data_9EN7
# 
_entry.id   9EN7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   9EN7         pdb_00009en7 10.2210/pdb9en7/pdb 
WWPDB D_1292128961 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-13 
2 'Structure model' 1 1 2024-11-20 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_last'               
3 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
4 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EN7 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              Janosch.Hennig@uni-bayreuth.de 
_pdbx_contact_author.name_first         Janosch 
_pdbx_contact_author.name_last          Hennig 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5214-7002 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lomoschitz, A.' 1 0000-0003-0683-2003 
'Hennig, J.'     2 0000-0001-5214-7002 
'Murciano, B.'   3 0000-0001-8886-2972 
'Meyer, J.'      4 0009-0003-1430-9981 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   NE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biophys.Chem. 
_citation.journal_id_ASTM           BICIAZ 
_citation.journal_id_CSD            0829 
_citation.journal_id_ISSN           0301-4622 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            316 
_citation.language                  ? 
_citation.page_first                107346 
_citation.page_last                 107346 
_citation.title                     
;The Drosophila RNA binding protein Hrp48 binds a specific RNA sequence of the msl-2 mRNA 3' UTR to regulate translation.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bpc.2024.107346 
_citation.pdbx_database_id_PubMed   39504588 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lomoschitz, A.' 1  ? 
primary 'Meyer, J.'      2  ? 
primary 'Guitart, T.'    3  ? 
primary 'Krepl, M.'      4  ? 
primary 'Lapouge, K.'    5  ? 
primary 'Hayn, C.'       6  ? 
primary 'Schweimer, K.'  7  ? 
primary 'Simon, B.'      8  ? 
primary 'Sponer, J.'     9  ? 
primary 'Gebauer, F.'    10 ? 
primary 'Hennig, J.'     11 ? 
# 
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 'Heterogeneous nuclear ribonucleoprotein 27C' 10102.257 1   ? ? ? ? 
2 non-polymer syn GLYCEROL                                      92.094    2   ? ? ? ? 
3 water       nat water                                         18.015    121 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Hrb27-C,HRP48.1,hnRNP 48' 
# 
_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       
;GAMEEDERGKLFVGGLSWETTQENLSRYFCRFGDIIDCVVMKNNESGRSRGFGFVTFADPTNVNHVLQNGPHTLDGRTID
PKPCNPRTLQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAMEEDERGKLFVGGLSWETTQENLSRYFCRFGDIIDCVVMKNNESGRSRGFGFVTFADPTNVNHVLQNGPHTLDGRTID
PKPCNPRTLQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 GLYCEROL GOL 
3 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  ALA n 
1 3  MET n 
1 4  GLU n 
1 5  GLU n 
1 6  ASP n 
1 7  GLU n 
1 8  ARG n 
1 9  GLY n 
1 10 LYS n 
1 11 LEU n 
1 12 PHE n 
1 13 VAL n 
1 14 GLY n 
1 15 GLY n 
1 16 LEU n 
1 17 SER n 
1 18 TRP n 
1 19 GLU n 
1 20 THR n 
1 21 THR n 
1 22 GLN n 
1 23 GLU n 
1 24 ASN n 
1 25 LEU n 
1 26 SER n 
1 27 ARG n 
1 28 TYR n 
1 29 PHE n 
1 30 CYS n 
1 31 ARG n 
1 32 PHE n 
1 33 GLY n 
1 34 ASP n 
1 35 ILE n 
1 36 ILE n 
1 37 ASP n 
1 38 CYS n 
1 39 VAL n 
1 40 VAL n 
1 41 MET n 
1 42 LYS n 
1 43 ASN n 
1 44 ASN n 
1 45 GLU n 
1 46 SER n 
1 47 GLY n 
1 48 ARG n 
1 49 SER n 
1 50 ARG n 
1 51 GLY n 
1 52 PHE n 
1 53 GLY n 
1 54 PHE n 
1 55 VAL n 
1 56 THR n 
1 57 PHE n 
1 58 ALA n 
1 59 ASP n 
1 60 PRO n 
1 61 THR n 
1 62 ASN n 
1 63 VAL n 
1 64 ASN n 
1 65 HIS n 
1 66 VAL n 
1 67 LEU n 
1 68 GLN n 
1 69 ASN n 
1 70 GLY n 
1 71 PRO n 
1 72 HIS n 
1 73 THR n 
1 74 LEU n 
1 75 ASP n 
1 76 GLY n 
1 77 ARG n 
1 78 THR n 
1 79 ILE n 
1 80 ASP n 
1 81 PRO n 
1 82 LYS n 
1 83 PRO n 
1 84 CYS n 
1 85 ASN n 
1 86 PRO n 
1 87 ARG n 
1 88 THR n 
1 89 LEU n 
1 90 GLN 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                   90 
_entity_src_gen.gene_src_common_name               'fruit fly' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'Hrb27C, hrp48, Rbp7, CG10377' 
_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      'Drosophila melanogaster' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     7227 
_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               'BL-21 (DE3)' 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ?                               'C3 H7 N O2 S'   121.158 
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  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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 
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  1  ?  ?   ?   A . n 
A 1 2  ALA 2  2  ?  ?   ?   A . n 
A 1 3  MET 3  3  ?  ?   ?   A . n 
A 1 4  GLU 4  4  ?  ?   ?   A . n 
A 1 5  GLU 5  5  ?  ?   ?   A . n 
A 1 6  ASP 6  6  ?  ?   ?   A . n 
A 1 7  GLU 7  7  7  GLU GLU A . n 
A 1 8  ARG 8  8  8  ARG ARG A . n 
A 1 9  GLY 9  9  9  GLY GLY A . n 
A 1 10 LYS 10 10 10 LYS LYS A . n 
A 1 11 LEU 11 11 11 LEU LEU A . n 
A 1 12 PHE 12 12 12 PHE PHE A . n 
A 1 13 VAL 13 13 13 VAL VAL A . n 
