data_7HHB
# 
_entry.id   7HHB 
# 
_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   7HHB         pdb_00007hhb 10.2210/pdb7hhb/pdb 
WWPDB D_1001407473 ?            ?                   
# 
_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                        7HHB 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-29 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.email 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
5 'von Delft' Frank  ?  frank.von-delft@diamond.ac.uk 'principal investigator/group leader' 0000-0003-0378-0017 
6 Strelkov    Sergei V. sergei.strelkov@kuleuven.be   'principal investigator/group leader' 0000-0003-3101-2867 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Vantieghem, T.'  1 
'Osipov, E.'      2 
'Fearon, D.'      3 
'Douangamath, A.' 4 
'von Delft, F.'   5 
'Strelkov, S.'    6 
# 
_citation.id                        primary 
_citation.title                     'Rational fragment-based design of compounds targeting the PWWP domain of the HRP family.' 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_volume            280 
_citation.page_first                116960 
_citation.page_last                 116960 
_citation.year                      2024 
_citation.pdbx_database_id_PubMed   39461037 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2024.116960 
_citation.journal_id_ASTM           EJMCA5 
_citation.country                   FR 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_id_CSD            0493 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Vantieghem, T.'   ? 1  
primary 'Aslam, N.A.'      ? 2  
primary 'Osipov, E.M.'     ? 3  
primary 'Akele, M.'        ? 4  
primary 'Van Belle, S.'    ? 5  
primary 'Beelen, S.'       ? 6  
primary 'Drexler, M.'      ? 7  
primary 'Paulovcakova, T.' ? 8  
primary 'Lux, V.'          ? 9  
primary 'Fearon, D.'       ? 10 
primary 'Douangamath, A.'  ? 11 
primary 'von Delft, F.'    ? 12 
primary 'Christ, F.'       ? 13 
primary 'Veverka, V.'      ? 14 
primary 'Verwilst, P.'     ? 15 
primary 'Van Aerschot, A.' ? 16 
primary 'Debyser, Z.'      ? 17 
primary 'Strelkov, S.V.'   ? 18 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Hepatoma-derived growth factor-related protein 2' 10698.171 3   ? C64S ? ? 
2 non-polymer syn 'SULFATE ION'                                      96.063    6   ? ?    ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    1   ? ?    ? ? 
4 non-polymer syn 'N-[(1S)-1-(pyridin-3-yl)ethyl]cyclopropanamine'   162.232   2   ? ?    ? ? 
5 water       nat water                                              18.015    282 ? ?    ? ? 
# 
_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-[(1S)-1-(pyridin-3-yl)ethyl]cyclopropanamine' A1A3U 
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 
A1A3U non-polymer         . 'N-[(1S)-1-(pyridin-3-yl)ethyl]cyclopropanamine' ?                 'C10 H14 N2'     162.232 
ALA   'L-peptide linking' y ALANINE                                          ?                 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                         ?                 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                       ?                 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                  ?                 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                         ?                 'C3 H7 N O2 S'   121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL                                   'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN   'L-peptide linking' y GLUTAMINE                                        ?                 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                  ?                 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                          ?                 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                        ?                 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                            ?                 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                       ?                 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                          ?                 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                           ?                 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                       ?                 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                    ?                 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                          ?                 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                           ?                 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION'                                    ?                 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                                        ?                 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                       ?                 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                         ?                 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                           ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1  GLY 1  0  ?  ?   ?   A . n 
A 1 2  MET 2  1  1  MET MET A . n 
A 1 3  PRO 3  2  2  PRO PRO A . n 
A 1 4  HIS 4  3  3  HIS HIS A . n 
A 1 5  ALA 5  4  4  ALA ALA A . n 
A 1 6  PHE 6  5  5  PHE PHE A . n 
A 1 7  LYS 7  6  6  LYS LYS A . n 
A 1 8  PRO 8  7  7  PRO PRO A . n 
A 1 9  GLY 9  8  8  GLY GLY A . n 
A 1 10 ASP 10 9  9  ASP ASP A . n 
A 1 11 LEU 11 10 10 LEU LEU A . n 
A 1 12 VAL 12 11 11 VAL VAL A . n 
A 1 13 PHE 13 12 12 PHE PHE A . n 
A 1 14 ALA 14 13 13 ALA ALA A . n 
A 1 15 LYS 15 14 14 LYS LYS A . n 
A 1 16 MET 16 15 15 MET MET A . n 
A 1 17 LYS 17 16 16 LYS LYS A . n 
A 1 18 GLY 18 17 17 GLY GLY A . n 
A 1 19 TYR 19 18 18 TYR TYR A . n 
A 1 20 PRO 20 19 19 PRO PRO A . n 
A 1 21 HIS 21 20 20 HIS HIS A . n 
A 1 22 TRP 22 21 21 TRP TRP A . n 
A 1 23 PRO 23 22 22 PRO PRO A . n 
A 1 24 ALA 24 23 23 ALA ALA A . n 
A 1 25 ARG 25 24 24 ARG ARG A . n 
A 1 26 ILE 26 25 25 ILE ILE A . n 
A 1 27 ASP 27 26 26 ASP ASP A . n 
A 1 28 ASP 28 27 27 ASP ASP A . n 
A 1 29 ILE 29 28 28 ILE ILE A . n 
A 1 30 ALA 30 29 29 ALA ALA A . n 
A 1 31 ASP 31 30 30 ASP ASP A . n 
A 1 32 GLY 32 31 31 GLY GLY A . n 
A 1 33 ALA 33 32 32 ALA ALA A . n 
A 1 34 VAL 34 33 33 VAL VAL A . n 
A 1 35 LYS 35 34 34 LYS LYS A . n 
A 1 36 PRO 36 35 35 PRO PRO A . n 
A 1 37 PRO 37 36 36 PRO PRO A . n 
A 1 38 PRO 38 37 37 PRO PRO A . n 
A 1 39 ASN 39 38 38 ASN ASN A . n 
A 1 40 LYS 40 39 39 LYS LYS A . n 
A 1 41 TYR 41 40 40 TYR TYR A . n 
A 1 42 PRO 42 41 41 PRO PRO A . n 
A 1 43 ILE 43 42 42 ILE ILE A . n 
A 1 44 PHE 44 43 43 PHE PHE A . n 
A 1 45 PHE 45 44 44 PHE PHE A . n 
A 1 46 PHE 46 45 45 PHE PHE A . n 
A 1 47 GLY 47 46 46 GLY GLY A . n 
A 1 48 THR 48 47 47 THR THR A . n 
A 1 49 HIS 49 48 48 HIS HIS A . n 
A 1 50 GLU 50 49 49 GLU GLU A . n 
A 1 51 THR 51 50 50 THR THR A . n 
A 1 52 ALA 52 51 51 ALA ALA A . n 
A 1 53 PHE 53 52 52 PHE PHE A . n 
A 1 54 LEU 54 53 53 LEU LEU A . n 
A 1 55 GLY 55 54 54 GLY GLY A . n 
A 1 56 PRO 56 55 55 PRO PRO A . n 
A 1 57 LYS 57 56 56 LYS LYS A . n 
A 1 58 ASP 58 57 57 ASP ASP A . n 
A 1 59 LEU 59 58 58 LEU LEU A . n 
A 1 60 PHE 60 59 59 PHE PHE A . n 
A 1 61 PRO 61 60 60 PRO PRO A . n 
A 1 62 TYR 62 61 61 TYR TYR A . n 
A 1 63 ASP 63 62 62 ASP ASP A . n 
A 1 64 LYS 64 63 63 LYS LYS A . n 
A 1 65 SER 65 64 64 SER SER A . n 
A 1 66 LYS 66 65 65 LYS LYS A . n 
A 1 67 ASP 67 66 66 ASP ASP A . n 
A 1 68 LYS 68 67 67 LYS LYS A . n 
A 1 69 TYR 69 68 68 TYR TYR A . n 
A 1 70 GLY 70 69 69 GLY GLY A . n 
A 1 71 LYS 71 70 70 LYS LYS A . n 
A 1 72 PRO 72 71 71 PRO PRO A . n 
A 1 73 ASN 73 72 72 ASN ASN A . n 
A 1 74 LYS 74 73 73 LYS LYS A . n 
A 1 75 ARG 75 74 74 ARG ARG A . n 
A 1 76 LYS 76 75 75 LYS LYS A . n 
A 1 77 GLY 77 76 76 GLY GLY A . n 
A 1 78 PHE 78 77 77 PHE PHE A . n 
A 1 79 ASN 79 78 78 ASN ASN A . n 
A 1 80 GLU 80 79 79 GLU GLU A . n 
A 1 81 GLY 81 80 80 GLY GLY A . n 
A 1 82 LEU 82 81 81 LEU LEU A . n 
A 1 83 TRP 83 82 82 TRP TRP A . n 
A 1 84 GLU 84 83 83 GLU GLU A . n 
A 1 85 ILE 85 84 84 ILE ILE A . n 
A 1 86 GLN 86 85 85 GLN GLN A . n 
A 1 87 ASN 87 86 86 ASN ASN A . n 
A 1 88 ASN 88 87 87 ASN ASN A . n 
A 1 89 PRO 89 88 88 PRO PRO A . n 
A 1 90 HIS 90 89 89 HIS HIS A . n 
A 1 91 ALA 91 90 90 ALA ALA A . n 
A 1 92 SER 92 91 91 SER SER A . n 
A 1 93 TYR 93 92 92 TYR TYR A . n 
A 1 94 SER 94 93 93 SER SER A . n 
B 1 1  GLY 1  0  ?  ?   ?   B . n 
B 1 2  MET 2  1  1  MET MET B . n 
B 1 3  PRO 3  2  2  PRO PRO B . n 
B 1 4  HIS 4  3  3  HIS HIS B . n 
B 1 5  ALA 5  4  4  ALA ALA B . n 
B 1 6  PHE 6  5  5  PHE PHE B . n 
B 1 7  LYS 7  6  6  LYS LYS B . n 
B 1 8  PRO 8  7  7  PRO PRO B . n 
B 1 9  GLY 9  8  8  GLY GLY B . n 
B 1 10 ASP 10 9  9  ASP ASP B . n 
B 1 11 LEU 11 10 10 LEU LEU B . n 
B 1 12 VAL 12 11 11 VAL VAL B . n 
B 1 13 PHE 13 12 12 PHE PHE B . n 
B 1 14 ALA 14 13 13 ALA ALA B . n 
B 1 15 LYS 15 14 14 LYS LYS B . n 
B 1 16 MET 16 15 15 MET MET B . n 
B 1 17 LYS 17 16 16 LYS LYS B . n 
B 1 18 GLY 18 17 17 GLY GLY B . n 
B 1 19 TYR 19 18 18 TYR TYR B . n 
B 1 20 PRO 20 19 19 PRO PRO B . n 
B 1 21 HIS 21 20 20 HIS HIS B . n 
B 1 22 TRP 22 21 21 TRP TRP B . n 
B 1 23 PRO 23 22 22 PRO PRO B . n 
B 1 24 ALA 24 23 23 ALA ALA B . n 
B 1 25 ARG 25 24 24 ARG ARG B . n 
B 1 26 ILE 26 25 25 ILE ILE B . n 
B 1 27 ASP 27 26 26 ASP ASP B . n 
B 1 28 ASP 28 27 27 ASP ASP B . n 
B 1 29 ILE 29 28 28 ILE ILE B . n 
B 1 30 ALA 30 29 ?  ?   ?   B . n 
B 1 31 ASP 31 30 ?  ?   ?   B . n 
B 1 32 GLY 32 31 ?  ?   ?   B . n 
B 1 33 ALA 33 32 ?  ?   ?   B . n 
B 1 34 VAL 34 33 33 VAL VAL B . n 
B 1 35 LYS 35 34 34 LYS LYS B . n 
B 1 36 PRO 36 35 35 PRO PRO B . n 
B 1 37 PRO 37 36 36 PRO PRO B . n 
B 1 38 PRO 38 37 37 PRO PRO B . n 
B 1 39 ASN 39 38 38 ASN ASN B . n 
B 1 40 LYS 40 39 39 LYS LYS B . n 
B 1 41 TYR 41 40 40 TYR TYR B . n 
B 1 42 PRO 42 41 41 PRO PRO B . n 
B 1 43 ILE 43 42 42 ILE ILE B . n 
B 1 44 PHE 44 43 43 PHE PHE B . n 
B 1 45 PHE 45 44 44 PHE PHE B . n 
B 1 46 PHE 46 45 45 PHE PHE B . n 
B 1 47 GLY 47 46 46 GLY GLY B . n 
B 1 48 THR 48 47 47 THR THR B . n 
B 1 49 HIS 49 48 48 HIS HIS B . n 
B 1 50 GLU 50 49 49 GLU GLU B . n 
B 1 51 THR 51 50 50 THR THR B . n 
B 1 52 ALA 52 51 51 ALA ALA B . n 
B 1 53 PHE 53 52 52 PHE PHE B . n 
B 1 54 LEU 54 53 53 LEU LEU B . n 
B 1 55 GLY 55 54 54 GLY GLY B . n 
B 1 56 PRO 56 55 55 PRO PRO B . n 
B 1 57 LYS 57 56 56 LYS LYS B . n 
B 1 58 ASP 58 57 57 ASP ASP B . n 
B 1 59 LEU 59 58 58 LEU LEU B . n 
B 1 60 PHE 60 59 59 PHE PHE B . n 
B 1 61 PRO 61 60 60 PRO PRO B . n 
B 1 62 TYR 62 61 61 TYR TYR B . n 
B 1 63 ASP 63 62 62 ASP ASP B . n 
B 1 64 LYS 64 63 63 LYS LYS B . n 
B 1 65 SER 65 64 64 SER SER B . n 
B 1 66 LYS 66 65 65 LYS LYS B . n 
B 1 67 ASP 67 66 66 ASP ASP B . n 
B 1 68 LYS 68 67 67 LYS LYS B . n 
B 1 69 TYR 69 68 68 TYR TYR B . n 
B 1 70 GLY 70 69 69 GLY GLY B . n 
B 1 71 LYS 71 70 70 LYS LYS B . n 
B 1 72 PRO 72 71 71 PRO PRO B . n 
B 1 73 ASN 73 72 72 ASN ASN B . n 
B 1 74 LYS 74 73 73 LYS LYS B . n 
B 1 75 ARG 75 74 74 ARG ARG B . n 
B 1 76 LYS 76 75 75 LYS LYS B . n 
B 1 77 GLY 77 76 76 GLY GLY B . n 
B 1 78 PHE 78 77 77 PHE PHE B . n 
B 1 79 ASN 79 78 78 ASN ASN B . n 
B 1 80 GLU 80 79 79 GLU GLU B . n 
B 1 81 GLY 81 80 80 GLY GLY B . n 
B 1 82 LEU 82 81 81 LEU LEU B . n 
B 1 83 TRP 83 82 82 TRP TRP B . n 
B 1 84 GLU 84 83 83 GLU GLU B . n 
B 1 85 ILE 85 84 84 ILE ILE B . n 
B 1 86 GLN 86 85 85 GLN GLN B . n 
B 1 87 ASN 87 86 86 ASN ASN B . n 
B 1 88 ASN 88 87 87 ASN ASN B . n 
B 1 89 PRO 89 88 88 PRO PRO B . n 
B 1 90 HIS 90 89 89 HIS HIS B . n 
B 1 91 ALA 91 90 90 ALA ALA B . n 
B 1 92 SER 92 91 91 SER SER B . n 
B 1 93 TYR 93 92 92 TYR TYR B . n 
B 1 94 SER 94 93 93 SER SER B . n 
C 1 1  GLY 1  0  ?  ?   ?   C . n 
C 1 2  MET 2  1  ?  ?   ?   C . n 
C 1 3  PRO 3  2  ?  ?   ?   C . n 
C 1 4  HIS 4  3  3  HIS HIS C . n 
C 1 5  ALA 5  4  4  ALA ALA C . n 
C 1 6  PHE 6  5  5  PHE PHE C . n 
C 1 7  LYS 7  6  6  LYS LYS C . n 
C 1 8  PRO 8  7  7  PRO PRO C . n 
C 1 9  GLY 9  8  8  GLY GLY C . n 
C 1 10 ASP 10 9  9  ASP ASP C . n 
C 1 11 LEU 11 10 10 LEU LEU C . n 
C 1 12 VAL 12 11 11 VAL VAL C . n 
C 1 13 PHE 13 12 12 PHE PHE C . n 
C 1 14 ALA 14 13 13 ALA ALA C . n 
C 1 15 LYS 15 14 14 LYS LYS C . n 
C 1 16 MET 16 15 15 MET MET C . n 
C 1 17 LYS 17 16 16 LYS LYS C . n 
C 1 18 GLY 18 17 17 GLY GLY C . n 
C 1 19 TYR 19 18 18 TYR TYR C . n 
C 1 20 PRO 20 19 19 PRO PRO C . n 
C 1 21 HIS 21 20 20 HIS HIS C . n 
C 1 22 TRP 22 21 21 TRP TRP C . n 
C 1 23 PRO 23 22 22 PRO PRO C . n 
C 1 24 ALA 24 23 23 ALA ALA C . n 
C 1 25 ARG 25 24 24 ARG ARG C . n 
C 1 26 ILE 26 25 25 ILE ILE C . n 
C 1 27 ASP 27 26 26 ASP ASP C . n 
C 1 28 ASP 28 27 27 ASP ASP C . n 
C 1 29 ILE 29 28 28 ILE ILE C . n 
C 1 30 ALA 30 29 29 ALA ALA C . n 
C 1 31 ASP 31 30 ?  ?   ?   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        A1A3U 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A3U 
_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 A1A3U 1   103 101 A1A3U LIG B . 
K 2 SO4   1   101 5   SO4   SO4 C . 
L 4 A1A3U 1   102 101 A1A3U LIG C . 
M 5 HOH   1   201 304 HOH   HOH A . 
M 5 HOH   2   202 341 HOH   HOH A . 
M 5 HOH   3   203 307 HOH   HOH A . 
M 5 HOH   4   204 202 HOH   HOH A . 
M 5 HOH   5   205 357 HOH   HOH A . 
M 5 HOH   6   206 71  HOH   HOH A . 
M 5 HOH   7   207 139 HOH   HOH A . 
M 5 HOH   8   208 66  HOH   HOH A . 
M 5 HOH   9   209 339 HOH   HOH A . 
M 5 HOH   10  210 84  HOH   HOH A . 
M 5 HOH   11  211 337 HOH   HOH A . 
M 5 HOH   12  212 353 HOH   HOH A . 
M 5 HOH   13  213 85  HOH   HOH A . 
M 5 HOH   14  214 91  HOH   HOH A . 
M 5 HOH   15  215 38  HOH   HOH A . 
M 5 HOH   16  216 188 HOH   HOH A . 
M 5 HOH   17  217 383 HOH   HOH A . 
M 5 HOH   18  218 55  HOH   HOH A . 
M 5 HOH   19  219 346 HOH   HOH A . 
M 5 HOH   20  220 78  HOH   HOH A . 
M 5 HOH   21  221 293 HOH   HOH A . 
M 5 HOH   22  222 87  HOH   HOH A . 
M 5 HOH   23  223 23  HOH   HOH A . 
M 5 HOH   24  224 97  HOH   HOH A . 
M 5 HOH   25  225 28  HOH   HOH A . 
M 5 HOH   26  226 356 HOH   HOH A . 
M 5 HOH   27  227 86  HOH   HOH A . 
M 5 HOH   28  228 167 HOH   HOH A . 
M 5 HOH   29  229 37  HOH   HOH A . 
M 5 HOH   30  230 8   HOH   HOH A . 
M 5 HOH   31  231 60  HOH   HOH A . 
M 5 HOH   32  232 289 HOH   HOH A . 
M 5 HOH   33  233 94  HOH   HOH A . 
M 5 HOH   34  234 299 HOH   HOH A . 
M 5 HOH   35  235 41  HOH   HOH A . 
M 5 HOH   36  236 42  HOH   HOH A . 
M 5 HOH   37  237 367 HOH   HOH A . 
M 5 HOH   38  238 199 HOH   HOH A . 
M 5 HOH   39  239 95  HOH   HOH A . 
M 5 HOH   40  240 288 HOH   HOH A . 
M 5 HOH   41  241 2   HOH   HOH A . 
M 5 HOH   42  242 274 HOH   HOH A . 
M 5 HOH   43  243 190 HOH   HOH A . 
M 5 HOH   44  244 32  HOH   HOH A . 
M 5 HOH   45  245 260 HOH   HOH A . 
M 5 HOH   46  246 99  HOH   HOH A . 
M 5 HOH   47  247 12  HOH   HOH A . 
M 5 HOH   48  248 7   HOH   HOH A . 
M 5 HOH   49  249 292 HOH   HOH A . 
M 5 HOH   50  250 1   HOH   HOH A . 
M 5 HOH   51  251 179 HOH   HOH A . 
M 5 HOH   52  252 26  HOH   HOH A . 
M 5 HOH   53  253 165 HOH   HOH A . 
M 5 HOH   54  254 152 HOH   HOH A . 
M 5 HOH   55  255 27  HOH   HOH A . 
M 5 HOH   56  256 318 HOH   HOH A . 
M 5 HOH   57  257 145 HOH   HOH A . 
M 5 HOH   58  258 116 HOH   HOH A . 
M 5 HOH   59  259 20  HOH   HOH A . 
M 5 HOH   60  260 222 HOH   HOH A . 
M 5 HOH   61  261 203 HOH   HOH A . 
M 5 HOH   62  262 301 HOH   HOH A . 
M 5 HOH   63  263 211 HOH   HOH A . 
M 5 HOH   64  264 111 HOH   HOH A . 
M 5 HOH   65  265 267 HOH   HOH A . 
M 5 HOH   66  266 218 HOH   HOH A . 
M 5 HOH   67  267 77  HOH   HOH A . 
M 5 HOH   68  268 290 HOH   HOH A . 
M 5 HOH   69  269 350 HOH   HOH A . 
M 5 HOH   70  270 109 HOH   HOH A . 
M 5 HOH   71  271 93  HOH   HOH A . 
M 5 HOH   72  272 34  HOH   HOH A . 
M 5 HOH   73  273 18  HOH   HOH A . 
M 5 HOH   74  274 343 HOH   HOH A . 
M 5 HOH   75  275 300 HOH   HOH A . 
M 5 HOH   76  276 371 HOH   HOH A . 
M 5 HOH   77  277 164 HOH   HOH A . 
M 5 HOH   78  278 287 HOH   HOH A . 
M 5 HOH   79  279 14  HOH   HOH A . 
M 5 HOH   80  280 64  HOH   HOH A . 
M 5 HOH   81  281 143 HOH   HOH A . 
M 5 HOH   82  282 385 HOH   HOH A . 
M 5 HOH   83  283 21  HOH   HOH A . 
M 5 HOH   84  284 115 HOH   HOH A . 
M 5 HOH   85  285 47  HOH   HOH A . 
M 5 HOH   86  286 58  HOH   HOH A . 
M 5 HOH   87  287 35  HOH   HOH A . 
M 5 HOH   88  288 259 HOH   HOH A . 
M 5 HOH   89  289 22  HOH   HOH A . 
M 5 HOH   90  290 9   HOH   HOH A . 
M 5 HOH   91  291 19  HOH   HOH A . 
M 5 HOH   92  292 376 HOH   HOH A . 
M 5 HOH   93  293 281 HOH   HOH A . 
M 5 HOH   94  294 16  HOH   HOH A . 
M 5 HOH   95  295 113 HOH   HOH A . 
M 5 HOH   96  296 358 HOH   HOH A . 
M 5 HOH   97  297 278 HOH   HOH A . 
M 5 HOH   98  298 31  HOH   HOH A . 
M 5 HOH   99  299 75  HOH   HOH A . 
M 5 HOH   100 300 208 HOH   HOH A . 
M 5 HOH   101 301 377 HOH   HOH A . 
M 5 HOH   102 302 131 HOH   HOH A . 
M 5 HOH   103 303 366 HOH   HOH A . 
M 5 HOH   104 304 73  HOH   HOH A . 
M 5 HOH   105 305 327 HOH   HOH A . 
M 5 HOH   106 306 83  HOH   HOH A . 
M 5 HOH   107 307 156 HOH   HOH A . 
M 5 HOH   108 308 210 HOH   HOH A . 
M 5 HOH   109 309 108 HOH   HOH A . 
M 5 HOH   110 310 219 HOH   HOH A . 
M 5 HOH   111 311 283 HOH   HOH A . 
M 5 HOH   112 312 185 HOH   HOH A . 
M 5 HOH   113 313 205 HOH   HOH A . 
M 5 HOH   114 314 57  HOH   HOH A . 
M 5 HOH   115 315 206 HOH   HOH A . 
M 5 HOH   116 316 313 HOH   HOH A . 
M 5 HOH   117 317 125 HOH   HOH A . 
M 5 HOH   118 318 332 HOH   HOH A . 
M 5 HOH   119 319 364 HOH   HOH A . 
N 5 HOH   1   201 247 HOH   HOH B . 
N 5 HOH   2   202 258 HOH   HOH B . 
N 5 HOH   3   203 123 HOH   HOH B . 
N 5 HOH   4   204 338 HOH   HOH B . 
N 5 HOH   5   205 98  HOH   HOH B . 
N 5 HOH   6   206 272 HOH   HOH B . 
N 5 HOH   7   207 89  HOH   HOH B . 
N 5 HOH   8   208 184 HOH   HOH B . 
N 5 HOH   9   209 69  HOH   HOH B . 
N 5 HOH   10  210 249 HOH   HOH B . 
N 5 HOH   11  211 279 HOH   HOH B . 
N 5 HOH   12  212 331 HOH   HOH B . 
N 5 HOH   13  213 215 HOH   HOH B . 
N 5 HOH   14  214 46  HOH   HOH B . 
N 5 HOH   15  215 117 HOH   HOH B . 
N 5 HOH   16  216 25  HOH   HOH B . 
N 5 HOH   17  217 10  HOH   HOH B . 
N 5 HOH   18  218 119 HOH   HOH B . 
N 5 HOH   19  219 375 HOH   HOH B . 
N 5 HOH   20  220 242 HOH   HOH B . 
N 5 HOH   21  221 54  HOH   HOH B . 
N 5 HOH   22  222 17  HOH   HOH B . 
N 5 HOH   23  223 5   HOH   HOH B . 
N 5 HOH   24  224 360 HOH   HOH B . 
N 5 HOH   25  225 137 HOH   HOH B . 
N 5 HOH   26  226 172 HOH   HOH B . 
N 5 HOH   27  227 223 HOH   HOH B . 
N 5 HOH   28  228 6   HOH   HOH B . 
N 5 HOH   29  229 329 HOH   HOH B . 
N 5 HOH   30  230 68  HOH   HOH B . 
N 5 HOH   31  231 354 HOH   HOH B . 
N 5 HOH   32  232 96  HOH   HOH B . 
N 5 HOH   33  233 224 HOH   HOH B . 
N 5 HOH   34  234 24  HOH   HOH B . 
N 5 HOH   35  235 150 HOH   HOH B . 
N 5 HOH   36  236 169 HOH   HOH B . 
N 5 HOH   37  237 280 HOH   HOH B . 
N 5 HOH   38  238 120 HOH   HOH B . 
N 5 HOH   39  239 101 HOH   HOH B . 
N 5 HOH   40  240 261 HOH   HOH B . 
N 5 HOH   41  241 61  HOH   HOH B . 
N 5 HOH   42  242 355 HOH   HOH B . 
N 5 HOH   43  243 168 HOH   HOH B . 
N 5 HOH   44  244 44  HOH   HOH B . 
N 5 HOH   45  245 197 HOH   HOH B . 
N 5 HOH   46  246 315 HOH   HOH B . 
N 5 HOH   47  247 76  HOH   HOH B . 
N 5 HOH   48  248 36  HOH   HOH B . 
N 5 HOH   49  249 74  HOH   HOH B . 
N 5 HOH   50  250 59  HOH   HOH B . 
N 5 HOH   51  251 182 HOH   HOH B . 
N 5 HOH   52  252 214 HOH   HOH B . 
N 5 HOH   53  253 160 HOH   HOH B . 
N 5 HOH   54  254 13  HOH   HOH B . 
N 5 HOH   55  255 320 HOH   HOH B . 
N 5 HOH   56  256 359 HOH   HOH B . 
N 5 HOH   57  257 79  HOH   HOH B . 
N 5 HOH   58  258 175 HOH   HOH B . 
N 5 HOH   59  259 72  HOH   HOH B . 
N 5 HOH   60  260 157 HOH   HOH B . 
N 5 HOH   61  261 217 HOH   HOH B . 
N 5 HOH   62  262 104 HOH   HOH B . 
N 5 HOH   63  263 303 HOH   HOH B . 
N 5 HOH   64  264 340 HOH   HOH B . 
N 5 HOH   65  265 322 HOH   HOH B . 
N 5 HOH   66  266 177 HOH   HOH B . 
N 5 HOH   67  267 153 HOH   HOH B . 
N 5 HOH   68  268 347 HOH   HOH B . 
N 5 HOH   69  269 201 HOH   HOH B . 
N 5 HOH   70  270 316 HOH   HOH B . 
N 5 HOH   71  271 163 HOH   HOH B . 
N 5 HOH   72  272 342 HOH   HOH B . 
N 5 HOH   73  273 361 HOH   HOH B . 
N 5 HOH   74  274 291 HOH   HOH B . 
N 5 HOH   75  275 335 HOH   HOH B . 
N 5 HOH   76  276 378 HOH   HOH B . 
N 5 HOH   77  277 170 HOH   HOH B . 
N 5 HOH   78  278 344 HOH   HOH B . 
N 5 HOH   79  279 314 HOH   HOH B . 
N 5 HOH   80  280 107 HOH   HOH B . 
N 5 HOH   81  281 312 HOH   HOH B . 
O 5 HOH   1   201 323 HOH   HOH C . 
O 5 HOH   2   202 321 HOH   HOH C . 
O 5 HOH   3   203 317 HOH   HOH C . 
O 5 HOH   4   204 330 HOH   HOH C . 
O 5 HOH   5   205 382 HOH   HOH C . 
O 5 HOH   6   206 173 HOH   HOH C . 
O 5 HOH   7   207 254 HOH   HOH C . 
O 5 HOH   8   208 226 HOH   HOH C . 
O 5 HOH   9   209 352 HOH   HOH C . 
O 5 HOH   10  210 49  HOH   HOH C . 
O 5 HOH   11  211 334 HOH   HOH C . 
O 5 HOH   12  212 296 HOH   HOH C . 
O 5 HOH   13  213 384 HOH   HOH C . 
O 5 HOH   14  214 90  HOH   HOH C . 
O 5 HOH   15  215 102 HOH   HOH C . 
O 5 HOH   16  216 118 HOH   HOH C . 
O 5 HOH   17  217 269 HOH   HOH C . 
O 5 HOH   18  218 45  HOH   HOH C . 
O 5 HOH   19  219 15  HOH   HOH C . 
O 5 HOH   20  220 284 HOH   HOH C . 
O 5 HOH   21  221 161 HOH   HOH C . 
O 5 HOH   22  222 363 HOH   HOH C . 
O 5 HOH   23  223 271 HOH   HOH C . 
O 5 HOH   24  224 295 HOH   HOH C . 
O 5 HOH   25  225 142 HOH   HOH C . 
O 5 HOH   26  226 4   HOH   HOH C . 
O 5 HOH   27  227 209 HOH   HOH C . 
O 5 HOH   28  228 336 HOH   HOH C . 
O 5 HOH   29  229 149 HOH   HOH C . 
O 5 HOH   30  230 126 HOH   HOH C . 
O 5 HOH   31  231 275 HOH   HOH C . 
O 5 HOH   32  232 40  HOH   HOH C . 
O 5 HOH   33  233 368 HOH   HOH C . 
O 5 HOH   34  234 48  HOH   HOH C . 
O 5 HOH   35  235 134 HOH   HOH C . 
O 5 HOH   36  236 122 HOH   HOH C . 
O 5 HOH   37  237 56  HOH   HOH C . 
O 5 HOH   38  238 43  HOH   HOH C . 
O 5 HOH   39  239 294 HOH   HOH C . 
O 5 HOH   40  240 53  HOH   HOH C . 
O 5 HOH   41  241 189 HOH   HOH C . 
O 5 HOH   42  242 379 HOH   HOH C . 
O 5 HOH   43  243 148 HOH   HOH C . 
O 5 HOH   44  244 82  HOH   HOH C . 
O 5 HOH   45  245 151 HOH   HOH C . 
O 5 HOH   46  246 171 HOH   HOH C . 
O 5 HOH   47  247 309 HOH   HOH C . 
O 5 HOH   48  248 67  HOH   HOH C . 
O 5 HOH   49  249 298 HOH   HOH C . 
O 5 HOH   50  250 62  HOH   HOH C . 
O 5 HOH   51  251 362 HOH   HOH C . 
O 5 HOH   52  252 135 HOH   HOH C . 
O 5 HOH   53  253 305 HOH   HOH C . 
O 5 HOH   54  254 372 HOH   HOH C . 
O 5 HOH   55  255 302 HOH   HOH C . 
O 5 HOH   56  256 198 HOH   HOH C . 
O 5 HOH   57  257 132 HOH   HOH C . 
O 5 HOH   58  258 65  HOH   HOH C . 
O 5 HOH   59  259 130 HOH   HOH C . 
O 5 HOH   60  260 328 HOH   HOH C . 
O 5 HOH   61  261 373 HOH   HOH C . 
O 5 HOH   62  262 146 HOH   HOH C . 
O 5 HOH   63  263 369 HOH   HOH C . 
O 5 HOH   64  264 381 HOH   HOH C . 
O 5 HOH   65  265 319 HOH   HOH C . 
O 5 HOH   66  266 324 HOH   HOH C . 
O 5 HOH   67  267 246 HOH   HOH C . 
O 5 HOH   68  268 241 HOH   HOH C . 
O 5 HOH   69  269 270 HOH   HOH C . 
O 5 HOH   70  270 310 HOH   HOH C . 
O 5 HOH   71  271 70  HOH   HOH C . 
O 5 HOH   72  272 345 HOH   HOH C . 
O 5 HOH   73  273 63  HOH   HOH C . 
O 5 HOH   74  274 349 HOH   HOH C . 
O 5 HOH   75  275 374 HOH   HOH C . 
O 5 HOH   76  276 103 HOH   HOH C . 
O 5 HOH   77  277 348 HOH   HOH C . 
O 5 HOH   78  278 92  HOH   HOH C . 
O 5 HOH   79  279 370 HOH   HOH C . 
O 5 HOH   80  280 380 HOH   HOH C . 
O 5 HOH   81  281 365 HOH   HOH C . 
O 5 HOH   82  282 351 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 ILE 28 ? CG1 ? B ILE 29 CG1 
10 1 Y 1 B ILE 28 ? CG2 ? B ILE 29 CG2 
11 1 Y 1 B ILE 28 ? CD1 ? B ILE 29 CD1 
12 1 Y 1 B LYS 34 ? CG  ? B LYS 35 CG  
13 1 Y 1 B LYS 34 ? CD  ? B LYS 35 CD  
14 1 Y 1 B LYS 34 ? CE  ? B LYS 35 CE  
15 1 Y 1 B LYS 34 ? NZ  ? B LYS 35 NZ  
16 1 Y 1 B LYS 73 ? CG  ? B LYS 74 CG  
17 1 Y 1 B LYS 73 ? CD  ? B LYS 74 CD  
18 1 Y 1 B LYS 73 ? CE  ? B LYS 74 CE  
19 1 Y 1 B LYS 73 ? NZ  ? B LYS 74 NZ  
20 1 Y 1 B GLU 79 ? CD  ? B GLU 80 CD  
21 1 Y 1 B GLU 79 ? OE1 ? B GLU 80 OE1 
22 1 Y 1 B GLU 79 ? OE2 ? B GLU 80 OE2 
23 1 Y 1 B GLN 85 ? CG  ? B GLN 86 CG  
24 1 Y 1 B GLN 85 ? CD  ? B GLN 86 CD  
25 1 Y 1 B GLN 85 ? OE1 ? B GLN 86 OE1 
26 1 Y 1 B GLN 85 ? NE2 ? B GLN 86 NE2 
27 1 Y 1 C LYS 6  ? CG  ? C LYS 7  CG  
28 1 Y 1 C LYS 6  ? CD  ? C LYS 7  CD  
29 1 Y 1 C LYS 6  ? CE  ? C LYS 7  CE  
30 1 Y 1 C LYS 6  ? NZ  ? C LYS 7  NZ  
31 1 Y 1 C ILE 28 ? CG1 ? C ILE 29 CG1 
32 1 Y 1 C ILE 28 ? CG2 ? C ILE 29 CG2 
33 1 Y 1 C ILE 28 ? CD1 ? C ILE 29 CD1 
34 1 Y 1 C LYS 34 ? CG  ? C LYS 35 CG  
35 1 Y 1 C LYS 34 ? CD  ? C LYS 35 CD  
36 1 Y 1 C LYS 34 ? CE  ? C LYS 35 CE  
37 1 Y 1 C LYS 34 ? NZ  ? C LYS 35 NZ  
38 1 Y 1 C LYS 56 ? CG  ? C LYS 57 CG  
39 1 Y 1 C LYS 56 ? CD  ? C LYS 57 CD  
40 1 Y 1 C LYS 56 ? CE  ? C LYS 57 CE  
41 1 Y 1 C LYS 56 ? NZ  ? C LYS 57 NZ  
42 1 Y 1 C LYS 63 ? CG  ? C LYS 64 CG  
43 1 Y 1 C LYS 63 ? CD  ? C LYS 64 CD  
44 1 Y 1 C LYS 63 ? CE  ? C LYS 64 CE  
45 1 Y 1 C LYS 63 ? NZ  ? C LYS 64 NZ  
46 1 Y 1 C LYS 70 ? NZ  ? C LYS 71 NZ  
47 1 Y 1 C LYS 73 ? CD  ? C LYS 74 CD  
48 1 Y 1 C LYS 73 ? CE  ? C LYS 74 CE  
49 1 Y 1 C LYS 73 ? NZ  ? C LYS 74 NZ  
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0425 ? 1 
'data scaling'   Aimless .        ? 2 
'data reduction' xia2    .        ? 3 
phasing          REFMAC  .        ? 4 
# 
_cell.entry_id           7HHB 
_cell.length_a           41.660 
_cell.length_b           42.070 
_cell.length_c           158.390 
_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                         7HHB 
_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          7HHB 
_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                     7HHB 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             41.66 
_reflns.d_resolution_high            1.78 
_reflns.number_obs                   27646 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.106 
_reflns.pdbx_netI_over_sigmaI        9.6 
_reflns.pdbx_redundancy              6.4 
_reflns.pdbx_Rrim_I_all              0.116 
_reflns.pdbx_Rpim_I_all              0.045 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     177840 
_reflns.pdbx_chi_squared             0.98 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.78 
_reflns_shell.d_res_low                   1.83 
_reflns_shell.number_measured_all         13574 
_reflns_shell.number_unique_obs           2017 
_reflns_shell.Rmerge_I_obs                2.648 
_reflns_shell.pdbx_chi_squared            0.89 
_reflns_shell.pdbx_redundancy             6.7 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.7 
_reflns_shell.pdbx_Rrim_I_all             2.867 
_reflns_shell.pdbx_Rpim_I_all             1.090 
_reflns_shell.pdbx_CC_half                0.350 
_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                                 7HHB 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     26161 
_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                             40.69 
_refine.ls_d_res_high                            1.78 
_refine.ls_percent_reflns_obs                    99.87 
_refine.ls_R_factor_obs                          0.19737 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.19427 
_refine.ls_R_factor_R_free                       0.25320 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1419 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.948 
_refine.B_iso_mean                               39.824 
_refine.aniso_B[1][1]                            0.52 
_refine.aniso_B[2][2]                            -0.05 
_refine.aniso_B[3][3]                            -0.48 
_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                       0.138 
_refine.pdbx_overall_ESU_R_Free                  0.142 
_refine.overall_SU_ML                            0.131 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             4.548 
_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        2150 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         58 
_refine_hist.number_atoms_solvent             282 
_refine_hist.number_atoms_total               2490 
_refine_hist.d_res_high                       1.78 
_refine_hist.d_res_low                        40.69 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.007  0.012  ? 2305 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.619  1.828  ? 3134 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.974  5.000  ? 265  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       6.365  5.000  ? 6    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.885 10.000 ? 310  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.120  0.200  ? 290  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 1920 '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                  3.517  3.713  ? 1072 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.869  6.624  ? 1335 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  4.379  4.033  ? 1233 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       9.883  56.85  ? 3620 '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                       1.780 
_refine_ls_shell.d_res_low                        1.826 
_refine_ls_shell.number_reflns_R_work             1908 
_refine_ls_shell.R_factor_R_work                  0.344 
_refine_ls_shell.percent_reflns_obs               99.75 
_refine_ls_shell.R_factor_R_free                  0.368 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             96 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7HHB 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of HRP-2 PWWP domain in complex with Z1263529721' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HHB 
_struct_keywords.pdbx_keywords   'GENE REGULATION' 
_struct_keywords.text            
'Inhibitor, Fragment screening, Epigenetic reader, methyllysine, PWWP, Diamond Light Source, I04-1, PanDDA, XChem, GENE REGULATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 4 ? 
K N N 2 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    HDGR2_HUMAN 
_struct_ref.pdbx_db_accession          Q7Z4V5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHAFKPGDLVFAKMKGYPHWPARIDDIADGAVKPPPNKYPIFFFGTHETAFLGPKDLFPYDKCKDKYGKPNKRKGFNEG
LWEIQNNPHASYS
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HHB A 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
2 1 7HHB B 2 ? 94 ? Q7Z4V5 1 ? 93 ? 1 93 
3 1 7HHB 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 7HHB GLY A 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  1 
1 7HHB SER A 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 2 
2 7HHB GLY B 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  3 
2 7HHB SER B 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 4 
3 7HHB GLY C 1  ? UNP Q7Z4V5 ?   ?  'expression tag'      0  5 
3 7HHB SER C 65 ? UNP Q7Z4V5 CYS 64 'engineered mutation' 64 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,G,M 
2 1 B,H,I,J,N   
3 1 C,K,L,O     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 55 ? LYS A 57 ? GLY A 54 LYS A 56 5 ? 3  
HELX_P HELX_P2 AA2 TYR A 62 ? GLY A 70 ? TYR A 61 GLY A 69 1 ? 9  
HELX_P HELX_P3 AA3 GLY A 77 ? ASN A 88 ? GLY A 76 ASN A 87 1 ? 12 
HELX_P HELX_P4 AA4 GLY B 55 ? LYS B 57 ? GLY B 54 LYS B 56 5 ? 3  
HELX_P HELX_P5 AA5 TYR B 62 ? GLY B 70 ? TYR B 61 GLY B 69 1 ? 9  
HELX_P HELX_P6 AA6 GLY B 77 ? ASN B 88 ? GLY B 76 ASN B 87 1 ? 12 
HELX_P HELX_P7 AA7 GLY C 55 ? LYS C 57 ? GLY C 54 LYS C 56 5 ? 3  
HELX_P HELX_P8 AA8 TYR C 62 ? GLY C 70 ? TYR C 61 GLY C 69 1 ? 9  
HELX_P HELX_P9 AA9 GLY C 77 ? ASN C 88 ? GLY C 76 ASN C 87 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 5 ? 
AA3 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 THR A 51 ? LEU A 54 ? THR A 50 LEU A 53 
AA1 2 TYR A 41 ? PHE A 45 ? TYR A 40 PHE A 44 
AA1 3 TRP A 22 ? ILE A 26 ? TRP A 21 ILE A 25 
AA1 4 LEU A 11 ? ALA A 14 ? LEU A 10 ALA A 13 
AA1 5 LEU A 59 ? PRO A 61 ? LEU A 58 PRO A 60 
AA2 1 THR B 51 ? LEU B 54 ? THR B 50 LEU B 53 
AA2 2 TYR B 41 ? PHE B 45 ? TYR B 40 PHE B 44 
AA2 3 TRP B 22 ? ILE B 26 ? TRP B 21 ILE B 25 
AA2 4 LEU B 11 ? ALA B 14 ? LEU B 10 ALA B 13 
AA2 5 LEU B 59 ? PRO B 61 ? LEU B 58 PRO B 60 
AA3 1 THR C 51 ? LEU C 54 ? THR C 50 LEU C 53 
AA3 2 TYR C 41 ? PHE C 45 ? TYR C 40 PHE C 44 
AA3 3 TRP C 22 ? ILE C 26 ? TRP C 21 ILE C 25 
AA3 4 LEU C 11 ? ALA C 14 ? LEU C 10 ALA C 13 
AA3 5 LEU C 59 ? PRO C 61 ? LEU C 58 PRO C 60 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 52 ? O ALA A 51 N ILE A 43 ? N ILE A 42 
AA1 2 3 O PHE A 44 ? O PHE A 43 N ARG A 25 ? N ARG A 24 
AA1 3 4 O TRP A 22 ? O TRP A 21 N ALA A 14 ? N ALA A 13 
AA1 4 5 N PHE A 13 ? N PHE A 12 O PHE A 60 ? O PHE A 59 
AA2 1 2 O ALA B 52 ? O ALA B 51 N ILE B 43 ? N ILE B 42 
AA2 2 3 O PHE B 44 ? O PHE B 43 N ARG B 25 ? N ARG B 24 
AA2 3 4 O 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 TRP C 22 ? O TRP C 21 N ALA C 14 ? N ALA C 13 
AA3 4 5 N PHE C 13 ? N PHE C 12 O PHE C 60 ? O PHE C 59 
# 
_pdbx_entry_details.entry_id                   7HHB 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 234 ? ? O C HOH 211 ? ? 1.47 
2  1 O   B HOH 237 ? ? O B HOH 265 ? ? 1.69 
3  1 O   A HOH 237 ? ? O A HOH 295 ? ? 1.87 
4  1 OH  A TYR 18  ? ? O A HOH 201 ? ? 1.95 
5  1 O   C HOH 262 ? ? O C HOH 266 ? ? 1.97 
6  1 OD1 A ASP 27  ? ? O A HOH 202 ? ? 1.98 
7  1 O   A HOH 236 ? ? O A HOH 303 ? ? 2.04 
8  1 O   A HOH 205 ? ? O A HOH 305 ? ? 2.05 
9  1 O   C HOH 239 ? ? O C HOH 265 ? ? 2.06 
10 1 O2  A SO4 104 ? ? O A HOH 203 ? ? 2.13 
11 1 O   A ARG 74  ? ? O A HOH 204 ? ? 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 A HOH 249 ? ? 1_555 O A HOH 260 ? ? 4_545 2.02 
2 1 O A HOH 255 ? ? 1_555 O C HOH 274 ? ? 4_445 2.06 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_1              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             SD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_2              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_3              15 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                110.70 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            10.50 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 87 ? ? -154.32 64.97   
2 1 ASN B 87 ? ? -155.78 59.45   
3 1 ALA C 4  ? ? -162.45 114.62  
4 1 ASN C 87 ? ? -158.78 51.35   
5 1 ALA C 90 ? ? -80.15  -156.68 
6 1 SER C 91 ? ? -106.60 -90.23  
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    C 
_pdbx_validate_planes.auth_seq_id     74 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.087 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 318 ? 5.95 . 
2 1 O ? A HOH 319 ? 7.33 . 
3 1 O ? C HOH 282 ? 7.14 . 
