 1 63 ? 22.223  -15.466 19.061  1.00 72.04  ? 62  ASP   C CG  1 
ATOM   1924 O OD1 . ASP   C 1 63 ? 21.322  -15.649 19.909  1.00 74.94  ? 62  ASP   C OD1 1 
ATOM   1925 O OD2 . ASP   C 1 63 ? 22.108  -14.728 18.051  1.00 71.03  ? 62  ASP   C OD2 1 
ATOM   1926 N N   . LYS   C 1 64 ? 25.948  -18.203 18.133  1.00 41.62  ? 63  LYS   C N   1 
ATOM   1927 C CA  . LYS   C 1 64 ? 27.272  -18.247 17.536  1.00 40.68  ? 63  LYS   C CA  1 
ATOM   1928 C C   . LYS   C 1 64 ? 27.288  -19.159 16.317  1.00 42.27  ? 63  LYS   C C   1 
ATOM   1929 O O   . LYS   C 1 64 ? 28.037  -18.899 15.384  1.00 40.95  ? 63  LYS   C O   1 
ATOM   1930 C CB  . LYS   C 1 64 ? 28.338  -18.719 18.533  1.00 47.92  ? 63  LYS   C CB  1 
ATOM   1931 N N   . SER   C 1 65 ? 26.445  -20.213 16.305  1.00 38.65  ? 64  SER   C N   1 
ATOM   1932 C CA  . SER   C 1 65 ? 26.621  -21.235 15.283  1.00 37.46  ? 64  SER   C CA  1 
ATOM   1933 C C   . SER   C 1 65 ? 25.437  -21.337 14.310  1.00 31.59  ? 64  SER   C C   1 
ATOM   1934 O O   . SER   C 1 65 ? 25.513  -22.166 13.410  1.00 34.72  ? 64  SER   C O   1 
ATOM   1935 C CB  . SER   C 1 65 ? 26.978  -22.590 15.873  1.00 40.98  ? 64  SER   C CB  1 
ATOM   1936 O OG  . SER   C 1 65 ? 25.887  -23.064 16.653  1.00 39.99  ? 64  SER   C OG  1 
ATOM   1937 N N   . LYS   C 1 66 ? 24.373  -20.541 14.498  1.00 33.98  ? 65  LYS   C N   1 
ATOM   1938 C CA  . LYS   C 1 66 ? 23.204  -20.686 13.625  1.00 35.43  ? 65  LYS   C CA  1 
ATOM   1939 C C   . LYS   C 1 66 ? 23.539  -20.420 12.155  1.00 36.26  ? 65  LYS   C C   1 
ATOM   1940 O O   . LYS   C 1 66 ? 22.921  -21.019 11.281  1.00 36.90  ? 65  LYS   C O   1 
ATOM   1941 C CB  . LYS   C 1 66 ? 21.965  -19.903 14.054  1.00 36.56  ? 65  LYS   C CB  1 
ATOM   1942 C CG  . LYS   C 1 66 ? 22.232  -18.403 14.083  1.00 37.35  ? 65  LYS   C CG  1 
ATOM   1943 C CD  . LYS   C 1 66 ? 21.003  -17.696 14.621  1.00 41.58  ? 65  LYS   C CD  1 
ATOM   1944 C CE  . LYS   C 1 66 ? 21.162  -16.226 14.522  1.00 46.70  ? 65  LYS   C CE  1 
ATOM   1945 N NZ  . LYS   C 1 66 ? 20.115  -15.714 15.395  1.00 43.91  ? 65  LYS   C NZ  1 
ATOM   1946 N N   . ASP   C 1 67 ? 24.496  -19.525 11.865  1.00 39.04  ? 66  ASP   C N   1 
ATOM   1947 C CA  . ASP   C 1 67 ? 24.868  -19.283 10.468  1.00 44.19  ? 66  ASP   C CA  1 
ATOM   1948 C C   . ASP   C 1 67 ? 25.278  -20.589 9.783   1.00 44.94  ? 66  ASP   C C   1 
ATOM   1949 O O   . ASP   C 1 67 ? 24.987  -20.799 8.602   1.00 39.43  ? 66  ASP   C O   1 
ATOM   1950 C CB  . ASP   C 1 67 ? 25.860  -18.130 10.298  1.00 41.47  ? 66  ASP   C CB  1 
ATOM   1951 C CG  . ASP   C 1 67 ? 27.245  -18.283 10.925  1.00 53.01  ? 66  ASP   C CG  1 
ATOM   1952 O OD1 . ASP   C 1 67 ? 27.493  -19.290 11.646  1.00 54.79  ? 66  ASP   C OD1 1 
ATOM   1953 O OD2 . ASP   C 1 67 ? 28.075  -17.365 10.723  1.00 49.68  ? 66  ASP   C OD2 1 
ATOM   1954 N N   . LYS   C 1 68 ? 25.902  -21.495 10.549  1.00 36.14  ? 67  LYS   C N   1 
ATOM   1955 C CA  . LYS   C 1 68 ? 26.384  -22.760 10.028  1.00 33.93  ? 67  LYS   C CA  1 
ATOM   1956 C C   . LYS   C 1 68 ? 25.322  -23.873 10.108  1.00 31.52  ? 67  LYS   C C   1 
ATOM   1957 O O   . LYS   C 1 68 ? 25.145  -24.637 9.154   1.00 35.14  ? 67  LYS   C O   1 
ATOM   1958 C CB  . LYS   C 1 68 ? 27.709  -23.051 10.737  1.00 34.78  ? 67  LYS   C CB  1 
ATOM   1959 C CG  . LYS   C 1 68 ? 28.389  -24.343 10.373  1.00 41.31  ? 67  LYS   C CG  1 
ATOM   1960 C CD  . LYS   C 1 68 ? 29.744  -24.387 11.085  1.00 52.30  ? 67  LYS   C CD  1 
ATOM   1961 C CE  . LYS   C 1 68 ? 30.370  -25.752 11.211  1.00 57.52  ? 67  LYS   C CE  1 
ATOM   1962 N NZ  . LYS   C 1 68 ? 30.615  -26.430 9.933   1.00 75.23  ? 67  LYS   C NZ  1 
ATOM   1963 N N   . TYR   C 1 69 ? 24.629  -23.994 11.250  1.00 31.53  ? 68  TYR   C N   1 
ATOM   1964 C CA  . TYR   C 1 69 ? 23.806  -25.189 11.443  1.00 29.74  ? 68  TYR   C CA  1 
ATOM   1965 C C   . TYR   C 1 69 ? 22.332  -24.838 11.254  1.00 30.95  ? 68  TYR   C C   1 
ATOM   1966 O O   . TYR   C 1 69 ? 21.510  -25.741 11.111  1.00 29.14  ? 68  TYR   C O   1 
ATOM   1967 C CB  . TYR   C 1 69 ? 23.964  -25.823 12.832  1.00 29.28  ? 68  TYR   C CB  1 
ATOM   1968 C CG  . TYR   C 1 69 ? 25.406  -26.248 13.100  1.00 28.57  ? 68  TYR   C CG  1 
ATOM   1969 C CD1 . TYR   C 1 69 ? 26.119  -26.987 12.165  1.00 29.62  ? 68  TYR   C CD1 1 
ATOM   1970 C CD2 . TYR   C 1 69 ? 26.052  -25.843 14.265  1.00 33.25  ? 68  TYR   C CD2 1 
ATOM   1971 C CE1 . TYR   C 1 69 ? 27.404  -27.447 12.429  1.00 34.06  ? 68  TYR   C CE1 1 
ATOM   1972 C CE2 . TYR   C 1 69 ? 27.348  -26.271 14.518  1.00 31.62  ? 68  TYR   C CE2 1 
ATOM   1973 C CZ  . TYR   C 1 69 ? 28.033  -27.022 13.587  1.00 35.41  ? 68  TYR   C CZ  1 
ATOM   1974 O OH  . TYR   C 1 69 ? 29.321  -27.381 13.901  1.00 40.67  ? 68  TYR   C OH  1 
ATOM   1975 N N   . GLY   C 1 70 ? 21.999  -23.548 11.259  1.00 30.22  ? 69  GLY   C N   1 
ATOM   1976 C CA  . GLY   C 1 70 ? 20.591  -23.180 11.194  1.00 31.12  ? 69  GLY   C CA  1 
ATOM   1977 C C   . GLY   C 1 70 ? 20.157  -23.062 9.735   1.00 32.03  ? 69  GLY   C C   1 
ATOM   1978 O O   . GLY   C 1 70 ? 20.110  -21.969 9.166   1.00 32.77  ? 69  GLY   C O   1 
ATOM   1979 N N   . LYS   C 1 71 ? 19.914  -24.211 9.136   1.00 30.71  ? 70  LYS   C N   1 
ATOM   1980 C CA  . LYS   C 1 71 ? 19.528  -24.279 7.731   1.00 34.35  ? 70  LYS   C CA  1 
ATOM   1981 C C   . LYS   C 1 71 ? 18.693  -25.542 7.604   1.00 31.89  ? 70  LYS   C C   1 
ATOM   1982 O O   . LYS   C 1 71 ? 18.860  -26.489 8.379   1.00 33.00  ? 70  LYS   C O   1 
ATOM   1983 C CB  . LYS   C 1 71 ? 20.722  -24.373 6.774   1.00 36.95  ? 70  LYS   C CB  1 
ATOM   1984 C CG  . LYS   C 1 71 ? 21.659  -25.535 7.073   1.00 43.92  ? 70  LYS   C CG  1 
ATOM   1985 C CD  . LYS   C 1 71 ? 22.898  -25.804 6.225   1.00 51.06  ? 70  LYS   C CD  1 
ATOM   1986 C CE  . LYS   C 1 71 ? 23.855  -26.732 6.925   1.00 53.51  ? 70  LYS   C CE  1 
ATOM   1987 N N   . PRO   C 1 72 ? 17.685  -25.553 6.707   1.00 30.73  ? 71  PRO   C N   1 
ATOM   1988 C CA  . PRO   C 1 72 ? 16.763  -26.672 6.663   1.00 27.36  ? 71  PRO   C CA  1 
ATOM   1989 C C   . PRO   C 1 72 ? 17.415  -28.004 6.347   1.00 28.46  ? 71  PRO   C C   1 