A 1 14 GLY 14 14 14 GLY GLY A . n 
A 1 15 GLY 15 15 15 GLY GLY A . n 
A 1 16 LEU 16 16 16 LEU LEU A . n 
A 1 17 SER 17 17 17 SER SER A . n 
A 1 18 TRP 18 18 18 TRP TRP A . n 
A 1 19 GLU 19 19 19 GLU GLU A . n 
A 1 20 THR 20 20 20 THR THR A . n 
A 1 21 THR 21 21 21 THR THR A . n 
A 1 22 GLN 22 22 22 GLN GLN A . n 
A 1 23 GLU 23 23 23 GLU GLU A . n 
A 1 24 ASN 24 24 24 ASN ASN A . n 
A 1 25 LEU 25 25 25 LEU LEU A . n 
A 1 26 SER 26 26 26 SER SER A . n 
A 1 27 ARG 27 27 27 ARG ARG A . n 
A 1 28 TYR 28 28 28 TYR TYR A . n 
A 1 29 PHE 29 29 29 PHE PHE A . n 
A 1 30 CYS 30 30 30 CYS CYS A . n 
A 1 31 ARG 31 31 31 ARG ARG A . n 
A 1 32 PHE 32 32 32 PHE PHE A . n 
A 1 33 GLY 33 33 33 GLY GLY A . n 
A 1 34 ASP 34 34 34 ASP ASP A . n 
A 1 35 ILE 35 35 35 ILE ILE A . n 
A 1 36 ILE 36 36 36 ILE ILE A . n 
A 1 37 ASP 37 37 37 ASP ASP A . n 
A 1 38 CYS 38 38 38 CYS CYS A . n 
A 1 39 VAL 39 39 39 VAL VAL A . n 
A 1 40 VAL 40 40 40 VAL VAL A . n 
A 1 41 MET 41 41 41 MET MET A . n 
A 1 42 LYS 42 42 42 LYS LYS A . n 
A 1 43 ASN 43 43 43 ASN ASN A . n 
A 1 44 ASN 44 44 44 ASN ASN A . n 
A 1 45 GLU 45 45 45 GLU GLU A . n 
A 1 46 SER 46 46 46 SER SER A . n 
A 1 47 GLY 47 47 47 GLY GLY A . n 
A 1 48 ARG 48 48 48 ARG ARG A . n 
A 1 49 SER 49 49 49 SER SER A . n 
A 1 50 ARG 50 50 50 ARG ARG A . n 
A 1 51 GLY 51 51 51 GLY GLY A . n 
A 1 52 PHE 52 52 52 PHE PHE A . n 
A 1 53 GLY 53 53 53 GLY GLY A . n 
A 1 54 PHE 54 54 54 PHE PHE A . n 
A 1 55 VAL 55 55 55 VAL VAL A . n 
A 1 56 THR 56 56 56 THR THR A . n 
A 1 57 PHE 57 57 57 PHE PHE A . n 
A 1 58 ALA 58 58 58 ALA ALA A . n 
A 1 59 ASP 59 59 59 ASP ASP A . n 
A 1 60 PRO 60 60 60 PRO PRO A . n 
A 1 61 THR 61 61 61 THR THR A . n 
A 1 62 ASN 62 62 62 ASN ASN A . n 
A 1 63 VAL 63 63 63 VAL VAL A . n 
A 1 64 ASN 64 64 64 ASN ASN A . n 
A 1 65 HIS 65 65 65 HIS HIS A . n 
A 1 66 VAL 66 66 66 VAL VAL A . n 
A 1 67 LEU 67 67 67 LEU LEU A . n 
A 1 68 GLN 68 68 68 GLN GLN A . n 
A 1 69 ASN 69 69 69 ASN ASN A . n 
A 1 70 GLY 70 70 70 GLY GLY A . n 
A 1 71 PRO 71 71 71 PRO PRO A . n 
A 1 72 HIS 72 72 72 HIS HIS A . n 
A 1 73 THR 73 73 73 THR THR A . n 
A 1 74 LEU 74 74 74 LEU LEU A . n 
A 1 75 ASP 75 75 75 ASP ASP A . n 
A 1 76 GLY 76 76 76 GLY GLY A . n 
A 1 77 ARG 77 77 77 ARG ARG A . n 
A 1 78 THR 78 78 78 THR THR A . n 
A 1 79 ILE 79 79 79 ILE ILE A . n 
A 1 80 ASP 80 80 80 ASP ASP A . n 
A 1 81 PRO 81 81 81 PRO PRO A . n 
A 1 82 LYS 82 82 82 LYS LYS A . n 
A 1 83 PRO 83 83 83 PRO PRO A . n 
A 1 84 CYS 84 84 84 CYS CYS A . n 
A 1 85 ASN 85 85 85 ASN ASN A . n 
A 1 86 PRO 86 86 86 PRO PRO A . n 
A 1 87 ARG 87 87 87 ARG ARG A . n 
A 1 88 THR 88 88 88 THR THR A . n 
A 1 89 LEU 89 89 89 LEU LEU A . n 
A 1 90 GLN 90 90 90 GLN GLN A . n 
# 
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 
B 2 GOL 1   101 101 GOL GOL A . 
C 2 GOL 1   102 102 GOL GOL A . 
D 3 HOH 1   201 25  HOH HOH A . 
D 3 HOH 2   202 34  HOH HOH A . 
D 3 HOH 3   203 122 HOH HOH A . 
D 3 HOH 4   204 62  HOH HOH A . 
D 3 HOH 5   205 54  HOH HOH A . 
D 3 HOH 6   206 11  HOH HOH A . 
D 3 HOH 7   207 60  HOH HOH A . 
D 3 HOH 8   208 72  HOH HOH A . 
D 3 HOH 9   209 31  HOH HOH A . 
D 3 HOH 10  210 2   HOH HOH A . 
D 3 HOH 11  211 45  HOH HOH A . 
D 3 HOH 12  212 92  HOH HOH A . 
D 3 HOH 13  213 19  HOH HOH A . 
D 3 HOH 14  214 104 HOH HOH A . 
D 3 HOH 15  215 18  HOH HOH A . 
D 3 HOH 16  216 21  HOH HOH A . 
D 3 HOH 17  217 36  HOH HOH A . 
D 3 HOH 18  218 4   HOH HOH A . 
D 3 HOH 19  219 99  HOH HOH A . 
D 3 HOH 20  220 16  HOH HOH A . 
D 3 HOH 21  221 39  HOH HOH A . 
D 3 HOH 22  222 90  HOH HOH A . 
D 3 HOH 23  223 27  HOH HOH A . 
D 3 HOH 24  224 47  HOH HOH A . 
D 3 HOH 25  225 20  HOH HOH A . 
D 3 HOH 26  226 9   HOH HOH A . 
D 3 HOH 27  227 5   HOH HOH A . 
D 3 HOH 28  228 3   HOH HOH A . 
D 3 HOH 29  229 58  HOH HOH A . 
D 3 HOH 30  230 28  HOH HOH A . 
D 3 HOH 31  231 94  HOH HOH A . 
D 3 HOH 32  232 120 HOH HOH A . 
D 3 HOH 33  233 48  HOH HOH A . 
D 3 HOH 34  234 107 HOH HOH A . 
D 3 HOH 35  235 64  HOH HOH A . 
D 3 HOH 36  236 32  HOH HOH A . 
D 3 HOH 37  237 38  HOH HOH A . 
D 3 HOH 38  238 8   HOH HOH A . 
D 3 HOH 39  239 67  HOH HOH A . 
D 3 HOH 40  240 106 HOH HOH A . 
D 3 HOH 41  241 52  HOH HOH A . 
D 3 HOH 42  242 42  HOH HOH A . 
D 3 HOH 43  243 1   HOH HOH A . 
D 3 HOH 44  244 49  HOH HOH A . 
D 3 HOH 45  245 29  HOH HOH A . 
D 3 HOH 46  246 6   HOH HOH A . 
D 3 HOH 47  247 57  HOH HOH A . 
D 3 HOH 48  248 50  HOH HOH A . 
D 3 HOH 49  249 7   HOH HOH A . 
D 3 HOH 50  250 121 HOH HOH A . 
D 3 HOH 51  251 13  HOH HOH A . 
D 3 HOH 52  252 15  HOH HOH A . 
D 3 HOH 53  253 80  HOH HOH A . 
D 3 HOH 54  254 51  HOH HOH A . 
D 3 HOH 55  255 23  HOH HOH A . 
D 3 HOH 56  256 56  HOH HOH A . 
D 3 HOH 57  257 30  HOH HOH A . 
D 3 HOH 58  258 87  HOH HOH A . 
D 3 HOH 59  259 124 HOH HOH A . 
D 3 HOH 60  260 43  HOH HOH A . 
D 3 HOH 61  261 110 HOH HOH A . 
D 3 HOH 62  262 12  HOH HOH A . 
D 3 HOH 63  263 40  HOH HOH A . 
D 3 HOH 64  264 86  HOH HOH A . 
D 3 HOH 65  265 66  HOH HOH A . 
D 3 HOH 66  266 96  HOH HOH A . 
D 3 HOH 67  267 22  HOH HOH A . 
D 3 HOH 68  268 14  HOH HOH A . 
D 3 HOH 69  269 68  HOH HOH A . 
D 3 HOH 70  270 95  HOH HOH A . 
