data_7HHG
# 
_entry.id   7HHG 
# 
_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   7HHG         pdb_00007hhg 10.2210/pdb7hhg/pdb 
WWPDB D_1001407478 ?            ?                   
# 
_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                        7HHG 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    2   ? ?    ? ? 
4 non-polymer syn 'N-[(piperidin-4-yl)methyl]methanesulfonamide'     192.279   1   ? ?    ? ? 
5 water       nat water                                              18.015    295 ? ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'HDGF-related protein 2,HRP-2,Hepatoma-derived growth factor 2,HDGF-2' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GMPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKSKDKYGKPNKRKGFNE
GLWEIQNNPHASYS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                                  SO4 
3 1,2-ETHANEDIOL                                 EDO 
4 'N-[(piperidin-4-yl)methyl]methanesulfonamide' W1A 
5 water                                          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1  GLY n 
1 2  MET n 
1 3  PRO n 
1 4  HIS n 
1 5  ALA n 
1 6  PHE n 
1 7  LYS n 
1 8  PRO n 
1 9  GLY n 
1 10 ASP n 
1 11 LEU n 
1 12 VAL n 
1 13 PHE n 
1 14 ALA n 
1 15 LYS n 
1 16 MET n 
1 17 LYS n 
1 18 GLY n 
1 19 TYR n 
1 20 PRO n 
1 21 HIS n 
1 22 TRP n 
1 23 PRO n 
1 24 ALA n 
1 25 ARG n 
1 26 ILE n 
1 27 ASP n 
1 28 ASP n 
1 29 ILE n 
1 30 ALA n 
1 31 ASP n 
1 32 GLY n 
1 33 ALA n 
1 34 VAL n 
1 35 LYS n 
1 36 PRO n 
1 37 PRO n 
1 38 PRO n 
1 39 ASN n 
1 40 LYS n 
1 41 TYR n 
1 42 PRO n 
1 43 ILE n 
1 44 PHE n 
1 45 PHE n 
1 46 PHE n 
1 47 GLY n 
1 48 THR n 
1 49 HIS n 
1 50 GLU n 
1 51 THR n 
1 52 ALA n 
1 53 PHE n 
1 54 LEU n 
1 55 GLY n 
1 56 PRO n 
1 57 LYS n 
1 58 ASP n 
1 59 LEU n 
1 60 PHE n 
1 61 PRO n 
1 62 TYR n 
1 63 ASP n 
1 64 LYS n 
1 65 SER n 
1 66 LYS n 
1 67 ASP n 
1 68 LYS n 
1 69 TYR n 
1 70 GLY n 
1 71 LYS n 
1 72 PRO n 
1 73 ASN n 
1 74 LYS n 
1 75 ARG n 
1 76 LYS n 
1 77 GLY n 
1 78 PHE n 
1 79 ASN n 
1 80 GLU n 
1 81 GLY n 
1 82 LEU n 
1 83 TRP n 
1 84 GLU n 
1 85 ILE n 
1 86 GLN n 
1 87 ASN n 
1 88 ASN n 
1 89 PRO n 
1 90 HIS n 
1 91 ALA n 
1 92 SER n 
1 93 TYR n 
1 94 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   94 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HDGFL2, HDGF2, HDGFRP2, HRP2, UNQ785/PRO1604' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                        ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                       ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                     ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                       ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                 'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE                                      ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                        ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                      ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                          ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                     ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                        ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                         ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                     ?                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                  ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                        ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                         ?                 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'                                  ?                 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE                                      ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                     ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                       ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                         ?                 'C5 H11 N O2'    117.146 
W1A non-polymer         . 'N-[(piperidin-4-yl)methyl]methanesulfonamide' ?                 'C7 H16 N2 O2 S' 192.279 
# 
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 ?  ?   ?   C . n 
C 1 29 ILE 29 28 ?  ?   ?   C . n 
C 1 30 ALA 30 29 ?  ?   ?   C . n 
C 1 31 ASP 31 30 ?  ?   ?   C . n 
C 1 32 GLY 32 31 ?  ?   ?   C . n 
C 1 33 ALA 33 32 ?  ?   ?   C . n 
C 1 34 VAL 34 33 ?  ?   ?   C . n 
C 1 35 LYS 35 34 34 LYS LYS C . n 
C 1 36 PRO 36 35 35 PRO PRO C . n 
C 1 37 PRO 37 36 36 PRO PRO C . n 
C 1 38 PRO 38 37 37 PRO PRO C . n 
C 1 39 ASN 39 38 38 ASN ASN C . n 
C 1 40 LYS 40 39 39 LYS LYS C . n 
C 1 41 TYR 41 40 40 TYR TYR C . n 
C 1 42 PRO 42 41 41 PRO PRO C . n 
C 1 43 ILE 43 42 42 ILE ILE C . n 
C 1 44 PHE 44 43 43 PHE PHE C . n 
C 1 45 PHE 45 44 44 PHE PHE C . n 
C 1 46 PHE 46 45 45 PHE PHE C . n 
C 1 47 GLY 47 46 46 GLY GLY C . n 
C 1 48 THR 48 47 47 THR THR C . n 
C 1 49 HIS 49 48 48 HIS HIS C . n 
C 1 50 GLU 50 49 49 GLU GLU C . n 
C 1 51 THR 51 50 50 THR THR C . n 
C 1 52 ALA 52 51 51 ALA ALA C . n 
C 1 53 PHE 53 52 52 PHE PHE C . n 
C 1 54 LEU 54 53 53 LEU LEU C . n 
C 1 55 GLY 55 54 54 GLY GLY C . n 
C 1 56 PRO 56 55 55 PRO PRO C . n 
C 1 57 LYS 57 56 56 LYS LYS C . n 
C 1 58 ASP 58 57 57 ASP ASP C . n 
C 1 59 LEU 59 58 58 LEU LEU C . n 
C 1 60 PHE 60 59 59 PHE PHE C . n 
C 1 61 PRO 61 60 60 PRO PRO C . n 
C 1 62 TYR 62 61 61 TYR TYR C . n 
C 1 63 ASP 63 62 62 ASP ASP C . n 
C 1 64 LYS 64 63 63 LYS LYS C . n 
C 1 65 SER 65 64 64 SER SER C . n 
C 1 66 LYS 66 65 65 LYS LYS C . n 
C 1 67 ASP 67 66 66 ASP ASP C . n 
C 1 68 LYS 68 67 67 LYS LYS C . n 
C 1 69 TYR 69 68 68 TYR TYR C . n 
C 1 70 GLY 70 69 69 GLY GLY C . n 
C 1 71 LYS 71 70 70 LYS LYS C . n 
C 1 72 PRO 72 71 71 PRO PRO C . n 
C 1 73 ASN 73 72 72 ASN ASN C . n 
C 1 74 LYS 74 73 73 LYS LYS C . n 
C 1 75 ARG 75 74 74 ARG ARG C . n 
C 1 76 LYS 76 75 75 LYS LYS C . n 
C 1 77 GLY 77 76 76 GLY GLY C . n 
C 1 78 PHE 78 77 77 PHE PHE C . n 
C 1 79 ASN 79 78 78 ASN ASN C . n 
C 1 80 GLU 80 79 79 GLU GLU C . n 
C 1 81 GLY 81 80 80 GLY GLY C . n 
C 1 82 LEU 82 81 81 LEU LEU C . n 
C 1 83 TRP 83 82 82 TRP TRP C . n 
C 1 84 GLU 84 83 83 GLU GLU C . n 
C 1 85 ILE 85 84 84 ILE ILE C . n 
C 1 86 GLN 86 85 85 GLN GLN C . n 
C 1 87 ASN 87 86 86 ASN ASN C . n 
C 1 88 ASN 88 87 87 ASN ASN C . n 
C 1 89 PRO 89 88 88 PRO PRO C . n 
C 1 90 HIS 90 89 89 HIS HIS C . n 
C 1 91 ALA 91 90 90 ALA ALA C . n 
C 1 92 SER 92 91 91 SER SER C . n 
C 1 93 TYR 93 92 92 TYR TYR C . n 
C 1 94 SER 94 93 ?  ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        W1A 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   W1A 
_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 W1A 1   103 101 W1A LIG B . 
K 3 EDO 1   101 101 EDO EDO C . 
L 2 SO4 1   102 5   SO4 SO4 C . 
M 5 HOH 1   201 371 HOH HOH A . 
M 5 HOH 2   202 307 HOH HOH A . 
M 5 HOH 3   203 372 HOH HOH A . 
M 5 HOH 4   204 259 HOH HOH A . 
M 5 HOH 5   205 202 HOH HOH A . 
M 5 HOH 6   206 334 HOH HOH A . 
M 5 HOH 7   207 340 HOH HOH A . 
M 5 HOH 8   208 66  HOH HOH A . 
M 5 HOH 9   209 375 HOH HOH A . 
M 5 HOH 10  210 84  HOH HOH A . 
M 5 HOH 11  211 199 HOH HOH A . 
M 5 HOH 12  212 357 HOH HOH A . 
M 5 HOH 13  213 339 HOH HOH A . 
M 5 HOH 14  214 304 HOH HOH A . 
M 5 HOH 15  215 353 HOH HOH A . 
M 5 HOH 16  216 139 HOH HOH A . 
M 5 HOH 17  217 87  HOH HOH A . 
M 5 HOH 18  218 37  HOH HOH A . 
M 5 HOH 19  219 346 HOH HOH A . 
M 5 HOH 20  220 26  HOH HOH A . 
M 5 HOH 21  221 278 HOH HOH A . 
M 5 HOH 22  222 95  HOH HOH A . 
M 5 HOH 23  223 91  HOH HOH A . 
M 5 HOH 24  224 167 HOH HOH A . 
M 5 HOH 25  225 341 HOH HOH A . 
M 5 HOH 26  226 86  HOH HOH A . 
M 5 HOH 27  227 8   HOH HOH A . 
M 5 HOH 28  228 142 HOH HOH A . 
M 5 HOH 29  229 188 HOH HOH A . 
M 5 HOH 30  230 28  HOH HOH A . 
M 5 HOH 31  231 55  HOH HOH A . 
M 5 HOH 32  232 289 HOH HOH A . 
M 5 HOH 33  233 208 HOH HOH A . 
M 5 HOH 34  234 32  HOH HOH A . 
M 5 HOH 35  235 34  HOH HOH A . 
M 5 HOH 36  236 293 HOH HOH A . 
M 5 HOH 37  237 190 HOH HOH A . 
M 5 HOH 38  238 41  HOH HOH A . 
M 5 HOH 39  239 260 HOH HOH A . 
M 5 HOH 40  240 179 HOH HOH A . 
M 5 HOH 41  241 290 HOH HOH A . 
M 5 HOH 42  242 71  HOH HOH A . 
M 5 HOH 43  243 42  HOH HOH A . 
M 5 HOH 44  244 12  HOH HOH A . 
M 5 HOH 45  245 27  HOH HOH A . 
M 5 HOH 46  246 97  HOH HOH A . 
M 5 HOH 47  247 1   HOH HOH A . 
M 5 HOH 48  248 2   HOH HOH A . 
M 5 HOH 49  249 165 HOH HOH A . 
M 5 HOH 50  250 333 HOH HOH A . 
M 5 HOH 51  251 292 HOH HOH A . 
M 5 HOH 52  252 109 HOH HOH A . 
M 5 HOH 53  253 23  HOH HOH A . 
M 5 HOH 54  254 267 HOH HOH A . 
M 5 HOH 55  255 99  HOH HOH A . 
M 5 HOH 56  256 288 HOH HOH A . 
M 5 HOH 57  257 7   HOH HOH A . 
M 5 HOH 58  258 111 HOH HOH A . 
M 5 HOH 59  259 18  HOH HOH A . 
M 5 HOH 60  260 164 HOH HOH A . 
M 5 HOH 61  261 274 HOH HOH A . 
M 5 HOH 62  262 21  HOH HOH A . 
M 5 HOH 63  263 93  HOH HOH A . 
M 5 HOH 64  264 115 HOH HOH A . 
M 5 HOH 65  265 60  HOH HOH A . 
M 5 HOH 66  266 38  HOH HOH A . 
M 5 HOH 67  267 78  HOH HOH A . 
M 5 HOH 68  268 77  HOH HOH A . 
M 5 HOH 69  269 47  HOH HOH A . 
M 5 HOH 70  270 360 HOH HOH A . 
M 5 HOH 71  271 300 HOH HOH A . 
M 5 HOH 72  272 222 HOH HOH A . 
M 5 HOH 73  273 145 HOH HOH A . 
M 5 HOH 74  274 20  HOH HOH A . 
M 5 HOH 75  275 113 HOH HOH A . 
M 5 HOH 76  276 116 HOH HOH A . 
M 5 HOH 77  277 73  HOH HOH A . 
M 5 HOH 78  278 35  HOH HOH A . 
M 5 HOH 79  279 203 HOH HOH A . 
M 5 HOH 80  280 143 HOH HOH A . 
M 5 HOH 81  281 287 HOH HOH A . 
M 5 HOH 82  282 31  HOH HOH A . 
M 5 HOH 83  283 14  HOH HOH A . 
M 5 HOH 84  284 350 HOH HOH A . 
M 5 HOH 85  285 152 HOH HOH A . 
M 5 HOH 86  286 393 HOH HOH A . 
M 5 HOH 87  287 281 HOH HOH A . 
M 5 HOH 88  288 211 HOH HOH A . 
M 5 HOH 89  289 58  HOH HOH A . 
M 5 HOH 90  290 327 HOH HOH A . 
M 5 HOH 91  291 94  HOH HOH A . 
M 5 HOH 92  292 64  HOH HOH A . 
M 5 HOH 93  293 16  HOH HOH A . 
M 5 HOH 94  294 9   HOH HOH A . 
M 5 HOH 95  295 301 HOH HOH A . 
M 5 HOH 96  296 218 HOH HOH A . 
M 5 HOH 97  297 19  HOH HOH A . 
M 5 HOH 98  298 318 HOH HOH A . 
M 5 HOH 99  299 381 HOH HOH A . 
M 5 HOH 100 300 296 HOH HOH A . 
M 5 HOH 101 301 131 HOH HOH A . 
M 5 HOH 102 302 22  HOH HOH A . 
M 5 HOH 103 303 108 HOH HOH A . 
M 5 HOH 104 304 63  HOH HOH A . 
M 5 HOH 105 305 210 HOH HOH A . 
M 5 HOH 106 306 185 HOH HOH A . 
M 5 HOH 107 307 379 HOH HOH A . 
M 5 HOH 108 308 83  HOH HOH A . 
M 5 HOH 109 309 347 HOH HOH A . 
M 5 HOH 110 310 205 HOH HOH A . 
M 5 HOH 111 311 219 HOH HOH A . 
M 5 HOH 112 312 57  HOH HOH A . 
M 5 HOH 113 313 283 HOH HOH A . 
M 5 HOH 114 314 156 HOH HOH A . 
M 5 HOH 115 315 352 HOH HOH A . 
M 5 HOH 116 316 394 HOH HOH A . 
M 5 HOH 117 317 75  HOH HOH A . 
M 5 HOH 118 318 313 HOH HOH A . 
M 5 HOH 119 319 125 HOH HOH A . 
M 5 HOH 120 320 332 HOH HOH A . 
M 5 HOH 121 321 365 HOH HOH A . 
N 5 HOH 1   201 390 HOH HOH B . 
N 5 HOH 2   202 272 HOH HOH B . 
N 5 HOH 3   203 355 HOH HOH B . 
N 5 HOH 4   204 172 HOH HOH B . 
N 5 HOH 5   205 380 HOH HOH B . 
N 5 HOH 6   206 258 HOH HOH B . 
N 5 HOH 7   207 343 HOH HOH B . 
N 5 HOH 8   208 98  HOH HOH B . 
N 5 HOH 9   209 17  HOH HOH B . 
N 5 HOH 10  210 247 HOH HOH B . 
N 5 HOH 11  211 89  HOH HOH B . 
N 5 HOH 12  212 354 HOH HOH B . 
N 5 HOH 13  213 331 HOH HOH B . 
N 5 HOH 14  214 69  HOH HOH B . 
N 5 HOH 15  215 224 HOH HOH B . 
N 5 HOH 16  216 123 HOH HOH B . 
N 5 HOH 17  217 54  HOH HOH B . 
N 5 HOH 18  218 389 HOH HOH B . 
N 5 HOH 19  219 335 HOH HOH B . 
N 5 HOH 20  220 366 HOH HOH B . 
N 5 HOH 21  221 215 HOH HOH B . 
N 5 HOH 22  222 249 HOH HOH B . 
N 5 HOH 23  223 374 HOH HOH B . 
N 5 HOH 24  224 137 HOH HOH B . 
N 5 HOH 25  225 329 HOH HOH B . 
N 5 HOH 26  226 59  HOH HOH B . 
N 5 HOH 27  227 10  HOH HOH B . 
N 5 HOH 28  228 117 HOH HOH B . 
N 5 HOH 29  229 261 HOH HOH B . 
N 5 HOH 30  230 153 HOH HOH B . 
N 5 HOH 31  231 6   HOH HOH B . 
N 5 HOH 32  232 280 HOH HOH B . 
N 5 HOH 33  233 157 HOH HOH B . 
N 5 HOH 34  234 315 HOH HOH B . 
N 5 HOH 35  235 150 HOH HOH B . 
N 5 HOH 36  236 5   HOH HOH B . 
N 5 HOH 37  237 169 HOH HOH B . 
N 5 HOH 38  238 96  HOH HOH B . 
N 5 HOH 39  239 383 HOH HOH B . 
N 5 HOH 40  240 395 HOH HOH B . 
N 5 HOH 41  241 242 HOH HOH B . 
N 5 HOH 42  242 392 HOH HOH B . 
N 5 HOH 43  243 119 HOH HOH B . 
N 5 HOH 44  244 74  HOH HOH B . 
N 5 HOH 45  245 384 HOH HOH B . 
N 5 HOH 46  246 13  HOH HOH B . 
N 5 HOH 47  247 25  HOH HOH B . 
N 5 HOH 48  248 320 HOH HOH B . 
N 5 HOH 49  249 61  HOH HOH B . 
N 5 HOH 50  250 168 HOH HOH B . 
N 5 HOH 51  251 24  HOH HOH B . 
N 5 HOH 52  252 351 HOH HOH B . 
N 5 HOH 53  253 223 HOH HOH B . 
N 5 HOH 54  254 175 HOH HOH B . 
N 5 HOH 55  255 120 HOH HOH B . 
N 5 HOH 56  256 373 HOH HOH B . 
N 5 HOH 57  257 68  HOH HOH B . 
N 5 HOH 58  258 197 HOH HOH B . 
N 5 HOH 59  259 101 HOH HOH B . 
N 5 HOH 60  260 36  HOH HOH B . 
N 5 HOH 61  261 79  HOH HOH B . 
N 5 HOH 62  262 217 HOH HOH B . 
N 5 HOH 63  263 214 HOH HOH B . 
N 5 HOH 64  264 76  HOH HOH B . 
N 5 HOH 65  265 72  HOH HOH B . 
N 5 HOH 66  266 344 HOH HOH B . 
N 5 HOH 67  267 177 HOH HOH B . 
N 5 HOH 68  268 104 HOH HOH B . 
N 5 HOH 69  269 46  HOH HOH B . 
N 5 HOH 70  270 182 HOH HOH B . 
N 5 HOH 71  271 369 HOH HOH B . 
N 5 HOH 72  272 279 HOH HOH B . 
N 5 HOH 73  273 303 HOH HOH B . 
N 5 HOH 74  274 376 HOH HOH B . 
N 5 HOH 75  275 322 HOH HOH B . 
N 5 HOH 76  276 44  HOH HOH B . 
N 5 HOH 77  277 319 HOH HOH B . 
N 5 HOH 78  278 170 HOH HOH B . 
N 5 HOH 79  279 391 HOH HOH B . 
N 5 HOH 80  280 291 HOH HOH B . 
N 5 HOH 81  281 163 HOH HOH B . 
N 5 HOH 82  282 160 HOH HOH B . 
N 5 HOH 83  283 316 HOH HOH B . 
N 5 HOH 84  284 201 HOH HOH B . 
N 5 HOH 85  285 358 HOH HOH B . 
N 5 HOH 86  286 370 HOH HOH B . 
N 5 HOH 87  287 368 HOH HOH B . 
N 5 HOH 88  288 314 HOH HOH B . 
N 5 HOH 89  289 92  HOH HOH B . 
N 5 HOH 90  290 363 HOH HOH B . 
N 5 HOH 91  291 107 HOH HOH B . 
N 5 HOH 92  292 312 HOH HOH B . 
N 5 HOH 93  293 367 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   203 348 HOH HOH C . 
O 5 HOH 4   204 349 HOH HOH C . 
O 5 HOH 5   205 323 HOH HOH C . 
O 5 HOH 6   206 385 HOH HOH C . 
O 5 HOH 7   207 226 HOH HOH C . 
O 5 HOH 8   208 161 HOH HOH C . 
O 5 HOH 9   209 309 HOH HOH C . 
O 5 HOH 10  210 271 HOH HOH C . 
O 5 HOH 11  211 317 HOH HOH C . 
O 5 HOH 12  212 184 HOH HOH C . 
O 5 HOH 13  213 134 HOH HOH C . 
O 5 HOH 14  214 90  HOH HOH C . 
O 5 HOH 15  215 118 HOH HOH C . 
O 5 HOH 16  216 382 HOH HOH C . 
O 5 HOH 17  217 302 HOH HOH C . 
O 5 HOH 18  218 284 HOH HOH C . 
O 5 HOH 19  219 173 HOH HOH C . 
O 5 HOH 20  220 82  HOH HOH C . 
O 5 HOH 21  221 85  HOH HOH C . 
O 5 HOH 22  222 56  HOH HOH C . 
O 5 HOH 23  223 189 HOH HOH C . 
O 5 HOH 24  224 325 HOH HOH C . 
O 5 HOH 25  225 151 HOH HOH C . 
O 5 HOH 26  226 126 HOH HOH C . 
O 5 HOH 27  227 15  HOH HOH C . 
O 5 HOH 28  228 48  HOH HOH C . 
O 5 HOH 29  229 387 HOH HOH C . 
O 5 HOH 30  230 53  HOH HOH C . 
O 5 HOH 31  231 326 HOH HOH C . 
O 5 HOH 32  232 269 HOH HOH C . 
O 5 HOH 33  233 40  HOH HOH C . 
O 5 HOH 34  234 49  HOH HOH C . 
O 5 HOH 35  235 45  HOH HOH C . 
O 5 HOH 36  236 102 HOH HOH C . 
O 5 HOH 37  237 356 HOH HOH C . 
O 5 HOH 38  238 294 HOH HOH C . 
O 5 HOH 39  239 4   HOH HOH C . 
O 5 HOH 40  240 122 HOH HOH C . 
O 5 HOH 41  241 149 HOH HOH C . 
O 5 HOH 42  242 275 HOH HOH C . 
O 5 HOH 43  243 305 HOH HOH C . 
O 5 HOH 44  244 43  HOH HOH C . 
O 5 HOH 45  245 298 HOH HOH C . 
O 5 HOH 46  246 342 HOH HOH C . 
O 5 HOH 47  247 330 HOH HOH C . 
O 5 HOH 48  248 130 HOH HOH C . 
O 5 HOH 49  249 132 HOH HOH C . 
O 5 HOH 50  250 336 HOH HOH C . 
O 5 HOH 51  251 295 HOH HOH C . 
O 5 HOH 52  252 337 HOH HOH C . 
O 5 HOH 53  253 338 HOH HOH C . 
O 5 HOH 54  254 388 HOH HOH C . 
O 5 HOH 55  255 299 HOH HOH C . 
O 5 HOH 56  256 62  HOH HOH C . 
O 5 HOH 57  257 135 HOH HOH C . 
O 5 HOH 58  258 328 HOH HOH C . 
O 5 HOH 59  259 148 HOH HOH C . 
O 5 HOH 60  260 359 HOH HOH C . 
O 5 HOH 61  261 65  HOH HOH C . 
O 5 HOH 62  262 386 HOH HOH C . 
O 5 HOH 63  263 198 HOH HOH C . 
O 5 HOH 64  264 209 HOH HOH C . 
O 5 HOH 65  265 67  HOH HOH C . 
O 5 HOH 66  266 171 HOH HOH C . 
O 5 HOH 67  267 246 HOH HOH C . 
O 5 HOH 68  268 146 HOH HOH C . 
O 5 HOH 69  269 270 HOH HOH C . 
O 5 HOH 70  270 364 HOH HOH C . 
O 5 HOH 71  271 241 HOH HOH C . 
O 5 HOH 72  272 345 HOH HOH C . 
O 5 HOH 73  273 70  HOH HOH C . 
O 5 HOH 74  274 324 HOH HOH C . 
O 5 HOH 75  275 377 HOH HOH C . 
O 5 HOH 76  276 103 HOH HOH C . 
O 5 HOH 77  277 378 HOH HOH C . 
O 5 HOH 78  278 361 HOH HOH C . 
O 5 HOH 79  279 362 HOH HOH C . 
O 5 HOH 80  280 206 HOH HOH C . 
O 5 HOH 81  281 310 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 16 ? CE  ? A LYS 17 CE  
2  1 Y 1 A LYS 16 ? NZ  ? A LYS 17 NZ  
3  1 Y 1 A LYS 70 ? CE  ? A LYS 71 CE  
4  1 Y 1 A LYS 70 ? NZ  ? A LYS 71 NZ  
5  1 Y 1 A LYS 73 ? CD  ? A LYS 74 CD  
6  1 Y 1 A LYS 73 ? CE  ? A LYS 74 CE  
7  1 Y 1 A LYS 73 ? NZ  ? A LYS 74 NZ  
8  1 Y 1 A LYS 75 ? NZ  ? A LYS 76 NZ  
9  1 Y 1 B LYS 16 ? CE  ? B LYS 17 CE  
10 1 Y 1 B LYS 16 ? NZ  ? B LYS 17 NZ  
11 1 Y 1 B ILE 28 ? CG1 ? B ILE 29 CG1 
12 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
13 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
14 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
15 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
16 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
17 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
18 1 Y 1 B LYS 65 ? CE  ? B LYS 66 CE  
19 1 Y 1 B LYS 65 ? NZ  ? B LYS 66 NZ  
20 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
21 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
22 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
23 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
24 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
25 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
26 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
27 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
28 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
29 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
30 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
31 1 Y 1 C HIS 3  ? CG  ? C HIS 4  CG  
32 1 Y 1 C HIS 3  ? ND1 ? C HIS 4  ND1 
33 1 Y 1 C HIS 3  ? CD2 ? C HIS 4  CD2 
34 1 Y 1 C HIS 3  ? CE1 ? C HIS 4  CE1 
35 1 Y 1 C HIS 3  ? NE2 ? C HIS 4  NE2 
36 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
37 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
38 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
39 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
40 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
41 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
42 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
43 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
44 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
45 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
46 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
47 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
48 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
49 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
50 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
51 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
52 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
53 1 Y 1 C LYS 73 ? CG  ? C LYS 74 CG  
54 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
55 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
56 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
57 1 Y 1 C LYS 75 ? CE  ? C LYS 76 CE  
58 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           7HHG 
_cell.length_a           41.600 
_cell.length_b           42.160 
_cell.length_c           158.650 
_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                         7HHG 
_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          7HHG 
_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                     7HHG 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             52.88 
_reflns.d_resolution_high            1.50 
_reflns.number_obs                   45804 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.072 
_reflns.pdbx_netI_over_sigmaI        11.0 
_reflns.pdbx_redundancy              6.1 
_reflns.pdbx_Rrim_I_all              0.079 
_reflns.pdbx_Rpim_I_all              0.031 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     277980 
_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                  1.50 
_reflns_shell.d_res_low                   1.54 
_reflns_shell.number_measured_all         16326 
_reflns_shell.number_unique_obs           3310 
_reflns_shell.Rmerge_I_obs                1.521 
_reflns_shell.pdbx_chi_squared            0.79 
_reflns_shell.pdbx_redundancy             4.9 
_reflns_shell.percent_possible_obs        99.8 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             1.705 
_reflns_shell.pdbx_Rpim_I_all             0.759 
_reflns_shell.pdbx_CC_half                0.382 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HHG 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     43302 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             40.78 
_refine.ls_d_res_high                            1.50 
_refine.ls_percent_reflns_obs                    99.91 
_refine.ls_R_factor_obs                          0.20709 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20537 
_refine.ls_R_factor_R_free                       0.23772 
_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                  2426 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.959 
_refine.B_iso_mean                               35.111 
_refine.aniso_B[1][1]                            0.27 
_refine.aniso_B[2][2]                            0.00 
_refine.aniso_B[3][3]                            -0.28 
_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                       0.086 
_refine.pdbx_overall_ESU_R_Free                  0.087 
_refine.overall_SU_ML                            0.076 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.178 
_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        2121 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         50 
_refine_hist.number_atoms_solvent             295 
_refine_hist.number_atoms_total               2466 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        40.78 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.010  0.012  ? 2273 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.922  1.834  ? 3094 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.859  5.000  ? 264  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       3.668  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.317 10.000 ? 297  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.132  0.200  ? 286  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.011  0.020  ? 1858 '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                  3.178  3.238  ? 1065 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.273  5.796  ? 1329 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.355  3.527  ? 1208 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       8.465  48.51  ? 3585 '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                       1.500 
_refine_ls_shell.d_res_low                        1.539 
_refine_ls_shell.number_reflns_R_work             3132 
_refine_ls_shell.R_factor_R_work                  0.329 
_refine_ls_shell.percent_reflns_obs               99.64 
_refine_ls_shell.R_factor_R_free                  0.370 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             173 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HHG 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z1741966151' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HHG 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 3 ? 
L N N 2 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HHG A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HHG B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HHG 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 7HHG GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HHG SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HHG GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HHG SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HHG GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HHG 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                   7HHG 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   B HOH 232 ? ? O B HOH 275 ? ? 1.59 
2  1 O   A HOH 219 ? ? O A HOH 267 ? ? 1.77 
3  1 CE  A LYS 39  ? ? O A HOH 284 ? ? 1.95 
4  1 NE  A ARG 74  ? ? O A HOH 201 ? ? 2.00 
5  1 O2  A SO4 104 ? ? O A HOH 202 ? ? 2.01 
6  1 O2  C SO4 102 ? ? O C HOH 201 ? ? 2.01 
7  1 O   A HOH 212 ? ? O A HOH 275 ? ? 2.06 
8  1 O2  C SO4 102 ? ? O C HOH 202 ? ? 2.07 
9  1 N   C PHE 5   ? ? O C HOH 203 ? ? 2.09 
10 1 NE2 C HIS 89  ? ? O C HOH 204 ? ? 2.15 
11 1 OD1 C ASP 9   ? ? O C HOH 205 ? ? 2.18 
12 1 O   A HOH 316 ? ? O A HOH 320 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O B HOH 242 ? ? 1_555 O B HOH 244 ? ? 3_654 2.10 
2 1 O A HOH 263 ? ? 1_555 O C HOH 252 ? ? 4_435 2.15 
3 1 O A HOH 251 ? ? 1_555 O A HOH 272 ? ? 4_545 2.16 
# 
_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             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              24 
_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             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              24 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NH2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              24 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                116.10 
_pdbx_validate_rmsd_angle.angle_target_value         120.30 
_pdbx_validate_rmsd_angle.angle_deviation            -4.20 
_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 ? ? -156.34 65.58 
2 1 ASN B 38 ? ? 76.16   -2.32 
3 1 ASN B 87 ? ? -158.11 60.17 
4 1 ASN C 87 ? ? -160.38 50.80 
# 
loop_
_pdbx_validate_peptide_omega.id 
_pdbx_validate_peptide_omega.PDB_model_num 
_pdbx_validate_peptide_omega.auth_comp_id_1 
_pdbx_validate_peptide_omega.auth_asym_id_1 
_pdbx_validate_peptide_omega.auth_seq_id_1 
_pdbx_validate_peptide_omega.PDB_ins_code_1 
_pdbx_validate_peptide_omega.label_alt_id_1 
_pdbx_validate_peptide_omega.auth_comp_id_2 
_pdbx_validate_peptide_omega.auth_asym_id_2 
_pdbx_validate_peptide_omega.auth_seq_id_2 
_pdbx_validate_peptide_omega.PDB_ins_code_2 
_pdbx_validate_peptide_omega.label_alt_id_2 
_pdbx_validate_peptide_omega.omega 
1 1 VAL A 11 ? ? PHE A 12 ? ? 149.28 
2 1 VAL B 11 ? ? PHE B 12 ? ? 148.79 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 320 ? 5.87 .    
2 1 O ? A HOH 321 ? .    7.10 
# 
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 ASP 27 ? C ASP 28 
11 1 Y 1 C ILE 28 ? C ILE 29 
12 1 Y 1 C ALA 29 ? C ALA 30 
13 1 Y 1 C ASP 30 ? C ASP 31 
14 1 Y 1 C GLY 31 ? C GLY 32 
15 1 Y 1 C ALA 32 ? C ALA 33 
16 1 Y 1 C VAL 33 ? C VAL 34 
17 1 Y 1 C SER 93 ? C SER 94 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
PHE N    N N N 260 
PHE CA   C N S 261 
PHE C    C N N 262 
PHE O    O N N 263 
PHE CB   C N N 264 
PHE CG   C Y N 265 
PHE CD1  C Y N 266 
PHE CD2  C Y N 267 
PHE CE1  C Y N 268 
PHE CE2  C Y N 269 
PHE CZ   C Y N 270 
PHE OXT  O N N 271 
PHE H    H N N 272 
PHE H2   H N N 273 
PHE HA   H N N 274 
PHE HB2  H N N 275 
PHE HB3  H N N 276 
PHE HD1  H N N 277 
PHE HD2  H N N 278 
PHE HE1  H N N 279 
PHE HE2  H N N 280 
PHE HZ   H N N 281 
PHE HXT  H N N 282 
PRO N    N N N 283 
PRO CA   C N S 284 
PRO C    C N N 285 
PRO O    O N N 286 
PRO CB   C N N 287 
PRO CG   C N N 288 
PRO CD   C N N 289 
PRO OXT  O N N 290 
PRO H    H N N 291 
PRO HA   H N N 292 
PRO HB2  H N N 293 
PRO HB3  H N N 294 
PRO HG2  H N N 295 
PRO HG3  H N N 296 
PRO HD2  H N N 297 
PRO HD3  H N N 298 
PRO HXT  H N N 299 
SER N    N N N 300 
SER CA   C N S 301 
SER C    C N N 302 
SER O    O N N 303 
SER CB   C N N 304 
SER OG   O N N 305 
SER OXT  O N N 306 
SER H    H N N 307 
SER H2   H N N 308 
SER HA   H N N 309 
SER HB2  H N N 310 
SER HB3  H N N 311 
SER HG   H N N 312 
SER HXT  H N N 313 
SO4 S    S N N 314 
SO4 O1   O N N 315 
SO4 O2   O N N 316 
SO4 O3   O N N 317 
SO4 O4   O N N 318 
THR N    N N N 319 
THR CA   C N S 320 
THR C    C N N 321 
THR O    O N N 322 
THR CB   C N R 323 
THR OG1  O N N 324 
THR CG2  C N N 325 
THR OXT  O N N 326 
THR H    H N N 327 
THR H2   H N N 328 
THR HA   H N N 329 
THR HB   H N N 330 
THR HG1  H N N 331 
THR HG21 H N N 332 
THR HG22 H N N 333 
THR HG23 H N N 334 
THR HXT  H N N 335 
TRP N    N N N 336 
TRP CA   C N S 337 
TRP C    C N N 338 
TRP O    O N N 339 
TRP CB   C N N 340 
TRP CG   C Y N 341 
TRP CD1  C Y N 342 
TRP CD2  C Y N 343 
TRP NE1  N Y N 344 
TRP CE2  C Y N 345 
TRP CE3  C Y N 346 
TRP CZ2  C Y N 347 
TRP CZ3  C Y N 348 
TRP CH2  C Y N 349 
TRP OXT  O N N 350 
TRP H    H N N 351 
TRP H2   H N N 352 
TRP HA   H N N 353 
TRP HB2  H N N 354 
TRP HB3  H N N 355 
TRP HD1  H N N 356 
TRP HE1  H N N 357 
TRP HE3  H N N 358 
TRP HZ2  H N N 359 
TRP HZ3  H N N 360 
TRP HH2  H N N 361 
TRP HXT  H N N 362 
TYR N    N N N 363 
TYR CA   C N S 364 
TYR C    C N N 365 
TYR O    O N N 366 
TYR CB   C N N 367 
TYR CG   C Y N 368 
TYR CD1  C Y N 369 
TYR CD2  C Y N 370 
TYR CE1  C Y N 371 
TYR CE2  C Y N 372 
TYR CZ   C Y N 373 
TYR OH   O N N 374 
TYR OXT  O N N 375 
TYR H    H N N 376 
TYR H2   H N N 377 
TYR HA   H N N 378 
TYR HB2  H N N 379 
TYR HB3  H N N 380 
TYR HD1  H N N 381 
TYR HD2  H N N 382 
TYR HE1  H N N 383 
TYR HE2  H N N 384 
TYR HH   H N N 385 
TYR HXT  H N N 386 
VAL N    N N N 387 
VAL CA   C N S 388 
VAL C    C N N 389 
VAL O    O N N 390 
VAL CB   C N N 391 
VAL CG1  C N N 392 
VAL CG2  C N N 393 
VAL OXT  O N N 394 
VAL H    H N N 395 
VAL H2   H N N 396 
VAL HA   H N N 397 
VAL HB   H N N 398 
VAL HG11 H N N 399 
VAL HG12 H N N 400 
VAL HG13 H N N 401 
VAL HG21 H N N 402 
VAL HG22 H N N 403 
VAL HG23 H N N 404 
VAL HXT  H N N 405 
W1A N1   N N N 406 
W1A C4   C N N 407 
W1A C5   C N N 408 
W1A C6   C N N 409 
W1A O1   O N N 410 
W1A S    S N N 411 
W1A O    O N N 412 
W1A C    C N N 413 
W1A N    N N N 414 
W1A C1   C N N 415 
W1A C2   C N N 416 
W1A C3   C N N 417 
W1A H1   H N N 418 
W1A H3   H N N 419 
W1A H4   H N N 420 
W1A H5   H N N 421 
W1A H6   H N N 422 
W1A H7   H N N 423 
W1A H8   H N N 424 
W1A H9   H N N 425 
W1A H10  H N N 426 
W1A H11  H N N 427 
W1A H12  H N N 428 
W1A H13  H N N 429 
W1A H14  H N N 430 
W1A H15  H N N 431 
W1A H16  H N N 432 
W1A H17  H N N 433 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
SO4 S   O1   doub N N 299 
SO4 S   O2   doub N N 300 
SO4 S   O3   sing N N 301 
SO4 S   O4   sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
W1A O1  S    doub N N 389 
W1A S   O    doub N N 390 
W1A S   C    sing N N 391 
W1A S   N    sing N N 392 
W1A N   C1   sing N N 393 
W1A C1  C2   sing N N 394 
W1A C4  N1   sing N N 395 
W1A C4  C3   sing N N 396 
W1A C5  N1   sing N N 397 