ATOM   1990 O O   . PRO   C 1 72 ? 18.456  -28.069 5.699   1.00 31.04  ? 71  PRO   C O   1 
ATOM   1991 C CB  . PRO   C 1 72 ? 15.776  -26.263 5.569   1.00 32.12  ? 71  PRO   C CB  1 
ATOM   1992 C CG  . PRO   C 1 72 ? 15.817  -24.770 5.699   1.00 30.16  ? 71  PRO   C CG  1 
ATOM   1993 C CD  . PRO   C 1 72 ? 17.306  -24.424 5.821   1.00 28.41  ? 71  PRO   C CD  1 
ATOM   1994 N N   . ASN   C 1 73 ? 16.732  -29.041 6.790   1.00 33.08  ? 72  ASN   C N   1 
ATOM   1995 C CA  . ASN   C 1 73 ? 17.033  -30.315 6.175   1.00 40.22  ? 72  ASN   C CA  1 
ATOM   1996 C C   . ASN   C 1 73 ? 15.810  -31.199 6.315   1.00 31.30  ? 72  ASN   C C   1 
ATOM   1997 O O   . ASN   C 1 73 ? 14.825  -30.832 6.936   1.00 36.61  ? 72  ASN   C O   1 
ATOM   1998 C CB  . ASN   C 1 73 ? 18.370  -30.897 6.610   1.00 46.77  ? 72  ASN   C CB  1 
ATOM   1999 C CG  . ASN   C 1 73 ? 18.247  -31.528 7.963   1.00 43.83  ? 72  ASN   C CG  1 
ATOM   2000 O OD1 . ASN   C 1 73 ? 17.823  -32.679 8.080   1.00 43.68  ? 72  ASN   C OD1 1 
ATOM   2001 N ND2 . ASN   C 1 73 ? 18.610  -30.781 8.981   1.00 46.86  ? 72  ASN   C ND2 1 
ATOM   2002 N N   . LYS   C 1 74 ? 15.894  -32.377 5.699   1.00 34.14  ? 73  LYS   C N   1 
ATOM   2003 C CA  . LYS   C 1 74 ? 14.689  -33.148 5.474   1.00 31.86  ? 73  LYS   C CA  1 
ATOM   2004 C C   . LYS   C 1 74 ? 14.425  -34.116 6.622   1.00 35.91  ? 73  LYS   C C   1 
ATOM   2005 O O   . LYS   C 1 74 ? 13.412  -34.812 6.601   1.00 37.30  ? 73  LYS   C O   1 
ATOM   2006 C CB  . LYS   C 1 74 ? 14.842  -33.893 4.138   1.00 40.29  ? 73  LYS   C CB  1 
ATOM   2007 N N   . ARG   C 1 75 ? 15.310  -34.180 7.638   1.00 32.14  ? 74  ARG   C N   1 
ATOM   2008 C CA  . ARG   C 1 75 ? 15.054  -35.127 8.717   1.00 28.55  ? 74  ARG   C CA  1 
ATOM   2009 C C   . ARG   C 1 75 ? 13.777  -34.773 9.475   1.00 30.09  ? 74  ARG   C C   1 
ATOM   2010 O O   . ARG   C 1 75 ? 13.453  -33.597 9.675   1.00 32.23  ? 74  ARG   C O   1 
ATOM   2011 C CB  . ARG   C 1 75 ? 16.195  -35.281 9.742   1.00 32.89  ? 74  ARG   C CB  1 
ATOM   2012 C CG  . ARG   C 1 75 ? 17.589  -35.447 9.150   1.00 35.85  ? 74  ARG   C CG  1 
ATOM   2013 C CD  . ARG   C 1 75 ? 17.958  -36.711 8.343   1.00 40.73  ? 74  ARG   C CD  1 
ATOM   2014 N NE  . ARG   C 1 75 ? 18.082  -37.744 9.366   1.00 38.12  ? 74  ARG   C NE  1 
ATOM   2015 C CZ  . ARG   C 1 75 ? 19.226  -38.208 9.919   1.00 33.81  ? 74  ARG   C CZ  1 
ATOM   2016 N NH1 . ARG   C 1 75 ? 19.113  -38.765 11.101  1.00 38.82  ? 74  ARG   C NH1 1 
ATOM   2017 N NH2 . ARG   C 1 75 ? 20.430  -37.974 9.374   1.00 34.10  ? 74  ARG   C NH2 1 
ATOM   2018 N N   . LYS   C 1 76 ? 13.044  -35.821 9.885   1.00 35.37  ? 75  LYS   C N   1 
ATOM   2019 C CA  . LYS   C 1 76 ? 11.770  -35.675 10.584  1.00 39.22  ? 75  LYS   C CA  1 
ATOM   2020 C C   . LYS   C 1 76 ? 11.872  -34.736 11.791  1.00 36.45  ? 75  LYS   C C   1 
ATOM   2021 O O   . LYS   C 1 76 ? 12.668  -34.922 12.715  1.00 33.09  ? 75  LYS   C O   1 
ATOM   2022 C CB  . LYS   C 1 76 ? 11.053  -36.999 10.898  1.00 42.62  ? 75  LYS   C CB  1 
ATOM   2023 C CG  . LYS   C 1 76 ? 9.594   -36.826 11.338  1.00 47.90  ? 75  LYS   C CG  1 
ATOM   2024 C CD  . LYS   C 1 76 ? 8.886   -38.028 11.969  1.00 51.10  ? 75  LYS   C CD  1 
ATOM   2025 N N   . GLY   C 1 77 ? 11.008  -33.707 11.771  1.00 36.78  ? 76  GLY   C N   1 
ATOM   2026 C CA  . GLY   C 1 77 ? 10.855  -32.811 12.897  1.00 30.04  ? 76  GLY   C CA  1 
ATOM   2027 C C   . GLY   C 1 77 ? 11.823  -31.624 12.827  1.00 28.30  ? 76  GLY   C C   1 
ATOM   2028 O O   . GLY   C 1 77 ? 11.674  -30.678 13.605  1.00 32.12  ? 76  GLY   C O   1 
ATOM   2029 N N   . PHE   C 1 78 ? 12.794  -31.683 11.907  1.00 27.61  ? 77  PHE   C N   1 
ATOM   2030 C CA  . PHE   C 1 78 ? 13.918  -30.753 11.933  1.00 28.29  ? 77  PHE   C CA  1 
ATOM   2031 C C   . PHE   C 1 78 ? 13.460  -29.307 11.697  1.00 29.81  ? 77  PHE   C C   1 
ATOM   2032 O O   . PHE   C 1 78 ? 13.795  -28.375 12.427  1.00 28.42  ? 77  PHE   C O   1 
ATOM   2033 C CB  . PHE   C 1 78 ? 15.052  -31.142 10.992  1.00 32.19  ? 77  PHE   C CB  1 
ATOM   2034 C CG  . PHE   C 1 78 ? 16.348  -30.367 11.218  1.00 27.60  ? 77  PHE   C CG  1 
ATOM   2035 C CD1 . PHE   C 1 78 ? 16.532  -29.084 10.709  1.00 26.91  ? 77  PHE   C CD1 1 
ATOM   2036 C CD2 . PHE   C 1 78 ? 17.371  -30.919 11.986  1.00 25.91  ? 77  PHE   C CD2 1 
ATOM   2037 C CE1 . PHE   C 1 78 ? 17.722  -28.389 10.931  1.00 25.32  ? 77  PHE   C CE1 1 
ATOM   2038 C CE2 . PHE   C 1 78 ? 18.572  -30.245 12.157  1.00 26.69  ? 77  PHE   C CE2 1 
ATOM   2039 C CZ  . PHE   C 1 78 ? 18.738  -28.982 11.664  1.00 27.94  ? 77  PHE   C CZ  1 
ATOM   2040 N N   . ASN   C 1 79 ? 12.674  -29.133 10.640  1.00 28.83  ? 78  ASN   C N   1 
ATOM   2041 C CA  . ASN   C 1 79 ? 12.361  -27.777 10.242  1.00 29.91  ? 78  ASN   C CA  1 
ATOM   2042 C C   . ASN   C 1 79 ? 11.366  -27.154 11.201  1.00 30.15  ? 78  ASN   C C   1 
ATOM   2043 O O   . ASN   C 1 79 ? 11.433  -25.956 11.440  1.00 29.40  ? 78  ASN   C O   1 
ATOM   2044 C CB  . ASN   C 1 79 ? 11.946  -27.688 8.778   1.00 28.46  ? 78  ASN   C CB  1 
ATOM   2045 C CG  . ASN   C 1 79 ? 13.041  -28.142 7.848   1.00 29.36  ? 78  ASN   C CG  1 
ATOM   2046 O OD1 . ASN   C 1 79 ? 14.224  -27.885 8.094   1.00 29.66  ? 78  ASN   C OD1 1 
ATOM   2047 N ND2 . ASN   C 1 79 ? 12.651  -28.747 6.737   1.00 28.49  ? 78  ASN   C ND2 1 
ATOM   2048 N N   . GLU   C 1 80 ? 10.474  -27.948 11.794  1.00 32.62  ? 79  GLU   C N   1 
ATOM   2049 C CA  . GLU   C 1 80 ? 9.653   -27.404 12.860  1.00 30.60  ? 79  GLU   C CA  1 
ATOM   2050 C C   . GLU   C 1 80 ? 10.546  -27.004 14.023  1.00 31.33  ? 79  GLU   C C   1 
ATOM   2051 O O   . GLU   C 1 80 ? 10.331  -25.994 14.671  1.00 30.77  ? 79  GLU   C O   1 
ATOM   2052 C CB  . GLU   C 1 80 ? 8.557   -28.383 13.266  1.00 37.39  ? 79  GLU   C CB  1 
ATOM   2053 C CG  . GLU   C 1 80 ? 7.734   -27.894 14.446  1.00 39.81  ? 79  GLU   C CG  1 
ATOM   2054 C CD  . GLU   C 1 80 ? 6.446   -28.669 14.532  1.00 47.92  ? 79  GLU   C CD  1 
ATOM   2055 O OE1 . GLU   C 1 80 ? 6.312   -29.722 13.869  1.00 54.96  ? 79  GLU   C OE1 1 