D 3 HOH 71  271 101 HOH HOH A . 
D 3 HOH 72  272 41  HOH HOH A . 
D 3 HOH 73  273 82  HOH HOH A . 
D 3 HOH 74  274 17  HOH HOH A . 
D 3 HOH 75  275 10  HOH HOH A . 
D 3 HOH 76  276 33  HOH HOH A . 
D 3 HOH 77  277 26  HOH HOH A . 
D 3 HOH 78  278 35  HOH HOH A . 
D 3 HOH 79  279 113 HOH HOH A . 
D 3 HOH 80  280 46  HOH HOH A . 
D 3 HOH 81  281 77  HOH HOH A . 
D 3 HOH 82  282 24  HOH HOH A . 
D 3 HOH 83  283 91  HOH HOH A . 
D 3 HOH 84  284 75  HOH HOH A . 
D 3 HOH 85  285 111 HOH HOH A . 
D 3 HOH 86  286 69  HOH HOH A . 
D 3 HOH 87  287 73  HOH HOH A . 
D 3 HOH 88  288 61  HOH HOH A . 
D 3 HOH 89  289 79  HOH HOH A . 
D 3 HOH 90  290 71  HOH HOH A . 
D 3 HOH 91  291 108 HOH HOH A . 
D 3 HOH 92  292 105 HOH HOH A . 
D 3 HOH 93  293 97  HOH HOH A . 
D 3 HOH 94  294 102 HOH HOH A . 
D 3 HOH 95  295 85  HOH HOH A . 
D 3 HOH 96  296 109 HOH HOH A . 
D 3 HOH 97  297 100 HOH HOH A . 
D 3 HOH 98  298 103 HOH HOH A . 
D 3 HOH 99  299 53  HOH HOH A . 
D 3 HOH 100 300 63  HOH HOH A . 
D 3 HOH 101 301 44  HOH HOH A . 
D 3 HOH 102 302 98  HOH HOH A . 
D 3 HOH 103 303 70  HOH HOH A . 
D 3 HOH 104 304 112 HOH HOH A . 
D 3 HOH 105 305 78  HOH HOH A . 
D 3 HOH 106 306 55  HOH HOH A . 
D 3 HOH 107 307 89  HOH HOH A . 
D 3 HOH 108 308 81  HOH HOH A . 
D 3 HOH 109 309 74  HOH HOH A . 
D 3 HOH 110 310 115 HOH HOH A . 
D 3 HOH 111 311 83  HOH HOH A . 
D 3 HOH 112 312 37  HOH HOH A . 
D 3 HOH 113 313 76  HOH HOH A . 
D 3 HOH 114 314 84  HOH HOH A . 
D 3 HOH 115 315 65  HOH HOH A . 
D 3 HOH 116 316 117 HOH HOH A . 
D 3 HOH 117 317 123 HOH HOH A . 
D 3 HOH 118 318 59  HOH HOH A . 
D 3 HOH 119 319 88  HOH HOH A . 
D 3 HOH 120 320 116 HOH HOH A . 
D 3 HOH 121 321 125 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? 1.20.1_4487 1 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot      ? ? ? v1.0.0      2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EN7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     38.344 
_cell.length_a_esd                 ? 
_cell.length_b                     45.496 
_cell.length_b_esd                 ? 
_cell.length_c                     57.026 
_cell.length_c_esd                 ? 
_cell.volume                       99481.779 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9EN7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EN7 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.46 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.08 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M K2SO4 and 20% (w/v) PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            302 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-03-09 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9762 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9762 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          14.59 
_reflns.entry_id                                       9EN7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.19 
_reflns.d_resolution_low                               31.82 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     32496 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           91.18 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.30 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.06773 
_reflns.pdbx_Rpim_I_all                                0.01881 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.06499 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.19 
_reflns_shell.d_res_low                                     1.233 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.27 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             856 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               13.1 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.597 
_reflns_shell.pdbx_Rpim_I_all                               0.4347 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.609 
_reflns_shell.pdbx_CC_star                                  0.87 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          26.81 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.536 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               24.44 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EN7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.19 
_refine.ls_d_res_low                             31.82 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     29742 
_refine.ls_number_reflns_R_free                  2000 
_refine.ls_number_reflns_R_work                  27742 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    90.32 
_refine.ls_percent_reflns_R_free                 6.72 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1630 
_refine.ls_R_factor_R_free                       0.1703 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1625 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 16.5900 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.0924 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.19 
_refine_hist.d_res_low                        31.82 
_refine_hist.number_atoms_solvent             121 
_refine_hist.number_atoms_total               797 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        664 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         12 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0059  ? 696 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8667  ? 939 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0905  ? 98  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0089  ? 126 ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 12.9887 ? 259 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.19 1.22  . . 21  294  13.55  . . . . 0.2260 . . . . . . . . . . . 0.1749 
'X-RAY DIFFRACTION' 1.22 1.25  . . 90  1256 58.45  . . . . 0.2111 . . . . . . . . . . . 0.2257 
'X-RAY DIFFRACTION' 1.25 1.29  . . 144 1996 93.16  . . . . 0.2244 . . . . . . . . . . . 0.2044 
'X-RAY DIFFRACTION' 1.29 1.33  . . 157 2161 98.72  . . . . 0.2045 . . . . . . . . . . . 0.2194 
'X-RAY DIFFRACTION' 1.33 1.38  . . 155 2160 99.61  . . . . 0.2091 . . . . . . . . . . . 0.1864 
'X-RAY DIFFRACTION' 1.38 1.43  . . 155 2160 99.70  . . . . 0.1690 . . . . . . . . . . . 0.1892 
'X-RAY DIFFRACTION' 1.43 1.50  . . 157 2164 99.87  . . . . 0.1603 . . . . . . . . . . . 0.1857 
'X-RAY DIFFRACTION' 1.50 1.57  . . 156 2172 99.83  . . . . 0.1474 . . . . . . . . . . . 0.1562 
'X-RAY DIFFRACTION' 1.57 1.67  . . 159 2187 99.91  . . . . 0.1507 . . . . . . . . . . . 0.1506 
'X-RAY DIFFRACTION' 1.67 1.80  . . 157 2180 99.91  . . . . 0.1629 . . . . . . . . . . . 0.1705 
'X-RAY DIFFRACTION' 1.80 1.98  . . 158 2202 99.92  . . . . 0.1478 . . . . . . . . . . . 0.1703 
'X-RAY DIFFRACTION' 1.98 2.27  . . 160 2222 100.00 . . . . 0.1522 . . . . . . . . . . . 0.1707 
'X-RAY DIFFRACTION' 2.27 2.86  . . 162 2240 99.88  . . . . 0.1669 . . . . . . . . . . . 0.1697 
'X-RAY DIFFRACTION' 2.86 31.82 . . 169 2348 99.96  . . . . 0.1598 . . . . . . . . . . . 0.1641 
# 
_struct.entry_id                     9EN7 
_struct.title                        'Hrp48 RRM1 domain' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9EN7 
_struct_keywords.text            'RNA-recognition motif, RRM, translational control, RNA BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'RNA BINDING PROTEIN' 
# 
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 2 ? 
C N N 2 ? 
D N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RB27C_DROME 
_struct_ref.pdbx_db_accession          P48809 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MEEDERGKLFVGGLSWETTQENLSRYFCRFGDIIDCVVMKNNESGRSRGFGFVTFADPTNVNHVLQNGPHTLDGRTIDPK
PCNPRTLQ
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9EN7 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 90 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P48809 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  88 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       3 
_struct_ref_seq.pdbx_auth_seq_align_end       90 
# 
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 9EN7 GLY A 1 ? UNP P48809 ? ? 'expression tag' 1 1 
1 9EN7 ALA A 2 ? UNP P48809 ? ? 'expression tag' 2 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 360  ? 