W1A C5  C6   sing N N 398 
W1A C2  C6   sing N N 399 
W1A C2  C3   sing N N 400 
W1A N1  H1   sing N N 401 
W1A C4  H3   sing N N 402 
W1A C4  H4   sing N N 403 
W1A C5  H5   sing N N 404 
W1A C5  H6   sing N N 405 
W1A C6  H7   sing N N 406 
W1A C6  H8   sing N N 407 
W1A C   H9   sing N N 408 
W1A C   H10  sing N N 409 
W1A C   H11  sing N N 410 
W1A N   H12  sing N N 411 
W1A C1  H13  sing N N 412 
W1A C1  H14  sing N N 413 
W1A C2  H15  sing N N 414 
W1A C3  H16  sing N N 415 
W1A C3  H17  sing N N 416 
# 
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                    7HHG 
_atom_sites.fract_transf_matrix[1][1]   0.024038 
_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]   0.023719 
_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]   0.006303 
_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  ? 0.789   4.284   2.374   1.00 44.75 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 2  ? -0.275  3.487   1.711   1.00 48.89 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 2  ? 0.324   2.402   0.810   1.00 47.12 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 2  ? 1.454   2.522   0.327   1.00 41.61 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 2  ? -1.255  4.393   0.960   1.00 57.44 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 2  ? -2.220  5.141   1.876   1.00 61.57 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 2  ? -3.525  4.211   2.720   1.00 59.85 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 2  ? -4.360  5.509   3.651   1.00 65.32 ? 1   MET A CE  1 
ATOM   9    N N   . PRO A 1 3  ? -0.404  1.274   0.611   1.00 40.40 ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 3  ? 0.016   0.182   -0.278  1.00 38.17 ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 3  ? 0.233   0.560   -1.743  1.00 34.71 ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 3  ? -0.463  1.402   -2.306  1.00 36.16 ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 3  ? -1.211  -0.801  -0.116  1.00 38.34 ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 3  ? -1.657  -0.557  1.320   1.00 42.81 ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 3  ? -1.664  0.957   1.315   1.00 40.25 ? 2   PRO A CD  1 
ATOM   16   N N   . HIS A 1 4  ? 1.218   -0.101  -2.358  1.00 33.27 ? 3   HIS A N   1 
ATOM   17   C CA  . HIS A 1 4  ? 1.429   0.005   -3.784  1.00 33.75 ? 3   HIS A CA  1 
ATOM   18   C C   . HIS A 1 4  ? 0.890   -1.286  -4.384  1.00 30.60 ? 3   HIS A C   1 
ATOM   19   O O   . HIS A 1 4  ? 0.440   -2.176  -3.655  1.00 29.43 ? 3   HIS A O   1 
ATOM   20   C CB  . HIS A 1 4  ? 2.935   0.132   -4.066  1.00 38.77 ? 3   HIS A CB  1 
ATOM   21   C CG  . HIS A 1 4  ? 3.533   1.423   -3.591  1.00 50.86 ? 3   HIS A CG  1 
ATOM   22   N ND1 . HIS A 1 4  ? 3.685   1.761   -2.261  1.00 59.82 ? 3   HIS A ND1 1 
ATOM   23   C CD2 . HIS A 1 4  ? 4.020   2.465   -4.282  1.00 59.41 ? 3   HIS A CD2 1 
ATOM   24   C CE1 . HIS A 1 4  ? 4.235   2.966   -2.163  1.00 62.99 ? 3   HIS A CE1 1 
ATOM   25   N NE2 . HIS A 1 4  ? 4.459   3.410   -3.379  1.00 57.54 ? 3   HIS A NE2 1 
ATOM   26   N N   . ALA A 1 5  ? 0.909   -1.392  -5.706  1.00 27.02 ? 4   ALA A N   1 
ATOM   27   C CA  . ALA A 1 5  ? 0.681   -2.694  -6.301  1.00 25.76 ? 4   ALA A CA  1 
ATOM   28   C C   . ALA A 1 5  ? 1.837   -3.637  -5.951  1.00 25.72 ? 4   ALA A C   1 
ATOM   29   O O   . ALA A 1 5  ? 2.938   -3.211  -5.547  1.00 28.23 ? 4   ALA A O   1 
ATOM   30   C CB  . ALA A 1 5  ? 0.568   -2.534  -7.804  1.00 29.68 ? 4   ALA A CB  1 
ATOM   31   N N   . PHE A 1 6  ? 1.541   -4.931  -6.064  1.00 24.23 ? 5   PHE A N   1 
ATOM   32   C CA  . PHE A 1 6  ? 2.523   -5.989  -5.899  1.00 23.52 ? 5   PHE A CA  1 
ATOM   33   C C   . PHE A 1 6  ? 3.649   -5.799  -6.917  1.00 25.04 ? 5   PHE A C   1 
ATOM   34   O O   . PHE A 1 6  ? 3.421   -5.410  -8.063  1.00 26.85 ? 5   PHE A O   1 
ATOM   35   C CB  . PHE A 1 6  ? 1.973   -7.418  -5.990  1.00 24.40 ? 5   PHE A CB  1 
ATOM   36   C CG  . PHE A 1 6  ? 1.214   -7.752  -4.712  1.00 25.80 ? 5   PHE A CG  1 
ATOM   37   C CD1 . PHE A 1 6  ? 1.878   -7.950  -3.504  1.00 23.25 ? 5   PHE A CD1 1 
ATOM   38   C CD2 . PHE A 1 6  ? -0.184  -7.930  -4.764  1.00 23.56 ? 5   PHE A CD2 1 
ATOM   39   C CE1 . PHE A 1 6  ? 1.207   -8.272  -2.325  1.00 22.64 ? 5   PHE A CE1 1 
ATOM   40   C CE2 . PHE A 1 6  ? -0.838  -8.281  -3.577  1.00 22.50 ? 5   PHE A CE2 1 
ATOM   41   C CZ  . PHE A 1 6  ? -0.183  -8.403  -2.373  1.00 24.07 ? 5   PHE A CZ  1 
ATOM   42   N N   . LYS A 1 7  ? 4.891   -6.022  -6.449  1.00 23.03 ? 6   LYS A N   1 
ATOM   43   C CA  . LYS A 1 7  ? 6.070   -5.974  -7.317  1.00 24.87 ? 6   LYS A CA  1 
ATOM   44   C C   . LYS A 1 7  ? 6.956   -7.192  -7.035  1.00 23.51 ? 6   LYS A C   1 
ATOM   45   O O   . LYS A 1 7  ? 6.941   -7.767  -5.951  1.00 21.39 ? 6   LYS A O   1 
ATOM   46   C CB  . LYS A 1 7  ? 6.873   -4.685  -7.087  1.00 25.66 ? 6   LYS A CB  1 
ATOM   47   C CG  . LYS A 1 7  ? 7.332   -4.552  -5.660  1.00 27.58 ? 6   LYS A CG  1 
ATOM   48   C CD  . LYS A 1 7  ? 8.044   -3.220  -5.346  1.00 35.47 ? 6   LYS A CD  1 
ATOM   49   C CE  . LYS A 1 7  ? 8.691   -3.205  -3.982  1.00 36.31 ? 6   LYS A CE  1 
ATOM   50   N NZ  . LYS A 1 7  ? 7.675   -3.275  -2.928  1.00 34.06 ? 6   LYS A NZ  1 
ATOM   51   N N   . PRO A 1 8  ? 7.862   -7.578  -7.955  1.00 23.26 ? 7   PRO A N   1 
ATOM   52   C CA  . PRO A 1 8  ? 8.800   -8.669  -7.689  1.00 23.56 ? 7   PRO A CA  1 
ATOM   53   C C   . PRO A 1 8  ? 9.587   -8.399  -6.404  1.00 21.32 ? 7   PRO A C   1 
ATOM   54   O O   . PRO A 1 8  ? 10.041  -7.282  -6.134  1.00 23.05 ? 7   PRO A O   1 
ATOM   55   C CB  . PRO A 1 8  ? 9.697   -8.702  -8.953  1.00 24.88 ? 7   PRO A CB  1 
ATOM   56   C CG  . PRO A 1 8  ? 8.839   -8.053  -10.021 1.00 26.32 ? 7   PRO A CG  1 
ATOM   57   C CD  . PRO A 1 8  ? 8.011   -6.983  -9.308  1.00 24.87 ? 7   PRO A CD  1 
ATOM   58   N N   . GLY A 1 9  ? 9.758   -9.459  -5.606  1.00 20.61 ? 8   GLY A N   1 
ATOM   59   C CA  . GLY A 1 9  ? 10.486  -9.360  -4.357  1.00 20.56 ? 8   GLY A CA  1 
ATOM   60   C C   . GLY A 1 9  ? 9.541   -9.242  -3.166  1.00 22.03 ? 8   GLY A C   1 
ATOM   61   O O   . GLY A 1 9  ? 9.928   -9.532  -2.031  1.00 21.63 ? 8   GLY A O   1 
ATOM   62   N N   . ASP A 1 10 ? 8.285   -8.782  -3.385  1.00 19.12 ? 9   ASP A N   1 
ATOM   63   C CA  . ASP A 1 10 ? 7.379   -8.763  -2.247  1.00 19.25 ? 9   ASP A CA  1 
ATOM   64   C C   . ASP A 1 10 ? 7.107   -10.156 -1.648  1.00 16.92 ? 9   ASP A C   1 
ATOM   65   O O   . ASP A 1 10 ? 6.969   -11.134 -2.368  1.00 19.05 ? 9   ASP A O   1 
ATOM   66   C CB  . ASP A 1 10 ? 6.042   -8.173  -2.680  1.00 18.83 ? 9   ASP A CB  1 
ATOM   67   C CG  . ASP A 1 10 ? 6.060   -6.679  -2.911  1.00 22.79 ? 9   ASP A CG  1 
ATOM   68   O OD1 . ASP A 1 10 ? 7.012   -5.997  -2.449  1.00 22.95 ? 9   ASP A OD1 1 
ATOM   69   O OD2 . ASP A 1 10 ? 5.070   -6.162  -3.506  1.00 23.49 ? 9   ASP A OD2 1 
ATOM   70   N N   . LEU A 1 11 ? 7.001   -10.186 -0.310  1.00 18.14 ? 10  LEU A N   1 
ATOM   71   C CA  . LEU A 1 11 ? 6.844   -11.436 0.441   1.00 19.00 ? 10  LEU A CA  1 
ATOM   72   C C   . LEU A 1 11 ? 5.362   -11.526 0.833   1.00 17.99 ? 10  LEU A C   1 
ATOM   73   O O   . LEU A 1 11 ? 4.777   -10.489 1.253   1.00 20.66 ? 10  LEU A O   1 
ATOM   74   C CB  . LEU A 1 11 ? 7.799   -11.496 1.659   1.00 18.96 ? 10  LEU A CB  1 
ATOM   75   C CG  . LEU A 1 11 ? 9.288   -11.278 1.323   1.00 19.78 ? 10  LEU A CG  1 
ATOM   76   C CD1 . LEU A 1 11 ? 10.151  -11.367 2.591   1.00 20.98 ? 10  LEU A CD1 1 
ATOM   77   C CD2 . LEU A 1 11 ? 9.674   -12.311 0.299   1.00 20.14 ? 10  LEU A CD2 1 
ATOM   78   N N   . VAL A 1 12 ? 4.805   -12.732 0.698   1.00 16.88 ? 11  VAL A N   1 
ATOM   79   C CA  . VAL A 1 12 ? 3.367   -12.938 0.935   1.00 18.27 ? 11  VAL A CA  1 
ATOM   80   C C   . VAL A 1 12 ? 3.147   -14.302 1.578   1.00 19.19 ? 11  VAL A C   1 
ATOM   81   O O   . VAL A 1 12 ? 3.997   -15.190 1.611   1.00 19.11 ? 11  VAL A O   1 
ATOM   82   C CB  . VAL A 1 12 ? 2.567   -12.842 -0.370  1.00 18.38 ? 11  VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 12 ? 2.719   -11.450 -0.985  1.00 20.91 ? 11  VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 12 ? 2.946   -13.946 -1.343  1.00 19.89 ? 11  VAL A CG2 1 
ATOM   85   N N   . PHE A 1 13 ? 1.897   -14.518 2.069   1.00 18.58 ? 12  PHE A N   1 
ATOM   86   C CA  . PHE A 1 13 ? 1.331   -15.853 2.090   1.00 20.73 ? 12  PHE A CA  1 
ATOM   87   C C   . PHE A 1 13 ? 0.381   -15.911 0.904   1.00 21.37 ? 12  PHE A C   1 
ATOM   88   O O   . PHE A 1 13 ? -0.411  -14.964 0.727   1.00 20.99 ? 12  PHE A O   1 
ATOM   89   C CB  . PHE A 1 13 ? 0.595   -16.184 3.406   1.00 20.83 ? 12  PHE A CB  1 
ATOM   90   C CG  . PHE A 1 13 ? 1.549   -16.252 4.587   1.00 20.64 ? 12  PHE A CG  1 
ATOM   91   C CD1 . PHE A 1 13 ? 1.865   -15.080 5.269   1.00 22.64 ? 12  PHE A CD1 1 
ATOM   92   C CD2 . PHE A 1 13 ? 2.072   -17.479 4.998   1.00 23.93 ? 12  PHE A CD2 1 
ATOM   93   C CE1 . PHE A 1 13 ? 2.761   -15.130 6.338   1.00 27.21 ? 12  PHE A CE1 1 
ATOM   94   C CE2 . PHE A 1 13 ? 2.991   -17.521 6.061   1.00 23.50 ? 12  PHE A CE2 1 
ATOM   95   C CZ  . PHE A 1 13 ? 3.318   -16.350 6.705   1.00 25.98 ? 12  PHE A CZ  1 
ATOM   96   N N   . ALA A 1 14 ? 0.496   -17.009 0.129   1.00 20.14 ? 13  ALA A N   1 
ATOM   97   C CA  . ALA A 1 14 ? -0.292  -17.143 -1.094  1.00 21.17 ? 13  ALA A CA  1 
ATOM   98   C C   . ALA A 1 14 ? -1.296  -18.281 -0.900  1.00 21.95 ? 13  ALA A C   1 
ATOM   99   O O   . ALA A 1 14 ? -0.949  -19.340 -0.376  1.00 22.63 ? 13  ALA A O   1 
ATOM   100  C CB  . ALA A 1 14 ? 0.594   -17.390 -2.311  1.00 20.99 ? 13  ALA A CB  1 
ATOM   101  N N   . LYS A 1 15 ? -2.581  -18.056 -1.275  1.00 21.29 ? 14  LYS A N   1 
ATOM   102  C CA  . LYS A 1 15 ? -3.587  -19.089 -1.038  1.00 23.81 ? 14  LYS A CA  1 
ATOM   103  C C   . LYS A 1 15 ? -3.970  -19.803 -2.335  1.00 25.08 ? 14  LYS A C   1 
ATOM   104  O O   . LYS A 1 15 ? -4.338  -19.151 -3.295  1.00 26.48 ? 14  LYS A O   1 
ATOM   105  C CB  . LYS A 1 15 ? -4.813  -18.422 -0.398  1.00 24.24 ? 14  LYS A CB  1 
ATOM   106  C CG  . LYS A 1 15 ? -5.903  -19.501 -0.020  1.00 28.10 ? 14  LYS A CG  1 
ATOM   107  C CD  . LYS A 1 15 ? -5.432  -20.339 1.183   1.00 29.58 ? 14  LYS A CD  1 
ATOM   108  C CE  . LYS A 1 15 ? -6.535  -21.222 1.769   1.00 32.49 ? 14  LYS A CE  1 
ATOM   109  N NZ  . LYS A 1 15 ? -6.968  -22.253 0.812   1.00 33.90 ? 14  LYS A NZ  1 
ATOM   110  N N   . MET A 1 16 ? -3.898  -21.146 -2.285  1.00 26.10 ? 15  MET A N   1 
ATOM   111  C CA  . MET A 1 16 ? -4.286  -22.070 -3.339  1.00 30.44 ? 15  MET A CA  1 
ATOM   112  C C   . MET A 1 16 ? -5.400  -22.936 -2.751  1.00 31.75 ? 15  MET A C   1 
ATOM   113  O O   . MET A 1 16 ? -5.364  -23.259 -1.573  1.00 25.90 ? 15  MET A O   1 
ATOM   114  C CB  . MET A 1 16 ? -3.091  -22.999 -3.604  1.00 29.90 ? 15  MET A CB  1 
ATOM   115  C CG  . MET A 1 16 ? -1.840  -22.239 -4.068  1.00 29.36 ? 15  MET A CG  1 
ATOM   116  S SD  . MET A 1 16 ? -1.993  -21.740 -5.791  1.00 34.93 ? 15  MET A SD  1 
ATOM   117  C CE  . MET A 1 16 ? -1.575  -23.288 -6.502  1.00 27.47 ? 15  MET A CE  1 
ATOM   118  N N   . LYS A 1 17 ? -6.381  -23.286 -3.580  1.00 36.87 ? 16  LYS A N   1 
ATOM   119  C CA  . LYS A 1 17 ? -7.481  -24.143 -3.151  1.00 39.07 ? 16  LYS A CA  1 
ATOM   120  C C   . LYS A 1 17 ? -6.906  -25.423 -2.562  1.00 33.15 ? 16  LYS A C   1 
ATOM   121  O O   . LYS A 1 17 ? -5.966  -26.009 -3.108  1.00 34.72 ? 16  LYS A O   1 
ATOM   122  C CB  . LYS A 1 17 ? -8.242  -24.520 -4.427  1.00 44.41 ? 16  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 17 ? -9.475  -25.389 -4.225  1.00 50.60 ? 16  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 17 ? -10.673 -24.555 -3.775  1.00 61.88 ? 16  LYS A CD  1 
ATOM   125  N N   . GLY A 1 18 ? -7.417  -25.824 -1.382  1.00 35.47 ? 17  GLY A N   1 
ATOM   126  C CA  . GLY A 1 18 ? -6.975  -27.083 -0.810  1.00 34.65 ? 17  GLY A CA  1 
ATOM   127  C C   . GLY A 1 18 ? -5.624  -27.001 -0.106  1.00 39.57 ? 17  GLY A C   1 
ATOM   128  O O   . GLY A 1 18 ? -5.126  -27.992 0.396   1.00 40.85 ? 17  GLY A O   1 
ATOM   129  N N   . TYR A 1 19 ? -5.009  -25.812 -0.059  1.00 32.46 ? 18  TYR A N   1 
ATOM   130  C CA  . TYR A 1 19 ? -3.763  -25.718 0.662   1.00 31.45 ? 18  TYR A CA  1 
ATOM   131  C C   . TYR A 1 19 ? -3.856  -24.587 1.667   1.00 27.70 ? 18  TYR A C   1 
ATOM   132  O O   . TYR A 1 19 ? -4.576  -23.619 1.454   1.00 29.05 ? 18  TYR A O   1 
ATOM   133  C CB  . TYR A 1 19 ? -2.627  -25.306 -0.281  1.00 33.12 ? 18  TYR A CB  1 
ATOM   134  C CG  . TYR A 1 19 ? -2.111  -26.366 -1.244  1.00 36.58 ? 18  TYR A CG  1 
ATOM   135  C CD1 . TYR A 1 19 ? -0.967  -27.087 -0.924  1.00 47.91 ? 18  TYR A CD1 1 
ATOM   136  C CD2 . TYR A 1 19 ? -2.702  -26.569 -2.487  1.00 39.96 ? 18  TYR A CD2 1 
ATOM   137  C CE1 . TYR A 1 19 ? -0.443  -28.024 -1.799  1.00 48.18 ? 18  TYR A CE1 1 
ATOM   138  C CE2 . TYR A 1 19 ? -2.174  -27.493 -3.387  1.00 44.38 ? 18  TYR A CE2 1 
ATOM   139  C CZ  . TYR A 1 19 ? -1.039  -28.215 -3.031  1.00 47.20 ? 18  TYR A CZ  1 
ATOM   140  O OH  . TYR A 1 19 ? -0.465  -29.158 -3.843  1.00 62.96 ? 18  TYR A OH  1 
ATOM   141  N N   . PRO A 1 20 ? -3.079  -24.654 2.760   1.00 28.40 ? 19  PRO A N   1 
ATOM   142  C CA  . PRO A 1 20 ? -3.036  -23.566 3.742   1.00 28.17 ? 19  PRO A CA  1 
ATOM   143  C C   . PRO A 1 20 ? -2.325  -22.381 3.062   1.00 26.36 ? 19  PRO A C   1 
ATOM   144  O O   . PRO A 1 20 ? -1.571  -22.587 2.123   1.00 26.71 ? 19  PRO A O   1 
ATOM   145  C CB  . PRO A 1 20 ? -2.219  -24.192 4.894   1.00 32.43 ? 19  PRO A CB  1 
ATOM   146  C CG  . PRO A 1 20 ? -1.352  -25.248 4.205   1.00 31.62 ? 19  PRO A CG  1 
ATOM   147  C CD  . PRO A 1 20 ? -2.165  -25.782 3.056   1.00 32.33 ? 19  PRO A CD  1 
ATOM   148  N N   . HIS A 1 21 ? -2.581  -21.195 3.581   1.00 24.87 ? 20  HIS A N   1 
ATOM   149  C CA  . HIS A 1 21 ? -1.903  -19.968 3.159   1.00 21.43 ? 20  HIS A CA  1 
ATOM   150  C C   . HIS A 1 21 ? -0.402  -20.222 3.289   1.00 24.11 ? 20  HIS A C   1 
ATOM   151  O O   . HIS A 1 21 ? 0.048   -20.675 4.335   1.00 24.40 ? 20  HIS A O   1 
ATOM   152  C CB  . HIS A 1 21 ? -2.332  -18.800 4.037   1.00 21.99 ? 20  HIS A CB  1 
ATOM   153  C CG  . HIS A 1 21 ? -3.787  -18.425 3.893   1.00 22.80 ? 20  HIS A CG  1 
ATOM   154  N ND1 . HIS A 1 21 ? -4.816  -19.066 4.563   1.00 28.05 ? 20  HIS A ND1 1 
ATOM   155  C CD2 . HIS A 1 21 ? -4.345  -17.403 3.160   1.00 22.86 ? 20  HIS A CD2 1 
ATOM   156  C CE1 . HIS A 1 21 ? -5.973  -18.486 4.206   1.00 27.46 ? 20  HIS A CE1 1 
ATOM   157  N NE2 . HIS A 1 21 ? -5.743  -17.478 3.374   1.00 26.96 ? 20  HIS A NE2 1 
ATOM   158  N N   . TRP A 1 22 ? 0.341   -19.998 2.181   1.00 22.13 ? 21  TRP A N   1 
ATOM   159  C CA  . TRP A 1 22 ? 1.655   -20.630 2.041   1.00 20.88 ? 21  TRP A CA  1 
ATOM   160  C C   . TRP A 1 22 ? 2.713   -19.539 1.921   1.00 22.52 ? 21  TRP A C   1 
ATOM   161  O O   . TRP A 1 22 ? 2.563   -18.659 1.096   1.00 21.79 ? 21  TRP A O   1 
ATOM   162  C CB  . TRP A 1 22 ? 1.687   -21.495 0.784   1.00 20.97 ? 21  TRP A CB  1 
ATOM   163  C CG  . TRP A 1 22 ? 2.791   -22.532 0.861   1.00 23.74 ? 21  TRP A CG  1 
ATOM   164  C CD1 . TRP A 1 22 ? 4.150   -22.368 0.697   1.00 24.74 ? 21  TRP A CD1 1 
ATOM   165  C CD2 . TRP A 1 22 ? 2.575   -23.927 1.154   1.00 25.91 ? 21  TRP A CD2 1 
ATOM   166  N NE1 . TRP A 1 22 ? 4.763   -23.601 0.806   1.00 23.98 ? 21  TRP A NE1 1 
ATOM   167  C CE2 . TRP A 1 22 ? 3.835   -24.564 1.125   1.00 27.25 ? 21  TRP A CE2 1 
ATOM   168  C CE3 . TRP A 1 22 ? 1.446   -24.710 1.431   1.00 28.10 ? 21  TRP A CE3 1 
ATOM   169  C CZ2 . TRP A 1 22 ? 4.010   -25.927 1.371   1.00 30.11 ? 21  TRP A CZ2 1 
ATOM   170  C CZ3 . TRP A 1 22 ? 1.633   -26.056 1.705   1.00 29.70 ? 21  TRP A CZ3 1 
ATOM   171  C CH2 . TRP A 1 22 ? 2.888   -26.665 1.670   1.00 32.66 ? 21  TRP A CH2 1 
ATOM   172  N N   . PRO A 1 23 ? 3.858   -19.621 2.635   1.00 21.08 ? 22  PRO A N   1 
ATOM   173  C CA  . PRO A 1 23 ? 4.899   -18.587 2.453   1.00 19.35 ? 22  PRO A CA  1 
ATOM   174  C C   . PRO A 1 23 ? 5.413   -18.550 1.005   1.00 18.64 ? 22  PRO A C   1 
ATOM   175  O O   . PRO A 1 23 ? 5.757   -19.588 0.402   1.00 20.97 ? 22  PRO A O   1 
ATOM   176  C CB  . PRO A 1 23 ? 5.985   -19.040 3.461   1.00 20.29 ? 22  PRO A CB  1 
ATOM   177  C CG  . PRO A 1 23 ? 5.793   -20.533 3.633   1.00 19.74 ? 22  PRO A CG  1 
ATOM   178  C CD  . PRO A 1 23 ? 4.226   -20.674 3.592   1.00 21.05 ? 22  PRO A CD  1 
ATOM   179  N N   . ALA A 1 24 ? 5.506   -17.338 0.456   1.00 17.03 ? 23  ALA A N   1 
ATOM   180  C CA  . ALA A 1 24 ? 5.817   -17.227 -0.965  1.00 18.84 ? 23  ALA A CA  1 
ATOM   181  C C   . ALA A 1 24 ? 6.351   -15.829 -1.294  1.00 18.51 ? 23  ALA A C   1 
ATOM   182  O O   . ALA A 1 24 ? 6.361   -14.938 -0.469  1.00 18.10 ? 23  ALA A O   1 
ATOM   183  C CB  . ALA A 1 24 ? 4.551   -17.561 -1.834  1.00 20.85 ? 23  ALA A CB  1 
ATOM   184  N N   . ARG A 1 25 ? 6.858   -15.656 -2.536  1.00 18.50 ? 24  ARG A N   1 
ATOM   185  C CA  . ARG A 1 25 ? 7.249   -14.327 -2.982  1.00 17.17 ? 24  ARG A CA  1 
ATOM   186  C C   . ARG A 1 25 ? 6.674   -14.081 -4.370  1.00 17.94 ? 24  ARG A C   1 
ATOM   187  O O   . ARG A 1 25 ? 6.419   -15.054 -5.103  1.00 19.08 ? 24  ARG A O   1 
ATOM   188  C CB  . ARG A 1 25 ? 8.788   -14.224 -2.926  1.00 18.20 ? 24  ARG A CB  1 
ATOM   189  C CG  . ARG A 1 25 ? 9.488   -15.096 -3.951  1.00 18.41 ? 24  ARG A CG  1 
ATOM   190  C CD  . ARG A 1 25 ? 11.040  -14.915 -3.773  1.00 19.44 ? 24  ARG A CD  1 
ATOM   191  N NE  . ARG A 1 25 ? 11.685  -15.730 -4.837  1.00 21.30 ? 24  ARG A NE  1 
ATOM   192  C CZ  . ARG A 1 25 ? 12.982  -16.120 -4.722  1.00 21.65 ? 24  ARG A CZ  1 
ATOM   193  N NH1 . ARG A 1 25 ? 13.663  -15.962 -3.591  1.00 23.35 ? 24  ARG A NH1 1 
ATOM   194  N NH2 . ARG A 1 25 ? 13.505  -16.744 -5.783  1.00 25.45 ? 24  ARG A NH2 1 
ATOM   195  N N   . ILE A 1 26 ? 6.561   -12.779 -4.700  1.00 19.19 ? 25  ILE A N   1 
ATOM   196  C CA  . ILE A 1 26 ? 6.371   -12.425 -6.107  1.00 19.03 ? 25  ILE A CA  1 
ATOM   197  C C   . ILE A 1 26 ? 7.704   -12.581 -6.806  1.00 21.68 ? 25  ILE A C   1 
ATOM   198  O O   . ILE A 1 26 ? 8.659   -11.928 -6.426  1.00 21.62 ? 25  ILE A O   1 
ATOM   199  C CB  . ILE A 1 26 ? 5.906   -10.965 -6.218  1.00 21.70 ? 25  ILE A CB  1 
ATOM   200  C CG1 . ILE A 1 26 ? 4.702   -10.627 -5.298  1.00 26.85 ? 25  ILE A CG1 1 
ATOM   201  C CG2 . ILE A 1 26 ? 5.614   -10.662 -7.707  1.00 21.99 ? 25  ILE A CG2 1 
ATOM   202  C CD1 . ILE A 1 26 ? 3.412   -11.316 -5.654  1.00 30.15 ? 25  ILE A CD1 1 
ATOM   203  N N   . ASP A 1 27 ? 7.734   -13.398 -7.860  1.00 21.82 ? 26  ASP A N   1 
ATOM   204  C CA  . ASP A 1 27 ? 8.994   -13.601 -8.569  1.00 23.52 ? 26  ASP A CA  1 
ATOM   205  C C   . ASP A 1 27 ? 9.130   -12.610 -9.730  1.00 26.30 ? 26  ASP A C   1 
ATOM   206  O O   . ASP A 1 27 ? 8.192   -11.962 -10.202 1.00 24.82 ? 26  ASP A O   1 
ATOM   207  C CB  . ASP A 1 27 ? 9.116   -14.970 -9.186  1.00 22.30 ? 26  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 27 ? 10.134  -15.886 -8.541  1.00 23.10 ? 26  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 27 ? 10.705  -15.481 -7.480  1.00 29.06 ? 26  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 27 ? 10.245  -17.000 -8.987  1.00 24.87 ? 26  ASP A OD2 1 
ATOM   211  N N   . ASP A 1 28 ? 10.394  -12.458 -10.178 1.00 27.33 ? 27  ASP A N   1 
ATOM   212  C CA  . ASP A 1 28 ? 10.614  -11.777 -11.434 1.00 30.75 ? 27  ASP A CA  1 
ATOM   213  C C   . ASP A 1 28 ? 10.348  -12.788 -12.549 1.00 30.62 ? 27  ASP A C   1 
ATOM   214  O O   . ASP A 1 28 ? 10.272  -13.984 -12.322 1.00 29.94 ? 27  ASP A O   1 
ATOM   215  C CB  . ASP A 1 28 ? 12.077  -11.350 -11.570 1.00 35.81 ? 27  ASP A CB  1 
ATOM   216  C CG  . ASP A 1 28 ? 12.583  -10.150 -10.768 1.00 44.85 ? 27  ASP A CG  1 
ATOM   217  O OD1 . ASP A 1 28 ? 12.255  -8.986  -11.133 1.00 41.20 ? 27  ASP A OD1 1 
ATOM   218  O OD2 . ASP A 1 28 ? 13.364  -10.385 -9.812  1.00 52.00 ? 27  ASP A OD2 1 
ATOM   219  N N   . ILE A 1 29 ? 10.227  -12.301 -13.771 1.00 34.12 ? 28  ILE A N   1 
ATOM   220  C CA  . ILE A 1 29 ? 10.188  -13.188 -14.934 1.00 30.51 ? 28  ILE A CA  1 
ATOM   221  C C   . ILE A 1 29 ? 11.533  -12.974 -15.627 1.00 31.15 ? 28  ILE A C   1 
ATOM   222  O O   . ILE A 1 29 ? 11.839  -11.833 -15.915 1.00 32.24 ? 28  ILE A O   1 
ATOM   223  C CB  . ILE A 1 29 ? 9.059   -12.683 -15.828 1.00 32.82 ? 28  ILE A CB  1 
ATOM   224  C CG1 . ILE A 1 29 ? 7.691   -12.693 -15.089 1.00 37.36 ? 28  ILE A CG1 1 
ATOM   225  C CG2 . ILE A 1 29 ? 9.038   -13.463 -17.145 1.00 32.38 ? 28  ILE A CG2 1 
ATOM   226  C CD1 . ILE A 1 29 ? 6.731   -11.619 -15.554 1.00 35.96 ? 28  ILE A CD1 1 
ATOM   227  N N   . ALA A 1 30 ? 12.333  -14.036 -15.774 1.00 34.56 ? 29  ALA A N   1 
ATOM   228  C CA  . ALA A 1 30 ? 13.627  -13.933 -16.460 1.00 30.98 ? 29  ALA A CA  1 
ATOM   229  C C   . ALA A 1 30 ? 13.416  -13.611 -17.949 1.00 29.92 ? 29  ALA A C   1 
ATOM   230  O O   . ALA A 1 30 ? 12.360  -13.859 -18.534 1.00 31.94 ? 29  ALA A O   1 
ATOM   231  C CB  . ALA A 1 30 ? 14.385  -15.228 -16.314 1.00 31.84 ? 29  ALA A CB  1 
ATOM   232  N N   . ASP A 1 31 ? 14.421  -12.955 -18.530 1.00 28.35 ? 30  ASP A N   1 
ATOM   233  C CA  . ASP A 1 31 ? 14.431  -12.854 -19.988 1.00 28.46 ? 30  ASP A CA  1 
ATOM   234  C C   . ASP A 1 31 ? 14.184  -14.232 -20.587 1.00 26.39 ? 30  ASP A C   1 
ATOM   235  O O   . ASP A 1 31 ? 14.797  -15.196 -20.172 1.00 31.29 ? 30  ASP A O   1 
ATOM   236  C CB  . ASP A 1 31 ? 15.792  -12.332 -20.436 1.00 31.22 ? 30  ASP A CB  1 
ATOM   237  C CG  . ASP A 1 31 ? 16.023  -10.843 -20.230 1.00 33.96 ? 30  ASP A CG  1 
ATOM   238  O OD1 . ASP A 1 31 ? 15.050  -10.112 -20.094 1.00 34.08 ? 30  ASP A OD1 1 
ATOM   239  O OD2 . ASP A 1 31 ? 17.192  -10.421 -20.223 1.00 38.25 ? 30  ASP A OD2 1 
ATOM   240  N N   . GLY A 1 32 ? 13.338  -14.259 -21.632 1.00 27.13 ? 31  GLY A N   1 
ATOM   241  C CA  . GLY A 1 32 ? 13.052  -15.436 -22.428 1.00 26.71 ? 31  GLY A CA  1 
ATOM   242  C C   . GLY A 1 32 ? 12.148  -16.457 -21.743 1.00 32.41 ? 31  GLY A C   1 
ATOM   243  O O   . GLY A 1 32 ? 11.841  -17.483 -22.326 1.00 33.55 ? 31  GLY A O   1 
ATOM   244  N N   . ALA A 1 33 ? 11.763  -16.178 -20.490 1.00 30.94 ? 32  ALA A N   1 
ATOM   245  C CA  . ALA A 1 33 ? 10.962  -17.126 -19.729 1.00 31.71 ? 32  ALA A CA  1 
ATOM   246  C C   . ALA A 1 33 ? 9.472   -16.904 -19.992 1.00 28.36 ? 32  ALA A C   1 
ATOM   247  O O   . ALA A 1 33 ? 9.008   -15.849 -20.417 1.00 29.30 ? 32  ALA A O   1 
ATOM   248  C CB  . ALA A 1 33 ? 11.257  -16.933 -18.238 1.00 30.47 ? 32  ALA A CB  1 
ATOM   249  N N   . VAL A 1 34 ? 8.677   -17.943 -19.678 1.00 31.39 ? 33  VAL A N   1 
ATOM   250  C CA  . VAL A 1 34 ? 7.229   -17.845 -19.881 1.00 30.80 ? 33  VAL A CA  1 
ATOM   251  C C   . VAL A 1 34 ? 6.593   -16.821 -18.935 1.00 29.75 ? 33  VAL A C   1 
ATOM   252  O O   . VAL A 1 34 ? 6.830   -16.870 -17.725 1.00 32.41 ? 33  VAL A O   1 
ATOM   253  C CB  . VAL A 1 34 ? 6.646   -19.246 -19.598 1.00 33.71 ? 33  VAL A CB  1 
ATOM   254  C CG1 . VAL A 1 34 ? 5.122   -19.185 -19.493 1.00 34.59 ? 33  VAL A CG1 1 
ATOM   255  C CG2 . VAL A 1 34 ? 7.077   -20.255 -20.663 1.00 35.82 ? 33  VAL A CG2 1 
ATOM   256  N N   . LYS A 1 35 ? 5.810   -15.905 -19.500 1.00 32.48 ? 34  LYS A N   1 
ATOM   257  C CA  . LYS A 1 35 ? 5.114   -14.852 -18.766 1.00 33.59 ? 34  LYS A CA  1 
ATOM   258  C C   . LYS A 1 35 ? 3.774   -15.342 -18.227 1.00 36.86 ? 34  LYS A C   1 
ATOM   259  O O   . LYS A 1 35 ? 3.140   -16.235 -18.782 1.00 36.50 ? 34  LYS A O   1 
ATOM   260  C CB  . LYS A 1 35 ? 4.801   -13.608 -19.589 1.00 31.83 ? 34  LYS A CB  1 
ATOM   261  C CG  . LYS A 1 35 ? 6.064   -12.902 -20.134 1.00 32.56 ? 34  LYS A CG  1 
ATOM   262  C CD  . LYS A 1 35 ? 5.754   -11.712 -21.037 1.00 37.67 ? 34  LYS A CD  1 
ATOM   263  C CE  . LYS A 1 35 ? 5.258   -12.093 -22.405 1.00 41.82 ? 34  LYS A CE  1 
ATOM   264  N NZ  . LYS A 1 35 ? 5.127   -10.910 -23.256 1.00 41.06 ? 34  LYS A NZ  1 
ATOM   265  N N   . PRO A 1 36 ? 3.290   -14.730 -17.128 1.00 34.86 ? 35  PRO A N   1 
ATOM   266  C CA  . PRO A 1 36 ? 2.001   -15.117 -16.564 1.00 35.60 ? 35  PRO A CA  1 
ATOM   267  C C   . PRO A 1 36 ? 0.880   -14.605 -17.454 1.00 32.24 ? 35  PRO A C   1 
ATOM   268  O O   . PRO A 1 36 ? 1.049   -13.656 -18.203 1.00 33.41 ? 35  PRO A O   1 
ATOM   269  C CB  . PRO A 1 36 ? 1.937   -14.449 -15.187 1.00 33.55 ? 35  PRO A CB  1 
ATOM   270  C CG  . PRO A 1 36 ? 2.955   -13.309 -15.224 1.00 36.13 ? 35  PRO A CG  1 
ATOM   271  C CD  . PRO A 1 36 ? 3.913   -13.620 -16.408 1.00 34.55 ? 35  PRO A CD  1 
ATOM   272  N N   . PRO A 1 37 ? -0.353  -15.117 -17.278 1.00 36.13 ? 36  PRO A N   1 
ATOM   273  C CA  . PRO A 1 37 ? -1.533  -14.471 -17.870 1.00 40.84 ? 36  PRO A CA  1 
ATOM   274  C C   . PRO A 1 37 ? -1.732  -13.032 -17.404 1.00 43.52 ? 36  PRO A C   1 
ATOM   275  O O   . PRO A 1 37 ? -1.228  -12.644 -16.347 1.00 34.78 ? 36  PRO A O   1 
ATOM   276  C CB  . PRO A 1 37 ? -2.706  -15.345 -17.400 1.00 39.56 ? 36  PRO A CB  1 
ATOM   277  C CG  . PRO A 1 37 ? -2.085  -16.638 -16.930 1.00 37.21 ? 36  PRO A CG  1 
ATOM   278  C CD  . PRO A 1 37 ? -0.651  -16.346 -16.520 1.00 38.02 ? 36  PRO A CD  1 
ATOM   279  N N   . PRO A 1 38 ? -2.506  -12.190 -18.132 1.00 39.64 ? 37  PRO A N   1 
ATOM   280  C CA  . PRO A 1 38 ? -2.863  -10.859 -17.634 1.00 40.52 ? 37  PRO A CA  1 
ATOM   281  C C   . PRO A 1 38 ? -3.502  -10.923 -16.252 1.00 35.66 ? 37  PRO A C   1 
ATOM   282  O O   . PRO A 1 38 ? -4.191  -11.891 -15.932 1.00 41.53 ? 37  PRO A O   1 
ATOM   283  C CB  . PRO A 1 38 ? -3.842  -10.276 -18.692 1.00 44.01 ? 37  PRO A CB  1 
ATOM   284  C CG  . PRO A 1 38 ? -4.225  -11.484 -19.500 1.00 38.56 ? 37  PRO A CG  1 
ATOM   285  C CD  . PRO A 1 38 ? -3.065  -12.464 -19.475 1.00 45.36 ? 37  PRO A CD  1 
ATOM   286  N N   . ASN A 1 39 ? -3.184  -9.907  -15.445 1.00 38.98 ? 38  ASN A N   1 
ATOM   287  C CA  . ASN A 1 39 ? -3.696  -9.709  -14.104 1.00 38.29 ? 38  ASN A CA  1 
ATOM   288  C C   . ASN A 1 39 ? -3.166  -10.770 -13.142 1.00 34.49 ? 38  ASN A C   1 
ATOM   289  O O   . ASN A 1 39 ? -3.612  -10.775 -11.993 1.00 35.17 ? 38  ASN A O   1 
ATOM   290  C CB  . ASN A 1 39 ? -5.217  -9.597  -14.066 1.00 44.23 ? 38  ASN A CB  1 
ATOM   291  C CG  . ASN A 1 39 ? -5.671  -8.445  -14.931 1.00 48.08 ? 38  ASN A CG  1 
ATOM   292  O OD1 . ASN A 1 39 ? -5.514  -7.276  -14.550 1.00 48.77 ? 38  ASN A OD1 1 
ATOM   293  N ND2 . ASN A 1 39 ? -6.166  -8.765  -16.114 1.00 48.24 ? 38  ASN A ND2 1 
ATOM   294  N N   . LYS A 1 40 ? -2.191  -11.605 -13.575 1.00 29.58 ? 39  LYS A N   1 
ATOM   295  C CA  . LYS A 1 40 ? -1.667  -12.633 -12.675 1.00 23.13 ? 39  LYS A CA  1 
ATOM   296  C C   . LYS A 1 40 ? -0.178  -12.353 -12.450 1.00 23.56 ? 39  LYS A C   1 
ATOM   297  O O   . LYS A 1 40 ? 0.504   -11.678 -13.225 1.00 27.06 ? 39  LYS A O   1 
ATOM   298  C CB  . LYS A 1 40 ? -1.804  -14.079 -13.145 1.00 25.24 ? 39  LYS A CB  1 
ATOM   299  C CG  . LYS A 1 40 ? -3.203  -14.602 -13.564 1.00 30.75 ? 39  LYS A CG  1 
ATOM   300  C CD  . LYS A 1 40 ? -4.108  -14.521 -12.356 1.00 34.48 ? 39  LYS A CD  1 
ATOM   301  C CE  . LYS A 1 40 ? -5.556  -14.857 -12.700 1.00 39.97 ? 39  LYS A CE  1 
ATOM   302  N NZ  . LYS A 1 40 ? -5.816  -16.285 -12.885 1.00 46.38 ? 39  LYS A NZ  1 
ATOM   303  N N   . TYR A 1 41 ? 0.287   -12.757 -11.277 1.00 20.49 ? 40  TYR A N   1 
ATOM   304  C CA  . TYR A 1 41 ? 1.698   -12.647 -10.899 1.00 21.48 ? 40  TYR A CA  1 
ATOM   305  C C   . TYR A 1 41 ? 2.315   -14.031 -10.794 1.00 21.35 ? 40  TYR A C   1 
ATOM   306  O O   . TYR A 1 41 ? 1.672   -15.003 -10.405 1.00 21.98 ? 40  TYR A O   1 
ATOM   307  C CB  . TYR A 1 41 ? 1.763   -12.038 -9.471  1.00 21.27 ? 40  TYR A CB  1 
ATOM   308  C CG  . TYR A 1 41 ? 1.288   -10.600 -9.463  1.00 22.47 ? 40  TYR A CG  1 
ATOM   309  C CD1 . TYR A 1 41 ? -0.076  -10.332 -9.298  1.00 26.11 ? 40  TYR A CD1 1 
ATOM   310  C CD2 . TYR A 1 41 ? 2.155   -9.530  -9.632  1.00 24.79 ? 40  TYR A CD2 1 
ATOM   311  C CE1 . TYR A 1 41 ? -0.561  -9.042  -9.419  1.00 27.07 ? 40  TYR A CE1 1 
ATOM   312  C CE2 . TYR A 1 41 ? 1.683   -8.219  -9.655  1.00 25.81 ? 40  TYR A CE2 1 
ATOM   313  C CZ  . TYR A 1 41 ? 0.320   -7.986  -9.544  1.00 30.89 ? 40  TYR A CZ  1 
ATOM   314  O OH  . TYR A 1 41 ? -0.187  -6.729  -9.680  1.00 31.48 ? 40  TYR A OH  1 
ATOM   315  N N   . PRO A 1 42 ? 3.649   -14.173 -11.038 1.00 21.33 ? 41  PRO A N   1 
ATOM   316  C CA  . PRO A 1 42 ? 4.332   -15.453 -10.816 1.00 21.44 ? 41  PRO A CA  1 
ATOM   317  C C   . PRO A 1 42 ? 4.666   -15.552 -9.339  1.00 21.06 ? 41  PRO A C   1 
ATOM   318  O O   . PRO A 1 42 ? 5.339   -14.656 -8.825  1.00 22.01 ? 41  PRO A O   1 
ATOM   319  C CB  . PRO A 1 42 ? 5.618   -15.323 -11.683 1.00 23.03 ? 41  PRO A CB  1 
ATOM   320  C CG  . PRO A 1 42 ? 5.818   -13.866 -11.876 1.00 22.81 ? 41  PRO A CG  1 
ATOM   321  C CD  . PRO A 1 42 ? 4.506   -13.101 -11.568 1.00 23.65 ? 41  PRO A CD  1 
ATOM   322  N N   . ILE A 1 43 ? 4.140   -16.587 -8.706  1.00 21.00 ? 42  ILE A N   1 
ATOM   323  C CA  . ILE A 1 43 ? 4.332   -16.732 -7.262  1.00 18.81 ? 42  ILE A CA  1 
ATOM   324  C C   . ILE A 1 43 ? 5.277   -17.915 -7.079  1.00 21.97 ? 42  ILE A C   1 
ATOM   325  O O   . ILE A 1 43 ? 4.974   -19.083 -7.490  1.00 23.33 ? 42  ILE A O   1 
ATOM   326  C CB  . ILE A 1 43 ? 2.980   -16.999 -6.582  1.00 19.73 ? 42  ILE A CB  1 
ATOM   327  C CG1 . ILE A 1 43 ? 1.956   -15.893 -6.907  1.00 21.11 ? 42  ILE A CG1 1 
ATOM   328  C CG2 . ILE A 1 43 ? 3.233   -17.139 -5.070  1.00 18.91 ? 42  ILE A CG2 1 
ATOM   329  C CD1 . ILE A 1 43 ? 2.492   -14.499 -6.573  1.00 22.16 ? 42  ILE A CD1 1 
ATOM   330  N N   . PHE A 1 44 ? 6.393   -17.648 -6.364  1.00 20.60 ? 43  PHE A N   1 
ATOM   331  C CA  . PHE A 1 44 ? 7.245   -18.746 -6.022  1.00 21.06 ? 43  PHE A CA  1 
ATOM   332  C C   . PHE A 1 44 ? 6.950   -19.132 -4.580  1.00 19.11 ? 43  PHE A C   1 
ATOM   333  O O   . PHE A 1 44 ? 7.009   -18.307 -3.677  1.00 20.99 ? 43  PHE A O   1 
ATOM   334  C CB  . PHE A 1 44 ? 8.695   -18.227 -6.133  1.00 20.62 ? 43  PHE A CB  1 
ATOM   335  C CG  . PHE A 1 44 ? 9.752   -19.253 -5.733  1.00 21.43 ? 43  PHE A CG  1 
ATOM   336  C CD1 . PHE A 1 44 ? 10.109  -20.265 -6.622  1.00 23.18 ? 43  PHE A CD1 1 
ATOM   337  C CD2 . PHE A 1 44 ? 10.331  -19.205 -4.465  1.00 24.29 ? 43  PHE A CD2 1 
ATOM   338  C CE1 . PHE A 1 44 ? 11.074  -21.194 -6.248  1.00 28.22 ? 43  PHE A CE1 1 
ATOM   339  C CE2 . PHE A 1 44 ? 11.304  -20.152 -4.099  1.00 25.26 ? 43  PHE A CE2 1 
ATOM   340  C CZ  . PHE A 1 44 ? 11.665  -21.118 -5.010  1.00 25.53 ? 43  PHE A CZ  1 
ATOM   341  N N   . PHE A 1 45 ? 6.659   -20.417 -4.391  1.00 20.59 ? 44  PHE A N   1 
ATOM   342  C CA  . PHE A 1 45 ? 6.300   -20.942 -3.091  1.00 20.40 ? 44  PHE A CA  1 
ATOM   343  C C   . PHE A 1 45 ? 7.561   -21.440 -2.401  1.00 23.10 ? 44  PHE A C   1 
ATOM   344  O O   . PHE A 1 45 ? 8.287   -22.297 -2.948  1.00 23.22 ? 44  PHE A O   1 
ATOM   345  C CB  . PHE A 1 45 ? 5.270   -22.081 -3.329  1.00 22.11 ? 44  PHE A CB  1 