ATOM   2056 O OE2 . GLU   C 1 80 ? 5.557   -28.183 15.251  1.00 52.27  ? 79  GLU   C OE2 1 
ATOM   2057 N N   . GLY   C 1 81 ? 11.590  -27.823 14.270  1.00 30.97  ? 80  GLY   C N   1 
ATOM   2058 C CA  . GLY   C 1 81 ? 12.562  -27.479 15.291  1.00 30.87  ? 80  GLY   C CA  1 
ATOM   2059 C C   . GLY   C 1 81 ? 13.165  -26.097 15.059  1.00 32.46  ? 80  GLY   C C   1 
ATOM   2060 O O   . GLY   C 1 81 ? 13.317  -25.327 15.997  1.00 31.86  ? 80  GLY   C O   1 
ATOM   2061 N N   . LEU   C 1 82 ? 13.583  -25.821 13.815  1.00 32.22  ? 81  LEU   C N   1 
ATOM   2062 C CA  . LEU   C 1 82 ? 14.162  -24.529 13.477  1.00 30.47  ? 81  LEU   C CA  1 
ATOM   2063 C C   . LEU   C 1 82 ? 13.137  -23.420 13.695  1.00 29.24  ? 81  LEU   C C   1 
ATOM   2064 O O   . LEU   C 1 82 ? 13.529  -22.318 14.089  1.00 33.09  ? 81  LEU   C O   1 
ATOM   2065 C CB  . LEU   C 1 82 ? 14.584  -24.489 12.013  1.00 29.73  ? 81  LEU   C CB  1 
ATOM   2066 C CG  . LEU   C 1 82 ? 15.821  -25.282 11.598  1.00 30.76  ? 81  LEU   C CG  1 
ATOM   2067 C CD1 . LEU   C 1 82 ? 16.074  -25.217 10.091  1.00 30.33  ? 81  LEU   C CD1 1 
ATOM   2068 C CD2 . LEU   C 1 82 ? 17.086  -24.819 12.308  1.00 29.77  ? 81  LEU   C CD2 1 
ATOM   2069 N N   . TRP   C 1 83 ? 11.856  -23.706 13.448  1.00 30.34  ? 82  TRP   C N   1 
ATOM   2070 C CA  . TRP   C 1 83 ? 10.882  -22.648 13.692  1.00 35.62  ? 82  TRP   C CA  1 
ATOM   2071 C C   . TRP   C 1 83 ? 10.833  -22.337 15.195  1.00 36.25  ? 82  TRP   C C   1 
ATOM   2072 O O   . TRP   C 1 83 ? 10.888  -21.170 15.628  1.00 36.59  ? 82  TRP   C O   1 
ATOM   2073 C CB  . TRP   C 1 83 ? 9.507   -23.023 13.130  1.00 33.70  ? 82  TRP   C CB  1 
ATOM   2074 C CG  . TRP   C 1 83 ? 8.559   -21.855 13.232  1.00 39.27  ? 82  TRP   C CG  1 
ATOM   2075 C CD1 . TRP   C 1 83 ? 8.382   -20.867 12.305  1.00 39.92  ? 82  TRP   C CD1 1 
ATOM   2076 C CD2 . TRP   C 1 83 ? 7.699   -21.528 14.344  1.00 40.26  ? 82  TRP   C CD2 1 
ATOM   2077 N NE1 . TRP   C 1 83 ? 7.466   -19.960 12.758  1.00 37.07  ? 82  TRP   C NE1 1 
ATOM   2078 C CE2 . TRP   C 1 83 ? 7.021   -20.335 13.995  1.00 40.26  ? 82  TRP   C CE2 1 
ATOM   2079 C CE3 . TRP   C 1 83 ? 7.438   -22.120 15.586  1.00 37.99  ? 82  TRP   C CE3 1 
ATOM   2080 C CZ2 . TRP   C 1 83 ? 6.107   -19.730 14.853  1.00 44.99  ? 82  TRP   C CZ2 1 
ATOM   2081 C CZ3 . TRP   C 1 83 ? 6.528   -21.527 16.439  1.00 44.78  ? 82  TRP   C CZ3 1 
ATOM   2082 C CH2 . TRP   C 1 83 ? 5.888   -20.341 16.078  1.00 43.82  ? 82  TRP   C CH2 1 
ATOM   2083 N N   . GLU   C 1 84 ? 10.868  -23.414 15.991  1.00 34.57  ? 83  GLU   C N   1 
ATOM   2084 C CA  . GLU   C 1 84 ? 10.665  -23.262 17.422  1.00 36.04  ? 83  GLU   C CA  1 
ATOM   2085 C C   . GLU   C 1 84 ? 11.818  -22.515 18.078  1.00 34.72  ? 83  GLU   C C   1 
ATOM   2086 O O   . GLU   C 1 84 ? 11.596  -21.667 18.951  1.00 39.91  ? 83  GLU   C O   1 
ATOM   2087 C CB  . GLU   C 1 84 ? 10.468  -24.621 18.092  1.00 31.69  ? 83  GLU   C CB  1 
ATOM   2088 C CG  . GLU   C 1 84 ? 9.170   -25.313 17.694  1.00 33.77  ? 83  GLU   C CG  1 
ATOM   2089 C CD  . GLU   C 1 84 ? 9.104   -26.677 18.317  1.00 39.66  ? 83  GLU   C CD  1 
ATOM   2090 O OE1 . GLU   C 1 84 ? 10.124  -27.092 18.921  1.00 34.03  ? 83  GLU   C OE1 1 
ATOM   2091 O OE2 . GLU   C 1 84 ? 8.047   -27.321 18.189  1.00 39.62  ? 83  GLU   C OE2 1 
ATOM   2092 N N   . ILE   C 1 85 ? 13.052  -22.793 17.645  1.00 33.22  ? 84  ILE   C N   1 
ATOM   2093 C CA  . ILE   C 1 85 ? 14.214  -22.188 18.270  1.00 34.78  ? 84  ILE   C CA  1 
ATOM   2094 C C   . ILE   C 1 85 ? 14.328  -20.681 17.983  1.00 35.84  ? 84  ILE   C C   1 
ATOM   2095 O O   . ILE   C 1 85 ? 14.846  -19.941 18.806  1.00 34.85  ? 84  ILE   C O   1 
ATOM   2096 C CB  . ILE   C 1 85 ? 15.494  -22.950 17.902  1.00 32.88  ? 84  ILE   C CB  1 
ATOM   2097 C CG1 . ILE   C 1 85 ? 16.601  -22.629 18.905  1.00 34.99  ? 84  ILE   C CG1 1 
ATOM   2098 C CG2 . ILE   C 1 85 ? 15.920  -22.719 16.446  1.00 33.88  ? 84  ILE   C CG2 1 
ATOM   2099 C CD1 . ILE   C 1 85 ? 17.786  -23.585 18.926  1.00 34.21  ? 84  ILE   C CD1 1 
ATOM   2100 N N   . GLN   C 1 86 ? 13.874  -20.247 16.802  1.00 33.95  ? 85  GLN   C N   1 
ATOM   2101 C CA  . GLN   C 1 86 ? 13.904  -18.840 16.441  1.00 36.02  ? 85  GLN   C CA  1 
ATOM   2102 C C   . GLN   C 1 86 ? 12.653  -18.109 16.937  1.00 38.25  ? 85  GLN   C C   1 
ATOM   2103 O O   . GLN   C 1 86 ? 12.724  -16.924 17.246  1.00 44.45  ? 85  GLN   C O   1 
ATOM   2104 C CB  . GLN   C 1 86 ? 14.119  -18.775 14.925  1.00 33.73  ? 85  GLN   C CB  1 
ATOM   2105 C CG  . GLN   C 1 86 ? 14.268  -17.361 14.371  1.00 33.53  ? 85  GLN   C CG  1 
ATOM   2106 C CD  . GLN   C 1 86 ? 14.542  -17.373 12.880  1.00 39.32  ? 85  GLN   C CD  1 
ATOM   2107 O OE1 . GLN   C 1 86 ? 14.392  -18.393 12.190  1.00 37.52  ? 85  GLN   C OE1 1 
ATOM   2108 N NE2 . GLN   C 1 86 ? 14.984  -16.235 12.368  1.00 38.50  ? 85  GLN   C NE2 1 
ATOM   2109 N N   . ASN   C 1 87 ? 11.521  -18.797 17.048  1.00 37.96  ? 86  ASN   C N   1 
ATOM   2110 C CA  . ASN   C 1 87 ? 10.265  -18.076 17.215  1.00 46.37  ? 86  ASN   C CA  1 
ATOM   2111 C C   . ASN   C 1 87 ? 9.596   -18.370 18.557  1.00 49.88  ? 86  ASN   C C   1 
ATOM   2112 O O   . ASN   C 1 87 ? 8.685   -17.644 18.947  1.00 49.27  ? 86  ASN   C O   1 
ATOM   2113 C CB  . ASN   C 1 87 ? 9.305   -18.320 16.057  1.00 44.96  ? 86  ASN   C CB  1 
ATOM   2114 C CG  . ASN   C 1 87 ? 9.879   -17.737 14.790  1.00 49.79  ? 86  ASN   C CG  1 
ATOM   2115 O OD1 . ASN   C 1 87 ? 9.915   -16.510 14.640  1.00 46.90  ? 86  ASN   C OD1 1 
ATOM   2116 N ND2 . ASN   C 1 87 ? 10.379  -18.587 13.905  1.00 41.66  ? 86  ASN   C ND2 1 
ATOM   2117 N N   . ASN   C 1 88 ? 10.018  -19.435 19.253  1.00 46.52  ? 87  ASN   C N   1 
ATOM   2118 C CA  . ASN   C 1 88 ? 9.326   -19.826 20.475  1.00 47.49  ? 87  ASN   C CA  1 
ATOM   2119 C C   . ASN   C 1 88 ? 10.261  -20.675 21.342  1.00 41.96  ? 87  ASN   C C   1 
ATOM   2120 O O   . ASN   C 1 88 ? 9.883   -21.773 21.743  1.00 48.71  ? 87  ASN   C O   1 
ATOM   2121 C CB  . ASN   C 1 88 ? 8.051   -20.601 20.144  1.00 49.95  ? 87  ASN   C CB  1 