1 MORE         0    ? 
1 'SSA (A^2)'  5580 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 THR A 21 ? CYS A 30 ? THR A 21 CYS A 30 1 ? 10 
HELX_P HELX_P2 AA2 ARG A 31 ? GLY A 33 ? ARG A 31 GLY A 33 5 ? 3  
HELX_P HELX_P3 AA3 THR A 61 ? ASN A 69 ? THR A 61 ASN A 69 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLY 
_struct_mon_prot_cis.label_seq_id           70 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLY 
_struct_mon_prot_cis.auth_seq_id            70 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    71 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     71 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -1.45 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   5 
_struct_sheet.details          ? 
# 
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 
# 
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 ILE A 35 ? LYS A 42 ? ILE A 35 LYS A 42 
AA1 2 SER A 49 ? PHE A 57 ? SER A 49 PHE A 57 
AA1 3 LYS A 10 ? GLY A 14 ? LYS A 10 GLY A 14 
AA1 4 ARG A 77 ? PRO A 83 ? ARG A 77 PRO A 83 
AA1 5 HIS A 72 ? LEU A 74 ? HIS A 72 LEU A 74 
# 
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 N MET A 41 ? N MET A 41 O ARG A 50 ? O ARG A 50 
AA1 2 3 O VAL A 55 ? O VAL A 55 N LEU A 11 ? N LEU A 11 
AA1 3 4 N PHE A 12 ? N PHE A 12 O LYS A 82 ? O LYS A 82 
AA1 4 5 O ARG A 77 ? O ARG A 77 N LEU A 74 ? N LEU A 74 
# 
_pdbx_entry_details.entry_id                   9EN7 
_pdbx_entry_details.has_ligand_of_interest     N 
_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_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
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 1 ? A GLY 1 
2 1 Y 1 A ALA 2 ? A ALA 2 
3 1 Y 1 A MET 3 ? A MET 3 
4 1 Y 1 A GLU 4 ? A GLU 4 
5 1 Y 1 A GLU 5 ? A GLU 5 
6 1 Y 1 A ASP 6 ? A ASP 6 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
GOL C1   C N N 137 
GOL O1   O N N 138 
GOL C2   C N N 139 
GOL O2   O N N 140 
GOL C3   C N N 141 
GOL O3   O N N 142 
GOL H11  H N N 143 
GOL H12  H N N 144 
GOL HO1  H N N 145 
GOL H2   H N N 146 
GOL HO2  H N N 147 
GOL H31  H N N 148 
GOL H32  H N N 149 
GOL HO3  H N N 150 
HIS N    N N N 151 
HIS CA   C N S 152 
HIS C    C N N 153 
HIS O    O N N 154 
HIS CB   C N N 155 
HIS CG   C Y N 156 
HIS ND1  N Y N 157 
HIS CD2  C Y N 158 
HIS CE1  C Y N 159 
HIS NE2  N Y N 160 
HIS OXT  O N N 161 
HIS H    H N N 162 
HIS H2   H N N 163 
HIS HA   H N N 164 
HIS HB2  H N N 165 
HIS HB3  H N N 166 
HIS HD1  H N N 167 
HIS HD2  H N N 168 
HIS HE1  H N N 169 
HIS HE2  H N N 170 
HIS HXT  H N N 171 
HOH O    O N N 172 
HOH H1   H N N 173 
HOH H2   H N N 174 
ILE N    N N N 175 
ILE CA   C N S 176 
ILE C    C N N 177 
ILE O    O N N 178 
ILE CB   C N S 179 
ILE CG1  C N N 180 
ILE CG2  C N N 181 
ILE CD1  C N N 182 
ILE OXT  O N N 183 
ILE H    H N N 184 
ILE H2   H N N 185 
ILE HA   H N N 186 
ILE HB   H N N 187 
ILE HG12 H N N 188 
ILE HG13 H N N 189 
ILE HG21 H N N 190 
ILE HG22 H N N 191 
ILE HG23 H N N 192 
ILE HD11 H N N 193 
ILE HD12 H N N 194 
ILE HD13 H N N 195 
ILE HXT  H N N 196 
LEU N    N N N 197 
LEU CA   C N S 198 
LEU C    C N N 199 
LEU O    O N N 200 
LEU CB   C N N 201 
LEU CG   C N N 202 
LEU CD1  C N N 203 
LEU CD2  C N N 204 
LEU OXT  O N N 205 
LEU H    H N N 206 
LEU H2   H N N 207 
LEU HA   H N N 208 
LEU HB2  H N N 209 
LEU HB3  H N N 210 
LEU HG   H N N 211 
LEU HD11 H N N 212 
LEU HD12 H N N 213 
LEU HD13 H N N 214 
LEU HD21 H N N 215 
LEU HD22 H N N 216 
LEU HD23 H N N 217 
LEU HXT  H N N 218 
LYS N    N N N 219 
LYS CA   C N S 220 
LYS C    C N N 221 
LYS O    O N N 222 
LYS CB   C N N 223 
LYS CG   C N N 224 
LYS CD   C N N 225 
LYS CE   C N N 226 
LYS NZ   N N N 227 
LYS OXT  O N N 228 
LYS H    H N N 229 
LYS H2   H N N 230 
LYS HA   H N N 231 
LYS HB2  H N N 232 
LYS HB3  H N N 233 
LYS HG2  H N N 234 
LYS HG3  H N N 235 
LYS HD2  H N N 236 
LYS HD3  H N N 237 
LYS HE2  H N N 238 
LYS HE3  H N N 239 
LYS HZ1  H N N 240 
LYS HZ2  H N N 241 
LYS HZ3  H N N 242 
LYS HXT  H N N 243 
MET N    N N N 244 
MET CA   C N S 245 
MET C    C N N 246 
MET O    O N N 247 
MET CB   C N N 248 
MET CG   C N N 249 
MET SD   S N N 250 
MET CE   C N N 251 
MET OXT  O N N 252 
MET H    H N N 253 
MET H2   H N N 254 
MET HA   H N N 255 
MET HB2  H N N 256 
MET HB3  H N N 257 
MET HG2  H N N 258 
MET HG3  H N N 259 
MET HE1  H N N 260 
MET HE2  H N N 261 
MET HE3  H N N 262 
MET HXT  H N N 263 
PHE N    N N N 264 
PHE CA   C N S 265 
PHE C    C N N 266 
PHE O    O N N 267 
PHE CB   C N N 268 
PHE CG   C Y N 269 
PHE CD1  C Y N 270 
PHE CD2  C Y N 271 
PHE CE1  C Y N 272 
PHE CE2  C Y N 273 
PHE CZ   C Y N 274 
PHE OXT  O N N 275 
PHE H    H N N 276 
PHE H2   H N N 277 
PHE HA   H N N 278 
PHE HB2  H N N 279 
PHE HB3  H N N 280 
PHE HD1  H N N 281 
PHE HD2  H N N 282 
PHE HE1  H N N 283 
PHE HE2  H N N 284 
PHE HZ   H N N 285 