ATOM   346  C CG  . PHE A 1 45 ? 3.880   -21.606 -3.725  1.00 21.76 ? 44  PHE A CG  1 
ATOM   347  C CD1 . PHE A 1 45 ? 3.554   -21.431 -5.061  1.00 25.20 ? 44  PHE A CD1 1 
ATOM   348  C CD2 . PHE A 1 45 ? 2.919   -21.343 -2.748  1.00 23.89 ? 44  PHE A CD2 1 
ATOM   349  C CE1 . PHE A 1 45 ? 2.284   -20.973 -5.424  1.00 28.67 ? 44  PHE A CE1 1 
ATOM   350  C CE2 . PHE A 1 45 ? 1.662   -20.867 -3.112  1.00 25.08 ? 44  PHE A CE2 1 
ATOM   351  C CZ  . PHE A 1 45 ? 1.382   -20.667 -4.444  1.00 26.58 ? 44  PHE A CZ  1 
ATOM   352  N N   . PHE A 1 46 ? 7.815   -20.885 -1.205  1.00 21.71 ? 45  PHE A N   1 
ATOM   353  C CA  . PHE A 1 46 ? 9.010   -21.353 -0.497  1.00 21.86 ? 45  PHE A CA  1 
ATOM   354  C C   . PHE A 1 46 ? 8.791   -22.796 -0.052  1.00 22.62 ? 45  PHE A C   1 
ATOM   355  O O   . PHE A 1 46 ? 7.645   -23.262 0.096   1.00 24.10 ? 45  PHE A O   1 
ATOM   356  C CB  . PHE A 1 46 ? 9.226   -20.452 0.729   1.00 19.75 ? 45  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 46 ? 9.700   -19.064 0.326   1.00 20.62 ? 45  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 46 ? 10.970  -18.881 -0.224  1.00 20.03 ? 45  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 46 ? 8.953   -17.907 0.610   1.00 21.31 ? 45  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 46 ? 11.403  -17.613 -0.594  1.00 19.77 ? 45  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 46 ? 9.371   -16.642 0.254   1.00 19.50 ? 45  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 46 ? 10.651  -16.468 -0.313  1.00 19.58 ? 45  PHE A CZ  1 
ATOM   363  N N   . GLY A 1 47 ? 9.899   -23.513 0.150   1.00 24.51 ? 46  GLY A N   1 
ATOM   364  C CA  . GLY A 1 47 ? 9.838   -24.882 0.648   1.00 23.69 ? 46  GLY A CA  1 
ATOM   365  C C   . GLY A 1 47 ? 9.589   -25.863 -0.504  1.00 29.49 ? 46  GLY A C   1 
ATOM   366  O O   . GLY A 1 47 ? 10.439  -26.693 -0.815  1.00 30.18 ? 46  GLY A O   1 
ATOM   367  N N   . THR A 1 48 ? 8.433   -25.766 -1.191  1.00 25.48 ? 47  THR A N   1 
ATOM   368  C CA  . THR A 1 48 ? 8.210   -26.622 -2.346  1.00 27.39 ? 47  THR A CA  1 
ATOM   369  C C   . THR A 1 48 ? 9.017   -26.146 -3.550  1.00 28.87 ? 47  THR A C   1 
ATOM   370  O O   . THR A 1 48 ? 9.306   -26.925 -4.471  1.00 29.01 ? 47  THR A O   1 
ATOM   371  C CB  . THR A 1 48 ? 6.718   -26.677 -2.677  1.00 29.45 ? 47  THR A CB  1 
ATOM   372  O OG1 . THR A 1 48 ? 6.325   -25.380 -3.120  1.00 29.22 ? 47  THR A OG1 1 
ATOM   373  C CG2 . THR A 1 48 ? 5.869   -27.189 -1.540  1.00 30.21 ? 47  THR A CG2 1 
ATOM   374  N N   . HIS A 1 49 ? 9.299   -24.832 -3.608  1.00 26.26 ? 48  HIS A N   1 
ATOM   375  C CA  . HIS A 1 49 ? 9.990   -24.203 -4.727  1.00 26.62 ? 48  HIS A CA  1 
ATOM   376  C C   . HIS A 1 49 ? 9.192   -24.355 -6.023  1.00 25.73 ? 48  HIS A C   1 
ATOM   377  O O   . HIS A 1 49 ? 9.757   -24.314 -7.105  1.00 28.44 ? 48  HIS A O   1 
ATOM   378  C CB  . HIS A 1 49 ? 11.455  -24.675 -4.896  1.00 24.92 ? 48  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 49 ? 12.156  -24.740 -3.568  1.00 28.16 ? 48  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 49 ? 12.969  -25.789 -3.212  1.00 31.04 ? 48  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 49 ? 12.203  -23.862 -2.525  1.00 26.30 ? 48  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 49 ? 13.447  -25.582 -1.988  1.00 32.70 ? 48  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 49 ? 13.011  -24.398 -1.552  1.00 29.24 ? 48  HIS A NE2 1 
ATOM   384  N N   . GLU A 1 50 ? 7.860   -24.442 -5.903  1.00 27.28 ? 49  GLU A N   1 
ATOM   385  C CA  . GLU A 1 50 ? 6.992   -24.460 -7.073  1.00 29.98 ? 49  GLU A CA  1 
ATOM   386  C C   . GLU A 1 50 ? 6.490   -23.055 -7.425  1.00 28.30 ? 49  GLU A C   1 
ATOM   387  O O   . GLU A 1 50 ? 6.631   -22.127 -6.626  1.00 25.95 ? 49  GLU A O   1 
ATOM   388  C CB  . GLU A 1 50 ? 5.787   -25.349 -6.791  1.00 32.13 ? 49  GLU A CB  1 
ATOM   389  C CG  . GLU A 1 50 ? 6.216   -26.795 -6.558  1.00 43.17 ? 49  GLU A CG  1 
ATOM   390  C CD  . GLU A 1 50 ? 5.120   -27.738 -6.111  1.00 49.36 ? 49  GLU A CD  1 
ATOM   391  O OE1 . GLU A 1 50 ? 3.924   -27.379 -6.137  1.00 47.72 ? 49  GLU A OE1 1 
ATOM   392  O OE2 . GLU A 1 50 ? 5.512   -28.860 -5.721  1.00 53.39 ? 49  GLU A OE2 1 
ATOM   393  N N   . THR A 1 51 ? 6.072   -22.882 -8.687  1.00 25.38 ? 50  THR A N   1 
ATOM   394  C CA  . THR A 1 51 ? 5.558   -21.610 -9.177  1.00 23.86 ? 50  THR A CA  1 
ATOM   395  C C   . THR A 1 51 ? 4.108   -21.824 -9.605  1.00 25.53 ? 50  THR A C   1 
ATOM   396  O O   . THR A 1 51 ? 3.803   -22.798 -10.309 1.00 28.65 ? 50  THR A O   1 
ATOM   397  C CB  . THR A 1 51 ? 6.353   -21.054 -10.362 1.00 26.78 ? 50  THR A CB  1 
ATOM   398  O OG1 . THR A 1 51 ? 7.676   -20.731 -9.922  1.00 28.15 ? 50  THR A OG1 1 
ATOM   399  C CG2 . THR A 1 51 ? 5.731   -19.794 -10.952 1.00 28.88 ? 50  THR A CG2 1 
ATOM   400  N N   . ALA A 1 52 ? 3.217   -20.911 -9.212  1.00 23.80 ? 51  ALA A N   1 
ATOM   401  C CA  . ALA A 1 52 ? 1.882   -20.844 -9.797  1.00 23.46 ? 51  ALA A CA  1 
ATOM   402  C C   . ALA A 1 52 ? 1.587   -19.382 -10.117 1.00 25.07 ? 51  ALA A C   1 
ATOM   403  O O   . ALA A 1 52 ? 2.284   -18.459 -9.654  1.00 25.80 ? 51  ALA A O   1 
ATOM   404  C CB  . ALA A 1 52 ? 0.859   -21.376 -8.822  1.00 24.93 ? 51  ALA A CB  1 
ATOM   405  N N   . PHE A 1 53 ? 0.490   -19.146 -10.860 1.00 24.03 ? 52  PHE A N   1 
ATOM   406  C CA  . PHE A 1 53 ? 0.121   -17.797 -11.233 1.00 24.13 ? 52  PHE A CA  1 
ATOM   407  C C   . PHE A 1 53 ? -1.136  -17.434 -10.471 1.00 26.72 ? 52  PHE A C   1 
ATOM   408  O O   . PHE A 1 53 ? -2.119  -18.152 -10.530 1.00 30.77 ? 52  PHE A O   1 
ATOM   409  C CB  . PHE A 1 53 ? -0.158  -17.742 -12.737 1.00 25.39 ? 52  PHE A CB  1 
ATOM   410  C CG  . PHE A 1 53 ? 1.035   -18.123 -13.579 1.00 26.89 ? 52  PHE A CG  1 
ATOM   411  C CD1 . PHE A 1 53 ? 2.195   -17.354 -13.555 1.00 30.95 ? 52  PHE A CD1 1 
ATOM   412  C CD2 . PHE A 1 53 ? 0.940   -19.182 -14.481 1.00 31.79 ? 52  PHE A CD2 1 
ATOM   413  C CE1 . PHE A 1 53 ? 3.288   -17.702 -14.336 1.00 41.98 ? 52  PHE A CE1 1 
ATOM   414  C CE2 . PHE A 1 53 ? 2.045   -19.523 -15.243 1.00 36.47 ? 52  PHE A CE2 1 
ATOM   415  C CZ  . PHE A 1 53 ? 3.188   -18.766 -15.208 1.00 35.61 ? 52  PHE A CZ  1 
ATOM   416  N N   . LEU A 1 54 ? -1.063  -16.347 -9.706  1.00 22.19 ? 53  LEU A N   1 
ATOM   417  C CA  . LEU A 1 54 ? -2.176  -15.963 -8.843  1.00 21.84 ? 53  LEU A CA  1 
ATOM   418  C C   . LEU A 1 54 ? -2.438  -14.484 -8.975  1.00 21.79 ? 53  LEU A C   1 
ATOM   419  O O   . LEU A 1 54 ? -1.592  -13.648 -9.330  1.00 22.42 ? 53  LEU A O   1 
ATOM   420  C CB  . LEU A 1 54 ? -1.830  -16.265 -7.380  1.00 23.59 ? 53  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 54 ? -1.704  -17.740 -7.027  1.00 23.90 ? 53  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 54 ? -1.354  -17.796 -5.539  1.00 24.43 ? 53  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 54 ? -3.087  -18.424 -7.214  1.00 28.18 ? 53  LEU A CD2 1 
ATOM   424  N N   . GLY A 1 55 ? -3.712  -14.129 -8.714  1.00 20.04 ? 54  GLY A N   1 
ATOM   425  C CA  . GLY A 1 55 ? -3.997  -12.710 -8.617  1.00 22.24 ? 54  GLY A CA  1 
ATOM   426  C C   . GLY A 1 55 ? -4.041  -12.216 -7.164  1.00 19.06 ? 54  GLY A C   1 
ATOM   427  O O   . GLY A 1 55 ? -4.014  -13.007 -6.226  1.00 19.59 ? 54  GLY A O   1 
ATOM   428  N N   . PRO A 1 56 ? -4.131  -10.887 -6.983  1.00 19.81 ? 55  PRO A N   1 
ATOM   429  C CA  . PRO A 1 56 ? -4.090  -10.287 -5.651  1.00 20.91 ? 55  PRO A CA  1 
ATOM   430  C C   . PRO A 1 56 ? -5.063  -10.816 -4.622  1.00 21.04 ? 55  PRO A C   1 
ATOM   431  O O   . PRO A 1 56 ? -4.786  -10.746 -3.432  1.00 20.63 ? 55  PRO A O   1 
ATOM   432  C CB  . PRO A 1 56 ? -4.297  -8.803  -5.928  1.00 21.50 ? 55  PRO A CB  1 
ATOM   433  C CG  . PRO A 1 56 ? -3.754  -8.578  -7.329  1.00 22.87 ? 55  PRO A CG  1 
ATOM   434  C CD  . PRO A 1 56 ? -4.085  -9.876  -8.061  1.00 21.66 ? 55  PRO A CD  1 
ATOM   435  N N   . LYS A 1 57 ? -6.231  -11.312 -5.096  1.00 21.94 ? 56  LYS A N   1 
ATOM   436  C CA  . LYS A 1 57 ? -7.192  -11.868 -4.123  1.00 21.63 ? 56  LYS A CA  1 
ATOM   437  C C   . LYS A 1 57 ? -6.651  -13.017 -3.268  1.00 21.17 ? 56  LYS A C   1 
ATOM   438  O O   . LYS A 1 57 ? -7.069  -13.231 -2.123  1.00 21.29 ? 56  LYS A O   1 
ATOM   439  C CB  . LYS A 1 57 ? -8.506  -12.325 -4.794  1.00 25.51 ? 56  LYS A CB  1 
ATOM   440  C CG  . LYS A 1 57 ? -8.290  -13.617 -5.559  1.00 27.77 ? 56  LYS A CG  1 
ATOM   441  C CD  . LYS A 1 57 ? -9.607  -14.074 -6.215  1.00 33.21 ? 56  LYS A CD  1 
ATOM   442  C CE  . LYS A 1 57 ? -9.460  -15.392 -6.932  1.00 35.05 ? 56  LYS A CE  1 
ATOM   443  N NZ  . LYS A 1 57 ? -9.449  -16.510 -5.983  1.00 41.11 ? 56  LYS A NZ  1 
ATOM   444  N N   . ASP A 1 58 ? -5.571  -13.688 -3.736  1.00 19.95 ? 57  ASP A N   1 
ATOM   445  C CA  . ASP A 1 58 ? -5.014  -14.842 -3.063  1.00 20.60 ? 57  ASP A CA  1 
ATOM   446  C C   . ASP A 1 58 ? -3.632  -14.466 -2.464  1.00 18.86 ? 57  ASP A C   1 
ATOM   447  O O   . ASP A 1 58 ? -2.951  -15.350 -1.985  1.00 22.50 ? 57  ASP A O   1 
ATOM   448  C CB  . ASP A 1 58 ? -4.926  -15.989 -4.068  1.00 21.56 ? 57  ASP A CB  1 
ATOM   449  C CG  . ASP A 1 58 ? -6.324  -16.533 -4.391  1.00 23.82 ? 57  ASP A CG  1 
ATOM   450  O OD1 . ASP A 1 58 ? -7.104  -16.604 -3.424  1.00 27.31 ? 57  ASP A OD1 1 
ATOM   451  O OD2 . ASP A 1 58 ? -6.551  -16.939 -5.544  1.00 27.79 ? 57  ASP A OD2 1 
ATOM   452  N N   . LEU A 1 59 ? -3.330  -13.165 -2.430  1.00 18.79 ? 58  LEU A N   1 
ATOM   453  C CA  . LEU A 1 59 ? -1.982  -12.743 -1.960  1.00 17.75 ? 58  LEU A CA  1 
ATOM   454  C C   . LEU A 1 59 ? -2.115  -11.869 -0.699  1.00 17.98 ? 58  LEU A C   1 
ATOM   455  O O   . LEU A 1 59 ? -2.683  -10.762 -0.723  1.00 18.93 ? 58  LEU A O   1 
ATOM   456  C CB  . LEU A 1 59 ? -1.257  -11.971 -3.072  1.00 18.68 ? 58  LEU A CB  1 
ATOM   457  C CG  . LEU A 1 59 ? -1.066  -12.779 -4.349  1.00 20.21 ? 58  LEU A CG  1 
ATOM   458  C CD1 . LEU A 1 59 ? -0.393  -11.911 -5.421  1.00 21.94 ? 58  LEU A CD1 1 
ATOM   459  C CD2 . LEU A 1 59 ? -0.280  -14.057 -4.184  1.00 19.88 ? 58  LEU A CD2 1 
ATOM   460  N N   . PHE A 1 60 ? -1.519  -12.352 0.400   1.00 19.02 ? 59  PHE A N   1 
ATOM   461  C CA  . PHE A 1 60 ? -1.604  -11.682 1.706   1.00 19.66 ? 59  PHE A CA  1 
ATOM   462  C C   . PHE A 1 60 ? -0.224  -11.170 2.120   1.00 20.38 ? 59  PHE A C   1 
ATOM   463  O O   . PHE A 1 60 ? 0.675   -11.983 2.310   1.00 22.06 ? 59  PHE A O   1 
ATOM   464  C CB  . PHE A 1 60 ? -2.061  -12.739 2.703   1.00 21.00 ? 59  PHE A CB  1 
ATOM   465  C CG  . PHE A 1 60 ? -3.514  -13.155 2.459   1.00 21.41 ? 59  PHE A CG  1 
ATOM   466  C CD1 . PHE A 1 60 ? -3.825  -14.060 1.457   1.00 21.25 ? 59  PHE A CD1 1 
ATOM   467  C CD2 . PHE A 1 60 ? -4.526  -12.621 3.241   1.00 22.96 ? 59  PHE A CD2 1 
ATOM   468  C CE1 . PHE A 1 60 ? -5.140  -14.433 1.197   1.00 25.35 ? 59  PHE A CE1 1 
ATOM   469  C CE2 . PHE A 1 60 ? -5.846  -13.016 2.964   1.00 22.13 ? 59  PHE A CE2 1 
ATOM   470  C CZ  . PHE A 1 60 ? -6.131  -13.920 1.988   1.00 24.75 ? 59  PHE A CZ  1 
ATOM   471  N N   . PRO A 1 61 ? -0.010  -9.862  2.269   1.00 22.79 ? 60  PRO A N   1 
ATOM   472  C CA  . PRO A 1 61 ? 1.357   -9.368  2.548   1.00 21.88 ? 60  PRO A CA  1 
ATOM   473  C C   . PRO A 1 61 ? 1.873   -10.051 3.806   1.00 20.56 ? 60  PRO A C   1 
ATOM   474  O O   . PRO A 1 61 ? 1.212   -10.216 4.819   1.00 23.84 ? 60  PRO A O   1 
ATOM   475  C CB  . PRO A 1 61 ? 1.135   -7.852  2.712   1.00 24.25 ? 60  PRO A CB  1 
ATOM   476  C CG  . PRO A 1 61 ? 0.008   -7.553  1.642   1.00 27.39 ? 60  PRO A CG  1 
ATOM   477  C CD  . PRO A 1 61 ? -0.927  -8.751  1.950   1.00 25.19 ? 60  PRO A CD  1 
ATOM   478  N N   . TYR A 1 62 ? 3.178   -10.459 3.792   1.00 20.91 ? 61  TYR A N   1 
ATOM   479  C CA  . TYR A 1 62 ? 3.712   -11.319 4.833   1.00 21.42 ? 61  TYR A CA  1 
ATOM   480  C C   . TYR A 1 62 ? 3.766   -10.642 6.211   1.00 20.40 ? 61  TYR A C   1 
ATOM   481  O O   . TYR A 1 62 ? 3.437   -11.310 7.176   1.00 24.50 ? 61  TYR A O   1 
ATOM   482  C CB  . TYR A 1 62 ? 5.145   -11.675 4.360   1.00 21.60 ? 61  TYR A CB  1 
ATOM   483  C CG  . TYR A 1 62 ? 5.930   -12.453 5.405   1.00 22.19 ? 61  TYR A CG  1 
ATOM   484  C CD1 . TYR A 1 62 ? 5.691   -13.793 5.635   1.00 21.09 ? 61  TYR A CD1 1 
ATOM   485  C CD2 . TYR A 1 62 ? 6.986   -11.835 6.071   1.00 27.44 ? 61  TYR A CD2 1 
ATOM   486  C CE1 . TYR A 1 62 ? 6.382   -14.536 6.603   1.00 24.42 ? 61  TYR A CE1 1 
ATOM   487  C CE2 . TYR A 1 62 ? 7.669   -12.566 7.028   1.00 26.24 ? 61  TYR A CE2 1 
ATOM   488  C CZ  . TYR A 1 62 ? 7.401   -13.889 7.277   1.00 26.47 ? 61  TYR A CZ  1 
ATOM   489  O OH  . TYR A 1 62 ? 8.153   -14.597 8.203   1.00 28.18 ? 61  TYR A OH  1 
ATOM   490  N N   . ASP A 1 63 ? 4.200   -9.372  6.239   1.00 23.59 ? 62  ASP A N   1 
ATOM   491  C CA  . ASP A 1 63 ? 4.330   -8.690  7.532   1.00 27.75 ? 62  ASP A CA  1 
ATOM   492  C C   . ASP A 1 63 ? 2.997   -8.641  8.280   1.00 28.22 ? 62  ASP A C   1 
ATOM   493  O O   . ASP A 1 63 ? 2.949   -9.102  9.418   1.00 34.95 ? 62  ASP A O   1 
ATOM   494  C CB  . ASP A 1 63 ? 5.094   -7.384  7.430   1.00 30.13 ? 62  ASP A CB  1 
ATOM   495  C CG  . ASP A 1 63 ? 6.449   -7.470  8.113   1.00 57.59 ? 62  ASP A CG  1 
ATOM   496  O OD1 . ASP A 1 63 ? 7.467   -7.429  7.395   1.00 61.60 ? 62  ASP A OD1 1 
ATOM   497  O OD2 . ASP A 1 63 ? 6.459   -7.617  9.368   1.00 59.36 ? 62  ASP A OD2 1 
ATOM   498  N N   . LYS A 1 64 ? 1.941   -8.206  7.588   1.00 29.82 ? 63  LYS A N   1 
ATOM   499  C CA  . LYS A 1 64 ? 0.604   -8.150  8.185   1.00 29.77 ? 63  LYS A CA  1 
ATOM   500  C C   . LYS A 1 64 ? 0.094   -9.521  8.629   1.00 31.23 ? 63  LYS A C   1 
ATOM   501  O O   . LYS A 1 64 ? -0.619  -9.601  9.631   1.00 29.95 ? 63  LYS A O   1 
ATOM   502  C CB  . LYS A 1 64 ? -0.376  -7.527  7.183   1.00 30.22 ? 63  LYS A CB  1 
ATOM   503  C CG  . LYS A 1 64 ? -1.821  -7.316  7.721   1.00 32.10 ? 63  LYS A CG  1 
ATOM   504  C CD  . LYS A 1 64 ? -2.577  -6.567  6.634   1.00 33.51 ? 63  LYS A CD  1 
ATOM   505  C CE  . LYS A 1 64 ? -3.631  -5.699  7.221   1.00 43.39 ? 63  LYS A CE  1 
ATOM   506  N NZ  . LYS A 1 64 ? -4.694  -6.397  7.938   1.00 42.43 ? 63  LYS A NZ  1 
ATOM   507  N N   . SER A 1 65 ? 0.410   -10.609 7.896   1.00 27.16 ? 64  SER A N   1 
ATOM   508  C CA  . SER A 1 65 ? -0.267  -11.891 7.990   1.00 27.34 ? 64  SER A CA  1 
ATOM   509  C C   . SER A 1 65 ? 0.505   -12.946 8.778   1.00 26.14 ? 64  SER A C   1 
ATOM   510  O O   . SER A 1 65 ? -0.005  -14.049 8.972   1.00 27.09 ? 64  SER A O   1 
ATOM   511  C CB  . SER A 1 65 ? -0.561  -12.432 6.606   1.00 29.04 ? 64  SER A CB  1 
ATOM   512  O OG  . SER A 1 65 ? -1.328  -11.458 5.924   1.00 34.02 ? 64  SER A OG  1 
ATOM   513  N N   . LYS A 1 66 ? 1.772   -12.678 9.128   1.00 26.48 ? 65  LYS A N   1 
ATOM   514  C CA  . LYS A 1 66 ? 2.583   -13.771 9.656   1.00 28.19 ? 65  LYS A CA  1 
ATOM   515  C C   . LYS A 1 66 ? 2.128   -14.280 11.024  1.00 26.42 ? 65  LYS A C   1 
ATOM   516  O O   . LYS A 1 66 ? 2.276   -15.466 11.314  1.00 29.76 ? 65  LYS A O   1 
ATOM   517  C CB  . LYS A 1 66 ? 4.070   -13.416 9.616   1.00 26.24 ? 65  LYS A CB  1 
ATOM   518  C CG  . LYS A 1 66 ? 4.454   -12.217 10.435  1.00 29.23 ? 65  LYS A CG  1 
ATOM   519  C CD  . LYS A 1 66 ? 5.950   -12.026 10.207  1.00 38.84 ? 65  LYS A CD  1 
ATOM   520  C CE  . LYS A 1 66 ? 6.455   -11.124 11.297  1.00 43.55 ? 65  LYS A CE  1 
ATOM   521  N NZ  . LYS A 1 66 ? 6.014   -9.753  11.028  1.00 49.83 ? 65  LYS A NZ  1 
ATOM   522  N N   A ASP A 1 67 ? 1.556   -13.384 11.838  0.50 30.73 ? 66  ASP A N   1 
ATOM   523  N N   B ASP A 1 67 ? 1.570   -13.379 11.844  0.50 30.18 ? 66  ASP A N   1 
ATOM   524  C CA  A ASP A 1 67 ? 1.057   -13.805 13.142  0.50 33.49 ? 66  ASP A CA  1 
ATOM   525  C CA  B ASP A 1 67 ? 1.044   -13.807 13.134  0.50 32.37 ? 66  ASP A CA  1 
ATOM   526  C C   A ASP A 1 67 ? -0.015  -14.885 12.978  0.50 35.46 ? 66  ASP A C   1 
ATOM   527  C C   B ASP A 1 67 ? 0.050   -14.946 12.917  0.50 34.72 ? 66  ASP A C   1 
ATOM   528  O O   A ASP A 1 67 ? -0.089  -15.828 13.753  0.50 36.19 ? 66  ASP A O   1 
ATOM   529  O O   B ASP A 1 67 ? 0.095   -15.971 13.587  0.50 35.22 ? 66  ASP A O   1 
ATOM   530  C CB  A ASP A 1 67 ? 0.657   -12.608 13.992  0.50 38.56 ? 66  ASP A CB  1 
ATOM   531  C CB  B ASP A 1 67 ? 0.377   -12.657 13.870  0.50 35.93 ? 66  ASP A CB  1 
ATOM   532  C CG  A ASP A 1 67 ? 1.816   -11.850 14.625  0.50 40.49 ? 66  ASP A CG  1 
ATOM   533  C CG  B ASP A 1 67 ? -0.023  -12.950 15.310  0.50 38.24 ? 66  ASP A CG  1 
ATOM   534  O OD1 A ASP A 1 67 ? 2.954   -12.372 14.581  0.50 46.23 ? 66  ASP A OD1 1 
ATOM   535  O OD1 B ASP A 1 67 ? 0.884   -13.024 16.164  0.50 39.53 ? 66  ASP A OD1 1 
ATOM   536  O OD2 A ASP A 1 67 ? 1.589   -10.741 15.147  0.50 43.80 ? 66  ASP A OD2 1 
ATOM   537  O OD2 B ASP A 1 67 ? -1.240  -13.095 15.565  0.50 45.81 ? 66  ASP A OD2 1 
ATOM   538  N N   . LYS A 1 68 ? -0.825  -14.778 11.919  1.00 30.68 ? 67  LYS A N   1 
ATOM   539  C CA  . LYS A 1 68 ? -1.900  -15.717 11.682  1.00 29.54 ? 67  LYS A CA  1 
ATOM   540  C C   . LYS A 1 68 ? -1.444  -16.948 10.920  1.00 31.15 ? 67  LYS A C   1 
ATOM   541  O O   . LYS A 1 68 ? -1.937  -18.043 11.177  1.00 32.65 ? 67  LYS A O   1 
ATOM   542  C CB  . LYS A 1 68 ? -3.000  -14.975 10.920  1.00 29.49 ? 67  LYS A CB  1 
ATOM   543  C CG  . LYS A 1 68 ? -4.265  -15.776 10.678  1.00 31.72 ? 67  LYS A CG  1 
ATOM   544  C CD  . LYS A 1 68 ? -5.300  -14.786 10.125  1.00 37.31 ? 67  LYS A CD  1 
ATOM   545  C CE  . LYS A 1 68 ? -6.672  -15.341 9.859   1.00 45.75 ? 67  LYS A CE  1 
ATOM   546  N NZ  . LYS A 1 68 ? -7.511  -14.297 9.235   1.00 38.99 ? 67  LYS A NZ  1 
ATOM   547  N N   . TYR A 1 69 ? -0.605  -16.756 9.876   1.00 26.66 ? 68  TYR A N   1 
ATOM   548  C CA  . TYR A 1 69 ? -0.351  -17.853 8.952   1.00 26.34 ? 68  TYR A CA  1 
ATOM   549  C C   . TYR A 1 69 ? 1.030   -18.499 9.145   1.00 25.01 ? 68  TYR A C   1 
ATOM   550  O O   . TYR A 1 69 ? 1.257   -19.587 8.599   1.00 27.84 ? 68  TYR A O   1 
ATOM   551  C CB  . TYR A 1 69 ? -0.510  -17.340 7.508   1.00 23.66 ? 68  TYR A CB  1 
ATOM   552  C CG  . TYR A 1 69 ? -1.915  -16.905 7.116   1.00 25.96 ? 68  TYR A CG  1 
ATOM   553  C CD1 . TYR A 1 69 ? -3.019  -17.649 7.520   1.00 27.14 ? 68  TYR A CD1 1 
ATOM   554  C CD2 . TYR A 1 69 ? -2.101  -15.723 6.396   1.00 25.48 ? 68  TYR A CD2 1 
ATOM   555  C CE1 . TYR A 1 69 ? -4.299  -17.243 7.148   1.00 28.11 ? 68  TYR A CE1 1 
ATOM   556  C CE2 . TYR A 1 69 ? -3.370  -15.305 6.033   1.00 28.21 ? 68  TYR A CE2 1 
ATOM   557  C CZ  . TYR A 1 69 ? -4.462  -16.068 6.427   1.00 29.51 ? 68  TYR A CZ  1 
ATOM   558  O OH  . TYR A 1 69 ? -5.701  -15.645 6.031   1.00 29.99 ? 68  TYR A OH  1 
ATOM   559  N N   . GLY A 1 70 ? 1.888   -17.854 9.933   1.00 28.03 ? 69  GLY A N   1 
ATOM   560  C CA  . GLY A 1 70 ? 3.292   -18.260 10.017  1.00 26.50 ? 69  GLY A CA  1 
ATOM   561  C C   . GLY A 1 70 ? 3.531   -19.230 11.183  1.00 30.97 ? 69  GLY A C   1 
ATOM   562  O O   . GLY A 1 70 ? 4.255   -18.927 12.099  1.00 36.75 ? 69  GLY A O   1 
ATOM   563  N N   . LYS A 1 71 ? 2.870   -20.363 11.135  1.00 31.97 ? 70  LYS A N   1 
ATOM   564  C CA  . LYS A 1 71 ? 2.946   -21.402 12.156  1.00 33.21 ? 70  LYS A CA  1 
ATOM   565  C C   . LYS A 1 71 ? 3.181   -22.734 11.451  1.00 33.37 ? 70  LYS A C   1 
ATOM   566  O O   . LYS A 1 71 ? 2.778   -22.955 10.311  1.00 33.57 ? 70  LYS A O   1 
ATOM   567  C CB  . LYS A 1 71 ? 1.700   -21.414 13.058  1.00 39.72 ? 70  LYS A CB  1 
ATOM   568  C CG  . LYS A 1 71 ? 1.643   -20.179 13.967  1.00 43.45 ? 70  LYS A CG  1 
ATOM   569  C CD  . LYS A 1 71 ? 0.446   -20.109 14.909  1.00 51.33 ? 70  LYS A CD  1 
ATOM   570  N N   . PRO A 1 72 ? 3.882   -23.704 12.086  1.00 35.24 ? 71  PRO A N   1 
ATOM   571  C CA  . PRO A 1 72 ? 4.176   -24.956 11.390  1.00 33.06 ? 71  PRO A CA  1 
ATOM   572  C C   . PRO A 1 72 ? 2.937   -25.687 10.909  1.00 34.05 ? 71  PRO A C   1 
ATOM   573  O O   . PRO A 1 72 ? 1.868   -25.544 11.501  1.00 41.69 ? 71  PRO A O   1 
ATOM   574  C CB  . PRO A 1 72 ? 4.988   -25.786 12.416  1.00 39.51 ? 71  PRO A CB  1 
ATOM   575  C CG  . PRO A 1 72 ? 5.510   -24.747 13.376  1.00 39.86 ? 71  PRO A CG  1 
ATOM   576  C CD  . PRO A 1 72 ? 4.466   -23.616 13.431  1.00 40.86 ? 71  PRO A CD  1 
ATOM   577  N N   . ASN A 1 73 ? 3.106   -26.463 9.843   1.00 36.87 ? 72  ASN A N   1 
ATOM   578  C CA  . ASN A 1 73 ? 2.035   -27.189 9.199   1.00 38.03 ? 72  ASN A CA  1 
ATOM   579  C C   . ASN A 1 73 ? 2.632   -28.524 8.787   1.00 48.48 ? 72  ASN A C   1 
ATOM   580  O O   . ASN A 1 73 ? 3.822   -28.613 8.481   1.00 45.99 ? 72  ASN A O   1 
ATOM   581  C CB  . ASN A 1 73 ? 1.524   -26.400 7.991   1.00 40.28 ? 72  ASN A CB  1 
ATOM   582  C CG  . ASN A 1 73 ? 0.199   -26.885 7.449   1.00 47.83 ? 72  ASN A CG  1 
ATOM   583  O OD1 . ASN A 1 73 ? 0.163   -27.770 6.585   1.00 47.60 ? 72  ASN A OD1 1 
ATOM   584  N ND2 . ASN A 1 73 ? -0.891  -26.271 7.885   1.00 45.76 ? 72  ASN A ND2 1 
ATOM   585  N N   . LYS A 1 74 ? 1.789   -29.552 8.789   1.00 50.74 ? 73  LYS A N   1 
ATOM   586  C CA  . LYS A 1 74 ? 2.194   -30.901 8.453   1.00 48.38 ? 73  LYS A CA  1 
ATOM   587  C C   . LYS A 1 74 ? 2.547   -31.028 6.971   1.00 43.59 ? 73  LYS A C   1 
ATOM   588  O O   . LYS A 1 74 ? 3.218   -31.979 6.574   1.00 44.09 ? 73  LYS A O   1 
ATOM   589  C CB  . LYS A 1 74 ? 1.041   -31.820 8.893   1.00 53.58 ? 73  LYS A CB  1 
ATOM   590  C CG  . LYS A 1 74 ? -0.176  -31.940 7.962   1.00 55.64 ? 73  LYS A CG  1 
ATOM   591  N N   . ARG A 1 75 ? 2.073   -30.100 6.127   1.00 41.60 ? 74  ARG A N   1 
ATOM   592  C CA  . ARG A 1 75 ? 2.155   -30.311 4.687   1.00 39.43 ? 74  ARG A CA  1 
ATOM   593  C C   . ARG A 1 75 ? 3.604   -30.287 4.204   1.00 36.18 ? 74  ARG A C   1 
ATOM   594  O O   . ARG A 1 75 ? 4.401   -29.514 4.738   1.00 33.60 ? 74  ARG A O   1 
ATOM   595  C CB  . ARG A 1 75 ? 1.310   -29.262 3.951   1.00 43.21 ? 74  ARG A CB  1 
ATOM   596  C CG  . ARG A 1 75 ? -0.164  -29.475 4.263   1.00 53.19 ? 74  ARG A CG  1 
ATOM   597  C CD  . ARG A 1 75 ? -0.784  -30.576 3.424   1.00 46.13 ? 74  ARG A CD  1 
ATOM   598  N NE  . ARG A 1 75 ? -1.723  -29.955 2.484   1.00 60.65 ? 74  ARG A NE  1 
ATOM   599  C CZ  . ARG A 1 75 ? -2.919  -29.441 2.805   1.00 55.37 ? 74  ARG A CZ  1 
ATOM   600  N NH1 . ARG A 1 75 ? -3.699  -28.985 1.852   1.00 61.68 ? 74  ARG A NH1 1 
ATOM   601  N NH2 . ARG A 1 75 ? -3.361  -29.439 4.058   1.00 62.65 ? 74  ARG A NH2 1 
ATOM   602  N N   . LYS A 1 76 ? 3.880   -31.083 3.159   1.00 35.16 ? 75  LYS A N   1 
ATOM   603  C CA  . LYS A 1 76 ? 5.211   -31.261 2.598   1.00 36.02 ? 75  LYS A CA  1 
ATOM   604  C C   . LYS A 1 76 ? 5.792   -29.903 2.211   1.00 33.78 ? 75  LYS A C   1 
ATOM   605  O O   . LYS A 1 76 ? 5.231   -29.221 1.360   1.00 29.97 ? 75  LYS A O   1 
ATOM   606  C CB  . LYS A 1 76 ? 5.197   -32.156 1.354   1.00 39.04 ? 75  LYS A CB  1 
ATOM   607  C CG  . LYS A 1 76 ? 6.529   -32.533 0.700   1.00 41.41 ? 75  LYS A CG  1 
ATOM   608  C CD  . LYS A 1 76 ? 6.439   -33.579 -0.413  1.00 45.06 ? 75  LYS A CD  1 
ATOM   609  C CE  . LYS A 1 76 ? 7.771   -34.040 -0.917  1.00 52.21 ? 75  LYS A CE  1 
ATOM   610  N N   . GLY A 1 77 ? 6.942   -29.553 2.797   1.00 31.55 ? 76  GLY A N   1 
ATOM   611  C CA  . GLY A 1 77 ? 7.670   -28.383 2.325   1.00 29.22 ? 76  GLY A CA  1 
ATOM   612  C C   . GLY A 1 77 ? 7.324   -27.123 3.107   1.00 29.25 ? 76  GLY A C   1 
ATOM   613  O O   . GLY A 1 77 ? 8.032   -26.131 2.997   1.00 29.52 ? 76  GLY A O   1 
ATOM   614  N N   . PHE A 1 78 ? 6.257   -27.149 3.898   1.00 27.59 ? 77  PHE A N   1 
ATOM   615  C CA  . PHE A 1 78 ? 5.793   -25.936 4.541   1.00 27.96 ? 77  PHE A CA  1 
ATOM   616  C C   . PHE A 1 78 ? 6.795   -25.359 5.547   1.00 29.77 ? 77  PHE A C   1 
ATOM   617  O O   . PHE A 1 78 ? 7.053   -24.157 5.575   1.00 27.58 ? 77  PHE A O   1 
ATOM   618  C CB  . PHE A 1 78 ? 4.427   -26.230 5.162   1.00 29.13 ? 77  PHE A CB  1 
ATOM   619  C CG  . PHE A 1 78 ? 3.691   -24.949 5.542   1.00 27.56 ? 77  PHE A CG  1 
ATOM   620  C CD1 . PHE A 1 78 ? 3.926   -24.296 6.744   1.00 28.49 ? 77  PHE A CD1 1 
ATOM   621  C CD2 . PHE A 1 78 ? 2.741   -24.402 4.666   1.00 29.49 ? 77  PHE A CD2 1 
ATOM   622  C CE1 . PHE A 1 78 ? 3.260   -23.133 7.077   1.00 29.12 ? 77  PHE A CE1 1 
ATOM   623  C CE2 . PHE A 1 78 ? 2.025   -23.250 5.031   1.00 26.69 ? 77  PHE A CE2 1 
ATOM   624  C CZ  . PHE A 1 78 ? 2.287   -22.613 6.228   1.00 27.62 ? 77  PHE A CZ  1 
ATOM   625  N N   . ASN A 1 79 ? 7.304   -26.187 6.470   1.00 26.30 ? 78  ASN A N   1 
ATOM   626  C CA  . ASN A 1 79 ? 8.186   -25.666 7.510   1.00 26.45 ? 78  ASN A CA  1 
ATOM   627  C C   . ASN A 1 79 ? 9.543   -25.208 6.913   1.00 23.88 ? 78  ASN A C   1 
ATOM   628  O O   . ASN A 1 79 ? 10.102  -24.219 7.397   1.00 27.44 ? 78  ASN A O   1 
ATOM   629  C CB  . ASN A 1 79 ? 8.370   -26.717 8.610   1.00 27.19 ? 78  ASN A CB  1 
ATOM   630  C CG  . ASN A 1 79 ? 7.030   -27.041 9.240   1.00 36.48 ? 78  ASN A CG  1 
ATOM   631  O OD1 . ASN A 1 79 ? 6.109   -26.213 9.183   1.00 31.17 ? 78  ASN A OD1 1 
ATOM   632  N ND2 . ASN A 1 79 ? 6.917   -28.195 9.896   1.00 32.01 ? 78  ASN A ND2 1 
ATOM   633  N N   . GLU A 1 80 ? 10.045  -25.908 5.878   1.00 24.75 ? 79  GLU A N   1 
ATOM   634  C CA  . GLU A 1 80 ? 11.217  -25.425 5.148   1.00 26.13 ? 79  GLU A CA  1 
ATOM   635  C C   . GLU A 1 80 ? 10.871  -24.044 4.594   1.00 22.71 ? 79  GLU A C   1 
ATOM   636  O O   . GLU A 1 80 ? 11.683  -23.104 4.607   1.00 23.37 ? 79  GLU A O   1 
ATOM   637  C CB  . GLU A 1 80 ? 11.607  -26.313 3.960   1.00 26.97 ? 79  GLU A CB  1 
ATOM   638  C CG  . GLU A 1 80 ? 12.873  -25.872 3.218   1.00 27.61 ? 79  GLU A CG  1 
ATOM   639  C CD  . GLU A 1 80 ? 13.426  -26.938 2.267   1.00 36.34 ? 79  GLU A CD  1 
ATOM   640  O OE1 . GLU A 1 80 ? 12.761  -27.965 2.036   1.00 43.02 ? 79  GLU A OE1 1 
ATOM   641  O OE2 . GLU A 1 80 ? 14.530  -26.752 1.755   1.00 38.36 ? 79  GLU A OE2 1 
ATOM   642  N N   . GLY A 1 81 ? 9.634   -23.927 4.089   1.00 24.74 ? 80  GLY A N   1 
ATOM   643  C CA  . GLY A 1 81 ? 9.207   -22.647 3.518   1.00 25.14 ? 80  GLY A CA  1 
ATOM   644  C C   . GLY A 1 81 ? 9.173   -21.512 4.551   1.00 21.36 ? 80  GLY A C   1 
ATOM   645  O O   . GLY A 1 81 ? 9.489   -20.363 4.218   1.00 21.68 ? 80  GLY A O   1 
ATOM   646  N N   . LEU A 1 82 ? 8.734   -21.813 5.784   1.00 21.53 ? 81  LEU A N   1 
ATOM   647  C CA  . LEU A 1 82 ? 8.770   -20.825 6.837   1.00 23.72 ? 81  LEU A CA  1 
ATOM   648  C C   . LEU A 1 82 ? 10.210  -20.361 7.110   1.00 21.82 ? 81  LEU A C   1 
ATOM   649  O O   . LEU A 1 82 ? 10.413  -19.167 7.373   1.00 21.94 ? 81  LEU A O   1 
ATOM   650  C CB  . LEU A 1 82 ? 8.126   -21.376 8.111   1.00 25.51 ? 81  LEU A CB  1 
ATOM   651  C CG  . LEU A 1 82 ? 6.614   -21.654 8.036   1.00 26.55 ? 81  LEU A CG  1 
ATOM   652  C CD1 . LEU A 1 82 ? 6.241   -22.211 9.396   1.00 28.67 ? 81  LEU A CD1 1 
ATOM   653  C CD2 . LEU A 1 82 ? 5.826   -20.374 7.849   1.00 25.18 ? 81  LEU A CD2 1 
ATOM   654  N N   . TRP A 1 83 ? 11.175  -21.310 7.032   1.00 23.70 ? 82  TRP A N   1 
ATOM   655  C CA  . TRP A 1 83 ? 12.556  -20.937 7.298   1.00 24.15 ? 82  TRP A CA  1 
ATOM   656  C C   . TRP A 1 83 ? 13.010  -19.974 6.213   1.00 21.02 ? 82  TRP A C   1 
ATOM   657  O O   . TRP A 1 83 ? 13.678  -18.994 6.492   1.00 22.81 ? 82  TRP A O   1 
ATOM   658  C CB  . TRP A 1 83 ? 13.480  -22.177 7.424   1.00 22.51 ? 82  TRP A CB  1 
ATOM   659  C CG  . TRP A 1 83 ? 14.926  -21.788 7.685   1.00 23.38 ? 82  TRP A CG  1 
ATOM   660  C CD1 . TRP A 1 83 ? 15.546  -21.661 8.899   1.00 26.27 ? 82  TRP A CD1 1 
ATOM   661  C CD2 . TRP A 1 83 ? 15.899  -21.467 6.665   1.00 23.95 ? 82  TRP A CD2 1 
ATOM   662  N NE1 . TRP A 1 83 ? 16.850  -21.298 8.703   1.00 26.31 ? 82  TRP A NE1 1 
ATOM   663  C CE2 . TRP A 1 83 ? 17.081  -21.137 7.357   1.00 24.37 ? 82  TRP A CE2 1 
ATOM   664  C CE3 . TRP A 1 83 ? 15.871  -21.429 5.257   1.00 23.47 ? 82  TRP A CE3 1 
ATOM   665  C CZ2 . TRP A 1 83 ? 18.246  -20.786 6.683   1.00 24.76 ? 82  TRP A CZ2 1 
ATOM   666  C CZ3 . TRP A 1 83 ? 17.018  -21.040 4.584   1.00 26.14 ? 82  TRP A CZ3 1 
ATOM   667  C CH2 . TRP A 1 83 ? 18.193  -20.743 5.303   1.00 26.08 ? 82  TRP A CH2 1 
ATOM   668  N N   . GLU A 1 84 ? 12.716  -20.340 4.964   1.00 21.16 ? 83  GLU A N   1 
ATOM   669  C CA  . GLU A 1 84 ? 13.157  -19.588 3.820   1.00 20.33 ? 83  GLU A CA  1 
ATOM   670  C C   . GLU A 1 84 ? 12.674  -18.145 3.868   1.00 22.72 ? 83  GLU A C   1 
ATOM   671  O O   . GLU A 1 84 ? 13.413  -17.212 3.649   1.00 21.64 ? 83  GLU A O   1 
ATOM   672  C CB  . GLU A 1 84 ? 12.790  -20.227 2.497   1.00 20.15 ? 83  GLU A CB  1 
ATOM   673  C CG  . GLU A 1 84 ? 13.518  -21.550 2.328   1.00 21.36 ? 83  GLU A CG  1 
ATOM   674  C CD  . GLU A 1 84 ? 13.118  -22.325 1.073   1.00 24.53 ? 83  GLU A CD  1 
ATOM   675  O OE1 . GLU A 1 84 ? 12.177  -21.894 0.381   1.00 24.12 ? 83  GLU A OE1 1 
ATOM   676  O OE2 . GLU A 1 84 ? 13.741  -23.399 0.750   1.00 25.91 ? 83  GLU A OE2 1 
ATOM   677  N N   . ILE A 1 85 ? 11.357  -17.981 4.115   1.00 19.62 ? 84  ILE A N   1 
ATOM   678  C CA  . ILE A 1 85 ? 10.813  -16.644 3.984   1.00 19.35 ? 84  ILE A CA  1 
ATOM   679  C C   . ILE A 1 85 ? 11.338  -15.734 5.104   1.00 20.39 ? 84  ILE A C   1 
ATOM   680  O O   . ILE A 1 85 ? 11.489  -14.540 4.912   1.00 21.73 ? 84  ILE A O   1 
ATOM   681  C CB  . ILE A 1 85 ? 9.265   -16.704 3.983   1.00 19.60 ? 84  ILE A CB  1 
ATOM   682  C CG1 . ILE A 1 85 ? 8.673   -15.326 3.555   1.00 18.75 ? 84  ILE A CG1 1 
ATOM   683  C CG2 . ILE A 1 85 ? 8.722   -17.080 5.383   1.00 21.33 ? 84  ILE A CG2 1 
ATOM   684  C CD1 . ILE A 1 85 ? 7.206   -15.420 3.049   1.00 18.56 ? 84  ILE A CD1 1 
ATOM   685  N N   . GLN A 1 86 ? 11.642  -16.335 6.274   1.00 21.04 ? 85  GLN A N   1 
ATOM   686  C CA  . GLN A 1 86 ? 12.198  -15.574 7.406   1.00 23.71 ? 85  GLN A CA  1 
ATOM   687  C C   . GLN A 1 86 ? 13.703  -15.299 7.263   1.00 23.33 ? 85  GLN A C   1 
ATOM   688  O O   . GLN A 1 86 ? 14.155  -14.183 7.640   1.00 27.08 ? 85  GLN A O   1 
ATOM   689  C CB  . GLN A 1 86 ? 11.843  -16.332 8.688   1.00 25.64 ? 85  GLN A CB  1 
ATOM   690  C CG  . GLN A 1 86 ? 12.380  -15.677 9.958   1.00 29.74 ? 85  GLN A CG  1 
ATOM   691  C CD  . GLN A 1 86 ? 11.749  -16.229 11.235  1.00 36.89 ? 85  GLN A CD  1 
ATOM   692  O OE1 . GLN A 1 86 ? 11.422  -17.427 11.348  1.00 36.29 ? 85  GLN A OE1 1 
ATOM   693  N NE2 . GLN A 1 86 ? 11.508  -15.337 12.191  1.00 40.12 ? 85  GLN A NE2 1 
ATOM   694  N N   . ASN A 1 87 ? 14.454  -16.271 6.715   1.00 20.70 ? 86  ASN A N   1 
ATOM   695  C CA  . ASN A 1 87 ? 15.932  -16.254 6.808   1.00 20.57 ? 86  ASN A CA  1 
ATOM   696  C C   . ASN A 1 87 ? 16.658  -15.913 5.512   1.00 23.00 ? 86  ASN A C   1 
ATOM   697  O O   . ASN A 1 87 ? 17.763  -15.354 5.576   1.00 23.80 ? 86  ASN A O   1 
ATOM   698  C CB  . ASN A 1 87 ? 16.450  -17.549 7.431   1.00 22.16 ? 86  ASN A CB  1 
ATOM   699  C CG  . ASN A 1 87 ? 15.982  -17.637 8.869   1.00 24.69 ? 86  ASN A CG  1 