ATOM   2122 C CG  . ASN   C 1 88 ? 7.019   -20.537 21.247  1.00 56.36  ? 87  ASN   C CG  1 
ATOM   2123 O OD1 . ASN   C 1 88 ? 7.164   -19.736 22.177  1.00 59.33  ? 87  ASN   C OD1 1 
ATOM   2124 N ND2 . ASN   C 1 88 ? 5.984   -21.363 21.160  1.00 55.61  ? 87  ASN   C ND2 1 
ATOM   2125 N N   . PRO   C 1 89 ? 11.508  -20.224 21.617  1.00 42.78  ? 88  PRO   C N   1 
ATOM   2126 C CA  . PRO   C 1 89 ? 12.526  -21.104 22.197  1.00 41.58  ? 88  PRO   C CA  1 
ATOM   2127 C C   . PRO   C 1 89 ? 12.281  -21.578 23.632  1.00 52.17  ? 88  PRO   C C   1 
ATOM   2128 O O   . PRO   C 1 89 ? 13.007  -22.449 24.117  1.00 46.75  ? 88  PRO   C O   1 
ATOM   2129 C CB  . PRO   C 1 89 ? 13.817  -20.299 22.058  1.00 43.39  ? 88  PRO   C CB  1 
ATOM   2130 C CG  . PRO   C 1 89 ? 13.342  -18.860 22.096  1.00 43.37  ? 88  PRO   C CG  1 
ATOM   2131 C CD  . PRO   C 1 89 ? 12.028  -18.882 21.333  1.00 43.74  ? 88  PRO   C CD  1 
ATOM   2132 N N   . HIS   C 1 90 ? 11.245  -21.028 24.290  1.00 52.49  ? 89  HIS   C N   1 
ATOM   2133 C CA  . HIS   C 1 90 ? 11.035  -21.288 25.711  1.00 51.09  ? 89  HIS   C CA  1 
ATOM   2134 C C   . HIS   C 1 90 ? 9.601   -21.706 26.030  1.00 52.50  ? 89  HIS   C C   1 
ATOM   2135 O O   . HIS   C 1 90 ? 9.252   -21.782 27.198  1.00 60.00  ? 89  HIS   C O   1 
ATOM   2136 C CB  . HIS   C 1 90 ? 11.524  -20.112 26.556  1.00 44.59  ? 89  HIS   C CB  1 
ATOM   2137 C CG  . HIS   C 1 90 ? 12.972  -19.810 26.370  1.00 43.40  ? 89  HIS   C CG  1 
ATOM   2138 N ND1 . HIS   C 1 90 ? 13.424  -18.598 25.904  1.00 40.85  ? 89  HIS   C ND1 1 
ATOM   2139 C CD2 . HIS   C 1 90 ? 14.072  -20.558 26.568  1.00 41.25  ? 89  HIS   C CD2 1 
ATOM   2140 C CE1 . HIS   C 1 90 ? 14.746  -18.597 25.834  1.00 39.13  ? 89  HIS   C CE1 1 
ATOM   2141 N NE2 . HIS   C 1 90 ? 15.168  -19.780 26.256  1.00 41.81  ? 89  HIS   C NE2 1 
ATOM   2142 N N   . ALA   C 1 91 ? 8.784   -22.021 25.019  1.00 56.10  ? 90  ALA   C N   1 
ATOM   2143 C CA  . ALA   C 1 91 ? 7.495   -22.665 25.253  1.00 64.76  ? 90  ALA   C CA  1 
ATOM   2144 C C   . ALA   C 1 91 ? 7.692   -24.052 25.876  1.00 73.36  ? 90  ALA   C C   1 
ATOM   2145 O O   . ALA   C 1 91 ? 8.829   -24.461 26.114  1.00 69.39  ? 90  ALA   C O   1 
ATOM   2146 C CB  . ALA   C 1 91 ? 6.675   -22.730 23.975  1.00 68.36  ? 90  ALA   C CB  1 
ATOM   2147 N N   . SER   C 1 92 ? 6.576   -24.773 26.099  1.00 71.66  ? 91  SER   C N   1 
ATOM   2148 C CA  . SER   C 1 92 ? 6.511   -25.940 26.972  1.00 74.06  ? 91  SER   C CA  1 
ATOM   2149 C C   . SER   C 1 92 ? 6.624   -27.250 26.193  1.00 77.98  ? 91  SER   C C   1 
ATOM   2150 O O   . SER   C 1 92 ? 7.384   -28.136 26.579  1.00 82.91  ? 91  SER   C O   1 
ATOM   2151 C CB  . SER   C 1 92 ? 5.238   -25.933 27.788  1.00 74.91  ? 91  SER   C CB  1 
ATOM   2152 O OG  . SER   C 1 92 ? 5.169   -24.777 28.608  1.00 82.01  ? 91  SER   C OG  1 
ATOM   2153 N N   . TYR   C 1 93 ? 5.805   -27.386 25.144  1.00 80.59  ? 92  TYR   C N   1 
ATOM   2154 C CA  . TYR   C 1 93 ? 5.755   -28.573 24.301  1.00 84.16  ? 92  TYR   C CA  1 
ATOM   2155 C C   . TYR   C 1 93 ? 5.447   -29.804 25.168  1.00 84.52  ? 92  TYR   C C   1 
ATOM   2156 O O   . TYR   C 1 93 ? 6.085   -30.852 24.922  1.00 90.90  ? 92  TYR   C O   1 
ATOM   2157 C CB  . TYR   C 1 93 ? 7.021   -28.694 23.440  1.00 83.85  ? 92  TYR   C CB  1 
ATOM   2158 C CG  . TYR   C 1 93 ? 7.393   -27.422 22.685  1.00 73.87  ? 92  TYR   C CG  1 
ATOM   2159 C CD1 . TYR   C 1 93 ? 6.707   -27.048 21.531  1.00 69.16  ? 92  TYR   C CD1 1 
ATOM   2160 C CD2 . TYR   C 1 93 ? 8.417   -26.591 23.132  1.00 69.39  ? 92  TYR   C CD2 1 
ATOM   2161 C CE1 . TYR   C 1 93 ? 7.023   -25.888 20.844  1.00 63.56  ? 92  TYR   C CE1 1 
ATOM   2162 C CE2 . TYR   C 1 93 ? 8.746   -25.430 22.447  1.00 69.68  ? 92  TYR   C CE2 1 
ATOM   2163 C CZ  . TYR   C 1 93 ? 8.050   -25.079 21.300  1.00 69.12  ? 92  TYR   C CZ  1 
ATOM   2164 O OH  . TYR   C 1 93 ? 8.356   -23.927 20.624  1.00 65.61  ? 92  TYR   C OH  1 
HETATM 2165 S S   . SO4   D 2 .  ? 0.940   -33.327 2.127   1.00 104.19 ? 101 SO4   A S   1 
HETATM 2166 O O1  . SO4   D 2 .  ? 1.390   -34.201 1.071   1.00 97.53  ? 101 SO4   A O1  1 
HETATM 2167 O O2  . SO4   D 2 .  ? 0.858   -31.974 1.637   1.00 105.03 ? 101 SO4   A O2  1 
HETATM 2168 O O3  . SO4   D 2 .  ? -0.360  -33.754 2.576   1.00 111.23 ? 101 SO4   A O3  1 
HETATM 2169 O O4  . SO4   D 2 .  ? 1.867   -33.385 3.223   1.00 100.75 ? 101 SO4   A O4  1 
HETATM 2170 S S   . SO4   E 2 .  ? -9.507  -24.853 1.218   1.00 96.92  ? 102 SO4   A S   1 
HETATM 2171 O O1  . SO4   E 2 .  ? -9.330  -24.616 -0.190  1.00 81.12  ? 102 SO4   A O1  1 
HETATM 2172 O O2  . SO4   E 2 .  ? -9.458  -23.602 1.933   1.00 98.95  ? 102 SO4   A O2  1 
HETATM 2173 O O3  . SO4   E 2 .  ? -10.782 -25.490 1.433   1.00 107.87 ? 102 SO4   A O3  1 
HETATM 2174 O O4  . SO4   E 2 .  ? -8.458  -25.713 1.703   1.00 100.01 ? 102 SO4   A O4  1 
HETATM 2175 C C1  . EDO   F 3 .  ? 13.847  -19.500 -7.294  1.00 39.28  ? 103 EDO   A C1  1 
HETATM 2176 O O1  . EDO   F 3 .  ? 15.033  -18.730 -7.177  1.00 34.00  ? 103 EDO   A O1  1 
HETATM 2177 C C2  . EDO   F 3 .  ? 12.913  -19.025 -8.372  1.00 37.34  ? 103 EDO   A C2  1 
HETATM 2178 O O2  . EDO   F 3 .  ? 12.446  -17.716 -8.190  1.00 37.40  ? 103 EDO   A O2  1 
HETATM 2179 S S   . SO4   G 2 .  ? 9.025   -29.228 6.019   1.00 55.71  ? 104 SO4   A S   1 
HETATM 2180 O O1  . SO4   G 2 .  ? 9.800   -28.209 5.390   1.00 68.92  ? 104 SO4   A O1  1 
HETATM 2181 O O2  . SO4   G 2 .  ? 8.764   -30.298 5.073   1.00 68.56  ? 104 SO4   A O2  1 
HETATM 2182 O O3  . SO4   G 2 .  ? 9.740   -29.763 7.157   1.00 69.13  ? 104 SO4   A O3  1 
HETATM 2183 O O4  . SO4   G 2 .  ? 7.768   -28.677 6.452   1.00 70.08  ? 104 SO4   A O4  1 
HETATM 2184 S S   . SO4   H 2 .  ? 7.727   -8.529  -24.845 1.00 82.79  ? 101 SO4   B S   1 
HETATM 2185 O O1  . SO4   H 2 .  ? 8.782   -8.706  -25.797 1.00 43.75  ? 101 SO4   B O1  1 
HETATM 2186 O O2  . SO4   H 2 .  ? 6.485   -9.011  -25.427 1.00 56.03  ? 101 SO4   B O2  1 
HETATM 2187 O O3  . SO4   H 2 .  ? 7.967   -9.285  -23.609 1.00 59.59  ? 101 SO4   B O3  1 
HETATM 2188 O O4  . SO4   H 2 .  ? 7.677   -7.098  -24.574 1.00 56.18  ? 101 SO4   B O4  1 