PHE HXT  H N N 286 
PRO N    N N N 287 
PRO CA   C N S 288 
PRO C    C N N 289 
PRO O    O N N 290 
PRO CB   C N N 291 
PRO CG   C N N 292 
PRO CD   C N N 293 
PRO OXT  O N N 294 
PRO H    H N N 295 
PRO HA   H N N 296 
PRO HB2  H N N 297 
PRO HB3  H N N 298 
PRO HG2  H N N 299 
PRO HG3  H N N 300 
PRO HD2  H N N 301 
PRO HD3  H N N 302 
PRO HXT  H N N 303 
SER N    N N N 304 
SER CA   C N S 305 
SER C    C N N 306 
SER O    O N N 307 
SER CB   C N N 308 
SER OG   O N N 309 
SER OXT  O N N 310 
SER H    H N N 311 
SER H2   H N N 312 
SER HA   H N N 313 
SER HB2  H N N 314 
SER HB3  H N N 315 
SER HG   H N N 316 
SER HXT  H N N 317 
THR N    N N N 318 
THR CA   C N S 319 
THR C    C N N 320 
THR O    O N N 321 
THR CB   C N R 322 
THR OG1  O N N 323 
THR CG2  C N N 324 
THR OXT  O N N 325 
THR H    H N N 326 
THR H2   H N N 327 
THR HA   H N N 328 
THR HB   H N N 329 
THR HG1  H N N 330 
THR HG21 H N N 331 
THR HG22 H N N 332 
THR HG23 H N N 333 
THR HXT  H N N 334 
TRP N    N N N 335 
TRP CA   C N S 336 
TRP C    C N N 337 
TRP O    O N N 338 
TRP CB   C N N 339 
TRP CG   C Y N 340 
TRP CD1  C Y N 341 
TRP CD2  C Y N 342 
TRP NE1  N Y N 343 
TRP CE2  C Y N 344 
TRP CE3  C Y N 345 
TRP CZ2  C Y N 346 
TRP CZ3  C Y N 347 
TRP CH2  C Y N 348 
TRP OXT  O N N 349 
TRP H    H N N 350 
TRP H2   H N N 351 
TRP HA   H N N 352 
TRP HB2  H N N 353 
TRP HB3  H N N 354 
TRP HD1  H N N 355 
TRP HE1  H N N 356 
TRP HE3  H N N 357 
TRP HZ2  H N N 358 
TRP HZ3  H N N 359 
TRP HH2  H N N 360 
TRP HXT  H N N 361 
TYR N    N N N 362 
TYR CA   C N S 363 
TYR C    C N N 364 
TYR O    O N N 365 
TYR CB   C N N 366 
TYR CG   C Y N 367 
TYR CD1  C Y N 368 
TYR CD2  C Y N 369 
TYR CE1  C Y N 370 
TYR CE2  C Y N 371 
TYR CZ   C Y N 372 
TYR OH   O N N 373 
TYR OXT  O N N 374 
TYR H    H N N 375 
TYR H2   H N N 376 
TYR HA   H N N 377 
TYR HB2  H N N 378 
TYR HB3  H N N 379 
TYR HD1  H N N 380 
TYR HD2  H N N 381 
TYR HE1  H N N 382 
TYR HE2  H N N 383 
TYR HH   H N N 384 
TYR HXT  H N N 385 
VAL N    N N N 386 
VAL CA   C N S 387 
VAL C    C N N 388 
VAL O    O N N 389 
VAL CB   C N N 390 
VAL CG1  C N N 391 
VAL CG2  C N N 392 
VAL OXT  O N N 393 
VAL H    H N N 394 
VAL H2   H N N 395 
VAL HA   H N N 396 
VAL HB   H N N 397 
VAL HG11 H N N 398 
VAL HG12 H N N 399 
VAL HG13 H N N 400 
VAL HG21 H N N 401 
VAL HG22 H N N 402 
VAL HG23 H N N 403 
VAL HXT  H N N 404 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
# 
_pdbx_audit_support.funding_organization   'German Research Foundation (DFG)' 
_pdbx_audit_support.country                Germany 
_pdbx_audit_support.grant_number           'HE 7291/5-1' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1ha1 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9EN7 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.026080 
_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]   0.021980 
_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]   0.017536 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . GLU A 1 7  ? 15.06916 16.54659  36.39752 1.000 55.69000  ? 7   GLU A N   1 
ATOM   2   C CA  . GLU A 1 7  ? 15.87111 16.24997  35.21697 1.000 88.29000  ? 7   GLU A CA  1 
ATOM   3   C C   . GLU A 1 7  ? 15.29067 16.94599  33.99025 1.000 149.67000 ? 7   GLU A C   1 
ATOM   4   O O   . GLU A 1 7  ? 14.07342 17.01748  33.82567 1.000 97.66000  ? 7   GLU A O   1 
ATOM   5   C CB  . GLU A 1 7  ? 15.94598 14.74110  34.98905 1.000 105.93000 ? 7   GLU A CB  1 
ATOM   6   C CG  . GLU A 1 7  ? 16.83856 14.33278  33.83411 1.000 79.91000  ? 7   GLU A CG  1 
ATOM   7   C CD  . GLU A 1 7  ? 16.94363 12.82987  33.69462 1.000 94.62000  ? 7   GLU A CD  1 
ATOM   8   O OE1 . GLU A 1 7  ? 16.27318 12.10942  34.46333 1.000 86.26000  ? 7   GLU A OE1 1 
ATOM   9   O OE2 . GLU A 1 7  ? 17.69786 12.36724  32.81839 1.000 161.82000 ? 7   GLU A OE2 1 
ATOM   10  N N   . ARG A 1 8  ? 16.16965 17.45244  33.12468 1.000 41.04000  ? 8   ARG A N   1 
ATOM   11  C CA  . ARG A 1 8  ? 15.75819 18.27323  31.99665 1.000 31.88000  ? 8   ARG A CA  1 
ATOM   12  C C   . ARG A 1 8  ? 16.10851 17.69375  30.63183 1.000 63.47000  ? 8   ARG A C   1 
ATOM   13  O O   . ARG A 1 8  ? 15.61248 18.20595  29.62190 1.000 35.52000  ? 8   ARG A O   1 
ATOM   14  C CB  . ARG A 1 8  ? 16.37912 19.67733  32.10263 1.000 43.21000  ? 8   ARG A CB  1 
ATOM   15  C CG  . ARG A 1 8  ? 15.38880 20.79325  32.38597 1.000 49.29000  ? 8   ARG A CG  1 
ATOM   16  C CD  . ARG A 1 8  ? 15.24503 21.05664  33.87446 1.000 97.48000  ? 8   ARG A CD  1 
ATOM   17  N NE  . ARG A 1 8  ? 14.28270 22.11979  34.13795 1.000 154.60000 ? 8   ARG A NE  1 
ATOM   18  C CZ  . ARG A 1 8  ? 14.09266 22.68471  35.32228 1.000 124.02000 ? 8   ARG A CZ  1 
ATOM   19  N NH1 . ARG A 1 8  ? 14.79669 22.32230  36.38216 1.000 66.99000  ? 8   ARG A NH1 1 
ATOM   20  N NH2 . ARG A 1 8  ? 13.17540 23.63993  35.44539 1.000 74.25000  ? 8   ARG A NH2 1 