# 
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 30 ? C ASP 31 
11 1 Y 1 C GLY 31 ? C GLY 32 
12 1 Y 1 C ALA 32 ? C ALA 33 
13 1 Y 1 C VAL 33 ? C VAL 34 
14 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 
A1A3U N1   N Y N 1   
A1A3U C4   C N N 2   
A1A3U C5   C Y N 3   
A1A3U C6   C Y N 4   
A1A3U C7   C Y N 5   
A1A3U C8   C Y N 6   
A1A3U C    C N N 7   
A1A3U C1   C N S 8   
A1A3U N    N N N 9   
A1A3U C2   C N N 10  
A1A3U C3   C N N 11  
A1A3U C9   C Y N 12  
A1A3U H9   H N N 13  
A1A3U H8   H N N 14  
A1A3U H10  H N N 15  
A1A3U H11  H N N 16  
A1A3U H12  H N N 17  
A1A3U H    H N N 18  
A1A3U H2   H N N 19  
A1A3U H1   H N N 20  
A1A3U H3   H N N 21  
A1A3U H4   H N N 22  
A1A3U H5   H N N 23  
A1A3U H7   H N N 24  
A1A3U H6   H N N 25  
A1A3U H13  H N N 26  
ALA   N    N N N 27  
ALA   CA   C N S 28  
ALA   C    C N N 29  
ALA   O    O N N 30  
ALA   CB   C N N 31  
ALA   OXT  O N N 32  
ALA   H    H N N 33  
ALA   H2   H N N 34  
ALA   HA   H N N 35  
ALA   HB1  H N N 36  
ALA   HB2  H N N 37  
ALA   HB3  H N N 38  
ALA   HXT  H N N 39  
ARG   N    N N N 40  
ARG   CA   C N S 41  
ARG   C    C N N 42  
ARG   O    O N N 43  
ARG   CB   C N N 44  
ARG   CG   C N N 45  
ARG   CD   C N N 46  
ARG   NE   N N N 47  
ARG   CZ   C N N 48  
ARG   NH1  N N N 49  
ARG   NH2  N N N 50  
ARG   OXT  O N N 51  
ARG   H    H N N 52  
ARG   H2   H N N 53  
ARG   HA   H N N 54  
ARG   HB2  H N N 55  
ARG   HB3  H N N 56  
ARG   HG2  H N N 57  
ARG   HG3  H N N 58  
ARG   HD2  H N N 59  
ARG   HD3  H N N 60  
ARG   HE   H N N 61  
ARG   HH11 H N N 62  
ARG   HH12 H N N 63  
ARG   HH21 H N N 64  
ARG   HH22 H N N 65  
ARG   HXT  H N N 66  
ASN   N    N N N 67  
ASN   CA   C N S 68  
ASN   C    C N N 69  
ASN   O    O N N 70  
ASN   CB   C N N 71  
ASN   CG   C N N 72  
ASN   OD1  O N N 73  
ASN   ND2  N N N 74  
ASN   OXT  O N N 75  
ASN   H    H N N 76  
ASN   H2   H N N 77  
ASN   HA   H N N 78  
ASN   HB2  H N N 79  
ASN   HB3  H N N 80  
ASN   HD21 H N N 81  
ASN   HD22 H N N 82  
ASN   HXT  H N N 83  
ASP   N    N N N 84  
ASP   CA   C N S 85  
ASP   C    C N N 86  
ASP   O    O N N 87  
ASP   CB   C N N 88  
ASP   CG   C N N 89  
ASP   OD1  O N N 90  
ASP   OD2  O N N 91  
ASP   OXT  O N N 92  
ASP   H    H N N 93  
ASP   H2   H N N 94  
ASP   HA   H N N 95  
ASP   HB2  H N N 96  
ASP   HB3  H N N 97  
ASP   HD2  H N N 98  
ASP   HXT  H N N 99  
CYS   N    N N N 100 
CYS   CA   C N R 101 
CYS   C    C N N 102 
CYS   O    O N N 103 
CYS   CB   C N N 104 
CYS   SG   S N N 105 
CYS   OXT  O N N 106 
CYS   H    H N N 107 
CYS   H2   H N N 108 
CYS   HA   H N N 109 
CYS   HB2  H N N 110 
CYS   HB3  H N N 111 
CYS   HG   H N N 112 
CYS   HXT  H N N 113 
EDO   C1   C N N 114 
EDO   O1   O N N 115 
EDO   C2   C N N 116 
EDO   O2   O N N 117 
EDO   H11  H N N 118 
EDO   H12  H N N 119 
EDO   HO1  H N N 120 
EDO   H21  H N N 121 
EDO   H22  H N N 122 
EDO   HO2  H N N 123 
GLN   N    N N N 124 
GLN   CA   C N S 125 
GLN   C    C N N 126 
GLN   O    O N N 127 
GLN   CB   C N N 128 
GLN   CG   C N N 129 
GLN   CD   C N N 130 
GLN   OE1  O N N 131 
GLN   NE2  N N N 132 
GLN   OXT  O N N 133 
GLN   H    H N N 134 
GLN   H2   H N N 135 
GLN   HA   H N N 136 
GLN   HB2  H N N 137 
GLN   HB3  H N N 138 
GLN   HG2  H N N 139 
GLN   HG3  H N N 140 
GLN   HE21 H N N 141 
GLN   HE22 H N N 142 
GLN   HXT  H N N 143 
GLU   N    N N N 144 
GLU   CA   C N S 145 
GLU   C    C N N 146 
GLU   O    O N N 147 
GLU   CB   C N N 148 
GLU   CG   C N N 149 
GLU   CD   C N N 150 
GLU   OE1  O N N 151 
GLU   OE2  O N N 152 
GLU   OXT  O N N 153 
GLU   H    H N N 154 
GLU   H2   H N N 155 
GLU   HA   H N N 156 
GLU   HB2  H N N 157 
GLU   HB3  H N N 158 
GLU   HG2  H N N 159 
GLU   HG3  H N N 160 
GLU   HE2  H N N 161 
GLU   HXT  H N N 162 
GLY   N    N N N 163 
GLY   CA   C N N 164 
GLY   C    C N N 165 
GLY   O    O N N 166 
GLY   OXT  O N N 167 
GLY   H    H N N 168 
GLY   H2   H N N 169 
GLY   HA2  H N N 170 
GLY   HA3  H N N 171 
GLY   HXT  H N N 172 
HIS   N    N N N 173 
HIS   CA   C N S 174 
HIS   C    C N N 175 
HIS   O    O N N 176 
HIS   CB   C N N 177 
HIS   CG   C Y N 178 
HIS   ND1  N Y N 179 
HIS   CD2  C Y N 180 
HIS   CE1  C Y N 181 
HIS   NE2  N Y N 182 
HIS   OXT  O N N 183 
HIS   H    H N N 184 
HIS   H2   H N N 185 
HIS   HA   H N N 186 
HIS   HB2  H N N 187 
HIS   HB3  H N N 188 
HIS   HD1  H N N 189 
HIS   HD2  H N N 190 
HIS   HE1  H N N 191 
HIS   HE2  H N N 192 
HIS   HXT  H N N 193 
HOH   O    O N N 194 
HOH   H1   H N N 195 
HOH   H2   H N N 196 
ILE   N    N N N 197 
ILE   CA   C N S 198 
ILE   C    C N N 199 
ILE   O    O N N 200 
ILE   CB   C N S 201 
ILE   CG1  C N N 202 
ILE   CG2  C N N 203 
ILE   CD1  C N N 204 
ILE   OXT  O N N 205 
ILE   H    H N N 206 
ILE   H2   H N N 207 
ILE   HA   H N N 208 
ILE   HB   H N N 209 
ILE   HG12 H N N 210 
ILE   HG13 H N N 211 
ILE   HG21 H N N 212 
ILE   HG22 H N N 213 
ILE   HG23 H N N 214 
ILE   HD11 H N N 215 
ILE   HD12 H N N 216 
ILE   HD13 H N N 217 
ILE   HXT  H N N 218 
LEU   N    N N N 219 
LEU   CA   C N S 220 
LEU   C    C N N 221 
LEU   O    O N N 222 
LEU   CB   C N N 223 
LEU   CG   C N N 224 
LEU   CD1  C N N 225 
LEU   CD2  C N N 226 
LEU   OXT  O N N 227 
LEU   H    H N N 228 
LEU   H2   H N N 229 
LEU   HA   H N N 230 
LEU   HB2  H N N 231 
LEU   HB3  H N N 232 
LEU   HG   H N N 233 
LEU   HD11 H N N 234 
LEU   HD12 H N N 235 
LEU   HD13 H N N 236 
LEU   HD21 H N N 237 
LEU   HD22 H N N 238 
LEU   HD23 H N N 239 
LEU   HXT  H N N 240 
LYS   N    N N N 241 
LYS   CA   C N S 242 
LYS   C    C N N 243 
LYS   O    O N N 244 
LYS   CB   C N N 245 
LYS   CG   C N N 246 
LYS   CD   C N N 247 
LYS   CE   C N N 248 
LYS   NZ   N N N 249 
LYS   OXT  O N N 250 
LYS   H    H N N 251 
LYS   H2   H N N 252 
LYS   HA   H N N 253 
LYS   HB2  H N N 254 
LYS   HB3  H N N 255 
LYS   HG2  H N N 256 
LYS   HG3  H N N 257 
LYS   HD2  H N N 258 
LYS   HD3  H N N 259 
LYS   HE2  H N N 260 
LYS   HE3  H N N 261 
LYS   HZ1  H N N 262 
LYS   HZ2  H N N 263 
LYS   HZ3  H N N 264 
LYS   HXT  H N N 265 
MET   N    N N N 266 
MET   CA   C N S 267 
MET   C    C N N 268 
MET   O    O N N 269 
MET   CB   C N N 270 
MET   CG   C N N 271 
MET   SD   S N N 272 
MET   CE   C N N 273 
MET   OXT  O N N 274 
MET   H    H N N 275 
MET   H2   H N N 276 
MET   HA   H N N 277 
MET   HB2  H N N 278 
MET   HB3  H N N 279 
MET   HG2  H N N 280 
MET   HG3  H N N 281 
MET   HE1  H N N 282 
MET   HE2  H N N 283 
MET   HE3  H N N 284 
MET   HXT  H N N 285 
PHE   N    N N N 286 
PHE   CA   C N S 287 
PHE   C    C N N 288 
PHE   O    O N N 289 
PHE   CB   C N N 290 
PHE   CG   C Y N 291 
PHE   CD1  C Y N 292 
PHE   CD2  C Y N 293 
PHE   CE1  C Y N 294 
PHE   CE2  C Y N 295 
PHE   CZ   C Y N 296 
PHE   OXT  O N N 297 
PHE   H    H N N 298 
PHE   H2   H N N 299 
PHE   HA   H N N 300 
PHE   HB2  H N N 301 
PHE   HB3  H N N 302 
PHE   HD1  H N N 303 
PHE   HD2  H N N 304 
PHE   HE1  H N N 305 
PHE   HE2  H N N 306 
PHE   HZ   H N N 307 
PHE   HXT  H N N 308 
PRO   N    N N N 309 
PRO   CA   C N S 310 
PRO   C    C N N 311 
PRO   O    O N N 312 
PRO   CB   C N N 313 
PRO   CG   C N N 314 
PRO   CD   C N N 315 
PRO   OXT  O N N 316 
PRO   H    H N N 317 
PRO   HA   H N N 318 
PRO   HB2  H N N 319 
PRO   HB3  H N N 320 
PRO   HG2  H N N 321 
PRO   HG3  H N N 322 
PRO   HD2  H N N 323 
PRO   HD3  H N N 324 
PRO   HXT  H N N 325 
SER   N    N N N 326 
SER   CA   C N S 327 
SER   C    C N N 328 
SER   O    O N N 329 
SER   CB   C N N 330 
SER   OG   O N N 331 
SER   OXT  O N N 332 
SER   H    H N N 333 
SER   H2   H N N 334 
SER   HA   H N N 335 
SER   HB2  H N N 336 
SER   HB3  H N N 337 
SER   HG   H N N 338 
SER   HXT  H N N 339 
SO4   S    S N N 340 
SO4   O1   O N N 341 
SO4   O2   O N N 342 
SO4   O3   O N N 343 
SO4   O4   O N N 344 
THR   N    N N N 345 
THR   CA   C N S 346 
THR   C    C N N 347 
THR   O    O N N 348 
THR   CB   C N R 349 
THR   OG1  O N N 350 
THR   CG2  C N N 351 
THR   OXT  O N N 352 
THR   H    H N N 353 
THR   H2   H N N 354 
THR   HA   H N N 355 
THR   HB   H N N 356 
THR   HG1  H N N 357 
THR   HG21 H N N 358 
THR   HG22 H N N 359 
THR   HG23 H N N 360 
THR   HXT  H N N 361 
TRP   N    N N N 362 
TRP   CA   C N S 363 
TRP   C    C N N 364 
TRP   O    O N N 365 
TRP   CB   C N N 366 
TRP   CG   C Y N 367 
TRP   CD1  C Y N 368 
TRP   CD2  C Y N 369 
TRP   NE1  N Y N 370 
TRP   CE2  C Y N 371 
TRP   CE3  C Y N 372 
TRP   CZ2  C Y N 373 
TRP   CZ3  C Y N 374 
TRP   CH2  C Y N 375 
TRP   OXT  O N N 376 
TRP   H    H N N 377 
TRP   H2   H N N 378 
TRP   HA   H N N 379 
TRP   HB2  H N N 380 
TRP   HB3  H N N 381 
TRP   HD1  H N N 382 
TRP   HE1  H N N 383 
TRP   HE3  H N N 384 
TRP   HZ2  H N N 385 
TRP   HZ3  H N N 386 
TRP   HH2  H N N 387 
TRP   HXT  H N N 388 
TYR   N    N N N 389 
TYR   CA   C N S 390 
TYR   C    C N N 391 
TYR   O    O N N 392 
TYR   CB   C N N 393 
TYR   CG   C Y N 394 
TYR   CD1  C Y N 395 
TYR   CD2  C Y N 396 
TYR   CE1  C Y N 397 
TYR   CE2  C Y N 398 
TYR   CZ   C Y N 399 
TYR   OH   O N N 400 
TYR   OXT  O N N 401 
TYR   H    H N N 402 
TYR   H2   H N N 403 
TYR   HA   H N N 404 
TYR   HB2  H N N 405 
TYR   HB3  H N N 406 
TYR   HD1  H N N 407 
TYR   HD2  H N N 408 
TYR   HE1  H N N 409 
TYR   HE2  H N N 410 
TYR   HH   H N N 411 
TYR   HXT  H N N 412 
VAL   N    N N N 413 
VAL   CA   C N S 414 
VAL   C    C N N 415 
VAL   O    O N N 416 
VAL   CB   C N N 417 
VAL   CG1  C N N 418 
VAL   CG2  C N N 419 
VAL   OXT  O N N 420 
VAL   H    H N N 421 
VAL   H2   H N N 422 
VAL   HA   H N N 423 
VAL   HB   H N N 424 
VAL   HG11 H N N 425 
VAL   HG12 H N N 426 
VAL   HG13 H N N 427 
VAL   HG21 H N N 428 
VAL   HG22 H N N 429 
VAL   HG23 H N N 430 
VAL   HXT  H N N 431 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1A3U C1  C    sing N N 1   
A1A3U N   C1   sing N N 2   
A1A3U C2  N    sing N N 3   
A1A3U C2  C3   sing N N 4   
A1A3U C3  C4   sing N N 5   
A1A3U C4  C2   sing N N 6   
A1A3U C5  C1   sing N N 7   
A1A3U C5  C6   sing Y N 8   
A1A3U C6  C7   doub Y N 9   
A1A3U C7  C8   sing Y N 10  
A1A3U C8  N1   doub Y N 11  
A1A3U N1  C9   sing Y N 12  
A1A3U C9  C5   doub Y N 13  
A1A3U C4  H9   sing N N 14  
A1A3U C4  H8   sing N N 15  
A1A3U C6  H10  sing N N 16  
A1A3U C7  H11  sing N N 17  
A1A3U C8  H12  sing N N 18  
A1A3U C   H    sing N N 19  
A1A3U C   H2   sing N N 20  
A1A3U C   H1   sing N N 21  
A1A3U C1  H3   sing N N 22  
A1A3U N   H4   sing N N 23  
A1A3U C2  H5   sing N N 24  
A1A3U C3  H7   sing N N 25  
A1A3U C3  H6   sing N N 26  
A1A3U C9  H13  sing N N 27  
ALA   N   CA   sing N N 28  
ALA   N   H    sing N N 29  
ALA   N   H2   sing N N 30  
ALA   CA  C    sing N N 31  
ALA   CA  CB   sing N N 32  
ALA   CA  HA   sing N N 33  
ALA   C   O    doub N N 34  
ALA   C   OXT  sing N N 35  
ALA   CB  HB1  sing N N 36  
ALA   CB  HB2  sing N N 37  
ALA   CB  HB3  sing N N 38  
ALA   OXT HXT  sing N N 39  
ARG   N   CA   sing N N 40  
ARG   N   H    sing N N 41  
ARG   N   H2   sing N N 42  
ARG   CA  C    sing N N 43  
ARG   CA  CB   sing N N 44  
ARG   CA  HA   sing N N 45  
ARG   C   O    doub N N 46  
ARG   C   OXT  sing N N 47  
ARG   CB  CG   sing N N 48  
ARG   CB  HB2  sing N N 49  
ARG   CB  HB3  sing N N 50  
ARG   CG  CD   sing N N 51  
ARG   CG  HG2  sing N N 52  
ARG   CG  HG3  sing N N 53  
ARG   CD  NE   sing N N 54  
ARG   CD  HD2  sing N N 55  
ARG   CD  HD3  sing N N 56  
ARG   NE  CZ   sing N N 57  
ARG   NE  HE   sing N N 58  
ARG   CZ  NH1  sing N N 59  
ARG   CZ  NH2  doub N N 60  
ARG   NH1 HH11 sing N N 61  
ARG   NH1 HH12 sing N N 62  
ARG   NH2 HH21 sing N N 63  
ARG   NH2 HH22 sing N N 64  
ARG   OXT HXT  sing N N 65  
ASN   N   CA   sing N N 66  
ASN   N   H    sing N N 67  
ASN   N   H2   sing N N 68  
ASN   CA  C    sing N N 69  
ASN   CA  CB   sing N N 70  
ASN   CA  HA   sing N N 71  
ASN   C   O    doub N N 72  
ASN   C   OXT  sing N N 73  
ASN   CB  CG   sing N N 74  
ASN   CB  HB2  sing N N 75  
ASN   CB  HB3  sing N N 76  
ASN   CG  OD1  doub N N 77  
ASN   CG  ND2  sing N N 78  
ASN   ND2 HD21 sing N N 79  
ASN   ND2 HD22 sing N N 80  
ASN   OXT HXT  sing N N 81  
ASP   N   CA   sing N N 82  
ASP   N   H    sing N N 83  
ASP   N   H2   sing N N 84  
ASP   CA  C    sing N N 85  
ASP   CA  CB   sing N N 86  
ASP   CA  HA   sing N N 87  
ASP   C   O    doub N N 88  
ASP   C   OXT  sing N N 89  
ASP   CB  CG   sing N N 90  
ASP   CB  HB2  sing N N 91  
ASP   CB  HB3  sing N N 92  
ASP   CG  OD1  doub N N 93  
ASP   CG  OD2  sing N N 94  
ASP   OD2 HD2  sing N N 95  
ASP   OXT HXT  sing N N 96  
CYS   N   CA   sing N N 97  
CYS   N   H    sing N N 98  
CYS   N   H2   sing N N 99  
CYS   CA  C    sing N N 100 
CYS   CA  CB   sing N N 101 
CYS   CA  HA   sing N N 102 
CYS   C   O    doub N N 103 
CYS   C   OXT  sing N N 104 
CYS   CB  SG   sing N N 105 
CYS   CB  HB2  sing N N 106 
CYS   CB  HB3  sing N N 107 
CYS   SG  HG   sing N N 108 
CYS   OXT HXT  sing N N 109 
EDO   C1  O1   sing N N 110 
EDO   C1  C2   sing N N 111 
EDO   C1  H11  sing N N 112 
EDO   C1  H12  sing N N 113 
EDO   O1  HO1  sing N N 114 
EDO   C2  O2   sing N N 115 
EDO   C2  H21  sing N N 116 
EDO   C2  H22  sing N N 117 
EDO   O2  HO2  sing N N 118 
GLN   N   CA   sing N N 119 
GLN   N   H    sing N N 120 
GLN   N   H2   sing N N 121 
GLN   CA  C    sing N N 122 
GLN   CA  CB   sing N N 123 
GLN   CA  HA   sing N N 124 
GLN   C   O    doub N N 125 
GLN   C   OXT  sing N N 126 
GLN   CB  CG   sing N N 127 
GLN   CB  HB2  sing N N 128 
GLN   CB  HB3  sing N N 129 
GLN   CG  CD   sing N N 130 
GLN   CG  HG2  sing N N 131 
GLN   CG  HG3  sing N N 132 
GLN   CD  OE1  doub N N 133 
GLN   CD  NE2  sing N N 134 
GLN   NE2 HE21 sing N N 135 
GLN   NE2 HE22 sing N N 136 
GLN   OXT HXT  sing N N 137 
GLU   N   CA   sing N N 138 
GLU   N   H    sing N N 139 
GLU   N   H2   sing N N 140 
GLU   CA  C    sing N N 141 
GLU   CA  CB   sing N N 142 
GLU   CA  HA   sing N N 143 
GLU   C   O    doub N N 144 
GLU   C   OXT  sing N N 145 
GLU   CB  CG   sing N N 146 
GLU   CB  HB2  sing N N 147 
GLU   CB  HB3  sing N N 148 
GLU   CG  CD   sing N N 149 
GLU   CG  HG2  sing N N 150 
GLU   CG  HG3  sing N N 151 
GLU   CD  OE1  doub N N 152 
GLU   CD  OE2  sing N N 153 
GLU   OE2 HE2  sing N N 154 
GLU   OXT HXT  sing N N 155 
GLY   N   CA   sing N N 156 
GLY   N   H    sing N N 157 
GLY   N   H2   sing N N 158 
GLY   CA  C    sing N N 159 
GLY   CA  HA2  sing N N 160 
GLY   CA  HA3  sing N N 161 
GLY   C   O    doub N N 162 
GLY   C   OXT  sing N N 163 
GLY   OXT HXT  sing N N 164 
HIS   N   CA   sing N N 165 
HIS   N   H    sing N N 166 
HIS   N   H2   sing N N 167 
HIS   CA  C    sing N N 168 
HIS   CA  CB   sing N N 169 
HIS   CA  HA   sing N N 170 
HIS   C   O    doub N N 171 
HIS   C   OXT  sing N N 172 
HIS   CB  CG   sing N N 173 
HIS   CB  HB2  sing N N 174 
HIS   CB  HB3  sing N N 175 
HIS   CG  ND1  sing Y N 176 
HIS   CG  CD2  doub Y N 177 
HIS   ND1 CE1  doub Y N 178 
HIS   ND1 HD1  sing N N 179 
HIS   CD2 NE2  sing Y N 180 
HIS   CD2 HD2  sing N N 181 
HIS   CE1 NE2  sing Y N 182 
HIS   CE1 HE1  sing N N 183 
HIS   NE2 HE2  sing N N 184 
HIS   OXT HXT  sing N N 185 
HOH   O   H1   sing N N 186 
HOH   O   H2   sing N N 187 
ILE   N   CA   sing N N 188 
ILE   N   H    sing N N 189 
ILE   N   H2   sing N N 190 
ILE   CA  C    sing N N 191 
ILE   CA  CB   sing N N 192 
ILE   CA  HA   sing N N 193 
ILE   C   O    doub N N 194 
ILE   C   OXT  sing N N 195 
ILE   CB  CG1  sing N N 196 
ILE   CB  CG2  sing N N 197 
ILE   CB  HB   sing N N 198 
ILE   CG1 CD1  sing N N 199 
ILE   CG1 HG12 sing N N 200 
ILE   CG1 HG13 sing N N 201 
ILE   CG2 HG21 sing N N 202 
ILE   CG2 HG22 sing N N 203 
ILE   CG2 HG23 sing N N 204 
ILE   CD1 HD11 sing N N 205 
ILE   CD1 HD12 sing N N 206 
ILE   CD1 HD13 sing N N 207 
ILE   OXT HXT  sing N N 208 
LEU   N   CA   sing N N 209 
LEU   N   H    sing N N 210 
LEU   N   H2   sing N N 211 
LEU   CA  C    sing N N 212 
LEU   CA  CB   sing N N 213 
LEU   CA  HA   sing N N 214 
LEU   C   O    doub N N 215 
LEU   C   OXT  sing N N 216 
LEU   CB  CG   sing N N 217 
LEU   CB  HB2  sing N N 218 
LEU   CB  HB3  sing N N 219 
LEU   CG  CD1  sing N N 220 
LEU   CG  CD2  sing N N 221 
LEU   CG  HG   sing N N 222 
LEU   CD1 HD11 sing N N 223 
LEU   CD1 HD12 sing N N 224 
LEU   CD1 HD13 sing N N 225 
LEU   CD2 HD21 sing N N 226 
LEU   CD2 HD22 sing N N 227 
LEU   CD2 HD23 sing N N 228 
LEU   OXT HXT  sing N N 229 
LYS   N   CA   sing N N 230 
LYS   N   H    sing N N 231 
LYS   N   H2   sing N N 232 
LYS   CA  C    sing N N 233 
LYS   CA  CB   sing N N 234 
LYS   CA  HA   sing N N 235 
LYS   C   O    doub N N 236 
LYS   C   OXT  sing N N 237 
LYS   CB  CG   sing N N 238 
LYS   CB  HB2  sing N N 239 
LYS   CB  HB3  sing N N 240 
LYS   CG  CD   sing N N 241 
LYS   CG  HG2  sing N N 242 
LYS   CG  HG3  sing N N 243 
LYS   CD  CE   sing N N 244 
LYS   CD  HD2  sing N N 245 
LYS   CD  HD3  sing N N 246 
LYS   CE  NZ   sing N N 247 
LYS   CE  HE2  sing N N 248 
LYS   CE  HE3  sing N N 249 
LYS   NZ  HZ1  sing N N 250 
LYS   NZ  HZ2  sing N N 251 
LYS   NZ  HZ3  sing N N 252 
LYS   OXT HXT  sing N N 253 
MET   N   CA   sing N N 254 
MET   N   H    sing N N 255 
MET   N   H2   sing N N 256 
MET   CA  C    sing N N 257 
MET   CA  CB   sing N N 258 
MET   CA  HA   sing N N 259 
MET   C   O    doub N N 260 
MET   C   OXT  sing N N 261 
MET   CB  CG   sing N N 262 
MET   CB  HB2  sing N N 263 
MET   CB  HB3  sing N N 264 
MET   CG  SD   sing N N 265 
MET   CG  HG2  sing N N 266 
MET   CG  HG3  sing N N 267 
MET   SD  CE   sing N N 268 
MET   CE  HE1  sing N N 269 
MET   CE  HE2  sing N N 270 
MET   CE  HE3  sing N N 271 
MET   OXT HXT  sing N N 272 
PHE   N   CA   sing N N 273 
PHE   N   H    sing N N 274 
PHE   N   H2   sing N N 275 
PHE   CA  C    sing N N 276 
PHE   CA  CB   sing N N 277 
PHE   CA  HA   sing N N 278 
PHE   C   O    doub N N 279 
PHE   C   OXT  sing N N 280 
PHE   CB  CG   sing N N 281 
PHE   CB  HB2  sing N N 282 
PHE   CB  HB3  sing N N 283 
PHE   CG  CD1  doub Y N 284 
PHE   CG  CD2  sing Y N 285 
PHE   CD1 CE1  sing Y N 286 
PHE   CD1 HD1  sing N N 287 
PHE   CD2 CE2  doub Y N 288 
PHE   CD2 HD2  sing N N 289 
PHE   CE1 CZ   doub Y N 290 
PHE   CE1 HE1  sing N N 291 
PHE   CE2 CZ   sing Y N 292 
PHE   CE2 HE2  sing N N 293 
PHE   CZ  HZ   sing N N 294 
PHE   OXT HXT  sing N N 295 
PRO   N   CA   sing N N 296 
PRO   N   CD   sing N N 297 
PRO   N   H    sing N N 298 
PRO   CA  C    sing N N 299 
PRO   CA  CB   sing N N 300 
PRO   CA  HA   sing N N 301 
PRO   C   O    doub N N 302 
PRO   C   OXT  sing N N 303 
PRO   CB  CG   sing N N 304 
PRO   CB  HB2  sing N N 305 
PRO   CB  HB3  sing N N 306 
PRO   CG  CD   sing N N 307 
PRO   CG  HG2  sing N N 308 
PRO   CG  HG3  sing N N 309 
PRO   CD  HD2  sing N N 310 
PRO   CD  HD3  sing N N 311 
PRO   OXT HXT  sing N N 312 
SER   N   CA   sing N N 313 
SER   N   H    sing N N 314 
SER   N   H2   sing N N 315 
SER   CA  C    sing N N 316 
SER   CA  CB   sing N N 317 
SER   CA  HA   sing N N 318 
SER   C   O    doub N N 319 
SER   C   OXT  sing N N 320 
SER   CB  OG   sing N N 321 
SER   CB  HB2  sing N N 322 
SER   CB  HB3  sing N N 323 
SER   OG  HG   sing N N 324 
SER   OXT HXT  sing N N 325 
SO4   S   O1   doub N N 326 
SO4   S   O2   doub N N 327 
SO4   S   O3   sing N N 328 
SO4   S   O4   sing N N 329 
THR   N   CA   sing N N 330 
THR   N   H    sing N N 331 
THR   N   H2   sing N N 332 
THR   CA  C    sing N N 333 
THR   CA  CB   sing N N 334 
THR   CA  HA   sing N N 335 
THR   C   O    doub N N 336 
THR   C   OXT  sing N N 337 
THR   CB  OG1  sing N N 338 
THR   CB  CG2  sing N N 339 
THR   CB  HB   sing N N 340 
THR   OG1 HG1  sing N N 341 
THR   CG2 HG21 sing N N 342 
THR   CG2 HG22 sing N N 343 
THR   CG2 HG23 sing N N 344 
THR   OXT HXT  sing N N 345 
TRP   N   CA   sing N N 346 
TRP   N   H    sing N N 347 
TRP   N   H2   sing N N 348 
TRP   CA  C    sing N N 349 
TRP   CA  CB   sing N N 350 
TRP   CA  HA   sing N N 351 
TRP   C   O    doub N N 352 
TRP   C   OXT  sing N N 353 
TRP   CB  CG   sing N N 354 
TRP   CB  HB2  sing N N 355 
TRP   CB  HB3  sing N N 356 
TRP   CG  CD1  doub Y N 357 
TRP   CG  CD2  sing Y N 358 
TRP   CD1 NE1  sing Y N 359 
TRP   CD1 HD1  sing N N 360 
TRP   CD2 CE2  doub Y N 361 
TRP   CD2 CE3  sing Y N 362 
TRP   NE1 CE2  sing Y N 363 
TRP   NE1 HE1  sing N N 364 
TRP   CE2 CZ2  sing Y N 365 
TRP   CE3 CZ3  doub Y N 366 
TRP   CE3 HE3  sing N N 367 
TRP   CZ2 CH2  doub Y N 368 
TRP   CZ2 HZ2  sing N N 369 
TRP   CZ3 CH2  sing Y N 370 
TRP   CZ3 HZ3  sing N N 371 
TRP   CH2 HH2  sing N N 372 
TRP   OXT HXT  sing N N 373 
TYR   N   CA   sing N N 374 
TYR   N   H    sing N N 375 
TYR   N   H2   sing N N 376 
TYR   CA  C    sing N N 377 
TYR   CA  CB   sing N N 378 
TYR   CA  HA   sing N N 379 
TYR   C   O    doub N N 380 
TYR   C   OXT  sing N N 381 
TYR   CB  CG   sing N N 382 
TYR   CB  HB2  sing N N 383 
TYR   CB  HB3  sing N N 384 
TYR   CG  CD1  doub Y N 385 
TYR   CG  CD2  sing Y N 386 
TYR   CD1 CE1  sing Y N 387 
TYR   CD1 HD1  sing N N 388 
TYR   CD2 CE2  doub Y N 389 
TYR   CD2 HD2  sing N N 390 
TYR   CE1 CZ   doub Y N 391 
TYR   CE1 HE1  sing N N 392 
TYR   CE2 CZ   sing Y N 393 
TYR   CE2 HE2  sing N N 394 
TYR   CZ  OH   sing N N 395 
TYR   OH  HH   sing N N 396 
TYR   OXT HXT  sing N N 397 
VAL   N   CA   sing N N 398 
VAL   N   H    sing N N 399 
VAL   N   H2   sing N N 400 
VAL   CA  C    sing N N 401 
VAL   CA  CB   sing N N 402 
VAL   CA  HA   sing N N 403 
VAL   C   O    doub N N 404 
VAL   C   OXT  sing N N 405 
VAL   CB  CG1  sing N N 406 
VAL   CB  CG2  sing N N 407 
VAL   CB  HB   sing N N 408 
VAL   CG1 HG11 sing N N 409 
VAL   CG1 HG12 sing N N 410 
VAL   CG1 HG13 sing N N 411 
VAL   CG2 HG21 sing N N 412 
VAL   CG2 HG22 sing N N 413 
VAL   CG2 HG23 sing N N 414 
VAL   OXT HXT  sing N N 415 
# 
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                    7HHB 
_atom_sites.fract_transf_matrix[1][1]   0.024004 
_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]   0.023770 
_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]   0.006314 
_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  ? 0.321   4.313   2.438   1.00 55.88  ? 1   MET   A N   1 
ATOM   2    C CA  . MET   A 1 2  ? -0.804  3.581   1.796   1.00 64.64  ? 1   MET   A CA  1 
ATOM   3    C C   . MET   A 1 2  ? -0.254  2.578   0.779   1.00 57.56  ? 1   MET   A C   1 
ATOM   4    O O   . MET   A 1 2  ? 0.793   2.821   0.191   1.00 57.76  ? 1   MET   A O   1 
ATOM   5    C CB  . MET   A 1 2  ? -1.797  4.553   1.148   1.00 66.73  ? 1   MET   A CB  1 
ATOM   6    C CG  . MET   A 1 2  ? -2.730  5.241   2.137   1.00 77.21  ? 1   MET   A CG  1 
ATOM   7    S SD  . MET   A 1 2  ? -4.036  4.223   2.862   1.00 69.86  ? 1   MET   A SD  1 
ATOM   8    C CE  . MET   A 1 2  ? -5.093  5.469   3.615   1.00 68.93  ? 1   MET   A CE  1 
ATOM   9    N N   . PRO   A 1 3  ? -0.907  1.396   0.611   1.00 57.23  ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 3  ? -0.465  0.341   -0.318  1.00 51.86  ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 3  ? -0.164  0.693   -1.777  1.00 44.45  ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 3  ? -0.874  1.484   -2.391  1.00 40.10  ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 3  ? -1.679  -0.651  -0.232  1.00 47.26  ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 3  ? -2.115  -0.526  1.211   1.00 54.07  ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 3  ? -2.092  0.982   1.387   1.00 53.37  ? 2   PRO   A CD  1 
ATOM   16   N N   . HIS   A 1 4  ? 0.860   0.036   -2.336  1.00 42.52  ? 3   HIS   A N   1 
ATOM   17   C CA  . HIS   A 1 4  ? 1.117   0.095   -3.758  1.00 40.47  ? 3   HIS   A CA  1 
ATOM   18   C C   . HIS   A 1 4  ? 0.490   -1.158  -4.364  1.00 38.20  ? 3   HIS   A C   1 
ATOM   19   O O   . HIS   A 1 4  ? -0.061  -1.987  -3.624  1.00 33.93  ? 3   HIS   A O   1 
ATOM   20   C CB  . HIS   A 1 4  ? 2.631   0.181   -4.000  1.00 46.93  ? 3   HIS   A CB  1 
ATOM   21   C CG  . HIS   A 1 4  ? 3.222   1.498   -3.599  1.00 60.95  ? 3   HIS   A CG  1 
ATOM   22   N ND1 . HIS   A 1 4  ? 2.993   2.099   -2.378  1.00 67.38  ? 3   HIS   A ND1 1 
ATOM   23   C CD2 . HIS   A 1 4  ? 4.031   2.328   -4.268  1.00 67.00  ? 3   HIS   A CD2 1 
ATOM   24   C CE1 . HIS   A 1 4  ? 3.643   3.251   -2.316  1.00 63.73  ? 3   HIS   A CE1 1 
ATOM   25   N NE2 . HIS   A 1 4  ? 4.282   3.409   -3.455  1.00 68.82  ? 3   HIS   A NE2 1 
ATOM   26   N N   . ALA   A 1 5  ? 0.606   -1.301  -5.694  1.00 31.99  ? 4   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 5  ? 0.369   -2.570  -6.367  1.00 32.85  ? 4   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 5  ? 1.460   -3.567  -5.963  1.00 32.33  ? 4   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 5  ? 2.512   -3.157  -5.470  1.00 32.84  ? 4   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 5  ? 0.342   -2.341  -7.859  1.00 36.19  ? 4   ALA   A CB  1 
ATOM   31   N N   . PHE   A 1 6  ? 1.200   -4.866  -6.146  1.00 30.03  ? 5   PHE   A N   1 
ATOM   32   C CA  . PHE   A 1 6  ? 2.192   -5.895  -5.863  1.00 29.59  ? 5   PHE   A CA  1 
ATOM   33   C C   . PHE   A 1 6  ? 3.366   -5.735  -6.831  1.00 30.95  ? 5   PHE   A C   1 
ATOM   34   O O   . PHE   A 1 6  ? 3.143   -5.383  -7.985  1.00 29.40  ? 5   PHE   A O   1 
ATOM   35   C CB  . PHE   A 1 6  ? 1.581   -7.298  -5.975  1.00 25.96  ? 5   PHE   A CB  1 
ATOM   36   C CG  . PHE   A 1 6  ? 0.819   -7.687  -4.712  1.00 26.94  ? 5   PHE   A CG  1 
ATOM   37   C CD1 . PHE   A 1 6  ? 1.508   -7.898  -3.518  1.00 27.84  ? 5   PHE   A CD1 1 
ATOM   38   C CD2 . PHE   A 1 6  ? -0.571  -7.874  -4.734  1.00 26.95  ? 5   PHE   A CD2 1 
ATOM   39   C CE1 . PHE   A 1 6  ? 0.838   -8.275  -2.356  1.00 27.75  ? 5   PHE   A CE1 1 
ATOM   40   C CE2 . PHE   A 1 6  ? -1.251  -8.262  -3.573  1.00 23.70  ? 5   PHE   A CE2 1 
ATOM   41   C CZ  . PHE   A 1 6  ? -0.539  -8.466  -2.394  1.00 27.16  ? 5   PHE   A CZ  1 
ATOM   42   N N   . LYS   A 1 7  ? 4.602   -5.979  -6.359  1.00 28.03  ? 6   LYS   A N   1 
ATOM   43   C CA  . LYS   A 1 7  ? 5.763   -5.931  -7.240  1.00 29.58  ? 6   LYS   A CA  1 
ATOM   44   C C   . LYS   A 1 7  ? 6.669   -7.135  -6.964  1.00 28.05  ? 6   LYS   A C   1 
ATOM   45   O O   . LYS   A 1 7  ? 6.625   -7.735  -5.892  1.00 25.56  ? 6   LYS   A O   1 
ATOM   46   C CB  . LYS   A 1 7  ? 6.507   -4.602  -7.053  1.00 32.66  ? 6   LYS   A CB  1 
ATOM   47   C CG  . LYS   A 1 7  ? 7.146   -4.498  -5.678  1.00 34.73  ? 6   LYS   A CG  1 
ATOM   48   C CD  . LYS   A 1 7  ? 7.726   -3.120  -5.365  1.00 40.30  ? 6   LYS   A CD  1 
ATOM   49   C CE  . LYS   A 1 7  ? 8.397   -3.134  -4.027  1.00 42.70  ? 6   LYS   A CE  1 
ATOM   50   N NZ  . LYS   A 1 7  ? 7.402   -3.321  -2.967  1.00 42.52  ? 6   LYS   A NZ  1 
ATOM   51   N N   . PRO   A 1 8  ? 7.508   -7.559  -7.928  1.00 28.15  ? 7   PRO   A N   1 
ATOM   52   C CA  . PRO   A 1 8  ? 8.436   -8.664  -7.677  1.00 28.95  ? 7   PRO   A CA  1 
ATOM   53   C C   . PRO   A 1 8  ? 9.253   -8.376  -6.419  1.00 25.98  ? 7   PRO   A C   1 
ATOM   54   O O   . PRO   A 1 8  ? 9.675   -7.240  -6.194  1.00 27.17  ? 7   PRO   A O   1 
ATOM   55   C CB  . PRO   A 1 8  ? 9.295   -8.706  -8.960  1.00 28.38  ? 7   PRO   A CB  1 
ATOM   56   C CG  . PRO   A 1 8  ? 8.387   -8.104  -10.013 1.00 31.57  ? 7   PRO   A CG  1 
ATOM   57   C CD  . PRO   A 1 8  ? 7.594   -7.014  -9.292  1.00 31.49  ? 7   PRO   A CD  1 
ATOM   58   N N   . GLY   A 1 9  ? 9.433   -9.418  -5.592  1.00 25.56  ? 8   GLY   A N   1 
ATOM   59   C CA  . GLY   A 1 9  ? 10.172  -9.311  -4.346  1.00 24.26  ? 8   GLY   A CA  1 
ATOM   60   C C   . GLY   A 1 9  ? 9.230   -9.183  -3.140  1.00 24.79  ? 8   GLY   A C   1 
ATOM   61   O O   . GLY   A 1 9  ? 9.636   -9.451  -1.991  1.00 27.07  ? 8   GLY   A O   1 
ATOM   62   N N   . ASP   A 1 10 ? 7.975   -8.760  -3.368  1.00 22.42  ? 9   ASP   A N   1 
ATOM   63   C CA  . ASP   A 1 10 ? 7.017   -8.720  -2.265  1.00 21.84  ? 9   ASP   A CA  1 
ATOM   64   C C   . ASP   A 1 10 ? 6.790   -10.102 -1.633  1.00 21.28  ? 9   ASP   A C   1 
ATOM   65   O O   . ASP   A 1 10 ? 6.627   -11.094 -2.328  1.00 21.51  ? 9   ASP   A O   1 
ATOM   66   C CB  . ASP   A 1 10 ? 5.676   -8.128  -2.676  1.00 24.04  ? 9   ASP   A CB  1 
ATOM   67   C CG  . ASP   A 1 10 ? 5.672   -6.621  -2.890  1.00 25.60  ? 9   ASP   A CG  1 
ATOM   68   O OD1 . ASP   A 1 10 ? 6.639   -5.953  -2.469  1.00 26.38  ? 9   ASP   A OD1 1 
ATOM   69   O OD2 . ASP   A 1 10 ? 4.736   -6.144  -3.527  1.00 26.68  ? 9   ASP   A OD2 1 
ATOM   70   N N   . LEU   A 1 11 ? 6.709   -10.152 -0.294  1.00 20.49  ? 10  LEU   A N   1 
ATOM   71   C CA  . LEU   A 1 11 ? 6.549   -11.420 0.421   1.00 22.60  ? 10  LEU   A CA  1 
ATOM   72   C C   . LEU   A 1 11 ? 5.096   -11.516 0.875   1.00 24.26  ? 10  LEU   A C   1 
ATOM   73   O O   . LEU   A 1 11 ? 4.541   -10.525 1.356   1.00 25.93  ? 10  LEU   A O   1 
ATOM   74   C CB  . LEU   A 1 11 ? 7.492   -11.537 1.627   1.00 22.20  ? 10  LEU   A CB  1 
ATOM   75   C CG  . LEU   A 1 11 ? 8.963   -11.235 1.296   1.00 20.76  ? 10  LEU   A CG  1 
ATOM   76   C CD1 . LEU   A 1 11 ? 9.825   -11.313 2.534   1.00 25.97  ? 10  LEU   A CD1 1 
ATOM   77   C CD2 . LEU   A 1 11 ? 9.421   -12.226 0.214   1.00 23.20  ? 10  LEU   A CD2 1 
ATOM   78   N N   . VAL   A 1 12 ? 4.520   -12.714 0.756   1.00 20.88  ? 11  VAL   A N   1 
ATOM   79   C CA  . VAL   A 1 12 ? 3.088   -12.890 0.958   1.00 22.24  ? 11  VAL   A CA  1 
ATOM   80   C C   . VAL   A 1 12 ? 2.824   -14.225 1.634   1.00 24.57  ? 11  VAL   A C   1 
ATOM   81   O O   . VAL   A 1 12 ? 3.689   -15.096 1.674   1.00 22.49  ? 11  VAL   A O   1 
ATOM   82   C CB  . VAL   A 1 12 ? 2.311   -12.817 -0.377  1.00 19.42  ? 11  VAL   A CB  1 
ATOM   83   C CG1 . VAL   A 1 12 ? 2.428   -11.408 -0.960  1.00 21.53  ? 11  VAL   A CG1 1 
ATOM   84   C CG2 . VAL   A 1 12 ? 2.783   -13.902 -1.367  1.00 20.78  ? 11  VAL   A CG2 1 
ATOM   85   N N   . PHE   A 1 13 ? 1.592   -14.381 2.129   1.00 24.57  ? 12  PHE   A N   1 
ATOM   86   C CA  . PHE   A 1 13 ? 1.024   -15.721 2.196   1.00 23.74  ? 12  PHE   A CA  1 
ATOM   87   C C   . PHE   A 1 13 ? 0.089   -15.870 1.000   1.00 25.83  ? 12  PHE   A C   1 
ATOM   88   O O   . PHE   A 1 13 ? -0.711  -14.978 0.747   1.00 26.08  ? 12  PHE   A O   1 
ATOM   89   C CB  . PHE   A 1 13 ? 0.237   -15.994 3.489   1.00 23.78  ? 12  PHE   A CB  1 
ATOM   90   C CG  . PHE   A 1 13 ? 1.154   -16.126 4.691   1.00 24.07  ? 12  PHE   A CG  1 
ATOM   91   C CD1 . PHE   A 1 13 ? 1.572   -14.995 5.383   1.00 25.62  ? 12  PHE   A CD1 1 
ATOM   92   C CD2 . PHE   A 1 13 ? 1.617   -17.372 5.101   1.00 26.26  ? 12  PHE   A CD2 1 
ATOM   93   C CE1 . PHE   A 1 13 ? 2.448   -15.106 6.456   1.00 30.92  ? 12  PHE   A CE1 1 
ATOM   94   C CE2 . PHE   A 1 13 ? 2.482   -17.485 6.184   1.00 29.18  ? 12  PHE   A CE2 1 
ATOM   95   C CZ  . PHE   A 1 13 ? 2.892   -16.360 6.857   1.00 30.52  ? 12  PHE   A CZ  1 
ATOM   96   N N   . ALA   A 1 14 ? 0.240   -16.962 0.225   1.00 25.63  ? 13  ALA   A N   1 
ATOM   97   C CA  . ALA   A 1 14 ? -0.590  -17.150 -0.961  1.00 25.02  ? 13  ALA   A CA  1 
ATOM   98   C C   . ALA   A 1 14 ? -1.586  -18.299 -0.732  1.00 28.34  ? 13  ALA   A C   1 
ATOM   99   O O   . ALA   A 1 14 ? -1.232  -19.340 -0.149  1.00 28.60  ? 13  ALA   A O   1 
ATOM   100  C CB  . ALA   A 1 14 ? 0.275   -17.371 -2.211  1.00 22.75  ? 13  ALA   A CB  1 
ATOM   101  N N   . LYS   A 1 15 ? -2.841  -18.075 -1.161  1.00 25.24  ? 14  LYS   A N   1 
ATOM   102  C CA  . LYS   A 1 15 ? -3.907  -19.019 -0.888  1.00 28.14  ? 14  LYS   A CA  1 
ATOM   103  C C   . LYS   A 1 15 ? -4.248  -19.761 -2.175  1.00 30.43  ? 14  LYS   A C   1 
ATOM   104  O O   . LYS   A 1 15 ? -4.606  -19.140 -3.178  1.00 31.94  ? 14  LYS   A O   1 
ATOM   105  C CB  . LYS   A 1 15 ? -5.151  -18.376 -0.262  1.00 30.64  ? 14  LYS   A CB  1 
ATOM   106  C CG  . LYS   A 1 15 ? -6.178  -19.437 0.182   1.00 34.40  ? 14  LYS   A CG  1 
ATOM   107  C CD  . LYS   A 1 15 ? -5.728  -20.320 1.359   1.00 33.33  ? 14  LYS   A CD  1 
ATOM   108  C CE  . LYS   A 1 15 ? -6.830  -21.188 1.921   1.00 34.27  ? 14  LYS   A CE  1 
ATOM   109  N NZ  . LYS   A 1 15 ? -7.301  -22.116 0.889   1.00 35.95  ? 14  LYS   A NZ  1 
ATOM   110  N N   . MET   A 1 16 ? -4.122  -21.091 -2.114  1.00 29.74  ? 15  MET   A N   1 
ATOM   111  C CA  . MET   A 1 16 ? -4.716  -21.923 -3.146  1.00 32.70  ? 15  MET   A CA  1 
ATOM   112  C C   . MET   A 1 16 ? -5.705  -22.916 -2.553  1.00 33.82  ? 15  MET   A C   1 
ATOM   113  O O   . MET   A 1 16 ? -5.547  -23.341 -1.415  1.00 28.92  ? 15  MET   A O   1 
ATOM   114  C CB  . MET   A 1 16 ? -3.625  -22.633 -3.934  1.00 36.51  ? 15  MET   A CB  1 
ATOM   115  C CG  . MET   A 1 16 ? -2.958  -21.560 -4.791  1.00 39.97  ? 15  MET   A CG  1 
ATOM   116  S SD  . MET   A 1 16 ? -1.888  -22.265 -6.022  1.00 47.71  ? 15  MET   A SD  1 
ATOM   117  C CE  . MET   A 1 16 ? -3.060  -22.995 -7.173  1.00 54.88  ? 15  MET   A CE  1 
ATOM   118  N N   . LYS   A 1 17 ? -6.724  -23.222 -3.362  1.00 39.33  ? 16  LYS   A N   1 
ATOM   119  C CA  . LYS   A 1 17 ? -7.783  -24.178 -3.073  1.00 41.38  ? 16  LYS   A CA  1 
ATOM   120  C C   . LYS   A 1 17 ? -7.171  -25.428 -2.465  1.00 39.58  ? 16  LYS   A C   1 
ATOM   121  O O   . LYS   A 1 17 ? -6.249  -26.008 -3.036  1.00 38.39  ? 16  LYS   A O   1 
ATOM   122  C CB  . LYS   A 1 17 ? -8.448  -24.579 -4.396  1.00 49.43  ? 16  LYS   A CB  1 
ATOM   123  C CG  . LYS   A 1 17 ? -9.947  -24.843 -4.293  1.00 63.23  ? 16  LYS   A CG  1 
ATOM   124  C CD  . LYS   A 1 17 ? -10.803 -23.580 -4.391  1.00 67.37  ? 16  LYS   A CD  1 
ATOM   125  N N   . GLY   A 1 18 ? -7.643  -25.783 -1.268  1.00 36.74  ? 17  GLY   A N   1 
ATOM   126  C CA  . GLY   A 1 18 ? -7.237  -27.034 -0.661  1.00 39.65  ? 17  GLY   A CA  1 
ATOM   127  C C   . GLY   A 1 18 ? -5.892  -26.974 0.059   1.00 44.90  ? 17  GLY   A C   1 
ATOM   128  O O   . GLY   A 1 18 ? -5.434  -28.009 0.534   1.00 44.87  ? 17  GLY   A O   1 
ATOM   129  N N   . TYR   A 1 19 ? -5.234  -25.800 0.128   1.00 35.57  ? 18  TYR   A N   1 
ATOM   130  C CA  . TYR   A 1 19 ? -4.059  -25.697 0.973   1.00 34.29  ? 18  TYR   A CA  1 
ATOM   131  C C   . TYR   A 1 19 ? -4.183  -24.540 1.956   1.00 32.82  ? 18  TYR   A C   1 
ATOM   132  O O   . TYR   A 1 19 ? -4.862  -23.567 1.656   1.00 32.27  ? 18  TYR   A O   1 
ATOM   133  C CB  . TYR   A 1 19 ? -2.834  -25.306 0.149   1.00 37.38  ? 18  TYR   A CB  1 
ATOM   134  C CG  . TYR   A 1 19 ? -2.451  -26.421 -0.804  1.00 42.85  ? 18  TYR   A CG  1 
ATOM   135  C CD1 . TYR   A 1 19 ? -1.504  -27.365 -0.430  1.00 52.84  ? 18  TYR   A CD1 1 
ATOM   136  C CD2 . TYR   A 1 19 ? -3.060  -26.541 -2.043  1.00 44.09  ? 18  TYR   A CD2 1 
ATOM   137  C CE1 . TYR   A 1 19 ? -1.160  -28.395 -1.287  1.00 63.17  ? 18  TYR   A CE1 1 
ATOM   138  C CE2 . TYR   A 1 19 ? -2.729  -27.570 -2.910  1.00 52.77  ? 18  TYR   A CE2 1 
ATOM   139  C CZ  . TYR   A 1 19 ? -1.773  -28.492 -2.524  1.00 62.20  ? 18  TYR   A CZ  1 
ATOM   140  O OH  . TYR   A 1 19 ? -1.409  -29.507 -3.352  1.00 74.61  ? 18  TYR   A OH  1 
ATOM   141  N N   . PRO   A 1 20 ? -3.459  -24.563 3.101   1.00 29.19  ? 19  PRO   A N   1 
ATOM   142  C CA  . PRO   A 1 20 ? -3.411  -23.404 4.003   1.00 31.28  ? 19  PRO   A CA  1 
ATOM   143  C C   . PRO   A 1 20 ? -2.720  -22.234 3.296   1.00 31.44  ? 19  PRO   A C   1 
ATOM   144  O O   . PRO   A 1 20 ? -1.996  -22.443 2.312   1.00 29.11  ? 19  PRO   A O   1 
ATOM   145  C CB  . PRO   A 1 20 ? -2.628  -23.912 5.206   1.00 31.08  ? 19  PRO   A CB  1 
ATOM   146  C CG  . PRO   A 1 20 ? -1.765  -25.017 4.620   1.00 33.14  ? 19  PRO   A CG  1 
ATOM   147  C CD  . PRO   A 1 20 ? -2.646  -25.696 3.571   1.00 34.20  ? 19  PRO   A CD  1 
ATOM   148  N N   . HIS   A 1 21 ? -2.978  -21.018 3.783   1.00 26.90  ? 20  HIS   A N   1 
ATOM   149  C CA  . HIS   A 1 21 ? -2.251  -19.831 3.339   1.00 28.34  ? 20  HIS   A CA  1 
ATOM   150  C C   . HIS   A 1 21 ? -0.759  -20.155 3.443   1.00 30.03  ? 20  HIS   A C   1 
ATOM   151  O O   . HIS   A 1 21 ? -0.308  -20.577 4.504   1.00 28.68  ? 20  HIS   A O   1 