HETATM 2189 S S   . SO4   I 2 .  ? 14.589  -27.116 -26.627 1.00 52.94  ? 102 SO4   B S   1 
HETATM 2190 O O1  . SO4   I 2 .  ? 15.956  -26.790 -26.290 1.00 51.89  ? 102 SO4   B O1  1 
HETATM 2191 O O2  . SO4   I 2 .  ? 14.588  -28.346 -27.380 1.00 59.13  ? 102 SO4   B O2  1 
HETATM 2192 O O3  . SO4   I 2 .  ? 13.820  -27.280 -25.423 1.00 60.14  ? 102 SO4   B O3  1 
HETATM 2193 O O4  . SO4   I 2 .  ? 13.984  -26.069 -27.418 1.00 53.93  ? 102 SO4   B O4  1 
HETATM 2194 N N1  . A1A3W J 4 .  ? 22.113  -16.750 -23.867 0.84 56.01  ? 103 A1A3W B N1  1 
HETATM 2195 C C4  . A1A3W J 4 .  ? 19.335  -16.685 -24.212 0.84 44.43  ? 103 A1A3W B C4  1 
HETATM 2196 C C5  . A1A3W J 4 .  ? 19.930  -17.642 -23.409 0.84 43.58  ? 103 A1A3W B C5  1 
HETATM 2197 C C6  . A1A3W J 4 .  ? 21.305  -17.638 -23.269 0.84 53.96  ? 103 A1A3W B C6  1 
HETATM 2198 C C7  . A1A3W J 4 .  ? 21.528  -15.828 -24.635 0.84 47.24  ? 103 A1A3W B C7  1 
HETATM 2199 C C8  . A1A3W J 4 .  ? 20.160  -15.760 -24.841 0.84 44.22  ? 103 A1A3W B C8  1 
HETATM 2200 C C3  . A1A3W J 4 .  ? 17.226  -15.977 -21.853 0.84 51.76  ? 103 A1A3W B C3  1 
HETATM 2201 N N   . A1A3W J 4 .  ? 17.186  -15.782 -23.309 0.84 46.72  ? 103 A1A3W B N   1 
HETATM 2202 C C2  . A1A3W J 4 .  ? 17.826  -16.617 -24.345 0.84 37.11  ? 103 A1A3W B C2  1 
HETATM 2203 C C1  . A1A3W J 4 .  ? 17.439  -16.111 -25.731 0.84 41.65  ? 103 A1A3W B C1  1 
HETATM 2204 C C   . A1A3W J 4 .  ? 17.086  -14.625 -25.736 0.84 48.11  ? 103 A1A3W B C   1 
HETATM 2205 S S   . SO4   K 2 .  ? 29.112  -37.923 12.152  1.00 97.18  ? 101 SO4   C S   1 
HETATM 2206 O O1  . SO4   K 2 .  ? 30.102  -36.997 11.657  1.00 96.65  ? 101 SO4   C O1  1 
HETATM 2207 O O2  . SO4   K 2 .  ? 28.110  -38.154 11.143  1.00 69.91  ? 101 SO4   C O2  1 
HETATM 2208 O O3  . SO4   K 2 .  ? 29.743  -39.168 12.493  1.00 90.86  ? 101 SO4   C O3  1 
HETATM 2209 O O4  . SO4   K 2 .  ? 28.492  -37.373 13.325  1.00 104.79 ? 101 SO4   C O4  1 
HETATM 2210 N N1  . A1A3W L 4 .  ? 18.016  -39.146 21.248  0.62 34.01  ? 102 A1A3W C N1  1 
HETATM 2211 C C4  . A1A3W L 4 .  ? 17.585  -37.993 18.744  0.62 29.98  ? 102 A1A3W C C4  1 
HETATM 2212 C C5  . A1A3W L 4 .  ? 17.160  -37.370 19.903  0.62 30.40  ? 102 A1A3W C C5  1 
HETATM 2213 C C6  . A1A3W L 4 .  ? 17.393  -37.975 21.117  0.62 31.44  ? 102 A1A3W C C6  1 
HETATM 2214 C C7  . A1A3W L 4 .  ? 18.460  -39.722 20.131  0.62 33.08  ? 102 A1A3W C C7  1 
HETATM 2215 C C8  . A1A3W L 4 .  ? 18.267  -39.193 18.870  0.62 32.62  ? 102 A1A3W C C8  1 
HETATM 2216 C C3  . A1A3W L 4 .  ? 15.596  -39.292 17.023  0.62 36.99  ? 102 A1A3W C C3  1 
HETATM 2217 N N   . A1A3W L 4 .  ? 15.866  -37.846 16.968  0.62 33.43  ? 102 A1A3W C N   1 
HETATM 2218 C C2  . A1A3W L 4 .  ? 17.233  -37.449 17.369  0.62 31.83  ? 102 A1A3W C C2  1 
HETATM 2219 C C1  . A1A3W L 4 .  ? 17.425  -35.937 17.232  0.62 34.71  ? 102 A1A3W C C1  1 
HETATM 2220 C C   . A1A3W L 4 .  ? 16.210  -35.140 17.671  0.62 30.20  ? 102 A1A3W C C   1 
HETATM 2221 O O   . HOH   M 5 .  ? 8.885   -32.108 4.111   1.00 51.68  ? 201 HOH   A O   1 
HETATM 2222 O O   . HOH   M 5 .  ? 5.704   -28.850 7.351   1.00 43.02  ? 202 HOH   A O   1 
HETATM 2223 O O   . HOH   M 5 .  ? -5.705  -13.472 -16.729 1.00 51.49  ? 203 HOH   A O   1 
HETATM 2224 O O   . HOH   M 5 .  ? -2.176  -30.882 -4.107  1.00 51.29  ? 204 HOH   A O   1 
HETATM 2225 O O   . HOH   M 5 .  ? 10.969  -29.686 3.214   1.00 43.92  ? 205 HOH   A O   1 
HETATM 2226 O O   . HOH   M 5 .  ? 0.312   -33.759 5.155   1.00 62.50  ? 206 HOH   A O   1 
HETATM 2227 O O   . HOH   M 5 .  ? 9.063   -18.250 -10.835 1.00 33.16  ? 207 HOH   A O   1 
HETATM 2228 O O   . HOH   M 5 .  ? 2.209   -25.091 -6.452  1.00 44.70  ? 208 HOH   A O   1 
HETATM 2229 O O   . HOH   M 5 .  ? -3.875  -10.846 6.742   1.00 38.81  ? 209 HOH   A O   1 
HETATM 2230 O O   . HOH   M 5 .  ? 9.670   -30.533 9.632   1.00 35.34  ? 210 HOH   A O   1 
HETATM 2231 O O   . HOH   M 5 .  ? -6.858  -5.307  9.141   1.00 37.22  ? 211 HOH   A O   1 
HETATM 2232 O O   . HOH   M 5 .  ? 1.836   -24.536 14.310  1.00 77.98  ? 212 HOH   A O   1 
HETATM 2233 O O   . HOH   M 5 .  ? 12.664  -11.997 8.221   1.00 55.44  ? 213 HOH   A O   1 
HETATM 2234 O O   . HOH   M 5 .  ? 14.342  -29.404 4.209   1.00 40.30  ? 214 HOH   A O   1 
HETATM 2235 O O   . HOH   M 5 .  ? 0.463   -10.420 -15.494 1.00 45.24  ? 215 HOH   A O   1 
HETATM 2236 O O   . HOH   M 5 .  ? -2.566  3.234   -2.218  1.00 43.99  ? 216 HOH   A O   1 
HETATM 2237 O O   . HOH   M 5 .  ? 15.734  -24.530 2.040   1.00 38.01  ? 217 HOH   A O   1 
HETATM 2238 O O   . HOH   M 5 .  ? 11.050  -23.606 9.982   1.00 38.50  ? 218 HOH   A O   1 
HETATM 2239 O O   . HOH   M 5 .  ? -4.491  -21.112 6.118   1.00 42.67  ? 219 HOH   A O   1 
HETATM 2240 O O   . HOH   M 5 .  ? 0.167   -22.982 9.610   1.00 50.57  ? 220 HOH   A O   1 
HETATM 2241 O O   . HOH   M 5 .  ? 19.800  -15.417 7.281   1.00 30.33  ? 221 HOH   A O   1 
HETATM 2242 O O   . HOH   M 5 .  ? 9.422   -22.756 -9.400  1.00 37.01  ? 222 HOH   A O   1 
HETATM 2243 O O   . HOH   M 5 .  ? 4.324   -3.552  -3.277  1.00 32.21  ? 223 HOH   A O   1 
HETATM 2244 O O   . HOH   M 5 .  ? 6.882   -10.515 -12.054 1.00 40.60  ? 224 HOH   A O   1 
HETATM 2245 O O   . HOH   M 5 .  ? 1.585   0.547   -7.487  1.00 38.99  ? 225 HOH   A O   1 
HETATM 2246 O O   . HOH   M 5 .  ? 4.614   -7.773  1.328   1.00 34.93  ? 226 HOH   A O   1 
HETATM 2247 O O   . HOH   M 5 .  ? -7.960  -17.164 6.698   1.00 41.36  ? 227 HOH   A O   1 
HETATM 2248 O O   . HOH   M 5 .  ? 17.126  -12.894 1.320   1.00 20.38  ? 228 HOH   A O   1 
HETATM 2249 O O   . HOH   M 5 .  ? 15.014  -28.127 -0.401  1.00 57.94  ? 229 HOH   A O   1 
HETATM 2250 O O   . HOH   M 5 .  ? -1.848  -22.066 -0.400  1.00 28.53  ? 230 HOH   A O   1 
HETATM 2251 O O   . HOH   M 5 .  ? 9.564   -6.067  -1.661  1.00 35.50  ? 231 HOH   A O   1 
HETATM 2252 O O   . HOH   M 5 .  ? 3.889   -34.640 4.612   1.00 53.10  ? 232 HOH   A O   1 
HETATM 2253 O O   . HOH   M 5 .  ? -8.281  -15.795 -1.005  1.00 35.14  ? 233 HOH   A O   1 
HETATM 2254 O O   . HOH   M 5 .  ? 13.057  -28.164 -4.469  1.00 51.38  ? 234 HOH   A O   1 