ATOM   700  O OD1 . ASN A 1 87 ? 16.354  -16.771 9.681   1.00 30.29 ? 86  ASN A OD1 1 
ATOM   701  N ND2 . ASN A 1 87 ? 15.023  -18.498 9.181   1.00 24.22 ? 86  ASN A ND2 1 
ATOM   702  N N   . ASN A 1 88 ? 16.096  -16.243 4.343   1.00 20.80 ? 87  ASN A N   1 
ATOM   703  C CA  . ASN A 1 88 ? 16.728  -15.894 3.087   1.00 19.15 ? 87  ASN A CA  1 
ATOM   704  C C   . ASN A 1 88 ? 15.674  -15.838 1.979   1.00 20.71 ? 87  ASN A C   1 
ATOM   705  O O   . ASN A 1 88 ? 15.689  -16.548 0.972   1.00 20.75 ? 87  ASN A O   1 
ATOM   706  C CB  . ASN A 1 88 ? 17.928  -16.813 2.790   1.00 22.80 ? 87  ASN A CB  1 
ATOM   707  C CG  . ASN A 1 88 ? 18.969  -16.187 1.884   1.00 23.16 ? 87  ASN A CG  1 
ATOM   708  O OD1 . ASN A 1 88 ? 18.737  -15.176 1.204   1.00 21.81 ? 87  ASN A OD1 1 
ATOM   709  N ND2 . ASN A 1 88 ? 20.207  -16.718 1.885   1.00 26.82 ? 87  ASN A ND2 1 
ATOM   710  N N   . PRO A 1 89 ? 14.740  -14.875 2.083   1.00 19.58 ? 88  PRO A N   1 
ATOM   711  C CA  . PRO A 1 89 ? 13.604  -14.861 1.161   1.00 20.16 ? 88  PRO A CA  1 
ATOM   712  C C   . PRO A 1 89 ? 13.966  -14.409 -0.244  1.00 22.88 ? 88  PRO A C   1 
ATOM   713  O O   . PRO A 1 89 ? 13.198  -14.675 -1.144  1.00 21.05 ? 88  PRO A O   1 
ATOM   714  C CB  . PRO A 1 89 ? 12.677  -13.880 1.831   1.00 19.76 ? 88  PRO A CB  1 
ATOM   715  C CG  . PRO A 1 89 ? 13.619  -12.911 2.519   1.00 20.26 ? 88  PRO A CG  1 
ATOM   716  C CD  . PRO A 1 89 ? 14.652  -13.859 3.141   1.00 20.24 ? 88  PRO A CD  1 
ATOM   717  N N   . HIS A 1 90 ? 15.187  -13.832 -0.444  1.00 17.82 ? 89  HIS A N   1 
ATOM   718  C CA  . HIS A 1 90 ? 15.511  -13.323 -1.775  1.00 19.52 ? 89  HIS A CA  1 
ATOM   719  C C   . HIS A 1 90 ? 16.658  -14.120 -2.447  1.00 19.14 ? 89  HIS A C   1 
ATOM   720  O O   . HIS A 1 90 ? 17.073  -13.754 -3.552  1.00 22.20 ? 89  HIS A O   1 
ATOM   721  C CB  . HIS A 1 90 ? 15.891  -11.831 -1.650  1.00 19.23 ? 89  HIS A CB  1 
ATOM   722  C CG  . HIS A 1 90 ? 14.836  -10.951 -1.053  1.00 18.23 ? 89  HIS A CG  1 
ATOM   723  N ND1 . HIS A 1 90 ? 13.595  -10.865 -1.673  1.00 20.84 ? 89  HIS A ND1 1 
ATOM   724  C CD2 . HIS A 1 90 ? 14.776  -10.226 0.047   1.00 17.99 ? 89  HIS A CD2 1 
ATOM   725  C CE1 . HIS A 1 90 ? 12.813  -10.057 -0.972  1.00 20.01 ? 89  HIS A CE1 1 
ATOM   726  N NE2 . HIS A 1 90 ? 13.484  -9.660  0.106   1.00 20.91 ? 89  HIS A NE2 1 
ATOM   727  N N   . ALA A 1 91 ? 16.915  -15.309 -1.946  1.00 20.03 ? 90  ALA A N   1 
ATOM   728  C CA  . ALA A 1 91 ? 17.975  -16.152 -2.501  1.00 20.83 ? 90  ALA A CA  1 
ATOM   729  C C   . ALA A 1 91 ? 17.482  -16.852 -3.766  1.00 24.81 ? 90  ALA A C   1 
ATOM   730  O O   . ALA A 1 91 ? 16.289  -16.995 -4.037  1.00 23.92 ? 90  ALA A O   1 
ATOM   731  C CB  . ALA A 1 91 ? 18.422  -17.151 -1.471  1.00 22.87 ? 90  ALA A CB  1 
ATOM   732  N N   . SER A 1 92 ? 18.451  -17.418 -4.492  1.00 26.32 ? 91  SER A N   1 
ATOM   733  C CA  . SER A 1 92 ? 18.197  -18.328 -5.580  1.00 27.61 ? 91  SER A CA  1 
ATOM   734  C C   . SER A 1 92 ? 17.934  -19.716 -5.005  1.00 28.65 ? 91  SER A C   1 
ATOM   735  O O   . SER A 1 92 ? 18.759  -20.242 -4.244  1.00 30.50 ? 91  SER A O   1 
ATOM   736  C CB  . SER A 1 92 ? 19.423  -18.311 -6.435  1.00 31.74 ? 91  SER A CB  1 
ATOM   737  O OG  . SER A 1 92 ? 19.274  -19.328 -7.398  1.00 37.75 ? 91  SER A OG  1 
ATOM   738  N N   . TYR A 1 93 ? 16.759  -20.292 -5.325  1.00 26.80 ? 92  TYR A N   1 
ATOM   739  C CA  . TYR A 1 93 ? 16.389  -21.634 -4.908  1.00 27.47 ? 92  TYR A CA  1 
ATOM   740  C C   . TYR A 1 93 ? 16.281  -22.598 -6.090  1.00 31.91 ? 92  TYR A C   1 
ATOM   741  O O   . TYR A 1 93 ? 15.808  -23.715 -5.914  1.00 41.30 ? 92  TYR A O   1 
ATOM   742  C CB  . TYR A 1 93 ? 15.043  -21.580 -4.163  1.00 25.63 ? 92  TYR A CB  1 
ATOM   743  C CG  . TYR A 1 93 ? 15.215  -20.974 -2.779  1.00 25.18 ? 92  TYR A CG  1 
ATOM   744  C CD1 . TYR A 1 93 ? 15.653  -21.751 -1.685  1.00 25.27 ? 92  TYR A CD1 1 
ATOM   745  C CD2 . TYR A 1 93 ? 14.880  -19.632 -2.540  1.00 23.69 ? 92  TYR A CD2 1 
ATOM   746  C CE1 . TYR A 1 93 ? 15.816  -21.183 -0.425  1.00 28.69 ? 92  TYR A CE1 1 
ATOM   747  C CE2 . TYR A 1 93 ? 15.016  -19.076 -1.289  1.00 25.93 ? 92  TYR A CE2 1 
ATOM   748  C CZ  . TYR A 1 93 ? 15.512  -19.840 -0.245  1.00 25.57 ? 92  TYR A CZ  1 
ATOM   749  O OH  . TYR A 1 93 ? 15.737  -19.332 0.997   1.00 25.99 ? 92  TYR A OH  1 
ATOM   750  N N   . SER A 1 94 ? 16.690  -22.148 -7.275  1.00 40.94 ? 93  SER A N   1 
ATOM   751  C CA  . SER A 1 94 ? 16.859  -22.977 -8.460  1.00 52.82 ? 93  SER A CA  1 
ATOM   752  C C   . SER A 1 94 ? 17.895  -24.082 -8.196  1.00 65.73 ? 93  SER A C   1 
ATOM   753  O O   . SER A 1 94 ? 18.831  -23.828 -7.398  1.00 63.76 ? 93  SER A O   1 
ATOM   754  C CB  . SER A 1 94 ? 17.286  -22.122 -9.626  1.00 51.58 ? 93  SER A CB  1 
ATOM   755  O OG  . SER A 1 94 ? 16.249  -21.224 -10.000 1.00 59.98 ? 93  SER A OG  1 
ATOM   756  O OXT . SER A 1 94 ? 17.748  -25.163 -8.818  1.00 84.71 ? 93  SER A OXT 1 
ATOM   757  N N   . MET B 1 2  ? 38.867  -11.233 -42.127 1.00 61.79 ? 1   MET B N   1 
ATOM   758  C CA  . MET B 1 2  ? 38.460  -12.105 -43.259 1.00 60.37 ? 1   MET B CA  1 
ATOM   759  C C   . MET B 1 2  ? 36.932  -12.181 -43.253 1.00 52.55 ? 1   MET B C   1 
ATOM   760  O O   . MET B 1 2  ? 36.344  -12.380 -42.185 1.00 55.01 ? 1   MET B O   1 
ATOM   761  C CB  . MET B 1 2  ? 39.103  -13.492 -43.103 1.00 64.31 ? 1   MET B CB  1 
ATOM   762  C CG  . MET B 1 2  ? 39.167  -14.352 -44.365 1.00 79.21 ? 1   MET B CG  1 
ATOM   763  S SD  . MET B 1 2  ? 40.208  -13.801 -45.739 1.00 81.66 ? 1   MET B SD  1 
ATOM   764  C CE  . MET B 1 2  ? 41.563  -12.904 -44.968 1.00 66.62 ? 1   MET B CE  1 
ATOM   765  N N   . PRO B 1 3  ? 36.239  -11.972 -44.406 1.00 43.84 ? 2   PRO B N   1 
ATOM   766  C CA  . PRO B 1 3  ? 34.792  -12.200 -44.479 1.00 41.49 ? 2   PRO B CA  1 
ATOM   767  C C   . PRO B 1 3  ? 34.454  -13.644 -44.098 1.00 47.21 ? 2   PRO B C   1 
ATOM   768  O O   . PRO B 1 3  ? 35.250  -14.550 -44.324 1.00 45.08 ? 2   PRO B O   1 
ATOM   769  C CB  . PRO B 1 3  ? 34.388  -11.855 -45.913 1.00 41.93 ? 2   PRO B CB  1 
ATOM   770  C CG  . PRO B 1 3  ? 35.527  -10.959 -46.389 1.00 39.43 ? 2   PRO B CG  1 
ATOM   771  C CD  . PRO B 1 3  ? 36.785  -11.453 -45.674 1.00 41.24 ? 2   PRO B CD  1 
ATOM   772  N N   . HIS B 1 4  ? 33.294  -13.825 -43.454 1.00 44.72 ? 3   HIS B N   1 
ATOM   773  C CA  . HIS B 1 4  ? 32.839  -15.145 -43.030 1.00 43.11 ? 3   HIS B CA  1 
ATOM   774  C C   . HIS B 1 4  ? 31.473  -15.427 -43.646 1.00 42.36 ? 3   HIS B C   1 
ATOM   775  O O   . HIS B 1 4  ? 30.892  -14.561 -44.308 1.00 40.61 ? 3   HIS B O   1 
ATOM   776  C CB  . HIS B 1 4  ? 32.898  -15.287 -41.508 1.00 43.94 ? 3   HIS B CB  1 
ATOM   777  C CG  . HIS B 1 4  ? 34.308  -15.438 -41.025 1.00 57.32 ? 3   HIS B CG  1 
ATOM   778  N ND1 . HIS B 1 4  ? 35.188  -16.337 -41.601 1.00 55.68 ? 3   HIS B ND1 1 
ATOM   779  C CD2 . HIS B 1 4  ? 34.989  -14.829 -40.028 1.00 56.03 ? 3   HIS B CD2 1 
ATOM   780  C CE1 . HIS B 1 4  ? 36.360  -16.261 -40.974 1.00 53.61 ? 3   HIS B CE1 1 
ATOM   781  N NE2 . HIS B 1 4  ? 36.262  -15.355 -40.017 1.00 56.61 ? 3   HIS B NE2 1 
ATOM   782  N N   . ALA B 1 5  ? 30.960  -16.647 -43.436 1.00 39.29 ? 4   ALA B N   1 
ATOM   783  C CA  . ALA B 1 5  ? 29.658  -16.981 -43.987 1.00 38.00 ? 4   ALA B CA  1 
ATOM   784  C C   . ALA B 1 5  ? 28.657  -15.946 -43.503 1.00 38.70 ? 4   ALA B C   1 
ATOM   785  O O   . ALA B 1 5  ? 27.787  -15.512 -44.246 1.00 39.82 ? 4   ALA B O   1 
ATOM   786  C CB  . ALA B 1 5  ? 29.231  -18.348 -43.494 1.00 37.56 ? 4   ALA B CB  1 
ATOM   787  N N   . PHE B 1 6  ? 28.757  -15.645 -42.207 1.00 39.74 ? 5   PHE B N   1 
ATOM   788  C CA  . PHE B 1 6  ? 27.917  -14.632 -41.583 1.00 41.72 ? 5   PHE B CA  1 
ATOM   789  C C   . PHE B 1 6  ? 28.737  -13.369 -41.328 1.00 36.14 ? 5   PHE B C   1 
ATOM   790  O O   . PHE B 1 6  ? 29.856  -13.438 -40.828 1.00 41.19 ? 5   PHE B O   1 
ATOM   791  C CB  . PHE B 1 6  ? 27.381  -15.109 -40.232 1.00 38.66 ? 5   PHE B CB  1 
ATOM   792  C CG  . PHE B 1 6  ? 26.272  -16.149 -40.319 1.00 33.87 ? 5   PHE B CG  1 
ATOM   793  C CD1 . PHE B 1 6  ? 24.954  -15.769 -40.525 1.00 30.79 ? 5   PHE B CD1 1 
ATOM   794  C CD2 . PHE B 1 6  ? 26.555  -17.510 -40.221 1.00 35.71 ? 5   PHE B CD2 1 
ATOM   795  C CE1 . PHE B 1 6  ? 23.955  -16.721 -40.600 1.00 33.84 ? 5   PHE B CE1 1 
ATOM   796  C CE2 . PHE B 1 6  ? 25.534  -18.453 -40.292 1.00 30.03 ? 5   PHE B CE2 1 
ATOM   797  C CZ  . PHE B 1 6  ? 24.243  -18.069 -40.463 1.00 31.27 ? 5   PHE B CZ  1 
ATOM   798  N N   . LYS B 1 7  ? 28.159  -12.221 -41.670 1.00 40.26 ? 6   LYS B N   1 
ATOM   799  C CA  . LYS B 1 7  ? 28.884  -10.976 -41.455 1.00 39.07 ? 6   LYS B CA  1 
ATOM   800  C C   . LYS B 1 7  ? 28.147  -10.130 -40.414 1.00 37.35 ? 6   LYS B C   1 
ATOM   801  O O   . LYS B 1 7  ? 26.922  -10.229 -40.265 1.00 33.54 ? 6   LYS B O   1 
ATOM   802  C CB  . LYS B 1 7  ? 28.994  -10.236 -42.789 1.00 42.42 ? 6   LYS B CB  1 
ATOM   803  C CG  . LYS B 1 7  ? 27.687  -9.872  -43.445 1.00 42.45 ? 6   LYS B CG  1 
ATOM   804  C CD  . LYS B 1 7  ? 27.880  -9.344  -44.866 1.00 51.19 ? 6   LYS B CD  1 
ATOM   805  C CE  . LYS B 1 7  ? 26.597  -8.971  -45.539 1.00 52.81 ? 6   LYS B CE  1 
ATOM   806  N NZ  . LYS B 1 7  ? 25.803  -10.146 -45.919 1.00 48.85 ? 6   LYS B NZ  1 
ATOM   807  N N   . PRO B 1 8  ? 28.844  -9.184  -39.749 1.00 40.37 ? 7   PRO B N   1 
ATOM   808  C CA  . PRO B 1 8  ? 28.199  -8.237  -38.830 1.00 33.78 ? 7   PRO B CA  1 
ATOM   809  C C   . PRO B 1 8  ? 27.030  -7.534  -39.488 1.00 32.86 ? 7   PRO B C   1 
ATOM   810  O O   . PRO B 1 8  ? 27.121  -7.057  -40.636 1.00 36.41 ? 7   PRO B O   1 
ATOM   811  C CB  . PRO B 1 8  ? 29.364  -7.294  -38.545 1.00 40.77 ? 7   PRO B CB  1 
ATOM   812  C CG  . PRO B 1 8  ? 30.573  -8.220  -38.589 1.00 40.81 ? 7   PRO B CG  1 
ATOM   813  C CD  . PRO B 1 8  ? 30.289  -8.918  -39.897 1.00 44.63 ? 7   PRO B CD  1 
ATOM   814  N N   . GLY B 1 9  ? 25.899  -7.493  -38.767 1.00 28.32 ? 8   GLY B N   1 
ATOM   815  C CA  . GLY B 1 9  ? 24.671  -6.878  -39.233 1.00 29.44 ? 8   GLY B CA  1 
ATOM   816  C C   . GLY B 1 9  ? 23.703  -7.857  -39.880 1.00 26.24 ? 8   GLY B C   1 
ATOM   817  O O   . GLY B 1 9  ? 22.564  -7.504  -40.192 1.00 29.12 ? 8   GLY B O   1 
ATOM   818  N N   . ASP B 1 10 ? 24.177  -9.088  -40.173 1.00 28.63 ? 9   ASP B N   1 
ATOM   819  C CA  . ASP B 1 10 ? 23.284  -10.103 -40.706 1.00 32.59 ? 9   ASP B CA  1 
ATOM   820  C C   . ASP B 1 10 ? 22.215  -10.453 -39.657 1.00 24.79 ? 9   ASP B C   1 
ATOM   821  O O   . ASP B 1 10 ? 22.517  -10.480 -38.453 1.00 28.65 ? 9   ASP B O   1 
ATOM   822  C CB  . ASP B 1 10 ? 24.050  -11.371 -41.035 1.00 31.50 ? 9   ASP B CB  1 
ATOM   823  C CG  . ASP B 1 10 ? 24.755  -11.450 -42.384 1.00 39.78 ? 9   ASP B CG  1 
ATOM   824  O OD1 . ASP B 1 10 ? 24.427  -10.626 -43.251 1.00 36.33 ? 9   ASP B OD1 1 
ATOM   825  O OD2 . ASP B 1 10 ? 25.607  -12.374 -42.535 1.00 36.61 ? 9   ASP B OD2 1 
ATOM   826  N N   . LEU B 1 11 ? 20.994  -10.586 -40.127 1.00 25.53 ? 10  LEU B N   1 
ATOM   827  C CA  . LEU B 1 11 ? 19.841  -10.833 -39.253 1.00 25.85 ? 10  LEU B CA  1 
ATOM   828  C C   . LEU B 1 11 ? 19.581  -12.332 -39.237 1.00 26.97 ? 10  LEU B C   1 
ATOM   829  O O   . LEU B 1 11 ? 19.595  -12.952 -40.304 1.00 28.73 ? 10  LEU B O   1 
ATOM   830  C CB  . LEU B 1 11 ? 18.619  -10.020 -39.658 1.00 27.36 ? 10  LEU B CB  1 
ATOM   831  C CG  . LEU B 1 11 ? 18.904  -8.513  -39.807 1.00 25.82 ? 10  LEU B CG  1 
ATOM   832  C CD1 . LEU B 1 11 ? 17.611  -7.795  -40.150 1.00 26.82 ? 10  LEU B CD1 1 
ATOM   833  C CD2 . LEU B 1 11 ? 19.551  -8.002  -38.514 1.00 28.26 ? 10  LEU B CD2 1 
ATOM   834  N N   . VAL B 1 12 ? 19.222  -12.889 -38.061 1.00 24.79 ? 11  VAL B N   1 
ATOM   835  C CA  . VAL B 1 12 ? 19.021  -14.339 -37.968 1.00 23.23 ? 11  VAL B CA  1 
ATOM   836  C C   . VAL B 1 12 ? 17.908  -14.598 -36.952 1.00 24.79 ? 11  VAL B C   1 
ATOM   837  O O   . VAL B 1 12 ? 17.499  -13.691 -36.227 1.00 24.38 ? 11  VAL B O   1 
ATOM   838  C CB  . VAL B 1 12 ? 20.333  -15.023 -37.511 1.00 23.92 ? 11  VAL B CB  1 
ATOM   839  C CG1 . VAL B 1 12 ? 21.462  -14.853 -38.554 1.00 28.13 ? 11  VAL B CG1 1 
ATOM   840  C CG2 . VAL B 1 12 ? 20.813  -14.583 -36.107 1.00 24.37 ? 11  VAL B CG2 1 
ATOM   841  N N   . PHE B 1 13 ? 17.457  -15.857 -36.885 1.00 22.99 ? 12  PHE B N   1 
ATOM   842  C CA  . PHE B 1 13 ? 16.969  -16.375 -35.628 1.00 23.79 ? 12  PHE B CA  1 
ATOM   843  C C   . PHE B 1 13 ? 18.067  -17.242 -35.039 1.00 25.23 ? 12  PHE B C   1 
ATOM   844  O O   . PHE B 1 13 ? 18.698  -18.030 -35.780 1.00 25.65 ? 12  PHE B O   1 
ATOM   845  C CB  . PHE B 1 13 ? 15.715  -17.208 -35.891 1.00 22.79 ? 12  PHE B CB  1 
ATOM   846  C CG  . PHE B 1 13 ? 14.499  -16.388 -36.293 1.00 24.17 ? 12  PHE B CG  1 
ATOM   847  C CD1 . PHE B 1 13 ? 14.273  -16.068 -37.632 1.00 26.74 ? 12  PHE B CD1 1 
ATOM   848  C CD2 . PHE B 1 13 ? 13.608  -15.932 -35.334 1.00 27.32 ? 12  PHE B CD2 1 
ATOM   849  C CE1 . PHE B 1 13 ? 13.173  -15.316 -38.002 1.00 31.05 ? 12  PHE B CE1 1 
ATOM   850  C CE2 . PHE B 1 13 ? 12.500  -15.181 -35.708 1.00 27.74 ? 12  PHE B CE2 1 
ATOM   851  C CZ  . PHE B 1 13 ? 12.287  -14.870 -37.048 1.00 32.44 ? 12  PHE B CZ  1 
ATOM   852  N N   . ALA B 1 14 ? 18.272  -17.088 -33.716 1.00 23.31 ? 13  ALA B N   1 
ATOM   853  C CA  . ALA B 1 14 ? 19.321  -17.819 -33.046 1.00 22.74 ? 13  ALA B CA  1 
ATOM   854  C C   . ALA B 1 14 ? 18.718  -18.778 -32.015 1.00 22.36 ? 13  ALA B C   1 
ATOM   855  O O   . ALA B 1 14 ? 17.826  -18.391 -31.256 1.00 24.92 ? 13  ALA B O   1 
ATOM   856  C CB  . ALA B 1 14 ? 20.284  -16.856 -32.366 1.00 24.29 ? 13  ALA B CB  1 
ATOM   857  N N   . LYS B 1 15 ? 19.254  -19.989 -31.968 1.00 22.99 ? 14  LYS B N   1 
ATOM   858  C CA  . LYS B 1 15 ? 18.659  -21.022 -31.102 1.00 25.74 ? 14  LYS B CA  1 
ATOM   859  C C   . LYS B 1 15 ? 19.534  -21.291 -29.882 1.00 27.66 ? 14  LYS B C   1 
ATOM   860  O O   . LYS B 1 15 ? 20.729  -21.580 -30.004 1.00 27.79 ? 14  LYS B O   1 
ATOM   861  C CB  . LYS B 1 15 ? 18.478  -22.327 -31.899 1.00 27.81 ? 14  LYS B CB  1 
ATOM   862  C CG  . LYS B 1 15 ? 17.719  -23.430 -31.099 1.00 24.97 ? 14  LYS B CG  1 
ATOM   863  C CD  . LYS B 1 15 ? 16.241  -23.098 -30.926 1.00 28.60 ? 14  LYS B CD  1 
ATOM   864  C CE  . LYS B 1 15 ? 15.400  -24.212 -30.237 1.00 28.38 ? 14  LYS B CE  1 
ATOM   865  N NZ  . LYS B 1 15 ? 15.910  -24.375 -28.884 1.00 28.56 ? 14  LYS B NZ  1 
ATOM   866  N N   . MET B 1 16 ? 18.905  -21.157 -28.704 1.00 28.04 ? 15  MET B N   1 
ATOM   867  C CA  . MET B 1 16 ? 19.464  -21.469 -27.389 1.00 29.36 ? 15  MET B CA  1 
ATOM   868  C C   . MET B 1 16 ? 18.650  -22.616 -26.779 1.00 28.10 ? 15  MET B C   1 
ATOM   869  O O   . MET B 1 16 ? 17.415  -22.658 -26.901 1.00 27.64 ? 15  MET B O   1 
ATOM   870  C CB  . MET B 1 16 ? 19.423  -20.246 -26.462 1.00 33.02 ? 15  MET B CB  1 
ATOM   871  C CG  . MET B 1 16 ? 20.232  -19.058 -26.938 1.00 34.42 ? 15  MET B CG  1 
ATOM   872  S SD  . MET B 1 16 ? 22.015  -19.231 -26.726 1.00 37.88 ? 15  MET B SD  1 
ATOM   873  C CE  . MET B 1 16 ? 22.081  -18.929 -24.949 1.00 34.82 ? 15  MET B CE  1 
ATOM   874  N N   . LYS B 1 17 ? 19.365  -23.560 -26.145 1.00 29.38 ? 16  LYS B N   1 
ATOM   875  C CA  . LYS B 1 17 ? 18.678  -24.628 -25.425 1.00 30.73 ? 16  LYS B CA  1 
ATOM   876  C C   . LYS B 1 17 ? 17.703  -24.000 -24.418 1.00 26.61 ? 16  LYS B C   1 
ATOM   877  O O   . LYS B 1 17 ? 18.073  -23.098 -23.674 1.00 31.13 ? 16  LYS B O   1 
ATOM   878  C CB  . LYS B 1 17 ? 19.736  -25.509 -24.739 1.00 38.70 ? 16  LYS B CB  1 
ATOM   879  C CG  . LYS B 1 17 ? 19.141  -26.835 -24.224 1.00 42.88 ? 16  LYS B CG  1 
ATOM   880  C CD  . LYS B 1 17 ? 20.059  -27.612 -23.285 1.00 44.52 ? 16  LYS B CD  1 
ATOM   881  N N   . GLY B 1 18 ? 16.442  -24.441 -24.470 1.00 29.76 ? 17  GLY B N   1 
ATOM   882  C CA  . GLY B 1 18 ? 15.404  -23.975 -23.558 1.00 32.05 ? 17  GLY B CA  1 
ATOM   883  C C   . GLY B 1 18 ? 14.576  -22.803 -24.092 1.00 33.13 ? 17  GLY B C   1 
ATOM   884  O O   . GLY B 1 18 ? 13.615  -22.385 -23.441 1.00 32.72 ? 17  GLY B O   1 
ATOM   885  N N   . TYR B 1 19 ? 14.911  -22.291 -25.301 1.00 29.40 ? 18  TYR B N   1 
ATOM   886  C CA  . TYR B 1 19 ? 14.181  -21.135 -25.816 1.00 26.05 ? 18  TYR B CA  1 
ATOM   887  C C   . TYR B 1 19 ? 13.803  -21.375 -27.279 1.00 27.16 ? 18  TYR B C   1 
ATOM   888  O O   . TYR B 1 19 ? 14.509  -22.093 -27.980 1.00 30.59 ? 18  TYR B O   1 
ATOM   889  C CB  . TYR B 1 19 ? 15.081  -19.889 -25.767 1.00 25.53 ? 18  TYR B CB  1 
ATOM   890  C CG  . TYR B 1 19 ? 15.526  -19.617 -24.331 1.00 28.42 ? 18  TYR B CG  1 
ATOM   891  C CD1 . TYR B 1 19 ? 14.738  -18.848 -23.483 1.00 30.47 ? 18  TYR B CD1 1 
ATOM   892  C CD2 . TYR B 1 19 ? 16.671  -20.232 -23.819 1.00 29.70 ? 18  TYR B CD2 1 
ATOM   893  C CE1 . TYR B 1 19 ? 15.096  -18.686 -22.144 1.00 29.65 ? 18  TYR B CE1 1 
ATOM   894  C CE2 . TYR B 1 19 ? 17.044  -20.058 -22.487 1.00 33.30 ? 18  TYR B CE2 1 
ATOM   895  C CZ  . TYR B 1 19 ? 16.250  -19.277 -21.660 1.00 31.32 ? 18  TYR B CZ  1 
ATOM   896  O OH  . TYR B 1 19 ? 16.658  -19.127 -20.347 1.00 35.97 ? 18  TYR B OH  1 
ATOM   897  N N   . PRO B 1 20 ? 12.747  -20.705 -27.786 1.00 27.05 ? 19  PRO B N   1 
ATOM   898  C CA  . PRO B 1 20 ? 12.393  -20.778 -29.203 1.00 24.94 ? 19  PRO B CA  1 
ATOM   899  C C   . PRO B 1 20 ? 13.459  -20.031 -30.004 1.00 24.37 ? 19  PRO B C   1 
ATOM   900  O O   . PRO B 1 20 ? 14.125  -19.160 -29.483 1.00 26.25 ? 19  PRO B O   1 
ATOM   901  C CB  . PRO B 1 20 ? 11.061  -20.093 -29.323 1.00 26.22 ? 19  PRO B CB  1 
ATOM   902  C CG  . PRO B 1 20 ? 11.027  -19.142 -28.133 1.00 28.22 ? 19  PRO B CG  1 
ATOM   903  C CD  . PRO B 1 20 ? 11.813  -19.858 -27.026 1.00 26.84 ? 19  PRO B CD  1 
ATOM   904  N N   . HIS B 1 21 ? 13.605  -20.429 -31.277 1.00 23.91 ? 20  HIS B N   1 
ATOM   905  C CA  . HIS B 1 21 ? 14.428  -19.654 -32.227 1.00 25.53 ? 20  HIS B CA  1 
ATOM   906  C C   . HIS B 1 21 ? 14.140  -18.159 -32.061 1.00 23.44 ? 20  HIS B C   1 
ATOM   907  O O   . HIS B 1 21 ? 12.997  -17.732 -32.143 1.00 25.06 ? 20  HIS B O   1 
ATOM   908  C CB  . HIS B 1 21 ? 14.106  -20.142 -33.650 1.00 26.11 ? 20  HIS B CB  1 
ATOM   909  C CG  . HIS B 1 21 ? 14.342  -21.624 -33.847 1.00 26.65 ? 20  HIS B CG  1 
ATOM   910  N ND1 . HIS B 1 21 ? 13.454  -22.603 -33.410 1.00 28.25 ? 20  HIS B ND1 1 
ATOM   911  C CD2 . HIS B 1 21 ? 15.391  -22.301 -34.376 1.00 27.80 ? 20  HIS B CD2 1 
ATOM   912  C CE1 . HIS B 1 21 ? 13.938  -23.804 -33.716 1.00 28.29 ? 20  HIS B CE1 1 
ATOM   913  N NE2 . HIS B 1 21 ? 15.098  -23.660 -34.324 1.00 27.37 ? 20  HIS B NE2 1 
ATOM   914  N N   . TRP B 1 22 ? 15.192  -17.360 -31.913 1.00 23.20 ? 21  TRP B N   1 
ATOM   915  C CA  . TRP B 1 22 ? 14.978  -16.029 -31.343 1.00 22.35 ? 21  TRP B CA  1 
ATOM   916  C C   . TRP B 1 22 ? 15.485  -14.952 -32.307 1.00 23.06 ? 21  TRP B C   1 
ATOM   917  O O   . TRP B 1 22 ? 16.613  -15.082 -32.746 1.00 22.99 ? 21  TRP B O   1 
ATOM   918  C CB  . TRP B 1 22 ? 15.686  -15.952 -29.986 1.00 24.41 ? 21  TRP B CB  1 
ATOM   919  C CG  . TRP B 1 22 ? 15.166  -14.817 -29.129 1.00 23.57 ? 21  TRP B CG  1 
ATOM   920  C CD1 . TRP B 1 22 ? 15.437  -13.474 -29.249 1.00 24.16 ? 21  TRP B CD1 1 
ATOM   921  C CD2 . TRP B 1 22 ? 14.249  -14.949 -28.011 1.00 25.38 ? 21  TRP B CD2 1 
ATOM   922  N NE1 . TRP B 1 22 ? 14.699  -12.754 -28.314 1.00 25.89 ? 21  TRP B NE1 1 
ATOM   923  C CE2 . TRP B 1 22 ? 13.985  -13.639 -27.528 1.00 26.20 ? 21  TRP B CE2 1 
ATOM   924  C CE3 . TRP B 1 22 ? 13.627  -16.061 -27.405 1.00 27.66 ? 21  TRP B CE3 1 
ATOM   925  C CZ2 . TRP B 1 22 ? 13.129  -13.386 -26.451 1.00 26.42 ? 21  TRP B CZ2 1 
ATOM   926  C CZ3 . TRP B 1 22 ? 12.804  -15.812 -26.319 1.00 27.98 ? 21  TRP B CZ3 1 
ATOM   927  C CH2 . TRP B 1 22 ? 12.542  -14.502 -25.880 1.00 25.93 ? 21  TRP B CH2 1 
ATOM   928  N N   . PRO B 1 23 ? 14.731  -13.857 -32.581 1.00 24.31 ? 22  PRO B N   1 
ATOM   929  C CA  . PRO B 1 23 ? 15.224  -12.818 -33.506 1.00 22.14 ? 22  PRO B CA  1 
ATOM   930  C C   . PRO B 1 23 ? 16.525  -12.251 -32.972 1.00 23.31 ? 22  PRO B C   1 
ATOM   931  O O   . PRO B 1 23 ? 16.657  -11.889 -31.788 1.00 23.73 ? 22  PRO B O   1 
ATOM   932  C CB  . PRO B 1 23 ? 14.052  -11.778 -33.542 1.00 22.47 ? 22  PRO B CB  1 
ATOM   933  C CG  . PRO B 1 23 ? 13.351  -11.986 -32.168 1.00 24.07 ? 22  PRO B CG  1 
ATOM   934  C CD  . PRO B 1 23 ? 13.433  -13.507 -31.977 1.00 25.14 ? 22  PRO B CD  1 
ATOM   935  N N   . ALA B 1 24 ? 17.537  -12.135 -33.835 1.00 23.50 ? 23  ALA B N   1 
ATOM   936  C CA  . ALA B 1 24 ? 18.859  -11.770 -33.361 1.00 23.57 ? 23  ALA B CA  1 
ATOM   937  C C   . ALA B 1 24 ? 19.645  -11.200 -34.543 1.00 22.70 ? 23  ALA B C   1 
ATOM   938  O O   . ALA B 1 24 ? 19.158  -11.246 -35.675 1.00 25.04 ? 23  ALA B O   1 
ATOM   939  C CB  . ALA B 1 24 ? 19.569  -12.961 -32.729 1.00 25.05 ? 23  ALA B CB  1 
ATOM   940  N N   . ARG B 1 25 ? 20.833  -10.677 -34.206 1.00 24.78 ? 24  ARG B N   1 
ATOM   941  C CA  . ARG B 1 25 ? 21.771  -10.194 -35.214 1.00 24.16 ? 24  ARG B CA  1 
ATOM   942  C C   . ARG B 1 25 ? 23.167  -10.690 -34.874 1.00 25.03 ? 24  ARG B C   1 
ATOM   943  O O   . ARG B 1 25 ? 23.508  -10.947 -33.735 1.00 25.09 ? 24  ARG B O   1 
ATOM   944  C CB  . ARG B 1 25 ? 21.841  -8.668  -35.337 1.00 25.89 ? 24  ARG B CB  1 
ATOM   945  C CG  . ARG B 1 25 ? 22.363  -7.942  -34.107 1.00 25.59 ? 24  ARG B CG  1 
ATOM   946  C CD  . ARG B 1 25 ? 22.144  -6.423  -34.272 1.00 24.38 ? 24  ARG B CD  1 
ATOM   947  N NE  . ARG B 1 25 ? 22.814  -5.798  -33.135 1.00 27.43 ? 24  ARG B NE  1 
ATOM   948  C CZ  . ARG B 1 25 ? 22.535  -4.536  -32.758 1.00 29.32 ? 24  ARG B CZ  1 
ATOM   949  N NH1 . ARG B 1 25 ? 21.550  -3.869  -33.370 1.00 28.00 ? 24  ARG B NH1 1 
ATOM   950  N NH2 . ARG B 1 25 ? 23.217  -4.006  -31.741 1.00 27.36 ? 24  ARG B NH2 1 
ATOM   951  N N   . ILE B 1 26 ? 24.010  -10.797 -35.919 1.00 26.97 ? 25  ILE B N   1 
ATOM   952  C CA  . ILE B 1 26 ? 25.440  -10.950 -35.722 1.00 28.47 ? 25  ILE B CA  1 
ATOM   953  C C   . ILE B 1 26 ? 26.012  -9.571  -35.403 1.00 31.57 ? 25  ILE B C   1 
ATOM   954  O O   . ILE B 1 26 ? 25.742  -8.613  -36.132 1.00 31.58 ? 25  ILE B O   1 
ATOM   955  C CB  . ILE B 1 26 ? 26.075  -11.448 -37.036 1.00 32.40 ? 25  ILE B CB  1 
ATOM   956  C CG1 . ILE B 1 26 ? 25.331  -12.647 -37.615 1.00 31.73 ? 25  ILE B CG1 1 
ATOM   957  C CG2 . ILE B 1 26 ? 27.573  -11.696 -36.864 1.00 34.43 ? 25  ILE B CG2 1 
ATOM   958  C CD1 . ILE B 1 26 ? 25.420  -13.910 -36.793 1.00 31.61 ? 25  ILE B CD1 1 
ATOM   959  N N   . ASP B 1 27 ? 26.783  -9.526  -34.322 1.00 30.76 ? 26  ASP B N   1 
ATOM   960  C CA  . ASP B 1 27 ? 27.465  -8.305  -33.892 1.00 35.15 ? 26  ASP B CA  1 
ATOM   961  C C   . ASP B 1 27 ? 28.908  -8.297  -34.395 1.00 39.34 ? 26  ASP B C   1 
ATOM   962  O O   . ASP B 1 27 ? 29.418  -9.337  -34.790 1.00 41.76 ? 26  ASP B O   1 
ATOM   963  C CB  . ASP B 1 27 ? 27.456  -8.203  -32.379 1.00 30.99 ? 26  ASP B CB  1 
ATOM   964  C CG  . ASP B 1 27 ? 26.254  -7.472  -31.789 1.00 33.98 ? 26  ASP B CG  1 
ATOM   965  O OD1 . ASP B 1 27 ? 25.448  -6.915  -32.577 1.00 35.87 ? 26  ASP B OD1 1 
ATOM   966  O OD2 . ASP B 1 27 ? 26.163  -7.419  -30.532 1.00 33.08 ? 26  ASP B OD2 1 
ATOM   967  N N   A ASP B 1 28 ? 29.544  -7.119  -34.302 0.50 48.31 ? 27  ASP B N   1 
ATOM   968  N N   B ASP B 1 28 ? 29.565  -7.128  -34.358 0.50 47.36 ? 27  ASP B N   1 
ATOM   969  C CA  A ASP B 1 28 ? 30.967  -6.905  -34.533 0.50 53.42 ? 27  ASP B CA  1 
ATOM   970  C CA  B ASP B 1 28 ? 30.993  -7.044  -34.646 0.50 51.33 ? 27  ASP B CA  1 
ATOM   971  C C   A ASP B 1 28 ? 31.768  -7.404  -33.333 0.50 54.67 ? 27  ASP B C   1 
ATOM   972  C C   B ASP B 1 28 ? 31.772  -7.262  -33.347 0.50 54.18 ? 27  ASP B C   1 
ATOM   973  O O   A ASP B 1 28 ? 31.196  -7.787  -32.315 0.50 57.98 ? 27  ASP B O   1 
ATOM   974  O O   B ASP B 1 28 ? 31.181  -7.324  -32.271 0.50 58.76 ? 27  ASP B O   1 
ATOM   975  C CB  A ASP B 1 28 ? 31.267  -5.420  -34.668 0.50 49.74 ? 27  ASP B CB  1 
ATOM   976  C CB  B ASP B 1 28 ? 31.365  -5.731  -35.323 0.50 47.23 ? 27  ASP B CB  1 
ATOM   977  C CG  A ASP B 1 28 ? 30.445  -4.690  -35.717 0.50 49.06 ? 27  ASP B CG  1 
ATOM   978  C CG  B ASP B 1 28 ? 32.396  -5.833  -36.442 0.50 42.89 ? 27  ASP B CG  1 
ATOM   979  O OD1 A ASP B 1 28 ? 30.777  -4.823  -36.913 0.50 52.88 ? 27  ASP B OD1 1 
ATOM   980  O OD1 B ASP B 1 28 ? 33.329  -6.669  -36.330 0.50 45.13 ? 27  ASP B OD1 1 
ATOM   981  O OD2 A ASP B 1 28 ? 29.467  -4.019  -35.331 0.50 50.11 ? 27  ASP B OD2 1 
ATOM   982  O OD2 B ASP B 1 28 ? 32.279  -5.057  -37.414 0.50 43.56 ? 27  ASP B OD2 1 
ATOM   983  N N   . ILE B 1 29 ? 33.100  -7.380  -33.460 1.00 63.72 ? 28  ILE B N   1 
ATOM   984  C CA  . ILE B 1 29 ? 33.977  -7.602  -32.321 1.00 69.00 ? 28  ILE B CA  1 
ATOM   985  C C   . ILE B 1 29 ? 34.646  -6.260  -31.974 1.00 76.97 ? 28  ILE B C   1 
ATOM   986  O O   . ILE B 1 29 ? 34.741  -5.972  -30.744 1.00 83.18 ? 28  ILE B O   1 
ATOM   987  C CB  . ILE B 1 29 ? 35.005  -8.713  -32.603 1.00 64.91 ? 28  ILE B CB  1 
ATOM   988  N N   . VAL B 1 34 ? 36.916  -9.791  -25.501 1.00 65.43 ? 33  VAL B N   1 
ATOM   989  C CA  . VAL B 1 34 ? 36.650  -11.260 -25.426 1.00 68.82 ? 33  VAL B CA  1 
ATOM   990  C C   . VAL B 1 34 ? 36.175  -11.697 -26.803 1.00 73.18 ? 33  VAL B C   1 
ATOM   991  O O   . VAL B 1 34 ? 35.016  -11.480 -27.145 1.00 84.59 ? 33  VAL B O   1 
ATOM   992  C CB  . VAL B 1 34 ? 35.617  -11.633 -24.339 1.00 67.62 ? 33  VAL B CB  1 
ATOM   993  C CG1 . VAL B 1 34 ? 34.407  -10.700 -24.341 1.00 70.96 ? 33  VAL B CG1 1 
ATOM   994  C CG2 . VAL B 1 34 ? 35.181  -13.097 -24.428 1.00 56.75 ? 33  VAL B CG2 1 
ATOM   995  N N   . LYS B 1 35 ? 37.084  -12.284 -27.591 1.00 75.31 ? 34  LYS B N   1 
ATOM   996  C CA  . LYS B 1 35 ? 36.742  -12.765 -28.923 1.00 64.31 ? 34  LYS B CA  1 
ATOM   997  C C   . LYS B 1 35 ? 35.887  -14.032 -28.811 1.00 62.53 ? 34  LYS B C   1 
ATOM   998  O O   . LYS B 1 35 ? 35.986  -14.773 -27.830 1.00 60.49 ? 34  LYS B O   1 
ATOM   999  C CB  . LYS B 1 35 ? 38.011  -12.920 -29.769 1.00 65.31 ? 34  LYS B CB  1 
ATOM   1000 N N   . PRO B 1 36 ? 34.992  -14.319 -29.791 1.00 56.64 ? 35  PRO B N   1 
ATOM   1001 C CA  . PRO B 1 36 ? 34.205  -15.558 -29.760 1.00 54.67 ? 35  PRO B CA  1 
ATOM   1002 C C   . PRO B 1 36 ? 35.118  -16.774 -29.672 1.00 47.22 ? 35  PRO B C   1 
ATOM   1003 O O   . PRO B 1 36 ? 36.258  -16.701 -30.105 1.00 51.57 ? 35  PRO B O   1 
ATOM   1004 C CB  . PRO B 1 36 ? 33.419  -15.541 -31.082 1.00 52.96 ? 35  PRO B CB  1 
ATOM   1005 C CG  . PRO B 1 36 ? 34.090  -14.462 -31.922 1.00 59.23 ? 35  PRO B CG  1 
ATOM   1006 C CD  . PRO B 1 36 ? 34.671  -13.458 -30.942 1.00 53.06 ? 35  PRO B CD  1 
ATOM   1007 N N   . PRO B 1 37 ? 34.670  -17.924 -29.118 1.00 48.02 ? 36  PRO B N   1 
ATOM   1008 C CA  . PRO B 1 37 ? 35.443  -19.154 -29.237 1.00 46.82 ? 36  PRO B CA  1 
ATOM   1009 C C   . PRO B 1 37 ? 35.542  -19.471 -30.725 1.00 53.48 ? 36  PRO B C   1 
ATOM   1010 O O   . PRO B 1 37 ? 34.805  -18.897 -31.536 1.00 48.57 ? 36  PRO B O   1 
ATOM   1011 C CB  . PRO B 1 37 ? 34.608  -20.191 -28.466 1.00 48.69 ? 36  PRO B CB  1 
ATOM   1012 C CG  . PRO B 1 37 ? 33.724  -19.359 -27.558 1.00 48.83 ? 36  PRO B CG  1 
ATOM   1013 C CD  . PRO B 1 37 ? 33.427  -18.098 -28.347 1.00 50.27 ? 36  PRO B CD  1 
ATOM   1014 N N   . PRO B 1 38 ? 36.460  -20.383 -31.130 1.00 51.02 ? 37  PRO B N   1 
ATOM   1015 C CA  . PRO B 1 38 ? 36.553  -20.818 -32.532 1.00 51.36 ? 37  PRO B CA  1 
ATOM   1016 C C   . PRO B 1 38 ? 35.201  -21.247 -33.103 1.00 43.77 ? 37  PRO B C   1 
ATOM   1017 O O   . PRO B 1 38 ? 34.415  -21.878 -32.395 1.00 47.27 ? 37  PRO B O   1 
ATOM   1018 C CB  . PRO B 1 38 ? 37.537  -22.017 -32.450 1.00 50.72 ? 37  PRO B CB  1 
ATOM   1019 C CG  . PRO B 1 38 ? 38.400  -21.720 -31.235 1.00 47.86 ? 37  PRO B CG  1 
ATOM   1020 C CD  . PRO B 1 38 ? 37.461  -21.025 -30.253 1.00 56.47 ? 37  PRO B CD  1 
ATOM   1021 N N   . ASN B 1 39 ? 34.953  -20.890 -34.372 1.00 44.01 ? 38  ASN B N   1 
ATOM   1022 C CA  . ASN B 1 39 ? 33.774  -21.311 -35.128 1.00 46.19 ? 38  ASN B CA  1 
ATOM   1023 C C   . ASN B 1 39 ? 32.494  -20.564 -34.740 1.00 40.31 ? 38  ASN B C   1 
ATOM   1024 O O   . ASN B 1 39 ? 31.462  -20.820 -35.335 1.00 40.09 ? 38  ASN B O   1 
ATOM   1025 C CB  . ASN B 1 39 ? 33.470  -22.799 -34.956 1.00 44.45 ? 38  ASN B CB  1 
ATOM   1026 C CG  . ASN B 1 39 ? 34.683  -23.668 -35.211 1.00 57.71 ? 38  ASN B CG  1 
ATOM   1027 O OD1 . ASN B 1 39 ? 35.021  -24.522 -34.382 1.00 63.01 ? 38  ASN B OD1 1 
ATOM   1028 N ND2 . ASN B 1 39 ? 35.357  -23.461 -36.334 1.00 51.60 ? 38  ASN B ND2 1 
ATOM   1029 N N   . LYS B 1 40 ? 32.539  -19.657 -33.748 1.00 39.31 ? 39  LYS B N   1 
ATOM   1030 C CA  . LYS B 1 40 ? 31.328  -19.051 -33.209 1.00 36.13 ? 39  LYS B CA  1 
ATOM   1031 C C   . LYS B 1 40 ? 31.278  -17.560 -33.528 1.00 34.18 ? 39  LYS B C   1 
ATOM   1032 O O   . LYS B 1 40 ? 32.284  -16.987 -33.902 1.00 39.86 ? 39  LYS B O   1 
ATOM   1033 C CB  . LYS B 1 40 ? 31.335  -19.321 -31.702 1.00 38.72 ? 39  LYS B CB  1 
ATOM   1034 C CG  . LYS B 1 40 ? 31.126  -20.786 -31.348 1.00 41.58 ? 39  LYS B CG  1 
ATOM   1035 C CD  . LYS B 1 40 ? 30.966  -20.878 -29.837 1.00 51.73 ? 39  LYS B CD  1 
ATOM   1036 C CE  . LYS B 1 40 ? 29.786  -21.659 -29.368 1.00 61.35 ? 39  LYS B CE  1 
ATOM   1037 N NZ  . LYS B 1 40 ? 30.020  -23.100 -29.442 1.00 65.65 ? 39  LYS B NZ  1 
ATOM   1038 N N   . TYR B 1 41 ? 30.098  -16.944 -33.377 1.00 31.70 ? 40  TYR B N   1 
ATOM   1039 C CA  . TYR B 1 41 ? 29.866  -15.541 -33.699 1.00 31.50 ? 40  TYR B CA  1 
ATOM   1040 C C   . TYR B 1 41 ? 29.288  -14.851 -32.471 1.00 35.57 ? 40  TYR B C   1 
ATOM   1041 O O   . TYR B 1 41 ? 28.584  -15.479 -31.688 1.00 31.24 ? 40  TYR B O   1 
ATOM   1042 C CB  . TYR B 1 41 ? 28.831  -15.384 -34.813 1.00 31.47 ? 40  TYR B CB  1 
ATOM   1043 C CG  . TYR B 1 41 ? 29.298  -15.869 -36.182 1.00 34.51 ? 40  TYR B CG  1 
ATOM   1044 C CD1 . TYR B 1 41 ? 29.907  -15.005 -37.082 1.00 32.95 ? 40  TYR B CD1 1 
ATOM   1045 C CD2 . TYR B 1 41 ? 29.115  -17.186 -36.570 1.00 31.36 ? 40  TYR B CD2 1 
ATOM   1046 C CE1 . TYR B 1 41 ? 30.327  -15.441 -38.333 1.00 37.43 ? 40  TYR B CE1 1 
ATOM   1047 C CE2 . TYR B 1 41 ? 29.544  -17.645 -37.805 1.00 36.25 ? 40  TYR B CE2 1 
ATOM   1048 C CZ  . TYR B 1 41 ? 30.179  -16.770 -38.683 1.00 38.35 ? 40  TYR B CZ  1 
ATOM   1049 O OH  . TYR B 1 41 ? 30.567  -17.187 -39.940 1.00 35.48 ? 40  TYR B OH  1 
ATOM   1050 N N   . PRO B 1 42 ? 29.545  -13.532 -32.274 1.00 35.66 ? 41  PRO B N   1 
ATOM   1051 C CA  . PRO B 1 42 ? 28.834  -12.787 -31.237 1.00 30.42 ? 41  PRO B CA  1 
ATOM   1052 C C   . PRO B 1 42 ? 27.415  -12.494 -31.705 1.00 28.19 ? 41  PRO B C   1 
ATOM   1053 O O   . PRO B 1 42 ? 27.230  -11.861 -32.757 1.00 30.32 ? 41  PRO B O   1 
ATOM   1054 C CB  . PRO B 1 42 ? 29.655  -11.482 -31.050 1.00 31.83 ? 41  PRO B CB  1 
ATOM   1055 C CG  . PRO B 1 42 ? 30.529  -11.363 -32.304 1.00 33.33 ? 41  PRO B CG  1 
ATOM   1056 C CD  . PRO B 1 42 ? 30.503  -12.706 -33.037 1.00 35.29 ? 41  PRO B CD  1 