ATOM   152  C CB  . HIS   A 1 21 ? -2.680  -18.615 4.177   1.00 25.41  ? 20  HIS   A CB  1 
ATOM   153  C CG  . HIS   A 1 21 ? -4.148  -18.292 4.028   1.00 32.41  ? 20  HIS   A CG  1 
ATOM   154  N ND1 . HIS   A 1 21 ? -5.133  -18.998 4.699   1.00 34.15  ? 20  HIS   A ND1 1 
ATOM   155  C CD2 . HIS   A 1 21 ? -4.803  -17.372 3.272   1.00 30.82  ? 20  HIS   A CD2 1 
ATOM   156  C CE1 . HIS   A 1 21 ? -6.338  -18.528 4.356   1.00 31.64  ? 20  HIS   A CE1 1 
ATOM   157  N NE2 . HIS   A 1 21 ? -6.165  -17.529 3.500   1.00 31.33  ? 20  HIS   A NE2 1 
ATOM   158  N N   . TRP   A 1 22 ? -0.001  -19.955 2.349   1.00 25.97  ? 21  TRP   A N   1 
ATOM   159  C CA  . TRP   A 1 22 ? 1.318   -20.550 2.221   1.00 26.00  ? 21  TRP   A CA  1 
ATOM   160  C C   . TRP   A 1 22 ? 2.398   -19.482 2.006   1.00 27.64  ? 21  TRP   A C   1 
ATOM   161  O O   . TRP   A 1 22 ? 2.225   -18.596 1.157   1.00 25.60  ? 21  TRP   A O   1 
ATOM   162  C CB  . TRP   A 1 22 ? 1.295   -21.531 1.033   1.00 26.35  ? 21  TRP   A CB  1 
ATOM   163  C CG  . TRP   A 1 22 ? 2.407   -22.540 1.080   1.00 28.24  ? 21  TRP   A CG  1 
ATOM   164  C CD1 . TRP   A 1 22 ? 3.737   -22.342 0.819   1.00 29.23  ? 21  TRP   A CD1 1 
ATOM   165  C CD2 . TRP   A 1 22 ? 2.264   -23.925 1.453   1.00 28.61  ? 21  TRP   A CD2 1 
ATOM   166  N NE1 . TRP   A 1 22 ? 4.425   -23.518 0.971   1.00 28.92  ? 21  TRP   A NE1 1 
ATOM   167  C CE2 . TRP   A 1 22 ? 3.549   -24.509 1.360   1.00 34.32  ? 21  TRP   A CE2 1 
ATOM   168  C CE3 . TRP   A 1 22 ? 1.181   -24.724 1.841   1.00 34.59  ? 21  TRP   A CE3 1 
ATOM   169  C CZ2 . TRP   A 1 22 ? 3.778   -25.861 1.649   1.00 34.26  ? 21  TRP   A CZ2 1 
ATOM   170  C CZ3 . TRP   A 1 22 ? 1.415   -26.059 2.122   1.00 38.39  ? 21  TRP   A CZ3 1 
ATOM   171  C CH2 . TRP   A 1 22 ? 2.697   -26.621 2.029   1.00 36.35  ? 21  TRP   A CH2 1 
ATOM   172  N N   . PRO   A 1 23 ? 3.553   -19.544 2.730   1.00 24.46  ? 22  PRO   A N   1 
ATOM   173  C CA  . PRO   A 1 23 ? 4.627   -18.557 2.547   1.00 24.21  ? 22  PRO   A CA  1 
ATOM   174  C C   . PRO   A 1 23 ? 5.100   -18.567 1.090   1.00 22.94  ? 22  PRO   A C   1 
ATOM   175  O O   . PRO   A 1 23 ? 5.338   -19.624 0.522   1.00 23.75  ? 22  PRO   A O   1 
ATOM   176  C CB  . PRO   A 1 23 ? 5.728   -19.008 3.543   1.00 24.17  ? 22  PRO   A CB  1 
ATOM   177  C CG  . PRO   A 1 23 ? 5.418   -20.496 3.767   1.00 23.55  ? 22  PRO   A CG  1 
ATOM   178  C CD  . PRO   A 1 23 ? 3.877   -20.537 3.764   1.00 24.31  ? 22  PRO   A CD  1 
ATOM   179  N N   . ALA   A 1 24 ? 5.211   -17.374 0.502   1.00 22.26  ? 23  ALA   A N   1 
ATOM   180  C CA  . ALA   A 1 24 ? 5.459   -17.222 -0.921  1.00 22.50  ? 23  ALA   A CA  1 
ATOM   181  C C   . ALA   A 1 24 ? 6.034   -15.833 -1.243  1.00 23.65  ? 23  ALA   A C   1 
ATOM   182  O O   . ALA   A 1 24 ? 6.122   -14.945 -0.406  1.00 24.19  ? 23  ALA   A O   1 
ATOM   183  C CB  . ALA   A 1 24 ? 4.158   -17.503 -1.699  1.00 22.19  ? 23  ALA   A CB  1 
ATOM   184  N N   . ARG   A 1 25 ? 6.479   -15.656 -2.489  1.00 24.18  ? 24  ARG   A N   1 
ATOM   185  C CA  . ARG   A 1 25 ? 6.922   -14.339 -2.893  1.00 22.52  ? 24  ARG   A CA  1 
ATOM   186  C C   . ARG   A 1 25 ? 6.390   -14.099 -4.304  1.00 21.48  ? 24  ARG   A C   1 
ATOM   187  O O   . ARG   A 1 25 ? 6.073   -15.053 -5.024  1.00 22.97  ? 24  ARG   A O   1 
ATOM   188  C CB  . ARG   A 1 25 ? 8.454   -14.199 -2.853  1.00 20.22  ? 24  ARG   A CB  1 
ATOM   189  C CG  . ARG   A 1 25 ? 9.126   -15.081 -3.901  1.00 19.92  ? 24  ARG   A CG  1 
ATOM   190  C CD  . ARG   A 1 25 ? 10.671  -14.982 -3.772  1.00 20.14  ? 24  ARG   A CD  1 
ATOM   191  N NE  . ARG   A 1 25 ? 11.392  -15.784 -4.781  1.00 21.92  ? 24  ARG   A NE  1 
ATOM   192  C CZ  . ARG   A 1 25 ? 12.693  -16.147 -4.691  1.00 24.75  ? 24  ARG   A CZ  1 
ATOM   193  N NH1 . ARG   A 1 25 ? 13.391  -15.988 -3.576  1.00 22.03  ? 24  ARG   A NH1 1 
ATOM   194  N NH2 . ARG   A 1 25 ? 13.252  -16.824 -5.677  1.00 26.97  ? 24  ARG   A NH2 1 
ATOM   195  N N   . ILE   A 1 26 ? 6.265   -12.825 -4.660  1.00 21.27  ? 25  ILE   A N   1 
ATOM   196  C CA  . ILE   A 1 26 ? 6.057   -12.459 -6.062  1.00 24.10  ? 25  ILE   A CA  1 
ATOM   197  C C   . ILE   A 1 26 ? 7.405   -12.581 -6.789  1.00 22.98  ? 25  ILE   A C   1 
ATOM   198  O O   . ILE   A 1 26 ? 8.367   -11.954 -6.368  1.00 25.22  ? 25  ILE   A O   1 
ATOM   199  C CB  . ILE   A 1 26 ? 5.563   -11.003 -6.168  1.00 26.72  ? 25  ILE   A CB  1 
ATOM   200  C CG1 . ILE   A 1 26 ? 4.397   -10.663 -5.212  1.00 30.32  ? 25  ILE   A CG1 1 
ATOM   201  C CG2 . ILE   A 1 26 ? 5.283   -10.621 -7.629  1.00 26.57  ? 25  ILE   A CG2 1 
ATOM   202  C CD1 . ILE   A 1 26 ? 3.039   -11.092 -5.679  1.00 33.42  ? 25  ILE   A CD1 1 
ATOM   203  N N   . ASP   A 1 27 ? 7.473   -13.364 -7.872  1.00 22.58  ? 26  ASP   A N   1 
ATOM   204  C CA  . ASP   A 1 27 ? 8.713   -13.546 -8.612  1.00 27.38  ? 26  ASP   A CA  1 
ATOM   205  C C   . ASP   A 1 27 ? 8.809   -12.542 -9.755  1.00 27.96  ? 26  ASP   A C   1 
ATOM   206  O O   . ASP   A 1 27 ? 7.811   -11.961 -10.177 1.00 28.53  ? 26  ASP   A O   1 
ATOM   207  C CB  . ASP   A 1 27 ? 8.860   -14.945 -9.212  1.00 27.08  ? 26  ASP   A CB  1 
ATOM   208  C CG  . ASP   A 1 27 ? 9.773   -15.905 -8.463  1.00 28.01  ? 26  ASP   A CG  1 
ATOM   209  O OD1 . ASP   A 1 27 ? 10.336  -15.504 -7.433  1.00 31.94  ? 26  ASP   A OD1 1 
ATOM   210  O OD2 . ASP   A 1 27 ? 9.910   -17.060 -8.892  1.00 31.80  ? 26  ASP   A OD2 1 
ATOM   211  N N   . ASP   A 1 28 ? 10.046  -12.339 -10.228 1.00 30.47  ? 27  ASP   A N   1 
ATOM   212  C CA  . ASP   A 1 28 ? 10.280  -11.680 -11.499 1.00 36.19  ? 27  ASP   A CA  1 
ATOM   213  C C   . ASP   A 1 28 ? 10.008  -12.722 -12.583 1.00 31.15  ? 27  ASP   A C   1 
ATOM   214  O O   . ASP   A 1 28 ? 10.019  -13.914 -12.306 1.00 35.21  ? 27  ASP   A O   1 
ATOM   215  C CB  . ASP   A 1 28 ? 11.739  -11.250 -11.613 1.00 41.19  ? 27  ASP   A CB  1 
ATOM   216  C CG  . ASP   A 1 28 ? 12.160  -10.041 -10.784 1.00 49.28  ? 27  ASP   A CG  1 
ATOM   217  O OD1 . ASP   A 1 28 ? 11.773  -8.914  -11.157 1.00 50.55  ? 27  ASP   A OD1 1 
ATOM   218  O OD2 . ASP   A 1 28 ? 12.878  -10.231 -9.774  1.00 62.62  ? 27  ASP   A OD2 1 
ATOM   219  N N   . ILE   A 1 29 ? 9.724   -12.273 -13.799 1.00 35.39  ? 28  ILE   A N   1 
ATOM   220  C CA  . ILE   A 1 29 ? 9.786   -13.172 -14.943 1.00 35.33  ? 28  ILE   A CA  1 
ATOM   221  C C   . ILE   A 1 29 ? 11.161  -12.985 -15.586 1.00 34.14  ? 28  ILE   A C   1 
ATOM   222  O O   . ILE   A 1 29 ? 11.559  -11.848 -15.845 1.00 34.78  ? 28  ILE   A O   1 
ATOM   223  C CB  . ILE   A 1 29 ? 8.673   -12.803 -15.930 1.00 37.33  ? 28  ILE   A CB  1 
ATOM   224  C CG1 . ILE   A 1 29 ? 7.318   -12.771 -15.231 1.00 38.55  ? 28  ILE   A CG1 1 
ATOM   225  C CG2 . ILE   A 1 29 ? 8.683   -13.765 -17.125 1.00 34.75  ? 28  ILE   A CG2 1 
ATOM   226  C CD1 . ILE   A 1 29 ? 6.467   -11.584 -15.635 1.00 39.11  ? 28  ILE   A CD1 1 
ATOM   227  N N   . ALA   A 1 30 ? 11.901  -14.085 -15.779 1.00 36.30  ? 29  ALA   A N   1 
ATOM   228  C CA  . ALA   A 1 30 ? 13.234  -14.002 -16.365 1.00 37.10  ? 29  ALA   A CA  1 
ATOM   229  C C   . ALA   A 1 30 ? 13.093  -13.666 -17.857 1.00 36.53  ? 29  ALA   A C   1 
ATOM   230  O O   . ALA   A 1 30 ? 12.075  -13.989 -18.481 1.00 35.63  ? 29  ALA   A O   1 
ATOM   231  C CB  . ALA   A 1 30 ? 13.967  -15.313 -16.148 1.00 35.31  ? 29  ALA   A CB  1 
ATOM   232  N N   . ASP   A 1 31 ? 14.096  -12.969 -18.410 1.00 36.87  ? 30  ASP   A N   1 
ATOM   233  C CA  . ASP   A 1 31 ? 14.172  -12.791 -19.858 1.00 34.62  ? 30  ASP   A CA  1 
ATOM   234  C C   . ASP   A 1 31 ? 14.069  -14.165 -20.503 1.00 26.47  ? 30  ASP   A C   1 
ATOM   235  O O   . ASP   A 1 31 ? 14.751  -15.087 -20.074 1.00 29.80  ? 30  ASP   A O   1 
ATOM   236  C CB  . ASP   A 1 31 ? 15.517  -12.205 -20.264 1.00 37.02  ? 30  ASP   A CB  1 
ATOM   237  C CG  . ASP   A 1 31 ? 15.677  -10.705 -20.063 1.00 39.43  ? 30  ASP   A CG  1 
ATOM   238  O OD1 . ASP   A 1 31 ? 14.648  -10.023 -19.899 1.00 44.34  ? 30  ASP   A OD1 1 
ATOM   239  O OD2 . ASP   A 1 31 ? 16.837  -10.230 -20.122 1.00 43.34  ? 30  ASP   A OD2 1 
ATOM   240  N N   . GLY   A 1 32 ? 13.203  -14.295 -21.520 1.00 29.96  ? 31  GLY   A N   1 
ATOM   241  C CA  . GLY   A 1 32 ? 13.081  -15.547 -22.254 1.00 30.96  ? 31  GLY   A CA  1 
ATOM   242  C C   . GLY   A 1 32 ? 12.056  -16.521 -21.668 1.00 38.28  ? 31  GLY   A C   1 
ATOM   243  O O   . GLY   A 1 32 ? 11.761  -17.543 -22.297 1.00 37.30  ? 31  GLY   A O   1 
ATOM   244  N N   . ALA   A 1 33 ? 11.539  -16.236 -20.460 1.00 30.74  ? 32  ALA   A N   1 
ATOM   245  C CA  . ALA   A 1 33 ? 10.664  -17.192 -19.785 1.00 35.43  ? 32  ALA   A CA  1 
ATOM   246  C C   . ALA   A 1 33 ? 9.184   -16.908 -20.041 1.00 34.73  ? 32  ALA   A C   1 
ATOM   247  O O   . ALA   A 1 33 ? 8.780   -15.803 -20.405 1.00 33.32  ? 32  ALA   A O   1 
ATOM   248  C CB  . ALA   A 1 33 ? 10.967  -17.254 -18.290 1.00 36.17  ? 32  ALA   A CB  1 
ATOM   249  N N   . VAL   A 1 34 ? 8.354   -17.918 -19.779 1.00 39.61  ? 33  VAL   A N   1 
ATOM   250  C CA  . VAL   A 1 34 ? 6.914   -17.807 -19.971 1.00 38.06  ? 33  VAL   A CA  1 
ATOM   251  C C   . VAL   A 1 34 ? 6.316   -16.753 -19.035 1.00 34.14  ? 33  VAL   A C   1 
ATOM   252  O O   . VAL   A 1 34 ? 6.540   -16.787 -17.831 1.00 35.42  ? 33  VAL   A O   1 
ATOM   253  C CB  . VAL   A 1 34 ? 6.299   -19.202 -19.745 1.00 42.35  ? 33  VAL   A CB  1 
ATOM   254  C CG1 . VAL   A 1 34 ? 4.778   -19.162 -19.783 1.00 45.24  ? 33  VAL   A CG1 1 
ATOM   255  C CG2 . VAL   A 1 34 ? 6.831   -20.216 -20.759 1.00 42.80  ? 33  VAL   A CG2 1 
ATOM   256  N N   . LYS   A 1 35 ? 5.558   -15.815 -19.612 1.00 34.93  ? 34  LYS   A N   1 
ATOM   257  C CA  . LYS   A 1 35 ? 4.851   -14.769 -18.878 1.00 38.64  ? 34  LYS   A CA  1 
ATOM   258  C C   . LYS   A 1 35 ? 3.535   -15.314 -18.319 1.00 40.17  ? 34  LYS   A C   1 
ATOM   259  O O   . LYS   A 1 35 ? 2.984   -16.276 -18.840 1.00 33.77  ? 34  LYS   A O   1 
ATOM   260  C CB  . LYS   A 1 35 ? 4.510   -13.569 -19.770 1.00 36.76  ? 34  LYS   A CB  1 
ATOM   261  C CG  . LYS   A 1 35 ? 5.741   -12.788 -20.270 1.00 35.60  ? 34  LYS   A CG  1 
ATOM   262  C CD  . LYS   A 1 35 ? 5.403   -11.657 -21.231 1.00 40.31  ? 34  LYS   A CD  1 
ATOM   263  C CE  . LYS   A 1 35 ? 5.304   -12.090 -22.649 1.00 46.54  ? 34  LYS   A CE  1 
ATOM   264  N NZ  . LYS   A 1 35 ? 5.054   -10.919 -23.488 1.00 49.94  ? 34  LYS   A NZ  1 
ATOM   265  N N   . PRO   A 1 36 ? 2.995   -14.737 -17.220 1.00 41.10  ? 35  PRO   A N   1 
ATOM   266  C CA  . PRO   A 1 36 ? 1.760   -15.242 -16.624 1.00 36.87  ? 35  PRO   A CA  1 
ATOM   267  C C   . PRO   A 1 36 ? 0.612   -14.738 -17.494 1.00 37.34  ? 35  PRO   A C   1 
ATOM   268  O O   . PRO   A 1 36 ? 0.820   -13.856 -18.319 1.00 40.44  ? 35  PRO   A O   1 
ATOM   269  C CB  . PRO   A 1 36 ? 1.707   -14.593 -15.221 1.00 37.52  ? 35  PRO   A CB  1 
ATOM   270  C CG  . PRO   A 1 36 ? 2.730   -13.467 -15.226 1.00 42.84  ? 35  PRO   A CG  1 
ATOM   271  C CD  . PRO   A 1 36 ? 3.526   -13.561 -16.516 1.00 43.70  ? 35  PRO   A CD  1 
ATOM   272  N N   . PRO   A 1 37 ? -0.643  -15.205 -17.279 1.00 40.06  ? 36  PRO   A N   1 
ATOM   273  C CA  . PRO   A 1 37 ? -1.807  -14.585 -17.916 1.00 42.78  ? 36  PRO   A CA  1 
ATOM   274  C C   . PRO   A 1 37 ? -1.965  -13.160 -17.415 1.00 43.30  ? 36  PRO   A C   1 
ATOM   275  O O   . PRO   A 1 37 ? -1.437  -12.817 -16.348 1.00 36.28  ? 36  PRO   A O   1 
ATOM   276  C CB  . PRO   A 1 37 ? -2.985  -15.459 -17.480 1.00 39.45  ? 36  PRO   A CB  1 
ATOM   277  C CG  . PRO   A 1 37 ? -2.344  -16.748 -17.082 1.00 37.52  ? 36  PRO   A CG  1 
ATOM   278  C CD  . PRO   A 1 37 ? -1.013  -16.365 -16.450 1.00 39.05  ? 36  PRO   A CD  1 
ATOM   279  N N   . PRO   A 1 38 ? -2.690  -12.299 -18.166 1.00 44.32  ? 37  PRO   A N   1 
ATOM   280  C CA  . PRO   A 1 38 ? -3.038  -10.961 -17.688 1.00 46.21  ? 37  PRO   A CA  1 
ATOM   281  C C   . PRO   A 1 38 ? -3.701  -11.009 -16.311 1.00 41.74  ? 37  PRO   A C   1 
ATOM   282  O O   . PRO   A 1 38 ? -4.408  -11.955 -15.981 1.00 42.47  ? 37  PRO   A O   1 
ATOM   283  C CB  . PRO   A 1 38 ? -4.000  -10.408 -18.765 1.00 50.16  ? 37  PRO   A CB  1 
ATOM   284  C CG  . PRO   A 1 38 ? -4.418  -11.622 -19.559 1.00 47.59  ? 37  PRO   A CG  1 
ATOM   285  C CD  . PRO   A 1 38 ? -3.223  -12.568 -19.518 1.00 50.65  ? 37  PRO   A CD  1 
ATOM   286  N N   . ASN   A 1 39 ? -3.412  -9.980  -15.518 1.00 41.04  ? 38  ASN   A N   1 
ATOM   287  C CA  . ASN   A 1 39 ? -3.947  -9.786  -14.184 1.00 44.40  ? 38  ASN   A CA  1 
ATOM   288  C C   . ASN   A 1 39 ? -3.451  -10.851 -13.206 1.00 39.06  ? 38  ASN   A C   1 
ATOM   289  O O   . ASN   A 1 39 ? -3.911  -10.855 -12.067 1.00 40.43  ? 38  ASN   A O   1 
ATOM   290  C CB  . ASN   A 1 39 ? -5.456  -9.571  -14.210 1.00 50.45  ? 38  ASN   A CB  1 
ATOM   291  C CG  . ASN   A 1 39 ? -5.793  -8.348  -15.027 1.00 55.18  ? 38  ASN   A CG  1 
ATOM   292  O OD1 . ASN   A 1 39 ? -5.579  -7.217  -14.577 1.00 54.15  ? 38  ASN   A OD1 1 
ATOM   293  N ND2 . ASN   A 1 39 ? -6.278  -8.558  -16.238 1.00 59.45  ? 38  ASN   A ND2 1 
ATOM   294  N N   . LYS   A 1 40 ? -2.507  -11.714 -13.623 1.00 32.99  ? 39  LYS   A N   1 
ATOM   295  C CA  . LYS   A 1 40 ? -1.951  -12.714 -12.709 1.00 29.64  ? 39  LYS   A CA  1 
ATOM   296  C C   . LYS   A 1 40 ? -0.474  -12.413 -12.434 1.00 27.56  ? 39  LYS   A C   1 
ATOM   297  O O   . LYS   A 1 40 ? 0.221   -11.897 -13.301 1.00 29.65  ? 39  LYS   A O   1 
ATOM   298  C CB  . LYS   A 1 40 ? -2.109  -14.170 -13.164 1.00 34.30  ? 39  LYS   A CB  1 
ATOM   299  C CG  . LYS   A 1 40 ? -3.533  -14.633 -13.473 1.00 39.60  ? 39  LYS   A CG  1 
ATOM   300  C CD  . LYS   A 1 40 ? -4.442  -14.602 -12.251 1.00 44.07  ? 39  LYS   A CD  1 
ATOM   301  C CE  . LYS   A 1 40 ? -5.874  -14.998 -12.542 1.00 47.99  ? 39  LYS   A CE  1 
ATOM   302  N NZ  . LYS   A 1 40 ? -6.082  -16.434 -12.744 1.00 45.16  ? 39  LYS   A NZ  1 
ATOM   303  N N   . TYR   A 1 41 ? -0.006  -12.776 -11.233 1.00 22.83  ? 40  TYR   A N   1 
ATOM   304  C CA  . TYR   A 1 41 ? 1.396   -12.661 -10.858 1.00 24.17  ? 40  TYR   A CA  1 
ATOM   305  C C   . TYR   A 1 41 ? 2.018   -14.038 -10.767 1.00 24.15  ? 40  TYR   A C   1 
ATOM   306  O O   . TYR   A 1 41 ? 1.339   -14.983 -10.397 1.00 24.43  ? 40  TYR   A O   1 
ATOM   307  C CB  . TYR   A 1 41 ? 1.539   -12.091 -9.441  1.00 25.11  ? 40  TYR   A CB  1 
ATOM   308  C CG  . TYR   A 1 41 ? 1.113   -10.640 -9.428  1.00 27.99  ? 40  TYR   A CG  1 
ATOM   309  C CD1 . TYR   A 1 41 ? -0.229  -10.316 -9.249  1.00 32.44  ? 40  TYR   A CD1 1 
ATOM   310  C CD2 . TYR   A 1 41 ? 2.021   -9.614  -9.623  1.00 29.33  ? 40  TYR   A CD2 1 
ATOM   311  C CE1 . TYR   A 1 41 ? -0.665  -9.004  -9.298  1.00 35.71  ? 40  TYR   A CE1 1 
ATOM   312  C CE2 . TYR   A 1 41 ? 1.595   -8.290  -9.651  1.00 33.45  ? 40  TYR   A CE2 1 
ATOM   313  C CZ  . TYR   A 1 41 ? 0.255   -7.990  -9.459  1.00 35.09  ? 40  TYR   A CZ  1 
ATOM   314  O OH  . TYR   A 1 41 ? -0.228  -6.711  -9.491  1.00 37.43  ? 40  TYR   A OH  1 
ATOM   315  N N   . PRO   A 1 42 ? 3.334   -14.195 -11.044 1.00 23.69  ? 41  PRO   A N   1 
ATOM   316  C CA  . PRO   A 1 42 ? 3.989   -15.490 -10.857 1.00 21.89  ? 41  PRO   A CA  1 
ATOM   317  C C   . PRO   A 1 42 ? 4.293   -15.611 -9.373  1.00 23.72  ? 41  PRO   A C   1 
ATOM   318  O O   . PRO   A 1 42 ? 4.992   -14.756 -8.837  1.00 24.83  ? 41  PRO   A O   1 
ATOM   319  C CB  . PRO   A 1 42 ? 5.279   -15.378 -11.690 1.00 24.65  ? 41  PRO   A CB  1 
ATOM   320  C CG  . PRO   A 1 42 ? 5.484   -13.902 -11.882 1.00 24.45  ? 41  PRO   A CG  1 
ATOM   321  C CD  . PRO   A 1 42 ? 4.232   -13.127 -11.507 1.00 28.59  ? 41  PRO   A CD  1 
ATOM   322  N N   . ILE   A 1 43 ? 3.783   -16.659 -8.732  1.00 22.89  ? 42  ILE   A N   1 
ATOM   323  C CA  . ILE   A 1 43 ? 4.013   -16.797 -7.302  1.00 22.47  ? 42  ILE   A CA  1 
ATOM   324  C C   . ILE   A 1 43 ? 4.977   -17.946 -7.052  1.00 25.99  ? 42  ILE   A C   1 
ATOM   325  O O   . ILE   A 1 43 ? 4.704   -19.067 -7.497  1.00 26.88  ? 42  ILE   A O   1 
ATOM   326  C CB  . ILE   A 1 43 ? 2.678   -17.029 -6.584  1.00 21.47  ? 42  ILE   A CB  1 
ATOM   327  C CG1 . ILE   A 1 43 ? 1.697   -15.882 -6.876  1.00 21.85  ? 42  ILE   A CG1 1 
ATOM   328  C CG2 . ILE   A 1 43 ? 2.924   -17.242 -5.075  1.00 21.04  ? 42  ILE   A CG2 1 
ATOM   329  C CD1 . ILE   A 1 43 ? 2.178   -14.479 -6.509  1.00 23.25  ? 42  ILE   A CD1 1 
ATOM   330  N N   . PHE   A 1 44 ? 6.065   -17.681 -6.298  1.00 22.80  ? 43  PHE   A N   1 
ATOM   331  C CA  . PHE   A 1 44 ? 6.975   -18.759 -5.930  1.00 23.55  ? 43  PHE   A CA  1 
ATOM   332  C C   . PHE   A 1 44 ? 6.699   -19.160 -4.486  1.00 23.27  ? 43  PHE   A C   1 
ATOM   333  O O   . PHE   A 1 44 ? 6.719   -18.309 -3.610  1.00 23.52  ? 43  PHE   A O   1 
ATOM   334  C CB  . PHE   A 1 44 ? 8.436   -18.287 -6.073  1.00 23.60  ? 43  PHE   A CB  1 
ATOM   335  C CG  . PHE   A 1 44 ? 9.450   -19.345 -5.636  1.00 26.42  ? 43  PHE   A CG  1 
ATOM   336  C CD1 . PHE   A 1 44 ? 9.811   -20.381 -6.496  1.00 28.87  ? 43  PHE   A CD1 1 
ATOM   337  C CD2 . PHE   A 1 44 ? 10.049  -19.302 -4.373  1.00 27.55  ? 43  PHE   A CD2 1 
ATOM   338  C CE1 . PHE   A 1 44 ? 10.744  -21.342 -6.112  1.00 31.16  ? 43  PHE   A CE1 1 
ATOM   339  C CE2 . PHE   A 1 44 ? 10.965  -20.276 -3.981  1.00 29.84  ? 43  PHE   A CE2 1 
ATOM   340  C CZ  . PHE   A 1 44 ? 11.324  -21.296 -4.859  1.00 29.98  ? 43  PHE   A CZ  1 
ATOM   341  N N   . PHE   A 1 45 ? 6.335   -20.435 -4.258  1.00 23.71  ? 44  PHE   A N   1 
ATOM   342  C CA  . PHE   A 1 45 ? 5.936   -20.939 -2.951  1.00 22.67  ? 44  PHE   A CA  1 
ATOM   343  C C   . PHE   A 1 45 ? 7.212   -21.438 -2.275  1.00 23.52  ? 44  PHE   A C   1 
ATOM   344  O O   . PHE   A 1 45 ? 7.907   -22.303 -2.827  1.00 25.65  ? 44  PHE   A O   1 
ATOM   345  C CB  . PHE   A 1 45 ? 4.930   -22.103 -3.092  1.00 25.80  ? 44  PHE   A CB  1 
ATOM   346  C CG  . PHE   A 1 45 ? 3.564   -21.604 -3.561  1.00 28.65  ? 44  PHE   A CG  1 
ATOM   347  C CD1 . PHE   A 1 45 ? 3.312   -21.387 -4.923  1.00 28.75  ? 44  PHE   A CD1 1 
ATOM   348  C CD2 . PHE   A 1 45 ? 2.567   -21.283 -2.641  1.00 28.16  ? 44  PHE   A CD2 1 
ATOM   349  C CE1 . PHE   A 1 45 ? 2.105   -20.841 -5.353  1.00 27.50  ? 44  PHE   A CE1 1 
ATOM   350  C CE2 . PHE   A 1 45 ? 1.341   -20.781 -3.073  1.00 27.85  ? 44  PHE   A CE2 1 
ATOM   351  C CZ  . PHE   A 1 45 ? 1.106   -20.570 -4.432  1.00 28.45  ? 44  PHE   A CZ  1 
ATOM   352  N N   . PHE   A 1 46 ? 7.559   -20.847 -1.128  1.00 22.20  ? 45  PHE   A N   1 
ATOM   353  C CA  . PHE   A 1 46 ? 8.666   -21.348 -0.323  1.00 27.39  ? 45  PHE   A CA  1 
ATOM   354  C C   . PHE   A 1 46 ? 8.388   -22.778 0.159   1.00 26.95  ? 45  PHE   A C   1 
ATOM   355  O O   . PHE   A 1 46 ? 7.229   -23.209 0.278   1.00 27.42  ? 45  PHE   A O   1 
ATOM   356  C CB  . PHE   A 1 46 ? 8.972   -20.422 0.862   1.00 24.08  ? 45  PHE   A CB  1 
ATOM   357  C CG  . PHE   A 1 46 ? 9.396   -19.025 0.438   1.00 24.36  ? 45  PHE   A CG  1 
ATOM   358  C CD1 . PHE   A 1 46 ? 10.655  -18.808 -0.138  1.00 23.41  ? 45  PHE   A CD1 1 
ATOM   359  C CD2 . PHE   A 1 46 ? 8.577   -17.922 0.675   1.00 21.69  ? 45  PHE   A CD2 1 
ATOM   360  C CE1 . PHE   A 1 46 ? 11.055  -17.522 -0.532  1.00 24.69  ? 45  PHE   A CE1 1 
ATOM   361  C CE2 . PHE   A 1 46 ? 8.993   -16.625 0.298   1.00 23.01  ? 45  PHE   A CE2 1 
ATOM   362  C CZ  . PHE   A 1 46 ? 10.236  -16.423 -0.300  1.00 23.58  ? 45  PHE   A CZ  1 
ATOM   363  N N   . GLY   A 1 47 ? 9.469   -23.545 0.346   1.00 26.65  ? 46  GLY   A N   1 
ATOM   364  C CA  . GLY   A 1 47 ? 9.334   -24.897 0.882   1.00 28.67  ? 46  GLY   A CA  1 
ATOM   365  C C   . GLY   A 1 47 ? 9.114   -25.932 -0.226  1.00 36.00  ? 46  GLY   A C   1 
ATOM   366  O O   . GLY   A 1 47 ? 9.939   -26.838 -0.390  1.00 35.31  ? 46  GLY   A O   1 
ATOM   367  N N   . THR   A 1 48 ? 8.001   -25.807 -0.967  1.00 32.24  ? 47  THR   A N   1 
ATOM   368  C CA  . THR   A 1 48 ? 7.712   -26.663 -2.114  1.00 31.43  ? 47  THR   A CA  1 
ATOM   369  C C   . THR   A 1 48 ? 8.552   -26.237 -3.316  1.00 29.31  ? 47  THR   A C   1 
ATOM   370  O O   . THR   A 1 48 ? 8.874   -27.045 -4.187  1.00 30.11  ? 47  THR   A O   1 
ATOM   371  C CB  . THR   A 1 48 ? 6.223   -26.642 -2.463  1.00 32.48  ? 47  THR   A CB  1 
ATOM   372  O OG1 . THR   A 1 48 ? 5.923   -25.277 -2.730  1.00 33.75  ? 47  THR   A OG1 1 
ATOM   373  C CG2 . THR   A 1 48 ? 5.332   -27.147 -1.347  1.00 33.92  ? 47  THR   A CG2 1 
ATOM   374  N N   . HIS   A 1 49 ? 8.839   -24.934 -3.410  1.00 28.53  ? 48  HIS   A N   1 
ATOM   375  C CA  . HIS   A 1 49 ? 9.558   -24.338 -4.532  1.00 30.43  ? 48  HIS   A CA  1 
ATOM   376  C C   . HIS   A 1 49 ? 8.763   -24.440 -5.831  1.00 33.25  ? 48  HIS   A C   1 
ATOM   377  O O   . HIS   A 1 49 ? 9.371   -24.414 -6.892  1.00 34.06  ? 48  HIS   A O   1 
ATOM   378  C CB  . HIS   A 1 49 ? 10.995  -24.890 -4.673  1.00 28.98  ? 48  HIS   A CB  1 
ATOM   379  C CG  . HIS   A 1 49 ? 11.712  -24.914 -3.369  1.00 29.63  ? 48  HIS   A CG  1 
ATOM   380  N ND1 . HIS   A 1 49 ? 12.405  -26.005 -2.911  1.00 34.98  ? 48  HIS   A ND1 1 
ATOM   381  C CD2 . HIS   A 1 49 ? 11.753  -23.989 -2.365  1.00 28.81  ? 48  HIS   A CD2 1 
ATOM   382  C CE1 . HIS   A 1 49 ? 12.874  -25.744 -1.689  1.00 38.86  ? 48  HIS   A CE1 1 
ATOM   383  N NE2 . HIS   A 1 49 ? 12.523  -24.504 -1.360  1.00 32.44  ? 48  HIS   A NE2 1 
ATOM   384  N N   . GLU   A 1 50 ? 7.426   -24.526 -5.752  1.00 35.40  ? 49  GLU   A N   1 
ATOM   385  C CA  . GLU   A 1 50 ? 6.557   -24.526 -6.929  1.00 30.71  ? 49  GLU   A CA  1 
ATOM   386  C C   . GLU   A 1 50 ? 6.174   -23.089 -7.309  1.00 31.37  ? 49  GLU   A C   1 
ATOM   387  O O   . GLU   A 1 50 ? 6.342   -22.180 -6.494  1.00 29.20  ? 49  GLU   A O   1 
ATOM   388  C CB  . GLU   A 1 50 ? 5.340   -25.419 -6.674  1.00 34.00  ? 49  GLU   A CB  1 
ATOM   389  C CG  . GLU   A 1 50 ? 5.738   -26.869 -6.392  1.00 43.01  ? 49  GLU   A CG  1 
ATOM   390  C CD  . GLU   A 1 50 ? 4.599   -27.751 -5.930  1.00 50.85  ? 49  GLU   A CD  1 
ATOM   391  O OE1 . GLU   A 1 50 ? 3.426   -27.369 -6.119  1.00 48.65  ? 49  GLU   A OE1 1 
ATOM   392  O OE2 . GLU   A 1 50 ? 4.894   -28.806 -5.334  1.00 55.02  ? 49  GLU   A OE2 1 
ATOM   393  N N   . THR   A 1 51 ? 5.784   -22.880 -8.578  1.00 27.56  ? 50  THR   A N   1 
ATOM   394  C CA  . THR   A 1 51 ? 5.233   -21.618 -9.081  1.00 30.45  ? 50  THR   A CA  1 
ATOM   395  C C   . THR   A 1 51 ? 3.787   -21.827 -9.518  1.00 32.01  ? 50  THR   A C   1 
ATOM   396  O O   . THR   A 1 51 ? 3.484   -22.794 -10.221 1.00 35.66  ? 50  THR   A O   1 
ATOM   397  C CB  . THR   A 1 51 ? 6.043   -21.061 -10.261 1.00 33.23  ? 50  THR   A CB  1 
ATOM   398  O OG1 . THR   A 1 51 ? 7.371   -20.786 -9.824  1.00 32.28  ? 50  THR   A OG1 1 
ATOM   399  C CG2 . THR   A 1 51 ? 5.420   -19.793 -10.841 1.00 32.62  ? 50  THR   A CG2 1 
ATOM   400  N N   . ALA   A 1 52 ? 2.895   -20.918 -9.121  1.00 28.37  ? 51  ALA   A N   1 
ATOM   401  C CA  . ALA   A 1 52 ? 1.584   -20.830 -9.753  1.00 29.19  ? 51  ALA   A CA  1 
ATOM   402  C C   . ALA   A 1 52 ? 1.295   -19.368 -10.061 1.00 28.49  ? 51  ALA   A C   1 
ATOM   403  O O   . ALA   A 1 52 ? 1.988   -18.490 -9.570  1.00 26.75  ? 51  ALA   A O   1 
ATOM   404  C CB  . ALA   A 1 52 ? 0.465   -21.406 -8.894  1.00 30.79  ? 51  ALA   A CB  1 
ATOM   405  N N   . PHE   A 1 53 ? 0.255   -19.122 -10.874 1.00 26.82  ? 52  PHE   A N   1 
ATOM   406  C CA  . PHE   A 1 53 ? -0.120  -17.764 -11.215 1.00 28.65  ? 52  PHE   A CA  1 
ATOM   407  C C   . PHE   A 1 53 ? -1.373  -17.398 -10.429 1.00 34.01  ? 52  PHE   A C   1 
ATOM   408  O O   . PHE   A 1 53 ? -2.402  -18.066 -10.583 1.00 32.67  ? 52  PHE   A O   1 
ATOM   409  C CB  . PHE   A 1 53 ? -0.408  -17.798 -12.720 1.00 28.72  ? 52  PHE   A CB  1 
ATOM   410  C CG  . PHE   A 1 53 ? 0.794   -18.127 -13.600 1.00 32.96  ? 52  PHE   A CG  1 
ATOM   411  C CD1 . PHE   A 1 53 ? 1.981   -17.414 -13.483 1.00 35.19  ? 52  PHE   A CD1 1 
ATOM   412  C CD2 . PHE   A 1 53 ? 0.717   -19.114 -14.578 1.00 37.47  ? 52  PHE   A CD2 1 
ATOM   413  C CE1 . PHE   A 1 53 ? 3.074   -17.707 -14.296 1.00 45.54  ? 52  PHE   A CE1 1 
ATOM   414  C CE2 . PHE   A 1 53 ? 1.814   -19.403 -15.387 1.00 40.30  ? 52  PHE   A CE2 1 
ATOM   415  C CZ  . PHE   A 1 53 ? 2.978   -18.689 -15.263 1.00 36.70  ? 52  PHE   A CZ  1 
ATOM   416  N N   . LEU   A 1 54 ? -1.295  -16.329 -9.619  1.00 29.15  ? 53  LEU   A N   1 
ATOM   417  C CA  . LEU   A 1 54 ? -2.431  -15.941 -8.795  1.00 30.75  ? 53  LEU   A CA  1 
ATOM   418  C C   . LEU   A 1 54 ? -2.720  -14.448 -8.951  1.00 28.48  ? 53  LEU   A C   1 
ATOM   419  O O   . LEU   A 1 54 ? -1.827  -13.664 -9.279  1.00 27.76  ? 53  LEU   A O   1 
ATOM   420  C CB  . LEU   A 1 54 ? -2.183  -16.272 -7.318  1.00 28.04  ? 53  LEU   A CB  1 
ATOM   421  C CG  . LEU   A 1 54 ? -2.076  -17.747 -6.933  1.00 29.74  ? 53  LEU   A CG  1 
ATOM   422  C CD1 . LEU   A 1 54 ? -1.769  -17.795 -5.439  1.00 30.63  ? 53  LEU   A CD1 1 
ATOM   423  C CD2 . LEU   A 1 54 ? -3.371  -18.499 -7.225  1.00 32.31  ? 53  LEU   A CD2 1 
ATOM   424  N N   . GLY   A 1 55 ? -3.992  -14.062 -8.701  1.00 26.43  ? 54  GLY   A N   1 
ATOM   425  C CA  . GLY   A 1 55 ? -4.377  -12.653 -8.688  1.00 25.11  ? 54  GLY   A CA  1 
ATOM   426  C C   . GLY   A 1 55 ? -4.386  -12.149 -7.236  1.00 23.17  ? 54  GLY   A C   1 
ATOM   427  O O   . GLY   A 1 55 ? -4.307  -12.962 -6.314  1.00 25.03  ? 54  GLY   A O   1 
ATOM   428  N N   . PRO   A 1 56 ? -4.450  -10.823 -7.016  1.00 23.43  ? 55  PRO   A N   1 
ATOM   429  C CA  . PRO   A 1 56 ? -4.391  -10.246 -5.671  1.00 26.65  ? 55  PRO   A CA  1 
ATOM   430  C C   . PRO   A 1 56 ? -5.348  -10.786 -4.615  1.00 25.15  ? 55  PRO   A C   1 
ATOM   431  O O   . PRO   A 1 56 ? -5.021  -10.760 -3.432  1.00 25.02  ? 55  PRO   A O   1 
ATOM   432  C CB  . PRO   A 1 56 ? -4.570  -8.762  -5.917  1.00 26.11  ? 55  PRO   A CB  1 
ATOM   433  C CG  . PRO   A 1 56 ? -4.048  -8.593  -7.314  1.00 26.73  ? 55  PRO   A CG  1 
ATOM   434  C CD  . PRO   A 1 56 ? -4.541  -9.798  -8.073  1.00 23.45  ? 55  PRO   A CD  1 
ATOM   435  N N   . LYS   A 1 57 ? -6.521  -11.294 -5.034  1.00 26.12  ? 56  LYS   A N   1 
ATOM   436  C CA  . LYS   A 1 57 ? -7.483  -11.808 -4.056  1.00 27.70  ? 56  LYS   A CA  1 
ATOM   437  C C   . LYS   A 1 57 ? -6.913  -12.979 -3.245  1.00 26.98  ? 56  LYS   A C   1 
ATOM   438  O O   . LYS   A 1 57 ? -7.383  -13.250 -2.137  1.00 23.65  ? 56  LYS   A O   1 
ATOM   439  C CB  . LYS   A 1 57 ? -8.772  -12.306 -4.724  1.00 27.93  ? 56  LYS   A CB  1 
ATOM   440  C CG  . LYS   A 1 57 ? -8.602  -13.527 -5.635  1.00 30.71  ? 56  LYS   A CG  1 
ATOM   441  C CD  . LYS   A 1 57 ? -9.934  -13.821 -6.327  1.00 43.74  ? 56  LYS   A CD  1 
ATOM   442  C CE  . LYS   A 1 57 ? -9.841  -15.054 -7.147  1.00 45.71  ? 56  LYS   A CE  1 
ATOM   443  N NZ  . LYS   A 1 57 ? -9.666  -16.208 -6.256  1.00 49.34  ? 56  LYS   A NZ  1 
ATOM   444  N N   . ASP   A 1 58 ? -5.864  -13.642 -3.761  1.00 25.56  ? 57  ASP   A N   1 
ATOM   445  C CA  . ASP   A 1 58 ? -5.288  -14.788 -3.087  1.00 24.58  ? 57  ASP   A CA  1 
ATOM   446  C C   . ASP   A 1 58 ? -3.939  -14.470 -2.418  1.00 25.24  ? 57  ASP   A C   1 
ATOM   447  O O   . ASP   A 1 58 ? -3.275  -15.388 -1.917  1.00 25.32  ? 57  ASP   A O   1 
ATOM   448  C CB  . ASP   A 1 58 ? -5.215  -15.983 -4.035  1.00 25.07  ? 57  ASP   A CB  1 
ATOM   449  C CG  . ASP   A 1 58 ? -6.578  -16.561 -4.390  1.00 32.28  ? 57  ASP   A CG  1 
ATOM   450  O OD1 . ASP   A 1 58 ? -7.452  -16.522 -3.510  1.00 30.76  ? 57  ASP   A OD1 1 
ATOM   451  O OD2 . ASP   A 1 58 ? -6.772  -16.966 -5.550  1.00 32.12  ? 57  ASP   A OD2 1 
ATOM   452  N N   . LEU   A 1 59 ? -3.564  -13.179 -2.360  1.00 23.64  ? 58  LEU   A N   1 
ATOM   453  C CA  . LEU   A 1 59 ? -2.229  -12.748 -1.922  1.00 22.57  ? 58  LEU   A CA  1 
ATOM   454  C C   . LEU   A 1 59 ? -2.387  -11.886 -0.663  1.00 21.20  ? 58  LEU   A C   1 
ATOM   455  O O   . LEU   A 1 59 ? -2.968  -10.804 -0.715  1.00 22.10  ? 58  LEU   A O   1 
ATOM   456  C CB  . LEU   A 1 59 ? -1.544  -11.980 -3.059  1.00 20.94  ? 58  LEU   A CB  1 
ATOM   457  C CG  . LEU   A 1 59 ? -1.381  -12.748 -4.377  1.00 23.64  ? 58  LEU   A CG  1 
ATOM   458  C CD1 . LEU   A 1 59 ? -0.706  -11.935 -5.412  1.00 21.82  ? 58  LEU   A CD1 1 
ATOM   459  C CD2 . LEU   A 1 59 ? -0.609  -14.077 -4.173  1.00 22.10  ? 58  LEU   A CD2 1 
ATOM   460  N N   . PHE   A 1 60 ? -1.862  -12.377 0.471   1.00 21.44  ? 59  PHE   A N   1 
ATOM   461  C CA  . PHE   A 1 60 ? -1.910  -11.631 1.728   1.00 24.52  ? 59  PHE   A CA  1 
ATOM   462  C C   . PHE   A 1 60 ? -0.513  -11.132 2.121   1.00 23.32  ? 59  PHE   A C   1 
ATOM   463  O O   . PHE   A 1 60 ? 0.395   -11.931 2.333   1.00 25.93  ? 59  PHE   A O   1 
ATOM   464  C CB  . PHE   A 1 60 ? -2.426  -12.656 2.745   1.00 22.71  ? 59  PHE   A CB  1 
ATOM   465  C CG  . PHE   A 1 60 ? -3.860  -13.095 2.452   1.00 25.07  ? 59  PHE   A CG  1 
ATOM   466  C CD1 . PHE   A 1 60 ? -4.124  -14.018 1.444   1.00 23.82  ? 59  PHE   A CD1 1 
ATOM   467  C CD2 . PHE   A 1 60 ? -4.931  -12.613 3.215   1.00 27.00  ? 59  PHE   A CD2 1 
ATOM   468  C CE1 . PHE   A 1 60 ? -5.439  -14.411 1.165   1.00 29.58  ? 59  PHE   A CE1 1 
ATOM   469  C CE2 . PHE   A 1 60 ? -6.239  -13.017 2.947   1.00 28.32  ? 59  PHE   A CE2 1 
ATOM   470  C CZ  . PHE   A 1 60 ? -6.498  -13.927 1.937   1.00 26.19  ? 59  PHE   A CZ  1 
ATOM   471  N N   . PRO   A 1 61 ? -0.264  -9.809  2.209   1.00 26.95  ? 60  PRO   A N   1 
ATOM   472  C CA  . PRO   A 1 61 ? 1.059   -9.323  2.627   1.00 26.63  ? 60  PRO   A CA  1 
ATOM   473  C C   . PRO   A 1 61 ? 1.621   -9.950  3.909   1.00 26.21  ? 60  PRO   A C   1 
ATOM   474  O O   . PRO   A 1 61 ? 0.923   -10.071 4.912   1.00 25.86  ? 60  PRO   A O   1 
ATOM   475  C CB  . PRO   A 1 61 ? 0.845   -7.781  2.716   1.00 29.14  ? 60  PRO   A CB  1 
ATOM   476  C CG  . PRO   A 1 61 ? -0.194  -7.513  1.604   1.00 31.89  ? 60  PRO   A CG  1 
ATOM   477  C CD  . PRO   A 1 61 ? -1.161  -8.718  1.764   1.00 29.39  ? 60  PRO   A CD  1 
ATOM   478  N N   . TYR   A 1 62 ? 2.895   -10.375 3.847   1.00 25.47  ? 61  TYR   A N   1 
ATOM   479  C CA  . TYR   A 1 62 ? 3.504   -11.229 4.860   1.00 26.53  ? 61  TYR   A CA  1 
ATOM   480  C C   . TYR   A 1 62 ? 3.483   -10.571 6.242   1.00 26.59  ? 61  TYR   A C   1 
ATOM   481  O O   . TYR   A 1 62 ? 3.068   -11.208 7.214   1.00 29.75  ? 61  TYR   A O   1 
ATOM   482  C CB  . TYR   A 1 62 ? 4.915   -11.634 4.406   1.00 29.95  ? 61  TYR   A CB  1 
ATOM   483  C CG  . TYR   A 1 62 ? 5.674   -12.410 5.477   1.00 28.47  ? 61  TYR   A CG  1 
ATOM   484  C CD1 . TYR   A 1 62 ? 5.375   -13.742 5.751   1.00 28.84  ? 61  TYR   A CD1 1 
ATOM   485  C CD2 . TYR   A 1 62 ? 6.723   -11.819 6.171   1.00 31.57  ? 61  TYR   A CD2 1 
ATOM   486  C CE1 . TYR   A 1 62 ? 6.081   -14.471 6.697   1.00 30.31  ? 61  TYR   A CE1 1 
ATOM   487  C CE2 . TYR   A 1 62 ? 7.413   -12.523 7.147   1.00 32.57  ? 61  TYR   A CE2 1 
ATOM   488  C CZ  . TYR   A 1 62 ? 7.103   -13.846 7.393   1.00 33.55  ? 61  TYR   A CZ  1 
ATOM   489  O OH  . TYR   A 1 62 ? 7.789   -14.530 8.354   1.00 36.31  ? 61  TYR   A OH  1 
ATOM   490  N N   . ASP   A 1 63 ? 3.892   -9.305  6.295   1.00 29.59  ? 62  ASP   A N   1 
ATOM   491  C CA  . ASP   A 1 63 ? 4.091   -8.594  7.550   1.00 35.50  ? 62  ASP   A CA  1 
ATOM   492  C C   . ASP   A 1 63 ? 2.766   -8.511  8.314   1.00 36.40  ? 62  ASP   A C   1 
ATOM   493  O O   . ASP   A 1 63 ? 2.704   -8.881  9.481   1.00 40.07  ? 62  ASP   A O   1 
ATOM   494  C CB  . ASP   A 1 63 ? 4.832   -7.282  7.335   1.00 42.17  ? 62  ASP   A CB  1 
ATOM   495  C CG  . ASP   A 1 63 ? 6.361   -7.346  7.381   1.00 59.63  ? 62  ASP   A CG  1 
ATOM   496  O OD1 . ASP   A 1 63 ? 7.005   -6.421  6.830   1.00 74.62  ? 62  ASP   A OD1 1 
ATOM   497  O OD2 . ASP   A 1 63 ? 6.919   -8.276  8.018   1.00 69.62  ? 62  ASP   A OD2 1 
ATOM   498  N N   . LYS   A 1 64 ? 1.698   -8.110  7.621   1.00 39.79  ? 63  LYS   A N   1 
ATOM   499  C CA  . LYS   A 1 64 ? 0.368   -7.996  8.207   1.00 36.63  ? 63  LYS   A CA  1 
ATOM   500  C C   . LYS   A 1 64 ? -0.159  -9.358  8.670   1.00 35.16  ? 63  LYS   A C   1 
ATOM   501  O O   . LYS   A 1 64 ? -0.877  -9.402  9.672   1.00 33.20  ? 63  LYS   A O   1 
ATOM   502  C CB  . LYS   A 1 64 ? -0.561  -7.343  7.173   1.00 35.22  ? 63  LYS   A CB  1 
ATOM   503  C CG  . LYS   A 1 64 ? -2.027  -7.159  7.571   1.00 37.19  ? 63  LYS   A CG  1 
ATOM   504  C CD  . LYS   A 1 64 ? -2.859  -6.627  6.413   1.00 34.84  ? 63  LYS   A CD  1 
ATOM   505  C CE  . LYS   A 1 64 ? -3.979  -5.765  6.912   1.00 37.73  ? 63  LYS   A CE  1 
ATOM   506  N NZ  . LYS   A 1 64 ? -4.739  -6.345  8.015   1.00 42.22  ? 63  LYS   A NZ  1 
ATOM   507  N N   . SER   A 1 65 ? 0.217   -10.461 7.983   1.00 31.65  ? 64  SER   A N   1 
ATOM   508  C CA  . SER   A 1 65 ? -0.477  -11.744 8.103   1.00 30.36  ? 64  SER   A CA  1 
ATOM   509  C C   . SER   A 1 65 ? 0.276   -12.814 8.884   1.00 32.46  ? 64  SER   A C   1 
ATOM   510  O O   . SER   A 1 65 ? -0.281  -13.896 9.074   1.00 29.54  ? 64  SER   A O   1 
ATOM   511  C CB  . SER   A 1 65 ? -0.753  -12.324 6.735   1.00 32.31  ? 64  SER   A CB  1 
ATOM   512  O OG  . SER   A 1 65 ? -1.715  -11.502 6.113   1.00 38.13  ? 64  SER   A OG  1 
ATOM   513  N N   . LYS   A 1 66 ? 1.546   -12.570 9.238   1.00 31.15  ? 65  LYS   A N   1 
ATOM   514  C CA  . LYS   A 1 66 ? 2.353   -13.666 9.777   1.00 35.95  ? 65  LYS   A CA  1 
ATOM   515  C C   . LYS   A 1 66 ? 1.824   -14.190 11.120  1.00 31.63  ? 65  LYS   A C   1 
ATOM   516  O O   . LYS   A 1 66 ? 1.916   -15.389 11.397  1.00 35.35  ? 65  LYS   A O   1 
ATOM   517  C CB  . LYS   A 1 66 ? 3.850   -13.346 9.829   1.00 39.83  ? 65  LYS   A CB  1 
ATOM   518  C CG  . LYS   A 1 66 ? 4.252   -12.090 10.555  1.00 47.04  ? 65  LYS   A CG  1 
ATOM   519  C CD  . LYS   A 1 66 ? 5.775   -12.055 10.558  1.00 55.28  ? 65  LYS   A CD  1 
ATOM   520  C CE  . LYS   A 1 66 ? 6.327   -10.814 11.191  1.00 63.76  ? 65  LYS   A CE  1 
ATOM   521  N NZ  . LYS   A 1 66 ? 6.146   -9.609  10.373  1.00 68.01  ? 65  LYS   A NZ  1 
ATOM   522  N N   A ASP   A 1 67 ? 1.237   -13.303 11.930  0.50 33.89  ? 66  ASP   A N   1 
ATOM   523  N N   B ASP   A 1 67 ? 1.263   -13.303 11.951  0.50 33.27  ? 66  ASP   A N   1 
ATOM   524  C CA  A ASP   A 1 67 ? 0.744   -13.706 13.244  0.50 37.71  ? 66  ASP   A CA  1 
ATOM   525  C CA  B ASP   A 1 67 ? 0.743   -13.752 13.239  0.50 36.14  ? 66  ASP   A CA  1 
ATOM   526  C C   A ASP   A 1 67 ? -0.447  -14.663 13.107  0.50 38.35  ? 66  ASP   A C   1 
ATOM   527  C C   B ASP   A 1 67 ? -0.366  -14.781 13.016  0.50 37.65  ? 66  ASP   A C   1 
ATOM   528  O O   A ASP   A 1 67 ? -0.625  -15.567 13.915  0.50 40.26  ? 66  ASP   A O   1 
ATOM   529  O O   B ASP   A 1 67 ? -0.405  -15.823 13.665  0.50 36.37  ? 66  ASP   A O   1 
ATOM   530  C CB  A ASP   A 1 67 ? 0.571   -12.504 14.166  0.50 42.58  ? 66  ASP   A CB  1 
ATOM   531  C CB  B ASP   A 1 67 ? 0.282   -12.594 14.114  0.50 40.87  ? 66  ASP   A CB  1 
ATOM   532  C CG  A ASP   A 1 67 ? 1.860   -11.846 14.646  0.50 45.65  ? 66  ASP   A CG  1 
ATOM   533  C CG  B ASP   A 1 67 ? -0.086  -12.980 15.542  0.50 41.29  ? 66  ASP   A CG  1 
ATOM   534  O OD1 A ASP   A 1 67 ? 2.950   -12.350 14.301  0.50 46.72  ? 66  ASP   A OD1 1 
ATOM   535  O OD1 B ASP   A 1 67 ? 0.843   -13.210 16.344  0.50 40.14  ? 66  ASP   A OD1 1 
ATOM   536  O OD2 A ASP   A 1 67 ? 1.773   -10.828 15.367  0.50 47.87  ? 66  ASP   A OD2 1 
ATOM   537  O OD2 B ASP   A 1 67 ? -1.298  -13.086 15.830  0.50 46.11  ? 66  ASP   A OD2 1 
ATOM   538  N N   . LYS   A 1 68 ? -1.242  -14.520 12.041  1.00 37.24  ? 67  LYS   A N   1 
ATOM   539  C CA  . LYS   A 1 68 ? -2.312  -15.463 11.776  1.00 35.12  ? 67  LYS   A CA  1 
ATOM   540  C C   . LYS   A 1 68 ? -1.793  -16.737 11.111  1.00 36.33  ? 67  LYS   A C   1 
ATOM   541  O O   . LYS   A 1 68 ? -2.225  -17.843 11.446  1.00 34.46  ? 67  LYS   A O   1 
ATOM   542  C CB  . LYS   A 1 68 ? -3.378  -14.765 10.927  1.00 35.90  ? 67  LYS   A CB  1 