HETATM 2255 O O   . HOH   M 5 .  ? -0.653  -29.087 10.524  1.00 55.43  ? 235 HOH   A O   1 
HETATM 2256 O O   . HOH   M 5 .  ? 10.744  -5.163  -7.737  1.00 37.17  ? 236 HOH   A O   1 
HETATM 2257 O O   . HOH   M 5 .  ? -6.288  -11.541 -11.406 1.00 42.85  ? 237 HOH   A O   1 
HETATM 2258 O O   . HOH   M 5 .  ? 11.414  -11.870 5.956   1.00 35.26  ? 238 HOH   A O   1 
HETATM 2259 O O   . HOH   M 5 .  ? -0.821  -20.808 7.110   1.00 34.68  ? 239 HOH   A O   1 
HETATM 2260 O O   . HOH   M 5 .  ? -5.808  -15.975 -7.935  1.00 28.46  ? 240 HOH   A O   1 
HETATM 2261 O O   . HOH   M 5 .  ? 2.353   -25.290 -10.048 1.00 38.64  ? 241 HOH   A O   1 
HETATM 2262 O O   . HOH   M 5 .  ? 15.646  -12.135 -5.318  1.00 33.17  ? 242 HOH   A O   1 
HETATM 2263 O O   . HOH   M 5 .  ? 0.796   -17.873 -18.871 1.00 56.51  ? 243 HOH   A O   1 
HETATM 2264 O O   . HOH   M 5 .  ? 12.796  -9.430  -7.123  1.00 46.18  ? 244 HOH   A O   1 
HETATM 2265 O O   . HOH   M 5 .  ? -8.058  -16.729 1.839   1.00 40.29  ? 245 HOH   A O   1 
HETATM 2266 O O   . HOH   M 5 .  ? 10.037  -13.013 9.519   1.00 41.12  ? 246 HOH   A O   1 
HETATM 2267 O O   . HOH   M 5 .  ? 2.492   -6.355  5.563   1.00 42.12  ? 247 HOH   A O   1 
HETATM 2268 O O   . HOH   M 5 .  ? 13.244  -12.007 -4.210  1.00 23.93  ? 248 HOH   A O   1 
HETATM 2269 O O   . HOH   M 5 .  ? 16.907  -18.253 -9.605  1.00 49.10  ? 249 HOH   A O   1 
HETATM 2270 O O   . HOH   M 5 .  ? -7.019  -21.932 -5.779  1.00 46.66  ? 250 HOH   A O   1 
HETATM 2271 O O   . HOH   M 5 .  ? -5.876  -19.754 -5.567  1.00 35.17  ? 251 HOH   A O   1 
HETATM 2272 O O   . HOH   M 5 .  ? 11.404  -12.349 -6.109  1.00 27.96  ? 252 HOH   A O   1 
HETATM 2273 O O   . HOH   M 5 .  ? 3.117   -29.474 -0.371  1.00 40.31  ? 253 HOH   A O   1 
HETATM 2274 O O   . HOH   M 5 .  ? -11.095 -26.937 -0.996  1.00 73.34  ? 254 HOH   A O   1 
HETATM 2275 O O   . HOH   M 5 .  ? -1.658  -7.461  11.523  1.00 44.55  ? 255 HOH   A O   1 
HETATM 2276 O O   . HOH   M 5 .  ? 12.525  -13.341 -8.486  1.00 39.74  ? 256 HOH   A O   1 
HETATM 2277 O O   . HOH   M 5 .  ? 7.754   -7.855  1.230   1.00 33.57  ? 257 HOH   A O   1 
HETATM 2278 O O   . HOH   M 5 .  ? 1.876   -4.701  -10.405 1.00 45.54  ? 258 HOH   A O   1 
HETATM 2279 O O   . HOH   M 5 .  ? -8.520  -21.237 -1.269  1.00 43.31  ? 259 HOH   A O   1 
HETATM 2280 O O   . HOH   M 5 .  ? 8.122   -17.913 -15.804 1.00 50.35  ? 260 HOH   A O   1 
HETATM 2281 O O   . HOH   M 5 .  ? 6.436   -16.059 -15.059 1.00 52.96  ? 261 HOH   A O   1 
HETATM 2282 O O   . HOH   M 5 .  ? -1.466  -11.768 11.298  1.00 35.52  ? 262 HOH   A O   1 
HETATM 2283 O O   . HOH   M 5 .  ? -4.373  -25.833 -5.462  1.00 39.73  ? 263 HOH   A O   1 
HETATM 2284 O O   . HOH   M 5 .  ? 1.726   -10.411 11.845  1.00 39.90  ? 264 HOH   A O   1 
HETATM 2285 O O   . HOH   M 5 .  ? 2.802   -9.972  -13.351 1.00 43.74  ? 265 HOH   A O   1 
HETATM 2286 O O   . HOH   M 5 .  ? 16.578  -12.280 -16.939 1.00 42.93  ? 266 HOH   A O   1 
HETATM 2287 O O   . HOH   M 5 .  ? 9.205   -2.799  -0.329  1.00 59.96  ? 267 HOH   A O   1 
HETATM 2288 O O   . HOH   M 5 .  ? -0.598  -20.459 11.460  1.00 48.79  ? 268 HOH   A O   1 
HETATM 2289 O O   . HOH   M 5 .  ? 11.327  -6.168  -3.735  1.00 43.27  ? 269 HOH   A O   1 
HETATM 2290 O O   . HOH   M 5 .  ? 7.935   -17.488 8.674   1.00 40.79  ? 270 HOH   A O   1 
HETATM 2291 O O   . HOH   M 5 .  ? -4.139  -7.776  10.588  1.00 54.71  ? 271 HOH   A O   1 
HETATM 2292 O O   . HOH   M 5 .  ? 5.034   -7.702  3.973   1.00 36.85  ? 272 HOH   A O   1 
HETATM 2293 O O   . HOH   M 5 .  ? -6.159  -12.686 6.733   1.00 38.20  ? 273 HOH   A O   1 
HETATM 2294 O O   . HOH   M 5 .  ? 8.802   -16.482 -13.172 1.00 37.31  ? 274 HOH   A O   1 
HETATM 2295 O O   . HOH   M 5 .  ? -6.119  -26.713 3.434   1.00 42.04  ? 275 HOH   A O   1 
HETATM 2296 O O   . HOH   M 5 .  ? -11.179 -16.112 -3.563  1.00 43.70  ? 276 HOH   A O   1 
HETATM 2297 O O   . HOH   M 5 .  ? -7.398  -11.520 -7.954  1.00 30.70  ? 277 HOH   A O   1 
HETATM 2298 O O   . HOH   M 5 .  ? 14.956  -13.332 10.574  1.00 50.34  ? 278 HOH   A O   1 
HETATM 2299 O O   . HOH   M 5 .  ? 12.827  -15.450 -12.147 1.00 49.48  ? 279 HOH   A O   1 
HETATM 2300 O O   . HOH   M 5 .  ? 21.257  -16.684 -3.427  1.00 32.63  ? 280 HOH   A O   1 
HETATM 2301 O O   . HOH   M 5 .  ? 10.968  -7.769  0.411   1.00 25.47  ? 281 HOH   A O   1 
HETATM 2302 O O   . HOH   M 5 .  ? 22.274  -16.606 -0.461  1.00 44.95  ? 282 HOH   A O   1 
HETATM 2303 O O   . HOH   M 5 .  ? 10.495  -27.720 -7.003  1.00 56.56  ? 283 HOH   A O   1 
HETATM 2304 O O   . HOH   M 5 .  ? 5.938   -5.805  0.611   1.00 43.27  ? 284 HOH   A O   1 
HETATM 2305 O O   . HOH   M 5 .  ? 7.562   -29.863 -3.814  1.00 60.42  ? 285 HOH   A O   1 
HETATM 2306 O O   . HOH   M 5 .  ? -8.261  -19.667 -3.364  1.00 45.98  ? 286 HOH   A O   1 
HETATM 2307 O O   . HOH   M 5 .  ? 9.492   -20.610 -18.303 1.00 48.35  ? 287 HOH   A O   1 
HETATM 2308 O O   . HOH   M 5 .  ? 8.762   -9.245  -13.735 1.00 44.03  ? 288 HOH   A O   1 
HETATM 2309 O O   . HOH   M 5 .  ? 1.117   -29.206 -6.996  1.00 53.34  ? 289 HOH   A O   1 
HETATM 2310 O O   . HOH   M 5 .  ? -5.707  -23.663 -6.830  1.00 40.51  ? 290 HOH   A O   1 
HETATM 2311 O O   . HOH   M 5 .  ? 4.747   -6.966  -10.847 1.00 47.09  ? 291 HOH   A O   1 
HETATM 2312 O O   . HOH   M 5 .  ? -3.974  -11.008 9.734   1.00 51.40  ? 292 HOH   A O   1 
HETATM 2313 O O   . HOH   M 5 .  ? -4.146  -26.805 7.151   1.00 51.35  ? 293 HOH   A O   1 
HETATM 2314 O O   . HOH   M 5 .  ? -7.435  -13.989 -9.334  1.00 35.71  ? 294 HOH   A O   1 
HETATM 2315 O O   . HOH   M 5 .  ? 11.321  -2.067  -1.437  1.00 45.12  ? 295 HOH   A O   1 
HETATM 2316 O O   . HOH   M 5 .  ? -11.340 -13.502 -2.871  1.00 41.70  ? 296 HOH   A O   1 
HETATM 2317 O O   . HOH   M 5 .  ? -6.284  -22.873 5.595   1.00 56.24  ? 297 HOH   A O   1 
HETATM 2318 O O   . HOH   M 5 .  ? -7.234  -19.159 8.230   1.00 43.12  ? 298 HOH   A O   1 
HETATM 2319 O O   . HOH   M 5 .  ? 8.034   -8.165  4.636   1.00 35.97  ? 299 HOH   A O   1 
HETATM 2320 O O   . HOH   M 5 .  ? 4.559   -9.593  -11.399 1.00 46.88  ? 300 HOH   A O   1 