ATOM   1057 N N   . ILE B 1 43 ? 26.414  -12.996 -30.936 1.00 28.44 ? 42  ILE B N   1 
ATOM   1058 C CA  . ILE B 1 43 ? 24.992  -12.783 -31.219 1.00 27.74 ? 42  ILE B CA  1 
ATOM   1059 C C   . ILE B 1 43 ? 24.389  -11.770 -30.249 1.00 26.63 ? 42  ILE B C   1 
ATOM   1060 O O   . ILE B 1 43 ? 24.692  -11.825 -29.082 1.00 29.79 ? 42  ILE B O   1 
ATOM   1061 C CB  . ILE B 1 43 ? 24.240  -14.127 -31.107 1.00 26.08 ? 42  ILE B CB  1 
ATOM   1062 C CG1 . ILE B 1 43 ? 25.002  -15.220 -31.933 1.00 28.39 ? 42  ILE B CG1 1 
ATOM   1063 C CG2 . ILE B 1 43 ? 22.768  -13.995 -31.517 1.00 29.18 ? 42  ILE B CG2 1 
ATOM   1064 C CD1 . ILE B 1 43 ? 25.153  -14.882 -33.401 1.00 27.82 ? 42  ILE B CD1 1 
ATOM   1065 N N   . PHE B 1 44 ? 23.531  -10.902 -30.758 1.00 26.39 ? 43  PHE B N   1 
ATOM   1066 C CA  . PHE B 1 44 ? 22.729  -9.981  -29.961 1.00 26.24 ? 43  PHE B CA  1 
ATOM   1067 C C   . PHE B 1 44 ? 21.272  -10.389 -30.169 1.00 25.60 ? 43  PHE B C   1 
ATOM   1068 O O   . PHE B 1 44 ? 20.809  -10.513 -31.300 1.00 25.71 ? 43  PHE B O   1 
ATOM   1069 C CB  . PHE B 1 44 ? 22.969  -8.522  -30.392 1.00 26.12 ? 43  PHE B CB  1 
ATOM   1070 C CG  . PHE B 1 44 ? 22.038  -7.510  -29.721 1.00 27.32 ? 43  PHE B CG  1 
ATOM   1071 C CD1 . PHE B 1 44 ? 20.862  -7.115  -30.350 1.00 24.94 ? 43  PHE B CD1 1 
ATOM   1072 C CD2 . PHE B 1 44 ? 22.328  -6.991  -28.468 1.00 32.68 ? 43  PHE B CD2 1 
ATOM   1073 C CE1 . PHE B 1 44 ? 20.007  -6.194  -29.760 1.00 29.68 ? 43  PHE B CE1 1 
ATOM   1074 C CE2 . PHE B 1 44 ? 21.470  -6.061  -27.876 1.00 27.81 ? 43  PHE B CE2 1 
ATOM   1075 C CZ  . PHE B 1 44 ? 20.333  -5.660  -28.534 1.00 31.36 ? 43  PHE B CZ  1 
ATOM   1076 N N   . PHE B 1 45 ? 20.565  -10.669 -29.062 1.00 25.17 ? 44  PHE B N   1 
ATOM   1077 C CA  . PHE B 1 45 ? 19.184  -11.108 -29.129 1.00 25.19 ? 44  PHE B CA  1 
ATOM   1078 C C   . PHE B 1 45 ? 18.284  -9.904  -28.934 1.00 24.29 ? 44  PHE B C   1 
ATOM   1079 O O   . PHE B 1 45 ? 18.388  -9.174  -27.917 1.00 26.01 ? 44  PHE B O   1 
ATOM   1080 C CB  . PHE B 1 45 ? 19.027  -12.099 -27.963 1.00 23.62 ? 44  PHE B CB  1 
ATOM   1081 C CG  . PHE B 1 45 ? 19.753  -13.424 -28.105 1.00 23.99 ? 44  PHE B CG  1 
ATOM   1082 C CD1 . PHE B 1 45 ? 21.122  -13.541 -27.890 1.00 25.16 ? 44  PHE B CD1 1 
ATOM   1083 C CD2 . PHE B 1 45 ? 19.087  -14.531 -28.618 1.00 24.80 ? 44  PHE B CD2 1 
ATOM   1084 C CE1 . PHE B 1 45 ? 21.779  -14.741 -28.084 1.00 25.61 ? 44  PHE B CE1 1 
ATOM   1085 C CE2 . PHE B 1 45 ? 19.747  -15.734 -28.798 1.00 26.48 ? 44  PHE B CE2 1 
ATOM   1086 C CZ  . PHE B 1 45 ? 21.097  -15.840 -28.566 1.00 24.88 ? 44  PHE B CZ  1 
ATOM   1087 N N   . PHE B 1 46 ? 17.452  -9.657  -29.942 1.00 24.99 ? 45  PHE B N   1 
ATOM   1088 C CA  . PHE B 1 46 ? 16.527  -8.543  -29.875 1.00 24.99 ? 45  PHE B CA  1 
ATOM   1089 C C   . PHE B 1 46 ? 15.523  -8.760  -28.731 1.00 28.27 ? 45  PHE B C   1 
ATOM   1090 O O   . PHE B 1 46 ? 15.240  -9.895  -28.328 1.00 25.50 ? 45  PHE B O   1 
ATOM   1091 C CB  . PHE B 1 46 ? 15.820  -8.359  -31.212 1.00 23.88 ? 45  PHE B CB  1 
ATOM   1092 C CG  . PHE B 1 46 ? 16.764  -7.892  -32.302 1.00 26.15 ? 45  PHE B CG  1 
ATOM   1093 C CD1 . PHE B 1 46 ? 17.225  -6.572  -32.279 1.00 27.91 ? 45  PHE B CD1 1 
ATOM   1094 C CD2 . PHE B 1 46 ? 17.114  -8.733  -33.379 1.00 25.57 ? 45  PHE B CD2 1 
ATOM   1095 C CE1 . PHE B 1 46 ? 18.087  -6.127  -33.293 1.00 25.76 ? 45  PHE B CE1 1 
ATOM   1096 C CE2 . PHE B 1 46 ? 17.952  -8.261  -34.416 1.00 27.27 ? 45  PHE B CE2 1 
ATOM   1097 C CZ  . PHE B 1 46 ? 18.409  -6.949  -34.362 1.00 25.45 ? 45  PHE B CZ  1 
ATOM   1098 N N   . GLY B 1 47 ? 15.009  -7.638  -28.211 1.00 27.72 ? 46  GLY B N   1 
ATOM   1099 C CA  . GLY B 1 47 ? 13.983  -7.676  -27.163 1.00 28.77 ? 46  GLY B CA  1 
ATOM   1100 C C   . GLY B 1 47 ? 14.591  -7.812  -25.764 1.00 29.89 ? 46  GLY B C   1 
ATOM   1101 O O   . GLY B 1 47 ? 14.411  -6.919  -24.925 1.00 31.36 ? 46  GLY B O   1 
ATOM   1102 N N   . THR B 1 48 ? 15.312  -8.913  -25.514 1.00 27.58 ? 47  THR B N   1 
ATOM   1103 C CA  . THR B 1 48 ? 16.014  -9.176  -24.271 1.00 27.60 ? 47  THR B CA  1 
ATOM   1104 C C   . THR B 1 48 ? 17.288  -8.340  -24.201 1.00 29.80 ? 47  THR B C   1 
ATOM   1105 O O   . THR B 1 48 ? 17.788  -8.042  -23.109 1.00 30.96 ? 47  THR B O   1 
ATOM   1106 C CB  . THR B 1 48 ? 16.331  -10.663 -24.099 1.00 30.72 ? 47  THR B CB  1 
ATOM   1107 O OG1 . THR B 1 48 ? 17.304  -11.124 -25.058 1.00 28.26 ? 47  THR B OG1 1 
ATOM   1108 C CG2 . THR B 1 48 ? 15.059  -11.499 -24.030 1.00 26.04 ? 47  THR B CG2 1 
ATOM   1109 N N   . HIS B 1 49 ? 17.850  -8.065  -25.374 1.00 29.18 ? 48  HIS B N   1 
ATOM   1110 C CA  . HIS B 1 49 ? 19.152  -7.426  -25.507 1.00 31.55 ? 48  HIS B CA  1 
ATOM   1111 C C   . HIS B 1 49 ? 20.260  -8.236  -24.847 1.00 30.98 ? 48  HIS B C   1 
ATOM   1112 O O   . HIS B 1 49 ? 21.301  -7.667  -24.509 1.00 33.94 ? 48  HIS B O   1 
ATOM   1113 C CB  . HIS B 1 49 ? 19.123  -5.950  -25.070 1.00 30.24 ? 48  HIS B CB  1 
ATOM   1114 C CG  . HIS B 1 49 ? 17.949  -5.231  -25.614 1.00 30.78 ? 48  HIS B CG  1 
ATOM   1115 N ND1 . HIS B 1 49 ? 17.208  -4.390  -24.817 1.00 34.05 ? 48  HIS B ND1 1 
ATOM   1116 C CD2 . HIS B 1 49 ? 17.328  -5.219  -26.812 1.00 27.48 ? 48  HIS B CD2 1 
ATOM   1117 C CE1 . HIS B 1 49 ? 16.156  -3.944  -25.498 1.00 37.12 ? 48  HIS B CE1 1 
ATOM   1118 N NE2 . HIS B 1 49 ? 16.230  -4.412  -26.740 1.00 33.06 ? 48  HIS B NE2 1 
ATOM   1119 N N   . GLU B 1 50 ? 20.089  -9.554  -24.722 1.00 30.31 ? 49  GLU B N   1 
ATOM   1120 C CA  . GLU B 1 50 ? 21.173  -10.397 -24.247 1.00 30.38 ? 49  GLU B CA  1 
ATOM   1121 C C   . GLU B 1 50 ? 22.173  -10.684 -25.376 1.00 28.97 ? 49  GLU B C   1 
ATOM   1122 O O   . GLU B 1 50 ? 21.898  -10.449 -26.555 1.00 28.60 ? 49  GLU B O   1 
ATOM   1123 C CB  . GLU B 1 50 ? 20.642  -11.777 -23.850 1.00 35.43 ? 49  GLU B CB  1 
ATOM   1124 C CG  . GLU B 1 50 ? 19.603  -11.707 -22.731 1.00 38.91 ? 49  GLU B CG  1 
ATOM   1125 C CD  . GLU B 1 50 ? 19.919  -12.438 -21.446 1.00 42.28 ? 49  GLU B CD  1 
ATOM   1126 O OE1 . GLU B 1 50 ? 20.882  -13.209 -21.360 1.00 44.17 ? 49  GLU B OE1 1 
ATOM   1127 O OE2 . GLU B 1 50 ? 19.173  -12.215 -20.491 1.00 41.65 ? 49  GLU B OE2 1 
ATOM   1128 N N   . THR B 1 51 ? 23.313  -11.238 -24.986 1.00 27.40 ? 50  THR B N   1 
ATOM   1129 C CA  . THR B 1 51 ? 24.393  -11.606 -25.895 1.00 28.83 ? 50  THR B CA  1 
ATOM   1130 C C   . THR B 1 51 ? 24.884  -13.008 -25.547 1.00 31.74 ? 50  THR B C   1 
ATOM   1131 O O   . THR B 1 51 ? 24.772  -13.470 -24.409 1.00 34.09 ? 50  THR B O   1 
ATOM   1132 C CB  . THR B 1 51 ? 25.533  -10.574 -25.980 1.00 33.49 ? 50  THR B CB  1 
ATOM   1133 O OG1 . THR B 1 51 ? 26.067  -10.412 -24.672 1.00 34.67 ? 50  THR B OG1 1 
ATOM   1134 C CG2 . THR B 1 51 ? 25.075  -9.190  -26.400 1.00 30.87 ? 50  THR B CG2 1 
ATOM   1135 N N   . ALA B 1 52 ? 25.349  -13.740 -26.567 1.00 31.69 ? 51  ALA B N   1 
ATOM   1136 C CA  . ALA B 1 52 ? 25.973  -15.032 -26.383 1.00 32.84 ? 51  ALA B CA  1 
ATOM   1137 C C   . ALA B 1 52 ? 26.808  -15.318 -27.628 1.00 29.97 ? 51  ALA B C   1 
ATOM   1138 O O   . ALA B 1 52 ? 26.685  -14.599 -28.639 1.00 31.74 ? 51  ALA B O   1 
ATOM   1139 C CB  . ALA B 1 52 ? 24.928  -16.122 -26.137 1.00 30.39 ? 51  ALA B CB  1 
ATOM   1140 N N   . PHE B 1 53 ? 27.635  -16.363 -27.524 1.00 31.43 ? 52  PHE B N   1 
ATOM   1141 C CA  . PHE B 1 53 ? 28.366  -16.860 -28.673 1.00 31.57 ? 52  PHE B CA  1 
ATOM   1142 C C   . PHE B 1 53 ? 27.695  -18.137 -29.183 1.00 31.95 ? 52  PHE B C   1 
ATOM   1143 O O   . PHE B 1 53 ? 27.473  -19.092 -28.423 1.00 33.97 ? 52  PHE B O   1 
ATOM   1144 C CB  . PHE B 1 53 ? 29.834  -17.115 -28.318 1.00 30.59 ? 52  PHE B CB  1 
ATOM   1145 C CG  . PHE B 1 53 ? 30.612  -15.896 -27.850 1.00 35.79 ? 52  PHE B CG  1 
ATOM   1146 C CD1 . PHE B 1 53 ? 30.938  -14.885 -28.740 1.00 38.20 ? 52  PHE B CD1 1 
ATOM   1147 C CD2 . PHE B 1 53 ? 31.003  -15.772 -26.521 1.00 39.73 ? 52  PHE B CD2 1 
ATOM   1148 C CE1 . PHE B 1 53 ? 31.645  -13.770 -28.315 1.00 41.66 ? 52  PHE B CE1 1 
ATOM   1149 C CE2 . PHE B 1 53 ? 31.703  -14.649 -26.091 1.00 41.74 ? 52  PHE B CE2 1 
ATOM   1150 C CZ  . PHE B 1 53 ? 32.039  -13.674 -26.988 1.00 37.83 ? 52  PHE B CZ  1 
ATOM   1151 N N   . LEU B 1 54 ? 27.434  -18.178 -30.494 1.00 29.25 ? 53  LEU B N   1 
ATOM   1152 C CA  . LEU B 1 54 ? 26.793  -19.339 -31.103 1.00 26.95 ? 53  LEU B CA  1 
ATOM   1153 C C   . LEU B 1 54 ? 27.531  -19.674 -32.408 1.00 28.85 ? 53  LEU B C   1 
ATOM   1154 O O   . LEU B 1 54 ? 28.006  -18.770 -33.106 1.00 32.45 ? 53  LEU B O   1 
ATOM   1155 C CB  . LEU B 1 54 ? 25.312  -19.124 -31.434 1.00 28.98 ? 53  LEU B CB  1 
ATOM   1156 C CG  . LEU B 1 54 ? 24.314  -19.053 -30.273 1.00 28.09 ? 53  LEU B CG  1 
ATOM   1157 C CD1 . LEU B 1 54 ? 22.909  -18.727 -30.759 1.00 27.55 ? 53  LEU B CD1 1 
ATOM   1158 C CD2 . LEU B 1 54 ? 24.320  -20.444 -29.628 1.00 32.06 ? 53  LEU B CD2 1 
ATOM   1159 N N   . GLY B 1 55 ? 27.529  -20.969 -32.756 1.00 30.06 ? 54  GLY B N   1 
ATOM   1160 C CA  . GLY B 1 55 ? 28.032  -21.478 -34.023 1.00 29.37 ? 54  GLY B CA  1 
ATOM   1161 C C   . GLY B 1 55 ? 26.919  -21.567 -35.070 1.00 28.33 ? 54  GLY B C   1 
ATOM   1162 O O   . GLY B 1 55 ? 25.724  -21.474 -34.747 1.00 28.65 ? 54  GLY B O   1 
ATOM   1163 N N   . PRO B 1 56 ? 27.277  -21.730 -36.367 1.00 27.79 ? 55  PRO B N   1 
ATOM   1164 C CA  . PRO B 1 56 ? 26.304  -21.790 -37.450 1.00 29.41 ? 55  PRO B CA  1 
ATOM   1165 C C   . PRO B 1 56 ? 25.140  -22.759 -37.336 1.00 26.34 ? 55  PRO B C   1 
ATOM   1166 O O   . PRO B 1 56 ? 24.060  -22.484 -37.845 1.00 26.90 ? 55  PRO B O   1 
ATOM   1167 C CB  . PRO B 1 56 ? 27.193  -22.197 -38.650 1.00 29.88 ? 55  PRO B CB  1 
ATOM   1168 C CG  . PRO B 1 56 ? 28.589  -21.746 -38.319 1.00 31.75 ? 55  PRO B CG  1 
ATOM   1169 C CD  . PRO B 1 56 ? 28.676  -21.852 -36.828 1.00 28.03 ? 55  PRO B CD  1 
ATOM   1170 N N   . LYS B 1 57 ? 25.331  -23.875 -36.613 1.00 28.52 ? 56  LYS B N   1 
ATOM   1171 C CA  . LYS B 1 57 ? 24.243  -24.845 -36.506 1.00 28.27 ? 56  LYS B CA  1 
ATOM   1172 C C   . LYS B 1 57 ? 23.009  -24.233 -35.835 1.00 27.93 ? 56  LYS B C   1 
ATOM   1173 O O   . LYS B 1 57 ? 21.893  -24.708 -36.047 1.00 28.28 ? 56  LYS B O   1 
ATOM   1174 C CB  . LYS B 1 57 ? 24.721  -26.120 -35.793 1.00 32.29 ? 56  LYS B CB  1 
ATOM   1175 C CG  . LYS B 1 57 ? 24.749  -26.009 -34.282 1.00 34.48 ? 56  LYS B CG  1 
ATOM   1176 C CD  . LYS B 1 57 ? 24.980  -27.376 -33.632 1.00 43.58 ? 56  LYS B CD  1 
ATOM   1177 C CE  . LYS B 1 57 ? 25.302  -27.352 -32.159 1.00 45.10 ? 56  LYS B CE  1 
ATOM   1178 N NZ  . LYS B 1 57 ? 24.155  -26.888 -31.382 1.00 44.66 ? 56  LYS B NZ  1 
ATOM   1179 N N   . ASP B 1 58 ? 23.234  -23.154 -35.045 1.00 27.15 ? 57  ASP B N   1 
ATOM   1180 C CA  . ASP B 1 58 ? 22.187  -22.534 -34.252 1.00 27.51 ? 57  ASP B CA  1 
ATOM   1181 C C   . ASP B 1 58 ? 21.755  -21.182 -34.826 1.00 25.52 ? 57  ASP B C   1 
ATOM   1182 O O   . ASP B 1 58 ? 20.984  -20.467 -34.170 1.00 26.94 ? 57  ASP B O   1 
ATOM   1183 C CB  . ASP B 1 58 ? 22.621  -22.418 -32.807 1.00 26.11 ? 57  ASP B CB  1 
ATOM   1184 C CG  . ASP B 1 58 ? 22.734  -23.748 -32.061 1.00 31.70 ? 57  ASP B CG  1 
ATOM   1185 O OD1 . ASP B 1 58 ? 21.807  -24.563 -32.205 1.00 32.40 ? 57  ASP B OD1 1 
ATOM   1186 O OD2 . ASP B 1 58 ? 23.724  -23.923 -31.330 1.00 34.46 ? 57  ASP B OD2 1 
ATOM   1187 N N   . LEU B 1 59 ? 22.193  -20.878 -36.063 1.00 25.03 ? 58  LEU B N   1 
ATOM   1188 C CA  . LEU B 1 59 ? 21.926  -19.580 -36.674 1.00 24.55 ? 58  LEU B CA  1 
ATOM   1189 C C   . LEU B 1 59 ? 21.188  -19.775 -37.986 1.00 24.22 ? 58  LEU B C   1 
ATOM   1190 O O   . LEU B 1 59 ? 21.663  -20.472 -38.887 1.00 27.28 ? 58  LEU B O   1 
ATOM   1191 C CB  . LEU B 1 59 ? 23.242  -18.829 -36.871 1.00 26.43 ? 58  LEU B CB  1 
ATOM   1192 C CG  . LEU B 1 59 ? 24.069  -18.588 -35.616 1.00 25.14 ? 58  LEU B CG  1 
ATOM   1193 C CD1 . LEU B 1 59 ? 25.368  -17.895 -36.012 1.00 28.33 ? 58  LEU B CD1 1 
ATOM   1194 C CD2 . LEU B 1 59 ? 23.315  -17.668 -34.668 1.00 29.78 ? 58  LEU B CD2 1 
ATOM   1195 N N   . PHE B 1 60 ? 19.992  -19.207 -38.069 1.00 21.80 ? 59  PHE B N   1 
ATOM   1196 C CA  . PHE B 1 60 ? 19.098  -19.396 -39.203 1.00 23.91 ? 59  PHE B CA  1 
ATOM   1197 C C   . PHE B 1 60 ? 18.907  -18.035 -39.883 1.00 26.87 ? 59  PHE B C   1 
ATOM   1198 O O   . PHE B 1 60 ? 18.360  -17.104 -39.308 1.00 25.85 ? 59  PHE B O   1 
ATOM   1199 C CB  . PHE B 1 60 ? 17.776  -19.942 -38.640 1.00 24.46 ? 59  PHE B CB  1 
ATOM   1200 C CG  . PHE B 1 60 ? 17.873  -21.337 -38.019 1.00 23.68 ? 59  PHE B CG  1 
ATOM   1201 C CD1 . PHE B 1 60 ? 18.425  -21.506 -36.742 1.00 26.85 ? 59  PHE B CD1 1 
ATOM   1202 C CD2 . PHE B 1 60 ? 17.412  -22.450 -38.729 1.00 27.02 ? 59  PHE B CD2 1 
ATOM   1203 C CE1 . PHE B 1 60 ? 18.552  -22.776 -36.186 1.00 26.92 ? 59  PHE B CE1 1 
ATOM   1204 C CE2 . PHE B 1 60 ? 17.504  -23.718 -38.154 1.00 26.46 ? 59  PHE B CE2 1 
ATOM   1205 C CZ  . PHE B 1 60 ? 18.116  -23.872 -36.921 1.00 27.88 ? 59  PHE B CZ  1 
ATOM   1206 N N   . PRO B 1 61 ? 19.386  -17.826 -41.129 1.00 27.72 ? 60  PRO B N   1 
ATOM   1207 C CA  . PRO B 1 61 ? 19.148  -16.537 -41.806 1.00 26.93 ? 60  PRO B CA  1 
ATOM   1208 C C   . PRO B 1 61 ? 17.693  -16.074 -41.734 1.00 24.95 ? 60  PRO B C   1 
ATOM   1209 O O   . PRO B 1 61 ? 16.736  -16.842 -41.950 1.00 28.69 ? 60  PRO B O   1 
ATOM   1210 C CB  . PRO B 1 61 ? 19.593  -16.881 -43.245 1.00 28.33 ? 60  PRO B CB  1 
ATOM   1211 C CG  . PRO B 1 61 ? 20.724  -17.841 -43.035 1.00 34.04 ? 60  PRO B CG  1 
ATOM   1212 C CD  . PRO B 1 61 ? 20.231  -18.771 -41.890 1.00 31.19 ? 60  PRO B CD  1 
ATOM   1213 N N   . TYR B 1 62 ? 17.523  -14.759 -41.402 1.00 26.80 ? 61  TYR B N   1 
ATOM   1214 C CA  . TYR B 1 62 ? 16.214  -14.242 -41.053 1.00 29.22 ? 61  TYR B CA  1 
ATOM   1215 C C   . TYR B 1 62 ? 15.239  -14.296 -42.208 1.00 30.91 ? 61  TYR B C   1 
ATOM   1216 O O   . TYR B 1 62 ? 14.105  -14.744 -42.021 1.00 32.96 ? 61  TYR B O   1 
ATOM   1217 C CB  . TYR B 1 62 ? 16.355  -12.794 -40.552 1.00 32.95 ? 61  TYR B CB  1 
ATOM   1218 C CG  . TYR B 1 62 ? 15.026  -12.099 -40.304 1.00 33.93 ? 61  TYR B CG  1 
ATOM   1219 C CD1 . TYR B 1 62 ? 14.317  -12.307 -39.128 1.00 33.48 ? 61  TYR B CD1 1 
ATOM   1220 C CD2 . TYR B 1 62 ? 14.548  -11.144 -41.205 1.00 38.32 ? 61  TYR B CD2 1 
ATOM   1221 C CE1 . TYR B 1 62 ? 13.117  -11.654 -38.898 1.00 32.75 ? 61  TYR B CE1 1 
ATOM   1222 C CE2 . TYR B 1 62 ? 13.373  -10.444 -40.961 1.00 39.86 ? 61  TYR B CE2 1 
ATOM   1223 C CZ  . TYR B 1 62 ? 12.661  -10.706 -39.800 1.00 36.03 ? 61  TYR B CZ  1 
ATOM   1224 O OH  . TYR B 1 62 ? 11.505  -10.046 -39.559 1.00 40.19 ? 61  TYR B OH  1 
ATOM   1225 N N   . ASP B 1 63 ? 15.708  -13.871 -43.404 1.00 34.31 ? 62  ASP B N   1 
ATOM   1226 C CA  . ASP B 1 63 ? 14.848  -13.864 -44.588 1.00 38.69 ? 62  ASP B CA  1 
ATOM   1227 C C   . ASP B 1 63 ? 14.261  -15.244 -44.877 1.00 33.84 ? 62  ASP B C   1 
ATOM   1228 O O   . ASP B 1 63 ? 13.052  -15.395 -45.000 1.00 41.65 ? 62  ASP B O   1 
ATOM   1229 C CB  . ASP B 1 63 ? 15.533  -13.252 -45.795 1.00 46.52 ? 62  ASP B CB  1 
ATOM   1230 C CG  . ASP B 1 63 ? 15.181  -11.797 -46.036 1.00 62.44 ? 62  ASP B CG  1 
ATOM   1231 O OD1 . ASP B 1 63 ? 14.637  -11.158 -45.101 1.00 64.24 ? 62  ASP B OD1 1 
ATOM   1232 O OD2 . ASP B 1 63 ? 15.400  -11.341 -47.178 1.00 71.38 ? 62  ASP B OD2 1 
ATOM   1233 N N   . LYS B 1 64 ? 15.129  -16.244 -44.947 1.00 35.52 ? 63  LYS B N   1 
ATOM   1234 C CA  . LYS B 1 64 ? 14.697  -17.604 -45.210 1.00 35.87 ? 63  LYS B CA  1 
ATOM   1235 C C   . LYS B 1 64 ? 13.707  -18.088 -44.151 1.00 35.99 ? 63  LYS B C   1 
ATOM   1236 O O   . LYS B 1 64 ? 12.752  -18.799 -44.468 1.00 38.74 ? 63  LYS B O   1 
ATOM   1237 C CB  . LYS B 1 64 ? 15.893  -18.555 -45.252 1.00 41.18 ? 63  LYS B CB  1 
ATOM   1238 C CG  . LYS B 1 64 ? 15.532  -19.948 -45.743 1.00 39.52 ? 63  LYS B CG  1 
ATOM   1239 C CD  . LYS B 1 64 ? 16.742  -20.870 -45.719 1.00 45.67 ? 63  LYS B CD  1 
ATOM   1240 C CE  . LYS B 1 64 ? 16.534  -22.234 -46.350 1.00 48.64 ? 63  LYS B CE  1 
ATOM   1241 N NZ  . LYS B 1 64 ? 15.313  -22.926 -45.943 1.00 44.48 ? 63  LYS B NZ  1 
ATOM   1242 N N   . SER B 1 65 ? 13.905  -17.684 -42.893 1.00 34.90 ? 64  SER B N   1 
ATOM   1243 C CA  . SER B 1 65 ? 13.239  -18.452 -41.830 1.00 36.10 ? 64  SER B CA  1 
ATOM   1244 C C   . SER B 1 65 ? 12.111  -17.695 -41.104 1.00 34.31 ? 64  SER B C   1 
ATOM   1245 O O   . SER B 1 65 ? 11.485  -18.242 -40.207 1.00 36.16 ? 64  SER B O   1 
ATOM   1246 C CB  . SER B 1 65 ? 14.279  -18.981 -40.903 1.00 37.00 ? 64  SER B CB  1 
ATOM   1247 O OG  . SER B 1 65 ? 14.931  -17.889 -40.276 1.00 47.62 ? 64  SER B OG  1 
ATOM   1248 N N   . LYS B 1 66 ? 11.821  -16.442 -41.492 1.00 35.39 ? 65  LYS B N   1 
ATOM   1249 C CA  . LYS B 1 66 ? 10.913  -15.604 -40.707 1.00 34.82 ? 65  LYS B CA  1 
ATOM   1250 C C   . LYS B 1 66 ? 9.469   -16.122 -40.694 1.00 36.12 ? 65  LYS B C   1 
ATOM   1251 O O   . LYS B 1 66 ? 8.747   -15.946 -39.714 1.00 36.95 ? 65  LYS B O   1 
ATOM   1252 C CB  . LYS B 1 66 ? 10.970  -14.126 -41.109 1.00 35.01 ? 65  LYS B CB  1 
ATOM   1253 C CG  . LYS B 1 66 ? 10.644  -13.932 -42.588 1.00 36.06 ? 65  LYS B CG  1 
ATOM   1254 C CD  . LYS B 1 66 ? 10.884  -12.505 -43.080 1.00 51.12 ? 65  LYS B CD  1 
ATOM   1255 N N   . ASP B 1 67 ? 9.000   -16.740 -41.775 1.00 37.04 ? 66  ASP B N   1 
ATOM   1256 C CA  . ASP B 1 67 ? 7.609   -17.162 -41.743 1.00 42.26 ? 66  ASP B CA  1 
ATOM   1257 C C   . ASP B 1 67 ? 7.444   -18.354 -40.792 1.00 41.31 ? 66  ASP B C   1 
ATOM   1258 O O   . ASP B 1 67 ? 6.366   -18.557 -40.213 1.00 46.14 ? 66  ASP B O   1 
ATOM   1259 C CB  . ASP B 1 67 ? 7.016   -17.280 -43.142 1.00 57.18 ? 66  ASP B CB  1 
ATOM   1260 C CG  . ASP B 1 67 ? 7.454   -18.475 -43.972 1.00 72.47 ? 66  ASP B CG  1 
ATOM   1261 O OD1 . ASP B 1 67 ? 7.743   -18.260 -45.174 1.00 85.47 ? 66  ASP B OD1 1 
ATOM   1262 O OD2 . ASP B 1 67 ? 7.477   -19.606 -43.423 1.00 79.86 ? 66  ASP B OD2 1 
ATOM   1263 N N   . LYS B 1 68 ? 8.526   -19.126 -40.623 1.00 38.71 ? 67  LYS B N   1 
ATOM   1264 C CA  . LYS B 1 68 ? 8.500   -20.281 -39.740 1.00 34.01 ? 67  LYS B CA  1 
ATOM   1265 C C   . LYS B 1 68 ? 8.688   -19.862 -38.280 1.00 35.22 ? 67  LYS B C   1 
ATOM   1266 O O   . LYS B 1 68 ? 7.936   -20.322 -37.422 1.00 34.68 ? 67  LYS B O   1 
ATOM   1267 C CB  . LYS B 1 68 ? 9.564   -21.301 -40.143 1.00 35.43 ? 67  LYS B CB  1 
ATOM   1268 C CG  . LYS B 1 68 ? 9.650   -22.539 -39.277 1.00 42.05 ? 67  LYS B CG  1 
ATOM   1269 C CD  . LYS B 1 68 ? 10.663  -23.499 -39.897 1.00 50.81 ? 67  LYS B CD  1 
ATOM   1270 C CE  . LYS B 1 68 ? 10.883  -24.768 -39.138 1.00 56.69 ? 67  LYS B CE  1 
ATOM   1271 N NZ  . LYS B 1 68 ? 9.726   -25.659 -39.183 1.00 57.09 ? 67  LYS B NZ  1 
ATOM   1272 N N   . TYR B 1 69 ? 9.691   -19.009 -38.000 1.00 30.33 ? 68  TYR B N   1 
ATOM   1273 C CA  . TYR B 1 69 ? 10.103  -18.741 -36.621 1.00 25.69 ? 68  TYR B CA  1 
ATOM   1274 C C   . TYR B 1 69 ? 9.599   -17.390 -36.125 1.00 31.68 ? 68  TYR B C   1 
ATOM   1275 O O   . TYR B 1 69 ? 9.735   -17.106 -34.934 1.00 32.13 ? 68  TYR B O   1 
ATOM   1276 C CB  . TYR B 1 69 ? 11.625  -18.811 -36.461 1.00 25.44 ? 68  TYR B CB  1 
ATOM   1277 C CG  . TYR B 1 69 ? 12.240  -20.166 -36.767 1.00 30.25 ? 68  TYR B CG  1 
ATOM   1278 C CD1 . TYR B 1 69 ? 11.719  -21.336 -36.219 1.00 28.39 ? 68  TYR B CD1 1 
ATOM   1279 C CD2 . TYR B 1 69 ? 13.358  -20.281 -37.591 1.00 30.50 ? 68  TYR B CD2 1 
ATOM   1280 C CE1 . TYR B 1 69 ? 12.267  -22.582 -36.499 1.00 29.91 ? 68  TYR B CE1 1 
ATOM   1281 C CE2 . TYR B 1 69 ? 13.923  -21.513 -37.879 1.00 32.09 ? 68  TYR B CE2 1 
ATOM   1282 C CZ  . TYR B 1 69 ? 13.384  -22.662 -37.313 1.00 33.30 ? 68  TYR B CZ  1 
ATOM   1283 O OH  . TYR B 1 69 ? 13.912  -23.864 -37.646 1.00 34.73 ? 68  TYR B OH  1 
ATOM   1284 N N   . GLY B 1 70 ? 9.035   -16.562 -37.013 1.00 33.24 ? 69  GLY B N   1 
ATOM   1285 C CA  . GLY B 1 70 ? 8.814   -15.168 -36.659 1.00 32.46 ? 69  GLY B CA  1 
ATOM   1286 C C   . GLY B 1 70 ? 7.397   -14.904 -36.146 1.00 36.13 ? 69  GLY B C   1 
ATOM   1287 O O   . GLY B 1 70 ? 6.871   -13.824 -36.387 1.00 39.09 ? 69  GLY B O   1 
ATOM   1288 N N   . LYS B 1 71 ? 6.810   -15.864 -35.420 1.00 37.83 ? 70  LYS B N   1 
ATOM   1289 C CA  . LYS B 1 71 ? 5.464   -15.694 -34.896 1.00 37.05 ? 70  LYS B CA  1 
ATOM   1290 C C   . LYS B 1 71 ? 5.550   -15.325 -33.425 1.00 39.74 ? 70  LYS B C   1 
ATOM   1291 O O   . LYS B 1 71 ? 6.424   -15.821 -32.712 1.00 38.11 ? 70  LYS B O   1 
ATOM   1292 C CB  . LYS B 1 71 ? 4.657   -17.000 -34.875 1.00 43.24 ? 70  LYS B CB  1 
ATOM   1293 C CG  . LYS B 1 71 ? 3.887   -17.298 -36.158 1.00 58.76 ? 70  LYS B CG  1 
ATOM   1294 C CD  . LYS B 1 71 ? 4.524   -18.324 -37.084 1.00 60.06 ? 70  LYS B CD  1 
ATOM   1295 C CE  . LYS B 1 71 ? 3.700   -18.571 -38.327 1.00 64.05 ? 70  LYS B CE  1 
ATOM   1296 N NZ  . LYS B 1 71 ? 3.934   -17.550 -39.360 1.00 67.10 ? 70  LYS B NZ  1 
ATOM   1297 N N   . PRO B 1 72 ? 4.642   -14.451 -32.930 1.00 41.69 ? 71  PRO B N   1 
ATOM   1298 C CA  . PRO B 1 72 ? 4.623   -14.102 -31.508 1.00 40.05 ? 71  PRO B CA  1 
ATOM   1299 C C   . PRO B 1 72 ? 4.392   -15.295 -30.581 1.00 41.39 ? 71  PRO B C   1 
ATOM   1300 O O   . PRO B 1 72 ? 3.771   -16.291 -30.963 1.00 38.23 ? 71  PRO B O   1 
ATOM   1301 C CB  . PRO B 1 72 ? 3.522   -13.028 -31.398 1.00 42.44 ? 71  PRO B CB  1 
ATOM   1302 C CG  . PRO B 1 72 ? 3.396   -12.486 -32.805 1.00 42.66 ? 71  PRO B CG  1 
ATOM   1303 C CD  . PRO B 1 72 ? 3.675   -13.683 -33.729 1.00 39.70 ? 71  PRO B CD  1 
ATOM   1304 N N   . ASN B 1 73 ? 4.950   -15.192 -29.366 1.00 37.73 ? 72  ASN B N   1 
ATOM   1305 C CA  . ASN B 1 73 ? 4.753   -16.184 -28.322 1.00 34.42 ? 72  ASN B CA  1 
ATOM   1306 C C   . ASN B 1 73 ? 4.717   -15.476 -26.956 1.00 37.96 ? 72  ASN B C   1 
ATOM   1307 O O   . ASN B 1 73 ? 4.746   -14.242 -26.874 1.00 42.80 ? 72  ASN B O   1 
ATOM   1308 C CB  . ASN B 1 73 ? 5.794   -17.307 -28.373 1.00 36.53 ? 72  ASN B CB  1 
ATOM   1309 C CG  . ASN B 1 73 ? 7.210   -16.843 -28.128 1.00 34.58 ? 72  ASN B CG  1 
ATOM   1310 O OD1 . ASN B 1 73 ? 7.466   -16.091 -27.171 1.00 33.15 ? 72  ASN B OD1 1 
ATOM   1311 N ND2 . ASN B 1 73 ? 8.154   -17.284 -28.966 1.00 30.75 ? 72  ASN B ND2 1 
ATOM   1312 N N   . LYS B 1 74 ? 4.693   -16.273 -25.886 1.00 38.91 ? 73  LYS B N   1 
ATOM   1313 C CA  . LYS B 1 74 ? 4.568   -15.743 -24.524 1.00 45.24 ? 73  LYS B CA  1 
ATOM   1314 C C   . LYS B 1 74 ? 5.909   -15.693 -23.763 1.00 43.97 ? 73  LYS B C   1 
ATOM   1315 O O   . LYS B 1 74 ? 5.940   -15.536 -22.533 1.00 40.03 ? 73  LYS B O   1 
ATOM   1316 C CB  . LYS B 1 74 ? 3.462   -16.522 -23.792 1.00 40.93 ? 73  LYS B CB  1 
ATOM   1317 N N   . ARG B 1 75 ? 7.041   -15.802 -24.468 1.00 32.19 ? 74  ARG B N   1 
ATOM   1318 C CA  . ARG B 1 75 ? 8.331   -15.631 -23.811 1.00 29.00 ? 74  ARG B CA  1 
ATOM   1319 C C   . ARG B 1 75 ? 8.628   -14.132 -23.656 1.00 30.86 ? 74  ARG B C   1 
ATOM   1320 O O   . ARG B 1 75 ? 8.460   -13.327 -24.566 1.00 33.05 ? 74  ARG B O   1 
ATOM   1321 C CB  . ARG B 1 75 ? 9.486   -16.417 -24.470 1.00 30.36 ? 74  ARG B CB  1 
ATOM   1322 C CG  . ARG B 1 75 ? 9.290   -17.911 -24.702 1.00 29.26 ? 74  ARG B CG  1 
ATOM   1323 C CD  . ARG B 1 75 ? 9.285   -18.705 -23.389 1.00 30.07 ? 74  ARG B CD  1 
ATOM   1324 N NE  . ARG B 1 75 ? 9.441   -20.139 -23.653 1.00 29.21 ? 74  ARG B NE  1 
ATOM   1325 C CZ  . ARG B 1 75 ? 10.571  -20.776 -23.455 1.00 29.68 ? 74  ARG B CZ  1 
ATOM   1326 N NH1 . ARG B 1 75 ? 11.656  -20.124 -23.017 1.00 33.57 ? 74  ARG B NH1 1 
ATOM   1327 N NH2 . ARG B 1 75 ? 10.642  -22.062 -23.773 1.00 35.53 ? 74  ARG B NH2 1 
ATOM   1328 N N   . LYS B 1 76 ? 9.045   -13.725 -22.448 1.00 28.50 ? 75  LYS B N   1 
ATOM   1329 C CA  . LYS B 1 76 ? 9.425   -12.348 -22.182 1.00 26.15 ? 75  LYS B CA  1 
ATOM   1330 C C   . LYS B 1 76 ? 10.533  -11.853 -23.138 1.00 25.58 ? 75  LYS B C   1 
ATOM   1331 O O   . LYS B 1 76 ? 11.622  -12.448 -23.198 1.00 28.01 ? 75  LYS B O   1 
ATOM   1332 C CB  . LYS B 1 76 ? 9.919   -12.312 -20.713 1.00 28.29 ? 75  LYS B CB  1 
ATOM   1333 C CG  . LYS B 1 76 ? 10.389  -10.915 -20.258 1.00 29.53 ? 75  LYS B CG  1 
ATOM   1334 C CD  . LYS B 1 76 ? 10.747  -10.772 -18.786 1.00 32.04 ? 75  LYS B CD  1 
ATOM   1335 C CE  . LYS B 1 76 ? 11.188  -9.370  -18.435 1.00 35.59 ? 75  LYS B CE  1 
ATOM   1336 N NZ  . LYS B 1 76 ? 11.493  -9.280  -16.994 1.00 42.52 ? 75  LYS B NZ  1 
ATOM   1337 N N   . GLY B 1 77 ? 10.187  -10.763 -23.835 1.00 26.61 ? 76  GLY B N   1 
ATOM   1338 C CA  . GLY B 1 77 ? 11.119  -10.045 -24.713 1.00 25.56 ? 76  GLY B CA  1 
ATOM   1339 C C   . GLY B 1 77 ? 10.963  -10.499 -26.165 1.00 28.42 ? 76  GLY B C   1 
ATOM   1340 O O   . GLY B 1 77 ? 11.484  -9.871  -27.087 1.00 27.81 ? 76  GLY B O   1 
ATOM   1341 N N   . PHE B 1 78 ? 10.263  -11.605 -26.382 1.00 28.14 ? 77  PHE B N   1 
ATOM   1342 C CA  . PHE B 1 78 ? 10.114  -12.097 -27.757 1.00 26.67 ? 77  PHE B CA  1 
ATOM   1343 C C   . PHE B 1 78 ? 9.376   -11.120 -28.680 1.00 30.06 ? 77  PHE B C   1 
ATOM   1344 O O   . PHE B 1 78 ? 9.807   -10.840 -29.816 1.00 27.31 ? 77  PHE B O   1 
ATOM   1345 C CB  . PHE B 1 78 ? 9.453   -13.473 -27.786 1.00 27.62 ? 77  PHE B CB  1 
ATOM   1346 C CG  . PHE B 1 78 ? 9.684   -14.175 -29.115 1.00 25.83 ? 77  PHE B CG  1 
ATOM   1347 C CD1 . PHE B 1 78 ? 10.768  -15.029 -29.242 1.00 24.39 ? 77  PHE B CD1 1 
ATOM   1348 C CD2 . PHE B 1 78 ? 8.762   -14.043 -30.152 1.00 28.23 ? 77  PHE B CD2 1 
ATOM   1349 C CE1 . PHE B 1 78 ? 11.001  -15.656 -30.471 1.00 25.23 ? 77  PHE B CE1 1 
ATOM   1350 C CE2 . PHE B 1 78 ? 8.983   -14.699 -31.374 1.00 28.05 ? 77  PHE B CE2 1 
ATOM   1351 C CZ  . PHE B 1 78 ? 10.094  -15.516 -31.497 1.00 26.11 ? 77  PHE B CZ  1 
ATOM   1352 N N   . ASN B 1 79 ? 8.162   -10.693 -28.327 1.00 27.23 ? 78  ASN B N   1 
ATOM   1353 C CA  . ASN B 1 79 ? 7.450   -9.801  -29.238 1.00 29.91 ? 78  ASN B CA  1 
ATOM   1354 C C   . ASN B 1 79 ? 8.172   -8.446  -29.390 1.00 31.63 ? 78  ASN B C   1 
ATOM   1355 O O   . ASN B 1 79 ? 8.183   -7.892  -30.492 1.00 30.28 ? 78  ASN B O   1 
ATOM   1356 C CB  . ASN B 1 79 ? 5.952   -9.706  -28.939 1.00 32.70 ? 78  ASN B CB  1 
ATOM   1357 C CG  . ASN B 1 79 ? 5.285   -11.062 -28.894 1.00 38.28 ? 78  ASN B CG  1 
ATOM   1358 O OD1 . ASN B 1 79 ? 5.849   -12.059 -29.375 1.00 35.75 ? 78  ASN B OD1 1 
ATOM   1359 N ND2 . ASN B 1 79 ? 4.131   -11.139 -28.241 1.00 37.20 ? 78  ASN B ND2 1 
ATOM   1360 N N   . GLU B 1 80 ? 8.851   -7.966  -28.348 1.00 29.57 ? 79  GLU B N   1 
ATOM   1361 C CA  . GLU B 1 80 ? 9.651   -6.752  -28.472 1.00 30.63 ? 79  GLU B CA  1 
ATOM   1362 C C   . GLU B 1 80 ? 10.763  -6.999  -29.498 1.00 28.44 ? 79  GLU B C   1 
ATOM   1363 O O   . GLU B 1 80 ? 10.999  -6.144  -30.358 1.00 28.90 ? 79  GLU B O   1 
ATOM   1364 C CB  . GLU B 1 80 ? 10.267  -6.324  -27.144 1.00 31.61 ? 79  GLU B CB  1 
ATOM   1365 C CG  . GLU B 1 80 ? 9.242   -5.811  -26.135 1.00 42.64 ? 79  GLU B CG  1 
ATOM   1366 N N   . GLY B 1 81 ? 11.360  -8.197  -29.420 1.00 27.24 ? 80  GLY B N   1 
ATOM   1367 C CA  . GLY B 1 81 ? 12.426  -8.656  -30.313 1.00 27.67 ? 80  GLY B CA  1 
ATOM   1368 C C   . GLY B 1 81 ? 11.941  -8.693  -31.762 1.00 27.26 ? 80  GLY B C   1 
ATOM   1369 O O   . GLY B 1 81 ? 12.693  -8.281  -32.663 1.00 27.03 ? 80  GLY B O   1 
ATOM   1370 N N   . LEU B 1 82 ? 10.693  -9.117  -31.997 1.00 25.31 ? 81  LEU B N   1 
ATOM   1371 C CA  . LEU B 1 82 ? 10.157  -9.163  -33.350 1.00 28.05 ? 81  LEU B CA  1 
ATOM   1372 C C   . LEU B 1 82 ? 10.018  -7.732  -33.865 1.00 27.56 ? 81  LEU B C   1 
ATOM   1373 O O   . LEU B 1 82 ? 10.211  -7.465  -35.053 1.00 27.93 ? 81  LEU B O   1 
ATOM   1374 C CB  . LEU B 1 82 ? 8.823   -9.926  -33.420 1.00 28.85 ? 81  LEU B CB  1 
ATOM   1375 C CG  . LEU B 1 82 ? 8.895   -11.444 -33.240 1.00 27.44 ? 81  LEU B CG  1 
ATOM   1376 C CD1 . LEU B 1 82 ? 7.474   -12.076 -33.234 1.00 28.29 ? 81  LEU B CD1 1 
ATOM   1377 C CD2 . LEU B 1 82 ? 9.830   -12.151 -34.250 1.00 26.79 ? 81  LEU B CD2 1 
ATOM   1378 N N   . TRP B 1 83 ? 9.636   -6.815  -32.968 1.00 27.19 ? 82  TRP B N   1 
ATOM   1379 C CA  . TRP B 1 83 ? 9.485   -5.407  -33.314 1.00 29.27 ? 82  TRP B CA  1 
ATOM   1380 C C   . TRP B 1 83 ? 10.823  -4.812  -33.735 1.00 28.37 ? 82  TRP B C   1 
ATOM   1381 O O   . TRP B 1 83 ? 10.899  -4.193  -34.810 1.00 28.13 ? 82  TRP B O   1 
ATOM   1382 C CB  . TRP B 1 83 ? 8.866   -4.591  -32.165 1.00 29.16 ? 82  TRP B CB  1 
ATOM   1383 C CG  . TRP B 1 83 ? 8.585   -3.182  -32.637 1.00 31.16 ? 82  TRP B CG  1 
ATOM   1384 C CD1 . TRP B 1 83 ? 7.440   -2.726  -33.228 1.00 37.56 ? 82  TRP B CD1 1 
ATOM   1385 C CD2 . TRP B 1 83 ? 9.522   -2.076  -32.671 1.00 35.27 ? 82  TRP B CD2 1 
ATOM   1386 N NE1 . TRP B 1 83 ? 7.589   -1.411  -33.598 1.00 38.11 ? 82  TRP B NE1 1 
ATOM   1387 C CE2 . TRP B 1 83 ? 8.851   -0.984  -33.277 1.00 35.61 ? 82  TRP B CE2 1 
ATOM   1388 C CE3 . TRP B 1 83 ? 10.846  -1.887  -32.238 1.00 32.73 ? 82  TRP B CE3 1 
ATOM   1389 C CZ2 . TRP B 1 83 ? 9.459   0.271   -33.448 1.00 33.42 ? 82  TRP B CZ2 1 
ATOM   1390 C CZ3 . TRP B 1 83 ? 11.437  -0.646  -32.397 1.00 34.34 ? 82  TRP B CZ3 1 
ATOM   1391 C CH2 . TRP B 1 83 ? 10.758  0.413   -33.004 1.00 33.41 ? 82  TRP B CH2 1 
ATOM   1392 N N   . GLU B 1 84 ? 11.878  -5.162  -32.986 1.00 25.96 ? 83  GLU B N   1 
ATOM   1393 C CA  . GLU B 1 84 ? 13.210  -4.618  -33.191 1.00 29.48 ? 83  GLU B CA  1 
ATOM   1394 C C   . GLU B 1 84 ? 13.780  -5.113  -34.521 1.00 26.06 ? 83  GLU B C   1 
ATOM   1395 O O   . GLU B 1 84 ? 14.373  -4.318  -35.272 1.00 28.25 ? 83  GLU B O   1 
ATOM   1396 C CB  . GLU B 1 84 ? 14.130  -4.863  -32.008 1.00 27.01 ? 83  GLU B CB  1 
ATOM   1397 C CG  . GLU B 1 84 ? 13.670  -4.153  -30.728 1.00 27.27 ? 83  GLU B CG  1 
ATOM   1398 C CD  . GLU B 1 84 ? 14.578  -4.510  -29.602 1.00 28.89 ? 83  GLU B CD  1 
ATOM   1399 O OE1 . GLU B 1 84 ? 15.482  -5.381  -29.730 1.00 28.50 ? 83  GLU B OE1 1 
ATOM   1400 O OE2 . GLU B 1 84 ? 14.378  -3.894  -28.499 1.00 30.37 ? 83  GLU B OE2 1 
ATOM   1401 N N   . ILE B 1 85 ? 13.628  -6.413  -34.796 1.00 27.33 ? 84  ILE B N   1 
ATOM   1402 C CA  . ILE B 1 85 ? 14.330  -6.962  -35.960 1.00 25.71 ? 84  ILE B CA  1 
ATOM   1403 C C   . ILE B 1 85 ? 13.713  -6.405  -37.244 1.00 25.67 ? 84  ILE B C   1 
ATOM   1404 O O   . ILE B 1 85 ? 14.425  -6.169  -38.226 1.00 26.67 ? 84  ILE B O   1 
ATOM   1405 C CB  . ILE B 1 85 ? 14.395  -8.502  -35.944 1.00 24.82 ? 84  ILE B CB  1 
ATOM   1406 C CG1 . ILE B 1 85 ? 15.424  -9.024  -36.969 1.00 25.79 ? 84  ILE B CG1 1 
ATOM   1407 C CG2 . ILE B 1 85 ? 13.028  -9.122  -36.209 1.00 25.47 ? 84  ILE B CG2 1 
ATOM   1408 C CD1 . ILE B 1 85 ? 15.860  -10.443 -36.668 1.00 25.27 ? 84  ILE B CD1 1 
ATOM   1409 N N   . GLN B 1 86 ? 12.418  -6.094  -37.174 1.00 26.04 ? 85  GLN B N   1 
ATOM   1410 C CA  . GLN B 1 86 ? 11.654  -5.526  -38.267 1.00 28.24 ? 85  GLN B CA  1 
ATOM   1411 C C   . GLN B 1 86 ? 11.919  -4.026  -38.417 1.00 31.83 ? 85  GLN B C   1 
ATOM   1412 O O   . GLN B 1 86 ? 12.089  -3.543  -39.536 1.00 33.97 ? 85  GLN B O   1 
ATOM   1413 C CB  . GLN B 1 86 ? 10.186  -5.842  -37.969 1.00 34.32 ? 85  GLN B CB  1 