ATOM   543  C CG  . LYS   A 1 68 ? -4.642  -15.563 10.698  1.00 47.88  ? 67  LYS   A CG  1 
ATOM   544  C CD  . LYS   A 1 68 ? -5.648  -14.626 10.041  1.00 48.31  ? 67  LYS   A CD  1 
ATOM   545  C CE  . LYS   A 1 68 ? -6.963  -15.261 9.699   1.00 54.85  ? 67  LYS   A CE  1 
ATOM   546  N NZ  . LYS   A 1 68 ? -7.958  -14.275 9.254   1.00 48.61  ? 67  LYS   A NZ  1 
ATOM   547  N N   . TYR   A 1 69 ? -0.919  -16.596 10.104  1.00 34.29  ? 68  TYR   A N   1 
ATOM   548  C CA  . TYR   A 1 69 ? -0.718  -17.694 9.167   1.00 31.18  ? 68  TYR   A CA  1 
ATOM   549  C C   . TYR   A 1 69 ? 0.661   -18.336 9.336   1.00 31.62  ? 68  TYR   A C   1 
ATOM   550  O O   . TYR   A 1 69 ? 0.898   -19.402 8.766   1.00 34.23  ? 68  TYR   A O   1 
ATOM   551  C CB  . TYR   A 1 69 ? -0.855  -17.206 7.710   1.00 31.06  ? 68  TYR   A CB  1 
ATOM   552  C CG  . TYR   A 1 69 ? -2.255  -16.768 7.306   1.00 32.02  ? 68  TYR   A CG  1 
ATOM   553  C CD1 . TYR   A 1 69 ? -3.390  -17.451 7.749   1.00 34.71  ? 68  TYR   A CD1 1 
ATOM   554  C CD2 . TYR   A 1 69 ? -2.443  -15.690 6.439   1.00 34.89  ? 68  TYR   A CD2 1 
ATOM   555  C CE1 . TYR   A 1 69 ? -4.672  -17.040 7.405   1.00 32.10  ? 68  TYR   A CE1 1 
ATOM   556  C CE2 . TYR   A 1 69 ? -3.720  -15.280 6.071   1.00 32.80  ? 68  TYR   A CE2 1 
ATOM   557  C CZ  . TYR   A 1 69 ? -4.835  -15.942 6.572   1.00 29.58  ? 68  TYR   A CZ  1 
ATOM   558  O OH  . TYR   A 1 69 ? -6.079  -15.526 6.178   1.00 33.65  ? 68  TYR   A OH  1 
ATOM   559  N N   . GLY   A 1 70 ? 1.564   -17.693 10.080  1.00 30.33  ? 69  GLY   A N   1 
ATOM   560  C CA  . GLY   A 1 70 ? 2.947   -18.147 10.119  1.00 33.98  ? 69  GLY   A CA  1 
ATOM   561  C C   . GLY   A 1 70 ? 3.199   -19.140 11.260  1.00 32.46  ? 69  GLY   A C   1 
ATOM   562  O O   . GLY   A 1 70 ? 4.118   -18.966 12.034  1.00 39.70  ? 69  GLY   A O   1 
ATOM   563  N N   . LYS   A 1 71 ? 2.360   -20.162 11.376  1.00 38.63  ? 70  LYS   A N   1 
ATOM   564  C CA  . LYS   A 1 71 ? 2.546   -21.119 12.455  1.00 42.31  ? 70  LYS   A CA  1 
ATOM   565  C C   . LYS   A 1 71 ? 2.855   -22.455 11.806  1.00 43.95  ? 70  LYS   A C   1 
ATOM   566  O O   . LYS   A 1 71 ? 2.424   -22.672 10.675  1.00 37.03  ? 70  LYS   A O   1 
ATOM   567  C CB  . LYS   A 1 71 ? 1.290   -21.191 13.327  1.00 41.90  ? 70  LYS   A CB  1 
ATOM   568  C CG  . LYS   A 1 71 ? 0.972   -19.885 14.036  1.00 47.70  ? 70  LYS   A CG  1 
ATOM   569  C CD  . LYS   A 1 71 ? -0.153  -20.004 15.061  1.00 57.01  ? 70  LYS   A CD  1 
ATOM   570  N N   . PRO   A 1 72 ? 3.625   -23.368 12.457  1.00 39.47  ? 71  PRO   A N   1 
ATOM   571  C CA  . PRO   A 1 72 ? 3.891   -24.681 11.869  1.00 40.16  ? 71  PRO   A CA  1 
ATOM   572  C C   . PRO   A 1 72 ? 2.637   -25.394 11.392  1.00 40.38  ? 71  PRO   A C   1 
ATOM   573  O O   . PRO   A 1 72 ? 1.560   -25.200 11.937  1.00 47.39  ? 71  PRO   A O   1 
ATOM   574  C CB  . PRO   A 1 72 ? 4.617   -25.427 12.993  1.00 40.83  ? 71  PRO   A CB  1 
ATOM   575  C CG  . PRO   A 1 72 ? 5.356   -24.302 13.692  1.00 41.09  ? 71  PRO   A CG  1 
ATOM   576  C CD  . PRO   A 1 72 ? 4.306   -23.178 13.750  1.00 37.61  ? 71  PRO   A CD  1 
ATOM   577  N N   . ASN   A 1 73 ? 2.817   -26.182 10.342  1.00 41.58  ? 72  ASN   A N   1 
ATOM   578  C CA  . ASN   A 1 73 ? 1.750   -26.887 9.671   1.00 49.14  ? 72  ASN   A CA  1 
ATOM   579  C C   . ASN   A 1 73 ? 2.306   -28.250 9.284   1.00 55.03  ? 72  ASN   A C   1 
ATOM   580  O O   . ASN   A 1 73 ? 3.510   -28.386 9.054   1.00 51.61  ? 72  ASN   A O   1 
ATOM   581  C CB  . ASN   A 1 73 ? 1.299   -26.085 8.459   1.00 52.04  ? 72  ASN   A CB  1 
ATOM   582  C CG  . ASN   A 1 73 ? -0.034  -26.537 7.932   1.00 56.00  ? 72  ASN   A CG  1 
ATOM   583  O OD1 . ASN   A 1 73 ? -0.094  -27.462 7.119   1.00 57.41  ? 72  ASN   A OD1 1 
ATOM   584  N ND2 . ASN   A 1 73 ? -1.105  -25.867 8.334   1.00 64.84  ? 72  ASN   A ND2 1 
ATOM   585  N N   . LYS   A 1 74 ? 1.418   -29.246 9.223   1.00 53.21  ? 73  LYS   A N   1 
ATOM   586  C CA  . LYS   A 1 74 ? 1.818   -30.616 8.960   1.00 51.55  ? 73  LYS   A CA  1 
ATOM   587  C C   . LYS   A 1 74 ? 2.134   -30.792 7.478   1.00 48.78  ? 73  LYS   A C   1 
ATOM   588  O O   . LYS   A 1 74 ? 2.838   -31.727 7.114   1.00 45.87  ? 73  LYS   A O   1 
ATOM   589  C CB  . LYS   A 1 74 ? 0.806   -31.623 9.537   1.00 53.86  ? 73  LYS   A CB  1 
ATOM   590  C CG  . LYS   A 1 74 ? -0.617  -31.578 8.973   1.00 53.79  ? 73  LYS   A CG  1 
ATOM   591  N N   . ARG   A 1 75 ? 1.646   -29.881 6.624   1.00 44.45  ? 74  ARG   A N   1 
ATOM   592  C CA  . ARG   A 1 75 ? 1.744   -30.073 5.184   1.00 40.92  ? 74  ARG   A CA  1 
ATOM   593  C C   . ARG   A 1 75 ? 3.204   -30.110 4.715   1.00 37.65  ? 74  ARG   A C   1 
ATOM   594  O O   . ARG   A 1 75 ? 4.069   -29.433 5.278   1.00 39.24  ? 74  ARG   A O   1 
ATOM   595  C CB  . ARG   A 1 75 ? 0.876   -29.063 4.418   1.00 44.36  ? 74  ARG   A CB  1 
ATOM   596  C CG  . ARG   A 1 75 ? -0.606  -29.200 4.740   1.00 45.57  ? 74  ARG   A CG  1 
ATOM   597  C CD  . ARG   A 1 75 ? -1.120  -30.453 4.045   1.00 46.69  ? 74  ARG   A CD  1 
ATOM   598  N NE  . ARG   A 1 75 ? -1.871  -30.114 2.836   1.00 59.11  ? 74  ARG   A NE  1 
ATOM   599  C CZ  . ARG   A 1 75 ? -3.064  -29.514 2.877   1.00 61.30  ? 74  ARG   A CZ  1 
ATOM   600  N NH1 . ARG   A 1 75 ? -3.710  -29.241 1.755   1.00 63.10  ? 74  ARG   A NH1 1 
ATOM   601  N NH2 . ARG   A 1 75 ? -3.613  -29.205 4.045   1.00 63.18  ? 74  ARG   A NH2 1 
ATOM   602  N N   . LYS   A 1 76 ? 3.450   -30.895 3.658   1.00 38.06  ? 75  LYS   A N   1 
ATOM   603  C CA  . LYS   A 1 76 ? 4.786   -31.124 3.131   1.00 41.27  ? 75  LYS   A CA  1 
ATOM   604  C C   . LYS   A 1 76 ? 5.394   -29.816 2.632   1.00 38.99  ? 75  LYS   A C   1 
ATOM   605  O O   . LYS   A 1 76 ? 4.856   -29.175 1.723   1.00 32.68  ? 75  LYS   A O   1 
ATOM   606  C CB  . LYS   A 1 76 ? 4.770   -32.106 1.957   1.00 42.70  ? 75  LYS   A CB  1 
ATOM   607  C CG  . LYS   A 1 76 ? 6.109   -32.346 1.275   1.00 41.80  ? 75  LYS   A CG  1 
ATOM   608  C CD  . LYS   A 1 76 ? 6.056   -33.476 0.246   1.00 48.49  ? 75  LYS   A CD  1 
ATOM   609  C CE  . LYS   A 1 76 ? 7.376   -33.763 -0.429  1.00 51.76  ? 75  LYS   A CE  1 
ATOM   610  N N   . GLY   A 1 77 ? 6.569   -29.475 3.185   1.00 36.69  ? 76  GLY   A N   1 
ATOM   611  C CA  . GLY   A 1 77 ? 7.299   -28.322 2.692   1.00 35.63  ? 76  GLY   A CA  1 
ATOM   612  C C   . GLY   A 1 77 ? 6.911   -27.043 3.432   1.00 33.43  ? 76  GLY   A C   1 
ATOM   613  O O   . GLY   A 1 77 ? 7.609   -26.047 3.300   1.00 32.67  ? 76  GLY   A O   1 
ATOM   614  N N   . PHE   A 1 78 ? 5.846   -27.083 4.244   1.00 35.14  ? 77  PHE   A N   1 
ATOM   615  C CA  . PHE   A 1 78 ? 5.355   -25.865 4.871   1.00 32.74  ? 77  PHE   A CA  1 
ATOM   616  C C   . PHE   A 1 78 ? 6.370   -25.269 5.849   1.00 34.00  ? 77  PHE   A C   1 
ATOM   617  O O   . PHE   A 1 78 ? 6.564   -24.050 5.927   1.00 28.77  ? 77  PHE   A O   1 
ATOM   618  C CB  . PHE   A 1 78 ? 3.984   -26.078 5.516   1.00 35.91  ? 77  PHE   A CB  1 
ATOM   619  C CG  . PHE   A 1 78 ? 3.263   -24.783 5.866   1.00 33.71  ? 77  PHE   A CG  1 
ATOM   620  C CD1 . PHE   A 1 78 ? 3.554   -24.088 7.035   1.00 31.20  ? 77  PHE   A CD1 1 
ATOM   621  C CD2 . PHE   A 1 78 ? 2.307   -24.249 4.997   1.00 30.92  ? 77  PHE   A CD2 1 
ATOM   622  C CE1 . PHE   A 1 78 ? 2.911   -22.892 7.340   1.00 33.94  ? 77  PHE   A CE1 1 
ATOM   623  C CE2 . PHE   A 1 78 ? 1.669   -23.061 5.312   1.00 27.53  ? 77  PHE   A CE2 1 
ATOM   624  C CZ  . PHE   A 1 78 ? 1.962   -22.393 6.479   1.00 29.72  ? 77  PHE   A CZ  1 
ATOM   625  N N   . ASN   A 1 79 ? 6.965   -26.120 6.686   1.00 33.41  ? 78  ASN   A N   1 
ATOM   626  C CA  . ASN   A 1 79 ? 7.809   -25.605 7.749   1.00 30.48  ? 78  ASN   A CA  1 
ATOM   627  C C   . ASN   A 1 79 ? 9.140   -25.117 7.166   1.00 28.16  ? 78  ASN   A C   1 
ATOM   628  O O   . ASN   A 1 79 ? 9.727   -24.123 7.630   1.00 26.94  ? 78  ASN   A O   1 
ATOM   629  C CB  . ASN   A 1 79 ? 7.945   -26.629 8.871   1.00 34.60  ? 78  ASN   A CB  1 
ATOM   630  C CG  . ASN   A 1 79 ? 6.635   -26.872 9.589   1.00 42.78  ? 78  ASN   A CG  1 
ATOM   631  O OD1 . ASN   A 1 79 ? 5.749   -26.006 9.593   1.00 36.56  ? 78  ASN   A OD1 1 
ATOM   632  N ND2 . ASN   A 1 79 ? 6.500   -28.043 10.211  1.00 34.52  ? 78  ASN   A ND2 1 
ATOM   633  N N   . GLU   A 1 80 ? 9.592   -25.813 6.119   1.00 28.78  ? 79  GLU   A N   1 
ATOM   634  C CA  . GLU   A 1 80 ? 10.757  -25.370 5.362   1.00 31.81  ? 79  GLU   A CA  1 
ATOM   635  C C   . GLU   A 1 80 ? 10.458  -23.987 4.787   1.00 29.07  ? 79  GLU   A C   1 
ATOM   636  O O   . GLU   A 1 80 ? 11.295  -23.067 4.866   1.00 28.08  ? 79  GLU   A O   1 
ATOM   637  C CB  . GLU   A 1 80 ? 11.091  -26.380 4.266   1.00 29.84  ? 79  GLU   A CB  1 
ATOM   638  C CG  . GLU   A 1 80 ? 12.370  -26.024 3.506   1.00 34.84  ? 79  GLU   A CG  1 
ATOM   639  C CD  . GLU   A 1 80 ? 12.892  -27.046 2.506   1.00 41.61  ? 79  GLU   A CD  1 
ATOM   640  O OE1 . GLU   A 1 80 ? 12.226  -28.076 2.291   1.00 49.58  ? 79  GLU   A OE1 1 
ATOM   641  O OE2 . GLU   A 1 80 ? 13.975  -26.821 1.934   1.00 43.94  ? 79  GLU   A OE2 1 
ATOM   642  N N   . GLY   A 1 81 ? 9.224   -23.852 4.278   1.00 30.31  ? 80  GLY   A N   1 
ATOM   643  C CA  . GLY   A 1 81 ? 8.718   -22.613 3.691   1.00 26.63  ? 80  GLY   A CA  1 
ATOM   644  C C   . GLY   A 1 81 ? 8.751   -21.453 4.684   1.00 26.13  ? 80  GLY   A C   1 
ATOM   645  O O   . GLY   A 1 81 ? 9.113   -20.328 4.338   1.00 24.77  ? 80  GLY   A O   1 
ATOM   646  N N   . LEU   A 1 82 ? 8.418   -21.732 5.942   1.00 26.26  ? 81  LEU   A N   1 
ATOM   647  C CA  . LEU   A 1 82 ? 8.459   -20.693 6.952   1.00 28.13  ? 81  LEU   A CA  1 
ATOM   648  C C   . LEU   A 1 82 ? 9.899   -20.255 7.189   1.00 27.08  ? 81  LEU   A C   1 
ATOM   649  O O   . LEU   A 1 82 ? 10.139  -19.076 7.436   1.00 24.55  ? 81  LEU   A O   1 
ATOM   650  C CB  . LEU   A 1 82 ? 7.785   -21.095 8.264   1.00 27.67  ? 81  LEU   A CB  1 
ATOM   651  C CG  . LEU   A 1 82 ? 6.297   -21.448 8.184   1.00 30.26  ? 81  LEU   A CG  1 
ATOM   652  C CD1 . LEU   A 1 82 ? 5.957   -21.984 9.570   1.00 30.59  ? 81  LEU   A CD1 1 
ATOM   653  C CD2 . LEU   A 1 82 ? 5.379   -20.264 7.903   1.00 27.73  ? 81  LEU   A CD2 1 
ATOM   654  N N   . TRP   A 1 83 ? 10.845  -21.216 7.190   1.00 26.57  ? 82  TRP   A N   1 
ATOM   655  C CA  . TRP   A 1 83 ? 12.237  -20.868 7.443   1.00 27.54  ? 82  TRP   A CA  1 
ATOM   656  C C   . TRP   A 1 83 ? 12.717  -19.951 6.313   1.00 24.81  ? 82  TRP   A C   1 
ATOM   657  O O   . TRP   A 1 83 ? 13.351  -18.935 6.549   1.00 25.13  ? 82  TRP   A O   1 
ATOM   658  C CB  . TRP   A 1 83 ? 13.130  -22.117 7.611   1.00 27.68  ? 82  TRP   A CB  1 
ATOM   659  C CG  . TRP   A 1 83 ? 14.572  -21.745 7.848   1.00 28.62  ? 82  TRP   A CG  1 
ATOM   660  C CD1 . TRP   A 1 83 ? 15.186  -21.557 9.059   1.00 29.41  ? 82  TRP   A CD1 1 
ATOM   661  C CD2 . TRP   A 1 83 ? 15.549  -21.437 6.834   1.00 27.89  ? 82  TRP   A CD2 1 
ATOM   662  N NE1 . TRP   A 1 83 ? 16.483  -21.178 8.868   1.00 27.19  ? 82  TRP   A NE1 1 
ATOM   663  C CE2 . TRP   A 1 83 ? 16.727  -21.080 7.512   1.00 27.75  ? 82  TRP   A CE2 1 
ATOM   664  C CE3 . TRP   A 1 83 ? 15.527  -21.416 5.423   1.00 28.66  ? 82  TRP   A CE3 1 
ATOM   665  C CZ2 . TRP   A 1 83 ? 17.883  -20.701 6.828   1.00 24.39  ? 82  TRP   A CZ2 1 
ATOM   666  C CZ3 . TRP   A 1 83 ? 16.659  -21.022 4.743   1.00 30.62  ? 82  TRP   A CZ3 1 
ATOM   667  C CH2 . TRP   A 1 83 ? 17.830  -20.681 5.449   1.00 28.36  ? 82  TRP   A CH2 1 
ATOM   668  N N   . GLU   A 1 84 ? 12.347  -20.287 5.071   1.00 24.02  ? 83  GLU   A N   1 
ATOM   669  C CA  . GLU   A 1 84 ? 12.865  -19.530 3.946   1.00 23.45  ? 83  GLU   A CA  1 
ATOM   670  C C   . GLU   A 1 84 ? 12.354  -18.086 3.972   1.00 25.49  ? 83  GLU   A C   1 
ATOM   671  O O   . GLU   A 1 84 ? 13.117  -17.160 3.738   1.00 24.90  ? 83  GLU   A O   1 
ATOM   672  C CB  . GLU   A 1 84 ? 12.482  -20.211 2.640   1.00 21.38  ? 83  GLU   A CB  1 
ATOM   673  C CG  . GLU   A 1 84 ? 13.137  -21.582 2.475   1.00 23.41  ? 83  GLU   A CG  1 
ATOM   674  C CD  . GLU   A 1 84 ? 12.732  -22.339 1.231   1.00 27.86  ? 83  GLU   A CD  1 
ATOM   675  O OE1 . GLU   A 1 84 ? 11.817  -21.860 0.555   1.00 29.87  ? 83  GLU   A OE1 1 
ATOM   676  O OE2 . GLU   A 1 84 ? 13.298  -23.413 0.928   1.00 29.06  ? 83  GLU   A OE2 1 
ATOM   677  N N   . ILE   A 1 85 ? 11.046  -17.880 4.194   1.00 25.72  ? 84  ILE   A N   1 
ATOM   678  C CA  . ILE   A 1 85 ? 10.473  -16.546 4.061   1.00 23.56  ? 84  ILE   A CA  1 
ATOM   679  C C   . ILE   A 1 85 ? 11.035  -15.639 5.161   1.00 24.97  ? 84  ILE   A C   1 
ATOM   680  O O   . ILE   A 1 85 ? 11.188  -14.421 4.959   1.00 24.84  ? 84  ILE   A O   1 
ATOM   681  C CB  . ILE   A 1 85 ? 8.925   -16.580 4.039   1.00 24.49  ? 84  ILE   A CB  1 
ATOM   682  C CG1 . ILE   A 1 85 ? 8.301   -15.218 3.570   1.00 24.13  ? 84  ILE   A CG1 1 
ATOM   683  C CG2 . ILE   A 1 85 ? 8.373   -17.019 5.395   1.00 21.50  ? 84  ILE   A CG2 1 
ATOM   684  C CD1 . ILE   A 1 85 ? 6.859   -15.347 3.071   1.00 23.77  ? 84  ILE   A CD1 1 
ATOM   685  N N   . GLN   A 1 86 ? 11.375  -16.247 6.314   1.00 22.10  ? 85  GLN   A N   1 
ATOM   686  C CA  . GLN   A 1 86 ? 11.916  -15.504 7.451   1.00 23.54  ? 85  GLN   A CA  1 
ATOM   687  C C   . GLN   A 1 86 ? 13.421  -15.242 7.333   1.00 24.59  ? 85  GLN   A C   1 
ATOM   688  O O   . GLN   A 1 86 ? 13.874  -14.157 7.716   1.00 27.84  ? 85  GLN   A O   1 
ATOM   689  C CB  . GLN   A 1 86 ? 11.484  -16.150 8.778   1.00 23.42  ? 85  GLN   A CB  1 
ATOM   690  C CG  . GLN   A 1 86 ? 12.044  -15.448 10.009  1.00 34.04  ? 85  GLN   A CG  1 
ATOM   691  C CD  . GLN   A 1 86 ? 11.378  -15.932 11.290  1.00 44.88  ? 85  GLN   A CD  1 
ATOM   692  O OE1 . GLN   A 1 86 ? 10.958  -17.094 11.402  1.00 40.89  ? 85  GLN   A OE1 1 
ATOM   693  N NE2 . GLN   A 1 86 ? 11.232  -15.028 12.254  1.00 43.90  ? 85  GLN   A NE2 1 
ATOM   694  N N   . ASN   A 1 87 ? 14.175  -16.189 6.752   1.00 23.82  ? 86  ASN   A N   1 
ATOM   695  C CA  . ASN   A 1 87 ? 15.633  -16.227 6.880   1.00 24.41  ? 86  ASN   A CA  1 
ATOM   696  C C   . ASN   A 1 87 ? 16.338  -15.897 5.555   1.00 24.85  ? 86  ASN   A C   1 
ATOM   697  O O   . ASN   A 1 87 ? 17.437  -15.316 5.581   1.00 26.16  ? 86  ASN   A O   1 
ATOM   698  C CB  . ASN   A 1 87 ? 16.107  -17.528 7.522   1.00 25.87  ? 86  ASN   A CB  1 
ATOM   699  C CG  . ASN   A 1 87 ? 15.628  -17.582 8.959   1.00 28.20  ? 86  ASN   A CG  1 
ATOM   700  O OD1 . ASN   A 1 87 ? 16.043  -16.742 9.761   1.00 32.12  ? 86  ASN   A OD1 1 
ATOM   701  N ND2 . ASN   A 1 87 ? 14.673  -18.443 9.273   1.00 27.37  ? 86  ASN   A ND2 1 
ATOM   702  N N   . ASN   A 1 88 ? 15.764  -16.261 4.389   1.00 25.14  ? 87  ASN   A N   1 
ATOM   703  C CA  . ASN   A 1 88 ? 16.431  -15.896 3.135   1.00 24.56  ? 87  ASN   A CA  1 
ATOM   704  C C   . ASN   A 1 88 ? 15.403  -15.802 2.001   1.00 24.08  ? 87  ASN   A C   1 
ATOM   705  O O   . ASN   A 1 88 ? 15.409  -16.599 1.051   1.00 24.67  ? 87  ASN   A O   1 
ATOM   706  C CB  . ASN   A 1 88 ? 17.576  -16.844 2.771   1.00 27.35  ? 87  ASN   A CB  1 
ATOM   707  C CG  . ASN   A 1 88 ? 18.657  -16.211 1.911   1.00 28.33  ? 87  ASN   A CG  1 
ATOM   708  O OD1 . ASN   A 1 88 ? 18.450  -15.180 1.257   1.00 25.80  ? 87  ASN   A OD1 1 
ATOM   709  N ND2 . ASN   A 1 88 ? 19.852  -16.795 1.926   1.00 27.46  ? 87  ASN   A ND2 1 
ATOM   710  N N   . PRO   A 1 89 ? 14.465  -14.833 2.095   1.00 24.93  ? 88  PRO   A N   1 
ATOM   711  C CA  . PRO   A 1 89 ? 13.309  -14.831 1.205   1.00 23.14  ? 88  PRO   A CA  1 
ATOM   712  C C   . PRO   A 1 89 ? 13.652  -14.441 -0.229  1.00 24.49  ? 88  PRO   A C   1 
ATOM   713  O O   . PRO   A 1 89 ? 12.835  -14.662 -1.104  1.00 22.88  ? 88  PRO   A O   1 
ATOM   714  C CB  . PRO   A 1 89 ? 12.369  -13.841 1.865   1.00 23.98  ? 88  PRO   A CB  1 
ATOM   715  C CG  . PRO   A 1 89 ? 13.317  -12.850 2.537   1.00 24.59  ? 88  PRO   A CG  1 
ATOM   716  C CD  . PRO   A 1 89 ? 14.415  -13.779 3.127   1.00 23.74  ? 88  PRO   A CD  1 
ATOM   717  N N   . HIS   A 1 90 ? 14.844  -13.857 -0.455  1.00 21.86  ? 89  HIS   A N   1 
ATOM   718  C CA  . HIS   A 1 90 ? 15.200  -13.328 -1.764  1.00 22.27  ? 89  HIS   A CA  1 
ATOM   719  C C   . HIS   A 1 90 ? 16.309  -14.152 -2.419  1.00 24.38  ? 89  HIS   A C   1 
ATOM   720  O O   . HIS   A 1 90 ? 16.836  -13.735 -3.446  1.00 26.50  ? 89  HIS   A O   1 
ATOM   721  C CB  . HIS   A 1 90 ? 15.586  -11.845 -1.668  1.00 24.96  ? 89  HIS   A CB  1 
ATOM   722  C CG  . HIS   A 1 90 ? 14.501  -10.976 -1.088  1.00 22.92  ? 89  HIS   A CG  1 
ATOM   723  N ND1 . HIS   A 1 90 ? 13.244  -10.841 -1.657  1.00 23.35  ? 89  HIS   A ND1 1 
ATOM   724  C CD2 . HIS   A 1 90 ? 14.471  -10.287 0.066   1.00 22.00  ? 89  HIS   A CD2 1 
ATOM   725  C CE1 . HIS   A 1 90 ? 12.498  -10.054 -0.870  1.00 23.16  ? 89  HIS   A CE1 1 
ATOM   726  N NE2 . HIS   A 1 90 ? 13.237  -9.682  0.154   1.00 25.41  ? 89  HIS   A NE2 1 
ATOM   727  N N   . ALA   A 1 91 ? 16.603  -15.351 -1.888  1.00 25.72  ? 90  ALA   A N   1 
ATOM   728  C CA  . ALA   A 1 91 ? 17.661  -16.203 -2.435  1.00 25.30  ? 90  ALA   A CA  1 
ATOM   729  C C   . ALA   A 1 91 ? 17.183  -16.897 -3.704  1.00 27.07  ? 90  ALA   A C   1 
ATOM   730  O O   . ALA   A 1 91 ? 15.992  -17.008 -3.957  1.00 29.14  ? 90  ALA   A O   1 
ATOM   731  C CB  . ALA   A 1 91 ? 18.109  -17.250 -1.415  1.00 25.62  ? 90  ALA   A CB  1 
ATOM   732  N N   . SER   A 1 92 ? 18.151  -17.416 -4.465  1.00 26.52  ? 91  SER   A N   1 
ATOM   733  C CA  . SER   A 1 92 ? 17.882  -18.352 -5.540  1.00 29.92  ? 91  SER   A CA  1 
ATOM   734  C C   . SER   A 1 92 ? 17.568  -19.728 -4.952  1.00 32.96  ? 91  SER   A C   1 
ATOM   735  O O   . SER   A 1 92 ? 18.354  -20.279 -4.176  1.00 35.23  ? 91  SER   A O   1 
ATOM   736  C CB  . SER   A 1 92 ? 19.078  -18.385 -6.445  1.00 34.65  ? 91  SER   A CB  1 
ATOM   737  O OG  . SER   A 1 92 ? 19.029  -19.531 -7.271  1.00 42.47  ? 91  SER   A OG  1 
ATOM   738  N N   . TYR   A 1 93 ? 16.412  -20.289 -5.321  1.00 30.19  ? 92  TYR   A N   1 
ATOM   739  C CA  . TYR   A 1 93 ? 16.041  -21.633 -4.890  1.00 37.44  ? 92  TYR   A CA  1 
ATOM   740  C C   . TYR   A 1 93 ? 15.895  -22.565 -6.098  1.00 43.02  ? 92  TYR   A C   1 
ATOM   741  O O   . TYR   A 1 93 ? 15.242  -23.606 -5.999  1.00 46.28  ? 92  TYR   A O   1 
ATOM   742  C CB  . TYR   A 1 93 ? 14.727  -21.685 -4.093  1.00 32.84  ? 92  TYR   A CB  1 
ATOM   743  C CG  . TYR   A 1 93 ? 14.845  -21.009 -2.735  1.00 30.93  ? 92  TYR   A CG  1 
ATOM   744  C CD1 . TYR   A 1 93 ? 15.259  -21.732 -1.617  1.00 29.60  ? 92  TYR   A CD1 1 
ATOM   745  C CD2 . TYR   A 1 93 ? 14.536  -19.657 -2.571  1.00 29.55  ? 92  TYR   A CD2 1 
ATOM   746  C CE1 . TYR   A 1 93 ? 15.390  -21.117 -0.378  1.00 34.28  ? 92  TYR   A CE1 1 
ATOM   747  C CE2 . TYR   A 1 93 ? 14.643  -19.045 -1.330  1.00 29.33  ? 92  TYR   A CE2 1 
ATOM   748  C CZ  . TYR   A 1 93 ? 15.091  -19.769 -0.230  1.00 31.57  ? 92  TYR   A CZ  1 
ATOM   749  O OH  . TYR   A 1 93 ? 15.273  -19.204 1.014   1.00 29.42  ? 92  TYR   A OH  1 
ATOM   750  N N   . SER   A 1 94 ? 16.501  -22.183 -7.227  1.00 48.56  ? 93  SER   A N   1 
ATOM   751  C CA  . SER   A 1 94 ? 16.642  -23.079 -8.368  1.00 65.70  ? 93  SER   A CA  1 
ATOM   752  C C   . SER   A 1 94 ? 17.437  -24.315 -7.921  1.00 68.36  ? 93  SER   A C   1 
ATOM   753  O O   . SER   A 1 94 ? 18.482  -24.112 -7.261  1.00 65.69  ? 93  SER   A O   1 
ATOM   754  C CB  . SER   A 1 94 ? 17.328  -22.400 -9.538  1.00 58.44  ? 93  SER   A CB  1 
ATOM   755  O OG  . SER   A 1 94 ? 16.798  -21.103 -9.770  1.00 71.70  ? 93  SER   A OG  1 
ATOM   756  O OXT . SER   A 1 94 ? 16.979  -25.433 -8.232  1.00 82.47  ? 93  SER   A OXT 1 
ATOM   757  N N   . MET   B 1 2  ? 38.851  -11.121 -41.749 1.00 63.92  ? 1   MET   B N   1 
ATOM   758  C CA  . MET   B 1 2  ? 38.566  -12.063 -42.866 1.00 65.90  ? 1   MET   B CA  1 
ATOM   759  C C   . MET   B 1 2  ? 37.055  -12.277 -42.955 1.00 59.92  ? 1   MET   B C   1 
ATOM   760  O O   . MET   B 1 2  ? 36.405  -12.516 -41.938 1.00 56.24  ? 1   MET   B O   1 
ATOM   761  C CB  . MET   B 1 2  ? 39.278  -13.405 -42.644 1.00 74.11  ? 1   MET   B CB  1 
ATOM   762  C CG  . MET   B 1 2  ? 39.452  -14.264 -43.895 1.00 79.85  ? 1   MET   B CG  1 
ATOM   763  S SD  . MET   B 1 2  ? 40.462  -13.538 -45.208 1.00 79.82  ? 1   MET   B SD  1 
ATOM   764  C CE  . MET   B 1 2  ? 41.808  -12.817 -44.257 1.00 67.95  ? 1   MET   B CE  1 
ATOM   765  N N   . PRO   B 1 3  ? 36.438  -12.168 -44.159 1.00 55.01  ? 2   PRO   B N   1 
ATOM   766  C CA  . PRO   B 1 3  ? 35.002  -12.417 -44.297 1.00 52.84  ? 2   PRO   B CA  1 
ATOM   767  C C   . PRO   B 1 3  ? 34.683  -13.846 -43.854 1.00 53.43  ? 2   PRO   B C   1 
ATOM   768  O O   . PRO   B 1 3  ? 35.530  -14.733 -43.960 1.00 48.19  ? 2   PRO   B O   1 
ATOM   769  C CB  . PRO   B 1 3  ? 34.723  -12.153 -45.791 1.00 51.22  ? 2   PRO   B CB  1 
ATOM   770  C CG  . PRO   B 1 3  ? 35.873  -11.261 -46.220 1.00 49.30  ? 2   PRO   B CG  1 
ATOM   771  C CD  . PRO   B 1 3  ? 37.071  -11.768 -45.429 1.00 51.77  ? 2   PRO   B CD  1 
ATOM   772  N N   . HIS   B 1 4  ? 33.478  -14.030 -43.294 1.00 53.44  ? 3   HIS   B N   1 
ATOM   773  C CA  . HIS   B 1 4  ? 32.983  -15.342 -42.899 1.00 56.01  ? 3   HIS   B CA  1 
ATOM   774  C C   . HIS   B 1 4  ? 31.593  -15.558 -43.493 1.00 53.35  ? 3   HIS   B C   1 
ATOM   775  O O   . HIS   B 1 4  ? 31.042  -14.642 -44.119 1.00 45.96  ? 3   HIS   B O   1 
ATOM   776  C CB  . HIS   B 1 4  ? 33.095  -15.529 -41.382 1.00 60.46  ? 3   HIS   B CB  1 
ATOM   777  C CG  . HIS   B 1 4  ? 34.508  -15.666 -40.912 1.00 70.50  ? 3   HIS   B CG  1 
ATOM   778  N ND1 . HIS   B 1 4  ? 35.412  -16.527 -41.500 1.00 72.87  ? 3   HIS   B ND1 1 
ATOM   779  C CD2 . HIS   B 1 4  ? 35.158  -15.072 -39.894 1.00 66.30  ? 3   HIS   B CD2 1 
ATOM   780  C CE1 . HIS   B 1 4  ? 36.567  -16.447 -40.854 1.00 70.54  ? 3   HIS   B CE1 1 
ATOM   781  N NE2 . HIS   B 1 4  ? 36.436  -15.564 -39.881 1.00 68.75  ? 3   HIS   B NE2 1 
ATOM   782  N N   . ALA   B 1 5  ? 31.045  -16.777 -43.319 1.00 45.40  ? 4   ALA   B N   1 
ATOM   783  C CA  . ALA   B 1 5  ? 29.744  -17.097 -43.890 1.00 41.03  ? 4   ALA   B CA  1 
ATOM   784  C C   . ALA   B 1 5  ? 28.716  -16.109 -43.357 1.00 40.73  ? 4   ALA   B C   1 
ATOM   785  O O   . ALA   B 1 5  ? 27.916  -15.576 -44.129 1.00 43.19  ? 4   ALA   B O   1 
ATOM   786  C CB  . ALA   B 1 5  ? 29.340  -18.513 -43.563 1.00 44.90  ? 4   ALA   B CB  1 
ATOM   787  N N   . PHE   B 1 6  ? 28.765  -15.866 -42.038 1.00 36.43  ? 5   PHE   B N   1 
ATOM   788  C CA  . PHE   B 1 6  ? 27.951  -14.814 -41.440 1.00 45.38  ? 5   PHE   B CA  1 
ATOM   789  C C   . PHE   B 1 6  ? 28.824  -13.583 -41.158 1.00 42.01  ? 5   PHE   B C   1 
ATOM   790  O O   . PHE   B 1 6  ? 29.925  -13.706 -40.631 1.00 43.72  ? 5   PHE   B O   1 
ATOM   791  C CB  . PHE   B 1 6  ? 27.240  -15.250 -40.150 1.00 40.35  ? 5   PHE   B CB  1 
ATOM   792  C CG  . PHE   B 1 6  ? 26.197  -16.360 -40.237 1.00 35.73  ? 5   PHE   B CG  1 
ATOM   793  C CD1 . PHE   B 1 6  ? 24.848  -16.060 -40.432 1.00 34.60  ? 5   PHE   B CD1 1 
ATOM   794  C CD2 . PHE   B 1 6  ? 26.558  -17.697 -40.068 1.00 39.46  ? 5   PHE   B CD2 1 
ATOM   795  C CE1 . PHE   B 1 6  ? 23.893  -17.068 -40.465 1.00 33.43  ? 5   PHE   B CE1 1 
ATOM   796  C CE2 . PHE   B 1 6  ? 25.598  -18.707 -40.105 1.00 35.00  ? 5   PHE   B CE2 1 
ATOM   797  C CZ  . PHE   B 1 6  ? 24.269  -18.390 -40.311 1.00 34.35  ? 5   PHE   B CZ  1 
ATOM   798  N N   . LYS   B 1 7  ? 28.308  -12.394 -41.481 1.00 45.34  ? 6   LYS   B N   1 
ATOM   799  C CA  . LYS   B 1 7  ? 29.038  -11.154 -41.251 1.00 43.16  ? 6   LYS   B CA  1 
ATOM   800  C C   . LYS   B 1 7  ? 28.268  -10.231 -40.297 1.00 45.02  ? 6   LYS   B C   1 
ATOM   801  O O   . LYS   B 1 7  ? 27.039  -10.292 -40.195 1.00 37.26  ? 6   LYS   B O   1 
ATOM   802  C CB  . LYS   B 1 7  ? 29.240  -10.463 -42.599 1.00 44.48  ? 6   LYS   B CB  1 
ATOM   803  C CG  . LYS   B 1 7  ? 27.969  -9.999  -43.282 1.00 42.95  ? 6   LYS   B CG  1 
ATOM   804  C CD  . LYS   B 1 7  ? 28.236  -9.617  -44.737 1.00 50.25  ? 6   LYS   B CD  1 
ATOM   805  C CE  . LYS   B 1 7  ? 27.013  -9.167  -45.477 1.00 57.07  ? 6   LYS   B CE  1 
ATOM   806  N NZ  . LYS   B 1 7  ? 26.003  -10.226 -45.607 1.00 61.10  ? 6   LYS   B NZ  1 
ATOM   807  N N   . PRO   B 1 8  ? 28.970  -9.293  -39.618 1.00 44.94  ? 7   PRO   B N   1 
ATOM   808  C CA  . PRO   B 1 8  ? 28.331  -8.346  -38.703 1.00 37.66  ? 7   PRO   B CA  1 
ATOM   809  C C   . PRO   B 1 8  ? 27.135  -7.664  -39.344 1.00 39.40  ? 7   PRO   B C   1 
ATOM   810  O O   . PRO   B 1 8  ? 27.208  -7.233  -40.497 1.00 41.33  ? 7   PRO   B O   1 
ATOM   811  C CB  . PRO   B 1 8  ? 29.511  -7.400  -38.480 1.00 43.60  ? 7   PRO   B CB  1 
ATOM   812  C CG  . PRO   B 1 8  ? 30.692  -8.336  -38.423 1.00 44.71  ? 7   PRO   B CG  1 
ATOM   813  C CD  . PRO   B 1 8  ? 30.429  -9.091  -39.711 1.00 47.00  ? 7   PRO   B CD  1 
ATOM   814  N N   . GLY   B 1 9  ? 26.000  -7.654  -38.626 1.00 34.22  ? 8   GLY   B N   1 
ATOM   815  C CA  . GLY   B 1 9  ? 24.811  -7.027  -39.151 1.00 32.84  ? 8   GLY   B CA  1 
ATOM   816  C C   . GLY   B 1 9  ? 23.849  -8.035  -39.774 1.00 32.86  ? 8   GLY   B C   1 
ATOM   817  O O   . GLY   B 1 9  ? 22.705  -7.684  -40.034 1.00 33.71  ? 8   GLY   B O   1 
ATOM   818  N N   . ASP   B 1 10 ? 24.300  -9.282  -40.002 1.00 34.66  ? 9   ASP   B N   1 
ATOM   819  C CA  . ASP   B 1 10 ? 23.418  -10.326 -40.516 1.00 32.95  ? 9   ASP   B CA  1 
ATOM   820  C C   . ASP   B 1 10 ? 22.301  -10.605 -39.500 1.00 28.77  ? 9   ASP   B C   1 
ATOM   821  O O   . ASP   B 1 10 ? 22.542  -10.619 -38.292 1.00 30.57  ? 9   ASP   B O   1 
ATOM   822  C CB  . ASP   B 1 10 ? 24.181  -11.594 -40.874 1.00 37.46  ? 9   ASP   B CB  1 
ATOM   823  C CG  . ASP   B 1 10 ? 24.926  -11.614 -42.208 1.00 40.83  ? 9   ASP   B CG  1 
ATOM   824  O OD1 . ASP   B 1 10 ? 24.729  -10.691 -43.018 1.00 42.76  ? 9   ASP   B OD1 1 
ATOM   825  O OD2 . ASP   B 1 10 ? 25.729  -12.547 -42.409 1.00 37.99  ? 9   ASP   B OD2 1 
ATOM   826  N N   . LEU   B 1 11 ? 21.077  -10.773 -40.003 1.00 28.86  ? 10  LEU   B N   1 
ATOM   827  C CA  . LEU   B 1 11 ? 19.941  -10.996 -39.132 1.00 29.50  ? 10  LEU   B CA  1 
ATOM   828  C C   . LEU   B 1 11 ? 19.603  -12.479 -39.147 1.00 30.51  ? 10  LEU   B C   1 
ATOM   829  O O   . LEU   B 1 11 ? 19.653  -13.112 -40.212 1.00 32.21  ? 10  LEU   B O   1 
ATOM   830  C CB  . LEU   B 1 11 ? 18.778  -10.137 -39.596 1.00 28.33  ? 10  LEU   B CB  1 
ATOM   831  C CG  . LEU   B 1 11 ? 19.099  -8.635  -39.658 1.00 28.92  ? 10  LEU   B CG  1 
ATOM   832  C CD1 . LEU   B 1 11 ? 17.831  -7.908  -40.039 1.00 28.77  ? 10  LEU   B CD1 1 
ATOM   833  C CD2 . LEU   B 1 11 ? 19.665  -8.193  -38.311 1.00 26.66  ? 10  LEU   B CD2 1 
ATOM   834  N N   . VAL   B 1 12 ? 19.271  -13.016 -37.965 1.00 27.50  ? 11  VAL   B N   1 
ATOM   835  C CA  . VAL   B 1 12 ? 19.077  -14.458 -37.833 1.00 25.97  ? 11  VAL   B CA  1 
ATOM   836  C C   . VAL   B 1 12 ? 17.972  -14.724 -36.806 1.00 29.60  ? 11  VAL   B C   1 
ATOM   837  O O   . VAL   B 1 12 ? 17.532  -13.819 -36.076 1.00 25.73  ? 11  VAL   B O   1 
ATOM   838  C CB  . VAL   B 1 12 ? 20.372  -15.192 -37.424 1.00 27.08  ? 11  VAL   B CB  1 
ATOM   839  C CG1 . VAL   B 1 12 ? 21.545  -15.001 -38.400 1.00 27.91  ? 11  VAL   B CG1 1 
ATOM   840  C CG2 . VAL   B 1 12 ? 20.787  -14.850 -35.991 1.00 27.75  ? 11  VAL   B CG2 1 
ATOM   841  N N   . PHE   B 1 13 ? 17.552  -15.996 -36.759 1.00 28.12  ? 12  PHE   B N   1 
ATOM   842  C CA  . PHE   B 1 13 ? 17.019  -16.566 -35.536 1.00 28.56  ? 12  PHE   B CA  1 
ATOM   843  C C   . PHE   B 1 13 ? 18.125  -17.420 -34.937 1.00 30.41  ? 12  PHE   B C   1 
ATOM   844  O O   . PHE   B 1 13 ? 18.747  -18.206 -35.676 1.00 28.05  ? 12  PHE   B O   1 
ATOM   845  C CB  . PHE   B 1 13 ? 15.762  -17.406 -35.763 1.00 25.43  ? 12  PHE   B CB  1 
ATOM   846  C CG  . PHE   B 1 13 ? 14.573  -16.576 -36.211 1.00 29.22  ? 12  PHE   B CG  1 
ATOM   847  C CD1 . PHE   B 1 13 ? 14.364  -16.306 -37.569 1.00 30.27  ? 12  PHE   B CD1 1 
ATOM   848  C CD2 . PHE   B 1 13 ? 13.684  -16.050 -35.281 1.00 28.97  ? 12  PHE   B CD2 1 
ATOM   849  C CE1 . PHE   B 1 13 ? 13.292  -15.541 -37.989 1.00 32.08  ? 12  PHE   B CE1 1 
ATOM   850  C CE2 . PHE   B 1 13 ? 12.596  -15.285 -35.700 1.00 28.10  ? 12  PHE   B CE2 1 
ATOM   851  C CZ  . PHE   B 1 13 ? 12.404  -15.037 -37.053 1.00 31.91  ? 12  PHE   B CZ  1 
ATOM   852  N N   . ALA   B 1 14 ? 18.343  -17.249 -33.612 1.00 25.08  ? 13  ALA   B N   1 
ATOM   853  C CA  . ALA   B 1 14 ? 19.355  -17.985 -32.891 1.00 26.67  ? 13  ALA   B CA  1 
ATOM   854  C C   . ALA   B 1 14 ? 18.674  -18.924 -31.888 1.00 25.31  ? 13  ALA   B C   1 
ATOM   855  O O   . ALA   B 1 14 ? 17.748  -18.539 -31.183 1.00 26.45  ? 13  ALA   B O   1 
ATOM   856  C CB  . ALA   B 1 14 ? 20.308  -17.011 -32.216 1.00 26.39  ? 13  ALA   B CB  1 
ATOM   857  N N   . LYS   B 1 15 ? 19.136  -20.178 -31.844 1.00 29.43  ? 14  LYS   B N   1 
ATOM   858  C CA  . LYS   B 1 15 ? 18.481  -21.219 -31.056 1.00 30.31  ? 14  LYS   B CA  1 
ATOM   859  C C   . LYS   B 1 15 ? 19.342  -21.545 -29.841 1.00 31.03  ? 14  LYS   B C   1 
ATOM   860  O O   . LYS   B 1 15 ? 20.535  -21.829 -29.966 1.00 33.00  ? 14  LYS   B O   1 
ATOM   861  C CB  . LYS   B 1 15 ? 18.234  -22.501 -31.874 1.00 30.99  ? 14  LYS   B CB  1 
ATOM   862  C CG  . LYS   B 1 15 ? 17.485  -23.634 -31.142 1.00 29.75  ? 14  LYS   B CG  1 
ATOM   863  C CD  . LYS   B 1 15 ? 16.036  -23.216 -30.880 1.00 30.29  ? 14  LYS   B CD  1 
ATOM   864  C CE  . LYS   B 1 15 ? 15.176  -24.273 -30.177 1.00 30.84  ? 14  LYS   B CE  1 
ATOM   865  N NZ  . LYS   B 1 15 ? 15.736  -24.545 -28.856 1.00 29.17  ? 14  LYS   B NZ  1 
ATOM   866  N N   . MET   B 1 16 ? 18.707  -21.547 -28.660 1.00 32.05  ? 15  MET   B N   1 
ATOM   867  C CA  . MET   B 1 16 ? 19.355  -21.986 -27.432 1.00 35.13  ? 15  MET   B CA  1 
ATOM   868  C C   . MET   B 1 16 ? 18.453  -23.036 -26.794 1.00 33.98  ? 15  MET   B C   1 
ATOM   869  O O   . MET   B 1 16 ? 17.226  -22.975 -26.919 1.00 30.08  ? 15  MET   B O   1 
ATOM   870  C CB  . MET   B 1 16 ? 19.486  -20.843 -26.417 1.00 38.92  ? 15  MET   B CB  1 
ATOM   871  C CG  . MET   B 1 16 ? 20.121  -19.571 -26.935 1.00 46.04  ? 15  MET   B CG  1 
ATOM   872  S SD  . MET   B 1 16 ? 21.843  -19.227 -26.520 1.00 45.83  ? 15  MET   B SD  1 
ATOM   873  C CE  . MET   B 1 16 ? 22.182  -19.656 -24.806 1.00 41.05  ? 15  MET   B CE  1 
ATOM   874  N N   . LYS   B 1 17 ? 19.081  -23.983 -26.096 1.00 32.64  ? 16  LYS   B N   1 
ATOM   875  C CA  . LYS   B 1 17 ? 18.338  -24.988 -25.351 1.00 37.09  ? 16  LYS   B CA  1 
ATOM   876  C C   . LYS   B 1 17 ? 17.351  -24.299 -24.401 1.00 32.84  ? 16  LYS   B C   1 
ATOM   877  O O   . LYS   B 1 17 ? 17.707  -23.355 -23.696 1.00 33.57  ? 16  LYS   B O   1 
ATOM   878  C CB  . LYS   B 1 17 ? 19.353  -25.893 -24.638 1.00 43.16  ? 16  LYS   B CB  1 
ATOM   879  C CG  . LYS   B 1 17 ? 18.760  -27.181 -24.054 1.00 52.40  ? 16  LYS   B CG  1 
ATOM   880  C CD  . LYS   B 1 17 ? 19.718  -27.887 -23.095 1.00 58.93  ? 16  LYS   B CD  1 
ATOM   881  C CE  . LYS   B 1 17 ? 19.311  -29.280 -22.682 1.00 64.68  ? 16  LYS   B CE  1 
ATOM   882  N NZ  . LYS   B 1 17 ? 17.960  -29.370 -22.113 1.00 66.47  ? 16  LYS   B NZ  1 
ATOM   883  N N   . GLY   B 1 18 ? 16.093  -24.735 -24.446 1.00 35.63  ? 17  GLY   B N   1 
ATOM   884  C CA  . GLY   B 1 18 ? 15.074  -24.219 -23.549 1.00 37.12  ? 17  GLY   B CA  1 
ATOM   885  C C   . GLY   B 1 18 ? 14.344  -22.980 -24.075 1.00 36.56  ? 17  GLY   B C   1 
ATOM   886  O O   . GLY   B 1 18 ? 13.468  -22.475 -23.381 1.00 35.11  ? 17  GLY   B O   1 
ATOM   887  N N   . TYR   B 1 19 ? 14.650  -22.525 -25.306 1.00 31.26  ? 18  TYR   B N   1 
ATOM   888  C CA  . TYR   B 1 19 ? 14.036  -21.315 -25.832 1.00 28.89  ? 18  TYR   B CA  1 
ATOM   889  C C   . TYR   B 1 19 ? 13.647  -21.527 -27.296 1.00 29.27  ? 18  TYR   B C   1 
ATOM   890  O O   . TYR   B 1 19 ? 14.308  -22.261 -28.015 1.00 33.09  ? 18  TYR   B O   1 
ATOM   891  C CB  . TYR   B 1 19 ? 15.017  -20.133 -25.731 1.00 26.57  ? 18  TYR   B CB  1 
ATOM   892  C CG  . TYR   B 1 19 ? 15.426  -19.835 -24.296 1.00 27.36  ? 18  TYR   B CG  1 
ATOM   893  C CD1 . TYR   B 1 19 ? 14.640  -19.000 -23.493 1.00 30.19  ? 18  TYR   B CD1 1 
ATOM   894  C CD2 . TYR   B 1 19 ? 16.557  -20.430 -23.735 1.00 28.90  ? 18  TYR   B CD2 1 
ATOM   895  C CE1 . TYR   B 1 19 ? 14.972  -18.769 -22.163 1.00 31.71  ? 18  TYR   B CE1 1 
ATOM   896  C CE2 . TYR   B 1 19 ? 16.901  -20.192 -22.406 1.00 34.56  ? 18  TYR   B CE2 1 
ATOM   897  C CZ  . TYR   B 1 19 ? 16.110  -19.354 -21.631 1.00 33.78  ? 18  TYR   B CZ  1 
ATOM   898  O OH  . TYR   B 1 19 ? 16.459  -19.126 -20.329 1.00 39.17  ? 18  TYR   B OH  1 
ATOM   899  N N   . PRO   B 1 20 ? 12.579  -20.864 -27.794 1.00 29.46  ? 19  PRO   B N   1 
ATOM   900  C CA  . PRO   B 1 20 ? 12.247  -20.916 -29.222 1.00 27.40  ? 19  PRO   B CA  1 
ATOM   901  C C   . PRO   B 1 20 ? 13.324  -20.191 -30.036 1.00 27.05  ? 19  PRO   B C   1 
ATOM   902  O O   . PRO   B 1 20 ? 14.051  -19.357 -29.490 1.00 24.87  ? 19  PRO   B O   1 
ATOM   903  C CB  . PRO   B 1 20 ? 10.897  -20.202 -29.268 1.00 25.40  ? 19  PRO   B CB  1 
ATOM   904  C CG  . PRO   B 1 20 ? 10.969  -19.196 -28.101 1.00 29.45  ? 19  PRO   B CG  1 
ATOM   905  C CD  . PRO   B 1 20 ? 11.689  -19.985 -27.019 1.00 28.89  ? 19  PRO   B CD  1 
ATOM   906  N N   . HIS   B 1 21 ? 13.451  -20.542 -31.328 1.00 25.73  ? 20  HIS   B N   1 
ATOM   907  C CA  . HIS   B 1 21 ? 14.347  -19.803 -32.226 1.00 26.45  ? 20  HIS   B CA  1 
ATOM   908  C C   . HIS   B 1 21 ? 14.116  -18.299 -32.064 1.00 25.17  ? 20  HIS   B C   1 
ATOM   909  O O   . HIS   B 1 21 ? 12.979  -17.842 -32.206 1.00 28.29  ? 20  HIS   B O   1 
ATOM   910  C CB  . HIS   B 1 21 ? 14.064  -20.228 -33.673 1.00 25.25  ? 20  HIS   B CB  1 
ATOM   911  C CG  . HIS   B 1 21 ? 14.279  -21.699 -33.867 1.00 27.56  ? 20  HIS   B CG  1 
ATOM   912  N ND1 . HIS   B 1 21 ? 13.331  -22.616 -33.462 1.00 29.40  ? 20  HIS   B ND1 1 
ATOM   913  C CD2 . HIS   B 1 21 ? 15.320  -22.424 -34.327 1.00 28.87  ? 20  HIS   B CD2 1 
ATOM   914  C CE1 . HIS   B 1 21 ? 13.764  -23.847 -33.732 1.00 29.54  ? 20  HIS   B CE1 1 
ATOM   915  N NE2 . HIS   B 1 21 ? 14.974  -23.764 -34.242 1.00 29.70  ? 20  HIS   B NE2 1 
ATOM   916  N N   . TRP   B 1 22 ? 15.185  -17.530 -31.808 1.00 25.82  ? 21  TRP   B N   1 
ATOM   917  C CA  . TRP   B 1 22 ? 14.994  -16.203 -31.213 1.00 22.64  ? 21  TRP   B CA  1 
ATOM   918  C C   . TRP   B 1 22 ? 15.494  -15.098 -32.157 1.00 24.18  ? 21  TRP   B C   1 
ATOM   919  O O   . TRP   B 1 22 ? 16.633  -15.189 -32.629 1.00 25.76  ? 21  TRP   B O   1 
ATOM   920  C CB  . TRP   B 1 22 ? 15.695  -16.139 -29.843 1.00 23.97  ? 21  TRP   B CB  1 
ATOM   921  C CG  . TRP   B 1 22 ? 15.198  -14.987 -29.001 1.00 27.40  ? 21  TRP   B CG  1 
ATOM   922  C CD1 . TRP   B 1 22 ? 15.460  -13.658 -29.166 1.00 28.55  ? 21  TRP   B CD1 1 
ATOM   923  C CD2 . TRP   B 1 22 ? 14.238  -15.068 -27.921 1.00 28.94  ? 21  TRP   B CD2 1 
ATOM   924  N NE1 . TRP   B 1 22 ? 14.763  -12.908 -28.242 1.00 26.42  ? 21  TRP   B NE1 1 
ATOM   925  C CE2 . TRP   B 1 22 ? 14.001  -13.749 -27.469 1.00 28.17  ? 21  TRP   B CE2 1 
ATOM   926  C CE3 . TRP   B 1 22 ? 13.586  -16.135 -27.284 1.00 31.66  ? 21  TRP   B CE3 1 
ATOM   927  C CZ2 . TRP   B 1 22 ? 13.141  -13.467 -26.405 1.00 27.24  ? 21  TRP   B CZ2 1 
ATOM   928  C CZ3 . TRP   B 1 22 ? 12.731  -15.859 -26.234 1.00 30.86  ? 21  TRP   B CZ3 1 
ATOM   929  C CH2 . TRP   B 1 22 ? 12.480  -14.533 -25.832 1.00 26.32  ? 21  TRP   B CH2 1 
ATOM   930  N N   . PRO   B 1 23 ? 14.703  -14.034 -32.488 1.00 25.87  ? 22  PRO   B N   1 
ATOM   931  C CA  . PRO   B 1 23 ? 15.176  -12.988 -33.413 1.00 26.45  ? 22  PRO   B CA  1 
ATOM   932  C C   . PRO   B 1 23 ? 16.503  -12.429 -32.892 1.00 26.57  ? 22  PRO   B C   1 
ATOM   933  O O   . PRO   B 1 23 ? 16.621  -12.090 -31.716 1.00 26.59  ? 22  PRO   B O   1 