HETATM 2321 O O   . HOH   M 5 .  ? 12.603  -18.634 -15.246 1.00 41.42  ? 301 HOH   A O   1 
HETATM 2322 O O   . HOH   M 5 .  ? -5.211  -20.964 -8.220  1.00 58.54  ? 302 HOH   A O   1 
HETATM 2323 O O   . HOH   M 5 .  ? 3.768   -3.570  2.031   1.00 63.72  ? 303 HOH   A O   1 
HETATM 2324 O O   . HOH   N 5 .  ? 10.200  -19.875 -43.285 1.00 44.43  ? 201 HOH   B O   1 
HETATM 2325 O O   . HOH   N 5 .  ? 30.052  -12.936 -45.631 1.00 60.63  ? 202 HOH   B O   1 
HETATM 2326 O O   . HOH   N 5 .  ? 20.084  -22.076 -23.360 1.00 46.84  ? 203 HOH   B O   1 
HETATM 2327 O O   . HOH   N 5 .  ? 26.263  -4.876  -33.582 1.00 52.01  ? 204 HOH   B O   1 
HETATM 2328 O O   . HOH   N 5 .  ? 10.023  -11.438 -38.167 1.00 46.51  ? 205 HOH   B O   1 
HETATM 2329 O O   . HOH   N 5 .  ? 28.020  -8.304  -29.044 1.00 45.53  ? 206 HOH   B O   1 
HETATM 2330 O O   . HOH   N 5 .  ? 25.306  -5.243  -30.044 1.00 38.07  ? 207 HOH   B O   1 
HETATM 2331 O O   . HOH   N 5 .  ? 6.727   -12.277 -26.236 1.00 33.26  ? 208 HOH   B O   1 
HETATM 2332 O O   . HOH   N 5 .  ? 26.169  -0.406  -29.350 1.00 49.16  ? 209 HOH   B O   1 
HETATM 2333 O O   . HOH   N 5 .  ? 12.978  -4.899  -41.957 1.00 46.44  ? 210 HOH   B O   1 
HETATM 2334 O O   . HOH   N 5 .  ? 30.780  -8.324  -30.061 1.00 47.72  ? 211 HOH   B O   1 
HETATM 2335 O O   . HOH   N 5 .  ? 30.503  -19.952 -40.490 1.00 34.75  ? 212 HOH   B O   1 
HETATM 2336 O O   . HOH   N 5 .  ? 24.571  -1.943  -36.488 1.00 50.34  ? 213 HOH   B O   1 
HETATM 2337 O O   . HOH   N 5 .  ? 25.494  -6.116  -35.963 1.00 37.84  ? 214 HOH   B O   1 
HETATM 2338 O O   . HOH   N 5 .  ? 21.294  -26.369 -30.255 1.00 57.52  ? 215 HOH   B O   1 
HETATM 2339 O O   . HOH   N 5 .  ? 22.232  3.335   -32.836 1.00 48.25  ? 216 HOH   B O   1 
HETATM 2340 O O   . HOH   N 5 .  ? 26.371  -23.229 -31.277 1.00 33.97  ? 217 HOH   B O   1 
HETATM 2341 O O   . HOH   N 5 .  ? 10.714  -18.981 -33.068 1.00 30.30  ? 218 HOH   B O   1 
HETATM 2342 O O   . HOH   N 5 .  ? 34.895  -23.346 -30.133 1.00 51.40  ? 219 HOH   B O   1 
HETATM 2343 O O   . HOH   N 5 .  ? 20.947  -13.519 -42.807 1.00 38.43  ? 220 HOH   B O   1 
HETATM 2344 O O   . HOH   N 5 .  ? 16.826  -19.537 -28.916 1.00 27.45  ? 221 HOH   B O   1 
HETATM 2345 O O   . HOH   N 5 .  ? 27.871  -17.754 -25.146 1.00 51.53  ? 222 HOH   B O   1 
HETATM 2346 O O   . HOH   N 5 .  ? 22.788  -23.348 -28.912 1.00 40.03  ? 223 HOH   B O   1 
HETATM 2347 O O   . HOH   N 5 .  ? 18.247  -0.744  -38.509 1.00 30.19  ? 224 HOH   B O   1 
HETATM 2348 O O   . HOH   N 5 .  ? 32.607  -19.063 -42.630 1.00 45.19  ? 225 HOH   B O   1 
HETATM 2349 O O   . HOH   N 5 .  ? 23.803  -4.335  -37.000 1.00 29.51  ? 226 HOH   B O   1 
HETATM 2350 O O   . HOH   N 5 .  ? 32.043  -12.383 -39.491 1.00 56.30  ? 227 HOH   B O   1 
HETATM 2351 O O   . HOH   N 5 .  ? 20.642  -3.293  -23.307 1.00 68.11  ? 228 HOH   B O   1 
HETATM 2352 O O   . HOH   N 5 .  ? 23.738  -2.447  -29.251 1.00 36.80  ? 229 HOH   B O   1 
HETATM 2353 O O   . HOH   N 5 .  ? 20.641  -10.335 -43.043 1.00 38.20  ? 230 HOH   B O   1 
HETATM 2354 O O   . HOH   N 5 .  ? 18.467  -25.982 -28.824 1.00 43.15  ? 231 HOH   B O   1 
HETATM 2355 O O   . HOH   N 5 .  ? 17.455  -19.832 -42.191 1.00 52.11  ? 232 HOH   B O   1 
HETATM 2356 O O   . HOH   N 5 .  ? 7.761   -18.373 -31.995 1.00 45.47  ? 233 HOH   B O   1 
HETATM 2357 O O   . HOH   N 5 .  ? 18.052  -3.722  -22.323 1.00 54.65  ? 234 HOH   B O   1 
HETATM 2358 O O   . HOH   N 5 .  ? 8.743   -8.577  -16.465 1.00 45.42  ? 235 HOH   B O   1 
HETATM 2359 O O   . HOH   N 5 .  ? 14.557  -6.518  -41.223 1.00 44.64  ? 236 HOH   B O   1 
HETATM 2360 O O   . HOH   N 5 .  ? 7.291   -19.145 -35.017 1.00 49.09  ? 237 HOH   B O   1 
HETATM 2361 O O   . HOH   N 5 .  ? 32.009  -21.249 -38.335 1.00 44.36  ? 238 HOH   B O   1 
HETATM 2362 O O   . HOH   N 5 .  ? 19.894  -25.772 -34.232 1.00 40.99  ? 239 HOH   B O   1 
HETATM 2363 O O   . HOH   N 5 .  ? 10.757  -21.967 -32.855 1.00 37.05  ? 240 HOH   B O   1 
HETATM 2364 O O   . HOH   N 5 .  ? 13.145  -22.500 -20.693 1.00 56.52  ? 241 HOH   B O   1 
HETATM 2365 O O   . HOH   N 5 .  ? 10.659  -16.987 -44.432 1.00 43.72  ? 242 HOH   B O   1 
HETATM 2366 O O   . HOH   N 5 .  ? 14.732  -24.535 -40.461 1.00 42.43  ? 243 HOH   B O   1 
HETATM 2367 O O   . HOH   N 5 .  ? 7.668   -12.649 -38.965 1.00 50.72  ? 244 HOH   B O   1 
HETATM 2368 O O   . HOH   N 5 .  ? 3.150   -8.676  -27.331 1.00 54.31  ? 245 HOH   B O   1 
HETATM 2369 O O   . HOH   N 5 .  ? 27.632  -10.865 -28.890 1.00 46.11  ? 246 HOH   B O   1 
HETATM 2370 O O   . HOH   N 5 .  ? 8.478   -28.203 -38.391 1.00 61.94  ? 247 HOH   B O   1 
HETATM 2371 O O   . HOH   N 5 .  ? 18.037  -15.959 -45.798 1.00 37.71  ? 248 HOH   B O   1 
HETATM 2372 O O   . HOH   N 5 .  ? 21.148  -6.661  -42.724 1.00 37.70  ? 249 HOH   B O   1 
HETATM 2373 O O   . HOH   N 5 .  ? 17.941  -23.432 -20.756 1.00 63.07  ? 250 HOH   B O   1 
HETATM 2374 O O   . HOH   N 5 .  ? 27.997  -24.977 -35.368 1.00 36.00  ? 251 HOH   B O   1 
HETATM 2375 O O   . HOH   N 5 .  ? 23.723  -11.328 -22.072 1.00 43.40  ? 252 HOH   B O   1 
HETATM 2376 O O   . HOH   N 5 .  ? 1.821   -13.131 -28.569 1.00 50.33  ? 253 HOH   B O   1 
HETATM 2377 O O   . HOH   N 5 .  ? 7.384   -8.153  -20.720 1.00 51.02  ? 254 HOH   B O   1 
HETATM 2378 O O   . HOH   N 5 .  ? 24.860  -6.689  -42.821 1.00 43.92  ? 255 HOH   B O   1 
HETATM 2379 O O   . HOH   N 5 .  ? 20.732  3.596   -33.023 1.00 33.52  ? 256 HOH   B O   1 
HETATM 2380 O O   . HOH   N 5 .  ? 39.239  -13.265 -39.398 1.00 69.60  ? 257 HOH   B O   1 
HETATM 2381 O O   . HOH   N 5 .  ? 12.563  -20.555 -19.902 1.00 62.76  ? 258 HOH   B O   1 
HETATM 2382 O O   . HOH   N 5 .  ? 17.437  -9.929  -43.869 1.00 47.51  ? 259 HOH   B O   1 
HETATM 2383 O O   . HOH   N 5 .  ? 18.706  4.249   -34.236 1.00 42.68  ? 260 HOH   B O   1 
HETATM 2384 O O   . HOH   N 5 .  ? 17.879  -0.450  -25.681 1.00 51.98  ? 261 HOH   B O   1 
HETATM 2385 O O   . HOH   N 5 .  ? 15.178  -8.213  -43.071 1.00 47.04  ? 262 HOH   B O   1 
HETATM 2386 O O   . HOH   N 5 .  ? 9.759   -6.405  -41.087 1.00 44.04  ? 263 HOH   B O   1 
HETATM 2387 O O   . HOH   N 5 .  ? 5.799   -19.934 -25.527 1.00 54.86  ? 264 HOH   B O   1 