ATOM   21  N N   . GLY A 1 9  ? 16.92845 16.64869  30.56165 1.000 43.38152  ? 9   GLY A N   1 
ATOM   22  C CA  . GLY A 1 9  ? 17.48309 16.24151  29.28360 1.000 27.41381  ? 9   GLY A CA  1 
ATOM   23  C C   . GLY A 1 9  ? 17.00873 14.91478  28.72894 1.000 16.24142  ? 9   GLY A C   1 
ATOM   24  O O   . GLY A 1 9  ? 17.73273 14.27543  27.95728 1.000 13.58847  ? 9   GLY A O   1 
ATOM   25  N N   . LYS A 1 10 ? 15.79396 14.50374  29.07826 1.000 14.20697  ? 10  LYS A N   1 
ATOM   26  C CA  . LYS A 1 10 ? 15.27956 13.19727  28.69275 1.000 13.50425  ? 10  LYS A CA  1 
ATOM   27  C C   . LYS A 1 10 ? 14.32795 13.30997  27.50486 1.000 12.25410  ? 10  LYS A C   1 
ATOM   28  O O   . LYS A 1 10 ? 13.42432 14.15550  27.48769 1.000 13.88851  ? 10  LYS A O   1 
ATOM   29  C CB  . LYS A 1 10 ? 14.62380 12.49164  29.88147 1.000 14.02800  ? 10  LYS A CB  1 
ATOM   30  C CG  . LYS A 1 10 ? 14.36535 11.00099  29.66697 1.000 13.82008  ? 10  LYS A CG  1 
ATOM   31  C CD  . LYS A 1 10 ? 13.83654 10.35287  30.95244 1.000 14.06221  ? 10  LYS A CD  1 
ATOM   32  C CE  . LYS A 1 10 ? 13.81011 8.84348   30.85519 1.000 14.61228  ? 10  LYS A CE  1 
ATOM   33  N NZ  . LYS A 1 10 ? 13.34459 8.22341   32.11618 1.000 15.15971  ? 10  LYS A NZ  1 
ATOM   34  N N   . LEU A 1 11 ? 14.52252 12.41952  26.54077 1.000 12.45939  ? 11  LEU A N   1 
ATOM   35  C CA  . LEU A 1 11 ? 13.73013 12.33739  25.32538 1.000 14.45963  ? 11  LEU A CA  1 
ATOM   36  C C   . LEU A 1 11 ? 13.04520 10.97676  25.26527 1.000 14.05958  ? 11  LEU A C   1 
ATOM   37  O O   . LEU A 1 11 ? 13.70966 9.94513   25.36137 1.000 15.78610  ? 11  LEU A O   1 
ATOM   38  C CB  . LEU A 1 11 ? 14.71476 12.44192  24.16238 1.000 18.08901  ? 11  LEU A CB  1 
ATOM   39  C CG  . LEU A 1 11 ? 14.31207 12.70516  22.72527 1.000 19.56814  ? 11  LEU A CG  1 
ATOM   40  C CD1 . LEU A 1 11 ? 13.74708 14.11700  22.59752 1.000 18.53643  ? 11  LEU A CD1 1 
ATOM   41  C CD2 . LEU A 1 11 ? 15.51916 12.49530  21.82198 1.000 20.63405  ? 11  LEU A CD2 1 
ATOM   42  N N   . PHE A 1 12 ? 11.72393 10.97393  25.10766 1.000 12.95155  ? 12  PHE A N   1 
ATOM   43  C CA  . PHE A 1 12 ? 11.00955 9.78188   24.66032 1.000 11.76457  ? 12  PHE A CA  1 
ATOM   44  C C   . PHE A 1 12 ? 11.22614 9.62950   23.15971 1.000 10.76182  ? 12  PHE A C   1 
ATOM   45  O O   . PHE A 1 12 ? 11.27644 10.62846  22.43429 1.000 12.52255  ? 12  PHE A O   1 
ATOM   46  C CB  . PHE A 1 12 ? 9.51627  9.98597   24.95253 1.000 13.19895  ? 12  PHE A CB  1 
ATOM   47  C CG  . PHE A 1 12 ? 8.58519  9.07938   24.17092 1.000 13.38582  ? 12  PHE A CG  1 
ATOM   48  C CD1 . PHE A 1 12 ? 8.30223  7.78922   24.60829 1.000 14.53069  ? 12  PHE A CD1 1 
ATOM   49  C CD2 . PHE A 1 12 ? 7.97650  9.52385   23.00463 1.000 14.28066  ? 12  PHE A CD2 1 
ATOM   50  C CE1 . PHE A 1 12 ? 7.42449  6.97084   23.89668 1.000 15.05180  ? 12  PHE A CE1 1 
ATOM   51  C CE2 . PHE A 1 12 ? 7.10248  8.70181   22.29350 1.000 15.12023  ? 12  PHE A CE2 1 
ATOM   52  C CZ  . PHE A 1 12 ? 6.82480  7.43361   22.74386 1.000 14.99917  ? 12  PHE A CZ  1 
ATOM   53  N N   . VAL A 1 13 ? 11.39351 8.38820   22.69513 1.000 11.11186  ? 13  VAL A N   1 
ATOM   54  C CA  . VAL A 1 13 ? 11.48424 8.12604   21.26244 1.000 11.91195  ? 13  VAL A CA  1 
ATOM   55  C C   . VAL A 1 13 ? 10.50346 7.02888   20.89528 1.000 11.93564  ? 13  VAL A C   1 
ATOM   56  O O   . VAL A 1 13 ? 10.71041 5.86107   21.25078 1.000 12.60941  ? 13  VAL A O   1 
ATOM   57  C CB  . VAL A 1 13 ? 12.90493 7.77135   20.80056 1.000 12.83838  ? 13  VAL A CB  1 
ATOM   58  C CG1 . VAL A 1 13 ? 12.94388 7.71569   19.27628 1.000 13.52794  ? 13  VAL A CG1 1 
ATOM   59  C CG2 . VAL A 1 13 ? 13.92498 8.77723   21.33237 1.000 13.67532  ? 13  VAL A CG2 1 
ATOM   60  N N   . GLY A 1 14 ? 9.44970  7.39348   20.17299 1.000 11.89616  ? 14  GLY A N   1 
ATOM   61  C CA  . GLY A 1 14 ? 8.46808  6.43226   19.73270 1.000 12.79364  ? 14  GLY A CA  1 
ATOM   62  C C   . GLY A 1 14 ? 8.66133  6.01061   18.28475 1.000 12.69100  ? 14  GLY A C   1 
ATOM   63  O O   . GLY A 1 14 ? 9.46423  6.56072   17.53486 1.000 13.27791  ? 14  GLY A O   1 
ATOM   64  N N   . GLY A 1 15 ? 7.87950  5.01142   17.89235 1.000 13.54110  ? 15  GLY A N   1 
ATOM   65  C CA  . GLY A 1 15 ? 7.84984  4.58885   16.50626 1.000 14.25171  ? 15  GLY A CA  1 
ATOM   66  C C   . GLY A 1 15 ? 9.04395  3.78567   16.04960 1.000 13.66216  ? 15  GLY A C   1 
ATOM   67  O O   . GLY A 1 15 ? 9.30196  3.70514   14.84724 1.000 16.34670  ? 15  GLY A O   1 
ATOM   68  N N   . LEU A 1 16 ? 9.78663  3.18533   16.97097 1.000 13.10683  ? 16  LEU A N   1 
ATOM   69  C CA  . LEU A 1 16 ? 10.93863 2.38569   16.58938 1.000 13.41477  ? 16  LEU A CA  1 
ATOM   70  C C   . LEU A 1 16 ? 10.49738 1.04132   16.03295 1.000 16.00718  ? 16  LEU A C   1 
ATOM   71  O O   . LEU A 1 16 ? 9.51433  0.45340   16.48652 1.000 16.67305  ? 16  LEU A O   1 