ATOM   934  C CB  . PRO   B 1 23 ? 14.018  -11.951 -33.393 1.00 26.19  ? 22  PRO   B CB  1 
ATOM   935  C CG  . PRO   B 1 23 ? 13.345  -12.226 -32.056 1.00 25.52  ? 22  PRO   B CG  1 
ATOM   936  C CD  . PRO   B 1 23 ? 13.328  -13.762 -32.024 1.00 25.29  ? 22  PRO   B CD  1 
ATOM   937  N N   . ALA   B 1 24 ? 17.544  -12.388 -33.728 1.00 26.81  ? 23  ALA   B N   1 
ATOM   938  C CA  . ALA   B 1 24 ? 18.863  -11.978 -33.250 1.00 22.19  ? 23  ALA   B CA  1 
ATOM   939  C C   . ALA   B 1 24 ? 19.704  -11.400 -34.398 1.00 24.93  ? 23  ALA   B C   1 
ATOM   940  O O   . ALA   B 1 24 ? 19.244  -11.385 -35.542 1.00 28.68  ? 23  ALA   B O   1 
ATOM   941  C CB  . ALA   B 1 24 ? 19.552  -13.157 -32.586 1.00 23.43  ? 23  ALA   B CB  1 
ATOM   942  N N   . ARG   B 1 25 ? 20.917  -10.917 -34.073 1.00 28.41  ? 24  ARG   B N   1 
ATOM   943  C CA  . ARG   B 1 25 ? 21.840  -10.411 -35.087 1.00 25.84  ? 24  ARG   B CA  1 
ATOM   944  C C   . ARG   B 1 25 ? 23.256  -10.842 -34.758 1.00 24.44  ? 24  ARG   B C   1 
ATOM   945  O O   . ARG   B 1 25 ? 23.566  -11.162 -33.611 1.00 26.32  ? 24  ARG   B O   1 
ATOM   946  C CB  . ARG   B 1 25 ? 21.829  -8.881  -35.217 1.00 27.35  ? 24  ARG   B CB  1 
ATOM   947  C CG  . ARG   B 1 25 ? 22.478  -8.122  -34.072 1.00 28.75  ? 24  ARG   B CG  1 
ATOM   948  C CD  . ARG   B 1 25 ? 22.256  -6.597  -34.187 1.00 31.21  ? 24  ARG   B CD  1 
ATOM   949  N NE  . ARG   B 1 25 ? 22.859  -5.913  -33.035 1.00 27.44  ? 24  ARG   B NE  1 
ATOM   950  C CZ  . ARG   B 1 25 ? 22.553  -4.679  -32.649 1.00 31.48  ? 24  ARG   B CZ  1 
ATOM   951  N NH1 . ARG   B 1 25 ? 21.620  -3.993  -33.308 1.00 27.64  ? 24  ARG   B NH1 1 
ATOM   952  N NH2 . ARG   B 1 25 ? 23.172  -4.149  -31.599 1.00 30.41  ? 24  ARG   B NH2 1 
ATOM   953  N N   . ILE   B 1 26 ? 24.090  -10.922 -35.810 1.00 26.70  ? 25  ILE   B N   1 
ATOM   954  C CA  . ILE   B 1 26 ? 25.524  -11.114 -35.679 1.00 29.13  ? 25  ILE   B CA  1 
ATOM   955  C C   . ILE   B 1 26 ? 26.094  -9.744  -35.344 1.00 31.78  ? 25  ILE   B C   1 
ATOM   956  O O   . ILE   B 1 26 ? 25.930  -8.789  -36.109 1.00 33.81  ? 25  ILE   B O   1 
ATOM   957  C CB  . ILE   B 1 26 ? 26.152  -11.606 -37.000 1.00 32.70  ? 25  ILE   B CB  1 
ATOM   958  C CG1 . ILE   B 1 26 ? 25.443  -12.849 -37.535 1.00 32.96  ? 25  ILE   B CG1 1 
ATOM   959  C CG2 . ILE   B 1 26 ? 27.659  -11.826 -36.818 1.00 31.95  ? 25  ILE   B CG2 1 
ATOM   960  C CD1 . ILE   B 1 26 ? 25.550  -14.054 -36.614 1.00 32.64  ? 25  ILE   B CD1 1 
ATOM   961  N N   . ASP   B 1 27 ? 26.767  -9.673  -34.203 1.00 34.02  ? 26  ASP   B N   1 
ATOM   962  C CA  . ASP   B 1 27 ? 27.439  -8.451  -33.783 1.00 40.14  ? 26  ASP   B CA  1 
ATOM   963  C C   . ASP   B 1 27 ? 28.899  -8.456  -34.256 1.00 45.12  ? 26  ASP   B C   1 
ATOM   964  O O   . ASP   B 1 27 ? 29.457  -9.519  -34.515 1.00 44.23  ? 26  ASP   B O   1 
ATOM   965  C CB  . ASP   B 1 27 ? 27.372  -8.355  -32.270 1.00 33.98  ? 26  ASP   B CB  1 
ATOM   966  C CG  . ASP   B 1 27 ? 26.201  -7.575  -31.686 1.00 38.99  ? 26  ASP   B CG  1 
ATOM   967  O OD1 . ASP   B 1 27 ? 25.375  -7.056  -32.468 1.00 36.56  ? 26  ASP   B OD1 1 
ATOM   968  O OD2 . ASP   B 1 27 ? 26.153  -7.440  -30.438 1.00 37.62  ? 26  ASP   B OD2 1 
ATOM   969  N N   . ASP   B 1 28 ? 29.529  -7.270  -34.308 1.00 52.05  ? 27  ASP   B N   1 
ATOM   970  C CA  . ASP   B 1 28 ? 30.957  -7.132  -34.582 1.00 56.12  ? 27  ASP   B CA  1 
ATOM   971  C C   . ASP   B 1 28 ? 31.747  -7.507  -33.331 1.00 58.90  ? 27  ASP   B C   1 
ATOM   972  O O   . ASP   B 1 28 ? 31.189  -7.491  -32.237 1.00 61.11  ? 27  ASP   B O   1 
ATOM   973  C CB  . ASP   B 1 28 ? 31.298  -5.734  -35.075 1.00 55.42  ? 27  ASP   B CB  1 
ATOM   974  C CG  . ASP   B 1 28 ? 32.159  -5.703  -36.333 1.00 59.58  ? 27  ASP   B CG  1 
ATOM   975  O OD1 . ASP   B 1 28 ? 33.226  -6.353  -36.337 1.00 67.60  ? 27  ASP   B OD1 1 
ATOM   976  O OD2 . ASP   B 1 28 ? 31.743  -5.052  -37.316 1.00 57.84  ? 27  ASP   B OD2 1 
ATOM   977  N N   . ILE   B 1 29 ? 33.034  -7.852  -33.504 1.00 70.01  ? 28  ILE   B N   1 
ATOM   978  C CA  . ILE   B 1 29 ? 33.886  -8.353  -32.431 1.00 70.41  ? 28  ILE   B CA  1 
ATOM   979  C C   . ILE   B 1 29 ? 35.009  -7.337  -32.156 1.00 75.77  ? 28  ILE   B C   1 
ATOM   980  O O   . ILE   B 1 29 ? 34.667  -6.160  -31.873 1.00 82.24  ? 28  ILE   B O   1 
ATOM   981  C CB  . ILE   B 1 29 ? 34.452  -9.745  -32.773 1.00 60.46  ? 28  ILE   B CB  1 
ATOM   982  N N   . VAL   B 1 34 ? 37.501  -10.345 -24.938 1.00 91.70  ? 33  VAL   B N   1 
ATOM   983  C CA  . VAL   B 1 34 ? 37.039  -11.760 -25.061 1.00 78.68  ? 33  VAL   B CA  1 
ATOM   984  C C   . VAL   B 1 34 ? 36.568  -11.958 -26.497 1.00 84.04  ? 33  VAL   B C   1 
ATOM   985  O O   . VAL   B 1 34 ? 35.503  -11.465 -26.860 1.00 99.43  ? 33  VAL   B O   1 
ATOM   986  C CB  . VAL   B 1 34 ? 35.928  -12.057 -24.027 1.00 70.93  ? 33  VAL   B CB  1 
ATOM   987  C CG1 . VAL   B 1 34 ? 34.897  -10.936 -23.965 1.00 69.64  ? 33  VAL   B CG1 1 
ATOM   988  C CG2 . VAL   B 1 34 ? 35.249  -13.414 -24.229 1.00 60.25  ? 33  VAL   B CG2 1 
ATOM   989  N N   . LYS   B 1 35 ? 37.388  -12.641 -27.310 1.00 81.35  ? 34  LYS   B N   1 
ATOM   990  C CA  . LYS   B 1 35 ? 37.015  -13.011 -28.672 1.00 73.91  ? 34  LYS   B CA  1 
ATOM   991  C C   . LYS   B 1 35 ? 36.142  -14.271 -28.641 1.00 73.49  ? 34  LYS   B C   1 
ATOM   992  O O   . LYS   B 1 35 ? 36.273  -15.091 -27.728 1.00 74.57  ? 34  LYS   B O   1 
ATOM   993  C CB  . LYS   B 1 35 ? 38.259  -13.158 -29.559 1.00 62.08  ? 34  LYS   B CB  1 
ATOM   994  N N   . PRO   B 1 36 ? 35.221  -14.482 -29.622 1.00 72.79  ? 35  PRO   B N   1 
ATOM   995  C CA  . PRO   B 1 36 ? 34.346  -15.661 -29.610 1.00 63.16  ? 35  PRO   B CA  1 
ATOM   996  C C   . PRO   B 1 36 ? 35.215  -16.911 -29.659 1.00 55.82  ? 35  PRO   B C   1 
ATOM   997  O O   . PRO   B 1 36 ? 36.281  -16.882 -30.262 1.00 54.71  ? 35  PRO   B O   1 
ATOM   998  C CB  . PRO   B 1 36 ? 33.476  -15.511 -30.878 1.00 59.60  ? 35  PRO   B CB  1 
ATOM   999  C CG  . PRO   B 1 36 ? 34.247  -14.544 -31.760 1.00 66.87  ? 35  PRO   B CG  1 
ATOM   1000 C CD  . PRO   B 1 36 ? 35.004  -13.630 -30.808 1.00 67.99  ? 35  PRO   B CD  1 
ATOM   1001 N N   . PRO   B 1 37 ? 34.814  -18.036 -29.027 1.00 55.05  ? 36  PRO   B N   1 
ATOM   1002 C CA  . PRO   B 1 37 ? 35.543  -19.294 -29.195 1.00 52.81  ? 36  PRO   B CA  1 
ATOM   1003 C C   . PRO   B 1 37 ? 35.641  -19.613 -30.689 1.00 62.18  ? 36  PRO   B C   1 
ATOM   1004 O O   . PRO   B 1 37 ? 34.928  -19.028 -31.507 1.00 54.71  ? 36  PRO   B O   1 
ATOM   1005 C CB  . PRO   B 1 37 ? 34.664  -20.312 -28.442 1.00 55.17  ? 36  PRO   B CB  1 
ATOM   1006 C CG  . PRO   B 1 37 ? 33.886  -19.484 -27.442 1.00 50.27  ? 36  PRO   B CG  1 
ATOM   1007 C CD  . PRO   B 1 37 ? 33.660  -18.147 -28.120 1.00 55.07  ? 36  PRO   B CD  1 
ATOM   1008 N N   . PRO   B 1 38 ? 36.519  -20.548 -31.119 1.00 63.23  ? 37  PRO   B N   1 
ATOM   1009 C CA  . PRO   B 1 38 ? 36.591  -20.915 -32.539 1.00 64.11  ? 37  PRO   B CA  1 
ATOM   1010 C C   . PRO   B 1 38 ? 35.257  -21.425 -33.094 1.00 55.15  ? 37  PRO   B C   1 
ATOM   1011 O O   . PRO   B 1 38 ? 34.537  -22.156 -32.410 1.00 52.10  ? 37  PRO   B O   1 
ATOM   1012 C CB  . PRO   B 1 38 ? 37.708  -21.983 -32.581 1.00 57.53  ? 37  PRO   B CB  1 
ATOM   1013 C CG  . PRO   B 1 38 ? 38.513  -21.733 -31.315 1.00 60.74  ? 37  PRO   B CG  1 
ATOM   1014 C CD  . PRO   B 1 38 ? 37.491  -21.276 -30.283 1.00 66.87  ? 37  PRO   B CD  1 
ATOM   1015 N N   . ASN   B 1 39 ? 34.941  -20.994 -34.327 1.00 48.75  ? 38  ASN   B N   1 
ATOM   1016 C CA  . ASN   B 1 39 ? 33.763  -21.377 -35.103 1.00 49.06  ? 38  ASN   B CA  1 
ATOM   1017 C C   . ASN   B 1 39 ? 32.483  -20.688 -34.620 1.00 42.57  ? 38  ASN   B C   1 
ATOM   1018 O O   . ASN   B 1 39 ? 31.416  -20.992 -35.132 1.00 43.23  ? 38  ASN   B O   1 
ATOM   1019 C CB  . ASN   B 1 39 ? 33.446  -22.871 -35.069 1.00 48.48  ? 38  ASN   B CB  1 
ATOM   1020 C CG  . ASN   B 1 39 ? 34.664  -23.759 -35.139 1.00 64.48  ? 38  ASN   B CG  1 
ATOM   1021 O OD1 . ASN   B 1 39 ? 34.809  -24.656 -34.300 1.00 74.51  ? 38  ASN   B OD1 1 
ATOM   1022 N ND2 . ASN   B 1 39 ? 35.539  -23.540 -36.114 1.00 59.02  ? 38  ASN   B ND2 1 
ATOM   1023 N N   . LYS   B 1 40 ? 32.568  -19.785 -33.637 1.00 42.72  ? 39  LYS   B N   1 
ATOM   1024 C CA  . LYS   B 1 40 ? 31.369  -19.219 -33.031 1.00 44.61  ? 39  LYS   B CA  1 
ATOM   1025 C C   . LYS   B 1 40 ? 31.292  -17.726 -33.330 1.00 43.05  ? 39  LYS   B C   1 
ATOM   1026 O O   . LYS   B 1 40 ? 32.296  -17.108 -33.658 1.00 40.19  ? 39  LYS   B O   1 
ATOM   1027 C CB  . LYS   B 1 40 ? 31.410  -19.460 -31.522 1.00 42.20  ? 39  LYS   B CB  1 
ATOM   1028 C CG  . LYS   B 1 40 ? 31.129  -20.891 -31.153 1.00 43.76  ? 39  LYS   B CG  1 
ATOM   1029 C CD  . LYS   B 1 40 ? 31.044  -21.031 -29.640 1.00 55.14  ? 39  LYS   B CD  1 
ATOM   1030 C CE  . LYS   B 1 40 ? 30.031  -22.026 -29.176 1.00 58.98  ? 39  LYS   B CE  1 
ATOM   1031 N NZ  . LYS   B 1 40 ? 30.187  -23.298 -29.882 1.00 63.20  ? 39  LYS   B NZ  1 
ATOM   1032 N N   . TYR   B 1 41 ? 30.094  -17.155 -33.203 1.00 39.02  ? 40  TYR   B N   1 
ATOM   1033 C CA  . TYR   B 1 41 ? 29.923  -15.740 -33.488 1.00 35.18  ? 40  TYR   B CA  1 
ATOM   1034 C C   . TYR   B 1 41 ? 29.360  -15.035 -32.259 1.00 39.03  ? 40  TYR   B C   1 
ATOM   1035 O O   . TYR   B 1 41 ? 28.615  -15.651 -31.501 1.00 34.11  ? 40  TYR   B O   1 
ATOM   1036 C CB  . TYR   B 1 41 ? 28.901  -15.609 -34.614 1.00 34.44  ? 40  TYR   B CB  1 
ATOM   1037 C CG  . TYR   B 1 41 ? 29.417  -16.064 -35.972 1.00 36.43  ? 40  TYR   B CG  1 
ATOM   1038 C CD1 . TYR   B 1 41 ? 30.060  -15.170 -36.826 1.00 35.63  ? 40  TYR   B CD1 1 
ATOM   1039 C CD2 . TYR   B 1 41 ? 29.217  -17.367 -36.416 1.00 34.67  ? 40  TYR   B CD2 1 
ATOM   1040 C CE1 . TYR   B 1 41 ? 30.534  -15.576 -38.070 1.00 38.82  ? 40  TYR   B CE1 1 
ATOM   1041 C CE2 . TYR   B 1 41 ? 29.689  -17.782 -37.657 1.00 37.02  ? 40  TYR   B CE2 1 
ATOM   1042 C CZ  . TYR   B 1 41 ? 30.376  -16.890 -38.472 1.00 36.97  ? 40  TYR   B CZ  1 
ATOM   1043 O OH  . TYR   B 1 41 ? 30.801  -17.269 -39.719 1.00 38.89  ? 40  TYR   B OH  1 
ATOM   1044 N N   . PRO   B 1 42 ? 29.612  -13.709 -32.098 1.00 39.15  ? 41  PRO   B N   1 
ATOM   1045 C CA  . PRO   B 1 42 ? 28.891  -12.912 -31.100 1.00 33.47  ? 41  PRO   B CA  1 
ATOM   1046 C C   . PRO   B 1 42 ? 27.452  -12.674 -31.574 1.00 33.17  ? 41  PRO   B C   1 
ATOM   1047 O O   . PRO   B 1 42 ? 27.219  -12.036 -32.617 1.00 35.95  ? 41  PRO   B O   1 
ATOM   1048 C CB  . PRO   B 1 42 ? 29.688  -11.590 -31.011 1.00 35.31  ? 41  PRO   B CB  1 
ATOM   1049 C CG  . PRO   B 1 42 ? 30.591  -11.545 -32.236 1.00 37.98  ? 41  PRO   B CG  1 
ATOM   1050 C CD  . PRO   B 1 42 ? 30.520  -12.902 -32.938 1.00 36.94  ? 41  PRO   B CD  1 
ATOM   1051 N N   . ILE   B 1 43 ? 26.488  -13.157 -30.773 1.00 31.44  ? 42  ILE   B N   1 
ATOM   1052 C CA  . ILE   B 1 43 ? 25.071  -12.980 -31.053 1.00 30.62  ? 42  ILE   B CA  1 
ATOM   1053 C C   . ILE   B 1 43 ? 24.443  -11.949 -30.106 1.00 30.70  ? 42  ILE   B C   1 
ATOM   1054 O O   . ILE   B 1 43 ? 24.639  -12.019 -28.909 1.00 35.40  ? 42  ILE   B O   1 
ATOM   1055 C CB  . ILE   B 1 43 ? 24.340  -14.325 -30.909 1.00 31.42  ? 42  ILE   B CB  1 
ATOM   1056 C CG1 . ILE   B 1 43 ? 25.078  -15.463 -31.672 1.00 30.18  ? 42  ILE   B CG1 1 
ATOM   1057 C CG2 . ILE   B 1 43 ? 22.879  -14.180 -31.337 1.00 32.32  ? 42  ILE   B CG2 1 
ATOM   1058 C CD1 . ILE   B 1 43 ? 25.392  -15.137 -33.122 1.00 29.56  ? 42  ILE   B CD1 1 
ATOM   1059 N N   . PHE   B 1 44 ? 23.588  -11.080 -30.652 1.00 29.64  ? 43  PHE   B N   1 
ATOM   1060 C CA  . PHE   B 1 44 ? 22.774  -10.133 -29.898 1.00 31.58  ? 43  PHE   B CA  1 
ATOM   1061 C C   . PHE   B 1 44 ? 21.314  -10.543 -30.071 1.00 28.34  ? 43  PHE   B C   1 
ATOM   1062 O O   . PHE   B 1 44 ? 20.823  -10.651 -31.197 1.00 28.90  ? 43  PHE   B O   1 
ATOM   1063 C CB  . PHE   B 1 44 ? 23.027  -8.684  -30.359 1.00 29.27  ? 43  PHE   B CB  1 
ATOM   1064 C CG  . PHE   B 1 44 ? 22.120  -7.662  -29.682 1.00 27.83  ? 43  PHE   B CG  1 
ATOM   1065 C CD1 . PHE   B 1 44 ? 20.914  -7.269  -30.270 1.00 29.16  ? 43  PHE   B CD1 1 
ATOM   1066 C CD2 . PHE   B 1 44 ? 22.422  -7.174  -28.416 1.00 34.49  ? 43  PHE   B CD2 1 
ATOM   1067 C CE1 . PHE   B 1 44 ? 20.062  -6.364  -29.642 1.00 30.06  ? 43  PHE   B CE1 1 
ATOM   1068 C CE2 . PHE   B 1 44 ? 21.577  -6.257  -27.780 1.00 30.59  ? 43  PHE   B CE2 1 
ATOM   1069 C CZ  . PHE   B 1 44 ? 20.397  -5.876  -28.391 1.00 30.78  ? 43  PHE   B CZ  1 
ATOM   1070 N N   . PHE   B 1 45 ? 20.652  -10.893 -28.962 1.00 29.26  ? 44  PHE   B N   1 
ATOM   1071 C CA  . PHE   B 1 45 ? 19.245  -11.257 -28.977 1.00 25.56  ? 44  PHE   B CA  1 
ATOM   1072 C C   . PHE   B 1 45 ? 18.390  -10.006 -28.866 1.00 27.25  ? 44  PHE   B C   1 
ATOM   1073 O O   . PHE   B 1 45 ? 18.482  -9.273  -27.884 1.00 28.37  ? 44  PHE   B O   1 
ATOM   1074 C CB  . PHE   B 1 45 ? 18.931  -12.225 -27.824 1.00 25.12  ? 44  PHE   B CB  1 
ATOM   1075 C CG  . PHE   B 1 45 ? 19.672  -13.551 -27.976 1.00 24.07  ? 44  PHE   B CG  1 
ATOM   1076 C CD1 . PHE   B 1 45 ? 21.019  -13.682 -27.626 1.00 26.58  ? 44  PHE   B CD1 1 
ATOM   1077 C CD2 . PHE   B 1 45 ? 19.013  -14.678 -28.454 1.00 25.30  ? 44  PHE   B CD2 1 
ATOM   1078 C CE1 . PHE   B 1 45 ? 21.689  -14.891 -27.810 1.00 30.26  ? 44  PHE   B CE1 1 
ATOM   1079 C CE2 . PHE   B 1 45 ? 19.674  -15.894 -28.603 1.00 28.63  ? 44  PHE   B CE2 1 
ATOM   1080 C CZ  . PHE   B 1 45 ? 21.021  -16.001 -28.304 1.00 26.91  ? 44  PHE   B CZ  1 
ATOM   1081 N N   . PHE   B 1 46 ? 17.527  -9.765  -29.862 1.00 26.71  ? 45  PHE   B N   1 
ATOM   1082 C CA  . PHE   B 1 46 ? 16.591  -8.658  -29.755 1.00 27.17  ? 45  PHE   B CA  1 
ATOM   1083 C C   . PHE   B 1 46 ? 15.609  -8.918  -28.605 1.00 28.86  ? 45  PHE   B C   1 
ATOM   1084 O O   . PHE   B 1 46 ? 15.372  -10.055 -28.216 1.00 26.56  ? 45  PHE   B O   1 
ATOM   1085 C CB  . PHE   B 1 46 ? 15.857  -8.433  -31.073 1.00 26.94  ? 45  PHE   B CB  1 
ATOM   1086 C CG  . PHE   B 1 46 ? 16.800  -7.999  -32.192 1.00 30.48  ? 45  PHE   B CG  1 
ATOM   1087 C CD1 . PHE   B 1 46 ? 17.245  -6.677  -32.274 1.00 33.00  ? 45  PHE   B CD1 1 
ATOM   1088 C CD2 . PHE   B 1 46 ? 17.180  -8.883  -33.206 1.00 30.71  ? 45  PHE   B CD2 1 
ATOM   1089 C CE1 . PHE   B 1 46 ? 18.057  -6.247  -33.324 1.00 31.61  ? 45  PHE   B CE1 1 
ATOM   1090 C CE2 . PHE   B 1 46 ? 18.030  -8.457  -34.233 1.00 29.10  ? 45  PHE   B CE2 1 
ATOM   1091 C CZ  . PHE   B 1 46 ? 18.460  -7.135  -34.288 1.00 28.64  ? 45  PHE   B CZ  1 
ATOM   1092 N N   . GLY   B 1 47 ? 15.055  -7.840  -28.042 1.00 29.20  ? 46  GLY   B N   1 
ATOM   1093 C CA  . GLY   B 1 47 ? 14.005  -7.980  -27.043 1.00 30.14  ? 46  GLY   B CA  1 
ATOM   1094 C C   . GLY   B 1 47 ? 14.629  -8.127  -25.665 1.00 34.72  ? 46  GLY   B C   1 
ATOM   1095 O O   . GLY   B 1 47 ? 14.473  -7.241  -24.846 1.00 30.79  ? 46  GLY   B O   1 
ATOM   1096 N N   . THR   B 1 48 ? 15.358  -9.221  -25.433 1.00 30.20  ? 47  THR   B N   1 
ATOM   1097 C CA  . THR   B 1 48 ? 16.060  -9.423  -24.175 1.00 33.99  ? 47  THR   B CA  1 
ATOM   1098 C C   . THR   B 1 48 ? 17.313  -8.554  -24.109 1.00 36.72  ? 47  THR   B C   1 
ATOM   1099 O O   . THR   B 1 48 ? 17.739  -8.173  -23.023 1.00 32.97  ? 47  THR   B O   1 
ATOM   1100 C CB  . THR   B 1 48 ? 16.388  -10.902 -23.967 1.00 33.67  ? 47  THR   B CB  1 
ATOM   1101 O OG1 . THR   B 1 48 ? 17.328  -11.280 -24.977 1.00 29.65  ? 47  THR   B OG1 1 
ATOM   1102 C CG2 . THR   B 1 48 ? 15.121  -11.745 -23.966 1.00 30.64  ? 47  THR   B CG2 1 
ATOM   1103 N N   . HIS   B 1 49 ? 17.922  -8.296  -25.272 1.00 31.89  ? 48  HIS   B N   1 
ATOM   1104 C CA  . HIS   B 1 49 ? 19.161  -7.544  -25.381 1.00 33.59  ? 48  HIS   B CA  1 
ATOM   1105 C C   . HIS   B 1 49 ? 20.340  -8.258  -24.733 1.00 34.43  ? 48  HIS   B C   1 
ATOM   1106 O O   . HIS   B 1 49 ? 21.297  -7.596  -24.351 1.00 39.05  ? 48  HIS   B O   1 
ATOM   1107 C CB  . HIS   B 1 49 ? 19.006  -6.090  -24.908 1.00 32.58  ? 48  HIS   B CB  1 
ATOM   1108 C CG  . HIS   B 1 49 ? 17.832  -5.395  -25.497 1.00 34.34  ? 48  HIS   B CG  1 
ATOM   1109 N ND1 . HIS   B 1 49 ? 17.049  -4.548  -24.748 1.00 37.29  ? 48  HIS   B ND1 1 
ATOM   1110 C CD2 . HIS   B 1 49 ? 17.264  -5.440  -26.718 1.00 31.77  ? 48  HIS   B CD2 1 
ATOM   1111 C CE1 . HIS   B 1 49 ? 16.060  -4.079  -25.505 1.00 37.70  ? 48  HIS   B CE1 1 
ATOM   1112 N NE2 . HIS   B 1 49 ? 16.171  -4.611  -26.714 1.00 34.51  ? 48  HIS   B NE2 1 
ATOM   1113 N N   . GLU   B 1 50 ? 20.304  -9.590  -24.646 1.00 31.86  ? 49  GLU   B N   1 
ATOM   1114 C CA  . GLU   B 1 50 ? 21.439  -10.357 -24.157 1.00 34.62  ? 49  GLU   B CA  1 
ATOM   1115 C C   . GLU   B 1 50 ? 22.352  -10.737 -25.322 1.00 36.50  ? 49  GLU   B C   1 
ATOM   1116 O O   . GLU   B 1 50 ? 21.981  -10.586 -26.493 1.00 35.15  ? 49  GLU   B O   1 
ATOM   1117 C CB  . GLU   B 1 50 ? 21.016  -11.653 -23.472 1.00 36.08  ? 49  GLU   B CB  1 
ATOM   1118 C CG  . GLU   B 1 50 ? 20.110  -11.364 -22.271 1.00 34.38  ? 49  GLU   B CG  1 
ATOM   1119 C CD  . GLU   B 1 50 ? 19.668  -12.602 -21.502 1.00 37.91  ? 49  GLU   B CD  1 
ATOM   1120 O OE1 . GLU   B 1 50 ? 18.669  -12.532 -20.770 1.00 39.20  ? 49  GLU   B OE1 1 
ATOM   1121 O OE2 . GLU   B 1 50 ? 20.356  -13.622 -21.583 1.00 35.88  ? 49  GLU   B OE2 1 
ATOM   1122 N N   . THR   B 1 51 ? 23.547  -11.213 -24.960 1.00 33.38  ? 50  THR   B N   1 
ATOM   1123 C CA  . THR   B 1 51 ? 24.560  -11.664 -25.903 1.00 35.29  ? 50  THR   B CA  1 
ATOM   1124 C C   . THR   B 1 51 ? 24.980  -13.069 -25.495 1.00 35.03  ? 50  THR   B C   1 
ATOM   1125 O O   . THR   B 1 51 ? 24.892  -13.449 -24.330 1.00 38.07  ? 50  THR   B O   1 
ATOM   1126 C CB  . THR   B 1 51 ? 25.762  -10.712 -25.990 1.00 35.69  ? 50  THR   B CB  1 
ATOM   1127 O OG1 . THR   B 1 51 ? 26.134  -10.544 -24.628 1.00 44.36  ? 50  THR   B OG1 1 
ATOM   1128 C CG2 . THR   B 1 51 ? 25.433  -9.327  -26.525 1.00 35.91  ? 50  THR   B CG2 1 
ATOM   1129 N N   . ALA   B 1 52 ? 25.361  -13.863 -26.489 1.00 36.07  ? 51  ALA   B N   1 
ATOM   1130 C CA  . ALA   B 1 52 ? 25.995  -15.145 -26.259 1.00 33.02  ? 51  ALA   B CA  1 
ATOM   1131 C C   . ALA   B 1 52 ? 26.838  -15.476 -27.484 1.00 36.19  ? 51  ALA   B C   1 
ATOM   1132 O O   . ALA   B 1 52 ? 26.787  -14.754 -28.480 1.00 38.94  ? 51  ALA   B O   1 
ATOM   1133 C CB  . ALA   B 1 52 ? 24.975  -16.219 -25.970 1.00 30.64  ? 51  ALA   B CB  1 
ATOM   1134 N N   . PHE   B 1 53 ? 27.639  -16.539 -27.379 1.00 33.22  ? 52  PHE   B N   1 
ATOM   1135 C CA  . PHE   B 1 53 ? 28.388  -17.015 -28.529 1.00 38.54  ? 52  PHE   B CA  1 
ATOM   1136 C C   . PHE   B 1 53 ? 27.703  -18.284 -29.042 1.00 39.33  ? 52  PHE   B C   1 
ATOM   1137 O O   . PHE   B 1 53 ? 27.454  -19.205 -28.275 1.00 37.33  ? 52  PHE   B O   1 
ATOM   1138 C CB  . PHE   B 1 53 ? 29.869  -17.286 -28.224 1.00 37.44  ? 52  PHE   B CB  1 
ATOM   1139 C CG  . PHE   B 1 53 ? 30.680  -16.085 -27.761 1.00 39.22  ? 52  PHE   B CG  1 
ATOM   1140 C CD1 . PHE   B 1 53 ? 30.897  -15.007 -28.608 1.00 44.86  ? 52  PHE   B CD1 1 
ATOM   1141 C CD2 . PHE   B 1 53 ? 31.221  -16.039 -26.481 1.00 45.98  ? 52  PHE   B CD2 1 
ATOM   1142 C CE1 . PHE   B 1 53 ? 31.626  -13.903 -28.185 1.00 44.06  ? 52  PHE   B CE1 1 
ATOM   1143 C CE2 . PHE   B 1 53 ? 31.957  -14.939 -26.058 1.00 45.49  ? 52  PHE   B CE2 1 
ATOM   1144 C CZ  . PHE   B 1 53 ? 32.154  -13.875 -26.908 1.00 43.27  ? 52  PHE   B CZ  1 
ATOM   1145 N N   . LEU   B 1 54 ? 27.421  -18.346 -30.349 1.00 34.87  ? 53  LEU   B N   1 
ATOM   1146 C CA  . LEU   B 1 54 ? 26.804  -19.546 -30.903 1.00 34.10  ? 53  LEU   B CA  1 
ATOM   1147 C C   . LEU   B 1 54 ? 27.509  -19.911 -32.210 1.00 35.96  ? 53  LEU   B C   1 
ATOM   1148 O O   . LEU   B 1 54 ? 28.051  -19.027 -32.872 1.00 31.20  ? 53  LEU   B O   1 
ATOM   1149 C CB  . LEU   B 1 54 ? 25.322  -19.289 -31.183 1.00 33.92  ? 53  LEU   B CB  1 
ATOM   1150 C CG  . LEU   B 1 54 ? 24.371  -19.213 -29.986 1.00 34.42  ? 53  LEU   B CG  1 
ATOM   1151 C CD1 . LEU   B 1 54 ? 22.996  -18.915 -30.553 1.00 34.27  ? 53  LEU   B CD1 1 
ATOM   1152 C CD2 . LEU   B 1 54 ? 24.350  -20.533 -29.212 1.00 28.62  ? 53  LEU   B CD2 1 
ATOM   1153 N N   . GLY   B 1 55 ? 27.417  -21.194 -32.588 1.00 32.90  ? 54  GLY   B N   1 
ATOM   1154 C CA  . GLY   B 1 55 ? 27.935  -21.679 -33.858 1.00 32.52  ? 54  GLY   B CA  1 
ATOM   1155 C C   . GLY   B 1 55 ? 26.827  -21.775 -34.903 1.00 30.04  ? 54  GLY   B C   1 
ATOM   1156 O O   . GLY   B 1 55 ? 25.625  -21.711 -34.583 1.00 30.80  ? 54  GLY   B O   1 
ATOM   1157 N N   . PRO   B 1 56 ? 27.208  -21.949 -36.186 1.00 28.99  ? 55  PRO   B N   1 
ATOM   1158 C CA  . PRO   B 1 56 ? 26.248  -21.947 -37.293 1.00 28.30  ? 55  PRO   B CA  1 
ATOM   1159 C C   . PRO   B 1 56 ? 25.087  -22.934 -37.217 1.00 27.78  ? 55  PRO   B C   1 
ATOM   1160 O O   . PRO   B 1 56 ? 24.038  -22.651 -37.760 1.00 28.89  ? 55  PRO   B O   1 
ATOM   1161 C CB  . PRO   B 1 56 ? 27.108  -22.166 -38.549 1.00 32.60  ? 55  PRO   B CB  1 
ATOM   1162 C CG  . PRO   B 1 56 ? 28.549  -21.895 -38.109 1.00 31.24  ? 55  PRO   B CG  1 
ATOM   1163 C CD  . PRO   B 1 56 ? 28.606  -22.122 -36.622 1.00 31.23  ? 55  PRO   B CD  1 
ATOM   1164 N N   . LYS   B 1 57 ? 25.247  -24.062 -36.499 1.00 29.51  ? 56  LYS   B N   1 
ATOM   1165 C CA  . LYS   B 1 57 ? 24.190  -25.066 -36.432 1.00 31.38  ? 56  LYS   B CA  1 
ATOM   1166 C C   . LYS   B 1 57 ? 22.961  -24.461 -35.752 1.00 29.21  ? 56  LYS   B C   1 
ATOM   1167 O O   . LYS   B 1 57 ? 21.838  -24.910 -35.983 1.00 28.85  ? 56  LYS   B O   1 
ATOM   1168 C CB  . LYS   B 1 57 ? 24.613  -26.360 -35.719 1.00 33.75  ? 56  LYS   B CB  1 
ATOM   1169 C CG  . LYS   B 1 57 ? 24.830  -26.214 -34.223 1.00 33.80  ? 56  LYS   B CG  1 
ATOM   1170 C CD  . LYS   B 1 57 ? 24.864  -27.605 -33.595 1.00 39.57  ? 56  LYS   B CD  1 
ATOM   1171 C CE  . LYS   B 1 57 ? 25.179  -27.629 -32.119 1.00 46.16  ? 56  LYS   B CE  1 
ATOM   1172 N NZ  . LYS   B 1 57 ? 24.139  -27.015 -31.286 1.00 48.39  ? 56  LYS   B NZ  1 
ATOM   1173 N N   . ASP   B 1 58 ? 23.195  -23.395 -34.971 1.00 29.98  ? 57  ASP   B N   1 
ATOM   1174 C CA  . ASP   B 1 58 ? 22.159  -22.749 -34.179 1.00 31.32  ? 57  ASP   B CA  1 
ATOM   1175 C C   . ASP   B 1 58 ? 21.739  -21.387 -34.747 1.00 28.60  ? 57  ASP   B C   1 
ATOM   1176 O O   . ASP   B 1 58 ? 20.947  -20.681 -34.104 1.00 26.73  ? 57  ASP   B O   1 
ATOM   1177 C CB  . ASP   B 1 58 ? 22.580  -22.672 -32.720 1.00 31.47  ? 57  ASP   B CB  1 
ATOM   1178 C CG  . ASP   B 1 58 ? 22.643  -24.029 -32.024 1.00 35.94  ? 57  ASP   B CG  1 
ATOM   1179 O OD1 . ASP   B 1 58 ? 21.712  -24.822 -32.231 1.00 34.35  ? 57  ASP   B OD1 1 
ATOM   1180 O OD2 . ASP   B 1 58 ? 23.609  -24.265 -31.280 1.00 36.40  ? 57  ASP   B OD2 1 
ATOM   1181 N N   . LEU   B 1 59 ? 22.168  -21.069 -35.979 1.00 28.10  ? 58  LEU   B N   1 
ATOM   1182 C CA  . LEU   B 1 59 ? 21.909  -19.765 -36.583 1.00 26.36  ? 58  LEU   B CA  1 
ATOM   1183 C C   . LEU   B 1 59 ? 21.164  -19.961 -37.894 1.00 27.13  ? 58  LEU   B C   1 
ATOM   1184 O O   . LEU   B 1 59 ? 21.633  -20.662 -38.790 1.00 29.61  ? 58  LEU   B O   1 
ATOM   1185 C CB  . LEU   B 1 59 ? 23.225  -19.018 -36.818 1.00 30.42  ? 58  LEU   B CB  1 
ATOM   1186 C CG  . LEU   B 1 59 ? 24.057  -18.773 -35.552 1.00 29.24  ? 58  LEU   B CG  1 
ATOM   1187 C CD1 . LEU   B 1 59 ? 25.379  -18.075 -35.848 1.00 29.24  ? 58  LEU   B CD1 1 
ATOM   1188 C CD2 . LEU   B 1 59 ? 23.237  -17.951 -34.554 1.00 26.76  ? 58  LEU   B CD2 1 
ATOM   1189 N N   . PHE   B 1 60 ? 20.005  -19.338 -37.981 1.00 24.96  ? 59  PHE   B N   1 
ATOM   1190 C CA  . PHE   B 1 60 ? 19.096  -19.518 -39.101 1.00 26.80  ? 59  PHE   B CA  1 
ATOM   1191 C C   . PHE   B 1 60 ? 18.905  -18.160 -39.780 1.00 28.83  ? 59  PHE   B C   1 
ATOM   1192 O O   . PHE   B 1 60 ? 18.285  -17.278 -39.204 1.00 25.47  ? 59  PHE   B O   1 
ATOM   1193 C CB  . PHE   B 1 60 ? 17.783  -20.033 -38.508 1.00 26.95  ? 59  PHE   B CB  1 
ATOM   1194 C CG  . PHE   B 1 60 ? 17.859  -21.456 -37.960 1.00 25.64  ? 59  PHE   B CG  1 
ATOM   1195 C CD1 . PHE   B 1 60 ? 18.345  -21.700 -36.681 1.00 26.98  ? 59  PHE   B CD1 1 
ATOM   1196 C CD2 . PHE   B 1 60 ? 17.449  -22.545 -38.743 1.00 28.08  ? 59  PHE   B CD2 1 
ATOM   1197 C CE1 . PHE   B 1 60 ? 18.427  -23.004 -36.186 1.00 28.24  ? 59  PHE   B CE1 1 
ATOM   1198 C CE2 . PHE   B 1 60 ? 17.533  -23.850 -38.252 1.00 30.11  ? 59  PHE   B CE2 1 
ATOM   1199 C CZ  . PHE   B 1 60 ? 18.019  -24.072 -36.967 1.00 28.29  ? 59  PHE   B CZ  1 
ATOM   1200 N N   . PRO   B 1 61 ? 19.391  -17.962 -41.034 1.00 33.74  ? 60  PRO   B N   1 
ATOM   1201 C CA  . PRO   B 1 61 ? 19.165  -16.697 -41.749 1.00 34.28  ? 60  PRO   B CA  1 
ATOM   1202 C C   . PRO   B 1 61 ? 17.712  -16.225 -41.697 1.00 32.06  ? 60  PRO   B C   1 
ATOM   1203 O O   . PRO   B 1 61 ? 16.791  -16.999 -41.968 1.00 32.71  ? 60  PRO   B O   1 
ATOM   1204 C CB  . PRO   B 1 61 ? 19.673  -17.007 -43.166 1.00 35.92  ? 60  PRO   B CB  1 
ATOM   1205 C CG  . PRO   B 1 61 ? 20.783  -18.006 -42.918 1.00 39.36  ? 60  PRO   B CG  1 
ATOM   1206 C CD  . PRO   B 1 61 ? 20.212  -18.911 -41.804 1.00 37.60  ? 60  PRO   B CD  1 
ATOM   1207 N N   . TYR   B 1 62 ? 17.519  -14.938 -41.341 1.00 28.72  ? 61  TYR   B N   1 
ATOM   1208 C CA  . TYR   B 1 62 ? 16.224  -14.408 -40.944 1.00 31.05  ? 61  TYR   B CA  1 
ATOM   1209 C C   . TYR   B 1 62 ? 15.212  -14.438 -42.090 1.00 35.42  ? 61  TYR   B C   1 
ATOM   1210 O O   . TYR   B 1 62 ? 14.075  -14.855 -41.902 1.00 35.59  ? 61  TYR   B O   1 
ATOM   1211 C CB  . TYR   B 1 62 ? 16.376  -12.973 -40.430 1.00 35.30  ? 61  TYR   B CB  1 
ATOM   1212 C CG  . TYR   B 1 62 ? 15.040  -12.282 -40.191 1.00 34.41  ? 61  TYR   B CG  1 
ATOM   1213 C CD1 . TYR   B 1 62 ? 14.308  -12.499 -39.031 1.00 33.54  ? 61  TYR   B CD1 1 
ATOM   1214 C CD2 . TYR   B 1 62 ? 14.534  -11.391 -41.125 1.00 40.63  ? 61  TYR   B CD2 1 
ATOM   1215 C CE1 . TYR   B 1 62 ? 13.108  -11.843 -38.802 1.00 35.06  ? 61  TYR   B CE1 1 
ATOM   1216 C CE2 . TYR   B 1 62 ? 13.339  -10.726 -40.914 1.00 38.32  ? 61  TYR   B CE2 1 
ATOM   1217 C CZ  . TYR   B 1 62 ? 12.627  -10.957 -39.753 1.00 36.57  ? 61  TYR   B CZ  1 
ATOM   1218 O OH  . TYR   B 1 62 ? 11.446  -10.291 -39.614 1.00 42.66  ? 61  TYR   B OH  1 
ATOM   1219 N N   . ASP   B 1 63 ? 15.661  -14.026 -43.283 1.00 44.14  ? 62  ASP   B N   1 
ATOM   1220 C CA  . ASP   B 1 63 ? 14.845  -13.982 -44.489 1.00 49.08  ? 62  ASP   B CA  1 
ATOM   1221 C C   . ASP   B 1 63 ? 14.249  -15.350 -44.826 1.00 40.61  ? 62  ASP   B C   1 
ATOM   1222 O O   . ASP   B 1 63 ? 13.052  -15.463 -45.059 1.00 40.12  ? 62  ASP   B O   1 
ATOM   1223 C CB  . ASP   B 1 63 ? 15.635  -13.402 -45.647 1.00 54.92  ? 62  ASP   B CB  1 
ATOM   1224 C CG  . ASP   B 1 63 ? 15.235  -11.986 -46.020 1.00 71.75  ? 62  ASP   B CG  1 
ATOM   1225 O OD1 . ASP   B 1 63 ? 15.381  -11.091 -45.160 1.00 76.54  ? 62  ASP   B OD1 1 
ATOM   1226 O OD2 . ASP   B 1 63 ? 14.749  -11.807 -47.160 1.00 82.02  ? 62  ASP   B OD2 1 
ATOM   1227 N N   . LYS   B 1 64 ? 15.090  -16.386 -44.824 1.00 40.47  ? 63  LYS   B N   1 
ATOM   1228 C CA  . LYS   B 1 64 ? 14.640  -17.727 -45.162 1.00 40.74  ? 63  LYS   B CA  1 
ATOM   1229 C C   . LYS   B 1 64 ? 13.624  -18.267 -44.149 1.00 39.60  ? 63  LYS   B C   1 
ATOM   1230 O O   . LYS   B 1 64 ? 12.712  -19.003 -44.514 1.00 38.38  ? 63  LYS   B O   1 
ATOM   1231 C CB  . LYS   B 1 64 ? 15.870  -18.638 -45.231 1.00 44.14  ? 63  LYS   B CB  1 
ATOM   1232 C CG  . LYS   B 1 64 ? 15.565  -20.049 -45.720 1.00 43.15  ? 63  LYS   B CG  1 
ATOM   1233 C CD  . LYS   B 1 64 ? 16.828  -20.888 -45.651 1.00 47.97  ? 63  LYS   B CD  1 
ATOM   1234 C CE  . LYS   B 1 64 ? 16.776  -22.161 -46.424 1.00 47.00  ? 63  LYS   B CE  1 
ATOM   1235 N NZ  . LYS   B 1 64 ? 15.624  -22.982 -46.077 1.00 44.40  ? 63  LYS   B NZ  1 
ATOM   1236 N N   . SER   B 1 65 ? 13.790  -17.921 -42.871 1.00 37.75  ? 64  SER   B N   1 
ATOM   1237 C CA  . SER   B 1 65 ? 13.174  -18.692 -41.802 1.00 35.00  ? 64  SER   B CA  1 
ATOM   1238 C C   . SER   B 1 65 ? 12.098  -17.897 -41.050 1.00 34.66  ? 64  SER   B C   1 
ATOM   1239 O O   . SER   B 1 65 ? 11.464  -18.416 -40.134 1.00 36.29  ? 64  SER   B O   1 
ATOM   1240 C CB  . SER   B 1 65 ? 14.250  -19.216 -40.889 1.00 36.44  ? 64  SER   B CB  1 
ATOM   1241 O OG  . SER   B 1 65 ? 14.954  -18.125 -40.318 1.00 48.44  ? 64  SER   B OG  1 
ATOM   1242 N N   . LYS   B 1 66 ? 11.835  -16.656 -41.470 1.00 35.87  ? 65  LYS   B N   1 
ATOM   1243 C CA  . LYS   B 1 66 ? 10.982  -15.776 -40.685 1.00 39.57  ? 65  LYS   B CA  1 
ATOM   1244 C C   . LYS   B 1 66 ? 9.535   -16.259 -40.661 1.00 44.13  ? 65  LYS   B C   1 
ATOM   1245 O O   . LYS   B 1 66 ? 8.829   -15.994 -39.695 1.00 43.29  ? 65  LYS   B O   1 
ATOM   1246 C CB  . LYS   B 1 66 ? 11.046  -14.298 -41.091 1.00 41.85  ? 65  LYS   B CB  1 
ATOM   1247 C CG  . LYS   B 1 66 ? 10.752  -14.047 -42.566 1.00 46.05  ? 65  LYS   B CG  1 
ATOM   1248 C CD  . LYS   B 1 66 ? 11.140  -12.671 -43.093 1.00 57.25  ? 65  LYS   B CD  1 
ATOM   1249 C CE  . LYS   B 1 66 ? 10.175  -11.604 -42.679 1.00 66.07  ? 65  LYS   B CE  1 
ATOM   1250 N NZ  . LYS   B 1 66 ? 10.172  -10.497 -43.640 1.00 67.30  ? 65  LYS   B NZ  1 
ATOM   1251 N N   . ASP   B 1 67 ? 9.067   -16.960 -41.694 1.00 42.37  ? 66  ASP   B N   1 
ATOM   1252 C CA  . ASP   B 1 67 ? 7.656   -17.295 -41.603 1.00 50.52  ? 66  ASP   B CA  1 
ATOM   1253 C C   . ASP   B 1 67 ? 7.462   -18.531 -40.727 1.00 45.30  ? 66  ASP   B C   1 
ATOM   1254 O O   . ASP   B 1 67 ? 6.391   -18.716 -40.156 1.00 53.17  ? 66  ASP   B O   1 
ATOM   1255 C CB  . ASP   B 1 67 ? 6.914   -17.199 -42.924 1.00 62.49  ? 66  ASP   B CB  1 
ATOM   1256 C CG  . ASP   B 1 67 ? 7.376   -18.147 -44.013 1.00 72.82  ? 66  ASP   B CG  1 
ATOM   1257 O OD1 . ASP   B 1 67 ? 7.530   -17.670 -45.160 1.00 79.16  ? 66  ASP   B OD1 1 
ATOM   1258 O OD2 . ASP   B 1 67 ? 7.565   -19.345 -43.698 1.00 76.05  ? 66  ASP   B OD2 1 
ATOM   1259 N N   . LYS   B 1 68 ? 8.524   -19.326 -40.567 1.00 41.54  ? 67  LYS   B N   1 
ATOM   1260 C CA  . LYS   B 1 68 ? 8.497   -20.473 -39.670 1.00 39.54  ? 67  LYS   B CA  1 
ATOM   1261 C C   . LYS   B 1 68 ? 8.717   -20.037 -38.218 1.00 37.59  ? 67  LYS   B C   1 
ATOM   1262 O O   . LYS   B 1 68 ? 8.019   -20.514 -37.326 1.00 37.52  ? 67  LYS   B O   1 
ATOM   1263 C CB  . LYS   B 1 68 ? 9.542   -21.476 -40.154 1.00 42.24  ? 67  LYS   B CB  1 
ATOM   1264 C CG  . LYS   B 1 68 ? 9.634   -22.769 -39.372 1.00 52.72  ? 67  LYS   B CG  1 
ATOM   1265 C CD  . LYS   B 1 68 ? 10.692  -23.653 -40.020 1.00 60.90  ? 67  LYS   B CD  1 
ATOM   1266 C CE  . LYS   B 1 68 ? 10.957  -24.930 -39.281 1.00 71.78  ? 67  LYS   B CE  1 
ATOM   1267 N NZ  . LYS   B 1 68 ? 9.783   -25.802 -39.190 1.00 76.25  ? 67  LYS   B NZ  1 
ATOM   1268 N N   . TYR   B 1 69 ? 9.695   -19.148 -37.970 1.00 33.30  ? 68  TYR   B N   1 
ATOM   1269 C CA  . TYR   B 1 69 ? 10.115  -18.867 -36.596 1.00 29.40  ? 68  TYR   B CA  1 
ATOM   1270 C C   . TYR   B 1 69 ? 9.589   -17.526 -36.093 1.00 32.07  ? 68  TYR   B C   1 
ATOM   1271 O O   . TYR   B 1 69 ? 9.703   -17.232 -34.900 1.00 31.17  ? 68  TYR   B O   1 
ATOM   1272 C CB  . TYR   B 1 69 ? 11.642  -18.921 -36.458 1.00 28.57  ? 68  TYR   B CB  1 
ATOM   1273 C CG  . TYR   B 1 69 ? 12.243  -20.291 -36.752 1.00 31.60  ? 68  TYR   B CG  1 
ATOM   1274 C CD1 . TYR   B 1 69 ? 11.682  -21.456 -36.242 1.00 31.84  ? 68  TYR   B CD1 1 
ATOM   1275 C CD2 . TYR   B 1 69 ? 13.367  -20.411 -37.564 1.00 32.23  ? 68  TYR   B CD2 1 
ATOM   1276 C CE1 . TYR   B 1 69 ? 12.242  -22.706 -36.501 1.00 34.32  ? 68  TYR   B CE1 1 
ATOM   1277 C CE2 . TYR   B 1 69 ? 13.909  -21.646 -37.862 1.00 35.31  ? 68  TYR   B CE2 1 
ATOM   1278 C CZ  . TYR   B 1 69 ? 13.342  -22.799 -37.338 1.00 35.78  ? 68  TYR   B CZ  1 
ATOM   1279 O OH  . TYR   B 1 69 ? 13.940  -23.987 -37.652 1.00 34.11  ? 68  TYR   B OH  1 
ATOM   1280 N N   . GLY   B 1 70 ? 9.048   -16.704 -37.000 1.00 30.34  ? 69  GLY   B N   1 
ATOM   1281 C CA  . GLY   B 1 70 ? 8.778   -15.318 -36.651 1.00 37.85  ? 69  GLY   B CA  1 
ATOM   1282 C C   . GLY   B 1 70 ? 7.369   -15.085 -36.104 1.00 40.37  ? 69  GLY   B C   1 
ATOM   1283 O O   . GLY   B 1 70 ? 6.784   -14.049 -36.385 1.00 44.08  ? 69  GLY   B O   1 
ATOM   1284 N N   . LYS   B 1 71 ? 6.821   -16.043 -35.347 1.00 41.55  ? 70  LYS   B N   1 
ATOM   1285 C CA  . LYS   B 1 71 ? 5.467   -15.917 -34.836 1.00 44.71  ? 70  LYS   B CA  1 
ATOM   1286 C C   . LYS   B 1 71 ? 5.526   -15.477 -33.383 1.00 44.34  ? 70  LYS   B C   1 
ATOM   1287 O O   . LYS   B 1 71 ? 6.343   -16.002 -32.631 1.00 45.45  ? 70  LYS   B O   1 
ATOM   1288 C CB  . LYS   B 1 71 ? 4.701   -17.245 -34.798 1.00 49.42  ? 70  LYS   B CB  1 
ATOM   1289 C CG  . LYS   B 1 71 ? 3.713   -17.487 -35.932 1.00 63.07  ? 70  LYS   B CG  1 
ATOM   1290 C CD  . LYS   B 1 71 ? 4.334   -17.578 -37.317 1.00 65.12  ? 70  LYS   B CD  1 
ATOM   1291 C CE  . LYS   B 1 71 ? 3.323   -17.806 -38.402 1.00 69.83  ? 70  LYS   B CE  1 
ATOM   1292 N NZ  . LYS   B 1 71 ? 3.892   -17.416 -39.697 1.00 72.70  ? 70  LYS   B NZ  1 
ATOM   1293 N N   . PRO   B 1 72 ? 4.623   -14.574 -32.932 1.00 43.56  ? 71  PRO   B N   1 
ATOM   1294 C CA  . PRO   B 1 72 ? 4.606   -14.138 -31.531 1.00 44.06  ? 71  PRO   B CA  1 
ATOM   1295 C C   . PRO   B 1 72 ? 4.343   -15.309 -30.582 1.00 44.43  ? 71  PRO   B C   1 
ATOM   1296 O O   . PRO   B 1 72 ? 3.662   -16.258 -30.959 1.00 39.67  ? 71  PRO   B O   1 
ATOM   1297 C CB  . PRO   B 1 72 ? 3.513   -13.047 -31.450 1.00 43.03  ? 71  PRO   B CB  1 
ATOM   1298 C CG  . PRO   B 1 72 ? 3.145   -12.767 -32.891 1.00 46.12  ? 71  PRO   B CG  1 
ATOM   1299 C CD  . PRO   B 1 72 ? 3.551   -13.966 -33.737 1.00 44.43  ? 71  PRO   B CD  1 
ATOM   1300 N N   . ASN   B 1 73 ? 4.923   -15.254 -29.366 1.00 39.57  ? 72  ASN   B N   1 
ATOM   1301 C CA  . ASN   B 1 73 ? 4.650   -16.243 -28.333 1.00 37.53  ? 72  ASN   B CA  1 
ATOM   1302 C C   . ASN   B 1 73 ? 4.618   -15.543 -26.967 1.00 38.96  ? 72  ASN   B C   1 
ATOM   1303 O O   . ASN   B 1 73 ? 4.645   -14.313 -26.892 1.00 40.66  ? 72  ASN   B O   1 
ATOM   1304 C CB  . ASN   B 1 73 ? 5.598   -17.436 -28.421 1.00 35.23  ? 72  ASN   B CB  1 
ATOM   1305 C CG  . ASN   B 1 73 ? 7.040   -17.024 -28.235 1.00 35.20  ? 72  ASN   B CG  1 
ATOM   1306 O OD1 . ASN   B 1 73 ? 7.359   -16.319 -27.270 1.00 36.91  ? 72  ASN   B OD1 1 
ATOM   1307 N ND2 . ASN   B 1 73 ? 7.918   -17.405 -29.157 1.00 34.91  ? 72  ASN   B ND2 1 
ATOM   1308 N N   . LYS   B 1 74 ? 4.606   -16.328 -25.889 1.00 40.46  ? 73  LYS   B N   1 
ATOM   1309 C CA  . LYS   B 1 74 ? 4.451   -15.774 -24.542 1.00 41.38  ? 73  LYS   B CA  1 
ATOM   1310 C C   . LYS   B 1 74 ? 5.786   -15.734 -23.775 1.00 43.67  ? 73  LYS   B C   1 
ATOM   1311 O O   . LYS   B 1 74 ? 5.805   -15.594 -22.548 1.00 37.16  ? 73  LYS   B O   1 
ATOM   1312 C CB  . LYS   B 1 74 ? 3.327   -16.570 -23.858 1.00 40.60  ? 73  LYS   B CB  1 
ATOM   1313 N N   . ARG   B 1 75 ? 6.920   -15.870 -24.477 1.00 31.71  ? 74  ARG   B N   1 
ATOM   1314 C CA  . ARG   B 1 75 ? 8.202   -15.728 -23.811 1.00 33.87  ? 74  ARG   B CA  1 
ATOM   1315 C C   . ARG   B 1 75 ? 8.513   -14.241 -23.655 1.00 34.95  ? 74  ARG   B C   1 
ATOM   1316 O O   . ARG   B 1 75 ? 8.286   -13.443 -24.572 1.00 35.40  ? 74  ARG   B O   1 
ATOM   1317 C CB  . ARG   B 1 75 ? 9.348   -16.501 -24.479 1.00 32.92  ? 74  ARG   B CB  1 
ATOM   1318 C CG  . ARG   B 1 75 ? 9.052   -17.978 -24.701 1.00 31.47  ? 74  ARG   B CG  1 
ATOM   1319 C CD  . ARG   B 1 75 ? 9.067   -18.739 -23.388 1.00 33.46  ? 74  ARG   B CD  1 
ATOM   1320 N NE  . ARG   B 1 75 ? 9.217   -20.177 -23.643 1.00 34.03  ? 74  ARG   B NE  1 
ATOM   1321 C CZ  . ARG   B 1 75 ? 10.359  -20.813 -23.488 1.00 34.79  ? 74  ARG   B CZ  1 
ATOM   1322 N NH1 . ARG   B 1 75 ? 11.450  -20.181 -23.064 1.00 40.71  ? 74  ARG   B NH1 1 
ATOM   1323 N NH2 . ARG   B 1 75 ? 10.429  -22.089 -23.787 1.00 40.14  ? 74  ARG   B NH2 1 
ATOM   1324 N N   . LYS   B 1 76 ? 9.021   -13.877 -22.469 1.00 33.47  ? 75  LYS   B N   1 