HETATM 2388 O O   . HOH   N 5 .  ? 15.351  -22.080 -41.996 1.00 47.69  ? 265 HOH   B O   1 
HETATM 2389 O O   . HOH   N 5 .  ? 7.425   -9.931  -18.619 1.00 49.94  ? 266 HOH   B O   1 
HETATM 2390 O O   . HOH   N 5 .  ? 22.547  -29.439 -35.655 1.00 48.97  ? 267 HOH   B O   1 
HETATM 2391 O O   . HOH   N 5 .  ? 16.711  2.970   -26.912 1.00 56.91  ? 268 HOH   B O   1 
HETATM 2392 O O   . HOH   O 5 .  ? 26.812  -37.453 9.798   1.00 41.93  ? 201 HOH   C O   1 
HETATM 2393 O O   . HOH   O 5 .  ? 26.496  -38.969 12.635  1.00 41.50  ? 202 HOH   C O   1 
HETATM 2394 O O   . HOH   O 5 .  ? 20.365  -19.852 29.862  1.00 55.84  ? 203 HOH   C O   1 
HETATM 2395 O O   . HOH   O 5 .  ? 5.781   -26.543 16.929  1.00 55.75  ? 204 HOH   C O   1 
HETATM 2396 O O   . HOH   O 5 .  ? 23.422  -41.251 18.324  1.00 50.67  ? 205 HOH   C O   1 
HETATM 2397 O O   . HOH   O 5 .  ? 30.197  -30.962 15.463  1.00 49.92  ? 206 HOH   C O   1 
HETATM 2398 O O   . HOH   O 5 .  ? 7.533   -31.418 12.415  1.00 42.95  ? 207 HOH   C O   1 
HETATM 2399 O O   . HOH   O 5 .  ? 12.678  -31.460 8.524   1.00 35.96  ? 208 HOH   C O   1 
HETATM 2400 O O   . HOH   O 5 .  ? 19.121  -20.045 10.546  1.00 39.29  ? 209 HOH   C O   1 
HETATM 2401 O O   . HOH   O 5 .  ? 23.508  -18.272 21.529  1.00 50.60  ? 210 HOH   C O   1 
HETATM 2402 O O   . HOH   O 5 .  ? 28.136  -37.182 15.867  1.00 44.25  ? 211 HOH   C O   1 
HETATM 2403 O O   . HOH   O 5 .  ? 12.264  -28.442 28.181  1.00 58.94  ? 212 HOH   C O   1 
HETATM 2404 O O   . HOH   O 5 .  ? 30.432  -17.435 9.576   1.00 46.57  ? 213 HOH   C O   1 
HETATM 2405 O O   . HOH   O 5 .  ? 13.874  -37.042 13.678  1.00 43.89  ? 214 HOH   C O   1 
HETATM 2406 O O   . HOH   O 5 .  ? 17.845  -17.000 14.825  1.00 53.24  ? 215 HOH   C O   1 
HETATM 2407 O O   . HOH   O 5 .  ? 25.625  -19.527 6.382   1.00 36.79  ? 216 HOH   C O   1 
HETATM 2408 O O   . HOH   O 5 .  ? 9.066   -36.852 18.270  1.00 59.90  ? 217 HOH   C O   1 
HETATM 2409 O O   . HOH   O 5 .  ? 9.423   -30.196 10.790  1.00 38.12  ? 218 HOH   C O   1 
HETATM 2410 O O   . HOH   O 5 .  ? 31.281  -39.779 27.244  1.00 53.71  ? 219 HOH   C O   1 
HETATM 2411 O O   . HOH   O 5 .  ? 25.680  -33.385 34.931  1.00 51.79  ? 220 HOH   C O   1 
HETATM 2412 O O   . HOH   O 5 .  ? 15.195  -20.978 12.404  1.00 39.90  ? 221 HOH   C O   1 
HETATM 2413 O O   . HOH   O 5 .  ? 32.004  -33.343 25.886  1.00 48.51  ? 222 HOH   C O   1 
HETATM 2414 O O   . HOH   O 5 .  ? 27.481  -15.461 12.587  1.00 60.84  ? 223 HOH   C O   1 
HETATM 2415 O O   . HOH   O 5 .  ? 19.926  -41.783 11.989  1.00 31.42  ? 224 HOH   C O   1 
HETATM 2416 O O   . HOH   O 5 .  ? 27.965  -36.907 24.979  1.00 51.74  ? 225 HOH   C O   1 
HETATM 2417 O O   . HOH   O 5 .  ? 25.177  -31.317 10.722  1.00 34.74  ? 226 HOH   C O   1 
HETATM 2418 O O   . HOH   O 5 .  ? 22.178  -28.485 11.157  1.00 30.95  ? 227 HOH   C O   1 
HETATM 2419 O O   . HOH   O 5 .  ? 22.151  -34.287 16.530  1.00 27.21  ? 228 HOH   C O   1 
HETATM 2420 O O   . HOH   O 5 .  ? 6.913   -17.865 10.982  1.00 41.47  ? 229 HOH   C O   1 
HETATM 2421 O O   . HOH   O 5 .  ? 30.074  -39.529 31.393  1.00 35.82  ? 230 HOH   C O   1 
HETATM 2422 O O   . HOH   O 5 .  ? 15.995  -17.403 19.351  1.00 50.70  ? 231 HOH   C O   1 
HETATM 2423 O O   . HOH   O 5 .  ? 25.877  -17.502 13.760  1.00 42.81  ? 232 HOH   C O   1 
HETATM 2424 O O   . HOH   O 5 .  ? 20.886  -39.773 26.605  1.00 37.08  ? 233 HOH   C O   1 
HETATM 2425 O O   . HOH   O 5 .  ? 20.650  -28.722 8.612   1.00 34.56  ? 234 HOH   C O   1 
HETATM 2426 O O   . HOH   O 5 .  ? 2.810   -28.634 14.464  1.00 63.40  ? 235 HOH   C O   1 
HETATM 2427 O O   . HOH   O 5 .  ? 20.824  -29.549 4.901   1.00 57.75  ? 236 HOH   C O   1 
HETATM 2428 O O   . HOH   O 5 .  ? 13.901  -35.127 45.345  1.00 59.76  ? 237 HOH   C O   1 
HETATM 2429 O O   . HOH   O 5 .  ? 19.133  -26.641 3.223   1.00 56.07  ? 238 HOH   C O   1 
HETATM 2430 O O   . HOH   O 5 .  ? 9.350   -18.809 23.941  1.00 50.14  ? 239 HOH   C O   1 
HETATM 2431 O O   . HOH   O 5 .  ? 33.327  -24.141 31.675  1.00 49.18  ? 240 HOH   C O   1 
HETATM 2432 O O   . HOH   O 5 .  ? 26.194  -17.680 21.080  1.00 66.35  ? 241 HOH   C O   1 
HETATM 2433 O O   . HOH   O 5 .  ? 31.487  -43.348 15.751  1.00 59.37  ? 242 HOH   C O   1 
HETATM 2434 O O   . HOH   O 5 .  ? 16.223  -38.263 11.837  1.00 42.51  ? 243 HOH   C O   1 
HETATM 2435 O O   . HOH   O 5 .  ? 25.602  -39.510 20.114  1.00 38.07  ? 244 HOH   C O   1 
HETATM 2436 O O   . HOH   O 5 .  ? 14.269  -38.607 9.997   1.00 47.54  ? 245 HOH   C O   1 
HETATM 2437 O O   . HOH   O 5 .  ? 31.930  -43.139 11.747  1.00 51.88  ? 246 HOH   C O   1 
HETATM 2438 O O   . HOH   O 5 .  ? 30.798  -35.316 28.832  1.00 52.01  ? 247 HOH   C O   1 
HETATM 2439 O O   . HOH   O 5 .  ? 20.037  -18.842 24.926  1.00 45.13  ? 248 HOH   C O   1 
HETATM 2440 O O   . HOH   O 5 .  ? 30.201  -32.584 18.214  1.00 41.74  ? 249 HOH   C O   1 
HETATM 2441 O O   . HOH   O 5 .  ? 14.667  -22.113 28.227  1.00 70.96  ? 250 HOH   C O   1 
HETATM 2442 O O   . HOH   O 5 .  ? 30.075  -25.211 32.500  1.00 55.87  ? 251 HOH   C O   1 
HETATM 2443 O O   . HOH   O 5 .  ? 20.493  -12.867 13.391  1.00 48.28  ? 252 HOH   C O   1 
HETATM 2444 O O   . HOH   O 5 .  ? 17.462  -36.476 29.570  1.00 57.07  ? 253 HOH   C O   1 
HETATM 2445 O O   . HOH   O 5 .  ? 12.004  -21.099 10.845  1.00 38.67  ? 254 HOH   C O   1 
HETATM 2446 O O   . HOH   O 5 .  ? 27.746  -38.996 24.532  1.00 56.82  ? 255 HOH   C O   1 
HETATM 2447 O O   . HOH   O 5 .  ? 29.275  -41.542 27.249  1.00 45.89  ? 256 HOH   C O   1 
HETATM 2448 O O   . HOH   O 5 .  ? 5.064   -23.997 18.645  1.00 60.18  ? 257 HOH   C O   1 
HETATM 2449 O O   . HOH   O 5 .  ? 18.103  -41.672 39.654  1.00 65.88  ? 258 HOH   C O   1 
HETATM 2450 O O   . HOH   O 5 .  ? 22.568  -13.924 13.154  1.00 48.34  ? 259 HOH   C O   1 
HETATM 2451 O O   . HOH   O 5 .  ? 32.350  -38.956 30.090  1.00 51.06  ? 260 HOH   C O   1 
HETATM 2452 O O   . HOH   O 5 .  ? 28.622  -41.285 30.004  1.00 46.01  ? 261 HOH   C O   1 
HETATM 2453 O O   . HOH   O 5 .  ? 29.190  -40.554 19.420  1.00 66.54  ? 262 HOH   C O   1 
# 