ATOM   72  C CB  . LEU A 1 16 ? 11.80142 2.08356   17.81098 1.000 13.75954  ? 16  LEU A CB  1 
ATOM   73  C CG  . LEU A 1 16 ? 12.25598 3.23893   18.68100 1.000 13.92535  ? 16  LEU A CG  1 
ATOM   74  C CD1 . LEU A 1 16 ? 13.04960 2.69766   19.84374 1.000 15.01759  ? 16  LEU A CD1 1 
ATOM   75  C CD2 . LEU A 1 16 ? 13.06532 4.20237   17.84593 1.000 15.90980  ? 16  LEU A CD2 1 
ATOM   76  N N   A SER A 1 17 ? 11.22900 0.54947   15.04035 0.737 17.10468  ? 17  SER A N   1 
ATOM   77  N N   B SER A 1 17 ? 11.25651 0.53564   15.06766 0.263 16.85465  ? 17  SER A N   1 
ATOM   78  C CA  A SER A 1 17 ? 11.07804 -0.85437  14.70241 0.737 17.91004  ? 17  SER A CA  1 
ATOM   79  C CA  B SER A 1 17 ? 11.10178 -0.85722  14.67837 0.263 17.57053  ? 17  SER A CA  1 
ATOM   80  C C   A SER A 1 17 ? 11.51400 -1.69263  15.89246 0.737 17.27312  ? 17  SER A C   1 
ATOM   81  C C   B SER A 1 17 ? 11.58755 -1.74729  15.81567 0.263 17.54684  ? 17  SER A C   1 
ATOM   82  O O   A SER A 1 17 ? 12.40047 -1.30508  16.65573 0.737 14.63597  ? 17  SER A O   1 
ATOM   83  O O   B SER A 1 17 ? 12.58625 -1.44448  16.47368 0.263 16.60725  ? 17  SER A O   1 
ATOM   84  C CB  A SER A 1 17 ? 11.94697 -1.22657  13.50825 0.737 19.07597  ? 17  SER A CB  1 
ATOM   85  C CB  B SER A 1 17 ? 11.91611 -1.14077  13.41772 0.263 18.36536  ? 17  SER A CB  1 
ATOM   86  O OG  A SER A 1 17 ? 11.95603 -2.63995  13.35215 0.737 18.28903  ? 17  SER A OG  1 
ATOM   87  O OG  B SER A 1 17 ? 13.30420 -0.99033  13.65764 0.263 18.59170  ? 17  SER A OG  1 
ATOM   88  N N   . TRP A 1 18 ? 10.87043 -2.84860  16.05975 1.000 17.69423  ? 18  TRP A N   1 
ATOM   89  C CA  . TRP A 1 18 ? 11.27263 -3.74466  17.13476 1.000 18.73383  ? 18  TRP A CA  1 
ATOM   90  C C   . TRP A 1 18 ? 12.67901 -4.29060  16.94714 1.000 16.68621  ? 18  TRP A C   1 
ATOM   91  O O   . TRP A 1 18 ? 13.24356 -4.82165  17.90823 1.000 18.43379  ? 18  TRP A O   1 
ATOM   92  C CB  . TRP A 1 18 ? 10.25285 -4.86829  17.36403 1.000 23.31069  ? 18  TRP A CB  1 
ATOM   93  C CG  . TRP A 1 18 ? 10.34312 -6.04485  16.42893 1.000 27.52962  ? 18  TRP A CG  1 
ATOM   94  C CD1 . TRP A 1 18 ? 9.78805  -6.14742  15.18405 1.000 29.07191  ? 18  TRP A CD1 1 
ATOM   95  C CD2 . TRP A 1 18 ? 11.00281 -7.29924  16.67590 1.000 30.60367  ? 18  TRP A CD2 1 
ATOM   96  N NE1 . TRP A 1 18 ? 10.06675 -7.38008  14.64076 1.000 30.25889  ? 18  TRP A NE1 1 
ATOM   97  C CE2 . TRP A 1 18 ? 10.81124 -8.10409  15.53384 1.000 31.06425  ? 18  TRP A CE2 1 
ATOM   98  C CE3 . TRP A 1 18 ? 11.74194 -7.81471  17.74743 1.000 32.42757  ? 18  TRP A CE3 1 
ATOM   99  C CZ2 . TRP A 1 18 ? 11.33162 -9.39306  15.43314 1.000 32.58549  ? 18  TRP A CZ2 1 
ATOM   100 C CZ3 . TRP A 1 18 ? 12.25580 -9.09636  17.64646 1.000 33.43559  ? 18  TRP A CZ3 1 
ATOM   101 C CH2 . TRP A 1 18 ? 12.04907 -9.86986  16.49767 1.000 33.41453  ? 18  TRP A CH2 1 
ATOM   102 N N   . GLU A 1 19 ? 13.26558 -4.14311  15.75441 1.000 15.50186  ? 19  GLU A N   1 
ATOM   103 C CA  . GLU A 1 19 ? 14.62276 -4.60314  15.50178 1.000 15.80189  ? 19  GLU A CA  1 
ATOM   104 C C   . GLU A 1 19 ? 15.67950 -3.65922  16.06551 1.000 14.78335  ? 19  GLU A C   1 
ATOM   105 O O   . GLU A 1 19 ? 16.84456 -4.04832  16.16678 1.000 16.10983  ? 19  GLU A O   1 
ATOM   106 C CB  . GLU A 1 19 ? 14.83585 -4.71624  13.98549 1.000 17.27576  ? 19  GLU A CB  1 
ATOM   107 C CG  . GLU A 1 19 ? 15.06474 -3.35338  13.30232 1.000 18.56012  ? 19  GLU A CG  1 
ATOM   108 C CD  . GLU A 1 19 ? 14.75509 -3.34326  11.81078 1.000 19.25231  ? 19  GLU A CD  1 
ATOM   109 O OE1 . GLU A 1 19 ? 13.55794 -3.33940  11.43172 1.000 18.46537  ? 19  GLU A OE1 1 
ATOM   110 O OE2 . GLU A 1 19 ? 15.70717 -3.32533  11.00776 1.000 20.19716  ? 19  GLU A OE2 1 
ATOM   111 N N   . THR A 1 20 ? 15.32170 -2.41702  16.38996 1.000 13.80429  ? 20  THR A N   1 
ATOM   112 C CA  . THR A 1 20 ? 16.31650 -1.40375  16.72118 1.000 13.71217  ? 20  THR A CA  1 
ATOM   113 C C   . THR A 1 20 ? 16.81554 -1.61498  18.14679 1.000 13.37529  ? 20  THR A C   1 
ATOM   114 O O   . THR A 1 20 ? 16.02220 -1.61589  19.09562 1.000 14.12538  ? 20  THR A O   1 
ATOM   115 C CB  . THR A 1 20 ? 15.68092 -0.02298  16.59609 1.000 14.22539  ? 20  THR A CB  1 
ATOM   116 O OG1 . THR A 1 20 ? 15.23668 0.18976   15.24993 1.000 15.71504  ? 20  THR A OG1 1 
ATOM   117 C CG2 . THR A 1 20 ? 16.67709 1.06524   16.99483 1.000 14.62544  ? 20  THR A CG2 1 
ATOM   118 N N   . THR A 1 21 ? 18.12376 -1.79381  18.30241 1.000 13.63058  ? 21  THR A N   1 
ATOM   119 C CA  . THR A 1 21 ? 18.70420 -1.96715  19.62596 1.000 13.65690  ? 21  THR A CA  1 
ATOM   120 C C   . THR A 1 21 ? 18.90683 -0.61073  20.29113 1.000 13.68848  ? 21  THR A C   1 
ATOM   121 O O   . THR A 1 21 ? 18.97683 0.43677   19.64225 1.000 13.37002  ? 21  THR A O   1 