ATOM   1325 C CA  . LYS   B 1 76 ? 9.300   -12.482 -22.149 1.00 30.45  ? 75  LYS   B CA  1 
ATOM   1326 C C   . LYS   B 1 76 ? 10.411  -11.954 -23.063 1.00 29.85  ? 75  LYS   B C   1 
ATOM   1327 O O   . LYS   B 1 76 ? 11.540  -12.488 -23.069 1.00 30.28  ? 75  LYS   B O   1 
ATOM   1328 C CB  . LYS   B 1 76 ? 9.759   -12.401 -20.689 1.00 31.86  ? 75  LYS   B CB  1 
ATOM   1329 C CG  . LYS   B 1 76 ? 10.078  -10.974 -20.232 1.00 32.88  ? 75  LYS   B CG  1 
ATOM   1330 C CD  . LYS   B 1 76 ? 10.570  -10.871 -18.795 1.00 37.94  ? 75  LYS   B CD  1 
ATOM   1331 C CE  . LYS   B 1 76 ? 10.829  -9.454  -18.367 1.00 46.44  ? 75  LYS   B CE  1 
ATOM   1332 N NZ  . LYS   B 1 76 ? 11.324  -9.457  -16.982 1.00 52.09  ? 75  LYS   B NZ  1 
ATOM   1333 N N   . GLY   B 1 77 ? 10.085  -10.874 -23.775 1.00 28.70  ? 76  GLY   B N   1 
ATOM   1334 C CA  . GLY   B 1 77 ? 11.031  -10.189 -24.648 1.00 31.13  ? 76  GLY   B CA  1 
ATOM   1335 C C   . GLY   B 1 77 ? 10.893  -10.616 -26.114 1.00 31.29  ? 76  GLY   B C   1 
ATOM   1336 O O   . GLY   B 1 77 ? 11.500  -10.010 -26.993 1.00 29.11  ? 76  GLY   B O   1 
ATOM   1337 N N   . PHE   B 1 78 ? 10.103  -11.668 -26.391 1.00 29.74  ? 77  PHE   B N   1 
ATOM   1338 C CA  . PHE   B 1 78 ? 10.091  -12.218 -27.747 1.00 27.81  ? 77  PHE   B CA  1 
ATOM   1339 C C   . PHE   B 1 78 ? 9.377   -11.270 -28.700 1.00 31.21  ? 77  PHE   B C   1 
ATOM   1340 O O   . PHE   B 1 78 ? 9.886   -10.954 -29.775 1.00 26.27  ? 77  PHE   B O   1 
ATOM   1341 C CB  . PHE   B 1 78 ? 9.432   -13.597 -27.767 1.00 27.73  ? 77  PHE   B CB  1 
ATOM   1342 C CG  . PHE   B 1 78 ? 9.706   -14.334 -29.070 1.00 27.12  ? 77  PHE   B CG  1 
ATOM   1343 C CD1 . PHE   B 1 78 ? 10.821  -15.164 -29.179 1.00 27.39  ? 77  PHE   B CD1 1 
ATOM   1344 C CD2 . PHE   B 1 78 ? 8.838   -14.227 -30.142 1.00 31.78  ? 77  PHE   B CD2 1 
ATOM   1345 C CE1 . PHE   B 1 78 ? 11.061  -15.878 -30.338 1.00 29.06  ? 77  PHE   B CE1 1 
ATOM   1346 C CE2 . PHE   B 1 78 ? 9.109   -14.910 -31.324 1.00 31.04  ? 77  PHE   B CE2 1 
ATOM   1347 C CZ  . PHE   B 1 78 ? 10.213  -15.736 -31.403 1.00 29.00  ? 77  PHE   B CZ  1 
ATOM   1348 N N   . ASN   B 1 79 ? 8.196   -10.783 -28.307 1.00 30.04  ? 78  ASN   B N   1 
ATOM   1349 C CA  . ASN   B 1 79 ? 7.463   -9.951  -29.248 1.00 30.71  ? 78  ASN   B CA  1 
ATOM   1350 C C   . ASN   B 1 79 ? 8.166   -8.608  -29.431 1.00 32.50  ? 78  ASN   B C   1 
ATOM   1351 O O   . ASN   B 1 79 ? 8.102   -8.016  -30.510 1.00 33.44  ? 78  ASN   B O   1 
ATOM   1352 C CB  . ASN   B 1 79 ? 5.996   -9.792  -28.858 1.00 32.30  ? 78  ASN   B CB  1 
ATOM   1353 C CG  . ASN   B 1 79 ? 5.266   -11.120 -28.822 1.00 40.21  ? 78  ASN   B CG  1 
ATOM   1354 O OD1 . ASN   B 1 79 ? 5.735   -12.117 -29.383 1.00 40.56  ? 78  ASN   B OD1 1 
ATOM   1355 N ND2 . ASN   B 1 79 ? 4.119   -11.172 -28.156 1.00 37.37  ? 78  ASN   B ND2 1 
ATOM   1356 N N   . GLU   B 1 80 ? 8.825   -8.132  -28.378 1.00 30.30  ? 79  GLU   B N   1 
ATOM   1357 C CA  . GLU   B 1 80 ? 9.636   -6.934  -28.519 1.00 32.35  ? 79  GLU   B CA  1 
ATOM   1358 C C   . GLU   B 1 80 ? 10.799  -7.213  -29.473 1.00 30.35  ? 79  GLU   B C   1 
ATOM   1359 O O   . GLU   B 1 80 ? 11.145  -6.356  -30.270 1.00 31.08  ? 79  GLU   B O   1 
ATOM   1360 C CB  . GLU   B 1 80 ? 10.116  -6.383  -27.184 1.00 31.94  ? 79  GLU   B CB  1 
ATOM   1361 C CG  . GLU   B 1 80 ? 9.047   -5.537  -26.505 1.00 41.47  ? 79  GLU   B CG  1 
ATOM   1362 N N   . GLY   B 1 81 ? 11.381  -8.418  -29.381 1.00 30.54  ? 80  GLY   B N   1 
ATOM   1363 C CA  . GLY   B 1 81 ? 12.470  -8.835  -30.251 1.00 25.75  ? 80  GLY   B CA  1 
ATOM   1364 C C   . GLY   B 1 81 ? 12.032  -8.849  -31.708 1.00 29.22  ? 80  GLY   B C   1 
ATOM   1365 O O   . GLY   B 1 81 ? 12.808  -8.479  -32.594 1.00 29.10  ? 80  GLY   B O   1 
ATOM   1366 N N   . LEU   B 1 82 ? 10.785  -9.278  -31.931 1.00 25.23  ? 81  LEU   B N   1 
ATOM   1367 C CA  . LEU   B 1 82 ? 10.222  -9.320  -33.266 1.00 32.25  ? 81  LEU   B CA  1 
ATOM   1368 C C   . LEU   B 1 82 ? 10.067  -7.898  -33.800 1.00 33.57  ? 81  LEU   B C   1 
ATOM   1369 O O   . LEU   B 1 82 ? 10.347  -7.670  -34.978 1.00 29.01  ? 81  LEU   B O   1 
ATOM   1370 C CB  . LEU   B 1 82 ? 8.903   -10.094 -33.320 1.00 31.21  ? 81  LEU   B CB  1 
ATOM   1371 C CG  . LEU   B 1 82 ? 9.028   -11.609 -33.110 1.00 28.31  ? 81  LEU   B CG  1 
ATOM   1372 C CD1 . LEU   B 1 82 ? 7.639   -12.171 -33.154 1.00 30.35  ? 81  LEU   B CD1 1 
ATOM   1373 C CD2 . LEU   B 1 82 ? 9.895   -12.257 -34.183 1.00 26.93  ? 81  LEU   B CD2 1 
ATOM   1374 N N   . TRP   B 1 83 ? 9.595   -6.973  -32.952 1.00 28.39  ? 82  TRP   B N   1 
ATOM   1375 C CA  . TRP   B 1 83 ? 9.502   -5.570  -33.340 1.00 28.24  ? 82  TRP   B CA  1 
ATOM   1376 C C   . TRP   B 1 83 ? 10.880  -5.017  -33.724 1.00 28.28  ? 82  TRP   B C   1 
ATOM   1377 O O   . TRP   B 1 83 ? 10.986  -4.303  -34.724 1.00 33.50  ? 82  TRP   B O   1 
ATOM   1378 C CB  . TRP   B 1 83 ? 8.821   -4.705  -32.261 1.00 30.62  ? 82  TRP   B CB  1 
ATOM   1379 C CG  . TRP   B 1 83 ? 8.558   -3.303  -32.744 1.00 35.92  ? 82  TRP   B CG  1 
ATOM   1380 C CD1 . TRP   B 1 83 ? 7.416   -2.840  -33.330 1.00 36.72  ? 82  TRP   B CD1 1 
ATOM   1381 C CD2 . TRP   B 1 83 ? 9.495   -2.194  -32.755 1.00 37.46  ? 82  TRP   B CD2 1 
ATOM   1382 N NE1 . TRP   B 1 83 ? 7.570   -1.522  -33.685 1.00 39.39  ? 82  TRP   B NE1 1 
ATOM   1383 C CE2 . TRP   B 1 83 ? 8.833   -1.103  -33.360 1.00 38.99  ? 82  TRP   B CE2 1 
ATOM   1384 C CE3 . TRP   B 1 83 ? 10.825  -2.029  -32.329 1.00 39.03  ? 82  TRP   B CE3 1 
ATOM   1385 C CZ2 . TRP   B 1 83 ? 9.447   0.143   -33.527 1.00 43.16  ? 82  TRP   B CZ2 1 
ATOM   1386 C CZ3 . TRP   B 1 83 ? 11.438  -0.798  -32.500 1.00 43.44  ? 82  TRP   B CZ3 1 
ATOM   1387 C CH2 . TRP   B 1 83 ? 10.757  0.267   -33.103 1.00 44.00  ? 82  TRP   B CH2 1 
ATOM   1388 N N   . GLU   B 1 84 ? 11.919  -5.346  -32.944 1.00 28.36  ? 83  GLU   B N   1 
ATOM   1389 C CA  . GLU   B 1 84 ? 13.254  -4.782  -33.132 1.00 29.17  ? 83  GLU   B CA  1 
ATOM   1390 C C   . GLU   B 1 84 ? 13.880  -5.255  -34.452 1.00 30.81  ? 83  GLU   B C   1 
ATOM   1391 O O   . GLU   B 1 84 ? 14.473  -4.454  -35.195 1.00 30.42  ? 83  GLU   B O   1 
ATOM   1392 C CB  . GLU   B 1 84 ? 14.210  -5.097  -31.987 1.00 29.21  ? 83  GLU   B CB  1 
ATOM   1393 C CG  . GLU   B 1 84 ? 13.822  -4.360  -30.705 1.00 35.32  ? 83  GLU   B CG  1 
ATOM   1394 C CD  . GLU   B 1 84 ? 14.650  -4.670  -29.482 1.00 33.90  ? 83  GLU   B CD  1 
ATOM   1395 O OE1 . GLU   B 1 84 ? 15.553  -5.528  -29.557 1.00 32.30  ? 83  GLU   B OE1 1 
ATOM   1396 O OE2 . GLU   B 1 84 ? 14.368  -4.069  -28.418 1.00 32.63  ? 83  GLU   B OE2 1 
ATOM   1397 N N   . ILE   B 1 85 ? 13.749  -6.559  -34.746 1.00 29.23  ? 84  ILE   B N   1 
ATOM   1398 C CA  . ILE   B 1 85 ? 14.452  -7.121  -35.894 1.00 27.11  ? 84  ILE   B CA  1 
ATOM   1399 C C   . ILE   B 1 85 ? 13.820  -6.576  -37.171 1.00 28.69  ? 84  ILE   B C   1 
ATOM   1400 O O   . ILE   B 1 85 ? 14.504  -6.417  -38.191 1.00 28.11  ? 84  ILE   B O   1 
ATOM   1401 C CB  . ILE   B 1 85 ? 14.460  -8.663  -35.858 1.00 30.95  ? 84  ILE   B CB  1 
ATOM   1402 C CG1 . ILE   B 1 85 ? 15.538  -9.249  -36.788 1.00 30.53  ? 84  ILE   B CG1 1 
ATOM   1403 C CG2 . ILE   B 1 85 ? 13.061  -9.230  -36.128 1.00 29.15  ? 84  ILE   B CG2 1 
ATOM   1404 C CD1 . ILE   B 1 85 ? 15.959  -10.681 -36.459 1.00 27.05  ? 84  ILE   B CD1 1 
ATOM   1405 N N   . GLN   B 1 86 ? 12.519  -6.260  -37.086 1.00 28.05  ? 85  GLN   B N   1 
ATOM   1406 C CA  . GLN   B 1 86 ? 11.753  -5.751  -38.213 1.00 32.75  ? 85  GLN   B CA  1 
ATOM   1407 C C   . GLN   B 1 86 ? 11.912  -4.236  -38.383 1.00 33.03  ? 85  GLN   B C   1 
ATOM   1408 O O   . GLN   B 1 86 ? 11.931  -3.758  -39.517 1.00 33.53  ? 85  GLN   B O   1 
ATOM   1409 C CB  . GLN   B 1 86 ? 10.292  -6.195  -38.068 1.00 37.53  ? 85  GLN   B CB  1 
ATOM   1410 N N   . ASN   B 1 87 ? 12.015  -3.472  -37.282 1.00 27.77  ? 86  ASN   B N   1 
ATOM   1411 C CA  . ASN   B 1 87 ? 11.901  -2.016  -37.385 1.00 30.99  ? 86  ASN   B CA  1 
ATOM   1412 C C   . ASN   B 1 87 ? 13.245  -1.302  -37.207 1.00 28.36  ? 86  ASN   B C   1 
ATOM   1413 O O   . ASN   B 1 87 ? 13.434  -0.189  -37.704 1.00 29.93  ? 86  ASN   B O   1 
ATOM   1414 C CB  . ASN   B 1 87 ? 10.812  -1.471  -36.456 1.00 34.45  ? 86  ASN   B CB  1 
ATOM   1415 C CG  . ASN   B 1 87 ? 9.451   -1.970  -36.889 1.00 38.72  ? 86  ASN   B CG  1 
ATOM   1416 O OD1 . ASN   B 1 87 ? 8.937   -1.517  -37.912 1.00 41.13  ? 86  ASN   B OD1 1 
ATOM   1417 N ND2 . ASN   B 1 87 ? 8.900   -2.969  -36.211 1.00 38.49  ? 86  ASN   B ND2 1 
ATOM   1418 N N   . ASN   B 1 88 ? 14.168  -1.873  -36.439 1.00 27.92  ? 87  ASN   B N   1 
ATOM   1419 C CA  . ASN   B 1 88 ? 15.421  -1.159  -36.221 1.00 33.52  ? 87  ASN   B CA  1 
ATOM   1420 C C   . ASN   B 1 88 ? 16.530  -2.140  -35.864 1.00 28.55  ? 87  ASN   B C   1 
ATOM   1421 O O   . ASN   B 1 88 ? 17.088  -2.101  -34.771 1.00 29.78  ? 87  ASN   B O   1 
ATOM   1422 C CB  . ASN   B 1 88 ? 15.294  -0.014  -35.215 1.00 35.76  ? 87  ASN   B CB  1 
ATOM   1423 C CG  . ASN   B 1 88 ? 16.368  1.027   -35.444 1.00 35.60  ? 87  ASN   B CG  1 
ATOM   1424 O OD1 . ASN   B 1 88 ? 17.406  0.766   -36.067 1.00 36.39  ? 87  ASN   B OD1 1 
ATOM   1425 N ND2 . ASN   B 1 88 ? 16.145  2.231   -34.949 1.00 41.01  ? 87  ASN   B ND2 1 
ATOM   1426 N N   . PRO   B 1 89 ? 16.831  -3.108  -36.752 1.00 27.67  ? 88  PRO   B N   1 
ATOM   1427 C CA  . PRO   B 1 89 ? 17.747  -4.198  -36.412 1.00 26.18  ? 88  PRO   B CA  1 
ATOM   1428 C C   . PRO   B 1 89 ? 19.190  -3.780  -36.146 1.00 27.77  ? 88  PRO   B C   1 
ATOM   1429 O O   . PRO   B 1 89 ? 19.939  -4.518  -35.508 1.00 28.75  ? 88  PRO   B O   1 
ATOM   1430 C CB  . PRO   B 1 89 ? 17.666  -5.110  -37.666 1.00 24.42  ? 88  PRO   B CB  1 
ATOM   1431 C CG  . PRO   B 1 89 ? 17.255  -4.198  -38.786 1.00 24.56  ? 88  PRO   B CG  1 
ATOM   1432 C CD  . PRO   B 1 89 ? 16.263  -3.225  -38.113 1.00 27.84  ? 88  PRO   B CD  1 
ATOM   1433 N N   . HIS   B 1 90 ? 19.577  -2.576  -36.607 1.00 27.04  ? 89  HIS   B N   1 
ATOM   1434 C CA  . HIS   B 1 90 ? 20.979  -2.187  -36.555 1.00 28.04  ? 89  HIS   B CA  1 
ATOM   1435 C C   . HIS   B 1 90 ? 21.220  -1.104  -35.491 1.00 31.62  ? 89  HIS   B C   1 
ATOM   1436 O O   . HIS   B 1 90 ? 22.315  -0.553  -35.395 1.00 32.72  ? 89  HIS   B O   1 
ATOM   1437 C CB  . HIS   B 1 90 ? 21.447  -1.769  -37.967 1.00 29.56  ? 89  HIS   B CB  1 
ATOM   1438 C CG  . HIS   B 1 90 ? 21.263  -2.856  -38.981 1.00 28.29  ? 89  HIS   B CG  1 
ATOM   1439 N ND1 . HIS   B 1 90 ? 21.864  -4.091  -38.837 1.00 26.38  ? 89  HIS   B ND1 1 
ATOM   1440 C CD2 . HIS   B 1 90 ? 20.561  -2.907  -40.140 1.00 26.83  ? 89  HIS   B CD2 1 
ATOM   1441 C CE1 . HIS   B 1 90 ? 21.555  -4.848  -39.890 1.00 26.32  ? 89  HIS   B CE1 1 
ATOM   1442 N NE2 . HIS   B 1 90 ? 20.788  -4.140  -40.698 1.00 29.14  ? 89  HIS   B NE2 1 
ATOM   1443 N N   . ALA   B 1 91 ? 20.239  -0.896  -34.616 1.00 30.62  ? 90  ALA   B N   1 
ATOM   1444 C CA  . ALA   B 1 91 ? 20.301  0.173   -33.628 1.00 31.61  ? 90  ALA   B CA  1 
ATOM   1445 C C   . ALA   B 1 91 ? 21.243  -0.198  -32.488 1.00 33.93  ? 90  ALA   B C   1 
ATOM   1446 O O   . ALA   B 1 91 ? 21.528  -1.370  -32.256 1.00 32.90  ? 90  ALA   B O   1 
ATOM   1447 C CB  . ALA   B 1 91 ? 18.902  0.498   -33.109 1.00 29.77  ? 90  ALA   B CB  1 
ATOM   1448 N N   . SER   B 1 92 ? 21.711  0.821   -31.761 1.00 33.37  ? 91  SER   B N   1 
ATOM   1449 C CA  . SER   B 1 92 ? 22.370  0.602   -30.480 1.00 38.12  ? 91  SER   B CA  1 
ATOM   1450 C C   . SER   B 1 92 ? 21.310  0.357   -29.399 1.00 41.33  ? 91  SER   B C   1 
ATOM   1451 O O   . SER   B 1 92 ? 20.386  1.168   -29.258 1.00 39.21  ? 91  SER   B O   1 
ATOM   1452 C CB  . SER   B 1 92 ? 23.249  1.790   -30.113 1.00 39.45  ? 91  SER   B CB  1 
ATOM   1453 O OG  . SER   B 1 92 ? 23.829  1.576   -28.832 1.00 46.80  ? 91  SER   B OG  1 
ATOM   1454 N N   . TYR   B 1 93 ? 21.459  -0.755  -28.652 1.00 38.54  ? 92  TYR   B N   1 
ATOM   1455 C CA  . TYR   B 1 93 ? 20.520  -1.209  -27.623 1.00 41.64  ? 92  TYR   B CA  1 
ATOM   1456 C C   . TYR   B 1 93 ? 21.192  -1.188  -26.244 1.00 45.77  ? 92  TYR   B C   1 
ATOM   1457 O O   . TYR   B 1 93 ? 20.557  -1.491  -25.237 1.00 50.87  ? 92  TYR   B O   1 
ATOM   1458 C CB  . TYR   B 1 93 ? 19.848  -2.553  -27.965 1.00 34.53  ? 92  TYR   B CB  1 
ATOM   1459 C CG  . TYR   B 1 93 ? 18.848  -2.462  -29.113 1.00 33.92  ? 92  TYR   B CG  1 
ATOM   1460 C CD1 . TYR   B 1 93 ? 17.555  -2.001  -28.901 1.00 32.15  ? 92  TYR   B CD1 1 
ATOM   1461 C CD2 . TYR   B 1 93 ? 19.192  -2.818  -30.420 1.00 29.43  ? 92  TYR   B CD2 1 
ATOM   1462 C CE1 . TYR   B 1 93 ? 16.641  -1.885  -29.934 1.00 35.77  ? 92  TYR   B CE1 1 
ATOM   1463 C CE2 . TYR   B 1 93 ? 18.272  -2.715  -31.454 1.00 29.88  ? 92  TYR   B CE2 1 
ATOM   1464 C CZ  . TYR   B 1 93 ? 16.993  -2.258  -31.219 1.00 31.41  ? 92  TYR   B CZ  1 
ATOM   1465 O OH  . TYR   B 1 93 ? 16.075  -2.135  -32.230 1.00 29.94  ? 92  TYR   B OH  1 
ATOM   1466 N N   . SER   B 1 94 ? 22.462  -0.762  -26.210 1.00 56.24  ? 93  SER   B N   1 
ATOM   1467 C CA  . SER   B 1 94 ? 23.298  -0.664  -25.019 1.00 63.63  ? 93  SER   B CA  1 
ATOM   1468 C C   . SER   B 1 94 ? 22.473  -0.193  -23.813 1.00 69.53  ? 93  SER   B C   1 
ATOM   1469 O O   . SER   B 1 94 ? 21.855  0.892   -23.940 1.00 68.45  ? 93  SER   B O   1 
ATOM   1470 C CB  . SER   B 1 94 ? 24.447  0.285   -25.254 1.00 67.37  ? 93  SER   B CB  1 
ATOM   1471 O OG  . SER   B 1 94 ? 25.142  -0.022  -26.454 1.00 69.38  ? 93  SER   B OG  1 
ATOM   1472 N N   . HIS   C 1 4  ? 33.781  -23.554 26.582  1.00 82.55  ? 3   HIS   C N   1 
ATOM   1473 C CA  . HIS   C 1 4  ? 32.549  -22.735 26.755  1.00 92.73  ? 3   HIS   C CA  1 
ATOM   1474 C C   . HIS   C 1 4  ? 31.924  -23.062 28.115  1.00 93.36  ? 3   HIS   C C   1 
ATOM   1475 O O   . HIS   C 1 4  ? 32.593  -23.615 28.992  1.00 85.10  ? 3   HIS   C O   1 
ATOM   1476 C CB  . HIS   C 1 4  ? 31.638  -22.880 25.523  1.00 98.66  ? 3   HIS   C CB  1 
ATOM   1477 C CG  . HIS   C 1 4  ? 30.558  -21.843 25.408  1.00 103.69 ? 3   HIS   C CG  1 
ATOM   1478 N ND1 . HIS   C 1 4  ? 30.791  -20.552 24.982  1.00 101.68 ? 3   HIS   C ND1 1 
ATOM   1479 C CD2 . HIS   C 1 4  ? 29.248  -21.900 25.689  1.00 100.28 ? 3   HIS   C CD2 1 
ATOM   1480 C CE1 . HIS   C 1 4  ? 29.658  -19.865 25.002  1.00 93.07  ? 3   HIS   C CE1 1 
ATOM   1481 N NE2 . HIS   C 1 4  ? 28.709  -20.665 25.430  1.00 98.35  ? 3   HIS   C NE2 1 
ATOM   1482 N N   . ALA   C 1 5  ? 30.637  -22.709 28.267  1.00 87.84  ? 4   ALA   C N   1 
ATOM   1483 C CA  . ALA   C 1 5  ? 29.892  -22.790 29.514  1.00 79.61  ? 4   ALA   C CA  1 
ATOM   1484 C C   . ALA   C 1 5  ? 28.394  -22.730 29.229  1.00 85.23  ? 4   ALA   C C   1 
ATOM   1485 O O   . ALA   C 1 5  ? 27.887  -21.702 28.773  1.00 90.05  ? 4   ALA   C O   1 
ATOM   1486 C CB  . ALA   C 1 5  ? 30.279  -21.622 30.372  1.00 87.15  ? 4   ALA   C CB  1 
ATOM   1487 N N   . PHE   C 1 6  ? 27.688  -23.829 29.520  1.00 75.17  ? 5   PHE   C N   1 
ATOM   1488 C CA  . PHE   C 1 6  ? 26.265  -23.909 29.224  1.00 67.85  ? 5   PHE   C CA  1 
ATOM   1489 C C   . PHE   C 1 6  ? 25.511  -23.879 30.539  1.00 62.89  ? 5   PHE   C C   1 
ATOM   1490 O O   . PHE   C 1 6  ? 25.959  -24.487 31.507  1.00 62.53  ? 5   PHE   C O   1 
ATOM   1491 C CB  . PHE   C 1 6  ? 25.838  -25.135 28.403  1.00 56.67  ? 5   PHE   C CB  1 
ATOM   1492 C CG  . PHE   C 1 6  ? 26.563  -25.201 27.071  1.00 52.25  ? 5   PHE   C CG  1 
ATOM   1493 C CD1 . PHE   C 1 6  ? 27.693  -26.000 26.914  1.00 57.46  ? 5   PHE   C CD1 1 
ATOM   1494 C CD2 . PHE   C 1 6  ? 26.156  -24.407 26.000  1.00 52.46  ? 5   PHE   C CD2 1 
ATOM   1495 C CE1 . PHE   C 1 6  ? 28.377  -26.044 25.700  1.00 57.29  ? 5   PHE   C CE1 1 
ATOM   1496 C CE2 . PHE   C 1 6  ? 26.835  -24.454 24.790  1.00 52.25  ? 5   PHE   C CE2 1 
ATOM   1497 C CZ  . PHE   C 1 6  ? 27.945  -25.266 24.644  1.00 56.32  ? 5   PHE   C CZ  1 
ATOM   1498 N N   . LYS   C 1 7  ? 24.372  -23.181 30.531  1.00 59.76  ? 6   LYS   C N   1 
ATOM   1499 C CA  . LYS   C 1 7  ? 23.499  -23.035 31.685  1.00 59.27  ? 6   LYS   C CA  1 
ATOM   1500 C C   . LYS   C 1 7  ? 22.091  -23.409 31.240  1.00 55.78  ? 6   LYS   C C   1 
ATOM   1501 O O   . LYS   C 1 7  ? 21.825  -23.412 30.044  1.00 67.76  ? 6   LYS   C O   1 
ATOM   1502 C CB  . LYS   C 1 7  ? 23.527  -21.576 32.170  1.00 61.08  ? 6   LYS   C CB  1 
ATOM   1503 N N   . PRO   C 1 8  ? 21.144  -23.750 32.148  1.00 51.30  ? 7   PRO   C N   1 
ATOM   1504 C CA  . PRO   C 1 8  ? 19.768  -24.035 31.731  1.00 50.15  ? 7   PRO   C CA  1 
ATOM   1505 C C   . PRO   C 1 8  ? 19.187  -22.865 30.937  1.00 57.93  ? 7   PRO   C C   1 
ATOM   1506 O O   . PRO   C 1 8  ? 19.507  -21.699 31.210  1.00 51.15  ? 7   PRO   C O   1 
ATOM   1507 C CB  . PRO   C 1 8  ? 18.983  -24.346 33.017  1.00 54.06  ? 7   PRO   C CB  1 
ATOM   1508 C CG  . PRO   C 1 8  ? 20.066  -24.670 34.027  1.00 54.75  ? 7   PRO   C CG  1 
ATOM   1509 C CD  . PRO   C 1 8  ? 21.347  -23.923 33.597  1.00 54.57  ? 7   PRO   C CD  1 
ATOM   1510 N N   . GLY   C 1 9  ? 18.387  -23.210 29.917  1.00 52.92  ? 8   GLY   C N   1 
ATOM   1511 C CA  . GLY   C 1 9  ? 17.707  -22.246 29.064  1.00 55.70  ? 8   GLY   C CA  1 
ATOM   1512 C C   . GLY   C 1 9  ? 18.503  -21.892 27.810  1.00 53.49  ? 8   GLY   C C   1 
ATOM   1513 O O   . GLY   C 1 9  ? 17.920  -21.406 26.844  1.00 62.50  ? 8   GLY   C O   1 
ATOM   1514 N N   . ASP   C 1 10 ? 19.827  -22.108 27.845  1.00 45.85  ? 9   ASP   C N   1 
ATOM   1515 C CA  . ASP   C 1 10 ? 20.688  -21.824 26.713  1.00 48.46  ? 9   ASP   C CA  1 
ATOM   1516 C C   . ASP   C 1 10 ? 20.149  -22.557 25.480  1.00 48.97  ? 9   ASP   C C   1 
ATOM   1517 O O   . ASP   C 1 10 ? 19.888  -23.756 25.523  1.00 46.93  ? 9   ASP   C O   1 
ATOM   1518 C CB  . ASP   C 1 10 ? 22.155  -22.071 27.035  1.00 53.70  ? 9   ASP   C CB  1 
ATOM   1519 C CG  . ASP   C 1 10 ? 22.804  -21.121 28.037  1.00 61.17  ? 9   ASP   C CG  1 
ATOM   1520 O OD1 . ASP   C 1 10 ? 22.088  -20.236 28.541  1.00 59.20  ? 9   ASP   C OD1 1 
ATOM   1521 O OD2 . ASP   C 1 10 ? 24.029  -21.267 28.302  1.00 62.65  ? 9   ASP   C OD2 1 
ATOM   1522 N N   . LEU   C 1 11 ? 19.975  -21.800 24.391  1.00 46.52  ? 10  LEU   C N   1 
ATOM   1523 C CA  . LEU   C 1 11 ? 19.636  -22.321 23.078  1.00 43.02  ? 10  LEU   C CA  1 
ATOM   1524 C C   . LEU   C 1 11 ? 20.899  -22.800 22.368  1.00 38.46  ? 10  LEU   C C   1 
ATOM   1525 O O   . LEU   C 1 11 ? 21.933  -22.128 22.378  1.00 37.85  ? 10  LEU   C O   1 
ATOM   1526 C CB  . LEU   C 1 11 ? 18.939  -21.210 22.291  1.00 41.10  ? 10  LEU   C CB  1 
ATOM   1527 C CG  . LEU   C 1 11 ? 17.622  -20.686 22.864  1.00 40.88  ? 10  LEU   C CG  1 
ATOM   1528 C CD1 . LEU   C 1 11 ? 16.980  -19.689 21.886  1.00 42.14  ? 10  LEU   C CD1 1 
ATOM   1529 C CD2 . LEU   C 1 11 ? 16.643  -21.792 23.252  1.00 43.81  ? 10  LEU   C CD2 1 
ATOM   1530 N N   . VAL   C 1 12 ? 20.808  -23.977 21.725  1.00 35.19  ? 11  VAL   C N   1 
ATOM   1531 C CA  . VAL   C 1 12 ? 21.984  -24.599 21.150  1.00 32.65  ? 11  VAL   C CA  1 
ATOM   1532 C C   . VAL   C 1 12 ? 21.586  -25.389 19.896  1.00 31.85  ? 11  VAL   C C   1 
ATOM   1533 O O   . VAL   C 1 12 ? 20.402  -25.593 19.631  1.00 30.75  ? 11  VAL   C O   1 
ATOM   1534 C CB  . VAL   C 1 12 ? 22.636  -25.543 22.183  1.00 35.58  ? 11  VAL   C CB  1 
ATOM   1535 C CG1 . VAL   C 1 12 ? 22.930  -24.865 23.522  1.00 33.74  ? 11  VAL   C CG1 1 
ATOM   1536 C CG2 . VAL   C 1 12 ? 21.811  -26.812 22.393  1.00 28.29  ? 11  VAL   C CG2 1 
ATOM   1537 N N   . PHE   C 1 13 ? 22.600  -25.820 19.134  1.00 32.60  ? 12  PHE   C N   1 
ATOM   1538 C CA  . PHE   C 1 13 ? 22.481  -26.991 18.278  1.00 30.27  ? 12  PHE   C CA  1 
ATOM   1539 C C   . PHE   C 1 13 ? 23.119  -28.176 18.995  1.00 32.46  ? 12  PHE   C C   1 
ATOM   1540 O O   . PHE   C 1 13 ? 24.206  -28.057 19.575  1.00 35.59  ? 12  PHE   C O   1 
ATOM   1541 C CB  . PHE   C 1 13 ? 23.095  -26.801 16.880  1.00 35.72  ? 12  PHE   C CB  1 
ATOM   1542 C CG  . PHE   C 1 13 ? 22.305  -25.797 16.055  1.00 37.28  ? 12  PHE   C CG  1 
ATOM   1543 C CD1 . PHE   C 1 13 ? 21.198  -26.203 15.303  1.00 36.62  ? 12  PHE   C CD1 1 
ATOM   1544 C CD2 . PHE   C 1 13 ? 22.617  -24.434 16.104  1.00 38.78  ? 12  PHE   C CD2 1 
ATOM   1545 C CE1 . PHE   C 1 13 ? 20.451  -25.268 14.588  1.00 36.50  ? 12  PHE   C CE1 1 
ATOM   1546 C CE2 . PHE   C 1 13 ? 21.862  -23.501 15.400  1.00 35.94  ? 12  PHE   C CE2 1 
ATOM   1547 C CZ  . PHE   C 1 13 ? 20.785  -23.920 14.637  1.00 41.61  ? 12  PHE   C CZ  1 
ATOM   1548 N N   . ALA   C 1 14 ? 22.406  -29.311 18.981  1.00 30.57  ? 13  ALA   C N   1 
ATOM   1549 C CA  . ALA   C 1 14 ? 22.879  -30.476 19.711  1.00 28.95  ? 13  ALA   C CA  1 
ATOM   1550 C C   . ALA   C 1 14 ? 23.145  -31.595 18.715  1.00 30.72  ? 13  ALA   C C   1 
ATOM   1551 O O   . ALA   C 1 14 ? 22.289  -31.887 17.885  1.00 27.76  ? 13  ALA   C O   1 
ATOM   1552 C CB  . ALA   C 1 14 ? 21.830  -30.897 20.732  1.00 28.59  ? 13  ALA   C CB  1 
ATOM   1553 N N   . LYS   C 1 15 ? 24.309  -32.225 18.829  1.00 29.25  ? 14  LYS   C N   1 
ATOM   1554 C CA  . LYS   C 1 15 ? 24.717  -33.176 17.812  1.00 32.87  ? 14  LYS   C CA  1 
ATOM   1555 C C   . LYS   C 1 15 ? 24.776  -34.558 18.445  1.00 32.51  ? 14  LYS   C C   1 
ATOM   1556 O O   . LYS   C 1 15 ? 25.514  -34.765 19.408  1.00 33.33  ? 14  LYS   C O   1 
ATOM   1557 C CB  . LYS   C 1 15 ? 26.116  -32.837 17.269  1.00 36.36  ? 14  LYS   C CB  1 
ATOM   1558 C CG  . LYS   C 1 15 ? 26.614  -33.781 16.160  1.00 37.17  ? 14  LYS   C CG  1 
ATOM   1559 C CD  . LYS   C 1 15 ? 25.678  -33.872 14.957  1.00 30.12  ? 14  LYS   C CD  1 
ATOM   1560 C CE  . LYS   C 1 15 ? 26.182  -34.715 13.776  1.00 35.92  ? 14  LYS   C CE  1 
ATOM   1561 N NZ  . LYS   C 1 15 ? 26.143  -36.151 14.081  1.00 31.76  ? 14  LYS   C NZ  1 
ATOM   1562 N N   . MET   C 1 16 ? 24.025  -35.489 17.862  1.00 31.48  ? 15  MET   C N   1 
ATOM   1563 C CA  . MET   C 1 16 ? 24.057  -36.891 18.257  1.00 34.09  ? 15  MET   C CA  1 
ATOM   1564 C C   . MET   C 1 16 ? 24.493  -37.694 17.040  1.00 35.73  ? 15  MET   C C   1 
ATOM   1565 O O   . MET   C 1 16 ? 24.198  -37.305 15.907  1.00 31.50  ? 15  MET   C O   1 
ATOM   1566 C CB  . MET   C 1 16 ? 22.671  -37.399 18.672  1.00 33.60  ? 15  MET   C CB  1 
ATOM   1567 C CG  . MET   C 1 16 ? 22.093  -36.712 19.903  1.00 37.16  ? 15  MET   C CG  1 
ATOM   1568 S SD  . MET   C 1 16 ? 20.612  -37.454 20.618  1.00 46.08  ? 15  MET   C SD  1 
ATOM   1569 C CE  . MET   C 1 16 ? 21.214  -38.973 21.377  1.00 49.93  ? 15  MET   C CE  1 
ATOM   1570 N N   . LYS   C 1 17 ? 25.137  -38.842 17.299  1.00 37.43  ? 16  LYS   C N   1 
ATOM   1571 C CA  . LYS   C 1 17 ? 25.547  -39.745 16.230  1.00 36.62  ? 16  LYS   C CA  1 
ATOM   1572 C C   . LYS   C 1 17 ? 24.309  -40.139 15.423  1.00 31.99  ? 16  LYS   C C   1 
ATOM   1573 O O   . LYS   C 1 17 ? 23.309  -40.601 15.987  1.00 29.13  ? 16  LYS   C O   1 
ATOM   1574 C CB  . LYS   C 1 17 ? 26.192  -40.988 16.867  1.00 38.73  ? 16  LYS   C CB  1 
ATOM   1575 C CG  . LYS   C 1 17 ? 26.891  -41.928 15.887  1.00 44.19  ? 16  LYS   C CG  1 
ATOM   1576 C CD  . LYS   C 1 17 ? 27.960  -41.155 15.135  1.00 45.96  ? 16  LYS   C CD  1 
ATOM   1577 C CE  . LYS   C 1 17 ? 28.716  -42.038 14.195  1.00 58.30  ? 16  LYS   C CE  1 
ATOM   1578 N NZ  . LYS   C 1 17 ? 29.912  -41.337 13.729  1.00 52.26  ? 16  LYS   C NZ  1 
ATOM   1579 N N   . GLY   C 1 18 ? 24.404  -40.006 14.097  1.00 30.87  ? 17  GLY   C N   1 
ATOM   1580 C CA  . GLY   C 1 18 ? 23.323  -40.470 13.233  1.00 36.16  ? 17  GLY   C CA  1 
ATOM   1581 C C   . GLY   C 1 18 ? 22.274  -39.389 12.924  1.00 37.42  ? 17  GLY   C C   1 
ATOM   1582 O O   . GLY   C 1 18 ? 21.242  -39.683 12.326  1.00 37.76  ? 17  GLY   C O   1 
ATOM   1583 N N   . TYR   C 1 19 ? 22.512  -38.148 13.378  1.00 34.39  ? 18  TYR   C N   1 
ATOM   1584 C CA  . TYR   C 1 19 ? 21.560  -37.052 13.222  1.00 34.70  ? 18  TYR   C CA  1 
ATOM   1585 C C   . TYR   C 1 19 ? 22.340  -35.781 12.938  1.00 33.86  ? 18  TYR   C C   1 
ATOM   1586 O O   . TYR   C 1 19 ? 23.457  -35.620 13.418  1.00 30.52  ? 18  TYR   C O   1 
ATOM   1587 C CB  . TYR   C 1 19 ? 20.732  -36.752 14.474  1.00 35.27  ? 18  TYR   C CB  1 
ATOM   1588 C CG  . TYR   C 1 19 ? 19.945  -37.976 14.885  1.00 32.81  ? 18  TYR   C CG  1 
ATOM   1589 C CD1 . TYR   C 1 19 ? 20.522  -38.950 15.700  1.00 32.78  ? 18  TYR   C CD1 1 
ATOM   1590 C CD2 . TYR   C 1 19 ? 18.674  -38.206 14.378  1.00 33.97  ? 18  TYR   C CD2 1 
ATOM   1591 C CE1 . TYR   C 1 19 ? 19.836  -40.103 16.024  1.00 34.68  ? 18  TYR   C CE1 1 
ATOM   1592 C CE2 . TYR   C 1 19 ? 17.980  -39.363 14.697  1.00 37.33  ? 18  TYR   C CE2 1 
ATOM   1593 C CZ  . TYR   C 1 19 ? 18.566  -40.307 15.520  1.00 39.62  ? 18  TYR   C CZ  1 
ATOM   1594 O OH  . TYR   C 1 19 ? 17.878  -41.428 15.863  1.00 41.95  ? 18  TYR   C OH  1 
ATOM   1595 N N   . PRO   C 1 20 ? 21.758  -34.850 12.152  1.00 33.76  ? 19  PRO   C N   1 
ATOM   1596 C CA  . PRO   C 1 20 ? 22.387  -33.547 11.916  1.00 28.22  ? 19  PRO   C CA  1 
ATOM   1597 C C   . PRO   C 1 20 ? 22.352  -32.742 13.217  1.00 28.87  ? 19  PRO   C C   1 
ATOM   1598 O O   . PRO   C 1 20 ? 21.596  -33.068 14.148  1.00 29.80  ? 19  PRO   C O   1 
ATOM   1599 C CB  . PRO   C 1 20 ? 21.453  -32.933 10.855  1.00 30.23  ? 19  PRO   C CB  1 
ATOM   1600 C CG  . PRO   C 1 20 ? 20.104  -33.548 11.174  1.00 30.59  ? 19  PRO   C CG  1 
ATOM   1601 C CD  . PRO   C 1 20 ? 20.435  -35.001 11.502  1.00 31.13  ? 19  PRO   C CD  1 
ATOM   1602 N N   . HIS   C 1 21 ? 23.146  -31.669 13.250  1.00 28.54  ? 20  HIS   C N   1 
ATOM   1603 C CA  . HIS   C 1 21 ? 23.103  -30.706 14.345  1.00 29.36  ? 20  HIS   C CA  1 
ATOM   1604 C C   . HIS   C 1 21 ? 21.669  -30.191 14.481  1.00 28.65  ? 20  HIS   C C   1 
ATOM   1605 O O   . HIS   C 1 21 ? 21.084  -29.679 13.512  1.00 31.74  ? 20  HIS   C O   1 
ATOM   1606 C CB  . HIS   C 1 21 ? 24.121  -29.579 14.118  1.00 29.51  ? 20  HIS   C CB  1 
ATOM   1607 C CG  . HIS   C 1 21 ? 25.541  -30.068 14.085  1.00 34.70  ? 20  HIS   C CG  1 
ATOM   1608 N ND1 . HIS   C 1 21 ? 26.113  -30.734 13.019  1.00 36.62  ? 20  HIS   C ND1 1 
ATOM   1609 C CD2 . HIS   C 1 21 ? 26.494  -30.005 15.030  1.00 38.67  ? 20  HIS   C CD2 1 
ATOM   1610 C CE1 . HIS   C 1 21 ? 27.372  -31.047 13.322  1.00 36.39  ? 20  HIS   C CE1 1 
ATOM   1611 N NE2 . HIS   C 1 21 ? 27.630  -30.597 14.538  1.00 37.31  ? 20  HIS   C NE2 1 
ATOM   1612 N N   . TRP   C 1 22 ? 21.105  -30.347 15.690  1.00 27.55  ? 21  TRP   C N   1 
ATOM   1613 C CA  . TRP   C 1 22 ? 19.665  -30.240 15.864  1.00 26.72  ? 21  TRP   C CA  1 
ATOM   1614 C C   . TRP   C 1 22 ? 19.350  -29.054 16.785  1.00 27.67  ? 21  TRP   C C   1 
ATOM   1615 O O   . TRP   C 1 22 ? 19.946  -28.932 17.859  1.00 28.94  ? 21  TRP   C O   1 
ATOM   1616 C CB  . TRP   C 1 22 ? 19.076  -31.546 16.429  1.00 31.12  ? 21  TRP   C CB  1 
ATOM   1617 C CG  . TRP   C 1 22 ? 17.607  -31.750 16.117  1.00 29.64  ? 21  TRP   C CG  1 
ATOM   1618 C CD1 . TRP   C 1 22 ? 16.518  -31.141 16.679  1.00 29.18  ? 21  TRP   C CD1 1 
ATOM   1619 C CD2 . TRP   C 1 22 ? 17.082  -32.662 15.121  1.00 28.70  ? 21  TRP   C CD2 1 
ATOM   1620 N NE1 . TRP   C 1 22 ? 15.356  -31.605 16.108  1.00 29.74  ? 21  TRP   C NE1 1 
ATOM   1621 C CE2 . TRP   C 1 22 ? 15.675  -32.539 15.148  1.00 28.12  ? 21  TRP   C CE2 1 
ATOM   1622 C CE3 . TRP   C 1 22 ? 17.672  -33.550 14.200  1.00 28.50  ? 21  TRP   C CE3 1 
ATOM   1623 C CZ2 . TRP   C 1 22 ? 14.864  -33.279 14.285  1.00 27.37  ? 21  TRP   C CZ2 1 
ATOM   1624 C CZ3 . TRP   C 1 22 ? 16.868  -34.287 13.349  1.00 27.21  ? 21  TRP   C CZ3 1 
ATOM   1625 C CH2 . TRP   C 1 22 ? 15.473  -34.167 13.422  1.00 27.56  ? 21  TRP   C CH2 1 
ATOM   1626 N N   . PRO   C 1 23 ? 18.373  -28.180 16.446  1.00 27.45  ? 22  PRO   C N   1 
ATOM   1627 C CA  . PRO   C 1 23 ? 17.991  -27.099 17.355  1.00 28.13  ? 22  PRO   C CA  1 
ATOM   1628 C C   . PRO   C 1 23 ? 17.396  -27.655 18.654  1.00 27.16  ? 22  PRO   C C   1 
ATOM   1629 O O   . PRO   C 1 23 ? 16.562  -28.555 18.643  1.00 28.57  ? 22  PRO   C O   1 
ATOM   1630 C CB  . PRO   C 1 23 ? 16.977  -26.293 16.522  1.00 28.58  ? 22  PRO   C CB  1 
ATOM   1631 C CG  . PRO   C 1 23 ? 16.356  -27.336 15.592  1.00 27.92  ? 22  PRO   C CG  1 
ATOM   1632 C CD  . PRO   C 1 23 ? 17.574  -28.183 15.201  1.00 28.43  ? 22  PRO   C CD  1 
ATOM   1633 N N   . ALA   C 1 24 ? 17.847  -27.105 19.780  1.00 30.73  ? 23  ALA   C N   1 
ATOM   1634 C CA  . ALA   C 1 24 ? 17.603  -27.680 21.092  1.00 29.76  ? 23  ALA   C CA  1 
ATOM   1635 C C   . ALA   C 1 24 ? 17.865  -26.608 22.153  1.00 30.81  ? 23  ALA   C C   1 
ATOM   1636 O O   . ALA   C 1 24 ? 18.330  -25.504 21.846  1.00 32.06  ? 23  ALA   C O   1 
ATOM   1637 C CB  . ALA   C 1 24 ? 18.486  -28.934 21.306  1.00 27.25  ? 23  ALA   C CB  1 
ATOM   1638 N N   . ARG   C 1 25 ? 17.578  -26.954 23.413  1.00 34.77  ? 24  ARG   C N   1 
ATOM   1639 C CA  . ARG   C 1 25 ? 17.930  -26.108 24.541  1.00 35.07  ? 24  ARG   C CA  1 
ATOM   1640 C C   . ARG   C 1 25 ? 18.365  -26.982 25.716  1.00 34.73  ? 24  ARG   C C   1 
ATOM   1641 O O   . ARG   C 1 25 ? 18.026  -28.177 25.786  1.00 33.68  ? 24  ARG   C O   1 
ATOM   1642 C CB  . ARG   C 1 25 ? 16.712  -25.307 25.012  1.00 35.40  ? 24  ARG   C CB  1 
ATOM   1643 C CG  . ARG   C 1 25 ? 15.435  -26.053 25.373  1.00 41.92  ? 24  ARG   C CG  1 
ATOM   1644 C CD  . ARG   C 1 25 ? 14.373  -25.096 25.942  1.00 44.67  ? 24  ARG   C CD  1 
ATOM   1645 N NE  . ARG   C 1 25 ? 13.244  -25.851 26.502  1.00 42.58  ? 24  ARG   C NE  1 
ATOM   1646 C CZ  . ARG   C 1 25 ? 11.938  -25.635 26.334  1.00 50.60  ? 24  ARG   C CZ  1 
ATOM   1647 N NH1 . ARG   C 1 25 ? 11.490  -24.633 25.585  1.00 47.93  ? 24  ARG   C NH1 1 
ATOM   1648 N NH2 . ARG   C 1 25 ? 11.070  -26.434 26.931  1.00 52.34  ? 24  ARG   C NH2 1 
ATOM   1649 N N   . ILE   C 1 26 ? 19.110  -26.358 26.619  1.00 35.74  ? 25  ILE   C N   1 
ATOM   1650 C CA  . ILE   C 1 26 ? 19.497  -26.968 27.882  1.00 40.52  ? 25  ILE   C CA  1 
ATOM   1651 C C   . ILE   C 1 26 ? 18.276  -26.920 28.798  1.00 48.14  ? 25  ILE   C C   1 
ATOM   1652 O O   . ILE   C 1 26 ? 17.723  -25.849 29.047  1.00 48.89  ? 25  ILE   C O   1 
ATOM   1653 C CB  . ILE   C 1 26 ? 20.671  -26.221 28.539  1.00 41.41  ? 25  ILE   C CB  1 
ATOM   1654 C CG1 . ILE   C 1 26 ? 21.709  -25.732 27.566  1.00 45.59  ? 25  ILE   C CG1 1 
ATOM   1655 C CG2 . ILE   C 1 26 ? 21.295  -27.065 29.655  1.00 44.10  ? 25  ILE   C CG2 1 
ATOM   1656 C CD1 . ILE   C 1 26 ? 22.683  -26.778 27.063  1.00 35.67  ? 25  ILE   C CD1 1 
ATOM   1657 N N   . ASP   C 1 27 ? 17.875  -28.088 29.298  1.00 46.15  ? 26  ASP   C N   1 
ATOM   1658 C CA  . ASP   C 1 27 ? 16.845  -28.182 30.316  1.00 59.82  ? 26  ASP   C CA  1 
ATOM   1659 C C   . ASP   C 1 27 ? 17.454  -27.980 31.700  1.00 65.89  ? 26  ASP   C C   1 
ATOM   1660 O O   . ASP   C 1 27 ? 18.658  -27.783 31.828  1.00 71.00  ? 26  ASP   C O   1 
ATOM   1661 C CB  . ASP   C 1 27 ? 16.119  -29.512 30.218  1.00 61.05  ? 26  ASP   C CB  1 
ATOM   1662 C CG  . ASP   C 1 27 ? 14.819  -29.454 29.436  1.00 64.40  ? 26  ASP   C CG  1 
ATOM   1663 O OD1 . ASP   C 1 27 ? 14.548  -28.373 28.859  1.00 59.93  ? 26  ASP   C OD1 1 
ATOM   1664 O OD2 . ASP   C 1 27 ? 14.074  -30.468 29.464  1.00 67.31  ? 26  ASP   C OD2 1 
ATOM   1665 N N   . ASP   C 1 28 ? 16.602  -28.017 32.730  1.00 75.65  ? 27  ASP   C N   1 
ATOM   1666 C CA  . ASP   C 1 28 ? 17.078  -28.163 34.096  1.00 75.07  ? 27  ASP   C CA  1 
ATOM   1667 C C   . ASP   C 1 28 ? 16.649  -29.548 34.571  1.00 75.32  ? 27  ASP   C C   1 
ATOM   1668 O O   . ASP   C 1 28 ? 15.666  -30.084 34.065  1.00 74.11  ? 27  ASP   C O   1 
ATOM   1669 C CB  . ASP   C 1 28 ? 16.680  -26.978 34.969  1.00 80.74  ? 27  ASP   C CB  1 
ATOM   1670 C CG  . ASP   C 1 28 ? 17.559  -26.694 36.186  1.00 75.82  ? 27  ASP   C CG  1 
ATOM   1671 O OD1 . ASP   C 1 28 ? 18.331  -27.591 36.596  1.00 66.92  ? 27  ASP   C OD1 1 
ATOM   1672 O OD2 . ASP   C 1 28 ? 17.493  -25.556 36.701  1.00 74.63  ? 27  ASP   C OD2 1 
ATOM   1673 N N   . ILE   C 1 29 ? 17.426  -30.128 35.497  1.00 73.86  ? 28  ILE   C N   1 
ATOM   1674 C CA  . ILE   C 1 29 ? 17.170  -31.451 36.048  1.00 72.35  ? 28  ILE   C CA  1 
ATOM   1675 C C   . ILE   C 1 29 ? 16.357  -31.282 37.330  1.00 76.49  ? 28  ILE   C C   1 
ATOM   1676 O O   . ILE   C 1 29 ? 16.710  -30.464 38.179  1.00 79.11  ? 28  ILE   C O   1 
ATOM   1677 C CB  . ILE   C 1 29 ? 18.493  -32.202 36.304  1.00 63.51  ? 28  ILE   C CB  1 
ATOM   1678 N N   . ALA   C 1 30 ? 15.278  -32.066 37.463  1.00 68.22  ? 29  ALA   C N   1 
ATOM   1679 C CA  . ALA   C 1 30 ? 14.359  -31.951 38.586  1.00 70.84  ? 29  ALA   C CA  1 
ATOM   1680 C C   . ALA   C 1 30 ? 15.057  -32.334 39.900  1.00 61.50  ? 29  ALA   C C   1 
ATOM   1681 O O   . ALA   C 1 30 ? 15.687  -33.422 39.913  1.00 62.89  ? 29  ALA   C O   1 
ATOM   1682 C CB  . ALA   C 1 30 ? 13.113  -32.779 38.330  1.00 67.06  ? 29  ALA   C CB  1 
ATOM   1683 N N   . LYS   C 1 35 ? 19.613  -38.313 37.815  1.00 65.61  ? 34  LYS   C N   1 
ATOM   1684 C CA  . LYS   C 1 35 ? 20.829  -37.467 37.680  1.00 60.19  ? 34  LYS   C CA  1 
ATOM   1685 C C   . LYS   C 1 35 ? 21.480  -37.780 36.332  1.00 55.64  ? 34  LYS   C C   1 
ATOM   1686 O O   . LYS   C 1 35 ? 21.535  -38.943 35.928  1.00 58.40  ? 34  LYS   C O   1 
ATOM   1687 C CB  . LYS   C 1 35 ? 21.721  -37.690 38.910  1.00 60.88  ? 34  LYS   C CB  1 
ATOM   1688 N N   . PRO   C 1 36 ? 21.965  -36.764 35.576  1.00 52.40  ? 35  PRO   C N   1 
ATOM   1689 C CA  . PRO   C 1 36 ? 22.671  -37.017 34.314  1.00 53.94  ? 35  PRO   C CA  1 
ATOM   1690 C C   . PRO   C 1 36 ? 23.875  -37.941 34.531  1.00 62.38  ? 35  PRO   C C   1 
ATOM   1691 O O   . PRO   C 1 36 ? 24.438  -37.990 35.630  1.00 52.71  ? 35  PRO   C O   1 
ATOM   1692 C CB  . PRO   C 1 36 ? 23.118  -35.606 33.865  1.00 57.70  ? 35  PRO   C CB  1 
ATOM   1693 C CG  . PRO   C 1 36 ? 22.199  -34.643 34.594  1.00 55.79  ? 35  PRO   C CG  1 
ATOM   1694 C CD  . PRO   C 1 36 ? 21.873  -35.332 35.912  1.00 52.04  ? 35  PRO   C CD  1 
ATOM   1695 N N   . PRO   C 1 37 ? 24.334  -38.704 33.508  1.00 53.69  ? 36  PRO   C N   1 
ATOM   1696 C CA  . PRO   C 1 37 ? 25.660  -39.323 33.582  1.00 52.45  ? 36  PRO   C CA  1 
ATOM   1697 C C   . PRO   C 1 37 ? 26.675  -38.213 33.863  1.00 48.96  ? 36  PRO   C C   1 
ATOM   1698 O O   . PRO   C 1 37 ? 26.393  -37.044 33.581  1.00 40.55  ? 36  PRO   C O   1 
ATOM   1699 C CB  . PRO   C 1 37 ? 25.807  -39.940 32.176  1.00 46.66  ? 36  PRO   C CB  1 
ATOM   1700 C CG  . PRO   C 1 37 ? 24.378  -40.267 31.816  1.00 48.52  ? 36  PRO   C CG  1 
ATOM   1701 C CD  . PRO   C 1 37 ? 23.611  -39.031 32.270  1.00 51.63  ? 36  PRO   C CD  1 
ATOM   1702 N N   . PRO   C 1 38 ? 27.868  -38.525 34.427  1.00 45.22  ? 37  PRO   C N   1 
ATOM   1703 C CA  . PRO   C 1 38 ? 28.855  -37.493 34.736  1.00 47.73  ? 37  PRO   C CA  1 
ATOM   1704 C C   . PRO   C 1 38 ? 29.146  -36.608 33.529  1.00 43.43  ? 37  PRO   C C   1 
ATOM   1705 O O   . PRO   C 1 38 ? 29.398  -37.111 32.431  1.00 40.94  ? 37  PRO   C O   1 
ATOM   1706 C CB  . PRO   C 1 38 ? 30.087  -38.314 35.183  1.00 50.39  ? 37  PRO   C CB  1 
ATOM   1707 C CG  . PRO   C 1 38 ? 29.498  -39.597 35.723  1.00 46.03  ? 37  PRO   C CG  1 
ATOM   1708 C CD  . PRO   C 1 38 ? 28.324  -39.874 34.804  1.00 46.43  ? 37  PRO   C CD  1 
ATOM   1709 N N   . ASN   C 1 39 ? 29.028  -35.294 33.760  1.00 41.10  ? 38  ASN   C N   1 
ATOM   1710 C CA  . ASN   C 1 39 ? 29.421  -34.220 32.857  1.00 41.26  ? 38  ASN   C CA  1 
ATOM   1711 C C   . ASN   C 1 39 ? 28.474  -34.102 31.657  1.00 45.06  ? 38  ASN   C C   1 
ATOM   1712 O O   . ASN   C 1 39 ? 28.881  -33.585 30.615  1.00 45.21  ? 38  ASN   C O   1 
ATOM   1713 C CB  . ASN   C 1 39 ? 30.903  -34.265 32.494  1.00 46.43  ? 38  ASN   C CB  1 
ATOM   1714 C CG  . ASN   C 1 39 ? 31.362  -32.998 31.803  1.00 61.43  ? 38  ASN   C CG  1 
ATOM   1715 O OD1 . ASN   C 1 39 ? 31.006  -31.885 32.220  1.00 64.39  ? 38  ASN   C OD1 1 
ATOM   1716 N ND2 . ASN   C 1 39 ? 32.123  -33.139 30.725  1.00 60.55  ? 38  ASN   C ND2 1 