ATOM   1414 N N   . ASN B 1 87 ? 11.936  -3.284  -37.302 1.00 26.35 ? 86  ASN B N   1 
ATOM   1415 C CA  . ASN B 1 87 ? 11.835  -1.830  -37.454 1.00 29.38 ? 86  ASN B CA  1 
ATOM   1416 C C   . ASN B 1 87 ? 13.156  -1.106  -37.226 1.00 28.13 ? 86  ASN B C   1 
ATOM   1417 O O   . ASN B 1 87 ? 13.294  0.046   -37.681 1.00 31.24 ? 86  ASN B O   1 
ATOM   1418 C CB  . ASN B 1 87 ? 10.847  -1.255  -36.437 1.00 32.13 ? 86  ASN B CB  1 
ATOM   1419 C CG  . ASN B 1 87 ? 9.446   -1.666  -36.811 1.00 36.62 ? 86  ASN B CG  1 
ATOM   1420 O OD1 . ASN B 1 87 ? 8.865   -1.110  -37.745 1.00 44.71 ? 86  ASN B OD1 1 
ATOM   1421 N ND2 . ASN B 1 87 ? 8.906   -2.673  -36.152 1.00 39.47 ? 86  ASN B ND2 1 
ATOM   1422 N N   . ASN B 1 88 ? 14.089  -1.692  -36.469 1.00 28.65 ? 87  ASN B N   1 
ATOM   1423 C CA  . ASN B 1 88 ? 15.352  -0.997  -36.257 1.00 29.75 ? 87  ASN B CA  1 
ATOM   1424 C C   . ASN B 1 88 ? 16.443  -1.987  -35.862 1.00 26.48 ? 87  ASN B C   1 
ATOM   1425 O O   . ASN B 1 88 ? 17.056  -1.905  -34.788 1.00 27.10 ? 87  ASN B O   1 
ATOM   1426 C CB  . ASN B 1 88 ? 15.234  0.172   -35.275 1.00 34.00 ? 87  ASN B CB  1 
ATOM   1427 C CG  . ASN B 1 88 ? 16.319  1.209   -35.469 1.00 34.14 ? 87  ASN B CG  1 
ATOM   1428 O OD1 . ASN B 1 88 ? 17.365  1.004   -36.115 1.00 31.50 ? 87  ASN B OD1 1 
ATOM   1429 N ND2 . ASN B 1 88 ? 16.066  2.376   -34.898 1.00 35.44 ? 87  ASN B ND2 1 
ATOM   1430 N N   . PRO B 1 89 ? 16.722  -2.972  -36.763 1.00 26.91 ? 88  PRO B N   1 
ATOM   1431 C CA  . PRO B 1 89 ? 17.675  -4.036  -36.449 1.00 24.74 ? 88  PRO B CA  1 
ATOM   1432 C C   . PRO B 1 89 ? 19.115  -3.610  -36.174 1.00 25.08 ? 88  PRO B C   1 
ATOM   1433 O O   . PRO B 1 89 ? 19.872  -4.382  -35.597 1.00 25.82 ? 88  PRO B O   1 
ATOM   1434 C CB  . PRO B 1 89 ? 17.581  -4.970  -37.699 1.00 25.22 ? 88  PRO B CB  1 
ATOM   1435 C CG  . PRO B 1 89 ? 17.147  -4.032  -38.840 1.00 25.15 ? 88  PRO B CG  1 
ATOM   1436 C CD  . PRO B 1 89 ? 16.209  -3.035  -38.151 1.00 25.53 ? 88  PRO B CD  1 
ATOM   1437 N N   . HIS B 1 90 ? 19.520  -2.404  -36.663 1.00 26.05 ? 89  HIS B N   1 
ATOM   1438 C CA  . HIS B 1 90 ? 20.921  -2.011  -36.630 1.00 26.44 ? 89  HIS B CA  1 
ATOM   1439 C C   . HIS B 1 90 ? 21.165  -0.914  -35.590 1.00 28.22 ? 89  HIS B C   1 
ATOM   1440 O O   . HIS B 1 90 ? 22.281  -0.412  -35.492 1.00 28.62 ? 89  HIS B O   1 
ATOM   1441 C CB  . HIS B 1 90 ? 21.400  -1.585  -38.029 1.00 26.14 ? 89  HIS B CB  1 
ATOM   1442 C CG  . HIS B 1 90 ? 21.225  -2.698  -39.010 1.00 29.47 ? 89  HIS B CG  1 
ATOM   1443 N ND1 . HIS B 1 90 ? 21.845  -3.921  -38.902 1.00 27.24 ? 89  HIS B ND1 1 
ATOM   1444 C CD2 . HIS B 1 90 ? 20.554  -2.711  -40.170 1.00 26.02 ? 89  HIS B CD2 1 
ATOM   1445 C CE1 . HIS B 1 90 ? 21.511  -4.662  -39.964 1.00 25.66 ? 89  HIS B CE1 1 
ATOM   1446 N NE2 . HIS B 1 90 ? 20.748  -3.943  -40.737 1.00 26.82 ? 89  HIS B NE2 1 
ATOM   1447 N N   . ALA B 1 91 ? 20.167  -0.697  -34.729 1.00 28.20 ? 90  ALA B N   1 
ATOM   1448 C CA  . ALA B 1 91 ? 20.280  0.328   -33.694 1.00 29.09 ? 90  ALA B CA  1 
ATOM   1449 C C   . ALA B 1 91 ? 21.247  -0.079  -32.582 1.00 33.33 ? 90  ALA B C   1 
ATOM   1450 O O   . ALA B 1 91 ? 21.551  -1.250  -32.358 1.00 29.00 ? 90  ALA B O   1 
ATOM   1451 C CB  . ALA B 1 91 ? 18.902  0.678   -33.169 1.00 28.51 ? 90  ALA B CB  1 
ATOM   1452 N N   . SER B 1 92 ? 21.738  0.942   -31.856 1.00 32.63 ? 91  SER B N   1 
ATOM   1453 C CA  . SER B 1 92 ? 22.365  0.749   -30.565 1.00 34.59 ? 91  SER B CA  1 
ATOM   1454 C C   . SER B 1 92 ? 21.266  0.561   -29.514 1.00 35.82 ? 91  SER B C   1 
ATOM   1455 O O   . SER B 1 92 ? 20.358  1.399   -29.411 1.00 37.55 ? 91  SER B O   1 
ATOM   1456 C CB  . SER B 1 92 ? 23.197  1.994   -30.218 1.00 37.20 ? 91  SER B CB  1 
ATOM   1457 O OG  . SER B 1 92 ? 23.811  1.774   -28.959 1.00 46.42 ? 91  SER B OG  1 
ATOM   1458 N N   . TYR B 1 93 ? 21.357  -0.576  -28.802 1.00 35.75 ? 92  TYR B N   1 
ATOM   1459 C CA  . TYR B 1 93 ? 20.517  -1.006  -27.701 1.00 38.73 ? 92  TYR B CA  1 
ATOM   1460 C C   . TYR B 1 93 ? 21.340  -1.001  -26.414 1.00 44.88 ? 92  TYR B C   1 
ATOM   1461 O O   . TYR B 1 93 ? 20.883  -1.481  -25.381 1.00 47.21 ? 92  TYR B O   1 
ATOM   1462 C CB  . TYR B 1 93 ? 19.936  -2.391  -28.007 1.00 33.57 ? 92  TYR B CB  1 
ATOM   1463 C CG  . TYR B 1 93 ? 18.933  -2.318  -29.146 1.00 30.17 ? 92  TYR B CG  1 
ATOM   1464 C CD1 . TYR B 1 93 ? 17.621  -1.899  -28.915 1.00 30.84 ? 92  TYR B CD1 1 
ATOM   1465 C CD2 . TYR B 1 93 ? 19.275  -2.634  -30.472 1.00 31.90 ? 92  TYR B CD2 1 
ATOM   1466 C CE1 . TYR B 1 93 ? 16.704  -1.756  -29.940 1.00 29.93 ? 92  TYR B CE1 1 
ATOM   1467 C CE2 . TYR B 1 93 ? 18.353  -2.505  -31.498 1.00 29.96 ? 92  TYR B CE2 1 
ATOM   1468 C CZ  . TYR B 1 93 ? 17.058  -2.080  -31.241 1.00 29.58 ? 92  TYR B CZ  1 
ATOM   1469 O OH  . TYR B 1 93 ? 16.054  -1.953  -32.174 1.00 30.85 ? 92  TYR B OH  1 
ATOM   1470 N N   . SER B 1 94 ? 22.533  -0.399  -26.492 1.00 56.10 ? 93  SER B N   1 
ATOM   1471 C CA  . SER B 1 94 ? 23.459  -0.259  -25.377 1.00 62.83 ? 93  SER B CA  1 
ATOM   1472 C C   . SER B 1 94 ? 22.965  0.807   -24.387 1.00 70.73 ? 93  SER B C   1 
ATOM   1473 O O   . SER B 1 94 ? 22.321  1.773   -24.856 1.00 65.72 ? 93  SER B O   1 
ATOM   1474 C CB  . SER B 1 94 ? 24.837  0.093   -25.868 1.00 64.10 ? 93  SER B CB  1 
ATOM   1475 O OG  . SER B 1 94 ? 25.601  -1.084  -26.069 1.00 75.96 ? 93  SER B OG  1 
ATOM   1476 O OXT . SER B 1 94 ? 23.271  0.647   -23.178 1.00 80.61 ? 93  SER B OXT 1 
ATOM   1477 N N   . HIS C 1 4  ? 33.277  -23.711 28.536  1.00 77.90 ? 3   HIS C N   1 
ATOM   1478 C CA  . HIS C 1 4  ? 31.968  -23.066 28.237  1.00 70.76 ? 3   HIS C CA  1 
ATOM   1479 C C   . HIS C 1 4  ? 30.948  -23.516 29.284  1.00 71.25 ? 3   HIS C C   1 
ATOM   1480 O O   . HIS C 1 4  ? 31.225  -24.397 30.096  1.00 68.50 ? 3   HIS C O   1 
ATOM   1481 C CB  . HIS C 1 4  ? 31.573  -23.342 26.781  1.00 60.05 ? 3   HIS C CB  1 
ATOM   1482 N N   . ALA C 1 5  ? 29.768  -22.892 29.268  1.00 68.14 ? 4   ALA C N   1 
ATOM   1483 C CA  . ALA C 1 5  ? 28.731  -23.208 30.234  1.00 62.33 ? 4   ALA C CA  1 
ATOM   1484 C C   . ALA C 1 5  ? 27.389  -23.309 29.532  1.00 69.35 ? 4   ALA C C   1 
ATOM   1485 O O   . ALA C 1 5  ? 27.132  -22.601 28.558  1.00 70.90 ? 4   ALA C O   1 
ATOM   1486 C CB  . ALA C 1 5  ? 28.653  -22.119 31.256  1.00 70.76 ? 4   ALA C CB  1 
ATOM   1487 N N   . PHE C 1 6  ? 26.525  -24.155 30.090  1.00 51.35 ? 5   PHE C N   1 
ATOM   1488 C CA  . PHE C 1 6  ? 25.201  -24.329 29.540  1.00 57.43 ? 5   PHE C CA  1 
ATOM   1489 C C   . PHE C 1 6  ? 24.236  -24.447 30.711  1.00 61.71 ? 5   PHE C C   1 
ATOM   1490 O O   . PHE C 1 6  ? 23.966  -25.550 31.189  1.00 77.73 ? 5   PHE C O   1 
ATOM   1491 C CB  . PHE C 1 6  ? 25.235  -25.533 28.589  1.00 45.41 ? 5   PHE C CB  1 
ATOM   1492 C CG  . PHE C 1 6  ? 26.111  -25.408 27.346  1.00 42.74 ? 5   PHE C CG  1 
ATOM   1493 C CD1 . PHE C 1 6  ? 27.288  -26.131 27.203  1.00 43.83 ? 5   PHE C CD1 1 
ATOM   1494 C CD2 . PHE C 1 6  ? 25.750  -24.559 26.304  1.00 45.54 ? 5   PHE C CD2 1 
ATOM   1495 C CE1 . PHE C 1 6  ? 28.055  -26.041 26.041  1.00 52.13 ? 5   PHE C CE1 1 
ATOM   1496 C CE2 . PHE C 1 6  ? 26.512  -24.471 25.151  1.00 41.01 ? 5   PHE C CE2 1 
ATOM   1497 C CZ  . PHE C 1 6  ? 27.662  -25.204 25.011  1.00 43.80 ? 5   PHE C CZ  1 
ATOM   1498 N N   . LYS C 1 7  ? 23.767  -23.293 31.190  1.00 60.36 ? 6   LYS C N   1 
ATOM   1499 C CA  . LYS C 1 7  ? 22.749  -23.266 32.227  1.00 60.49 ? 6   LYS C CA  1 
ATOM   1500 C C   . LYS C 1 7  ? 21.467  -23.767 31.575  1.00 46.08 ? 6   LYS C C   1 
ATOM   1501 O O   . LYS C 1 7  ? 21.363  -23.727 30.351  1.00 54.10 ? 6   LYS C O   1 
ATOM   1502 C CB  . LYS C 1 7  ? 22.590  -21.862 32.832  1.00 58.64 ? 6   LYS C CB  1 
ATOM   1503 N N   . PRO C 1 8  ? 20.472  -24.273 32.336  1.00 52.65 ? 7   PRO C N   1 
ATOM   1504 C CA  . PRO C 1 8  ? 19.172  -24.605 31.756  1.00 48.60 ? 7   PRO C CA  1 
ATOM   1505 C C   . PRO C 1 8  ? 18.655  -23.425 30.927  1.00 60.60 ? 7   PRO C C   1 
ATOM   1506 O O   . PRO C 1 8  ? 18.975  -22.268 31.220  1.00 57.72 ? 7   PRO C O   1 
ATOM   1507 C CB  . PRO C 1 8  ? 18.326  -24.907 33.001  1.00 53.59 ? 7   PRO C CB  1 
ATOM   1508 C CG  . PRO C 1 8  ? 19.330  -25.501 33.959  1.00 52.24 ? 7   PRO C CG  1 
ATOM   1509 C CD  . PRO C 1 8  ? 20.558  -24.617 33.770  1.00 49.33 ? 7   PRO C CD  1 
ATOM   1510 N N   . GLY C 1 9  ? 17.929  -23.747 29.844  1.00 53.92 ? 8   GLY C N   1 
ATOM   1511 C CA  . GLY C 1 9  ? 17.185  -22.779 29.048  1.00 52.85 ? 8   GLY C CA  1 
ATOM   1512 C C   . GLY C 1 9  ? 17.966  -22.295 27.827  1.00 48.46 ? 8   GLY C C   1 
ATOM   1513 O O   . GLY C 1 9  ? 17.352  -21.831 26.864  1.00 47.99 ? 8   GLY C O   1 
ATOM   1514 N N   . ASP C 1 10 ? 19.300  -22.413 27.896  1.00 47.05 ? 9   ASP C N   1 
ATOM   1515 C CA  . ASP C 1 10 ? 20.248  -22.084 26.845  1.00 41.63 ? 9   ASP C CA  1 
ATOM   1516 C C   . ASP C 1 10 ? 19.894  -22.811 25.542  1.00 45.32 ? 9   ASP C C   1 
ATOM   1517 O O   . ASP C 1 10 ? 19.493  -23.979 25.548  1.00 40.83 ? 9   ASP C O   1 
ATOM   1518 C CB  . ASP C 1 10 ? 21.688  -22.384 27.243  1.00 46.93 ? 9   ASP C CB  1 
ATOM   1519 C CG  . ASP C 1 10 ? 22.372  -21.443 28.237  1.00 57.54 ? 9   ASP C CG  1 
ATOM   1520 O OD1 . ASP C 1 10 ? 21.730  -20.473 28.665  1.00 59.63 ? 9   ASP C OD1 1 
ATOM   1521 O OD2 . ASP C 1 10 ? 23.556  -21.686 28.575  1.00 58.60 ? 9   ASP C OD2 1 
ATOM   1522 N N   . LEU C 1 11 ? 20.026  -22.083 24.424  1.00 40.33 ? 10  LEU C N   1 
ATOM   1523 C CA  . LEU C 1 11 ? 19.666  -22.596 23.115  1.00 38.08 ? 10  LEU C CA  1 
ATOM   1524 C C   . LEU C 1 11 ? 20.928  -23.059 22.416  1.00 34.16 ? 10  LEU C C   1 
ATOM   1525 O O   . LEU C 1 11 ? 21.941  -22.359 22.447  1.00 34.83 ? 10  LEU C O   1 
ATOM   1526 C CB  . LEU C 1 11 ? 19.010  -21.470 22.312  1.00 36.53 ? 10  LEU C CB  1 
ATOM   1527 C CG  . LEU C 1 11 ? 17.764  -20.861 22.936  1.00 36.31 ? 10  LEU C CG  1 
ATOM   1528 C CD1 . LEU C 1 11 ? 17.256  -19.859 21.923  1.00 36.74 ? 10  LEU C CD1 1 
ATOM   1529 C CD2 . LEU C 1 11 ? 16.754  -21.959 23.241  1.00 36.22 ? 10  LEU C CD2 1 
ATOM   1530 N N   . VAL C 1 12 ? 20.853  -24.227 21.733  1.00 30.68 ? 11  VAL C N   1 
ATOM   1531 C CA  . VAL C 1 12 ? 22.059  -24.830 21.193  1.00 31.34 ? 11  VAL C CA  1 
ATOM   1532 C C   . VAL C 1 12 ? 21.691  -25.565 19.890  1.00 28.62 ? 11  VAL C C   1 
ATOM   1533 O O   . VAL C 1 12 ? 20.496  -25.748 19.630  1.00 29.15 ? 11  VAL C O   1 
ATOM   1534 C CB  . VAL C 1 12 ? 22.696  -25.843 22.175  1.00 32.98 ? 11  VAL C CB  1 
ATOM   1535 C CG1 . VAL C 1 12 ? 23.031  -25.175 23.506  1.00 34.69 ? 11  VAL C CG1 1 
ATOM   1536 C CG2 . VAL C 1 12 ? 21.769  -27.033 22.428  1.00 31.29 ? 11  VAL C CG2 1 
ATOM   1537 N N   . PHE C 1 13 ? 22.738  -25.966 19.159  1.00 31.29 ? 12  PHE C N   1 
ATOM   1538 C CA  . PHE C 1 13 ? 22.695  -27.113 18.255  1.00 29.42 ? 12  PHE C CA  1 
ATOM   1539 C C   . PHE C 1 13 ? 23.404  -28.273 18.957  1.00 29.78 ? 12  PHE C C   1 
ATOM   1540 O O   . PHE C 1 13 ? 24.520  -28.127 19.486  1.00 30.68 ? 12  PHE C O   1 
ATOM   1541 C CB  . PHE C 1 13 ? 23.331  -26.868 16.876  1.00 32.29 ? 12  PHE C CB  1 
ATOM   1542 C CG  . PHE C 1 13 ? 22.547  -25.867 16.046  1.00 33.02 ? 12  PHE C CG  1 
ATOM   1543 C CD1 . PHE C 1 13 ? 21.527  -26.281 15.179  1.00 32.21 ? 12  PHE C CD1 1 
ATOM   1544 C CD2 . PHE C 1 13 ? 22.836  -24.505 16.138  1.00 33.76 ? 12  PHE C CD2 1 
ATOM   1545 C CE1 . PHE C 1 13 ? 20.817  -25.350 14.435  1.00 32.25 ? 12  PHE C CE1 1 
ATOM   1546 C CE2 . PHE C 1 13 ? 22.111  -23.583 15.408  1.00 37.45 ? 12  PHE C CE2 1 
ATOM   1547 C CZ  . PHE C 1 13 ? 21.108  -24.009 14.556  1.00 34.66 ? 12  PHE C CZ  1 
ATOM   1548 N N   . ALA C 1 14 ? 22.759  -29.447 18.951  1.00 30.07 ? 13  ALA C N   1 
ATOM   1549 C CA  . ALA C 1 14 ? 23.204  -30.623 19.685  1.00 26.08 ? 13  ALA C CA  1 
ATOM   1550 C C   . ALA C 1 14 ? 23.467  -31.733 18.673  1.00 30.00 ? 13  ALA C C   1 
ATOM   1551 O O   . ALA C 1 14 ? 22.609  -31.984 17.818  1.00 27.64 ? 13  ALA C O   1 
ATOM   1552 C CB  . ALA C 1 14 ? 22.104  -31.032 20.660  1.00 25.54 ? 13  ALA C CB  1 
ATOM   1553 N N   . LYS C 1 15 ? 24.652  -32.350 18.766  1.00 28.51 ? 14  LYS C N   1 
ATOM   1554 C CA  . LYS C 1 15 ? 25.072  -33.345 17.782  1.00 27.44 ? 14  LYS C CA  1 
ATOM   1555 C C   . LYS C 1 15 ? 25.076  -34.720 18.431  1.00 28.68 ? 14  LYS C C   1 
ATOM   1556 O O   . LYS C 1 15 ? 25.791  -34.964 19.405  1.00 30.73 ? 14  LYS C O   1 
ATOM   1557 C CB  . LYS C 1 15 ? 26.499  -33.061 17.280  1.00 29.28 ? 14  LYS C CB  1 
ATOM   1558 C CG  . LYS C 1 15 ? 26.944  -34.016 16.161  1.00 30.25 ? 14  LYS C CG  1 
ATOM   1559 C CD  . LYS C 1 15 ? 26.113  -33.857 14.881  1.00 30.05 ? 14  LYS C CD  1 
ATOM   1560 C CE  . LYS C 1 15 ? 26.619  -34.695 13.695  1.00 31.04 ? 14  LYS C CE  1 
ATOM   1561 N NZ  . LYS C 1 15 ? 26.498  -36.127 13.978  1.00 30.44 ? 14  LYS C NZ  1 
ATOM   1562 N N   . MET C 1 16 ? 24.252  -35.633 17.895  1.00 26.11 ? 15  MET C N   1 
ATOM   1563 C CA  . MET C 1 16 ? 24.273  -37.052 18.235  1.00 26.34 ? 15  MET C CA  1 
ATOM   1564 C C   . MET C 1 16 ? 24.753  -37.837 17.018  1.00 29.77 ? 15  MET C C   1 
ATOM   1565 O O   . MET C 1 16 ? 24.467  -37.482 15.868  1.00 26.98 ? 15  MET C O   1 
ATOM   1566 C CB  . MET C 1 16 ? 22.839  -37.521 18.537  1.00 28.61 ? 15  MET C CB  1 
ATOM   1567 C CG  . MET C 1 16 ? 22.244  -36.865 19.774  1.00 32.81 ? 15  MET C CG  1 
ATOM   1568 S SD  . MET C 1 16 ? 20.656  -37.656 20.119  1.00 37.39 ? 15  MET C SD  1 
ATOM   1569 C CE  . MET C 1 16 ? 19.698  -36.922 18.778  1.00 37.46 ? 15  MET C CE  1 
ATOM   1570 N N   . LYS C 1 17 ? 25.471  -38.946 17.266  1.00 29.99 ? 16  LYS C N   1 
ATOM   1571 C CA  . LYS C 1 17 ? 25.792  -39.872 16.184  1.00 31.59 ? 16  LYS C CA  1 
ATOM   1572 C C   . LYS C 1 17 ? 24.518  -40.300 15.453  1.00 26.43 ? 16  LYS C C   1 
ATOM   1573 O O   . LYS C 1 17 ? 23.550  -40.742 16.060  1.00 31.06 ? 16  LYS C O   1 
ATOM   1574 C CB  . LYS C 1 17 ? 26.525  -41.079 16.799  1.00 30.54 ? 16  LYS C CB  1 
ATOM   1575 C CG  . LYS C 1 17 ? 27.063  -42.080 15.778  1.00 32.32 ? 16  LYS C CG  1 
ATOM   1576 C CD  . LYS C 1 17 ? 28.260  -41.366 15.174  1.00 34.81 ? 16  LYS C CD  1 
ATOM   1577 C CE  . LYS C 1 17 ? 29.030  -42.314 14.297  1.00 47.01 ? 16  LYS C CE  1 
ATOM   1578 N NZ  . LYS C 1 17 ? 30.215  -41.646 13.761  1.00 41.76 ? 16  LYS C NZ  1 
ATOM   1579 N N   . GLY C 1 18 ? 24.582  -40.179 14.122  1.00 30.13 ? 17  GLY C N   1 
ATOM   1580 C CA  . GLY C 1 18 ? 23.521  -40.642 13.232  1.00 29.82 ? 17  GLY C CA  1 
ATOM   1581 C C   . GLY C 1 18 ? 22.560  -39.510 12.861  1.00 29.48 ? 17  GLY C C   1 
ATOM   1582 O O   . GLY C 1 18 ? 21.555  -39.762 12.207  1.00 28.75 ? 17  GLY C O   1 
ATOM   1583 N N   . TYR C 1 19 ? 22.830  -38.283 13.326  1.00 28.00 ? 18  TYR C N   1 
ATOM   1584 C CA  . TYR C 1 19 ? 21.874  -37.181 13.122  1.00 29.36 ? 18  TYR C CA  1 
ATOM   1585 C C   . TYR C 1 19 ? 22.643  -35.897 12.857  1.00 27.73 ? 18  TYR C C   1 
ATOM   1586 O O   . TYR C 1 19 ? 23.760  -35.716 13.359  1.00 27.12 ? 18  TYR C O   1 
ATOM   1587 C CB  . TYR C 1 19 ? 21.058  -36.877 14.388  1.00 25.82 ? 18  TYR C CB  1 
ATOM   1588 C CG  . TYR C 1 19 ? 20.210  -38.061 14.782  1.00 27.81 ? 18  TYR C CG  1 
ATOM   1589 C CD1 . TYR C 1 19 ? 20.711  -39.084 15.585  1.00 28.35 ? 18  TYR C CD1 1 
ATOM   1590 C CD2 . TYR C 1 19 ? 18.935  -38.171 14.266  1.00 28.59 ? 18  TYR C CD2 1 
ATOM   1591 C CE1 . TYR C 1 19 ? 19.911  -40.160 15.918  1.00 31.52 ? 18  TYR C CE1 1 
ATOM   1592 C CE2 . TYR C 1 19 ? 18.131  -39.245 14.599  1.00 35.77 ? 18  TYR C CE2 1 
ATOM   1593 C CZ  . TYR C 1 19 ? 18.627  -40.235 15.424  1.00 35.09 ? 18  TYR C CZ  1 
ATOM   1594 O OH  . TYR C 1 19 ? 17.802  -41.297 15.721  1.00 44.40 ? 18  TYR C OH  1 
ATOM   1595 N N   . PRO C 1 20 ? 22.095  -34.955 12.063  1.00 25.75 ? 19  PRO C N   1 
ATOM   1596 C CA  . PRO C 1 20 ? 22.759  -33.668 11.846  1.00 25.66 ? 19  PRO C CA  1 
ATOM   1597 C C   . PRO C 1 20 ? 22.700  -32.819 13.119  1.00 26.67 ? 19  PRO C C   1 
ATOM   1598 O O   . PRO C 1 20 ? 21.931  -33.091 14.025  1.00 25.01 ? 19  PRO C O   1 
ATOM   1599 C CB  . PRO C 1 20 ? 21.943  -33.059 10.691  1.00 29.93 ? 19  PRO C CB  1 
ATOM   1600 C CG  . PRO C 1 20 ? 20.560  -33.609 10.896  1.00 28.41 ? 19  PRO C CG  1 
ATOM   1601 C CD  . PRO C 1 20 ? 20.776  -35.041 11.403  1.00 26.49 ? 19  PRO C CD  1 
ATOM   1602 N N   . HIS C 1 21 ? 23.529  -31.778 13.160  1.00 25.80 ? 20  HIS C N   1 
ATOM   1603 C CA  . HIS C 1 21 ? 23.463  -30.871 14.297  1.00 23.48 ? 20  HIS C CA  1 
ATOM   1604 C C   . HIS C 1 21 ? 22.030  -30.355 14.413  1.00 27.08 ? 20  HIS C C   1 
ATOM   1605 O O   . HIS C 1 21 ? 21.471  -29.831 13.459  1.00 28.99 ? 20  HIS C O   1 
ATOM   1606 C CB  . HIS C 1 21 ? 24.439  -29.705 14.121  1.00 29.40 ? 20  HIS C CB  1 
ATOM   1607 C CG  . HIS C 1 21 ? 25.869  -30.147 14.123  1.00 29.90 ? 20  HIS C CG  1 
ATOM   1608 N ND1 . HIS C 1 21 ? 26.537  -30.791 13.105  1.00 34.96 ? 20  HIS C ND1 1 
ATOM   1609 C CD2 . HIS C 1 21 ? 26.776  -29.947 15.103  1.00 33.37 ? 20  HIS C CD2 1 
ATOM   1610 C CE1 . HIS C 1 21 ? 27.791  -31.005 13.477  1.00 36.35 ? 20  HIS C CE1 1 
ATOM   1611 N NE2 . HIS C 1 21 ? 27.951  -30.492 14.687  1.00 33.76 ? 20  HIS C NE2 1 
ATOM   1612 N N   . TRP C 1 22 ? 21.454  -30.497 15.618  1.00 24.33 ? 21  TRP C N   1 
ATOM   1613 C CA  . TRP C 1 22 ? 19.998  -30.377 15.741  1.00 24.38 ? 21  TRP C CA  1 
ATOM   1614 C C   . TRP C 1 22 ? 19.626  -29.211 16.649  1.00 25.22 ? 21  TRP C C   1 
ATOM   1615 O O   . TRP C 1 22 ? 20.201  -29.062 17.757  1.00 24.23 ? 21  TRP C O   1 
ATOM   1616 C CB  . TRP C 1 22 ? 19.433  -31.670 16.337  1.00 23.75 ? 21  TRP C CB  1 
ATOM   1617 C CG  . TRP C 1 22 ? 17.979  -31.876 15.988  1.00 24.28 ? 21  TRP C CG  1 
ATOM   1618 C CD1 . TRP C 1 22 ? 16.882  -31.279 16.532  1.00 27.75 ? 21  TRP C CD1 1 
ATOM   1619 C CD2 . TRP C 1 22 ? 17.507  -32.770 14.950  1.00 24.92 ? 21  TRP C CD2 1 
ATOM   1620 N NE1 . TRP C 1 22 ? 15.754  -31.755 15.911  1.00 26.93 ? 21  TRP C NE1 1 
ATOM   1621 C CE2 . TRP C 1 22 ? 16.096  -32.653 14.934  1.00 27.25 ? 21  TRP C CE2 1 
ATOM   1622 C CE3 . TRP C 1 22 ? 18.143  -33.658 14.068  1.00 26.36 ? 21  TRP C CE3 1 
ATOM   1623 C CZ2 . TRP C 1 22 ? 15.315  -33.410 14.043  1.00 26.17 ? 21  TRP C CZ2 1 
ATOM   1624 C CZ3 . TRP C 1 22 ? 17.381  -34.381 13.159  1.00 27.42 ? 21  TRP C CZ3 1 
ATOM   1625 C CH2 . TRP C 1 22 ? 15.987  -34.254 13.181  1.00 26.87 ? 21  TRP C CH2 1 
ATOM   1626 N N   . PRO C 1 23 ? 18.595  -28.402 16.307  1.00 26.95 ? 22  PRO C N   1 
ATOM   1627 C CA  . PRO C 1 23 ? 18.188  -27.316 17.204  1.00 25.27 ? 22  PRO C CA  1 
ATOM   1628 C C   . PRO C 1 23 ? 17.632  -27.873 18.512  1.00 23.62 ? 22  PRO C C   1 
ATOM   1629 O O   . PRO C 1 23 ? 16.793  -28.768 18.509  1.00 26.16 ? 22  PRO C O   1 
ATOM   1630 C CB  . PRO C 1 23 ? 17.124  -26.567 16.326  1.00 28.43 ? 22  PRO C CB  1 
ATOM   1631 C CG  . PRO C 1 23 ? 16.594  -27.604 15.342  1.00 24.86 ? 22  PRO C CG  1 
ATOM   1632 C CD  . PRO C 1 23 ? 17.858  -28.400 15.014  1.00 24.75 ? 22  PRO C CD  1 
ATOM   1633 N N   . ALA C 1 24 ? 18.108  -27.321 19.630  1.00 27.25 ? 23  ALA C N   1 
ATOM   1634 C CA  . ALA C 1 24 ? 17.793  -27.888 20.936  1.00 32.07 ? 23  ALA C CA  1 
ATOM   1635 C C   . ALA C 1 24 ? 17.929  -26.831 22.030  1.00 32.86 ? 23  ALA C C   1 
ATOM   1636 O O   . ALA C 1 24 ? 18.409  -25.724 21.789  1.00 32.68 ? 23  ALA C O   1 
ATOM   1637 C CB  . ALA C 1 24 ? 18.771  -29.029 21.218  1.00 28.58 ? 23  ALA C CB  1 
ATOM   1638 N N   . ARG C 1 25 ? 17.568  -27.219 23.265  1.00 32.07 ? 24  ARG C N   1 
ATOM   1639 C CA  . ARG C 1 25 ? 17.968  -26.416 24.414  1.00 31.04 ? 24  ARG C CA  1 
ATOM   1640 C C   . ARG C 1 25 ? 18.410  -27.324 25.571  1.00 33.10 ? 24  ARG C C   1 
ATOM   1641 O O   . ARG C 1 25 ? 18.086  -28.508 25.585  1.00 34.09 ? 24  ARG C O   1 
ATOM   1642 C CB  . ARG C 1 25 ? 16.779  -25.595 24.919  1.00 33.98 ? 24  ARG C CB  1 
ATOM   1643 C CG  . ARG C 1 25 ? 15.501  -26.362 25.199  1.00 36.51 ? 24  ARG C CG  1 
ATOM   1644 C CD  . ARG C 1 25 ? 14.478  -25.486 25.954  1.00 40.62 ? 24  ARG C CD  1 
ATOM   1645 N NE  . ARG C 1 25 ? 13.278  -26.315 26.136  1.00 47.17 ? 24  ARG C NE  1 
ATOM   1646 C CZ  . ARG C 1 25 ? 12.011  -26.053 25.851  1.00 52.95 ? 24  ARG C CZ  1 
ATOM   1647 N NH1 . ARG C 1 25 ? 11.661  -24.885 25.344  1.00 47.77 ? 24  ARG C NH1 1 
ATOM   1648 N NH2 . ARG C 1 25 ? 11.087  -26.968 26.102  1.00 51.16 ? 24  ARG C NH2 1 
ATOM   1649 N N   . ILE C 1 26 ? 19.098  -26.706 26.530  1.00 35.37 ? 25  ILE C N   1 
ATOM   1650 C CA  . ILE C 1 26 ? 19.472  -27.316 27.799  1.00 35.56 ? 25  ILE C CA  1 
ATOM   1651 C C   . ILE C 1 26 ? 18.252  -27.308 28.702  1.00 45.28 ? 25  ILE C C   1 
ATOM   1652 O O   . ILE C 1 26 ? 17.668  -26.252 28.915  1.00 46.37 ? 25  ILE C O   1 
ATOM   1653 C CB  . ILE C 1 26 ? 20.620  -26.511 28.434  1.00 38.77 ? 25  ILE C CB  1 
ATOM   1654 C CG1 . ILE C 1 26 ? 21.746  -26.249 27.459  1.00 39.57 ? 25  ILE C CG1 1 
ATOM   1655 C CG2 . ILE C 1 26 ? 21.127  -27.192 29.712  1.00 40.59 ? 25  ILE C CG2 1 
ATOM   1656 C CD1 . ILE C 1 26 ? 22.579  -27.456 27.071  1.00 42.72 ? 25  ILE C CD1 1 
ATOM   1657 N N   . ASP C 1 27 ? 17.885  -28.486 29.209  1.00 43.87 ? 26  ASP C N   1 
ATOM   1658 C CA  . ASP C 1 27 ? 16.837  -28.637 30.209  1.00 54.53 ? 26  ASP C CA  1 
ATOM   1659 C C   . ASP C 1 27 ? 17.388  -28.466 31.630  1.00 49.61 ? 26  ASP C C   1 
ATOM   1660 O O   . ASP C 1 27 ? 18.632  -28.495 31.765  1.00 54.62 ? 26  ASP C O   1 
ATOM   1661 C CB  . ASP C 1 27 ? 16.162  -29.992 30.103  1.00 53.05 ? 26  ASP C CB  1 
ATOM   1662 C CG  . ASP C 1 27 ? 14.874  -29.992 29.303  1.00 62.90 ? 26  ASP C CG  1 
ATOM   1663 O OD1 . ASP C 1 27 ? 14.638  -28.969 28.617  1.00 55.54 ? 26  ASP C OD1 1 
ATOM   1664 O OD2 . ASP C 1 27 ? 14.109  -30.988 29.424  1.00 55.87 ? 26  ASP C OD2 1 
ATOM   1665 N N   . LYS C 1 35 ? 19.613  -38.950 37.608  1.00 53.92 ? 34  LYS C N   1 
ATOM   1666 C CA  . LYS C 1 35 ? 20.754  -38.011 37.433  1.00 54.82 ? 34  LYS C CA  1 
ATOM   1667 C C   . LYS C 1 35 ? 21.430  -38.299 36.089  1.00 51.30 ? 34  LYS C C   1 
ATOM   1668 O O   . LYS C 1 35 ? 21.469  -39.441 35.632  1.00 53.23 ? 34  LYS C O   1 
ATOM   1669 C CB  . LYS C 1 35 ? 21.709  -38.109 38.630  1.00 60.69 ? 34  LYS C CB  1 
ATOM   1670 N N   . PRO C 1 36 ? 21.984  -37.277 35.399  1.00 48.94 ? 35  PRO C N   1 
ATOM   1671 C CA  . PRO C 1 36 ? 22.654  -37.515 34.122  1.00 47.59 ? 35  PRO C CA  1 
ATOM   1672 C C   . PRO C 1 36 ? 23.862  -38.420 34.370  1.00 50.69 ? 35  PRO C C   1 
ATOM   1673 O O   . PRO C 1 36 ? 24.343  -38.557 35.505  1.00 46.00 ? 35  PRO C O   1 
ATOM   1674 C CB  . PRO C 1 36 ? 23.064  -36.105 33.642  1.00 52.84 ? 35  PRO C CB  1 
ATOM   1675 C CG  . PRO C 1 36 ? 22.276  -35.150 34.513  1.00 50.93 ? 35  PRO C CG  1 
ATOM   1676 C CD  . PRO C 1 36 ? 22.016  -35.869 35.832  1.00 49.84 ? 35  PRO C CD  1 
ATOM   1677 N N   . PRO C 1 37 ? 24.413  -39.079 33.330  1.00 47.17 ? 36  PRO C N   1 
ATOM   1678 C CA  . PRO C 1 37 ? 25.744  -39.650 33.469  1.00 45.00 ? 36  PRO C CA  1 
ATOM   1679 C C   . PRO C 1 37 ? 26.650  -38.469 33.792  1.00 42.07 ? 36  PRO C C   1 
ATOM   1680 O O   . PRO C 1 37 ? 26.307  -37.303 33.555  1.00 35.90 ? 36  PRO C O   1 
ATOM   1681 C CB  . PRO C 1 37 ? 26.004  -40.231 32.080  1.00 42.70 ? 36  PRO C CB  1 
ATOM   1682 C CG  . PRO C 1 37 ? 24.611  -40.566 31.603  1.00 42.55 ? 36  PRO C CG  1 
ATOM   1683 C CD  . PRO C 1 37 ? 23.818  -39.345 32.010  1.00 42.00 ? 36  PRO C CD  1 
ATOM   1684 N N   . PRO C 1 38 ? 27.826  -38.746 34.386  1.00 39.33 ? 37  PRO C N   1 
ATOM   1685 C CA  . PRO C 1 38 ? 28.806  -37.706 34.669  1.00 37.51 ? 37  PRO C CA  1 
ATOM   1686 C C   . PRO C 1 38 ? 29.117  -36.831 33.465  1.00 34.73 ? 37  PRO C C   1 
ATOM   1687 O O   . PRO C 1 38 ? 29.387  -37.331 32.370  1.00 34.13 ? 37  PRO C O   1 
ATOM   1688 C CB  . PRO C 1 38 ? 30.043  -38.542 35.108  1.00 39.54 ? 37  PRO C CB  1 
ATOM   1689 C CG  . PRO C 1 38 ? 29.431  -39.782 35.688  1.00 40.38 ? 37  PRO C CG  1 
ATOM   1690 C CD  . PRO C 1 38 ? 28.267  -40.095 34.786  1.00 44.44 ? 37  PRO C CD  1 
ATOM   1691 N N   . ASN C 1 39 ? 29.058  -35.513 33.706  1.00 35.65 ? 38  ASN C N   1 
ATOM   1692 C CA  . ASN C 1 39 ? 29.481  -34.488 32.782  1.00 33.79 ? 38  ASN C CA  1 
ATOM   1693 C C   . ASN C 1 39 ? 28.553  -34.462 31.569  1.00 36.38 ? 38  ASN C C   1 
ATOM   1694 O O   . ASN C 1 39 ? 28.986  -34.073 30.485  1.00 43.62 ? 38  ASN C O   1 
ATOM   1695 C CB  . ASN C 1 39 ? 30.928  -34.672 32.338  1.00 35.17 ? 38  ASN C CB  1 
ATOM   1696 C CG  . ASN C 1 39 ? 31.522  -33.450 31.665  1.00 45.76 ? 38  ASN C CG  1 
ATOM   1697 O OD1 . ASN C 1 39 ? 31.098  -32.312 31.912  1.00 51.70 ? 38  ASN C OD1 1 
ATOM   1698 N ND2 . ASN C 1 39 ? 32.518  -33.655 30.811  1.00 48.90 ? 38  ASN C ND2 1 
ATOM   1699 N N   . LYS C 1 40 ? 27.290  -34.873 31.748  1.00 32.72 ? 39  LYS C N   1 
ATOM   1700 C CA  . LYS C 1 40 ? 26.368  -34.752 30.629  1.00 29.76 ? 39  LYS C CA  1 
ATOM   1701 C C   . LYS C 1 40 ? 25.203  -33.827 30.969  1.00 31.30 ? 39  LYS C C   1 
ATOM   1702 O O   . LYS C 1 40 ? 24.768  -33.730 32.102  1.00 32.94 ? 39  LYS C O   1 
ATOM   1703 C CB  . LYS C 1 40 ? 25.727  -36.093 30.256  1.00 30.06 ? 39  LYS C CB  1 
ATOM   1704 C CG  . LYS C 1 40 ? 26.726  -37.184 29.982  1.00 36.29 ? 39  LYS C CG  1 
ATOM   1705 C CD  . LYS C 1 40 ? 27.642  -36.960 28.792  1.00 41.84 ? 39  LYS C CD  1 
ATOM   1706 C CE  . LYS C 1 40 ? 28.492  -38.175 28.486  1.00 38.74 ? 39  LYS C CE  1 
ATOM   1707 N NZ  . LYS C 1 40 ? 29.366  -37.906 27.336  1.00 47.46 ? 39  LYS C NZ  1 
ATOM   1708 N N   . TYR C 1 41 ? 24.718  -33.120 29.945  1.00 31.23 ? 40  TYR C N   1 
ATOM   1709 C CA  . TYR C 1 41 ? 23.580  -32.218 30.091  1.00 32.35 ? 40  TYR C CA  1 
ATOM   1710 C C   . TYR C 1 41 ? 22.309  -32.882 29.572  1.00 32.00 ? 40  TYR C C   1 
ATOM   1711 O O   . TYR C 1 41 ? 22.342  -33.603 28.568  1.00 31.04 ? 40  TYR C O   1 
ATOM   1712 C CB  . TYR C 1 41 ? 23.707  -30.978 29.195  1.00 29.43 ? 40  TYR C CB  1 
ATOM   1713 C CG  . TYR C 1 41 ? 24.864  -30.085 29.605  1.00 30.28 ? 40  TYR C CG  1 
ATOM   1714 C CD1 . TYR C 1 41 ? 26.147  -30.311 29.121  1.00 32.88 ? 40  TYR C CD1 1 
ATOM   1715 C CD2 . TYR C 1 41 ? 24.685  -29.054 30.532  1.00 35.14 ? 40  TYR C CD2 1 
ATOM   1716 C CE1 . TYR C 1 41 ? 27.223  -29.536 29.514  1.00 40.66 ? 40  TYR C CE1 1 
ATOM   1717 C CE2 . TYR C 1 41 ? 25.753  -28.249 30.895  1.00 34.32 ? 40  TYR C CE2 1 
ATOM   1718 C CZ  . TYR C 1 41 ? 27.015  -28.493 30.402  1.00 38.30 ? 40  TYR C CZ  1 
ATOM   1719 O OH  . TYR C 1 41 ? 28.056  -27.709 30.796  1.00 51.28 ? 40  TYR C OH  1 
ATOM   1720 N N   . PRO C 1 42 ? 21.147  -32.562 30.190  1.00 33.31 ? 41  PRO C N   1 
ATOM   1721 C CA  . PRO C 1 42 ? 19.833  -32.956 29.676  1.00 31.77 ? 41  PRO C CA  1 
ATOM   1722 C C   . PRO C 1 42 ? 19.497  -32.026 28.519  1.00 31.03 ? 41  PRO C C   1 
ATOM   1723 O O   . PRO C 1 42 ? 19.537  -30.805 28.686  1.00 36.58 ? 41  PRO C O   1 
ATOM   1724 C CB  . PRO C 1 42 ? 18.878  -32.769 30.867  1.00 34.83 ? 41  PRO C CB  1 
ATOM   1725 C CG  . PRO C 1 42 ? 19.594  -31.834 31.788  1.00 39.09 ? 41  PRO C CG  1 
ATOM   1726 C CD  . PRO C 1 42 ? 21.066  -31.758 31.429  1.00 38.84 ? 41  PRO C CD  1 
ATOM   1727 N N   . ILE C 1 43 ? 19.279  -32.651 27.352  1.00 31.28 ? 42  ILE C N   1 
ATOM   1728 C CA  . ILE C 1 43 ? 18.968  -31.890 26.145  1.00 30.44 ? 42  ILE C CA  1 
ATOM   1729 C C   . ILE C 1 43 ? 17.520  -32.130 25.740  1.00 29.42 ? 42  ILE C C   1 
ATOM   1730 O O   . ILE C 1 43 ? 17.024  -33.268 25.751  1.00 31.26 ? 42  ILE C O   1 
ATOM   1731 C CB  . ILE C 1 43 ? 19.905  -32.325 25.012  1.00 28.63 ? 42  ILE C CB  1 
ATOM   1732 C CG1 . ILE C 1 43 ? 21.386  -32.120 25.399  1.00 29.69 ? 42  ILE C CG1 1 
ATOM   1733 C CG2 . ILE C 1 43 ? 19.513  -31.564 23.734  1.00 31.40 ? 42  ILE C CG2 1 
ATOM   1734 C CD1 . ILE C 1 43 ? 21.785  -30.698 25.768  1.00 33.04 ? 42  ILE C CD1 1 
ATOM   1735 N N   . PHE C 1 44 ? 16.858  -31.050 25.259  1.00 31.74 ? 43  PHE C N   1 
ATOM   1736 C CA  . PHE C 1 44 ? 15.557  -31.218 24.629  1.00 29.09 ? 43  PHE C CA  1 
ATOM   1737 C C   . PHE C 1 44 ? 15.672  -30.772 23.168  1.00 26.91 ? 43  PHE C C   1 
ATOM   1738 O O   . PHE C 1 44 ? 16.212  -29.678 22.911  1.00 30.19 ? 43  PHE C O   1 
ATOM   1739 C CB  . PHE C 1 44 ? 14.573  -30.249 25.302  1.00 34.47 ? 43  PHE C CB  1 
ATOM   1740 C CG  . PHE C 1 44 ? 13.182  -30.186 24.681  1.00 34.46 ? 43  PHE C CG  1 
ATOM   1741 C CD1 . PHE C 1 44 ? 12.221  -31.166 24.952  1.00 36.15 ? 43  PHE C CD1 1 
ATOM   1742 C CD2 . PHE C 1 44 ? 12.843  -29.149 23.796  1.00 36.28 ? 43  PHE C CD2 1 
ATOM   1743 C CE1 . PHE C 1 44 ? 10.953  -31.108 24.365  1.00 41.99 ? 43  PHE C CE1 1 
ATOM   1744 C CE2 . PHE C 1 44 ? 11.582  -29.095 23.210  1.00 36.89 ? 43  PHE C CE2 1 
ATOM   1745 C CZ  . PHE C 1 44 ? 10.639  -30.068 23.501  1.00 38.78 ? 43  PHE C CZ  1 
ATOM   1746 N N   . PHE C 1 45 ? 15.213  -31.648 22.272  1.00 28.30 ? 44  PHE C N   1 
ATOM   1747 C CA  . PHE C 1 45 ? 15.377  -31.429 20.842  1.00 30.34 ? 44  PHE C CA  1 
ATOM   1748 C C   . PHE C 1 45 ? 14.113  -30.779 20.302  1.00 28.78 ? 44  PHE C C   1 
ATOM   1749 O O   . PHE C 1 45 ? 13.019  -31.335 20.426  1.00 31.22 ? 44  PHE C O   1 
ATOM   1750 C CB  . PHE C 1 45 ? 15.671  -32.734 20.106  1.00 26.91 ? 44  PHE C CB  1 
ATOM   1751 C CG  . PHE C 1 45 ? 17.041  -33.313 20.410  1.00 26.47 ? 44  PHE C CG  1 
ATOM   1752 C CD1 . PHE C 1 45 ? 18.164  -32.902 19.690  1.00 26.96 ? 44  PHE C CD1 1 
ATOM   1753 C CD2 . PHE C 1 45 ? 17.195  -34.242 21.448  1.00 28.81 ? 44  PHE C CD2 1 
ATOM   1754 C CE1 . PHE C 1 45 ? 19.419  -33.426 19.978  1.00 30.03 ? 44  PHE C CE1 1 
ATOM   1755 C CE2 . PHE C 1 45 ? 18.450  -34.783 21.711  1.00 31.70 ? 44  PHE C CE2 1 
ATOM   1756 C CZ  . PHE C 1 45 ? 19.556  -34.365 20.997  1.00 29.96 ? 44  PHE C CZ  1 
ATOM   1757 N N   . PHE C 1 46 ? 14.273  -29.595 19.681  1.00 29.84 ? 45  PHE C N   1 
ATOM   1758 C CA  . PHE C 1 46 ? 13.102  -29.018 19.028  1.00 26.90 ? 45  PHE C CA  1 
ATOM   1759 C C   . PHE C 1 46 ? 12.621  -29.861 17.846  1.00 30.45 ? 45  PHE C C   1 
ATOM   1760 O O   . PHE C 1 46 ? 13.351  -30.645 17.232  1.00 28.48 ? 45  PHE C O   1 
ATOM   1761 C CB  . PHE C 1 46 ? 13.390  -27.579 18.602  1.00 27.94 ? 45  PHE C CB  1 
ATOM   1762 C CG  . PHE C 1 46 ? 13.651  -26.610 19.737  1.00 27.41 ? 45  PHE C CG  1 
ATOM   1763 C CD1 . PHE C 1 46 ? 12.580  -26.111 20.480  1.00 29.60 ? 45  PHE C CD1 1 
ATOM   1764 C CD2 . PHE C 1 46 ? 14.938  -26.130 19.985  1.00 28.68 ? 45  PHE C CD2 1 
ATOM   1765 C CE1 . PHE C 1 46 ? 12.821  -25.201 21.510  1.00 31.38 ? 45  PHE C CE1 1 
ATOM   1766 C CE2 . PHE C 1 46 ? 15.171  -25.236 21.026  1.00 32.99 ? 45  PHE C CE2 1 
ATOM   1767 C CZ  . PHE C 1 46 ? 14.111  -24.763 21.773  1.00 31.83 ? 45  PHE C CZ  1 
ATOM   1768 N N   . GLY C 1 47 ? 11.323  -29.741 17.546  1.00 28.20 ? 46  GLY C N   1 
ATOM   1769 C CA  . GLY C 1 47 ? 10.772  -30.439 16.401  1.00 31.46 ? 46  GLY C CA  1 