ATOM   1717 N N   . LYS   C 1 40 ? 27.222  -34.568 31.797  1.00 38.40  ? 39  LYS   C N   1 
ATOM   1718 C CA  . LYS   C 1 40 ? 26.288  -34.510 30.677  1.00 41.93  ? 39  LYS   C CA  1 
ATOM   1719 C C   . LYS   C 1 40 ? 25.162  -33.537 31.008  1.00 40.64  ? 39  LYS   C C   1 
ATOM   1720 O O   . LYS   C 1 40 ? 24.785  -33.415 32.168  1.00 40.59  ? 39  LYS   C O   1 
ATOM   1721 C CB  . LYS   C 1 40 ? 25.652  -35.865 30.350  1.00 37.30  ? 39  LYS   C CB  1 
ATOM   1722 C CG  . LYS   C 1 40 ? 26.630  -36.967 29.990  1.00 41.80  ? 39  LYS   C CG  1 
ATOM   1723 C CD  . LYS   C 1 40 ? 27.474  -36.714 28.753  1.00 43.31  ? 39  LYS   C CD  1 
ATOM   1724 C CE  . LYS   C 1 40 ? 28.160  -37.989 28.356  1.00 49.46  ? 39  LYS   C CE  1 
ATOM   1725 N NZ  . LYS   C 1 40 ? 29.129  -37.719 27.287  1.00 51.26  ? 39  LYS   C NZ  1 
ATOM   1726 N N   . TYR   C 1 41 ? 24.632  -32.857 29.985  1.00 36.01  ? 40  TYR   C N   1 
ATOM   1727 C CA  . TYR   C 1 41 ? 23.520  -31.927 30.164  1.00 33.81  ? 40  TYR   C CA  1 
ATOM   1728 C C   . TYR   C 1 41 ? 22.226  -32.548 29.661  1.00 36.49  ? 40  TYR   C C   1 
ATOM   1729 O O   . TYR   C 1 41 ? 22.249  -33.317 28.690  1.00 36.29  ? 40  TYR   C O   1 
ATOM   1730 C CB  . TYR   C 1 41 ? 23.733  -30.715 29.250  1.00 34.82  ? 40  TYR   C CB  1 
ATOM   1731 C CG  . TYR   C 1 41 ? 24.907  -29.837 29.646  1.00 36.83  ? 40  TYR   C CG  1 
ATOM   1732 C CD1 . TYR   C 1 41 ? 26.202  -30.123 29.210  1.00 40.15  ? 40  TYR   C CD1 1 
ATOM   1733 C CD2 . TYR   C 1 41 ? 24.714  -28.710 30.448  1.00 37.84  ? 40  TYR   C CD2 1 
ATOM   1734 C CE1 . TYR   C 1 41 ? 27.274  -29.321 29.574  1.00 46.85  ? 40  TYR   C CE1 1 
ATOM   1735 C CE2 . TYR   C 1 41 ? 25.772  -27.875 30.768  1.00 42.44  ? 40  TYR   C CE2 1 
ATOM   1736 C CZ  . TYR   C 1 41 ? 27.054  -28.196 30.356  1.00 47.76  ? 40  TYR   C CZ  1 
ATOM   1737 O OH  . TYR   C 1 41 ? 28.120  -27.405 30.676  1.00 58.62  ? 40  TYR   C OH  1 
ATOM   1738 N N   . PRO   C 1 42 ? 21.069  -32.249 30.310  1.00 36.96  ? 41  PRO   C N   1 
ATOM   1739 C CA  . PRO   C 1 42 ? 19.760  -32.677 29.810  1.00 34.51  ? 41  PRO   C CA  1 
ATOM   1740 C C   . PRO   C 1 42 ? 19.409  -31.731 28.669  1.00 33.09  ? 41  PRO   C C   1 
ATOM   1741 O O   . PRO   C 1 42 ? 19.413  -30.507 28.827  1.00 36.13  ? 41  PRO   C O   1 
ATOM   1742 C CB  . PRO   C 1 42 ? 18.826  -32.529 31.033  1.00 36.11  ? 41  PRO   C CB  1 
ATOM   1743 C CG  . PRO   C 1 42 ? 19.442  -31.381 31.785  1.00 40.91  ? 41  PRO   C CG  1 
ATOM   1744 C CD  . PRO   C 1 42 ? 20.957  -31.488 31.572  1.00 37.03  ? 41  PRO   C CD  1 
ATOM   1745 N N   . ILE   C 1 43 ? 19.180  -32.322 27.503  1.00 32.69  ? 42  ILE   C N   1 
ATOM   1746 C CA  . ILE   C 1 43 ? 18.893  -31.529 26.316  1.00 34.44  ? 42  ILE   C CA  1 
ATOM   1747 C C   . ILE   C 1 43 ? 17.442  -31.786 25.956  1.00 36.93  ? 42  ILE   C C   1 
ATOM   1748 O O   . ILE   C 1 43 ? 17.009  -32.929 26.003  1.00 34.98  ? 42  ILE   C O   1 
ATOM   1749 C CB  . ILE   C 1 43 ? 19.808  -31.962 25.159  1.00 33.54  ? 42  ILE   C CB  1 
ATOM   1750 C CG1 . ILE   C 1 43 ? 21.299  -31.675 25.488  1.00 29.25  ? 42  ILE   C CG1 1 
ATOM   1751 C CG2 . ILE   C 1 43 ? 19.360  -31.344 23.825  1.00 27.68  ? 42  ILE   C CG2 1 
ATOM   1752 C CD1 . ILE   C 1 43 ? 21.562  -30.279 26.033  1.00 30.22  ? 42  ILE   C CD1 1 
ATOM   1753 N N   . PHE   C 1 44 ? 16.723  -30.726 25.554  1.00 37.05  ? 43  PHE   C N   1 
ATOM   1754 C CA  . PHE   C 1 44 ? 15.436  -30.893 24.902  1.00 32.09  ? 43  PHE   C CA  1 
ATOM   1755 C C   . PHE   C 1 44 ? 15.572  -30.513 23.426  1.00 29.03  ? 43  PHE   C C   1 
ATOM   1756 O O   . PHE   C 1 44 ? 15.999  -29.391 23.128  1.00 30.43  ? 43  PHE   C O   1 
ATOM   1757 C CB  . PHE   C 1 44 ? 14.487  -29.891 25.563  1.00 34.69  ? 43  PHE   C CB  1 
ATOM   1758 C CG  . PHE   C 1 44 ? 13.106  -29.826 24.929  1.00 36.46  ? 43  PHE   C CG  1 
ATOM   1759 C CD1 . PHE   C 1 44 ? 12.182  -30.862 25.107  1.00 38.88  ? 43  PHE   C CD1 1 
ATOM   1760 C CD2 . PHE   C 1 44 ? 12.717  -28.709 24.179  1.00 42.34  ? 43  PHE   C CD2 1 
ATOM   1761 C CE1 . PHE   C 1 44 ? 10.912  -30.794 24.530  1.00 45.93  ? 43  PHE   C CE1 1 
ATOM   1762 C CE2 . PHE   C 1 44 ? 11.451  -28.652 23.592  1.00 40.92  ? 43  PHE   C CE2 1 
ATOM   1763 C CZ  . PHE   C 1 44 ? 10.556  -29.691 23.764  1.00 43.49  ? 43  PHE   C CZ  1 
ATOM   1764 N N   . PHE   C 1 45 ? 15.170  -31.425 22.529  1.00 30.21  ? 44  PHE   C N   1 
ATOM   1765 C CA  . PHE   C 1 45 ? 15.204  -31.199 21.086  1.00 31.75  ? 44  PHE   C CA  1 
ATOM   1766 C C   . PHE   C 1 45 ? 13.921  -30.520 20.603  1.00 34.50  ? 44  PHE   C C   1 
ATOM   1767 O O   . PHE   C 1 45 ? 12.827  -31.047 20.805  1.00 34.84  ? 44  PHE   C O   1 
ATOM   1768 C CB  . PHE   C 1 45 ? 15.409  -32.503 20.310  1.00 31.72  ? 44  PHE   C CB  1 
ATOM   1769 C CG  . PHE   C 1 45 ? 16.788  -33.089 20.570  1.00 30.92  ? 44  PHE   C CG  1 
ATOM   1770 C CD1 . PHE   C 1 45 ? 17.875  -32.726 19.784  1.00 33.26  ? 44  PHE   C CD1 1 
ATOM   1771 C CD2 . PHE   C 1 45 ? 17.007  -33.938 21.659  1.00 33.99  ? 44  PHE   C CD2 1 
ATOM   1772 C CE1 . PHE   C 1 45 ? 19.151  -33.240 20.035  1.00 31.04  ? 44  PHE   C CE1 1 
ATOM   1773 C CE2 . PHE   C 1 45 ? 18.285  -34.444 21.915  1.00 35.44  ? 44  PHE   C CE2 1 
ATOM   1774 C CZ  . PHE   C 1 45 ? 19.346  -34.104 21.098  1.00 33.61  ? 44  PHE   C CZ  1 
ATOM   1775 N N   . PHE   C 1 46 ? 14.065  -29.381 19.904  1.00 29.95  ? 45  PHE   C N   1 
ATOM   1776 C CA  . PHE   C 1 46 ? 12.910  -28.753 19.265  1.00 30.95  ? 45  PHE   C CA  1 
ATOM   1777 C C   . PHE   C 1 46 ? 12.417  -29.594 18.085  1.00 31.84  ? 45  PHE   C C   1 
ATOM   1778 O O   . PHE   C 1 46 ? 13.162  -30.392 17.522  1.00 31.56  ? 45  PHE   C O   1 
ATOM   1779 C CB  . PHE   C 1 46 ? 13.240  -27.311 18.855  1.00 30.56  ? 45  PHE   C CB  1 
ATOM   1780 C CG  . PHE   C 1 46 ? 13.503  -26.341 19.998  1.00 31.69  ? 45  PHE   C CG  1 
ATOM   1781 C CD1 . PHE   C 1 46 ? 12.454  -25.899 20.808  1.00 34.48  ? 45  PHE   C CD1 1 
ATOM   1782 C CD2 . PHE   C 1 46 ? 14.775  -25.806 20.208  1.00 29.84  ? 45  PHE   C CD2 1 
ATOM   1783 C CE1 . PHE   C 1 46 ? 12.698  -24.993 21.833  1.00 31.42  ? 45  PHE   C CE1 1 
ATOM   1784 C CE2 . PHE   C 1 46 ? 15.011  -24.891 21.237  1.00 31.78  ? 45  PHE   C CE2 1 
ATOM   1785 C CZ  . PHE   C 1 46 ? 13.970  -24.481 22.038  1.00 30.50  ? 45  PHE   C CZ  1 
ATOM   1786 N N   . GLY   C 1 47 ? 11.125  -29.436 17.747  1.00 31.75  ? 46  GLY   C N   1 
ATOM   1787 C CA  . GLY   C 1 47 ? 10.497  -30.194 16.682  1.00 38.07  ? 46  GLY   C CA  1 
ATOM   1788 C C   . GLY   C 1 47 ? 10.036  -31.567 17.161  1.00 46.04  ? 46  GLY   C C   1 
ATOM   1789 O O   . GLY   C 1 47 ? 8.835   -31.864 17.103  1.00 41.86  ? 46  GLY   C O   1 
ATOM   1790 N N   . THR   C 1 48 ? 11.000  -32.396 17.602  1.00 40.39  ? 47  THR   C N   1 
ATOM   1791 C CA  . THR   C 1 48 ? 10.690  -33.764 18.001  1.00 40.53  ? 47  THR   C CA  1 
ATOM   1792 C C   . THR   C 1 48 ? 10.233  -33.762 19.453  1.00 41.11  ? 47  THR   C C   1 
ATOM   1793 O O   . THR   C 1 48 ? 9.583   -34.717 19.886  1.00 46.15  ? 47  THR   C O   1 
ATOM   1794 C CB  . THR   C 1 48 ? 11.873  -34.723 17.835  1.00 35.67  ? 47  THR   C CB  1 
ATOM   1795 O OG1 . THR   C 1 48 ? 12.864  -34.239 18.744  1.00 39.31  ? 47  THR   C OG1 1 
ATOM   1796 C CG2 . THR   C 1 48 ? 12.355  -34.862 16.404  1.00 31.21  ? 47  THR   C CG2 1 
ATOM   1797 N N   . HIS   C 1 49 ? 10.626  -32.724 20.202  1.00 36.79  ? 48  HIS   C N   1 
ATOM   1798 C CA  . HIS   C 1 49 ? 10.334  -32.603 21.633  1.00 44.86  ? 48  HIS   C CA  1 
ATOM   1799 C C   . HIS   C 1 49 ? 10.817  -33.827 22.420  1.00 41.88  ? 48  HIS   C C   1 
ATOM   1800 O O   . HIS   C 1 49 ? 10.229  -34.172 23.441  1.00 48.94  ? 48  HIS   C O   1 
ATOM   1801 C CB  . HIS   C 1 49 ? 8.865   -32.233 21.912  1.00 46.31  ? 48  HIS   C CB  1 
ATOM   1802 C CG  . HIS   C 1 49 ? 8.336   -31.231 20.937  1.00 50.07  ? 48  HIS   C CG  1 
ATOM   1803 N ND1 . HIS   C 1 49 ? 7.378   -31.546 19.996  1.00 52.72  ? 48  HIS   C ND1 1 
ATOM   1804 C CD2 . HIS   C 1 49 ? 8.667   -29.948 20.723  1.00 45.19  ? 48  HIS   C CD2 1 
ATOM   1805 C CE1 . HIS   C 1 49 ? 7.132   -30.475 19.248  1.00 54.13  ? 48  HIS   C CE1 1 
ATOM   1806 N NE2 . HIS   C 1 49 ? 7.907   -29.497 19.672  1.00 53.83  ? 48  HIS   C NE2 1 
ATOM   1807 N N   . GLU   C 1 50 ? 11.912  -34.455 21.978  1.00 37.18  ? 49  GLU   C N   1 
ATOM   1808 C CA  . GLU   C 1 50 ? 12.526  -35.525 22.756  1.00 37.69  ? 49  GLU   C CA  1 
ATOM   1809 C C   . GLU   C 1 50 ? 13.640  -34.974 23.650  1.00 39.80  ? 49  GLU   C C   1 
ATOM   1810 O O   . GLU   C 1 50 ? 14.005  -33.800 23.573  1.00 35.50  ? 49  GLU   C O   1 
ATOM   1811 C CB  . GLU   C 1 50 ? 13.017  -36.629 21.828  1.00 37.69  ? 49  GLU   C CB  1 
ATOM   1812 C CG  . GLU   C 1 50 ? 11.914  -37.254 20.975  1.00 43.03  ? 49  GLU   C CG  1 
ATOM   1813 C CD  . GLU   C 1 50 ? 12.496  -38.280 20.014  1.00 49.50  ? 49  GLU   C CD  1 
ATOM   1814 O OE1 . GLU   C 1 50 ? 13.579  -38.865 20.273  1.00 49.19  ? 49  GLU   C OE1 1 
ATOM   1815 O OE2 . GLU   C 1 50 ? 11.880  -38.442 18.949  1.00 57.76  ? 49  GLU   C OE2 1 
ATOM   1816 N N   . THR   C 1 51 ? 14.167  -35.827 24.542  1.00 40.27  ? 50  THR   C N   1 
ATOM   1817 C CA  . THR   C 1 51 ? 15.217  -35.403 25.459  1.00 40.10  ? 50  THR   C CA  1 
ATOM   1818 C C   . THR   C 1 51 ? 16.351  -36.429 25.418  1.00 38.40  ? 50  THR   C C   1 
ATOM   1819 O O   . THR   C 1 51 ? 16.152  -37.571 25.027  1.00 36.30  ? 50  THR   C O   1 
ATOM   1820 C CB  . THR   C 1 51 ? 14.682  -35.191 26.878  1.00 45.05  ? 50  THR   C CB  1 
ATOM   1821 O OG1 . THR   C 1 51 ? 13.955  -36.378 27.177  1.00 51.48  ? 50  THR   C OG1 1 
ATOM   1822 C CG2 . THR   C 1 51 ? 13.776  -33.980 27.024  1.00 42.13  ? 50  THR   C CG2 1 
ATOM   1823 N N   . ALA   C 1 52 ? 17.566  -35.980 25.742  1.00 39.97  ? 51  ALA   C N   1 
ATOM   1824 C CA  . ALA   C 1 52 ? 18.694  -36.875 25.925  1.00 36.99  ? 51  ALA   C CA  1 
ATOM   1825 C C   . ALA   C 1 52 ? 19.689  -36.195 26.847  1.00 39.60  ? 51  ALA   C C   1 
ATOM   1826 O O   . ALA   C 1 52 ? 19.495  -35.042 27.238  1.00 39.25  ? 51  ALA   C O   1 
ATOM   1827 C CB  . ALA   C 1 52 ? 19.347  -37.240 24.607  1.00 40.05  ? 51  ALA   C CB  1 
ATOM   1828 N N   . PHE   C 1 53 ? 20.746  -36.940 27.189  1.00 39.39  ? 52  PHE   C N   1 
ATOM   1829 C CA  . PHE   C 1 53 ? 21.885  -36.389 27.896  1.00 39.26  ? 52  PHE   C CA  1 
ATOM   1830 C C   . PHE   C 1 53 ? 23.036  -36.298 26.907  1.00 35.60  ? 52  PHE   C C   1 
ATOM   1831 O O   . PHE   C 1 53 ? 23.346  -37.282 26.246  1.00 39.27  ? 52  PHE   C O   1 
ATOM   1832 C CB  . PHE   C 1 53 ? 22.214  -37.444 28.955  1.00 37.88  ? 52  PHE   C CB  1 
ATOM   1833 C CG  . PHE   C 1 53 ? 21.270  -37.352 30.134  1.00 40.69  ? 52  PHE   C CG  1 
ATOM   1834 C CD1 . PHE   C 1 53 ? 21.032  -36.129 30.761  1.00 44.03  ? 52  PHE   C CD1 1 
ATOM   1835 C CD2 . PHE   C 1 53 ? 20.600  -38.482 30.603  1.00 47.89  ? 52  PHE   C CD2 1 
ATOM   1836 C CE1 . PHE   C 1 53 ? 20.156  -36.036 31.838  1.00 45.16  ? 52  PHE   C CE1 1 
ATOM   1837 C CE2 . PHE   C 1 53 ? 19.746  -38.387 31.700  1.00 50.23  ? 52  PHE   C CE2 1 
ATOM   1838 C CZ  . PHE   C 1 53 ? 19.513  -37.166 32.308  1.00 43.76  ? 52  PHE   C CZ  1 
ATOM   1839 N N   . LEU   C 1 54 ? 23.666  -35.125 26.820  1.00 32.96  ? 53  LEU   C N   1 
ATOM   1840 C CA  . LEU   C 1 54 ? 24.799  -34.944 25.923  1.00 32.48  ? 53  LEU   C CA  1 
ATOM   1841 C C   . LEU   C 1 54 ? 25.905  -34.183 26.643  1.00 35.19  ? 53  LEU   C C   1 
ATOM   1842 O O   . LEU   C 1 54 ? 25.639  -33.381 27.533  1.00 34.65  ? 53  LEU   C O   1 
ATOM   1843 C CB  . LEU   C 1 54 ? 24.396  -34.182 24.657  1.00 32.63  ? 53  LEU   C CB  1 
ATOM   1844 C CG  . LEU   C 1 54 ? 23.513  -34.931 23.660  1.00 33.46  ? 53  LEU   C CG  1 
ATOM   1845 C CD1 . LEU   C 1 54 ? 23.221  -33.988 22.478  1.00 29.97  ? 53  LEU   C CD1 1 
ATOM   1846 C CD2 . LEU   C 1 54 ? 24.204  -36.192 23.173  1.00 39.38  ? 53  LEU   C CD2 1 
ATOM   1847 N N   . GLY   C 1 55 ? 27.142  -34.406 26.190  1.00 36.41  ? 54  GLY   C N   1 
ATOM   1848 C CA  . GLY   C 1 55 ? 28.299  -33.706 26.714  1.00 33.84  ? 54  GLY   C CA  1 
ATOM   1849 C C   . GLY   C 1 55 ? 28.513  -32.395 25.971  1.00 40.86  ? 54  GLY   C C   1 
ATOM   1850 O O   . GLY   C 1 55 ? 27.989  -32.204 24.867  1.00 34.28  ? 54  GLY   C O   1 
ATOM   1851 N N   . PRO   C 1 56 ? 29.317  -31.474 26.556  1.00 42.60  ? 55  PRO   C N   1 
ATOM   1852 C CA  . PRO   C 1 56 ? 29.447  -30.117 26.031  1.00 43.93  ? 55  PRO   C CA  1 
ATOM   1853 C C   . PRO   C 1 56 ? 30.135  -30.118 24.667  1.00 43.46  ? 55  PRO   C C   1 
ATOM   1854 O O   . PRO   C 1 56 ? 29.940  -29.207 23.866  1.00 49.45  ? 55  PRO   C O   1 
ATOM   1855 C CB  . PRO   C 1 56 ? 30.213  -29.349 27.137  1.00 46.60  ? 55  PRO   C CB  1 
ATOM   1856 C CG  . PRO   C 1 56 ? 30.965  -30.425 27.892  1.00 44.33  ? 55  PRO   C CG  1 
ATOM   1857 C CD  . PRO   C 1 56 ? 30.175  -31.721 27.732  1.00 45.66  ? 55  PRO   C CD  1 
ATOM   1858 N N   . LYS   C 1 57 ? 30.879  -31.187 24.383  1.00 41.03  ? 56  LYS   C N   1 
ATOM   1859 C CA  . LYS   C 1 57 ? 31.473  -31.414 23.075  1.00 42.52  ? 56  LYS   C CA  1 
ATOM   1860 C C   . LYS   C 1 57 ? 30.391  -31.395 21.992  1.00 49.09  ? 56  LYS   C C   1 
ATOM   1861 O O   . LYS   C 1 57 ? 30.669  -31.048 20.843  1.00 47.69  ? 56  LYS   C O   1 
ATOM   1862 C CB  . LYS   C 1 57 ? 32.138  -32.792 22.970  1.00 40.57  ? 56  LYS   C CB  1 
ATOM   1863 N N   . ASP   C 1 58 ? 29.166  -31.794 22.359  1.00 43.18  ? 57  ASP   C N   1 
ATOM   1864 C CA  . ASP   C 1 58 ? 28.147  -32.078 21.361  1.00 39.16  ? 57  ASP   C CA  1 
ATOM   1865 C C   . ASP   C 1 58 ? 27.212  -30.889 21.195  1.00 36.57  ? 57  ASP   C C   1 
ATOM   1866 O O   . ASP   C 1 58 ? 26.194  -31.015 20.518  1.00 35.83  ? 57  ASP   C O   1 
ATOM   1867 C CB  . ASP   C 1 58 ? 27.343  -33.312 21.730  1.00 43.52  ? 57  ASP   C CB  1 
ATOM   1868 C CG  . ASP   C 1 58 ? 28.146  -34.603 21.768  1.00 41.84  ? 57  ASP   C CG  1 
ATOM   1869 O OD1 . ASP   C 1 58 ? 28.952  -34.806 20.846  1.00 48.67  ? 57  ASP   C OD1 1 
ATOM   1870 O OD2 . ASP   C 1 58 ? 27.912  -35.406 22.689  1.00 48.29  ? 57  ASP   C OD2 1 
ATOM   1871 N N   . LEU   C 1 59 ? 27.547  -29.757 21.833  1.00 31.03  ? 58  LEU   C N   1 
ATOM   1872 C CA  . LEU   C 1 59 ? 26.631  -28.633 21.961  1.00 35.28  ? 58  LEU   C CA  1 
ATOM   1873 C C   . LEU   C 1 59 ? 27.283  -27.378 21.396  1.00 42.42  ? 58  LEU   C C   1 
ATOM   1874 O O   . LEU   C 1 59 ? 28.489  -27.179 21.593  1.00 44.32  ? 58  LEU   C O   1 
ATOM   1875 C CB  . LEU   C 1 59 ? 26.267  -28.421 23.426  1.00 35.30  ? 58  LEU   C CB  1 
ATOM   1876 C CG  . LEU   C 1 59 ? 25.685  -29.646 24.136  1.00 36.52  ? 58  LEU   C CG  1 
ATOM   1877 C CD1 . LEU   C 1 59 ? 25.491  -29.241 25.600  1.00 39.20  ? 58  LEU   C CD1 1 
ATOM   1878 C CD2 . LEU   C 1 59 ? 24.360  -30.089 23.501  1.00 26.31  ? 58  LEU   C CD2 1 
ATOM   1879 N N   . PHE   C 1 60 ? 26.460  -26.558 20.717  1.00 41.25  ? 59  PHE   C N   1 
ATOM   1880 C CA  . PHE   C 1 60 ? 26.893  -25.315 20.083  1.00 38.74  ? 59  PHE   C CA  1 
ATOM   1881 C C   . PHE   C 1 60 ? 25.921  -24.182 20.401  1.00 41.55  ? 59  PHE   C C   1 
ATOM   1882 O O   . PHE   C 1 60 ? 24.723  -24.309 20.154  1.00 40.31  ? 59  PHE   C O   1 
ATOM   1883 C CB  . PHE   C 1 60 ? 27.095  -25.537 18.581  1.00 40.33  ? 59  PHE   C CB  1 
ATOM   1884 C CG  . PHE   C 1 60 ? 28.006  -26.715 18.250  1.00 38.48  ? 59  PHE   C CG  1 
ATOM   1885 C CD1 . PHE   C 1 60 ? 27.524  -28.020 18.262  1.00 35.67  ? 59  PHE   C CD1 1 
ATOM   1886 C CD2 . PHE   C 1 60 ? 29.349  -26.514 17.933  1.00 41.77  ? 59  PHE   C CD2 1 
ATOM   1887 C CE1 . PHE   C 1 60 ? 28.356  -29.098 17.981  1.00 38.57  ? 59  PHE   C CE1 1 
ATOM   1888 C CE2 . PHE   C 1 60 ? 30.177  -27.592 17.628  1.00 41.89  ? 59  PHE   C CE2 1 
ATOM   1889 C CZ  . PHE   C 1 60 ? 29.678  -28.881 17.652  1.00 42.67  ? 59  PHE   C CZ  1 
ATOM   1890 N N   . PRO   C 1 61 ? 26.387  -23.029 20.959  1.00 44.36  ? 60  PRO   C N   1 
ATOM   1891 C CA  . PRO   C 1 61 ? 25.496  -21.893 21.220  1.00 43.07  ? 60  PRO   C CA  1 
ATOM   1892 C C   . PRO   C 1 61 ? 24.811  -21.460 19.922  1.00 38.68  ? 60  PRO   C C   1 
ATOM   1893 O O   . PRO   C 1 61 ? 25.459  -21.357 18.878  1.00 41.11  ? 60  PRO   C O   1 
ATOM   1894 C CB  . PRO   C 1 61 ? 26.390  -20.778 21.824  1.00 40.95  ? 60  PRO   C CB  1 
ATOM   1895 C CG  . PRO   C 1 61 ? 27.706  -21.475 22.155  1.00 41.41  ? 60  PRO   C CG  1 
ATOM   1896 C CD  . PRO   C 1 61 ? 27.786  -22.757 21.337  1.00 47.22  ? 60  PRO   C CD  1 
ATOM   1897 N N   . TYR   C 1 62 ? 23.495  -21.245 20.020  1.00 42.99  ? 61  TYR   C N   1 
ATOM   1898 C CA  . TYR   C 1 62 ? 22.588  -21.034 18.906  1.00 46.53  ? 61  TYR   C CA  1 
ATOM   1899 C C   . TYR   C 1 62 ? 23.003  -19.798 18.111  1.00 54.94  ? 61  TYR   C C   1 
ATOM   1900 O O   . TYR   C 1 62 ? 23.176  -19.882 16.901  1.00 54.28  ? 61  TYR   C O   1 
ATOM   1901 C CB  . TYR   C 1 62 ? 21.167  -20.849 19.444  1.00 47.62  ? 61  TYR   C CB  1 
ATOM   1902 C CG  . TYR   C 1 62 ? 20.151  -20.475 18.373  1.00 47.02  ? 61  TYR   C CG  1 
ATOM   1903 C CD1 . TYR   C 1 62 ? 19.990  -21.259 17.229  1.00 49.24  ? 61  TYR   C CD1 1 
ATOM   1904 C CD2 . TYR   C 1 62 ? 19.381  -19.318 18.493  1.00 47.72  ? 61  TYR   C CD2 1 
ATOM   1905 C CE1 . TYR   C 1 62 ? 19.068  -20.912 16.250  1.00 51.57  ? 61  TYR   C CE1 1 
ATOM   1906 C CE2 . TYR   C 1 62 ? 18.465  -18.960 17.518  1.00 51.01  ? 61  TYR   C CE2 1 
ATOM   1907 C CZ  . TYR   C 1 62 ? 18.315  -19.756 16.392  1.00 47.50  ? 61  TYR   C CZ  1 
ATOM   1908 O OH  . TYR   C 1 62 ? 17.407  -19.409 15.437  1.00 48.07  ? 61  TYR   C OH  1 
ATOM   1909 N N   . ASP   C 1 63 ? 23.188  -18.668 18.806  1.00 59.59  ? 62  ASP   C N   1 
ATOM   1910 C CA  . ASP   C 1 63 ? 23.521  -17.408 18.152  1.00 64.11  ? 62  ASP   C CA  1 
ATOM   1911 C C   . ASP   C 1 63 ? 24.866  -17.488 17.439  1.00 56.71  ? 62  ASP   C C   1 
ATOM   1912 O O   . ASP   C 1 63 ? 25.009  -16.977 16.329  1.00 64.40  ? 62  ASP   C O   1 
ATOM   1913 C CB  . ASP   C 1 63 ? 23.387  -16.223 19.094  1.00 69.48  ? 62  ASP   C CB  1 
ATOM   1914 C CG  . ASP   C 1 63 ? 21.994  -15.612 19.104  1.00 79.73  ? 62  ASP   C CG  1 
ATOM   1915 O OD1 . ASP   C 1 63 ? 21.211  -15.952 20.017  1.00 74.40  ? 62  ASP   C OD1 1 
ATOM   1916 O OD2 . ASP   C 1 63 ? 21.702  -14.814 18.184  1.00 89.72  ? 62  ASP   C OD2 1 
ATOM   1917 N N   . LYS   C 1 64 ? 25.839  -18.147 18.073  1.00 48.98  ? 63  LYS   C N   1 
ATOM   1918 C CA  . LYS   C 1 64 ? 27.177  -18.262 17.518  1.00 42.34  ? 63  LYS   C CA  1 
ATOM   1919 C C   . LYS   C 1 64 ? 27.151  -19.164 16.287  1.00 44.93  ? 63  LYS   C C   1 
ATOM   1920 O O   . LYS   C 1 64 ? 27.947  -18.959 15.371  1.00 46.12  ? 63  LYS   C O   1 
ATOM   1921 C CB  . LYS   C 1 64 ? 28.197  -18.800 18.532  1.00 44.17  ? 63  LYS   C CB  1 
ATOM   1922 N N   . SER   C 1 65 ? 26.228  -20.146 16.245  1.00 41.68  ? 64  SER   C N   1 
ATOM   1923 C CA  . SER   C 1 65 ? 26.429  -21.222 15.280  1.00 38.20  ? 64  SER   C CA  1 
ATOM   1924 C C   . SER   C 1 65 ? 25.296  -21.322 14.247  1.00 37.89  ? 64  SER   C C   1 
ATOM   1925 O O   . SER   C 1 65 ? 25.373  -22.138 13.337  1.00 35.39  ? 64  SER   C O   1 
ATOM   1926 C CB  . SER   C 1 65 ? 26.691  -22.546 15.984  1.00 43.98  ? 64  SER   C CB  1 
ATOM   1927 O OG  . SER   C 1 65 ? 25.487  -23.024 16.581  1.00 39.01  ? 64  SER   C OG  1 
ATOM   1928 N N   . LYS   C 1 66 ? 24.239  -20.512 14.384  1.00 37.84  ? 65  LYS   C N   1 
ATOM   1929 C CA  . LYS   C 1 66 ? 23.037  -20.695 13.571  1.00 37.91  ? 65  LYS   C CA  1 
ATOM   1930 C C   . LYS   C 1 66 ? 23.311  -20.455 12.081  1.00 41.91  ? 65  LYS   C C   1 
ATOM   1931 O O   . LYS   C 1 66 ? 22.610  -21.014 11.242  1.00 37.45  ? 65  LYS   C O   1 
ATOM   1932 C CB  . LYS   C 1 66 ? 21.821  -19.899 14.057  1.00 39.90  ? 65  LYS   C CB  1 
ATOM   1933 C CG  . LYS   C 1 66 ? 21.991  -18.378 13.999  1.00 43.09  ? 65  LYS   C CG  1 
ATOM   1934 C CD  . LYS   C 1 66 ? 20.797  -17.622 14.569  1.00 49.60  ? 65  LYS   C CD  1 
ATOM   1935 C CE  . LYS   C 1 66 ? 20.919  -16.138 14.421  1.00 52.19  ? 65  LYS   C CE  1 
ATOM   1936 N NZ  . LYS   C 1 66 ? 20.060  -15.438 15.380  1.00 56.58  ? 65  LYS   C NZ  1 
ATOM   1937 N N   . ASP   C 1 67 ? 24.323  -19.637 11.748  1.00 45.33  ? 66  ASP   C N   1 
ATOM   1938 C CA  . ASP   C 1 67 ? 24.670  -19.375 10.352  1.00 45.18  ? 66  ASP   C CA  1 
ATOM   1939 C C   . ASP   C 1 67 ? 25.119  -20.687 9.703   1.00 46.55  ? 66  ASP   C C   1 
ATOM   1940 O O   . ASP   C 1 67 ? 24.880  -20.921 8.518   1.00 45.81  ? 66  ASP   C O   1 
ATOM   1941 C CB  . ASP   C 1 67 ? 25.583  -18.161 10.197  1.00 46.67  ? 66  ASP   C CB  1 
ATOM   1942 C CG  . ASP   C 1 67 ? 26.941  -18.221 10.893  1.00 58.16  ? 66  ASP   C CG  1 
ATOM   1943 O OD1 . ASP   C 1 67 ? 27.223  -19.247 11.565  1.00 58.37  ? 66  ASP   C OD1 1 
ATOM   1944 O OD2 . ASP   C 1 67 ? 27.704  -17.221 10.793  1.00 57.16  ? 66  ASP   C OD2 1 
ATOM   1945 N N   . LYS   C 1 68 ? 25.690  -21.587 10.510  1.00 37.17  ? 67  LYS   C N   1 
ATOM   1946 C CA  . LYS   C 1 68 ? 26.190  -22.854 9.994   1.00 41.33  ? 67  LYS   C CA  1 
ATOM   1947 C C   . LYS   C 1 68 ? 25.134  -23.973 10.064  1.00 39.30  ? 67  LYS   C C   1 
ATOM   1948 O O   . LYS   C 1 68 ? 24.988  -24.737 9.111   1.00 40.90  ? 67  LYS   C O   1 
ATOM   1949 C CB  . LYS   C 1 68 ? 27.527  -23.164 10.683  1.00 41.71  ? 67  LYS   C CB  1 
ATOM   1950 C CG  . LYS   C 1 68 ? 28.147  -24.531 10.430  1.00 45.22  ? 67  LYS   C CG  1 
ATOM   1951 C CD  . LYS   C 1 68 ? 29.545  -24.474 11.052  1.00 58.55  ? 67  LYS   C CD  1 
ATOM   1952 C CE  . LYS   C 1 68 ? 30.271  -25.760 11.364  1.00 68.76  ? 67  LYS   C CE  1 
ATOM   1953 N NZ  . LYS   C 1 68 ? 30.478  -26.657 10.222  1.00 80.60  ? 67  LYS   C NZ  1 
ATOM   1954 N N   . TYR   C 1 69 ? 24.423  -24.104 11.195  1.00 32.99  ? 68  TYR   C N   1 
ATOM   1955 C CA  . TYR   C 1 69 ? 23.552  -25.260 11.374  1.00 35.19  ? 68  TYR   C CA  1 
ATOM   1956 C C   . TYR   C 1 69 ? 22.074  -24.905 11.195  1.00 34.16  ? 68  TYR   C C   1 
ATOM   1957 O O   . TYR   C 1 69 ? 21.224  -25.800 11.116  1.00 33.20  ? 68  TYR   C O   1 
ATOM   1958 C CB  . TYR   C 1 69 ? 23.749  -25.805 12.795  1.00 33.21  ? 68  TYR   C CB  1 
ATOM   1959 C CG  . TYR   C 1 69 ? 25.169  -26.252 13.090  1.00 36.00  ? 68  TYR   C CG  1 
ATOM   1960 C CD1 . TYR   C 1 69 ? 25.861  -27.067 12.204  1.00 33.44  ? 68  TYR   C CD1 1 
ATOM   1961 C CD2 . TYR   C 1 69 ? 25.826  -25.824 14.238  1.00 38.51  ? 68  TYR   C CD2 1 
ATOM   1962 C CE1 . TYR   C 1 69 ? 27.155  -27.493 12.459  1.00 37.98  ? 68  TYR   C CE1 1 
ATOM   1963 C CE2 . TYR   C 1 69 ? 27.122  -26.247 14.503  1.00 39.21  ? 68  TYR   C CE2 1 
ATOM   1964 C CZ  . TYR   C 1 69 ? 27.786  -27.080 13.619  1.00 40.40  ? 68  TYR   C CZ  1 
ATOM   1965 O OH  . TYR   C 1 69 ? 29.080  -27.444 13.891  1.00 41.52  ? 68  TYR   C OH  1 
ATOM   1966 N N   . GLY   C 1 70 ? 21.747  -23.607 11.214  1.00 32.77  ? 69  GLY   C N   1 
ATOM   1967 C CA  . GLY   C 1 70 ? 20.342  -23.224 11.165  1.00 41.76  ? 69  GLY   C CA  1 
ATOM   1968 C C   . GLY   C 1 70 ? 19.883  -23.103 9.714   1.00 38.45  ? 69  GLY   C C   1 
ATOM   1969 O O   . GLY   C 1 70 ? 19.858  -22.012 9.145   1.00 37.74  ? 69  GLY   C O   1 
ATOM   1970 N N   . LYS   C 1 71 ? 19.628  -24.251 9.099   1.00 36.72  ? 70  LYS   C N   1 
ATOM   1971 C CA  . LYS   C 1 71 ? 19.263  -24.309 7.694   1.00 38.17  ? 70  LYS   C CA  1 
ATOM   1972 C C   . LYS   C 1 71 ? 18.418  -25.565 7.544   1.00 35.82  ? 70  LYS   C C   1 
ATOM   1973 O O   . LYS   C 1 71 ? 18.609  -26.536 8.275   1.00 39.67  ? 70  LYS   C O   1 
ATOM   1974 C CB  . LYS   C 1 71 ? 20.474  -24.344 6.749   1.00 36.22  ? 70  LYS   C CB  1 
ATOM   1975 C CG  . LYS   C 1 71 ? 21.376  -25.550 6.979   1.00 46.89  ? 70  LYS   C CG  1 
ATOM   1976 C CD  . LYS   C 1 71 ? 22.670  -25.761 6.204   1.00 51.39  ? 70  LYS   C CD  1 
ATOM   1977 C CE  . LYS   C 1 71 ? 23.421  -26.952 6.739   1.00 53.78  ? 70  LYS   C CE  1 
ATOM   1978 N N   . PRO   C 1 72 ? 17.414  -25.562 6.648   1.00 33.28  ? 71  PRO   C N   1 
ATOM   1979 C CA  . PRO   C 1 72 ? 16.432  -26.641 6.637   1.00 31.22  ? 71  PRO   C CA  1 
ATOM   1980 C C   . PRO   C 1 72 ? 17.054  -28.007 6.378   1.00 35.11  ? 71  PRO   C C   1 
ATOM   1981 O O   . PRO   C 1 72 ? 18.142  -28.126 5.829   1.00 33.86  ? 71  PRO   C O   1 
ATOM   1982 C CB  . PRO   C 1 72 ? 15.471  -26.180 5.541   1.00 34.62  ? 71  PRO   C CB  1 
ATOM   1983 C CG  . PRO   C 1 72 ? 15.583  -24.663 5.618   1.00 33.15  ? 71  PRO   C CG  1 
ATOM   1984 C CD  . PRO   C 1 72 ? 17.096  -24.457 5.726   1.00 32.53  ? 71  PRO   C CD  1 
ATOM   1985 N N   . ASN   C 1 73 ? 16.360  -29.052 6.796   1.00 35.52  ? 72  ASN   C N   1 
ATOM   1986 C CA  . ASN   C 1 73 ? 16.680  -30.337 6.203   1.00 40.70  ? 72  ASN   C CA  1 
ATOM   1987 C C   . ASN   C 1 73 ? 15.458  -31.225 6.297   1.00 36.38  ? 72  ASN   C C   1 
ATOM   1988 O O   . ASN   C 1 73 ? 14.469  -30.833 6.900   1.00 32.79  ? 72  ASN   C O   1 
ATOM   1989 C CB  . ASN   C 1 73 ? 18.024  -30.927 6.617   1.00 48.27  ? 72  ASN   C CB  1 
ATOM   1990 C CG  . ASN   C 1 73 ? 17.994  -31.630 7.948   1.00 43.78  ? 72  ASN   C CG  1 
ATOM   1991 O OD1 . ASN   C 1 73 ? 17.311  -32.651 8.125   1.00 40.35  ? 72  ASN   C OD1 1 
ATOM   1992 N ND2 . ASN   C 1 73 ? 18.813  -31.134 8.852   1.00 49.30  ? 72  ASN   C ND2 1 
ATOM   1993 N N   . LYS   C 1 74 ? 15.540  -32.405 5.679   1.00 36.89  ? 73  LYS   C N   1 
ATOM   1994 C CA  . LYS   C 1 74 ? 14.318  -33.152 5.438   1.00 37.34  ? 73  LYS   C CA  1 
ATOM   1995 C C   . LYS   C 1 74 ? 14.063  -34.143 6.572   1.00 40.69  ? 73  LYS   C C   1 
ATOM   1996 O O   . LYS   C 1 74 ? 13.048  -34.834 6.550   1.00 43.57  ? 73  LYS   C O   1 
ATOM   1997 C CB  . LYS   C 1 74 ? 14.324  -33.712 4.006   1.00 45.16  ? 73  LYS   C CB  1 
ATOM   1998 C CG  . LYS   C 1 74 ? 13.990  -32.625 2.965   1.00 46.22  ? 73  LYS   C CG  1 
ATOM   1999 N N   . ARG   C 1 75 ? 14.966  -34.206 7.566   1.00 36.23  ? 74  ARG   C N   1 
ATOM   2000 C CA  . ARG   C 1 75 ? 14.775  -35.127 8.680   1.00 35.16  ? 74  ARG   C CA  1 
ATOM   2001 C C   . ARG   C 1 75 ? 13.516  -34.735 9.447   1.00 37.28  ? 74  ARG   C C   1 
ATOM   2002 O O   . ARG   C 1 75 ? 13.247  -33.546 9.650   1.00 31.89  ? 74  ARG   C O   1 
ATOM   2003 C CB  . ARG   C 1 75 ? 15.928  -35.274 9.691   1.00 34.28  ? 74  ARG   C CB  1 
ATOM   2004 C CG  . ARG   C 1 75 ? 17.287  -35.622 9.109   1.00 40.21  ? 74  ARG   C CG  1 
ATOM   2005 C CD  . ARG   C 1 75 ? 17.391  -37.002 8.437   1.00 43.00  ? 74  ARG   C CD  1 
ATOM   2006 N NE  . ARG   C 1 75 ? 17.667  -38.005 9.470   1.00 46.50  ? 74  ARG   C NE  1 
ATOM   2007 C CZ  . ARG   C 1 75 ? 18.874  -38.305 9.966   1.00 41.21  ? 74  ARG   C CZ  1 
ATOM   2008 N NH1 . ARG   C 1 75 ? 18.938  -38.931 11.116  1.00 43.94  ? 74  ARG   C NH1 1 
ATOM   2009 N NH2 . ARG   C 1 75 ? 19.991  -37.925 9.364   1.00 43.30  ? 74  ARG   C NH2 1 
ATOM   2010 N N   . LYS   C 1 76 ? 12.796  -35.757 9.934   1.00 38.60  ? 75  LYS   C N   1 
ATOM   2011 C CA  . LYS   C 1 76 ? 11.498  -35.573 10.573  1.00 45.31  ? 75  LYS   C CA  1 
ATOM   2012 C C   . LYS   C 1 76 ? 11.586  -34.631 11.774  1.00 42.84  ? 75  LYS   C C   1 
ATOM   2013 O O   . LYS   C 1 76 ? 12.365  -34.838 12.709  1.00 36.81  ? 75  LYS   C O   1 
ATOM   2014 C CB  . LYS   C 1 76 ? 10.837  -36.907 10.944  1.00 50.42  ? 75  LYS   C CB  1 
ATOM   2015 C CG  . LYS   C 1 76 ? 9.365   -36.749 11.319  1.00 57.76  ? 75  LYS   C CG  1 
ATOM   2016 C CD  . LYS   C 1 76 ? 8.704   -38.016 11.851  1.00 66.62  ? 75  LYS   C CD  1 
ATOM   2017 C CE  . LYS   C 1 76 ? 7.413   -37.747 12.573  1.00 68.40  ? 75  LYS   C CE  1 
ATOM   2018 N NZ  . LYS   C 1 76 ? 6.882   -38.978 13.163  1.00 73.87  ? 75  LYS   C NZ  1 
ATOM   2019 N N   . GLY   C 1 77 ? 10.733  -33.600 11.769  1.00 41.12  ? 76  GLY   C N   1 
ATOM   2020 C CA  . GLY   C 1 77 ? 10.652  -32.732 12.930  1.00 37.80  ? 76  GLY   C CA  1 
ATOM   2021 C C   . GLY   C 1 77 ? 11.663  -31.588 12.853  1.00 33.10  ? 76  GLY   C C   1 
ATOM   2022 O O   . GLY   C 1 77 ? 11.564  -30.621 13.603  1.00 33.62  ? 76  GLY   C O   1 
ATOM   2023 N N   . PHE   C 1 78 ? 12.584  -31.663 11.885  1.00 31.12  ? 77  PHE   C N   1 
ATOM   2024 C CA  . PHE   C 1 78 ? 13.694  -30.723 11.855  1.00 30.89  ? 77  PHE   C CA  1 
ATOM   2025 C C   . PHE   C 1 78 ? 13.190  -29.287 11.656  1.00 31.07  ? 77  PHE   C C   1 
ATOM   2026 O O   . PHE   C 1 78 ? 13.529  -28.389 12.425  1.00 31.05  ? 77  PHE   C O   1 
ATOM   2027 C CB  . PHE   C 1 78 ? 14.806  -31.090 10.866  1.00 32.41  ? 77  PHE   C CB  1 
ATOM   2028 C CG  . PHE   C 1 78 ? 16.097  -30.330 11.149  1.00 32.32  ? 77  PHE   C CG  1 
ATOM   2029 C CD1 . PHE   C 1 78 ? 16.288  -29.038 10.675  1.00 28.90  ? 77  PHE   C CD1 1 
ATOM   2030 C CD2 . PHE   C 1 78 ? 17.124  -30.908 11.896  1.00 30.08  ? 77  PHE   C CD2 1 
ATOM   2031 C CE1 . PHE   C 1 78 ? 17.482  -28.349 10.921  1.00 31.27  ? 77  PHE   C CE1 1 
ATOM   2032 C CE2 . PHE   C 1 78 ? 18.318  -30.215 12.138  1.00 27.21  ? 77  PHE   C CE2 1 
ATOM   2033 C CZ  . PHE   C 1 78 ? 18.484  -28.936 11.679  1.00 30.47  ? 77  PHE   C CZ  1 
ATOM   2034 N N   . ASN   C 1 79 ? 12.436  -29.067 10.575  1.00 29.15  ? 78  ASN   C N   1 
ATOM   2035 C CA  . ASN   C 1 79 ? 12.079  -27.715 10.181  1.00 33.57  ? 78  ASN   C CA  1 
ATOM   2036 C C   . ASN   C 1 79 ? 11.135  -27.106 11.211  1.00 34.11  ? 78  ASN   C C   1 
ATOM   2037 O O   . ASN   C 1 79 ? 11.233  -25.924 11.545  1.00 32.72  ? 78  ASN   C O   1 
ATOM   2038 C CB  . ASN   C 1 79 ? 11.626  -27.665 8.723   1.00 32.60  ? 78  ASN   C CB  1 
ATOM   2039 C CG  . ASN   C 1 79 ? 12.724  -28.164 7.808   1.00 35.59  ? 78  ASN   C CG  1 
ATOM   2040 O OD1 . ASN   C 1 79 ? 13.904  -27.964 8.101   1.00 32.92  ? 78  ASN   C OD1 1 
ATOM   2041 N ND2 . ASN   C 1 79 ? 12.365  -28.733 6.667   1.00 31.54  ? 78  ASN   C ND2 1 
ATOM   2042 N N   . GLU   C 1 80 ? 10.249  -27.915 11.786  1.00 34.76  ? 79  GLU   C N   1 
ATOM   2043 C CA  . GLU   C 1 80 ? 9.446   -27.371 12.873  1.00 34.15  ? 79  GLU   C CA  1 
ATOM   2044 C C   . GLU   C 1 80 ? 10.351  -26.974 14.033  1.00 33.36  ? 79  GLU   C C   1 
ATOM   2045 O O   . GLU   C 1 80 ? 10.138  -25.932 14.663  1.00 33.88  ? 79  GLU   C O   1 
ATOM   2046 C CB  . GLU   C 1 80 ? 8.346   -28.358 13.265  1.00 38.87  ? 79  GLU   C CB  1 
ATOM   2047 C CG  . GLU   C 1 80 ? 7.635   -27.979 14.556  1.00 40.12  ? 79  GLU   C CG  1 
ATOM   2048 C CD  . GLU   C 1 80 ? 6.403   -28.853 14.651  1.00 54.78  ? 79  GLU   C CD  1 
ATOM   2049 O OE1 . GLU   C 1 80 ? 6.499   -30.037 14.251  1.00 55.48  ? 79  GLU   C OE1 1 
ATOM   2050 O OE2 . GLU   C 1 80 ? 5.352   -28.352 15.104  1.00 52.90  ? 79  GLU   C OE2 1 
ATOM   2051 N N   . GLY   C 1 81 ? 11.392  -27.799 14.286  1.00 35.03  ? 80  GLY   C N   1 
ATOM   2052 C CA  . GLY   C 1 81 ? 12.364  -27.455 15.317  1.00 29.87  ? 80  GLY   C CA  1 
ATOM   2053 C C   . GLY   C 1 81 ? 12.970  -26.071 15.084  1.00 33.31  ? 80  GLY   C C   1 
ATOM   2054 O O   . GLY   C 1 81 ? 13.169  -25.299 16.018  1.00 31.52  ? 80  GLY   C O   1 
ATOM   2055 N N   . LEU   C 1 82 ? 13.334  -25.775 13.831  1.00 32.97  ? 81  LEU   C N   1 
ATOM   2056 C CA  . LEU   C 1 82 ? 13.921  -24.482 13.501  1.00 34.39  ? 81  LEU   C CA  1 
ATOM   2057 C C   . LEU   C 1 82 ? 12.917  -23.364 13.777  1.00 32.06  ? 81  LEU   C C   1 
ATOM   2058 O O   . LEU   C 1 82 ? 13.311  -22.295 14.237  1.00 35.22  ? 81  LEU   C O   1 
ATOM   2059 C CB  . LEU   C 1 82 ? 14.406  -24.394 12.051  1.00 35.65  ? 81  LEU   C CB  1 
ATOM   2060 C CG  . LEU   C 1 82 ? 15.580  -25.285 11.648  1.00 33.75  ? 81  LEU   C CG  1 
ATOM   2061 C CD1 . LEU   C 1 82 ? 15.793  -25.189 10.133  1.00 35.10  ? 81  LEU   C CD1 1 
ATOM   2062 C CD2 . LEU   C 1 82 ? 16.818  -24.796 12.347  1.00 34.15  ? 81  LEU   C CD2 1 
ATOM   2063 N N   . TRP   C 1 83 ? 11.636  -23.595 13.471  1.00 34.18  ? 82  TRP   C N   1 
ATOM   2064 C CA  . TRP   C 1 83 ? 10.634  -22.565 13.722  1.00 39.60  ? 82  TRP   C CA  1 
ATOM   2065 C C   . TRP   C 1 83 ? 10.532  -22.244 15.224  1.00 38.77  ? 82  TRP   C C   1 
ATOM   2066 O O   . TRP   C 1 83 ? 10.509  -21.077 15.629  1.00 36.60  ? 82  TRP   C O   1 
ATOM   2067 C CB  . TRP   C 1 83 ? 9.276   -22.945 13.116  1.00 41.90  ? 82  TRP   C CB  1 
ATOM   2068 C CG  . TRP   C 1 83 ? 8.279   -21.811 13.204  1.00 45.63  ? 82  TRP   C CG  1 
ATOM   2069 C CD1 . TRP   C 1 83 ? 8.064   -20.814 12.293  1.00 37.80  ? 82  TRP   C CD1 1 
ATOM   2070 C CD2 . TRP   C 1 83 ? 7.402   -21.536 14.317  1.00 44.56  ? 82  TRP   C CD2 1 
ATOM   2071 N NE1 . TRP   C 1 83 ? 7.103   -19.955 12.754  1.00 45.89  ? 82  TRP   C NE1 1 
ATOM   2072 C CE2 . TRP   C 1 83 ? 6.682   -20.363 13.990  1.00 45.08  ? 82  TRP   C CE2 1 
ATOM   2073 C CE3 . TRP   C 1 83 ? 7.161   -22.162 15.546  1.00 44.15  ? 82  TRP   C CE3 1 
ATOM   2074 C CZ2 . TRP   C 1 83 ? 5.730   -19.818 14.846  1.00 49.32  ? 82  TRP   C CZ2 1 
ATOM   2075 C CZ3 . TRP   C 1 83 ? 6.224   -21.617 16.398  1.00 48.56  ? 82  TRP   C CZ3 1 
ATOM   2076 C CH2 . TRP   C 1 83 ? 5.521   -20.459 16.050  1.00 51.03  ? 82  TRP   C CH2 1 
ATOM   2077 N N   . GLU   C 1 84 ? 10.538  -23.291 16.050  1.00 37.65  ? 83  GLU   C N   1 
ATOM   2078 C CA  . GLU   C 1 84 ? 10.444  -23.159 17.504  1.00 36.90  ? 83  GLU   C CA  1 
ATOM   2079 C C   . GLU   C 1 84 ? 11.634  -22.421 18.101  1.00 36.66  ? 83  GLU   C C   1 
ATOM   2080 O O   . GLU   C 1 84 ? 11.428  -21.553 18.950  1.00 38.50  ? 83  GLU   C O   1 
ATOM   2081 C CB  . GLU   C 1 84 ? 10.333  -24.510 18.214  1.00 31.04  ? 83  GLU   C CB  1 
ATOM   2082 C CG  . GLU   C 1 84 ? 9.018   -25.216 17.890  1.00 36.69  ? 83  GLU   C CG  1 
ATOM   2083 C CD  . GLU   C 1 84 ? 8.884   -26.643 18.366  1.00 39.10  ? 83  GLU   C CD  1 
ATOM   2084 O OE1 . GLU   C 1 84 ? 9.889   -27.192 18.881  1.00 39.77  ? 83  GLU   C OE1 1 
ATOM   2085 O OE2 . GLU   C 1 84 ? 7.778   -27.209 18.185  1.00 44.67  ? 83  GLU   C OE2 1 
ATOM   2086 N N   . ILE   C 1 85 ? 12.870  -22.763 17.690  1.00 32.23  ? 84  ILE   C N   1 
ATOM   2087 C CA  . ILE   C 1 85 ? 14.045  -22.178 18.326  1.00 33.64  ? 84  ILE   C CA  1 
ATOM   2088 C C   . ILE   C 1 85 ? 14.088  -20.669 18.064  1.00 37.78  ? 84  ILE   C C   1 
ATOM   2089 O O   . ILE   C 1 85 ? 14.701  -19.930 18.835  1.00 36.14  ? 84  ILE   C O   1 
ATOM   2090 C CB  . ILE   C 1 85 ? 15.368  -22.876 17.953  1.00 30.65  ? 84  ILE   C CB  1 
ATOM   2091 C CG1 . ILE   C 1 85 ? 16.492  -22.512 18.945  1.00 31.93  ? 84  ILE   C CG1 1 
ATOM   2092 C CG2 . ILE   C 1 85 ? 15.790  -22.644 16.495  1.00 29.16  ? 84  ILE   C CG2 1 
ATOM   2093 C CD1 . ILE   C 1 85 ? 17.692  -23.452 18.965  1.00 30.88  ? 84  ILE   C CD1 1 
ATOM   2094 N N   . GLN   C 1 86 ? 13.466  -20.248 16.957  1.00 36.40  ? 85  GLN   C N   1 
ATOM   2095 C CA  . GLN   C 1 86 ? 13.508  -18.879 16.468  1.00 37.93  ? 85  GLN   C CA  1 
ATOM   2096 C C   . GLN   C 1 86 ? 12.309  -18.107 17.003  1.00 37.91  ? 85  GLN   C C   1 
ATOM   2097 O O   . GLN   C 1 86 ? 12.448  -16.934 17.319  1.00 42.80  ? 85  GLN   C O   1 
ATOM   2098 C CB  . GLN   C 1 86 ? 13.507  -18.789 14.933  1.00 38.58  ? 85  GLN   C CB  1 
ATOM   2099 C CG  . GLN   C 1 86 ? 13.845  -17.401 14.376  1.00 40.59  ? 85  GLN   C CG  1 
ATOM   2100 C CD  . GLN   C 1 86 ? 14.287  -17.378 12.916  1.00 41.10  ? 85  GLN   C CD  1 
ATOM   2101 O OE1 . GLN   C 1 86 ? 14.103  -18.329 12.148  1.00 39.81  ? 85  GLN   C OE1 1 
ATOM   2102 N NE2 . GLN   C 1 86 ? 14.904  -16.279 12.508  1.00 40.74  ? 85  GLN   C NE2 1 
ATOM   2103 N N   . ASN   C 1 87 ? 11.151  -18.762 17.095  1.00 40.34  ? 86  ASN   C N   1 
ATOM   2104 C CA  . ASN   C 1 87 ? 9.875   -18.068 17.268  1.00 47.94  ? 86  ASN   C CA  1 
ATOM   2105 C C   . ASN   C 1 87 ? 9.193   -18.357 18.610  1.00 52.82  ? 86  ASN   C C   1 
ATOM   2106 O O   . ASN   C 1 87 ? 8.252   -17.650 18.957  1.00 54.65  ? 86  ASN   C O   1 
ATOM   2107 C CB  . ASN   C 1 87 ? 8.922   -18.336 16.106  1.00 44.16  ? 86  ASN   C CB  1 
ATOM   2108 C CG  . ASN   C 1 87 ? 9.506   -17.774 14.832  1.00 50.30  ? 86  ASN   C CG  1 
ATOM   2109 O OD1 . ASN   C 1 87 ? 9.564   -16.550 14.680  1.00 48.86  ? 86  ASN   C OD1 1 
ATOM   2110 N ND2 . ASN   C 1 87 ? 10.004  -18.630 13.945  1.00 40.56  ? 86  ASN   C ND2 1 
ATOM   2111 N N   . ASN   C 1 88 ? 9.632   -19.395 19.349  1.00 53.01  ? 87  ASN   C N   1 
ATOM   2112 C CA  . ASN   C 1 88 ? 8.957   -19.826 20.575  1.00 45.46  ? 87  ASN   C CA  1 
ATOM   2113 C C   . ASN   C 1 88 ? 9.947   -20.625 21.428  1.00 43.66  ? 87  ASN   C C   1 
ATOM   2114 O O   . ASN   C 1 88 ? 9.643   -21.748 21.817  1.00 52.30  ? 87  ASN   C O   1 
ATOM   2115 C CB  . ASN   C 1 88 ? 7.754   -20.721 20.243  1.00 51.60  ? 87  ASN   C CB  1 
ATOM   2116 C CG  . ASN   C 1 88 ? 6.650   -20.757 21.281  1.00 55.22  ? 87  ASN   C CG  1 
ATOM   2117 O OD1 . ASN   C 1 88 ? 6.618   -19.927 22.195  1.00 59.36  ? 87  ASN   C OD1 1 
ATOM   2118 N ND2 . ASN   C 1 88 ? 5.714   -21.689 21.143  1.00 56.31  ? 87  ASN   C ND2 1 
ATOM   2119 N N   . PRO   C 1 89 ? 11.172  -20.114 21.718  1.00 43.42  ? 88  PRO   C N   1 
ATOM   2120 C CA  . PRO   C 1 89 ? 12.257  -20.962 22.222  1.00 43.77  ? 88  PRO   C CA  1 
ATOM   2121 C C   . PRO   C 1 89 ? 12.135  -21.417 23.675  1.00 55.04  ? 88  PRO   C C   1 
ATOM   2122 O O   . PRO   C 1 89 ? 12.656  -22.472 24.046  1.00 49.48  ? 88  PRO   C O   1 
ATOM   2123 C CB  . PRO   C 1 89 ? 13.520  -20.124 22.029  1.00 42.81  ? 88  PRO   C CB  1 
ATOM   2124 C CG  . PRO   C 1 89 ? 13.040  -18.682 22.039  1.00 42.28  ? 88  PRO   C CG  1 
ATOM   2125 C CD  . PRO   C 1 89 ? 11.577  -18.707 21.577  1.00 43.43  ? 88  PRO   C CD  1 
ATOM   2126 N N   . HIS   C 1 90 ? 11.475  -20.584 24.487  1.00 56.75  ? 89  HIS   C N   1 
ATOM   2127 C CA  . HIS   C 1 90 ? 11.467  -20.750 25.932  1.00 56.07  ? 89  HIS   C CA  1 
ATOM   2128 C C   . HIS   C 1 90 ? 10.070  -21.156 26.382  1.00 56.58  ? 89  HIS   C C   1 
ATOM   2129 O O   . HIS   C 1 90 ? 9.708   -20.911 27.521  1.00 60.28  ? 89  HIS   C O   1 
ATOM   2130 C CB  . HIS   C 1 90 ? 11.930  -19.452 26.597  1.00 51.65  ? 89  HIS   C CB  1 
ATOM   2131 C CG  . HIS   C 1 90 ? 13.344  -19.137 26.287  1.00 46.08  ? 89  HIS   C CG  1 
ATOM   2132 N ND1 . HIS   C 1 90 ? 14.355  -20.043 26.519  1.00 51.17  ? 89  HIS   C ND1 1 
ATOM   2133 C CD2 . HIS   C 1 90 ? 13.922  -18.052 25.777  1.00 48.87  ? 89  HIS   C CD2 1 
ATOM   2134 C CE1 . HIS   C 1 90 ? 15.512  -19.509 26.151  1.00 51.74  ? 89  HIS   C CE1 1 
ATOM   2135 N NE2 . HIS   C 1 90 ? 15.271  -18.295 25.699  1.00 54.49  ? 89  HIS   C NE2 1 
ATOM   2136 N N   . ALA   C 1 91 ? 9.303   -21.777 25.480  1.00 60.41  ? 90  ALA   C N   1 
ATOM   2137 C CA  . ALA   C 1 91 ? 7.949   -22.224 25.771  1.00 66.87  ? 90  ALA   C CA  1 
ATOM   2138 C C   . ALA   C 1 91 ? 7.980   -23.548 26.536  1.00 81.80  ? 90  ALA   C C   1 
ATOM   2139 O O   . ALA   C 1 91 ? 8.987   -23.865 27.164  1.00 78.00  ? 90  ALA   C O   1 
ATOM   2140 C CB  . ALA   C 1 91 ? 7.162   -22.348 24.488  1.00 59.68  ? 90  ALA   C CB  1 
ATOM   2141 N N   . SER   C 1 92 ? 6.875   -24.318 26.456  1.00 92.26  ? 91  SER   C N   1 
ATOM   2142 C CA  . SER   C 1 92 ? 6.669   -25.521 27.257  1.00 89.02  ? 91  SER   C CA  1 
ATOM   2143 C C   . SER   C 1 92 ? 6.816   -26.804 26.435  1.00 92.76  ? 91  SER   C C   1 
ATOM   2144 O O   . SER   C 1 92 ? 7.920   -27.338 26.349  1.00 101.31 ? 91  SER   C O   1 
ATOM   2145 C CB  . SER   C 1 92 ? 5.373   -25.477 28.045  1.00 90.41  ? 91  SER   C CB  1 
ATOM   2146 O OG  . SER   C 1 92 ? 5.565   -24.842 29.303  1.00 81.93  ? 91  SER   C OG  1 
ATOM   2147 N N   . TYR   C 1 93 ? 5.711   -27.300 25.849  1.00 91.24  ? 92  TYR   C N   1 
ATOM   2148 C CA  . TYR   C 1 93 ? 5.653   -28.609 25.199  1.00 85.40  ? 92  TYR   C CA  1 
ATOM   2149 C C   . TYR   C 1 93 ? 6.526   -29.613 25.963  1.00 81.38  ? 92  TYR   C C   1 
ATOM   2150 O O   . TYR   C 1 93 ? 6.464   -29.544 27.210  1.00 77.71  ? 92  TYR   C O   1 
ATOM   2151 C CB  . TYR   C 1 93 ? 5.889   -28.701 23.682  1.00 86.93  ? 92  TYR   C CB  1 
ATOM   2152 C CG  . TYR   C 1 93 ? 6.638   -27.553 23.007  1.00 88.87  ? 92  TYR   C CG  1 
ATOM   2153 C CD1 . TYR   C 1 93 ? 6.227   -27.067 21.765  1.00 86.98  ? 92  TYR   C CD1 1 
ATOM   2154 C CD2 . TYR   C 1 93 ? 7.753   -26.953 23.592  1.00 79.14  ? 92  TYR   C CD2 1 
ATOM   2155 C CE1 . TYR   C 1 93 ? 6.883   -26.017 21.139  1.00 78.72  ? 92  TYR   C CE1 1 
ATOM   2156 C CE2 . TYR   C 1 93 ? 8.415   -25.898 22.980  1.00 79.69  ? 92  TYR   C CE2 1 
ATOM   2157 C CZ  . TYR   C 1 93 ? 7.981   -25.432 21.749  1.00 77.11  ? 92  TYR   C CZ  1 
ATOM   2158 O OH  . TYR   C 1 93 ? 8.628   -24.392 21.144  1.00 78.26  ? 92  TYR   C OH  1 
HETATM 2159 S S   . SO4   D 2 .  ? 0.402   -33.514 2.056   1.00 112.37 ? 101 SO4   A S   1 
HETATM 2160 O O1  . SO4   D 2 .  ? 1.066   -34.342 1.079   1.00 96.77  ? 101 SO4   A O1  1 
HETATM 2161 O O2  . SO4   D 2 .  ? 0.006   -32.267 1.448   1.00 117.07 ? 101 SO4   A O2  1 
HETATM 2162 O O3  . SO4   D 2 .  ? -0.765  -34.198 2.552   1.00 114.59 ? 101 SO4   A O3  1 
HETATM 2163 O O4  . SO4   D 2 .  ? 1.297   -33.247 3.147   1.00 97.48  ? 101 SO4   A O4  1 
HETATM 2164 S S   . SO4   E 2 .  ? -9.769  -24.554 1.274   1.00 92.32  ? 102 SO4   A S   1 
HETATM 2165 O O1  . SO4   E 2 .  ? -10.211 -24.595 -0.096  1.00 89.16  ? 102 SO4   A O1  1 
HETATM 2166 O O2  . SO4   E 2 .  ? -10.223 -23.334 1.893   1.00 96.93  ? 102 SO4   A O2  1 
HETATM 2167 O O3  . SO4   E 2 .  ? -10.303 -25.688 1.980   1.00 101.51 ? 102 SO4   A O3  1 
HETATM 2168 O O4  . SO4   E 2 .  ? -8.337  -24.602 1.324   1.00 97.23  ? 102 SO4   A O4  1 
HETATM 2169 C C1  . EDO   F 3 .  ? 13.631  -19.582 -7.325  1.00 39.55  ? 103 EDO   A C1  1 
HETATM 2170 O O1  . EDO   F 3 .  ? 14.883  -18.851 -7.271  1.00 34.70  ? 103 EDO   A O1  1 
HETATM 2171 C C2  . EDO   F 3 .  ? 12.595  -19.133 -8.312  1.00 37.23  ? 103 EDO   A C2  1 
HETATM 2172 O O2  . EDO   F 3 .  ? 12.276  -17.748 -8.238  1.00 34.58  ? 103 EDO   A O2  1 
HETATM 2173 S S   . SO4   G 2 .  ? 8.645   -29.277 6.104   1.00 66.77  ? 104 SO4   A S   1 
HETATM 2174 O O1  . SO4   G 2 .  ? 9.214   -28.255 5.286   1.00 68.90  ? 104 SO4   A O1  1 
HETATM 2175 O O2  . SO4   G 2 .  ? 8.354   -30.435 5.286   1.00 76.74  ? 104 SO4   A O2  1 
HETATM 2176 O O3  . SO4   G 2 .  ? 9.570   -29.639 7.147   1.00 75.38  ? 104 SO4   A O3  1 
HETATM 2177 O O4  . SO4   G 2 .  ? 7.418   -28.796 6.690   1.00 85.04  ? 104 SO4   A O4  1 
HETATM 2178 S S   . SO4   H 2 .  ? 7.439   -8.647  -24.702 1.00 70.41  ? 101 SO4   B S   1 
HETATM 2179 O O1  . SO4   H 2 .  ? 8.532   -8.752  -25.638 1.00 47.00  ? 101 SO4   B O1  1 
HETATM 2180 O O2  . SO4   H 2 .  ? 6.221   -9.116  -25.319 1.00 56.79  ? 101 SO4   B O2  1 
HETATM 2181 O O3  . SO4   H 2 .  ? 7.662   -9.458  -23.505 1.00 44.40  ? 101 SO4   B O3  1 
HETATM 2182 O O4  . SO4   H 2 .  ? 7.345   -7.244  -24.352 1.00 61.61  ? 101 SO4   B O4  1 
HETATM 2183 S S   . SO4   I 2 .  ? 14.262  -27.136 -26.428 1.00 61.36  ? 102 SO4   B S   1 
HETATM 2184 O O1  . SO4   I 2 .  ? 15.680  -26.903 -26.347 1.00 55.04  ? 102 SO4   B O1  1 
HETATM 2185 O O2  . SO4   I 2 .  ? 14.018  -28.468 -26.921 1.00 65.86  ? 102 SO4   B O2  1 
HETATM 2186 O O3  . SO4   I 2 .  ? 13.695  -26.998 -25.108 1.00 63.28  ? 102 SO4   B O3  1 
HETATM 2187 O O4  . SO4   I 2 .  ? 13.648  -26.181 -27.319 1.00 57.01  ? 102 SO4   B O4  1 
HETATM 2188 N N1  . A1A3U J 4 .  ? 17.168  -14.171 -25.230 0.80 32.86  ? 103 A1A3U B N1  1 
HETATM 2189 C C4  . A1A3U J 4 .  ? 18.234  -16.735 -20.175 0.80 36.39  ? 103 A1A3U B C4  1 
HETATM 2190 C C5  . A1A3U J 4 .  ? 18.725  -15.638 -24.118 0.80 37.05  ? 103 A1A3U B C5  1 
HETATM 2191 C C6  . A1A3U J 4 .  ? 18.059  -16.732 -24.650 0.80 34.16  ? 103 A1A3U B C6  1 
HETATM 2192 C C7  . A1A3U J 4 .  ? 16.990  -16.540 -25.500 0.80 33.60  ? 103 A1A3U B C7  1 
HETATM 2193 C C8  . A1A3U J 4 .  ? 16.588  -15.243 -25.768 0.80 34.08  ? 103 A1A3U B C8  1 
HETATM 2194 C C   . A1A3U J 4 .  ? 21.173  -16.437 -24.123 0.80 33.89  ? 103 A1A3U B C   1 
HETATM 2195 C C1  . A1A3U J 4 .  ? 20.037  -15.771 -23.352 0.80 43.64  ? 103 A1A3U B C1  1 
HETATM 2196 N N   . A1A3U J 4 .  ? 19.944  -16.389 -22.023 0.80 31.02  ? 103 A1A3U B N   1 
HETATM 2197 C C2  . A1A3U J 4 .  ? 18.628  -16.906 -21.602 0.80 36.68  ? 103 A1A3U B C2  1 
HETATM 2198 C C3  . A1A3U J 4 .  ? 17.549  -15.941 -21.241 0.80 34.07  ? 103 A1A3U B C3  1 
HETATM 2199 C C9  . A1A3U J 4 .  ? 18.209  -14.386 -24.419 0.80 34.03  ? 103 A1A3U B C9  1 
HETATM 2200 S S   . SO4   K 2 .  ? 28.977  -38.135 12.208  1.00 97.45  ? 101 SO4   C S   1 
HETATM 2201 O O1  . SO4   K 2 .  ? 30.112  -37.374 11.754  1.00 105.10 ? 101 SO4   C O1  1 
HETATM 2202 O O2  . SO4   K 2 .  ? 27.812  -37.744 11.464  1.00 91.91  ? 101 SO4   C O2  1 
HETATM 2203 O O3  . SO4   K 2 .  ? 29.217  -39.537 12.001  1.00 95.51  ? 101 SO4   C O3  1 
HETATM 2204 O O4  . SO4   K 2 .  ? 28.772  -37.884 13.611  1.00 103.63 ? 101 SO4   C O4  1 
HETATM 2205 N N1  . A1A3U L 4 .  ? 15.293  -35.529 18.140  0.72 28.20  ? 102 A1A3U C N1  1 
HETATM 2206 C C4  . A1A3U L 4 .  ? 17.057  -38.053 21.149  0.72 43.66  ? 102 A1A3U C C4  1 
HETATM 2207 C C5  . A1A3U L 4 .  ? 16.324  -37.706 17.943  0.72 38.88  ? 102 A1A3U C C5  1 
HETATM 2208 C C6  . A1A3U L 4 .  ? 17.480  -37.095 17.483  0.72 34.35  ? 102 A1A3U C C6  1 
HETATM 2209 C C7  . A1A3U L 4 .  ? 17.515  -35.723 17.299  0.72 31.72  ? 102 A1A3U C C7  1 
HETATM 2210 C C8  . A1A3U L 4 .  ? 16.404  -34.987 17.632  0.72 27.94  ? 102 A1A3U C C8  1 
HETATM 2211 C C   . A1A3U L 4 .  ? 15.086  -39.810 17.202  0.72 37.15  ? 102 A1A3U C C   1 
HETATM 2212 C C1  . A1A3U L 4 .  ? 16.214  -39.223 18.046  0.72 40.36  ? 102 A1A3U C C1  1 
HETATM 2213 N N   . A1A3U L 4 .  ? 16.011  -39.642 19.446  0.72 41.55  ? 102 A1A3U C N   1 
HETATM 2214 C C2  . A1A3U L 4 .  ? 17.100  -39.335 20.399  0.72 42.68  ? 102 A1A3U C C2  1 
HETATM 2215 C C3  . A1A3U L 4 .  ? 16.774  -39.342 21.847  0.72 43.56  ? 102 A1A3U C C3  1 
HETATM 2216 C C9  . A1A3U L 4 .  ? 15.268  -36.863 18.269  0.72 38.67  ? 102 A1A3U C C9  1 
HETATM 2217 O O   . HOH   M 5 .  ? -2.697  -30.827 -3.989  1.00 55.30  ? 201 HOH   A O   1 
HETATM 2218 O O   . HOH   M 5 .  ? 10.664  -8.827  -12.799 1.00 56.20  ? 202 HOH   A O   1 
HETATM 2219 O O   . HOH   M 5 .  ? 8.838   -32.002 3.922   1.00 58.07  ? 203 HOH   A O   1 
HETATM 2220 O O   . HOH   M 5 .  ? 5.214   -29.057 7.106   1.00 58.40  ? 204 HOH   A O   1 
HETATM 2221 O O   . HOH   M 5 .  ? -4.282  -28.048 5.881   1.00 66.66  ? 205 HOH   A O   1 
HETATM 2222 O O   . HOH   M 5 .  ? -0.138  -34.129 4.815   1.00 58.99  ? 206 HOH   A O   1 
HETATM 2223 O O   . HOH   M 5 .  ? 0.610   -10.945 -15.438 1.00 58.69  ? 207 HOH   A O   1 
HETATM 2224 O O   . HOH   M 5 .  ? 10.756  -29.598 3.431   1.00 47.31  ? 208 HOH   A O   1 
HETATM 2225 O O   . HOH   M 5 .  ? 9.746   -18.770 10.172  1.00 67.13  ? 209 HOH   A O   1 
HETATM 2226 O O   . HOH   M 5 .  ? -5.783  -13.791 -16.758 1.00 58.48  ? 210 HOH   A O   1 
HETATM 2227 O O   . HOH   M 5 .  ? 14.994  -17.332 -19.079 1.00 42.26  ? 211 HOH   A O   1 
HETATM 2228 O O   . HOH   M 5 .  ? 4.023   -10.256 13.499  1.00 66.22  ? 212 HOH   A O   1 
HETATM 2229 O O   . HOH   M 5 .  ? 8.853   -22.740 -9.414  1.00 43.51  ? 213 HOH   A O   1 
HETATM 2230 O O   . HOH   M 5 .  ? -2.749  3.114   -2.033  1.00 42.55  ? 214 HOH   A O   1 
HETATM 2231 O O   . HOH   M 5 .  ? -8.714  -21.156 -0.968  1.00 44.38  ? 215 HOH   A O   1 
HETATM 2232 O O   . HOH   M 5 .  ? -4.832  -21.077 6.130   1.00 42.33  ? 216 HOH   A O   1 
HETATM 2233 O O   . HOH   M 5 .  ? 5.188   -7.241  10.095  1.00 63.87  ? 217 HOH   A O   1 
HETATM 2234 O O   . HOH   M 5 .  ? 8.817   -18.313 -10.852 1.00 34.38  ? 218 HOH   A O   1 
HETATM 2235 O O   . HOH   M 5 .  ? -9.671  -15.361 10.844  1.00 60.32  ? 219 HOH   A O   1 
HETATM 2236 O O   . HOH   M 5 .  ? -8.452  -16.801 2.538   1.00 49.27  ? 220 HOH   A O   1 
HETATM 2237 O O   . HOH   M 5 .  ? -4.201  -11.048 6.665   1.00 43.67  ? 221 HOH   A O   1 
HETATM 2238 O O   . HOH   M 5 .  ? 6.688   -10.686 -12.135 1.00 39.51  ? 222 HOH   A O   1 
HETATM 2239 O O   . HOH   M 5 .  ? 11.089  -11.937 5.765   1.00 36.90  ? 223 HOH   A O   1 
HETATM 2240 O O   . HOH   M 5 .  ? 10.448  -5.300  -7.775  1.00 32.10  ? 224 HOH   A O   1 
HETATM 2241 O O   . HOH   M 5 .  ? 4.166   -3.575  -3.289  1.00 34.18  ? 225 HOH   A O   1 
HETATM 2242 O O   . HOH   M 5 .  ? -2.898  -11.842 14.088  1.00 51.40  ? 226 HOH   A O   1 
HETATM 2243 O O   . HOH   M 5 .  ? 15.385  -24.353 2.310   1.00 42.28  ? 227 HOH   A O   1 
HETATM 2244 O O   . HOH   M 5 .  ? -1.070  -28.988 10.168  1.00 56.47  ? 228 HOH   A O   1 
HETATM 2245 O O   . HOH   M 5 .  ? 4.171   -7.889  1.098   1.00 34.71  ? 229 HOH   A O   1 
HETATM 2246 O O   . HOH   M 5 .  ? -1.345  -5.627  -7.315  1.00 32.08  ? 230 HOH   A O   1 
HETATM 2247 O O   . HOH   M 5 .  ? -5.973  -19.533 -5.681  1.00 37.61  ? 231 HOH   A O   1 
HETATM 2248 O O   . HOH   M 5 .  ? -6.957  -5.349  9.173   1.00 36.99  ? 232 HOH   A O   1 
HETATM 2249 O O   . HOH   M 5 .  ? -6.911  -22.117 -5.811  1.00 52.84  ? 233 HOH   A O   1 
HETATM 2250 O O   . HOH   M 5 .  ? 9.264   -30.503 9.691   1.00 36.64  ? 234 HOH   A O   1 
HETATM 2251 O O   . HOH   M 5 .  ? 1.548   0.598   -7.375  1.00 44.00  ? 235 HOH   A O   1 
HETATM 2252 O O   . HOH   M 5 .  ? -6.402  -11.359 -11.133 1.00 41.06  ? 236 HOH   A O   1 
HETATM 2253 O O   . HOH   M 5 .  ? -7.326  -20.598 -3.670  1.00 73.52  ? 237 HOH   A O   1 
HETATM 2254 O O   . HOH   M 5 .  ? 8.086   -17.842 -15.871 1.00 42.89  ? 238 HOH   A O   1 
HETATM 2255 O O   . HOH   M 5 .  ? 12.519  -11.819 8.048   1.00 65.64  ? 239 HOH   A O   1 
HETATM 2256 O O   . HOH   M 5 .  ? 15.562  -12.257 -5.348  1.00 36.36  ? 240 HOH   A O   1 
HETATM 2257 O O   . HOH   M 5 .  ? -2.179  -22.012 -0.440  1.00 27.38  ? 241 HOH   A O   1 
HETATM 2258 O O   . HOH   M 5 .  ? 11.063  -12.337 -6.157  1.00 28.31  ? 242 HOH   A O   1 
HETATM 2259 O O   . HOH   M 5 .  ? 9.671   -13.100 9.730   1.00 44.28  ? 243 HOH   A O   1 
HETATM 2260 O O   . HOH   M 5 .  ? -8.299  -15.902 -0.983  1.00 34.78  ? 244 HOH   A O   1 
HETATM 2261 O O   . HOH   M 5 .  ? -8.335  -17.012 6.635   1.00 43.34  ? 245 HOH   A O   1 
HETATM 2262 O O   . HOH   M 5 .  ? 0.918   -18.074 -18.967 1.00 53.09  ? 246 HOH   A O   1 
HETATM 2263 O O   . HOH   M 5 .  ? -5.983  -15.832 -8.002  1.00 29.20  ? 247 HOH   A O   1 
HETATM 2264 O O   . HOH   M 5 .  ? -1.187  -20.826 7.106   1.00 39.83  ? 248 HOH   A O   1 
HETATM 2265 O O   . HOH   M 5 .  ? 12.684  -9.210  -7.199  1.00 50.36  ? 249 HOH   A O   1 
HETATM 2266 O O   . HOH   M 5 .  ? 16.926  -12.861 1.399   1.00 22.76  ? 250 HOH   A O   1 
HETATM 2267 O O   . HOH   M 5 .  ? 12.982  -28.397 -4.209  1.00 63.69  ? 251 HOH   A O   1 
HETATM 2268 O O   . HOH   M 5 .  ? 10.850  -23.474 10.093  1.00 42.94  ? 252 HOH   A O   1 
HETATM 2269 O O   . HOH   M 5 .  ? 12.105  -15.756 -12.132 1.00 52.10  ? 253 HOH   A O   1 
HETATM 2270 O O   . HOH   M 5 .  ? 7.561   -1.857  -0.565  1.00 63.83  ? 254 HOH   A O   1 
HETATM 2271 O O   . HOH   M 5 .  ? 1.659   -4.658  -10.270 1.00 37.85  ? 255 HOH   A O   1 
HETATM 2272 O O   . HOH   M 5 .  ? -4.167  -8.201  10.059  1.00 51.74  ? 256 HOH   A O   1 
HETATM 2273 O O   . HOH   M 5 .  ? -1.796  -7.395  11.431  1.00 48.84  ? 257 HOH   A O   1 
HETATM 2274 O O   . HOH   M 5 .  ? 2.494   -10.227 -13.492 1.00 54.04  ? 258 HOH   A O   1 
HETATM 2275 O O   . HOH   M 5 .  ? 7.430   -7.899  1.262   1.00 31.78  ? 259 HOH   A O   1 
HETATM 2276 O O   . HOH   M 5 .  ? -6.445  -12.753 6.621   1.00 40.47  ? 260 HOH   A O   1 
HETATM 2277 O O   . HOH   M 5 .  ? -0.161  -23.108 9.601   1.00 50.99  ? 261 HOH   A O   1 
HETATM 2278 O O   . HOH   M 5 .  ? 16.856  -18.271 -9.705  1.00 46.10  ? 262 HOH   A O   1 
HETATM 2279 O O   . HOH   M 5 .  ? 15.199  -28.244 -0.191  1.00 53.14  ? 263 HOH   A O   1 
HETATM 2280 O O   . HOH   M 5 .  ? 2.827   -29.649 -0.213  1.00 41.98  ? 264 HOH   A O   1 
HETATM 2281 O O   . HOH   M 5 .  ? 12.949  -12.039 -4.222  1.00 24.26  ? 265 HOH   A O   1 
HETATM 2282 O O   . HOH   M 5 .  ? -0.845  -20.335 11.308  1.00 59.21  ? 266 HOH   A O   1 
HETATM 2283 O O   . HOH   M 5 .  ? 16.275  -11.943 -16.879 1.00 46.54  ? 267 HOH   A O   1 
HETATM 2284 O O   . HOH   M 5 .  ? 2.187   -25.356 -10.225 1.00 47.52  ? 268 HOH   A O   1 
HETATM 2285 O O   . HOH   M 5 .  ? 2.281   -6.248  5.509   1.00 43.28  ? 269 HOH   A O   1 
HETATM 2286 O O   . HOH   M 5 .  ? 10.906  -6.065  -3.876  1.00 47.28  ? 270 HOH   A O   1 
HETATM 2287 O O   . HOH   M 5 .  ? -4.987  -25.770 -5.613  1.00 41.71  ? 271 HOH   A O   1 
HETATM 2288 O O   . HOH   M 5 .  ? 9.387   -6.076  -1.573  1.00 36.89  ? 272 HOH   A O   1 
HETATM 2289 O O   . HOH   M 5 .  ? 1.448   -10.412 11.722  1.00 36.21  ? 273 HOH   A O   1 
HETATM 2290 O O   . HOH   M 5 .  ? 10.931  -16.714 -14.960 1.00 48.50  ? 274 HOH   A O   1 
HETATM 2291 O O   . HOH   M 5 .  ? -1.647  -11.727 11.286  1.00 52.51  ? 275 HOH   A O   1 
HETATM 2292 O O   . HOH   M 5 .  ? 1.260   -28.944 -4.403  1.00 59.29  ? 276 HOH   A O   1 
HETATM 2293 O O   . HOH   M 5 .  ? 12.277  -13.198 -8.532  1.00 36.81  ? 277 HOH   A O   1 
HETATM 2294 O O   . HOH   M 5 .  ? 13.918  -29.556 4.215   1.00 63.60  ? 278 HOH   A O   1 
HETATM 2295 O O   . HOH   M 5 .  ? 4.816   -7.518  4.110   1.00 37.95  ? 279 HOH   A O   1 
HETATM 2296 O O   . HOH   M 5 .  ? 9.815   -27.843 -6.943  1.00 61.29  ? 280 HOH   A O   1 
HETATM 2297 O O   . HOH   M 5 .  ? 5.881   -5.943  0.465   1.00 52.16  ? 281 HOH   A O   1 
HETATM 2298 O O   . HOH   M 5 .  ? -5.931  -17.454 -9.884  1.00 51.76  ? 282 HOH   A O   1 
HETATM 2299 O O   . HOH   M 5 .  ? 8.511   -16.449 -13.043 1.00 46.89  ? 283 HOH   A O   1 
HETATM 2300 O O   . HOH   M 5 .  ? 6.254   -16.211 -14.850 1.00 56.69  ? 284 HOH   A O   1 
HETATM 2301 O O   . HOH   M 5 .  ? 9.458   -20.411 -18.404 1.00 42.19  ? 285 HOH   A O   1 
HETATM 2302 O O   . HOH   M 5 .  ? 7.754   -17.644 8.738   1.00 48.89  ? 286 HOH   A O   1 
HETATM 2303 O O   . HOH   M 5 .  ? 8.019   -8.241  4.554   1.00 41.63  ? 287 HOH   A O   1 
HETATM 2304 O O   . HOH   M 5 .  ? 3.710   -34.853 4.213   1.00 87.88  ? 288 HOH   A O   1 
HETATM 2305 O O   . HOH   M 5 .  ? 8.709   -9.352  -13.797 1.00 40.24  ? 289 HOH   A O   1 
HETATM 2306 O O   . HOH   M 5 .  ? 10.801  -7.769  0.402   1.00 28.19  ? 290 HOH   A O   1 
HETATM 2307 O O   . HOH   M 5 .  ? 20.993  -16.722 -3.408  1.00 30.89  ? 291 HOH   A O   1 
HETATM 2308 O O   . HOH   M 5 .  ? 8.897   -9.813  6.125   1.00 48.22  ? 292 HOH   A O   1 
HETATM 2309 O O   . HOH   M 5 .  ? 21.979  -16.745 -0.394  1.00 45.61  ? 293 HOH   A O   1 
HETATM 2310 O O   . HOH   M 5 .  ? -7.609  -11.520 -7.981  1.00 32.34  ? 294 HOH   A O   1 
HETATM 2311 O O   . HOH   M 5 .  ? -8.797  -19.487 -3.377  1.00 44.37  ? 295 HOH   A O   1 
HETATM 2312 O O   . HOH   M 5 .  ? 16.548  -28.969 2.191   1.00 53.81  ? 296 HOH   A O   1 
HETATM 2313 O O   . HOH   M 5 .  ? 0.954   -25.089 -6.041  1.00 48.44  ? 297 HOH   A O   1 
HETATM 2314 O O   . HOH   M 5 .  ? -6.287  -26.622 3.541   1.00 47.48  ? 298 HOH   A O   1 
HETATM 2315 O O   . HOH   M 5 .  ? 6.297   -30.610 -2.788  1.00 61.96  ? 299 HOH   A O   1 
HETATM 2316 O O   . HOH   M 5 .  ? 1.865   -24.742 15.336  1.00 70.98  ? 300 HOH   A O   1 
HETATM 2317 O O   . HOH   M 5 .  ? -0.707  -3.619  -10.955 1.00 59.65  ? 301 HOH   A O   1 
HETATM 2318 O O   . HOH   M 5 .  ? 16.292  -13.450 10.919  1.00 52.72  ? 302 HOH   A O   1 
HETATM 2319 O O   . HOH   M 5 .  ? -7.011  -13.211 -11.732 1.00 50.25  ? 303 HOH   A O   1 
HETATM 2320 O O   . HOH   M 5 .  ? -11.522 -16.853 -3.313  1.00 67.65  ? 304 HOH   A O   1 
HETATM 2321 O O   . HOH   M 5 .  ? -4.437  -26.776 7.484   1.00 59.92  ? 305 HOH   A O   1 
HETATM 2322 O O   . HOH   M 5 .  ? -7.497  -14.241 -9.348  1.00 48.55  ? 306 HOH   A O   1 
HETATM 2323 O O   . HOH   M 5 .  ? -7.626  -19.374 7.250   1.00 62.49  ? 307 HOH   A O   1 
HETATM 2324 O O   . HOH   M 5 .  ? -4.048  -11.262 9.977   1.00 50.70  ? 308 HOH   A O   1 
HETATM 2325 O O   . HOH   M 5 .  ? 4.655   -6.954  -11.091 1.00 52.68  ? 309 HOH   A O   1 
HETATM 2326 O O   . HOH   M 5 .  ? 10.629  -1.833  -1.406  1.00 64.58  ? 310 HOH   A O   1 
HETATM 2327 O O   . HOH   M 5 .  ? -11.299 -13.143 -2.656  1.00 68.65  ? 311 HOH   A O   1 
HETATM 2328 O O   . HOH   M 5 .  ? -10.370 -28.692 -1.535  1.00 58.82  ? 312 HOH   A O   1 
HETATM 2329 O O   . HOH   M 5 .  ? -6.673  -23.197 5.351   1.00 52.27  ? 313 HOH   A O   1 
HETATM 2330 O O   . HOH   M 5 .  ? 4.339   -9.798  -11.306 1.00 56.70  ? 314 HOH   A O   1 
HETATM 2331 O O   . HOH   M 5 .  ? 12.369  -18.743 -15.257 1.00 40.95  ? 315 HOH   A O   1 
HETATM 2332 O O   . HOH   M 5 .  ? 8.593   -22.586 -19.062 1.00 67.47  ? 316 HOH   A O   1 
HETATM 2333 O O   . HOH   M 5 .  ? -5.352  -20.989 -8.102  1.00 58.93  ? 317 HOH   A O   1 
HETATM 2334 O O   . HOH   M 5 .  ? 3.936   -3.294  2.119   1.00 63.81  ? 318 HOH   A O   1 
HETATM 2335 O O   . HOH   M 5 .  ? -5.645  -19.988 17.561  1.00 65.41  ? 319 HOH   A O   1 
HETATM 2336 O O   . HOH   N 5 .  ? 31.149  -8.492  -30.184 1.00 55.51  ? 201 HOH   B O   1 
HETATM 2337 O O   . HOH   N 5 .  ? 27.833  -8.121  -28.865 1.00 51.83  ? 202 HOH   B O   1 
HETATM 2338 O O   . HOH   N 5 .  ? 26.102  -4.969  -33.444 1.00 49.76  ? 203 HOH   B O   1 
HETATM 2339 O O   . HOH   N 5 .  ? 12.680  -26.068 -37.261 1.00 48.17  ? 204 HOH   B O   1 
HETATM 2340 O O   . HOH   N 5 .  ? 25.055  -5.309  -29.778 1.00 38.44  ? 205 HOH   B O   1 
HETATM 2341 O O   . HOH   N 5 .  ? 10.012  -11.571 -38.035 1.00 53.80  ? 206 HOH   B O   1 
HETATM 2342 O O   . HOH   N 5 .  ? 6.537   -12.426 -26.036 1.00 36.16  ? 207 HOH   B O   1 
HETATM 2343 O O   . HOH   N 5 .  ? 30.701  -12.759 -45.736 1.00 52.42  ? 208 HOH   B O   1 
HETATM 2344 O O   . HOH   N 5 .  ? 30.384  -19.782 -40.240 1.00 35.31  ? 209 HOH   B O   1 
HETATM 2345 O O   . HOH   N 5 .  ? 24.407  -1.902  -36.251 1.00 61.36  ? 210 HOH   B O   1 
HETATM 2346 O O   . HOH   N 5 .  ? 26.067  -0.489  -28.894 1.00 45.28  ? 211 HOH   B O   1 
HETATM 2347 O O   . HOH   N 5 .  ? 20.106  -22.280 -23.299 1.00 48.25  ? 212 HOH   B O   1 
HETATM 2348 O O   . HOH   N 5 .  ? 34.954  -23.407 -30.092 1.00 52.62  ? 213 HOH   B O   1 
HETATM 2349 O O   . HOH   N 5 .  ? 17.205  -9.708  -43.781 1.00 45.40  ? 214 HOH   B O   1 
HETATM 2350 O O   . HOH   N 5 .  ? 28.076  -17.334 -24.862 1.00 46.98  ? 215 HOH   B O   1 
HETATM 2351 O O   . HOH   N 5 .  ? 23.630  -4.308  -36.835 1.00 32.91  ? 216 HOH   B O   1 
HETATM 2352 O O   . HOH   N 5 .  ? 16.644  -19.438 -28.808 1.00 26.06  ? 217 HOH   B O   1 
HETATM 2353 O O   . HOH   N 5 .  ? 32.392  -18.714 -42.040 1.00 63.25  ? 218 HOH   B O   1 
HETATM 2354 O O   . HOH   N 5 .  ? 21.729  -24.356 -26.368 1.00 51.80  ? 219 HOH   B O   1 
HETATM 2355 O O   . HOH   N 5 .  ? 6.562   -7.577  -32.679 1.00 54.16  ? 220 HOH   B O   1 
HETATM 2356 O O   . HOH   N 5 .  ? 25.791  -6.117  -35.679 1.00 42.19  ? 221 HOH   B O   1 
HETATM 2357 O O   . HOH   N 5 .  ? 26.088  -23.179 -30.998 1.00 35.30  ? 222 HOH   B O   1 
HETATM 2358 O O   . HOH   N 5 .  ? 18.215  -0.662  -38.242 1.00 31.55  ? 223 HOH   B O   1 
HETATM 2359 O O   . HOH   N 5 .  ? 17.705  -28.446 -27.349 1.00 47.60  ? 224 HOH   B O   1 
HETATM 2360 O O   . HOH   N 5 .  ? 20.995  -13.569 -42.557 1.00 38.17  ? 225 HOH   B O   1 
HETATM 2361 O O   . HOH   N 5 .  ? 13.257  -4.763  -41.696 1.00 55.44  ? 226 HOH   B O   1 
HETATM 2362 O O   . HOH   N 5 .  ? 3.290   -9.229  -26.400 1.00 59.67  ? 227 HOH   B O   1 
HETATM 2363 O O   . HOH   N 5 .  ? 10.532  -19.021 -32.983 1.00 30.41  ? 228 HOH   B O   1 
HETATM 2364 O O   . HOH   N 5 .  ? 10.266  -19.622 -43.246 1.00 50.89  ? 229 HOH   B O   1 
HETATM 2365 O O   . HOH   N 5 .  ? 10.277  -17.138 -44.166 1.00 54.36  ? 230 HOH   B O   1 
HETATM 2366 O O   . HOH   N 5 .  ? 15.704  -26.378 -34.736 1.00 40.95  ? 231 HOH   B O   1 
HETATM 2367 O O   . HOH   N 5 .  ? 19.955  -25.858 -34.118 1.00 42.68  ? 232 HOH   B O   1 
HETATM 2368 O O   . HOH   N 5 .  ? 20.400  -3.325  -23.127 1.00 74.86  ? 233 HOH   B O   1 
HETATM 2369 O O   . HOH   N 5 .  ? 14.549  -6.402  -40.991 1.00 40.34  ? 234 HOH   B O   1 
HETATM 2370 O O   . HOH   N 5 .  ? 23.559  -2.584  -28.970 1.00 38.08  ? 235 HOH   B O   1 
HETATM 2371 O O   . HOH   N 5 .  ? 12.888  -22.612 -20.642 1.00 53.24  ? 236 HOH   B O   1 
HETATM 2372 O O   . HOH   N 5 .  ? 22.034  3.513   -32.571 1.00 47.63  ? 237 HOH   B O   1 
HETATM 2373 O O   . HOH   N 5 .  ? 18.098  -26.116 -28.850 1.00 44.92  ? 238 HOH   B O   1 
HETATM 2374 O O   . HOH   N 5 .  ? 7.661   -18.528 -31.772 1.00 49.67  ? 239 HOH   B O   1 
HETATM 2375 O O   . HOH   N 5 .  ? 22.607  -23.298 -28.646 1.00 41.97  ? 240 HOH   B O   1 
HETATM 2376 O O   . HOH   N 5 .  ? 20.663  -10.193 -42.776 1.00 31.75  ? 241 HOH   B O   1 
HETATM 2377 O O   . HOH   N 5 .  ? 19.072  -19.764 -19.331 1.00 53.71  ? 242 HOH   B O   1 
HETATM 2378 O O   . HOH   N 5 .  ? 8.488   -27.934 -37.749 1.00 66.75  ? 243 HOH   B O   1 
HETATM 2379 O O   . HOH   N 5 .  ? 25.098  -6.962  -42.441 1.00 55.09  ? 244 HOH   B O   1 
HETATM 2380 O O   . HOH   N 5 .  ? 1.818   -12.927 -28.261 1.00 50.56  ? 245 HOH   B O   1 
HETATM 2381 O O   . HOH   N 5 .  ? 7.130   -19.065 -34.924 1.00 51.03  ? 246 HOH   B O   1 
HETATM 2382 O O   . HOH   N 5 .  ? 7.380   -8.160  -20.845 1.00 49.45  ? 247 HOH   B O   1 
HETATM 2383 O O   . HOH   N 5 .  ? 21.398  -6.540  -42.448 1.00 41.80  ? 248 HOH   B O   1 
HETATM 2384 O O   . HOH   N 5 .  ? 14.556  -24.685 -40.507 1.00 46.80  ? 249 HOH   B O   1 
HETATM 2385 O O   . HOH   N 5 .  ? 8.477   -8.658  -16.425 1.00 48.32  ? 250 HOH   B O   1 
HETATM 2386 O O   . HOH   N 5 .  ? 6.586   -20.784 -24.979 1.00 53.54  ? 251 HOH   B O   1 
HETATM 2387 O O   . HOH   N 5 .  ? 17.987  -15.952 -45.595 1.00 42.50  ? 252 HOH   B O   1 
HETATM 2388 O O   . HOH   N 5 .  ? 18.071  -23.419 -20.670 1.00 70.80  ? 253 HOH   B O   1 
HETATM 2389 O O   . HOH   N 5 .  ? 10.450  -21.804 -32.811 1.00 34.21  ? 254 HOH   B O   1 
HETATM 2390 O O   . HOH   N 5 .  ? 24.332  0.948   -37.155 1.00 61.88  ? 255 HOH   B O   1 
HETATM 2391 O O   . HOH   N 5 .  ? 25.345  -27.084 -28.438 1.00 56.32  ? 256 HOH   B O   1 
HETATM 2392 O O   . HOH   N 5 .  ? 17.982  -3.640  -21.940 1.00 50.36  ? 257 HOH   B O   1 
HETATM 2393 O O   . HOH   N 5 .  ? 27.225  -10.323 -29.295 1.00 54.02  ? 258 HOH   B O   1 
HETATM 2394 O O   . HOH   N 5 .  ? 24.114  -11.300 -21.896 1.00 44.89  ? 259 HOH   B O   1 
HETATM 2395 O O   . HOH   N 5 .  ? 7.543   -12.745 -39.129 1.00 60.97  ? 260 HOH   B O   1 
HETATM 2396 O O   . HOH   N 5 .  ? 32.045  -21.273 -38.202 1.00 53.37  ? 261 HOH   B O   1 
HETATM 2397 O O   . HOH   N 5 .  ? 27.979  -24.906 -35.048 1.00 36.93  ? 262 HOH   B O   1 
HETATM 2398 O O   . HOH   N 5 .  ? 18.511  4.342   -34.217 1.00 41.91  ? 263 HOH   B O   1 
HETATM 2399 O O   . HOH   N 5 .  ? 4.783   -19.585 -25.761 1.00 48.85  ? 264 HOH   B O   1 
HETATM 2400 O O   . HOH   N 5 .  ? 20.389  3.620   -32.925 1.00 37.39  ? 265 HOH   B O   1 
HETATM 2401 O O   . HOH   N 5 .  ? 17.406  -0.424  -25.464 1.00 54.73  ? 266 HOH   B O   1 
HETATM 2402 O O   . HOH   N 5 .  ? 19.769  -27.147 -30.782 1.00 60.82  ? 267 HOH   B O   1 
HETATM 2403 O O   . HOH   N 5 .  ? 27.020  -22.855 -28.358 1.00 51.65  ? 268 HOH   B O   1 
HETATM 2404 O O   . HOH   N 5 .  ? 15.151  -8.245  -42.988 1.00 53.06  ? 269 HOH   B O   1 
HETATM 2405 O O   . HOH   N 5 .  ? 39.376  -13.144 -38.750 1.00 72.18  ? 270 HOH   B O   1 
HETATM 2406 O O   . HOH   N 5 .  ? 12.877  -20.496 -19.658 1.00 57.75  ? 271 HOH   B O   1 
HETATM 2407 O O   . HOH   N 5 .  ? 28.023  -4.627  -36.503 1.00 52.56  ? 272 HOH   B O   1 
HETATM 2408 O O   . HOH   N 5 .  ? 16.667  1.570   -29.787 1.00 57.28  ? 273 HOH   B O   1 
HETATM 2409 O O   . HOH   N 5 .  ? 9.613   -6.438  -40.867 1.00 46.19  ? 274 HOH   B O   1 
HETATM 2410 O O   . HOH   N 5 .  ? 20.591  -20.168 -21.820 1.00 43.94  ? 275 HOH   B O   1 
HETATM 2411 O O   . HOH   N 5 .  ? 22.355  -23.523 -24.066 1.00 55.98  ? 276 HOH   B O   1 
HETATM 2412 O O   . HOH   N 5 .  ? 31.559  -11.900 -36.777 1.00 61.83  ? 277 HOH   B O   1 
HETATM 2413 O O   . HOH   N 5 .  ? 24.511  -4.281  -27.680 1.00 53.91  ? 278 HOH   B O   1 
HETATM 2414 O O   . HOH   N 5 .  ? 15.056  -22.091 -41.702 1.00 62.72  ? 279 HOH   B O   1 
HETATM 2415 O O   . HOH   N 5 .  ? 7.153   -9.832  -18.500 1.00 51.44  ? 280 HOH   B O   1 
HETATM 2416 O O   . HOH   N 5 .  ? 22.298  -29.437 -35.432 1.00 56.37  ? 281 HOH   B O   1 
HETATM 2417 O O   . HOH   O 5 .  ? 20.428  -19.708 29.903  1.00 61.49  ? 201 HOH   C O   1 
HETATM 2418 O O   . HOH   O 5 .  ? 26.354  -37.495 9.724   1.00 43.95  ? 202 HOH   C O   1 
HETATM 2419 O O   . HOH   O 5 .  ? 12.263  -28.286 28.223  1.00 62.37  ? 203 HOH   C O   1 
HETATM 2420 O O   . HOH   O 5 .  ? 14.584  -21.974 27.887  1.00 80.69  ? 204 HOH   C O   1 
HETATM 2421 O O   . HOH   O 5 .  ? 16.941  -40.225 11.320  1.00 65.18  ? 205 HOH   C O   1 
HETATM 2422 O O   . HOH   O 5 .  ? 5.443   -26.566 16.700  1.00 48.77  ? 206 HOH   C O   1 
HETATM 2423 O O   . HOH   O 5 .  ? 26.144  -38.979 12.667  1.00 41.70  ? 207 HOH   C O   1 
HETATM 2424 O O   . HOH   O 5 .  ? 7.219   -31.415 12.355  1.00 41.62  ? 208 HOH   C O   1 
HETATM 2425 O O   . HOH   O 5 .  ? 15.902  -24.154 29.230  1.00 56.81  ? 209 HOH   C O   1 
HETATM 2426 O O   . HOH   O 5 .  ? 28.030  -37.052 15.908  1.00 41.80  ? 210 HOH   C O   1 
HETATM 2427 O O   . HOH   O 5 .  ? 9.180   -30.172 11.122  1.00 47.79  ? 211 HOH   C O   1 
HETATM 2428 O O   . HOH   O 5 .  ? 20.282  -35.707 8.068   1.00 47.21  ? 212 HOH   C O   1 
HETATM 2429 O O   . HOH   O 5 .  ? 17.490  -17.131 25.060  1.00 68.01  ? 213 HOH   C O   1 
HETATM 2430 O O   . HOH   O 5 .  ? 12.328  -31.409 8.283   1.00 49.23  ? 214 HOH   C O   1 
HETATM 2431 O O   . HOH   O 5 .  ? 24.893  -31.251 10.755  1.00 37.20  ? 215 HOH   C O   1 
HETATM 2432 O O   . HOH   O 5 .  ? 17.646  -16.860 14.843  1.00 54.34  ? 216 HOH   C O   1 
HETATM 2433 O O   . HOH   O 5 .  ? 14.762  -21.031 12.429  1.00 47.42  ? 217 HOH   C O   1 
HETATM 2434 O O   . HOH   O 5 .  ? 21.899  -28.358 11.142  1.00 34.11  ? 218 HOH   C O   1 
HETATM 2435 O O   . HOH   O 5 .  ? 19.603  -41.751 12.098  1.00 33.35  ? 219 HOH   C O   1 
HETATM 2436 O O   . HOH   O 5 .  ? 29.830  -31.477 15.733  1.00 64.92  ? 220 HOH   C O   1 
HETATM 2437 O O   . HOH   O 5 .  ? 9.550   -37.166 18.840  1.00 80.71  ? 221 HOH   C O   1 
HETATM 2438 O O   . HOH   O 5 .  ? 23.293  -20.516 24.003  1.00 60.40  ? 222 HOH   C O   1 
HETATM 2439 O O   . HOH   O 5 .  ? 18.918  -19.997 10.638  1.00 42.40  ? 223 HOH   C O   1 
HETATM 2440 O O   . HOH   O 5 .  ? 19.577  -40.846 38.696  1.00 82.88  ? 224 HOH   C O   1 
HETATM 2441 O O   . HOH   O 5 .  ? 25.379  -19.665 6.197   1.00 36.97  ? 225 HOH   C O   1 
HETATM 2442 O O   . HOH   O 5 .  ? 21.738  -34.203 16.632  1.00 27.73  ? 226 HOH   C O   1 
HETATM 2443 O O   . HOH   O 5 .  ? 27.241  -15.277 12.618  1.00 50.72  ? 227 HOH   C O   1 
HETATM 2444 O O   . HOH   O 5 .  ? 30.051  -29.112 11.993  1.00 51.91  ? 228 HOH   C O   1 
HETATM 2445 O O   . HOH   O 5 .  ? 31.332  -42.879 12.014  1.00 52.72  ? 229 HOH   C O   1 
HETATM 2446 O O   . HOH   O 5 .  ? 15.832  -17.522 19.430  1.00 52.43  ? 230 HOH   C O   1 
HETATM 2447 O O   . HOH   O 5 .  ? 25.511  -17.627 13.721  1.00 49.75  ? 231 HOH   C O   1 
HETATM 2448 O O   . HOH   O 5 .  ? 6.626   -17.849 11.061  1.00 38.76  ? 232 HOH   C O   1 
HETATM 2449 O O   . HOH   O 5 .  ? 19.070  -13.176 16.584  1.00 63.74  ? 233 HOH   C O   1 
HETATM 2450 O O   . HOH   O 5 .  ? 29.936  -39.555 31.293  1.00 34.93  ? 234 HOH   C O   1 
HETATM 2451 O O   . HOH   O 5 .  ? 22.734  -41.413 18.591  1.00 48.12  ? 235 HOH   C O   1 
HETATM 2452 O O   . HOH   O 5 .  ? 20.427  -28.654 8.572   1.00 41.27  ? 236 HOH   C O   1 
HETATM 2453 O O   . HOH   O 5 .  ? 31.168  -39.668 27.075  1.00 47.47  ? 237 HOH   C O   1 
HETATM 2454 O O   . HOH   O 5 .  ? 20.590  -39.754 26.496  1.00 41.75  ? 238 HOH   C O   1 
HETATM 2455 O O   . HOH   O 5 .  ? 27.461  -37.200 24.957  1.00 53.21  ? 239 HOH   C O   1 
HETATM 2456 O O   . HOH   O 5 .  ? 22.774  -18.312 21.684  1.00 60.04  ? 240 HOH   C O   1 
HETATM 2457 O O   . HOH   O 5 .  ? 13.474  -37.174 14.108  1.00 49.19  ? 241 HOH   C O   1 
HETATM 2458 O O   . HOH   O 5 .  ? 27.859  -36.438 18.636  1.00 47.12  ? 242 HOH   C O   1 
HETATM 2459 O O   . HOH   O 5 .  ? 9.218   -18.741 23.934  1.00 59.84  ? 243 HOH   C O   1 
HETATM 2460 O O   . HOH   O 5 .  ? 25.818  -33.490 34.958  1.00 60.90  ? 244 HOH   C O   1 
HETATM 2461 O O   . HOH   O 5 .  ? 30.533  -17.091 9.869   1.00 51.57  ? 245 HOH   C O   1 
HETATM 2462 O O   . HOH   O 5 .  ? 2.441   -28.258 14.453  1.00 57.58  ? 246 HOH   C O   1 
HETATM 2463 O O   . HOH   O 5 .  ? 33.447  -24.590 31.685  1.00 63.13  ? 247 HOH   C O   1 
HETATM 2464 O O   . HOH   O 5 .  ? 25.314  -17.906 21.020  1.00 60.21  ? 248 HOH   C O   1 
HETATM 2465 O O   . HOH   O 5 .  ? 30.773  -35.405 28.282  1.00 57.33  ? 249 HOH   C O   1 
HETATM 2466 O O   . HOH   O 5 .  ? 25.189  -39.625 20.204  1.00 38.78  ? 250 HOH   C O   1 
HETATM 2467 O O   . HOH   O 5 .  ? 30.516  -33.521 35.748  1.00 58.71  ? 251 HOH   C O   1 
HETATM 2468 O O   . HOH   O 5 .  ? 30.822  -43.294 15.888  1.00 66.98  ? 252 HOH   C O   1 
HETATM 2469 O O   . HOH   O 5 .  ? 30.924  -24.820 31.291  1.00 64.75  ? 253 HOH   C O   1 
HETATM 2470 O O   . HOH   O 5 .  ? 16.930  -21.083 12.851  1.00 54.83  ? 254 HOH   C O   1 
HETATM 2471 O O   . HOH   O 5 .  ? 31.946  -33.829 25.702  1.00 51.60  ? 255 HOH   C O   1 
HETATM 2472 O O   . HOH   O 5 .  ? 19.558  -18.754 25.039  1.00 61.31  ? 256 HOH   C O   1 
HETATM 2473 O O   . HOH   O 5 .  ? 18.944  -26.601 3.152   1.00 58.78  ? 257 HOH   C O   1 
HETATM 2474 O O   . HOH   O 5 .  ? 29.766  -32.588 18.202  1.00 47.40  ? 258 HOH   C O   1 
HETATM 2475 O O   . HOH   O 5 .  ? 20.691  -29.696 4.640   1.00 52.79  ? 259 HOH   C O   1 
HETATM 2476 O O   . HOH   O 5 .  ? 13.968  -38.885 9.962   1.00 58.86  ? 260 HOH   C O   1 
HETATM 2477 O O   . HOH   O 5 .  ? 12.511  -38.734 24.461  1.00 51.74  ? 261 HOH   C O   1 
HETATM 2478 O O   . HOH   O 5 .  ? 20.129  -12.746 13.386  1.00 48.52  ? 262 HOH   C O   1 
HETATM 2479 O O   . HOH   O 5 .  ? 29.675  -33.227 13.806  1.00 64.25  ? 263 HOH   C O   1 
HETATM 2480 O O   . HOH   O 5 .  ? 14.692  -41.880 14.337  1.00 60.42  ? 264 HOH   C O   1 
HETATM 2481 O O   . HOH   O 5 .  ? 27.731  -39.136 24.303  1.00 56.43  ? 265 HOH   C O   1 
HETATM 2482 O O   . HOH   O 5 .  ? 21.998  -13.333 13.213  1.00 49.44  ? 266 HOH   C O   1 
HETATM 2483 O O   . HOH   O 5 .  ? 5.183   -24.261 18.656  1.00 56.67  ? 267 HOH   C O   1 
HETATM 2484 O O   . HOH   O 5 .  ? 17.139  -36.559 29.544  1.00 60.05  ? 268 HOH   C O   1 
HETATM 2485 O O   . HOH   O 5 .  ? 11.778  -20.910 10.911  1.00 42.61  ? 269 HOH   C O   1 
HETATM 2486 O O   . HOH   O 5 .  ? 37.464  -24.337 26.131  1.00 63.71  ? 270 HOH   C O   1 
HETATM 2487 O O   . HOH   O 5 .  ? 29.005  -41.523 27.157  1.00 43.90  ? 271 HOH   C O   1 
HETATM 2488 O O   . HOH   O 5 .  ? 3.216   -31.100 25.807  1.00 54.45  ? 272 HOH   C O   1 
HETATM 2489 O O   . HOH   O 5 .  ? 14.848  -39.489 7.267   1.00 48.33  ? 273 HOH   C O   1 
HETATM 2490 O O   . HOH   O 5 .  ? 23.569  -15.790 11.921  1.00 48.97  ? 274 HOH   C O   1 
HETATM 2491 O O   . HOH   O 5 .  ? 9.781   -37.928 24.523  1.00 57.80  ? 275 HOH   C O   1 
HETATM 2492 O O   . HOH   O 5 .  ? 32.016  -38.886 29.740  1.00 54.57  ? 276 HOH   C O   1 
HETATM 2493 O O   . HOH   O 5 .  ? 29.687  -18.075 28.616  1.00 54.13  ? 277 HOH   C O   1 
HETATM 2494 O O   . HOH   O 5 .  ? 28.452  -41.271 29.724  1.00 47.61  ? 278 HOH   C O   1 
HETATM 2495 O O   . HOH   O 5 .  ? 4.119   -42.222 14.201  1.00 57.82  ? 279 HOH   C O   1 
HETATM 2496 O O   . HOH   O 5 .  ? 35.202  -31.249 20.223  1.00 59.30  ? 280 HOH   C O   1 
HETATM 2497 O O   . HOH   O 5 .  ? 30.403  -23.010 18.101  1.00 51.62  ? 281 HOH   C O   1 
HETATM 2498 O O   . HOH   O 5 .  ? 6.897   -38.052 4.866   1.00 67.97  ? 282 HOH   C O   1 
# 