ATOM   1770 C C   . GLY C 1 47 ? 10.348  -31.865 16.745  1.00 33.72 ? 46  GLY C C   1 
ATOM   1771 O O   . GLY C 1 47 ? 9.166   -32.211 16.657  1.00 36.83 ? 46  GLY C O   1 
ATOM   1772 N N   . THR C 1 48 ? 11.329  -32.720 17.103  1.00 30.70 ? 47  THR C N   1 
ATOM   1773 C CA  . THR C 1 48 ? 10.971  -34.057 17.558  1.00 32.10 ? 47  THR C CA  1 
ATOM   1774 C C   . THR C 1 48 ? 10.454  -34.017 19.004  1.00 32.38 ? 47  THR C C   1 
ATOM   1775 O O   . THR C 1 48 ? 9.712   -34.921 19.396  1.00 36.85 ? 47  THR C O   1 
ATOM   1776 C CB  . THR C 1 48 ? 12.169  -34.993 17.464  1.00 29.01 ? 47  THR C CB  1 
ATOM   1777 O OG1 . THR C 1 48 ? 13.024  -34.395 18.437  1.00 33.92 ? 47  THR C OG1 1 
ATOM   1778 C CG2 . THR C 1 48 ? 12.745  -35.098 16.061  1.00 28.80 ? 47  THR C CG2 1 
ATOM   1779 N N   . HIS C 1 49 ? 10.808  -32.993 19.785  1.00 31.41 ? 48  HIS C N   1 
ATOM   1780 C CA  . HIS C 1 49 ? 10.538  -32.909 21.216  1.00 35.26 ? 48  HIS C CA  1 
ATOM   1781 C C   . HIS C 1 49 ? 11.028  -34.139 21.991  1.00 35.24 ? 48  HIS C C   1 
ATOM   1782 O O   . HIS C 1 49 ? 10.442  -34.496 23.022  1.00 39.00 ? 48  HIS C O   1 
ATOM   1783 C CB  . HIS C 1 49 ? 9.058   -32.614 21.496  1.00 35.89 ? 48  HIS C CB  1 
ATOM   1784 C CG  . HIS C 1 49 ? 8.493   -31.572 20.585  1.00 38.70 ? 48  HIS C CG  1 
ATOM   1785 N ND1 . HIS C 1 49 ? 7.382   -31.832 19.807  1.00 43.83 ? 48  HIS C ND1 1 
ATOM   1786 C CD2 . HIS C 1 49 ? 8.908   -30.346 20.257  1.00 39.43 ? 48  HIS C CD2 1 
ATOM   1787 C CE1 . HIS C 1 49 ? 7.132   -30.778 19.043  1.00 44.76 ? 48  HIS C CE1 1 
ATOM   1788 N NE2 . HIS C 1 49 ? 8.041   -29.858 19.305  1.00 43.64 ? 48  HIS C NE2 1 
ATOM   1789 N N   . GLU C 1 50 ? 12.136  -34.741 21.552  1.00 34.54 ? 49  GLU C N   1 
ATOM   1790 C CA  . GLU C 1 50 ? 12.728  -35.841 22.301  1.00 35.64 ? 49  GLU C CA  1 
ATOM   1791 C C   . GLU C 1 50 ? 13.832  -35.331 23.222  1.00 36.11 ? 49  GLU C C   1 
ATOM   1792 O O   . GLU C 1 50 ? 14.184  -34.153 23.208  1.00 33.55 ? 49  GLU C O   1 
ATOM   1793 C CB  . GLU C 1 50 ? 13.157  -36.955 21.358  1.00 38.24 ? 49  GLU C CB  1 
ATOM   1794 C CG  . GLU C 1 50 ? 11.971  -37.547 20.602  1.00 43.55 ? 49  GLU C CG  1 
ATOM   1795 C CD  . GLU C 1 50 ? 12.540  -38.436 19.532  1.00 50.39 ? 49  GLU C CD  1 
ATOM   1796 O OE1 . GLU C 1 50 ? 13.785  -38.607 19.506  1.00 55.48 ? 49  GLU C OE1 1 
ATOM   1797 O OE2 . GLU C 1 50 ? 11.737  -38.907 18.707  1.00 60.15 ? 49  GLU C OE2 1 
ATOM   1798 N N   . THR C 1 51 ? 14.312  -36.232 24.101  1.00 39.16 ? 50  THR C N   1 
ATOM   1799 C CA  . THR C 1 51 ? 15.341  -35.901 25.084  1.00 35.29 ? 50  THR C CA  1 
ATOM   1800 C C   . THR C 1 51 ? 16.486  -36.908 25.011  1.00 30.27 ? 50  THR C C   1 
ATOM   1801 O O   . THR C 1 51 ? 16.346  -38.039 24.552  1.00 32.32 ? 50  THR C O   1 
ATOM   1802 C CB  . THR C 1 51 ? 14.770  -35.840 26.500  1.00 38.72 ? 50  THR C CB  1 
ATOM   1803 O OG1 . THR C 1 51 ? 14.215  -37.139 26.721  1.00 39.49 ? 50  THR C OG1 1 
ATOM   1804 C CG2 . THR C 1 51 ? 13.762  -34.720 26.693  1.00 41.73 ? 50  THR C CG2 1 
ATOM   1805 N N   . ALA C 1 52 ? 17.670  -36.425 25.379  1.00 31.51 ? 51  ALA C N   1 
ATOM   1806 C CA  . ALA C 1 52 ? 18.852  -37.259 25.520  1.00 34.91 ? 51  ALA C CA  1 
ATOM   1807 C C   . ALA C 1 52 ? 19.828  -36.553 26.458  1.00 35.27 ? 51  ALA C C   1 
ATOM   1808 O O   . ALA C 1 52 ? 19.593  -35.430 26.891  1.00 36.44 ? 51  ALA C O   1 
ATOM   1809 C CB  . ALA C 1 52 ? 19.466  -37.586 24.176  1.00 34.93 ? 51  ALA C CB  1 
ATOM   1810 N N   . PHE C 1 53 ? 20.908  -37.247 26.837  1.00 33.02 ? 52  PHE C N   1 
ATOM   1811 C CA  . PHE C 1 53 ? 21.981  -36.660 27.627  1.00 35.86 ? 52  PHE C CA  1 
ATOM   1812 C C   . PHE C 1 53 ? 23.182  -36.519 26.712  1.00 32.59 ? 52  PHE C C   1 
ATOM   1813 O O   . PHE C 1 53 ? 23.550  -37.480 26.038  1.00 35.61 ? 52  PHE C O   1 
ATOM   1814 C CB  . PHE C 1 53 ? 22.390  -37.620 28.758  1.00 35.61 ? 52  PHE C CB  1 
ATOM   1815 C CG  . PHE C 1 53 ? 21.396  -37.557 29.901  1.00 34.18 ? 52  PHE C CG  1 
ATOM   1816 C CD1 . PHE C 1 53 ? 21.091  -36.351 30.520  1.00 35.97 ? 52  PHE C CD1 1 
ATOM   1817 C CD2 . PHE C 1 53 ? 20.733  -38.705 30.326  1.00 48.52 ? 52  PHE C CD2 1 
ATOM   1818 C CE1 . PHE C 1 53 ? 20.151  -36.294 31.547  1.00 43.91 ? 52  PHE C CE1 1 
ATOM   1819 C CE2 . PHE C 1 53 ? 19.800  -38.639 31.360  1.00 47.51 ? 52  PHE C CE2 1 
ATOM   1820 C CZ  . PHE C 1 53 ? 19.506  -37.434 31.966  1.00 43.22 ? 52  PHE C CZ  1 
ATOM   1821 N N   . LEU C 1 54 ? 23.822  -35.343 26.701  1.00 30.48 ? 53  LEU C N   1 
ATOM   1822 C CA  . LEU C 1 54 ? 24.974  -35.128 25.835  1.00 29.23 ? 53  LEU C CA  1 
ATOM   1823 C C   . LEU C 1 54 ? 26.052  -34.354 26.578  1.00 28.93 ? 53  LEU C C   1 
ATOM   1824 O O   . LEU C 1 54 ? 25.758  -33.562 27.448  1.00 31.12 ? 53  LEU C O   1 
ATOM   1825 C CB  . LEU C 1 54 ? 24.611  -34.368 24.557  1.00 29.32 ? 53  LEU C CB  1 
ATOM   1826 C CG  . LEU C 1 54 ? 23.731  -35.115 23.552  1.00 33.70 ? 53  LEU C CG  1 
ATOM   1827 C CD1 . LEU C 1 54 ? 23.369  -34.121 22.467  1.00 32.95 ? 53  LEU C CD1 1 
ATOM   1828 C CD2 . LEU C 1 54 ? 24.507  -36.293 22.942  1.00 40.51 ? 53  LEU C CD2 1 
ATOM   1829 N N   . GLY C 1 55 ? 27.301  -34.578 26.185  1.00 31.64 ? 54  GLY C N   1 
ATOM   1830 C CA  . GLY C 1 55 ? 28.436  -33.873 26.753  1.00 31.93 ? 54  GLY C CA  1 
ATOM   1831 C C   . GLY C 1 55 ? 28.690  -32.542 26.042  1.00 37.98 ? 54  GLY C C   1 
ATOM   1832 O O   . GLY C 1 55 ? 28.165  -32.249 24.956  1.00 33.62 ? 54  GLY C O   1 
ATOM   1833 N N   . PRO C 1 56 ? 29.491  -31.645 26.650  1.00 36.53 ? 55  PRO C N   1 
ATOM   1834 C CA  . PRO C 1 56 ? 29.651  -30.290 26.136  1.00 38.68 ? 55  PRO C CA  1 
ATOM   1835 C C   . PRO C 1 56 ? 30.251  -30.178 24.738  1.00 38.83 ? 55  PRO C C   1 
ATOM   1836 O O   . PRO C 1 56 ? 29.964  -29.227 24.011  1.00 50.51 ? 55  PRO C O   1 
ATOM   1837 C CB  . PRO C 1 56 ? 30.494  -29.571 27.251  1.00 45.00 ? 55  PRO C CB  1 
ATOM   1838 C CG  . PRO C 1 56 ? 31.203  -30.706 27.946  1.00 37.08 ? 55  PRO C CG  1 
ATOM   1839 C CD  . PRO C 1 56 ? 30.231  -31.870 27.910  1.00 39.32 ? 55  PRO C CD  1 
ATOM   1840 N N   . LYS C 1 57 ? 31.052  -31.171 24.357  1.00 39.72 ? 56  LYS C N   1 
ATOM   1841 C CA  . LYS C 1 57 ? 31.709  -31.174 23.061  1.00 42.27 ? 56  LYS C CA  1 
ATOM   1842 C C   . LYS C 1 57 ? 30.669  -31.352 21.955  1.00 45.48 ? 56  LYS C C   1 
ATOM   1843 O O   . LYS C 1 57 ? 30.972  -31.143 20.779  1.00 42.25 ? 56  LYS C O   1 
ATOM   1844 C CB  . LYS C 1 57 ? 32.595  -32.417 22.930  1.00 44.65 ? 56  LYS C CB  1 
ATOM   1845 N N   . ASP C 1 58 ? 29.475  -31.817 22.347  1.00 39.26 ? 57  ASP C N   1 
ATOM   1846 C CA  . ASP C 1 58 ? 28.419  -32.134 21.390  1.00 37.75 ? 57  ASP C CA  1 
ATOM   1847 C C   . ASP C 1 58 ? 27.460  -30.961 21.235  1.00 36.51 ? 57  ASP C C   1 
ATOM   1848 O O   . ASP C 1 58 ? 26.433  -31.083 20.558  1.00 34.47 ? 57  ASP C O   1 
ATOM   1849 C CB  . ASP C 1 58 ? 27.622  -33.344 21.846  1.00 39.19 ? 57  ASP C CB  1 
ATOM   1850 C CG  . ASP C 1 58 ? 28.409  -34.637 21.874  1.00 41.31 ? 57  ASP C CG  1 
ATOM   1851 O OD1 . ASP C 1 58 ? 29.331  -34.734 21.082  1.00 40.81 ? 57  ASP C OD1 1 
ATOM   1852 O OD2 . ASP C 1 58 ? 28.085  -35.519 22.683  1.00 50.09 ? 57  ASP C OD2 1 
ATOM   1853 N N   . LEU C 1 59 ? 27.759  -29.826 21.867  1.00 30.65 ? 58  LEU C N   1 
ATOM   1854 C CA  . LEU C 1 59 ? 26.782  -28.761 21.993  1.00 32.20 ? 58  LEU C CA  1 
ATOM   1855 C C   . LEU C 1 59 ? 27.400  -27.458 21.503  1.00 35.68 ? 58  LEU C C   1 
ATOM   1856 O O   . LEU C 1 59 ? 28.557  -27.204 21.833  1.00 40.76 ? 58  LEU C O   1 
ATOM   1857 C CB  . LEU C 1 59 ? 26.372  -28.588 23.459  1.00 32.60 ? 58  LEU C CB  1 
ATOM   1858 C CG  . LEU C 1 59 ? 25.907  -29.861 24.160  1.00 30.83 ? 58  LEU C CG  1 
ATOM   1859 C CD1 . LEU C 1 59 ? 25.666  -29.630 25.644  1.00 31.99 ? 58  LEU C CD1 1 
ATOM   1860 C CD2 . LEU C 1 59 ? 24.582  -30.272 23.499  1.00 27.61 ? 58  LEU C CD2 1 
ATOM   1861 N N   . PHE C 1 60 ? 26.601  -26.656 20.781  1.00 36.89 ? 59  PHE C N   1 
ATOM   1862 C CA  . PHE C 1 60 ? 27.059  -25.431 20.114  1.00 36.98 ? 59  PHE C CA  1 
ATOM   1863 C C   . PHE C 1 60 ? 26.081  -24.296 20.413  1.00 38.46 ? 59  PHE C C   1 
ATOM   1864 O O   . PHE C 1 60 ? 24.887  -24.415 20.170  1.00 34.82 ? 59  PHE C O   1 
ATOM   1865 C CB  . PHE C 1 60 ? 27.247  -25.675 18.607  1.00 33.62 ? 59  PHE C CB  1 
ATOM   1866 C CG  . PHE C 1 60 ? 28.188  -26.840 18.324  1.00 36.11 ? 59  PHE C CG  1 
ATOM   1867 C CD1 . PHE C 1 60 ? 27.743  -28.159 18.363  1.00 36.05 ? 59  PHE C CD1 1 
ATOM   1868 C CD2 . PHE C 1 60 ? 29.546  -26.621 18.084  1.00 41.13 ? 59  PHE C CD2 1 
ATOM   1869 C CE1 . PHE C 1 60 ? 28.609  -29.228 18.173  1.00 32.31 ? 59  PHE C CE1 1 
ATOM   1870 C CE2 . PHE C 1 60 ? 30.410  -27.688 17.856  1.00 39.08 ? 59  PHE C CE2 1 
ATOM   1871 C CZ  . PHE C 1 60 ? 29.946  -28.986 17.898  1.00 42.40 ? 59  PHE C CZ  1 
ATOM   1872 N N   . PRO C 1 61 ? 26.498  -23.153 21.019  1.00 39.98 ? 60  PRO C N   1 
ATOM   1873 C CA  . PRO C 1 61 ? 25.523  -22.100 21.324  1.00 40.29 ? 60  PRO C CA  1 
ATOM   1874 C C   . PRO C 1 61 ? 24.824  -21.627 20.049  1.00 37.17 ? 60  PRO C C   1 
ATOM   1875 O O   . PRO C 1 61 ? 25.454  -21.493 19.004  1.00 42.69 ? 60  PRO C O   1 
ATOM   1876 C CB  . PRO C 1 61 ? 26.276  -20.969 22.077  1.00 42.17 ? 60  PRO C CB  1 
ATOM   1877 C CG  . PRO C 1 61 ? 27.720  -21.456 22.111  1.00 41.42 ? 60  PRO C CG  1 
ATOM   1878 C CD  . PRO C 1 61 ? 27.878  -22.814 21.426  1.00 45.51 ? 60  PRO C CD  1 
ATOM   1879 N N   . TYR C 1 62 ? 23.495  -21.444 20.174  1.00 38.59 ? 61  TYR C N   1 
ATOM   1880 C CA  . TYR C 1 62 ? 22.574  -21.214 19.072  1.00 38.03 ? 61  TYR C CA  1 
ATOM   1881 C C   . TYR C 1 62 ? 22.973  -19.961 18.294  1.00 45.21 ? 61  TYR C C   1 
ATOM   1882 O O   . TYR C 1 62 ? 23.050  -20.007 17.066  1.00 45.25 ? 61  TYR C O   1 
ATOM   1883 C CB  . TYR C 1 62 ? 21.119  -21.112 19.526  1.00 43.98 ? 61  TYR C CB  1 
ATOM   1884 C CG  . TYR C 1 62 ? 20.181  -20.742 18.390  1.00 45.42 ? 61  TYR C CG  1 
ATOM   1885 C CD1 . TYR C 1 62 ? 20.027  -21.589 17.288  1.00 42.18 ? 61  TYR C CD1 1 
ATOM   1886 C CD2 . TYR C 1 62 ? 19.431  -19.572 18.441  1.00 46.27 ? 61  TYR C CD2 1 
ATOM   1887 C CE1 . TYR C 1 62 ? 19.166  -21.257 16.244  1.00 40.29 ? 61  TYR C CE1 1 
ATOM   1888 C CE2 . TYR C 1 62 ? 18.558  -19.241 17.415  1.00 46.51 ? 61  TYR C CE2 1 
ATOM   1889 C CZ  . TYR C 1 62 ? 18.436  -20.076 16.312  1.00 43.00 ? 61  TYR C CZ  1 
ATOM   1890 O OH  . TYR C 1 62 ? 17.583  -19.715 15.301  1.00 43.13 ? 61  TYR C OH  1 
ATOM   1891 N N   . ASP C 1 63 ? 23.276  -18.870 19.009  1.00 46.95 ? 62  ASP C N   1 
ATOM   1892 C CA  . ASP C 1 63 ? 23.565  -17.616 18.324  1.00 51.66 ? 62  ASP C CA  1 
ATOM   1893 C C   . ASP C 1 63 ? 24.876  -17.695 17.560  1.00 46.31 ? 62  ASP C C   1 
ATOM   1894 O O   . ASP C 1 63 ? 24.948  -17.220 16.427  1.00 51.26 ? 62  ASP C O   1 
ATOM   1895 C CB  . ASP C 1 63 ? 23.393  -16.392 19.205  1.00 56.07 ? 62  ASP C CB  1 
ATOM   1896 C CG  . ASP C 1 63 ? 21.989  -15.814 19.132  1.00 71.18 ? 62  ASP C CG  1 
ATOM   1897 O OD1 . ASP C 1 63 ? 21.305  -15.801 20.179  1.00 65.21 ? 62  ASP C OD1 1 
ATOM   1898 O OD2 . ASP C 1 63 ? 21.581  -15.414 18.011  1.00 76.58 ? 62  ASP C OD2 1 
ATOM   1899 N N   . LYS C 1 64 ? 25.881  -18.317 18.171  1.00 41.21 ? 63  LYS C N   1 
ATOM   1900 C CA  . LYS C 1 64 ? 27.216  -18.385 17.605  1.00 43.28 ? 63  LYS C CA  1 
ATOM   1901 C C   . LYS C 1 64 ? 27.225  -19.281 16.374  1.00 45.02 ? 63  LYS C C   1 
ATOM   1902 O O   . LYS C 1 64 ? 28.035  -19.052 15.488  1.00 41.44 ? 63  LYS C O   1 
ATOM   1903 C CB  . LYS C 1 64 ? 28.293  -18.861 18.595  1.00 45.76 ? 63  LYS C CB  1 
ATOM   1904 N N   . SER C 1 65 ? 26.328  -20.297 16.304  1.00 38.72 ? 64  SER C N   1 
ATOM   1905 C CA  . SER C 1 65 ? 26.554  -21.319 15.295  1.00 36.21 ? 64  SER C CA  1 
ATOM   1906 C C   . SER C 1 65 ? 25.398  -21.427 14.293  1.00 35.45 ? 64  SER C C   1 
ATOM   1907 O O   . SER C 1 65 ? 25.497  -22.231 13.367  1.00 35.13 ? 64  SER C O   1 
ATOM   1908 C CB  . SER C 1 65 ? 26.876  -22.677 15.919  1.00 41.22 ? 64  SER C CB  1 
ATOM   1909 O OG  . SER C 1 65 ? 25.732  -23.179 16.599  1.00 41.12 ? 64  SER C OG  1 
ATOM   1910 N N   . LYS C 1 66 ? 24.332  -20.637 14.473  1.00 34.61 ? 65  LYS C N   1 
ATOM   1911 C CA  . LYS C 1 66 ? 23.177  -20.780 13.586  1.00 35.00 ? 65  LYS C CA  1 
ATOM   1912 C C   . LYS C 1 66 ? 23.541  -20.499 12.126  1.00 36.71 ? 65  LYS C C   1 
ATOM   1913 O O   . LYS C 1 66 ? 22.984  -21.115 11.224  1.00 36.38 ? 65  LYS C O   1 
ATOM   1914 C CB  . LYS C 1 66 ? 21.920  -19.990 13.956  1.00 38.67 ? 65  LYS C CB  1 
ATOM   1915 C CG  . LYS C 1 66 ? 22.170  -18.489 14.020  1.00 33.68 ? 65  LYS C CG  1 
ATOM   1916 C CD  . LYS C 1 66 ? 20.939  -17.804 14.603  1.00 39.09 ? 65  LYS C CD  1 
ATOM   1917 C CE  . LYS C 1 66 ? 21.155  -16.332 14.745  1.00 40.04 ? 65  LYS C CE  1 
ATOM   1918 N NZ  . LYS C 1 66 ? 19.915  -15.832 15.318  1.00 42.10 ? 65  LYS C NZ  1 
ATOM   1919 N N   . ASP C 1 67 ? 24.494  -19.596 11.867  1.00 38.02 ? 66  ASP C N   1 
ATOM   1920 C CA  . ASP C 1 67 ? 24.891  -19.346 10.479  1.00 36.80 ? 66  ASP C CA  1 
ATOM   1921 C C   . ASP C 1 67 ? 25.327  -20.648 9.792   1.00 40.47 ? 66  ASP C C   1 
ATOM   1922 O O   . ASP C 1 67 ? 25.026  -20.863 8.622   1.00 38.73 ? 66  ASP C O   1 
ATOM   1923 C CB  . ASP C 1 67 ? 25.785  -18.103 10.341  1.00 39.94 ? 66  ASP C CB  1 
ATOM   1924 C CG  . ASP C 1 67 ? 27.275  -18.214 10.674  1.00 50.18 ? 66  ASP C CG  1 
ATOM   1925 O OD1 . ASP C 1 67 ? 27.798  -19.348 10.755  1.00 54.19 ? 66  ASP C OD1 1 
ATOM   1926 O OD2 . ASP C 1 67 ? 27.925  -17.151 10.883  1.00 52.20 ? 66  ASP C OD2 1 
ATOM   1927 N N   . LYS C 1 68 ? 25.973  -21.548 10.545  1.00 33.62 ? 67  LYS C N   1 
ATOM   1928 C CA  . LYS C 1 68 ? 26.466  -22.818 10.034  1.00 34.84 ? 67  LYS C CA  1 
ATOM   1929 C C   . LYS C 1 68 ? 25.413  -23.950 10.104  1.00 32.03 ? 67  LYS C C   1 
ATOM   1930 O O   . LYS C 1 68 ? 25.265  -24.710 9.146   1.00 35.41 ? 67  LYS C O   1 
ATOM   1931 C CB  . LYS C 1 68 ? 27.774  -23.124 10.768  1.00 37.05 ? 67  LYS C CB  1 
ATOM   1932 C CG  . LYS C 1 68 ? 28.530  -24.362 10.322  1.00 41.93 ? 67  LYS C CG  1 
ATOM   1933 C CD  . LYS C 1 68 ? 29.828  -24.530 11.121  1.00 50.15 ? 67  LYS C CD  1 
ATOM   1934 C CE  . LYS C 1 68 ? 30.444  -25.900 11.083  1.00 61.71 ? 67  LYS C CE  1 
ATOM   1935 N NZ  . LYS C 1 68 ? 30.648  -26.473 9.746   1.00 69.62 ? 67  LYS C NZ  1 
ATOM   1936 N N   . TYR C 1 69 ? 24.716  -24.114 11.242  1.00 31.39 ? 68  TYR C N   1 
ATOM   1937 C CA  . TYR C 1 69 ? 23.848  -25.288 11.354  1.00 28.36 ? 68  TYR C CA  1 
ATOM   1938 C C   . TYR C 1 69 ? 22.368  -24.953 11.160  1.00 31.93 ? 68  TYR C C   1 
ATOM   1939 O O   . TYR C 1 69 ? 21.561  -25.872 11.029  1.00 29.63 ? 68  TYR C O   1 
ATOM   1940 C CB  . TYR C 1 69 ? 24.005  -25.894 12.757  1.00 28.47 ? 68  TYR C CB  1 
ATOM   1941 C CG  . TYR C 1 69 ? 25.430  -26.320 13.073  1.00 28.51 ? 68  TYR C CG  1 
ATOM   1942 C CD1 . TYR C 1 69 ? 26.155  -27.122 12.192  1.00 31.80 ? 68  TYR C CD1 1 
ATOM   1943 C CD2 . TYR C 1 69 ? 26.021  -25.910 14.267  1.00 34.52 ? 68  TYR C CD2 1 
ATOM   1944 C CE1 . TYR C 1 69 ? 27.445  -27.544 12.496  1.00 31.05 ? 68  TYR C CE1 1 
ATOM   1945 C CE2 . TYR C 1 69 ? 27.311  -26.318 14.565  1.00 32.58 ? 68  TYR C CE2 1 
ATOM   1946 C CZ  . TYR C 1 69 ? 28.013  -27.121 13.686  1.00 33.96 ? 68  TYR C CZ  1 
ATOM   1947 O OH  . TYR C 1 69 ? 29.300  -27.472 14.039  1.00 40.93 ? 68  TYR C OH  1 
ATOM   1948 N N   . GLY C 1 70 ? 22.012  -23.664 11.178  1.00 28.98 ? 69  GLY C N   1 
ATOM   1949 C CA  . GLY C 1 70 ? 20.601  -23.294 11.123  1.00 30.47 ? 69  GLY C CA  1 
ATOM   1950 C C   . GLY C 1 70 ? 20.150  -23.170 9.669   1.00 29.36 ? 69  GLY C C   1 
ATOM   1951 O O   . GLY C 1 70 ? 20.059  -22.061 9.126   1.00 31.40 ? 69  GLY C O   1 
ATOM   1952 N N   . LYS C 1 71 ? 20.043  -24.323 9.015   1.00 27.72 ? 70  LYS C N   1 
ATOM   1953 C CA  . LYS C 1 71 ? 19.686  -24.401 7.599   1.00 31.30 ? 70  LYS C CA  1 
ATOM   1954 C C   . LYS C 1 71 ? 18.824  -25.636 7.464   1.00 33.55 ? 70  LYS C C   1 
ATOM   1955 O O   . LYS C 1 71 ? 18.993  -26.609 8.207   1.00 32.82 ? 70  LYS C O   1 
ATOM   1956 C CB  . LYS C 1 71 ? 20.864  -24.635 6.647   1.00 35.84 ? 70  LYS C CB  1 
ATOM   1957 C CG  . LYS C 1 71 ? 21.920  -25.545 7.203   1.00 39.34 ? 70  LYS C CG  1 
ATOM   1958 C CD  . LYS C 1 71 ? 23.036  -26.096 6.327   1.00 45.28 ? 70  LYS C CD  1 
ATOM   1959 C CE  . LYS C 1 71 ? 23.912  -26.951 7.198   1.00 46.61 ? 70  LYS C CE  1 
ATOM   1960 N N   . PRO C 1 72 ? 17.838  -25.642 6.545   1.00 29.36 ? 71  PRO C N   1 
ATOM   1961 C CA  . PRO C 1 72 ? 16.907  -26.760 6.493   1.00 25.56 ? 71  PRO C CA  1 
ATOM   1962 C C   . PRO C 1 72 ? 17.561  -28.095 6.161   1.00 30.22 ? 71  PRO C C   1 
ATOM   1963 O O   . PRO C 1 72 ? 18.527  -28.145 5.399   1.00 32.56 ? 71  PRO C O   1 
ATOM   1964 C CB  . PRO C 1 72 ? 15.960  -26.336 5.362   1.00 27.67 ? 71  PRO C CB  1 
ATOM   1965 C CG  . PRO C 1 72 ? 15.977  -24.838 5.525   1.00 30.90 ? 71  PRO C CG  1 
ATOM   1966 C CD  . PRO C 1 72 ? 17.464  -24.508 5.665   1.00 29.31 ? 71  PRO C CD  1 
ATOM   1967 N N   . ASN C 1 73 ? 16.897  -29.142 6.618   1.00 31.80 ? 72  ASN C N   1 
ATOM   1968 C CA  . ASN C 1 73 ? 17.160  -30.427 6.004   1.00 38.57 ? 72  ASN C CA  1 
ATOM   1969 C C   . ASN C 1 73 ? 15.924  -31.302 6.167   1.00 28.62 ? 72  ASN C C   1 
ATOM   1970 O O   . ASN C 1 73 ? 14.974  -30.950 6.860   1.00 32.48 ? 72  ASN C O   1 
ATOM   1971 C CB  . ASN C 1 73 ? 18.521  -31.017 6.366   1.00 43.66 ? 72  ASN C CB  1 
ATOM   1972 C CG  . ASN C 1 73 ? 18.484  -31.694 7.712   1.00 41.75 ? 72  ASN C CG  1 
ATOM   1973 O OD1 . ASN C 1 73 ? 17.954  -32.808 7.852   1.00 38.63 ? 72  ASN C OD1 1 
ATOM   1974 N ND2 . ASN C 1 73 ? 19.076  -31.048 8.695   1.00 47.77 ? 72  ASN C ND2 1 
ATOM   1975 N N   . LYS C 1 74 ? 15.975  -32.447 5.494   1.00 31.63 ? 73  LYS C N   1 
ATOM   1976 C CA  . LYS C 1 74 ? 14.767  -33.232 5.281   1.00 27.00 ? 73  LYS C CA  1 
ATOM   1977 C C   . LYS C 1 74 ? 14.535  -34.219 6.414   1.00 31.35 ? 73  LYS C C   1 
ATOM   1978 O O   . LYS C 1 74 ? 13.499  -34.886 6.447   1.00 33.52 ? 73  LYS C O   1 
ATOM   1979 C CB  . LYS C 1 74 ? 14.927  -33.992 3.954   1.00 32.38 ? 73  LYS C CB  1 
ATOM   1980 N N   . ARG C 1 75 ? 15.462  -34.293 7.387   1.00 28.26 ? 74  ARG C N   1 
ATOM   1981 C CA  . ARG C 1 75 ? 15.241  -35.233 8.480   1.00 27.58 ? 74  ARG C CA  1 
ATOM   1982 C C   . ARG C 1 75 ? 13.967  -34.913 9.260   1.00 30.23 ? 74  ARG C C   1 
ATOM   1983 O O   . ARG C 1 75 ? 13.590  -33.752 9.505   1.00 29.66 ? 74  ARG C O   1 
ATOM   1984 C CB  . ARG C 1 75 ? 16.472  -35.338 9.410   1.00 31.97 ? 74  ARG C CB  1 
ATOM   1985 C CG  . ARG C 1 75 ? 17.829  -35.566 8.739   1.00 36.13 ? 74  ARG C CG  1 
ATOM   1986 C CD  . ARG C 1 75 ? 18.077  -36.969 8.132   1.00 36.27 ? 74  ARG C CD  1 
ATOM   1987 N NE  . ARG C 1 75 ? 18.151  -37.888 9.262   1.00 33.73 ? 74  ARG C NE  1 
ATOM   1988 C CZ  . ARG C 1 75 ? 19.339  -38.289 9.760   1.00 30.56 ? 74  ARG C CZ  1 
ATOM   1989 N NH1 . ARG C 1 75 ? 19.348  -38.942 10.882  1.00 37.50 ? 74  ARG C NH1 1 
ATOM   1990 N NH2 . ARG C 1 75 ? 20.468  -37.944 9.161   1.00 33.17 ? 74  ARG C NH2 1 
ATOM   1991 N N   . LYS C 1 76 ? 13.310  -35.991 9.701   1.00 31.66 ? 75  LYS C N   1 
ATOM   1992 C CA  . LYS C 1 76 ? 12.012  -35.896 10.352  1.00 33.72 ? 75  LYS C CA  1 
ATOM   1993 C C   . LYS C 1 76 ? 12.037  -34.922 11.529  1.00 33.14 ? 75  LYS C C   1 
ATOM   1994 O O   . LYS C 1 76 ? 12.841  -35.053 12.462  1.00 31.41 ? 75  LYS C O   1 
ATOM   1995 C CB  . LYS C 1 76 ? 11.443  -37.240 10.823  1.00 35.96 ? 75  LYS C CB  1 
ATOM   1996 C CG  . LYS C 1 76 ? 9.934   -37.195 11.084  1.00 41.69 ? 75  LYS C CG  1 
ATOM   1997 C CD  . LYS C 1 76 ? 9.358   -38.278 11.995  1.00 52.30 ? 75  LYS C CD  1 
ATOM   1998 N N   . GLY C 1 77 ? 11.168  -33.903 11.461  1.00 34.70 ? 76  GLY C N   1 
ATOM   1999 C CA  . GLY C 1 77 ? 10.991  -32.989 12.583  1.00 28.87 ? 76  GLY C CA  1 
ATOM   2000 C C   . GLY C 1 77 ? 11.974  -31.808 12.568  1.00 26.85 ? 76  GLY C C   1 
ATOM   2001 O O   . GLY C 1 77 ? 11.829  -30.869 13.345  1.00 32.50 ? 76  GLY C O   1 
ATOM   2002 N N   . PHE C 1 78 ? 12.942  -31.821 11.649  1.00 27.33 ? 77  PHE C N   1 
ATOM   2003 C CA  . PHE C 1 78 ? 14.035  -30.866 11.702  1.00 27.78 ? 77  PHE C CA  1 
ATOM   2004 C C   . PHE C 1 78 ? 13.521  -29.428 11.492  1.00 29.70 ? 77  PHE C C   1 
ATOM   2005 O O   . PHE C 1 78 ? 13.886  -28.482 12.200  1.00 27.68 ? 77  PHE C O   1 
ATOM   2006 C CB  . PHE C 1 78 ? 15.121  -31.222 10.689  1.00 30.66 ? 77  PHE C CB  1 
ATOM   2007 C CG  . PHE C 1 78 ? 16.403  -30.454 10.979  1.00 26.87 ? 77  PHE C CG  1 
ATOM   2008 C CD1 . PHE C 1 78 ? 16.588  -29.183 10.468  1.00 27.12 ? 77  PHE C CD1 1 
ATOM   2009 C CD2 . PHE C 1 78 ? 17.426  -31.019 11.738  1.00 26.69 ? 77  PHE C CD2 1 
ATOM   2010 C CE1 . PHE C 1 78 ? 17.770  -28.481 10.721  1.00 26.32 ? 77  PHE C CE1 1 
ATOM   2011 C CE2 . PHE C 1 78 ? 18.594  -30.307 12.012  1.00 25.95 ? 77  PHE C CE2 1 
ATOM   2012 C CZ  . PHE C 1 78 ? 18.771  -29.044 11.492  1.00 26.51 ? 77  PHE C CZ  1 
ATOM   2013 N N   . ASN C 1 79 ? 12.755  -29.266 10.407  1.00 28.71 ? 78  ASN C N   1 
ATOM   2014 C CA  . ASN C 1 79 ? 12.454  -27.906 9.990   1.00 31.73 ? 78  ASN C CA  1 
ATOM   2015 C C   . ASN C 1 79 ? 11.436  -27.287 10.938  1.00 28.78 ? 78  ASN C C   1 
ATOM   2016 O O   . ASN C 1 79 ? 11.470  -26.090 11.242  1.00 28.37 ? 78  ASN C O   1 
ATOM   2017 C CB  . ASN C 1 79 ? 11.988  -27.896 8.544   1.00 28.21 ? 78  ASN C CB  1 
ATOM   2018 C CG  . ASN C 1 79 ? 13.102  -28.265 7.596   1.00 28.92 ? 78  ASN C CG  1 
ATOM   2019 O OD1 . ASN C 1 79 ? 14.270  -27.951 7.856   1.00 28.45 ? 78  ASN C OD1 1 
ATOM   2020 N ND2 . ASN C 1 79 ? 12.747  -28.840 6.455   1.00 27.69 ? 78  ASN C ND2 1 
ATOM   2021 N N   . GLU C 1 80 ? 10.569  -28.129 11.459  1.00 31.74 ? 79  GLU C N   1 
ATOM   2022 C CA  . GLU C 1 80 ? 9.710   -27.607 12.504  1.00 28.86 ? 79  GLU C CA  1 
ATOM   2023 C C   . GLU C 1 80 ? 10.551  -27.240 13.724  1.00 35.04 ? 79  GLU C C   1 
ATOM   2024 O O   . GLU C 1 80 ? 10.266  -26.256 14.398  1.00 30.44 ? 79  GLU C O   1 
ATOM   2025 C CB  . GLU C 1 80 ? 8.634   -28.639 12.826  1.00 34.51 ? 79  GLU C CB  1 
ATOM   2026 C CG  . GLU C 1 80 ? 7.741   -28.188 13.971  1.00 34.09 ? 79  GLU C CG  1 
ATOM   2027 C CD  . GLU C 1 80 ? 6.480   -29.000 14.110  1.00 42.45 ? 79  GLU C CD  1 
ATOM   2028 O OE1 . GLU C 1 80 ? 6.341   -30.087 13.504  1.00 44.29 ? 79  GLU C OE1 1 
ATOM   2029 O OE2 . GLU C 1 80 ? 5.619   -28.523 14.862  1.00 43.83 ? 79  GLU C OE2 1 
ATOM   2030 N N   . GLY C 1 81 ? 11.609  -28.038 14.009  1.00 28.82 ? 80  GLY C N   1 
ATOM   2031 C CA  . GLY C 1 81 ? 12.526  -27.624 15.068  1.00 29.46 ? 80  GLY C CA  1 
ATOM   2032 C C   . GLY C 1 81 ? 13.160  -26.249 14.841  1.00 30.13 ? 80  GLY C C   1 
ATOM   2033 O O   . GLY C 1 81 ? 13.340  -25.485 15.781  1.00 29.48 ? 80  GLY C O   1 
ATOM   2034 N N   . LEU C 1 82 ? 13.598  -25.965 13.597  1.00 28.98 ? 81  LEU C N   1 
ATOM   2035 C CA  . LEU C 1 82 ? 14.192  -24.669 13.271  1.00 29.31 ? 81  LEU C CA  1 
ATOM   2036 C C   . LEU C 1 82 ? 13.176  -23.554 13.525  1.00 27.04 ? 81  LEU C C   1 
ATOM   2037 O O   . LEU C 1 82 ? 13.564  -22.469 13.992  1.00 30.57 ? 81  LEU C O   1 
ATOM   2038 C CB  . LEU C 1 82 ? 14.671  -24.644 11.815  1.00 29.77 ? 81  LEU C CB  1 
ATOM   2039 C CG  . LEU C 1 82 ? 15.934  -25.437 11.463  1.00 29.15 ? 81  LEU C CG  1 
ATOM   2040 C CD1 . LEU C 1 82 ? 16.256  -25.273 9.955   1.00 28.26 ? 81  LEU C CD1 1 
ATOM   2041 C CD2 . LEU C 1 82 ? 17.163  -25.028 12.252  1.00 26.85 ? 81  LEU C CD2 1 
ATOM   2042 N N   . TRP C 1 83 ? 11.897  -23.850 13.260  1.00 28.35 ? 82  TRP C N   1 
ATOM   2043 C CA  . TRP C 1 83 ? 10.870  -22.836 13.497  1.00 34.75 ? 82  TRP C CA  1 
ATOM   2044 C C   . TRP C 1 83 ? 10.783  -22.565 15.008  1.00 36.08 ? 82  TRP C C   1 
ATOM   2045 O O   . TRP C 1 83 ? 10.816  -21.409 15.446  1.00 34.37 ? 82  TRP C O   1 
ATOM   2046 C CB  . TRP C 1 83 ? 9.507   -23.212 12.891  1.00 32.91 ? 82  TRP C CB  1 
ATOM   2047 C CG  . TRP C 1 83 ? 8.517   -22.078 13.028  1.00 36.04 ? 82  TRP C CG  1 
ATOM   2048 C CD1 . TRP C 1 83 ? 8.359   -21.031 12.158  1.00 42.92 ? 82  TRP C CD1 1 
ATOM   2049 C CD2 . TRP C 1 83 ? 7.631   -21.810 14.141  1.00 40.56 ? 82  TRP C CD2 1 
ATOM   2050 N NE1 . TRP C 1 83 ? 7.409   -20.156 12.617  1.00 36.46 ? 82  TRP C NE1 1 
ATOM   2051 C CE2 . TRP C 1 83 ? 6.941   -20.609 13.828  1.00 41.05 ? 82  TRP C CE2 1 
ATOM   2052 C CE3 . TRP C 1 83 ? 7.338   -22.482 15.339  1.00 38.48 ? 82  TRP C CE3 1 
ATOM   2053 C CZ2 . TRP C 1 83 ? 5.997   -20.064 14.696  1.00 45.02 ? 82  TRP C CZ2 1 
ATOM   2054 C CZ3 . TRP C 1 83 ? 6.402   -21.944 16.198  1.00 44.12 ? 82  TRP C CZ3 1 
ATOM   2055 C CH2 . TRP C 1 83 ? 5.760   -20.741 15.882  1.00 45.62 ? 82  TRP C CH2 1 
ATOM   2056 N N   . GLU C 1 84 ? 10.814  -23.645 15.805  1.00 31.01 ? 83  GLU C N   1 
ATOM   2057 C CA  . GLU C 1 84 ? 10.684  -23.503 17.256  1.00 35.35 ? 83  GLU C CA  1 
ATOM   2058 C C   . GLU C 1 84 ? 11.843  -22.733 17.888  1.00 36.46 ? 83  GLU C C   1 
ATOM   2059 O O   . GLU C 1 84 ? 11.623  -21.849 18.744  1.00 36.85 ? 83  GLU C O   1 
ATOM   2060 C CB  . GLU C 1 84 ? 10.486  -24.864 17.923  1.00 30.58 ? 83  GLU C CB  1 
ATOM   2061 C CG  . GLU C 1 84 ? 9.205   -25.565 17.492  1.00 32.64 ? 83  GLU C CG  1 
ATOM   2062 C CD  . GLU C 1 84 ? 9.096   -26.969 18.030  1.00 37.54 ? 83  GLU C CD  1 
ATOM   2063 O OE1 . GLU C 1 84 ? 10.084  -27.382 18.694  1.00 33.68 ? 83  GLU C OE1 1 
ATOM   2064 O OE2 . GLU C 1 84 ? 8.081   -27.650 17.749  1.00 39.05 ? 83  GLU C OE2 1 
ATOM   2065 N N   . ILE C 1 85 ? 13.081  -23.021 17.462  1.00 30.81 ? 84  ILE C N   1 
ATOM   2066 C CA  . ILE C 1 85 ? 14.245  -22.414 18.088  1.00 32.39 ? 84  ILE C CA  1 
ATOM   2067 C C   . ILE C 1 85 ? 14.320  -20.899 17.836  1.00 35.45 ? 84  ILE C C   1 
ATOM   2068 O O   . ILE C 1 85 ? 14.770  -20.147 18.685  1.00 33.12 ? 84  ILE C O   1 
ATOM   2069 C CB  . ILE C 1 85 ? 15.551  -23.144 17.762  1.00 33.94 ? 84  ILE C CB  1 
ATOM   2070 C CG1 . ILE C 1 85 ? 16.619  -22.773 18.790  1.00 32.02 ? 84  ILE C CG1 1 
ATOM   2071 C CG2 . ILE C 1 85 ? 16.016  -22.899 16.312  1.00 30.66 ? 84  ILE C CG2 1 
ATOM   2072 C CD1 . ILE C 1 85 ? 17.834  -23.701 18.861  1.00 32.68 ? 84  ILE C CD1 1 
ATOM   2073 N N   . GLN C 1 86 ? 13.839  -20.457 16.672  1.00 33.05 ? 85  GLN C N   1 
ATOM   2074 C CA  . GLN C 1 86 ? 13.850  -19.043 16.339  1.00 34.88 ? 85  GLN C CA  1 
ATOM   2075 C C   . GLN C 1 86 ? 12.629  -18.273 16.852  1.00 34.42 ? 85  GLN C C   1 
ATOM   2076 O O   . GLN C 1 86 ? 12.762  -17.089 17.164  1.00 38.93 ? 85  GLN C O   1 
ATOM   2077 C CB  . GLN C 1 86 ? 13.866  -18.973 14.812  1.00 34.03 ? 85  GLN C CB  1 
ATOM   2078 C CG  . GLN C 1 86 ? 14.104  -17.554 14.299  1.00 35.33 ? 85  GLN C CG  1 
ATOM   2079 C CD  . GLN C 1 86 ? 14.481  -17.528 12.831  1.00 35.26 ? 85  GLN C CD  1 
ATOM   2080 O OE1 . GLN C 1 86 ? 14.323  -18.514 12.090  1.00 35.55 ? 85  GLN C OE1 1 
ATOM   2081 N NE2 . GLN C 1 86 ? 15.038  -16.404 12.410  1.00 34.66 ? 85  GLN C NE2 1 
ATOM   2082 N N   . ASN C 1 87 ? 11.479  -18.933 16.968  1.00 34.76 ? 86  ASN C N   1 
ATOM   2083 C CA  . ASN C 1 87 ? 10.189  -18.272 17.105  1.00 41.90 ? 86  ASN C CA  1 
ATOM   2084 C C   . ASN C 1 87 ? 9.436   -18.646 18.388  1.00 45.06 ? 86  ASN C C   1 
ATOM   2085 O O   . ASN C 1 87 ? 8.447   -17.991 18.698  1.00 46.58 ? 86  ASN C O   1 
ATOM   2086 C CB  . ASN C 1 87 ? 9.251   -18.566 15.936  1.00 40.61 ? 86  ASN C CB  1 
ATOM   2087 C CG  . ASN C 1 87 ? 9.773   -17.973 14.653  1.00 40.81 ? 86  ASN C CG  1 
ATOM   2088 O OD1 . ASN C 1 87 ? 9.743   -16.749 14.503  1.00 40.00 ? 86  ASN C OD1 1 
ATOM   2089 N ND2 . ASN C 1 87 ? 10.266  -18.804 13.739  1.00 34.81 ? 86  ASN C ND2 1 
ATOM   2090 N N   . ASN C 1 88 ? 9.823   -19.715 19.103  1.00 44.28 ? 87  ASN C N   1 
ATOM   2091 C CA  . ASN C 1 88 ? 9.052   -20.110 20.284  1.00 41.33 ? 87  ASN C CA  1 
ATOM   2092 C C   . ASN C 1 88 ? 9.912   -20.997 21.184  1.00 38.93 ? 87  ASN C C   1 
ATOM   2093 O O   . ASN C 1 88 ? 9.477   -22.102 21.551  1.00 45.22 ? 87  ASN C O   1 
ATOM   2094 C CB  . ASN C 1 88 ? 7.762   -20.842 19.915  1.00 46.85 ? 87  ASN C CB  1 
ATOM   2095 C CG  . ASN C 1 88 ? 6.745   -20.860 21.040  1.00 51.04 ? 87  ASN C CG  1 
ATOM   2096 O OD1 . ASN C 1 88 ? 6.907   -20.161 22.046  1.00 55.13 ? 87  ASN C OD1 1 
ATOM   2097 N ND2 . ASN C 1 88 ? 5.683   -21.637 20.886  1.00 48.31 ? 87  ASN C ND2 1 
ATOM   2098 N N   . PRO C 1 89 ? 11.144  -20.553 21.517  1.00 39.28 ? 88  PRO C N   1 
ATOM   2099 C CA  . PRO C 1 89 ? 12.171  -21.442 22.064  1.00 40.31 ? 88  PRO C CA  1 
ATOM   2100 C C   . PRO C 1 89 ? 11.955  -21.922 23.492  1.00 44.12 ? 88  PRO C C   1 
ATOM   2101 O O   . PRO C 1 89 ? 12.612  -22.877 23.916  1.00 41.23 ? 88  PRO C O   1 
ATOM   2102 C CB  . PRO C 1 89 ? 13.462  -20.656 21.928  1.00 37.88 ? 88  PRO C CB  1 
ATOM   2103 C CG  . PRO C 1 89 ? 12.993  -19.216 22.004  1.00 41.26 ? 88  PRO C CG  1 
ATOM   2104 C CD  . PRO C 1 89 ? 11.667  -19.200 21.273  1.00 40.99 ? 88  PRO C CD  1 
ATOM   2105 N N   . HIS C 1 90 ? 11.048  -21.240 24.202  1.00 47.08 ? 89  HIS C N   1 
ATOM   2106 C CA  . HIS C 1 90 ? 10.799  -21.537 25.606  1.00 48.50 ? 89  HIS C CA  1 
ATOM   2107 C C   . HIS C 1 90 ? 9.341   -21.924 25.848  1.00 50.49 ? 89  HIS C C   1 
ATOM   2108 O O   . HIS C 1 90 ? 8.866   -21.877 26.978  1.00 58.64 ? 89  HIS C O   1 
ATOM   2109 C CB  . HIS C 1 90 ? 11.276  -20.396 26.498  1.00 40.34 ? 89  HIS C CB  1 
ATOM   2110 C CG  . HIS C 1 90 ? 12.659  -19.916 26.219  1.00 39.79 ? 89  HIS C CG  1 
ATOM   2111 N ND1 . HIS C 1 90 ? 13.784  -20.675 26.490  1.00 43.86 ? 89  HIS C ND1 1 
ATOM   2112 C CD2 . HIS C 1 90 ? 13.101  -18.766 25.708  1.00 44.23 ? 89  HIS C CD2 1 
ATOM   2113 C CE1 . HIS C 1 90 ? 14.874  -19.978 26.174  1.00 43.63 ? 89  HIS C CE1 1 
ATOM   2114 N NE2 . HIS C 1 90 ? 14.482  -18.813 25.679  1.00 41.37 ? 89  HIS C NE2 1 
ATOM   2115 N N   . ALA C 1 91 ? 8.626   -22.327 24.799  1.00 51.10 ? 90  ALA C N   1 
ATOM   2116 C CA  . ALA C 1 91 ? 7.331   -22.958 24.997  1.00 54.26 ? 90  ALA C CA  1 
ATOM   2117 C C   . ALA C 1 91 ? 7.513   -24.371 25.562  1.00 65.61 ? 90  ALA C C   1 
ATOM   2118 O O   . ALA C 1 91 ? 8.626   -24.907 25.574  1.00 67.08 ? 90  ALA C O   1 
ATOM   2119 C CB  . ALA C 1 91 ? 6.515   -22.947 23.720  1.00 59.08 ? 90  ALA C CB  1 
ATOM   2120 N N   . SER C 1 92 ? 6.393   -24.967 26.001  1.00 64.51 ? 91  SER C N   1 
ATOM   2121 C CA  . SER C 1 92 ? 6.350   -26.224 26.738  1.00 69.21 ? 91  SER C CA  1 
ATOM   2122 C C   . SER C 1 92 ? 6.660   -27.431 25.854  1.00 72.22 ? 91  SER C C   1 
ATOM   2123 O O   . SER C 1 92 ? 7.584   -28.185 26.147  1.00 79.49 ? 91  SER C O   1 
ATOM   2124 C CB  . SER C 1 92 ? 5.008   -26.405 27.417  1.00 70.11 ? 91  SER C CB  1 
ATOM   2125 O OG  . SER C 1 92 ? 4.891   -25.524 28.522  1.00 70.79 ? 91  SER C OG  1 
ATOM   2126 N N   . TYR C 1 93 ? 5.834   -27.635 24.818  1.00 73.71 ? 92  TYR C N   1 
ATOM   2127 C CA  . TYR C 1 93 ? 5.891   -28.802 23.947  1.00 75.21 ? 92  TYR C CA  1 
ATOM   2128 C C   . TYR C 1 93 ? 5.639   -30.065 24.788  1.00 82.60 ? 92  TYR C C   1 
ATOM   2129 O O   . TYR C 1 93 ? 5.995   -31.175 24.332  1.00 89.70 ? 92  TYR C O   1 
ATOM   2130 C CB  . TYR C 1 93 ? 7.170   -28.825 23.093  1.00 68.40 ? 92  TYR C CB  1 
ATOM   2131 C CG  . TYR C 1 93 ? 7.392   -27.554 22.277  1.00 57.42 ? 92  TYR C CG  1 
ATOM   2132 C CD1 . TYR C 1 93 ? 6.590   -27.265 21.172  1.00 53.86 ? 92  TYR C CD1 1 
ATOM   2133 C CD2 . TYR C 1 93 ? 8.384   -26.635 22.619  1.00 55.79 ? 92  TYR C CD2 1 
ATOM   2134 C CE1 . TYR C 1 93 ? 6.757   -26.102 20.438  1.00 52.88 ? 92  TYR C CE1 1 
ATOM   2135 C CE2 . TYR C 1 93 ? 8.572   -25.477 21.879  1.00 53.11 ? 92  TYR C CE2 1 
ATOM   2136 C CZ  . TYR C 1 93 ? 7.757   -25.209 20.789  1.00 56.39 ? 92  TYR C CZ  1 
ATOM   2137 O OH  . TYR C 1 93 ? 7.945   -24.051 20.076  1.00 52.68 ? 92  TYR C OH  1 
HETATM 2138 S S   . SO4 D 2 .  ? 1.344   -33.919 1.894   1.00 82.03 ? 101 SO4 A S   1 
HETATM 2139 O O1  . SO4 D 2 .  ? 1.857   -34.420 0.641   1.00 65.36 ? 101 SO4 A O1  1 
HETATM 2140 O O2  . SO4 D 2 .  ? 1.386   -32.478 1.901   1.00 72.11 ? 101 SO4 A O2  1 
HETATM 2141 O O3  . SO4 D 2 .  ? -0.022  -34.355 2.065   1.00 92.66 ? 101 SO4 A O3  1 
HETATM 2142 O O4  . SO4 D 2 .  ? 2.147   -34.423 2.981   1.00 79.08 ? 101 SO4 A O4  1 
HETATM 2143 S S   . SO4 E 2 .  ? -9.386  -24.727 1.398   1.00 90.27 ? 102 SO4 A S   1 
HETATM 2144 O O1  . SO4 E 2 .  ? -9.561  -24.501 -0.014  1.00 76.87 ? 102 SO4 A O1  1 
HETATM 2145 O O2  . SO4 E 2 .  ? -9.589  -23.494 2.118   1.00 81.31 ? 102 SO4 A O2  1 
HETATM 2146 O O3  . SO4 E 2 .  ? -10.337 -25.721 1.836   1.00 98.05 ? 102 SO4 A O3  1 
HETATM 2147 O O4  . SO4 E 2 .  ? -8.055  -25.209 1.659   1.00 88.70 ? 102 SO4 A O4  1 
HETATM 2148 C C1  . EDO F 3 .  ? 13.855  -19.513 -7.361  1.00 39.05 ? 103 EDO A C1  1 
HETATM 2149 O O1  . EDO F 3 .  ? 15.124  -18.851 -7.215  1.00 30.79 ? 103 EDO A O1  1 
HETATM 2150 C C2  . EDO F 3 .  ? 13.010  -19.051 -8.516  1.00 35.40 ? 103 EDO A C2  1 
HETATM 2151 O O2  . EDO F 3 .  ? 12.521  -17.756 -8.314  1.00 33.15 ? 103 EDO A O2  1 
HETATM 2152 S S   . SO4 G 2 .  ? 9.030   -29.380 5.764   1.00 53.94 ? 104 SO4 A S   1 
HETATM 2153 O O1  . SO4 G 2 .  ? 9.908   -28.702 4.896   1.00 50.58 ? 104 SO4 A O1  1 
HETATM 2154 O O2  . SO4 G 2 .  ? 8.484   -30.540 5.062   1.00 61.04 ? 104 SO4 A O2  1 
HETATM 2155 O O3  . SO4 G 2 .  ? 9.758   -29.804 6.946   1.00 62.98 ? 104 SO4 A O3  1 
HETATM 2156 O O4  . SO4 G 2 .  ? 7.947   -28.513 6.131   1.00 68.84 ? 104 SO4 A O4  1 
HETATM 2157 S S   . SO4 H 2 .  ? 7.470   -8.600  -24.713 1.00 72.01 ? 101 SO4 B S   1 
HETATM 2158 O O1  . SO4 H 2 .  ? 8.590   -8.535  -25.635 1.00 40.27 ? 101 SO4 B O1  1 
HETATM 2159 O O2  . SO4 H 2 .  ? 6.306   -9.125  -25.387 1.00 55.81 ? 101 SO4 B O2  1 
HETATM 2160 O O3  . SO4 H 2 .  ? 7.729   -9.456  -23.554 1.00 46.79 ? 101 SO4 B O3  1 
HETATM 2161 O O4  . SO4 H 2 .  ? 7.252   -7.236  -24.281 1.00 65.53 ? 101 SO4 B O4  1 
HETATM 2162 S S   . SO4 I 2 .  ? 14.686  -27.040 -26.504 1.00 49.13 ? 102 SO4 B S   1 
HETATM 2163 O O1  . SO4 I 2 .  ? 15.973  -26.504 -26.167 1.00 50.45 ? 102 SO4 B O1  1 
HETATM 2164 O O2  . SO4 I 2 .  ? 14.890  -28.317 -27.151 1.00 56.51 ? 102 SO4 B O2  1 
HETATM 2165 O O3  . SO4 I 2 .  ? 13.917  -27.225 -25.308 1.00 59.28 ? 102 SO4 B O3  1 
HETATM 2166 O O4  . SO4 I 2 .  ? 13.978  -26.145 -27.383 1.00 47.81 ? 102 SO4 B O4  1 
HETATM 2167 N N1  . W1A J 4 .  ? 19.983  -15.708 -19.145 0.72 49.52 ? 103 W1A B N1  1 
HETATM 2168 C C4  . W1A J 4 .  ? 18.719  -15.139 -19.678 0.72 48.81 ? 103 W1A B C4  1 
HETATM 2169 C C5  . W1A J 4 .  ? 20.924  -16.181 -20.192 0.72 44.96 ? 103 W1A B C5  1 
HETATM 2170 C C6  . W1A J 4 .  ? 20.231  -17.073 -21.201 0.72 44.63 ? 103 W1A B C6  1 
HETATM 2171 O O1  . W1A J 4 .  ? 17.651  -13.784 -25.164 0.72 27.66 ? 103 W1A B O1  1 
HETATM 2172 S S   . W1A J 4 .  ? 17.211  -15.015 -24.582 0.72 32.34 ? 103 W1A B S   1 
HETATM 2173 O O   . W1A J 4 .  ? 16.179  -14.958 -23.596 0.72 34.38 ? 103 W1A B O   1 
HETATM 2174 C C   . W1A J 4 .  ? 16.731  -16.108 -25.866 0.72 33.13 ? 103 W1A B C   1 
HETATM 2175 N N   . W1A J 4 .  ? 18.501  -15.668 -23.878 0.72 33.81 ? 103 W1A B N   1 
HETATM 2176 C C1  . W1A J 4 .  ? 18.453  -16.857 -23.021 0.72 38.58 ? 103 W1A B C1  1 
HETATM 2177 C C2  . W1A J 4 .  ? 19.033  -16.300 -21.729 0.72 41.37 ? 103 W1A B C2  1 
HETATM 2178 C C3  . W1A J 4 .  ? 18.021  -16.099 -20.617 0.72 46.47 ? 103 W1A B C3  1 
HETATM 2179 C C1  . EDO K 3 .  ? 16.694  -36.303 16.329  1.00 31.47 ? 101 EDO C C1  1 
HETATM 2180 O O1  . EDO K 3 .  ? 15.642  -36.992 15.647  1.00 34.99 ? 101 EDO C O1  1 
HETATM 2181 C C2  . EDO K 3 .  ? 16.234  -35.381 17.419  1.00 29.98 ? 101 EDO C C2  1 
HETATM 2182 O O2  . EDO K 3 .  ? 15.346  -35.876 18.374  1.00 31.22 ? 101 EDO C O2  1 
HETATM 2183 S S   . SO4 L 2 .  ? 29.245  -38.643 12.349  1.00 90.47 ? 102 SO4 C S   1 
HETATM 2184 O O1  . SO4 L 2 .  ? 30.398  -37.921 11.861  1.00 91.01 ? 102 SO4 C O1  1 
HETATM 2185 O O2  . SO4 L 2 .  ? 28.047  -38.001 11.883  1.00 78.14 ? 102 SO4 C O2  1 
HETATM 2186 O O3  . SO4 L 2 .  ? 29.277  -39.998 11.867  1.00 80.25 ? 102 SO4 C O3  1 
HETATM 2187 O O4  . SO4 L 2 .  ? 29.255  -38.646 13.792  1.00 91.23 ? 102 SO4 C O4  1 
HETATM 2188 O O   . HOH M 5 .  ? -1.439  -30.149 0.510   1.00 64.02 ? 201 HOH A O   1 
HETATM 2189 O O   . HOH M 5 .  ? 8.489   -32.351 4.191   1.00 52.23 ? 202 HOH A O   1 
HETATM 2190 O O   . HOH M 5 .  ? -2.937  -28.133 5.786   1.00 62.44 ? 203 HOH A O   1 
HETATM 2191 O O   . HOH M 5 .  ? 3.930   -34.740 4.327   1.00 52.33 ? 204 HOH A O   1 
HETATM 2192 O O   . HOH M 5 .  ? 5.812   -28.938 6.828   1.00 48.85 ? 205 HOH A O   1 
HETATM 2193 O O   . HOH M 5 .  ? 10.796  -19.386 10.170  1.00 60.01 ? 206 HOH A O   1 
HETATM 2194 O O   . HOH M 5 .  ? 4.010   -10.484 13.587  1.00 47.73 ? 207 HOH A O   1 
HETATM 2195 O O   . HOH M 5 .  ? 11.091  -29.649 3.040   1.00 42.00 ? 208 HOH A O   1 
HETATM 2196 O O   . HOH M 5 .  ? 1.353   2.530   3.906   1.00 56.16 ? 209 HOH A O   1 
HETATM 2197 O O   . HOH M 5 .  ? -5.791  -13.622 -16.505 1.00 50.37 ? 210 HOH A O   1 
HETATM 2198 O O   . HOH M 5 .  ? 8.169   -17.855 -15.911 1.00 48.68 ? 211 HOH A O   1 
HETATM 2199 O O   . HOH M 5 .  ? -7.521  -21.099 -3.860  1.00 69.27 ? 212 HOH A O   1 
HETATM 2200 O O   . HOH M 5 .  ? 10.993  -9.349  -13.272 1.00 58.69 ? 213 HOH A O   1 
HETATM 2201 O O   . HOH M 5 .  ? -2.329  -30.870 -3.914  1.00 50.39 ? 214 HOH A O   1 
HETATM 2202 O O   . HOH M 5 .  ? -2.551  -11.758 13.837  1.00 50.61 ? 215 HOH A O   1 
HETATM 2203 O O   . HOH M 5 .  ? 0.521   -10.595 -15.545 1.00 45.75 ? 216 HOH A O   1 
HETATM 2204 O O   . HOH M 5 .  ? 7.029   -10.661 -12.078 1.00 36.95 ? 217 HOH A O   1 
HETATM 2205 O O   . HOH M 5 .  ? 4.631   -7.883  1.217   1.00 34.84 ? 218 HOH A O   1 
HETATM 2206 O O   . HOH M 5 .  ? -8.321  -17.017 3.253   1.00 50.34 ? 219 HOH A O   1 
HETATM 2207 O O   . HOH M 5 .  ? 11.080  -23.699 9.774   1.00 37.08 ? 220 HOH A O   1 
HETATM 2208 O O   . HOH M 5 .  ? 2.442   -25.245 -6.527  1.00 48.02 ? 221 HOH A O   1 
HETATM 2209 O O   . HOH M 5 .  ? 12.913  -11.917 8.123   1.00 61.23 ? 222 HOH A O   1 
HETATM 2210 O O   . HOH M 5 .  ? -2.323  3.255   -2.054  1.00 37.08 ? 223 HOH A O   1 
HETATM 2211 O O   . HOH M 5 .  ? -0.616  -29.474 9.878   1.00 52.39 ? 224 HOH A O   1 
HETATM 2212 O O   . HOH M 5 .  ? 5.007   -13.996 14.200  1.00 62.31 ? 225 HOH A O   1 
HETATM 2213 O O   . HOH M 5 .  ? 15.919  -24.502 1.889   1.00 38.69 ? 226 HOH A O   1 
HETATM 2214 O O   . HOH M 5 .  ? 19.827  -15.557 7.237   1.00 29.73 ? 227 HOH A O   1 
HETATM 2215 O O   . HOH M 5 .  ? 4.847   -1.540  -6.352  1.00 34.03 ? 228 HOH A O   1 
HETATM 2216 O O   . HOH M 5 .  ? -4.295  -21.159 6.126   1.00 38.55 ? 229 HOH A O   1 
HETATM 2217 O O   . HOH M 5 .  ? 4.384   -3.599  -3.270  1.00 30.33 ? 230 HOH A O   1 
HETATM 2218 O O   . HOH M 5 .  ? 8.993   -18.275 -10.967 1.00 32.17 ? 231 HOH A O   1 
HETATM 2219 O O   . HOH M 5 .  ? 14.017  -15.747 -9.280  1.00 33.27 ? 232 HOH A O   1 
HETATM 2220 O O   . HOH M 5 .  ? 1.280   -24.701 13.999  1.00 59.72 ? 233 HOH A O   1 
HETATM 2221 O O   . HOH M 5 .  ? -8.135  -15.741 -1.081  1.00 34.00 ? 234 HOH A O   1 
HETATM 2222 O O   . HOH M 5 .  ? 9.610   -6.086  -1.682  1.00 32.76 ? 235 HOH A O   1 
HETATM 2223 O O   . HOH M 5 .  ? -3.825  -10.878 6.805   1.00 34.62 ? 236 HOH A O   1 
HETATM 2224 O O   . HOH M 5 .  ? 9.955   -13.109 9.587   1.00 39.61 ? 237 HOH A O   1 
HETATM 2225 O O   . HOH M 5 .  ? 1.719   0.613   -7.367  1.00 35.73 ? 238 HOH A O   1 
HETATM 2226 O O   . HOH M 5 .  ? -7.863  -17.240 6.578   1.00 40.28 ? 239 HOH A O   1 
HETATM 2227 O O   . HOH M 5 .  ? 13.467  -27.944 -4.851  1.00 50.58 ? 240 HOH A O   1 
HETATM 2228 O O   . HOH M 5 .  ? 2.334   -25.105 -9.967  1.00 34.47 ? 241 HOH A O   1 
HETATM 2229 O O   . HOH M 5 .  ? 0.189   -33.680 4.775   1.00 55.31 ? 242 HOH A O   1 
HETATM 2230 O O   . HOH M 5 .  ? -6.184  -11.514 -11.323 1.00 38.53 ? 243 HOH A O   1 
HETATM 2231 O O   . HOH M 5 .  ? -5.807  -15.901 -7.999  1.00 28.26 ? 244 HOH A O   1 
HETATM 2232 O O   . HOH M 5 .  ? 1.835   -4.690  -10.217 1.00 35.61 ? 245 HOH A O   1 
HETATM 2233 O O   . HOH M 5 .  ? 10.804  -5.140  -7.738  1.00 32.46 ? 246 HOH A O   1 
HETATM 2234 O O   . HOH M 5 .  ? 17.130  -12.901 1.376   1.00 20.26 ? 247 HOH A O   1 
HETATM 2235 O O   . HOH M 5 .  ? -1.819  -22.039 -0.611  1.00 26.87 ? 248 HOH A O   1 
HETATM 2236 O O   . HOH M 5 .  ? 12.443  -15.725 -11.996 1.00 58.23 ? 249 HOH A O   1 
HETATM 2237 O O   . HOH M 5 .  ? 11.646  -16.552 -14.744 1.00 41.06 ? 250 HOH A O   1 
HETATM 2238 O O   . HOH M 5 .  ? 12.986  -9.539  -7.161  1.00 39.60 ? 251 HOH A O   1 
HETATM 2239 O O   . HOH M 5 .  ? 11.328  -6.118  -3.926  1.00 41.05 ? 252 HOH A O   1 
HETATM 2240 O O   . HOH M 5 .  ? 11.520  -11.933 5.964   1.00 32.28 ? 253 HOH A O   1 
HETATM 2241 O O   . HOH M 5 .  ? 13.282  -11.998 -4.230  1.00 20.84 ? 254 HOH A O   1 
HETATM 2242 O O   . HOH M 5 .  ? 1.493   -18.516 -18.657 1.00 42.18 ? 255 HOH A O   1 
HETATM 2243 O O   . HOH M 5 .  ? 15.661  -12.153 -5.395  1.00 32.57 ? 256 HOH A O   1 
HETATM 2244 O O   . HOH M 5 .  ? -0.691  -20.969 7.042   1.00 33.60 ? 257 HOH A O   1 
HETATM 2245 O O   . HOH M 5 .  ? 3.203   -29.583 -0.594  1.00 35.80 ? 258 HOH A O   1 
HETATM 2246 O O   . HOH M 5 .  ? 1.680   -10.543 11.703  1.00 36.51 ? 259 HOH A O   1 
HETATM 2247 O O   . HOH M 5 .  ? 12.558  -13.332 -8.549  1.00 40.13 ? 260 HOH A O   1 
HETATM 2248 O O   . HOH M 5 .  ? 11.468  -12.367 -6.199  1.00 25.75 ? 261 HOH A O   1 
HETATM 2249 O O   . HOH M 5 .  ? 8.828   -16.311 -13.140 1.00 34.70 ? 262 HOH A O   1 
HETATM 2250 O O   . HOH M 5 .  ? -4.343  -25.936 -5.469  1.00 39.90 ? 263 HOH A O   1 
HETATM 2251 O O   . HOH M 5 .  ? 6.241   -16.186 -15.001 1.00 43.30 ? 264 HOH A O   1 
HETATM 2252 O O   . HOH M 5 .  ? -5.902  -19.735 -5.666  1.00 35.79 ? 265 HOH A O   1 
HETATM 2253 O O   . HOH M 5 .  ? -8.626  -21.110 -1.250  1.00 37.49 ? 266 HOH A O   1 
HETATM 2254 O O   . HOH M 5 .  ? -7.865  -16.694 1.577   1.00 37.23 ? 267 HOH A O   1 
HETATM 2255 O O   . HOH M 5 .  ? 16.782  -12.320 -16.982 1.00 38.41 ? 268 HOH A O   1 
HETATM 2256 O O   . HOH M 5 .  ? 9.761   -20.312 -18.403 1.00 40.26 ? 269 HOH A O   1 
HETATM 2257 O O   . HOH M 5 .  ? 2.431   -6.306  5.428   1.00 37.75 ? 270 HOH A O   1 
HETATM 2258 O O   . HOH M 5 .  ? -1.412  -11.902 11.264  1.00 36.40 ? 271 HOH A O   1 
HETATM 2259 O O   . HOH M 5 .  ? -6.132  -12.830 6.733   1.00 39.47 ? 272 HOH A O   1 
HETATM 2260 O O   . HOH M 5 .  ? -1.387  -7.446  11.474  1.00 45.20 ? 273 HOH A O   1 
HETATM 2261 O O   . HOH M 5 .  ? 7.987   -7.884  1.229   1.00 31.08 ? 274 HOH A O   1 
HETATM 2262 O O   . HOH M 5 .  ? -8.320  -19.283 -3.288  1.00 45.27 ? 275 HOH A O   1 
HETATM 2263 O O   . HOH M 5 .  ? 2.889   -9.929  -13.292 1.00 44.84 ? 276 HOH A O   1 
HETATM 2264 O O   . HOH M 5 .  ? -10.961 -15.969 -3.494  1.00 50.21 ? 277 HOH A O   1 
HETATM 2265 O O   . HOH M 5 .  ? 8.038   -8.206  4.581   1.00 34.98 ? 278 HOH A O   1 
HETATM 2266 O O   . HOH M 5 .  ? 0.132   -23.360 8.994   1.00 43.63 ? 279 HOH A O   1 
HETATM 2267 O O   . HOH M 5 .  ? 6.407   -5.780  0.477   1.00 47.00 ? 280 HOH A O   1 
HETATM 2268 O O   . HOH M 5 .  ? 14.431  -29.480 4.014   1.00 37.49 ? 281 HOH A O   1 
HETATM 2269 O O   . HOH M 5 .  ? -6.074  -26.602 3.430   1.00 47.50 ? 282 HOH A O   1 
HETATM 2270 O O   . HOH M 5 .  ? 5.060   -7.614  3.957   1.00 35.94 ? 283 HOH A O   1 
HETATM 2271 O O   . HOH M 5 .  ? -6.709  -13.661 -11.680 1.00 56.75 ? 284 HOH A O   1 
HETATM 2272 O O   . HOH M 5 .  ? 9.147   -2.625  -0.360  1.00 65.52 ? 285 HOH A O   1 
HETATM 2273 O O   . HOH M 5 .  ? 4.677   6.171   -4.619  1.00 71.59 ? 286 HOH A O   1 
HETATM 2274 O O   . HOH M 5 .  ? 22.205  -16.539 -0.410  1.00 39.43 ? 287 HOH A O   1 
HETATM 2275 O O   . HOH M 5 .  ? 15.289  -28.109 -0.869  1.00 54.26 ? 288 HOH A O   1 
HETATM 2276 O O   . HOH M 5 .  ? 8.149   -17.630 8.731   1.00 45.32 ? 289 HOH A O   1 
HETATM 2277 O O   . HOH M 5 .  ? -3.888  -26.694 7.445   1.00 49.49 ? 290 HOH A O   1 
HETATM 2278 O O   . HOH M 5 .  ? -7.379  -21.690 -5.998  1.00 45.94 ? 291 HOH A O   1 
HETATM 2279 O O   . HOH M 5 .  ? 9.893   -27.525 -7.421  1.00 57.35 ? 292 HOH A O   1 
HETATM 2280 O O   . HOH M 5 .  ? -7.276  -11.402 -7.984  1.00 28.44 ? 293 HOH A O   1 
HETATM 2281 O O   . HOH M 5 .  ? 10.984  -7.854  0.373   1.00 23.59 ? 294 HOH A O   1 
HETATM 2282 O O   . HOH M 5 .  ? 16.842  -18.159 -9.712  1.00 50.02 ? 295 HOH A O   1 
HETATM 2283 O O   . HOH M 5 .  ? -0.457  -20.964 10.807  1.00 79.09 ? 296 HOH A O   1 
HETATM 2284 O O   . HOH M 5 .  ? 21.369  -16.692 -3.426  1.00 28.36 ? 297 HOH A O   1 
HETATM 2285 O O   . HOH M 5 .  ? -3.814  -7.888  10.620  1.00 47.53 ? 298 HOH A O   1 
HETATM 2286 O O   . HOH M 5 .  ? -5.514  -17.266 -15.956 1.00 54.32 ? 299 HOH A O   1 
HETATM 2287 O O   . HOH M 5 .  ? 1.398   -29.363 -7.121  1.00 54.03 ? 300 HOH A O   1 
HETATM 2288 O O   . HOH M 5 .  ? 15.673  -13.471 10.659  1.00 55.22 ? 301 HOH A O   1 
HETATM 2289 O O   . HOH M 5 .  ? 8.803   -9.145  -13.745 1.00 38.09 ? 302 HOH A O   1 
HETATM 2290 O O   . HOH M 5 .  ? 4.835   -6.874  -10.879 1.00 44.48 ? 303 HOH A O   1 
HETATM 2291 O O   . HOH M 5 .  ? -5.699  -23.504 -7.002  1.00 41.28 ? 304 HOH A O   1 
HETATM 2292 O O   . HOH M 5 .  ? 16.891  -10.001 -9.828  1.00 50.34 ? 305 HOH A O   1 
HETATM 2293 O O   . HOH M 5 .  ? -10.135 -28.237 -1.752  1.00 60.79 ? 306 HOH A O   1 
HETATM 2294 O O   . HOH M 5 .  ? 8.881   -12.745 12.252  1.00 52.83 ? 307 HOH A O   1 
HETATM 2295 O O   . HOH M 5 .  ? -7.387  -14.131 -9.165  1.00 36.76 ? 308 HOH A O   1 
HETATM 2296 O O   . HOH M 5 .  ? -0.593  -3.292  -11.061 1.00 53.16 ? 309 HOH A O   1 
HETATM 2297 O O   . HOH M 5 .  ? -6.179  -22.642 5.784   1.00 55.05 ? 310 HOH A O   1 
HETATM 2298 O O   . HOH M 5 .  ? -9.455  -19.163 1.524   1.00 46.67 ? 311 HOH A O   1 
HETATM 2299 O O   . HOH M 5 .  ? 4.725   -9.745  -11.360 1.00 42.07 ? 312 HOH A O   1 
HETATM 2300 O O   . HOH M 5 .  ? -11.314 -13.556 -2.834  1.00 38.19 ? 313 HOH A O   1 
HETATM 2301 O O   . HOH M 5 .  ? -7.132  -19.203 8.234   1.00 48.78 ? 314 HOH A O   1 
HETATM 2302 O O   . HOH M 5 .  ? -3.068  -21.548 7.945   1.00 43.72 ? 315 HOH A O   1 
HETATM 2303 O O   . HOH M 5 .  ? 5.828   -3.342  1.073   1.00 52.62 ? 316 HOH A O   1 
HETATM 2304 O O   . HOH M 5 .  ? 7.874   -30.617 -2.067  1.00 53.31 ? 317 HOH A O   1 
HETATM 2305 O O   . HOH M 5 .  ? 8.441   -22.482 -19.348 1.00 49.06 ? 318 HOH A O   1 
HETATM 2306 O O   . HOH M 5 .  ? -5.077  -21.110 -8.037  1.00 51.54 ? 319 HOH A O   1 
HETATM 2307 O O   . HOH M 5 .  ? 3.811   -3.197  1.905   1.00 66.91 ? 320 HOH A O   1 
HETATM 2308 O O   . HOH M 5 .  ? 7.527   -38.626 4.941   1.00 57.99 ? 321 HOH A O   1 
HETATM 2309 O O   . HOH N 5 .  ? 20.151  1.447   -24.373 1.00 71.98 ? 201 HOH B O   1 
HETATM 2310 O O   . HOH N 5 .  ? 10.040  -11.230 -37.997 1.00 46.54 ? 202 HOH B O   1 
HETATM 2311 O O   . HOH N 5 .  ? 22.939  -14.605 -23.168 1.00 42.30 ? 203 HOH B O   1 
HETATM 2312 O O   . HOH N 5 .  ? 12.910  -4.532  -41.686 1.00 48.04 ? 204 HOH B O   1 
HETATM 2313 O O   . HOH N 5 .  ? 1.823   -16.688 -32.498 1.00 58.12 ? 205 HOH B O   1 
HETATM 2314 O O   . HOH N 5 .  ? 27.942  -8.230  -28.927 1.00 42.74 ? 206 HOH B O   1 
HETATM 2315 O O   . HOH N 5 .  ? 12.907  -26.132 -37.105 1.00 47.50 ? 207 HOH B O   1 
HETATM 2316 O O   . HOH N 5 .  ? 25.116  -5.227  -29.786 1.00 34.56 ? 208 HOH B O   1 
HETATM 2317 O O   . HOH N 5 .  ? 26.113  -23.057 -31.204 1.00 35.47 ? 209 HOH B O   1 
HETATM 2318 O O   . HOH N 5 .  ? 30.711  -8.203  -29.812 1.00 51.75 ? 210 HOH B O   1 
HETATM 2319 O O   . HOH N 5 .  ? 6.613   -12.281 -26.049 1.00 36.94 ? 211 HOH B O   1 
HETATM 2320 O O   . HOH N 5 .  ? 15.245  -17.459 -18.942 1.00 43.38 ? 212 HOH B O   1 
HETATM 2321 O O   . HOH N 5 .  ? 20.313  -21.840 -23.258 1.00 48.22 ? 213 HOH B O   1 
HETATM 2322 O O   . HOH N 5 .  ? 30.426  -19.778 -40.297 1.00 36.67 ? 214 HOH B O   1 
HETATM 2323 O O   . HOH N 5 .  ? 21.799  -3.780  -24.497 1.00 62.73 ? 215 HOH B O   1 
HETATM 2324 O O   . HOH N 5 .  ? 15.599  -25.545 -45.815 1.00 42.76 ? 216 HOH B O   1 
HETATM 2325 O O   . HOH N 5 .  ? 25.546  -5.942  -35.898 1.00 38.75 ? 217 HOH B O   1 
HETATM 2326 O O   . HOH N 5 .  ? 28.040  -2.214  -26.026 1.00 56.59 ? 218 HOH B O   1 
HETATM 2327 O O   . HOH N 5 .  ? 20.942  -15.754 -25.007 1.00 43.42 ? 219 HOH B O   1 
HETATM 2328 O O   . HOH N 5 .  ? 18.922  -20.016 -19.192 1.00 45.31 ? 220 HOH B O   1 
HETATM 2329 O O   . HOH N 5 .  ? 34.802  -23.388 -30.198 1.00 60.15 ? 221 HOH B O   1 
HETATM 2330 O O   . HOH N 5 .  ? 24.493  -1.794  -36.213 1.00 47.93 ? 222 HOH B O   1 
HETATM 2331 O O   . HOH N 5 .  ? 11.298  -8.087  -41.415 1.00 50.70 ? 223 HOH B O   1 
HETATM 2332 O O   . HOH N 5 .  ? 20.749  -13.381 -42.746 1.00 38.55 ? 224 HOH B O   1 
HETATM 2333 O O   . HOH N 5 .  ? 10.222  -19.638 -43.180 1.00 44.89 ? 225 HOH B O   1 
HETATM 2334 O O   . HOH N 5 .  ? 8.848   -8.693  -16.473 1.00 41.60 ? 226 HOH B O   1 
HETATM 2335 O O   . HOH N 5 .  ? 16.798  -19.167 -28.788 1.00 25.21 ? 227 HOH B O   1 
HETATM 2336 O O   . HOH N 5 .  ? 27.995  -17.436 -25.002 1.00 38.77 ? 228 HOH B O   1 
HETATM 2337 O O   . HOH N 5 .  ? 22.668  -23.135 -28.754 1.00 37.71 ? 229 HOH B O   1 
HETATM 2338 O O   . HOH N 5 .  ? 21.310  -26.284 -30.076 1.00 58.30 ? 230 HOH B O   1 
HETATM 2339 O O   . HOH N 5 .  ? 10.583  -18.909 -32.991 1.00 27.55 ? 231 HOH B O   1 
HETATM 2340 O O   . HOH N 5 .  ? 22.111  3.601   -32.640 1.00 46.55 ? 232 HOH B O   1 
HETATM 2341 O O   . HOH N 5 .  ? 7.697   -12.453 -38.690 1.00 47.61 ? 233 HOH B O   1 
HETATM 2342 O O   . HOH N 5 .  ? 7.112   -19.109 -35.022 1.00 44.15 ? 234 HOH B O   1 
HETATM 2343 O O   . HOH N 5 .  ? 23.619  -2.251  -29.131 1.00 36.78 ? 235 HOH B O   1 
HETATM 2344 O O   . HOH N 5 .  ? 18.216  -0.539  -38.355 1.00 28.80 ? 236 HOH B O   1 
HETATM 2345 O O   . HOH N 5 .  ? 13.312  -22.400 -20.621 1.00 52.02 ? 237 HOH B O   1 
HETATM 2346 O O   . HOH N 5 .  ? 19.903  -25.580 -34.066 1.00 40.67 ? 238 HOH B O   1 
HETATM 2347 O O   . HOH N 5 .  ? 23.253  -5.604  -24.793 1.00 44.26 ? 239 HOH B O   1 
HETATM 2348 O O   . HOH N 5 .  ? 18.044  -23.283 -20.823 1.00 61.24 ? 240 HOH B O   1 
HETATM 2349 O O   . HOH N 5 .  ? 6.103   -7.261  -32.354 1.00 51.27 ? 241 HOH B O   1 
HETATM 2350 O O   . HOH N 5 .  ? 27.837  -4.615  -37.612 1.00 60.25 ? 242 HOH B O   1 
HETATM 2351 O O   . HOH N 5 .  ? 32.559  -18.820 -42.436 1.00 43.07 ? 243 HOH B O   1 
HETATM 2352 O O   . HOH N 5 .  ? 14.743  -24.453 -40.337 1.00 40.96 ? 244 HOH B O   1 
HETATM 2353 O O   . HOH N 5 .  ? 17.085  -25.747 -34.308 1.00 42.79 ? 245 HOH B O   1 
HETATM 2354 O O   . HOH N 5 .  ? 10.727  -21.885 -32.790 1.00 34.94 ? 246 HOH B O   1 
HETATM 2355 O O   . HOH N 5 .  ? 23.760  -4.242  -36.762 1.00 29.21 ? 247 HOH B O   1 
HETATM 2356 O O   . HOH N 5 .  ? 17.561  -19.836 -42.148 1.00 50.05 ? 248 HOH B O   1 
HETATM 2357 O O   . HOH N 5 .  ? 20.447  -10.095 -42.933 1.00 40.34 ? 249 HOH B O   1 
HETATM 2358 O O   . HOH N 5 .  ? 8.354   -28.065 -38.297 1.00 53.18 ? 250 HOH B O   1 
HETATM 2359 O O   . HOH N 5 .  ? 14.354  -6.381  -41.131 1.00 38.61 ? 251 HOH B O   1 
HETATM 2360 O O   . HOH N 5 .  ? 4.797   -19.198 -25.724 1.00 55.51 ? 252 HOH B O   1 
HETATM 2361 O O   . HOH N 5 .  ? 3.269   -8.670  -26.911 1.00 51.82 ? 253 HOH B O   1 
HETATM 2362 O O   . HOH N 5 .  ? 27.471  -10.859 -28.702 1.00 51.27 ? 254 HOH B O   1 
HETATM 2363 O O   . HOH N 5 .  ? 18.460  -25.910 -28.857 1.00 39.45 ? 255 HOH B O   1 
HETATM 2364 O O   . HOH N 5 .  ? 4.106   -19.250 -30.906 1.00 50.39 ? 256 HOH B O   1 
HETATM 2365 O O   . HOH N 5 .  ? 10.490  -16.826 -44.371 1.00 48.03 ? 257 HOH B O   1 
HETATM 2366 O O   . HOH N 5 .  ? 1.865   -13.098 -28.207 1.00 45.56 ? 258 HOH B O   1 
HETATM 2367 O O   . HOH N 5 .  ? 7.746   -18.344 -31.747 1.00 41.43 ? 259 HOH B O   1 
HETATM 2368 O O   . HOH N 5 .  ? 21.063  -6.385  -42.564 1.00 36.12 ? 260 HOH B O   1 
HETATM 2369 O O   . HOH N 5 .  ? 18.029  -3.676  -21.987 1.00 55.71 ? 261 HOH B O   1 
HETATM 2370 O O   . HOH N 5 .  ? 31.953  -21.180 -38.308 1.00 43.94 ? 262 HOH B O   1 
HETATM 2371 O O   . HOH N 5 .  ? 18.043  -15.832 -45.734 1.00 41.17 ? 263 HOH B O   1 
HETATM 2372 O O   . HOH N 5 .  ? 7.571   -8.184  -20.786 1.00 47.68 ? 264 HOH B O   1 
HETATM 2373 O O   . HOH N 5 .  ? 23.678  -11.156 -21.948 1.00 41.77 ? 265 HOH B O   1 
HETATM 2374 O O   . HOH N 5 .  ? 12.288  -4.719  -24.762 1.00 46.49 ? 266 HOH B O   1 
HETATM 2375 O O   . HOH N 5 .  ? 18.029  -0.294  -25.516 1.00 64.98 ? 267 HOH B O   1 
HETATM 2376 O O   . HOH N 5 .  ? 27.860  -24.800 -35.080 1.00 36.41 ? 268 HOH B O   1 
HETATM 2377 O O   . HOH N 5 .  ? 17.036  -9.621  -43.879 1.00 43.84 ? 269 HOH B O   1 
HETATM 2378 O O   . HOH N 5 .  ? 6.575   -20.764 -24.883 1.00 39.99 ? 270 HOH B O   1 
HETATM 2379 O O   . HOH N 5 .  ? 26.961  -22.924 -28.586 1.00 55.14 ? 271 HOH B O   1 
HETATM 2380 O O   . HOH N 5 .  ? 26.200  -0.323  -29.212 1.00 49.62 ? 272 HOH B O   1 
HETATM 2381 O O   . HOH N 5 .  ? 18.455  4.430   -34.224 1.00 40.51 ? 273 HOH B O   1 
HETATM 2382 O O   . HOH N 5 .  ? 18.642  -13.345 -44.668 1.00 48.30 ? 274 HOH B O   1 
HETATM 2383 O O   . HOH N 5 .  ? 20.549  3.798   -32.865 1.00 35.41 ? 275 HOH B O   1 
HETATM 2384 O O   . HOH N 5 .  ? 24.635  -6.714  -42.788 1.00 45.66 ? 276 HOH B O   1 
HETATM 2385 O O   . HOH N 5 .  ? 7.729   -23.565 -24.308 1.00 49.05 ? 277 HOH B O   1 
HETATM 2386 O O   . HOH N 5 .  ? 31.687  -12.189 -38.117 1.00 62.74 ? 278 HOH B O   1 
HETATM 2387 O O   . HOH N 5 .  ? 28.794  -12.416 -26.610 1.00 53.24 ? 279 HOH B O   1 
HETATM 2388 O O   . HOH N 5 .  ? 9.857   -6.065  -40.997 1.00 42.04 ? 280 HOH B O   1 
HETATM 2389 O O   . HOH N 5 .  ? 12.839  -20.077 -19.459 1.00 48.53 ? 281 HOH B O   1 
HETATM 2390 O O   . HOH N 5 .  ? 17.311  -25.775 -21.021 1.00 57.05 ? 282 HOH B O   1 
HETATM 2391 O O   . HOH N 5 .  ? 39.272  -13.173 -38.881 1.00 64.30 ? 283 HOH B O   1 
HETATM 2392 O O   . HOH N 5 .  ? 15.108  -7.988  -43.049 1.00 43.34 ? 284 HOH B O   1 
HETATM 2393 O O   . HOH N 5 .  ? 24.259  -4.126  -27.965 1.00 54.94 ? 285 HOH B O   1 
HETATM 2394 O O   . HOH N 5 .  ? 27.973  -24.780 -32.244 1.00 44.06 ? 286 HOH B O   1 
HETATM 2395 O O   . HOH N 5 .  ? 24.007  -17.002 -22.398 1.00 52.08 ? 287 HOH B O   1 
HETATM 2396 O O   . HOH N 5 .  ? 15.539  -21.949 -41.844 1.00 51.16 ? 288 HOH B O   1 
HETATM 2397 O O   . HOH N 5 .  ? 7.679   -21.579 -29.779 1.00 39.13 ? 289 HOH B O   1 
HETATM 2398 O O   . HOH N 5 .  ? 8.045   -3.188  -28.825 1.00 56.22 ? 290 HOH B O   1 
HETATM 2399 O O   . HOH N 5 .  ? 7.357   -9.913  -18.611 1.00 41.21 ? 291 HOH B O   1 
HETATM 2400 O O   . HOH N 5 .  ? 22.555  -29.166 -35.523 1.00 43.46 ? 292 HOH B O   1 
HETATM 2401 O O   . HOH N 5 .  ? 20.880  -20.099 -21.695 1.00 55.76 ? 293 HOH B O   1 
HETATM 2402 O O   . HOH O 5 .  ? 26.869  -37.837 10.261  1.00 40.16 ? 201 HOH C O   1 
HETATM 2403 O O   . HOH O 5 .  ? 26.548  -39.184 12.686  1.00 37.25 ? 202 HOH C O   1 
HETATM 2404 O O   . HOH O 5 .  ? 26.803  -24.891 32.021  1.00 88.97 ? 203 HOH C O   1 
HETATM 2405 O O   . HOH O 5 .  ? 16.268  -17.773 25.073  1.00 59.95 ? 204 HOH C O   1 
HETATM 2406 O O   . HOH O 5 .  ? 19.883  -20.219 29.797  1.00 67.48 ? 205 HOH C O   1 
HETATM 2407 O O   . HOH O 5 .  ? 27.228  -19.142 12.985  1.00 66.26 ? 206 HOH C O   1 
HETATM 2408 O O   . HOH O 5 .  ? 7.614   -31.661 12.190  1.00 47.02 ? 207 HOH C O   1 
HETATM 2409 O O   . HOH O 5 .  ? 9.054   -36.921 18.147  1.00 59.84 ? 208 HOH C O   1 
HETATM 2410 O O   . HOH O 5 .  ? 33.252  -24.288 31.537  1.00 50.85 ? 209 HOH C O   1 
HETATM 2411 O O   . HOH O 5 .  ? 19.116  -20.212 10.518  1.00 35.56 ? 210 HOH C O   1 
HETATM 2412 O O   . HOH O 5 .  ? 12.277  -28.362 28.054  1.00 52.61 ? 211 HOH C O   1 
HETATM 2413 O O   . HOH O 5 .  ? 31.394  -29.805 32.069  1.00 65.42 ? 212 HOH C O   1 
HETATM 2414 O O   . HOH O 5 .  ? 22.970  -41.659 18.420  1.00 38.76 ? 213 HOH C O   1 
HETATM 2415 O O   . HOH O 5 .  ? 12.797  -31.532 8.154   1.00 33.08 ? 214 HOH C O   1 
HETATM 2416 O O   . HOH O 5 .  ? 17.674  -17.086 14.875  1.00 46.36 ? 215 HOH C O   1 
HETATM 2417 O O   . HOH O 5 .  ? 23.561  -20.883 23.863  1.00 50.79 ? 216 HOH C O   1 
HETATM 2418 O O   . HOH O 5 .  ? 31.729  -33.301 25.714  1.00 45.07 ? 217 HOH C O   1 
HETATM 2419 O O   . HOH O 5 .  ? 30.298  -31.027 15.717  1.00 46.06 ? 218 HOH C O   1 
HETATM 2420 O O   . HOH O 5 .  ? 5.674   -26.675 16.720  1.00 48.11 ? 219 HOH C O   1 
HETATM 2421 O O   . HOH O 5 .  ? 25.550  -33.959 34.619  1.00 51.54 ? 220 HOH C O   1 
HETATM 2422 O O   . HOH O 5 .  ? 30.248  -40.558 9.468   1.00 32.46 ? 221 HOH C O   1 
HETATM 2423 O O   . HOH O 5 .  ? 31.205  -39.802 27.148  1.00 47.52 ? 222 HOH C O   1 
HETATM 2424 O O   . HOH O 5 .  ? 14.180  -37.206 13.449  1.00 42.10 ? 223 HOH C O   1 
HETATM 2425 O O   . HOH O 5 .  ? 15.138  -39.239 16.990  1.00 54.82 ? 224 HOH C O   1 
HETATM 2426 O O   . HOH O 5 .  ? 30.267  -17.420 9.631   1.00 45.30 ? 225 HOH C O   1 
HETATM 2427 O O   . HOH O 5 .  ? 15.563  -17.693 19.376  1.00 42.79 ? 226 HOH C O   1 
HETATM 2428 O O   . HOH O 5 .  ? 19.891  -41.863 12.126  1.00 29.55 ? 227 HOH C O   1 
HETATM 2429 O O   . HOH O 5 .  ? 29.843  -39.768 31.337  1.00 33.55 ? 228 HOH C O   1 
HETATM 2430 O O   . HOH O 5 .  ? 26.049  -24.168 6.625   1.00 56.79 ? 229 HOH C O   1 
HETATM 2431 O O   . HOH O 5 .  ? 23.081  -18.528 21.684  1.00 54.56 ? 230 HOH C O   1 
HETATM 2432 O O   . HOH O 5 .  ? 16.398  -37.938 19.773  1.00 54.49 ? 231 HOH C O   1 
HETATM 2433 O O   . HOH O 5 .  ? 15.157  -21.117 12.202  1.00 36.66 ? 232 HOH C O   1 
HETATM 2434 O O   . HOH O 5 .  ? 6.970   -18.087 10.846  1.00 38.47 ? 233 HOH C O   1 
HETATM 2435 O O   . HOH O 5 .  ? 28.176  -37.232 15.905  1.00 38.38 ? 234 HOH C O   1 
HETATM 2436 O O   . HOH O 5 .  ? 22.234  -28.553 11.053  1.00 31.13 ? 235 HOH C O   1 
HETATM 2437 O O   . HOH O 5 .  ? 25.212  -31.433 10.750  1.00 36.01 ? 236 HOH C O   1 
HETATM 2438 O O   . HOH O 5 .  ? 5.717   -33.804 23.445  1.00 60.78 ? 237 HOH C O   1 
HETATM 2439 O O   . HOH O 5 .  ? 28.014  -37.563 24.917  1.00 52.43 ? 238 HOH C O   1 
HETATM 2440 O O   . HOH O 5 .  ? 22.035  -34.394 16.527  1.00 25.57 ? 239 HOH C O   1 
HETATM 2441 O O   . HOH O 5 .  ? 20.789  -28.741 8.429   1.00 35.87 ? 240 HOH C O   1 
HETATM 2442 O O   . HOH O 5 .  ? 31.708  -43.322 12.068  1.00 47.42 ? 241 HOH C O   1 
HETATM 2443 O O   . HOH O 5 .  ? 25.770  -17.502 13.749  1.00 43.82 ? 242 HOH C O   1 
HETATM 2444 O O   . HOH O 5 .  ? 30.035  -25.334 32.480  1.00 64.24 ? 243 HOH C O   1 
HETATM 2445 O O   . HOH O 5 .  ? 20.655  -40.028 26.253  1.00 37.60 ? 244 HOH C O   1 
HETATM 2446 O O   . HOH O 5 .  ? 30.731  -35.670 28.474  1.00 57.60 ? 245 HOH C O   1 
HETATM 2447 O O   . HOH O 5 .  ? 30.495  -29.216 12.083  1.00 50.32 ? 246 HOH C O   1 
HETATM 2448 O O   . HOH O 5 .  ? 12.990  -23.082 27.888  1.00 69.04 ? 247 HOH C O   1 
HETATM 2449 O O   . HOH O 5 .  ? 20.981  -29.583 4.848   1.00 56.04 ? 248 HOH C O   1 
HETATM 2450 O O   . HOH O 5 .  ? 19.186  -26.719 2.940   1.00 48.36 ? 249 HOH C O   1 
HETATM 2451 O O   . HOH O 5 .  ? 17.733  -21.192 12.775  1.00 44.72 ? 250 HOH C O   1 
HETATM 2452 O O   . HOH O 5 .  ? 20.562  -41.121 39.335  1.00 63.29 ? 251 HOH C O   1 
HETATM 2453 O O   . HOH O 5 .  ? 14.421  -37.644 6.068   1.00 52.74 ? 252 HOH C O   1 
HETATM 2454 O O   . HOH O 5 .  ? 28.029  -36.685 18.559  1.00 40.75 ? 253 HOH C O   1 
HETATM 2455 O O   . HOH O 5 .  ? 16.507  -33.862 28.607  1.00 52.07 ? 254 HOH C O   1 
HETATM 2456 O O   . HOH O 5 .  ? 9.661   -30.465 9.871   1.00 33.86 ? 255 HOH C O   1 
HETATM 2457 O O   . HOH O 5 .  ? 25.546  -39.649 20.164  1.00 35.59 ? 256 HOH C O   1 
HETATM 2458 O O   . HOH O 5 .  ? 31.421  -43.512 15.758  1.00 50.07 ? 257 HOH C O   1 
HETATM 2459 O O   . HOH O 5 .  ? 14.216  -38.855 9.438   1.00 57.27 ? 258 HOH C O   1 
HETATM 2460 O O   . HOH O 5 .  ? 9.177   -18.908 23.772  1.00 45.38 ? 259 HOH C O   1 
HETATM 2461 O O   . HOH O 5 .  ? 12.661  -38.762 24.005  1.00 50.14 ? 260 HOH C O   1 
HETATM 2462 O O   . HOH O 5 .  ? 30.286  -32.581 18.195  1.00 40.17 ? 261 HOH C O   1 
HETATM 2463 O O   . HOH O 5 .  ? 29.504  -20.362 13.061  1.00 52.42 ? 262 HOH C O   1 
HETATM 2464 O O   . HOH O 5 .  ? 19.685  -19.093 25.104  1.00 51.26 ? 263 HOH C O   1 
HETATM 2465 O O   . HOH O 5 .  ? 28.033  -14.876 12.975  1.00 53.43 ? 264 HOH C O   1 
HETATM 2466 O O   . HOH O 5 .  ? 25.503  -17.771 21.202  1.00 58.12 ? 265 HOH C O   1 
HETATM 2467 O O   . HOH O 5 .  ? 2.559   -28.811 13.777  1.00 55.29 ? 266 HOH C O   1 
HETATM 2468 O O   . HOH O 5 .  ? 4.894   -24.169 18.510  1.00 59.88 ? 267 HOH C O   1 
HETATM 2469 O O   . HOH O 5 .  ? 20.433  -13.009 13.378  1.00 46.69 ? 268 HOH C O   1 
HETATM 2470 O O   . HOH O 5 .  ? 11.994  -21.322 10.654  1.00 38.82 ? 269 HOH C O   1 
HETATM 2471 O O   . HOH O 5 .  ? 25.095  -36.248 9.956   1.00 50.36 ? 270 HOH C O   1 
HETATM 2472 O O   . HOH O 5 .  ? 17.162  -36.457 29.487  1.00 58.45 ? 271 HOH C O   1 
HETATM 2473 O O   . HOH O 5 .  ? 23.982  -15.906 11.893  1.00 44.97 ? 272 HOH C O   1 
HETATM 2474 O O   . HOH O 5 .  ? 29.303  -41.640 27.158  1.00 37.70 ? 273 HOH C O   1 
HETATM 2475 O O   . HOH O 5 .  ? 22.433  -13.917 13.245  1.00 49.80 ? 274 HOH C O   1 
HETATM 2476 O O   . HOH O 5 .  ? 16.122  -19.396 29.499  1.00 53.66 ? 275 HOH C O   1 
HETATM 2477 O O   . HOH O 5 .  ? 32.217  -39.241 29.866  1.00 43.68 ? 276 HOH C O   1 
HETATM 2478 O O   . HOH O 5 .  ? 35.005  -32.041 24.218  1.00 55.42 ? 277 HOH C O   1 
HETATM 2479 O O   . HOH O 5 .  ? 30.021  -21.000 25.420  1.00 67.67 ? 278 HOH C O   1 
HETATM 2480 O O   . HOH O 5 .  ? 24.338  -29.216 9.426   1.00 39.66 ? 279 HOH C O   1 
HETATM 2481 O O   . HOH O 5 .  ? 33.479  -44.511 15.227  1.00 36.64 ? 280 HOH C O   1 
HETATM 2482 O O   . HOH O 5 .  ? 37.262  -24.294 26.294  1.00 67.70 ? 281 HOH C O   1 
# 