ATOM   122 C CB  . THR A 1 21 ? 20.07444 -2.64254  19.54303 1.000 14.40173  ? 21  THR A CB  1 
ATOM   123 O OG1 . THR A 1 21 ? 20.97855 -1.74687  18.89128 1.000 13.99641  ? 21  THR A OG1 1 
ATOM   124 C CG2 . THR A 1 21 ? 20.01688 -3.97524  18.77445 1.000 14.82020  ? 21  THR A CG2 1 
ATOM   125 N N   . GLN A 1 22 ? 19.02091 -0.63551  21.61757 1.000 14.16486  ? 22  GLN A N   1 
ATOM   126 C CA  . GLN A 1 22 ? 19.29947 0.61877   22.30956 1.000 14.52543  ? 22  GLN A CA  1 
ATOM   127 C C   . GLN A 1 22 ? 20.69563 1.13741   21.98785 1.000 13.89640  ? 22  GLN A C   1 
ATOM   128 O O   . GLN A 1 22 ? 20.91923 2.34818   22.02105 1.000 13.61479  ? 22  GLN A O   1 
ATOM   129 C CB  . GLN A 1 22 ? 19.01578 0.50833   23.80893 1.000 16.72832  ? 22  GLN A CB  1 
ATOM   130 C CG  . GLN A 1 22 ? 19.81196 -0.54069  24.51808 1.000 17.68633  ? 22  GLN A CG  1 
ATOM   131 C CD  . GLN A 1 22 ? 19.25139 -0.82859  25.90744 1.000 19.02860  ? 22  GLN A CD  1 
ATOM   132 O OE1 . GLN A 1 22 ? 18.03017 -0.93048  26.10309 1.000 19.14177  ? 22  GLN A OE1 1 
ATOM   133 N NE2 . GLN A 1 22 ? 20.14334 -0.94008  26.88026 1.000 20.14189  ? 22  GLN A NE2 1 
ATOM   134 N N   . GLU A 1 23 ? 21.63262 0.25444   21.63887 1.000 13.13315  ? 23  GLU A N   1 
ATOM   135 C CA  . GLU A 1 23 ? 22.94218 0.71878   21.18896 1.000 14.16486  ? 23  GLU A CA  1 
ATOM   136 C C   . GLU A 1 23 ? 22.84307 1.49201   19.87539 1.000 13.17790  ? 23  GLU A C   1 
ATOM   137 O O   . GLU A 1 23 ? 23.50405 2.52153   19.69687 1.000 13.05946  ? 23  GLU A O   1 
ATOM   138 C CB  . GLU A 1 23 ? 23.88946 -0.47222  21.06324 1.000 16.13615  ? 23  GLU A CB  1 
ATOM   139 C CG  . GLU A 1 23 ? 24.25030 -1.11587  22.41032 1.000 20.25243  ? 23  GLU A CG  1 
ATOM   140 C CD  . GLU A 1 23 ? 23.14819 -2.00988  23.02190 1.000 22.05001  ? 23  GLU A CD  1 
ATOM   141 O OE1 . GLU A 1 23 ? 22.28098 -2.54048  22.27810 1.000 20.73933  ? 23  GLU A OE1 1 
ATOM   142 O OE2 . GLU A 1 23 ? 23.16028 -2.18038  24.26757 1.000 25.35041  ? 23  GLU A OE2 1 
ATOM   143 N N   . ASN A 1 24 ? 22.02612 1.00996   18.94383 1.000 12.35674  ? 24  ASN A N   1 
ATOM   144 C CA  . ASN A 1 24 ? 21.80765 1.73238   17.69610 1.000 12.61993  ? 24  ASN A CA  1 
ATOM   145 C C   . ASN A 1 24 ? 21.06516 3.04499   17.94705 1.000 11.77773  ? 24  ASN A C   1 
ATOM   146 O O   . ASN A 1 24 ? 21.39494 4.08505   17.36304 1.000 12.31463  ? 24  ASN A O   1 
ATOM   147 C CB  . ASN A 1 24 ? 21.01962 0.82092   16.75285 1.000 13.69638  ? 24  ASN A CB  1 
ATOM   148 C CG  . ASN A 1 24 ? 20.93450 1.35701   15.33397 1.000 14.20170  ? 24  ASN A CG  1 
ATOM   149 O OD1 . ASN A 1 24 ? 21.78756 2.11727   14.88295 1.000 15.19393  ? 24  ASN A OD1 1 
ATOM   150 N ND2 . ASN A 1 24 ? 19.88669 0.95738   14.62440 1.000 16.36512  ? 24  ASN A ND2 1 
ATOM   151 N N   . LEU A 1 25 ? 20.06096 3.02054   18.82049 1.000 11.67508  ? 25  LEU A N   1 
ATOM   152 C CA  . LEU A 1 25 ? 19.35410 4.24798   19.17375 1.000 11.82773  ? 25  LEU A CA  1 
ATOM   153 C C   . LEU A 1 25 ? 20.31621 5.29193   19.73359 1.000 11.41453  ? 25  LEU A C   1 
ATOM   154 O O   . LEU A 1 25 ? 20.26098 6.47638   19.37963 1.000 12.08829  ? 25  LEU A O   1 
ATOM   155 C CB  . LEU A 1 25 ? 18.26631 3.90432   20.19347 1.000 12.80680  ? 25  LEU A CB  1 
ATOM   156 C CG  . LEU A 1 25 ? 17.30263 5.01701   20.59548 1.000 12.89365  ? 25  LEU A CG  1 
ATOM   157 C CD1 . LEU A 1 25 ? 16.47806 5.46272   19.38718 1.000 14.56227  ? 25  LEU A CD1 1 
ATOM   158 C CD2 . LEU A 1 25 ? 16.41174 4.54611   21.73416 1.000 13.66743  ? 25  LEU A CD2 1 
ATOM   159 N N   . SER A 1 26 ? 21.18479 4.87125   20.64777 1.000 12.56993  ? 26  SER A N   1 
ATOM   160 C CA  . SER A 1 26 ? 22.16022 5.78406   21.22687 1.000 13.27264  ? 26  SER A CA  1 
ATOM   161 C C   . SER A 1 26 ? 23.10658 6.31993   20.16221 1.000 13.56478  ? 26  SER A C   1 
ATOM   162 O O   . SER A 1 26 ? 23.37409 7.52750   20.10626 1.000 14.79651  ? 26  SER A O   1 
ATOM   163 C CB  . SER A 1 26 ? 22.92748 5.05869   22.32349 1.000 15.09391  ? 26  SER A CB  1 
ATOM   164 O OG  . SER A 1 26 ? 23.75845 5.96223   23.00649 1.000 17.83635  ? 26  SER A OG  1 
ATOM   165 N N   . ARG A 1 27 ? 23.61688 5.43293   19.30672 1.000 14.24381  ? 27  ARG A N   1 
ATOM   166 C CA  . ARG A 1 27 ? 24.49272 5.86321   18.22276 1.000 14.91758  ? 27  ARG A CA  1 
ATOM   167 C C   . ARG A 1 27 ? 23.84741 6.96376   17.38976 1.000 14.40436  ? 27  ARG A C   1 
ATOM   168 O O   . ARG A 1 27 ? 24.48014 7.98148   17.08210 1.000 16.12562  ? 27  ARG A O   1 
ATOM   169 C CB  . ARG A 1 27 ? 24.83880 4.66000   17.34464 1.000 16.26248  ? 27  ARG A CB  1 
ATOM   170 C CG  . ARG A 1 27 ? 25.69208 4.99554   16.12564 1.000 18.58381  ? 27  ARG A CG  1 
ATOM   171 C CD  . ARG A 1 27 ? 25.57794 3.91203   15.05602 1.000 20.34454  ? 27  ARG A CD  1 
ATOM   172 N NE  . ARG A 1 27 ? 24.21281 3.79771   14.55327 1.000 21.56574  ? 27  ARG A NE  1 
ATOM   173 C CZ  . ARG A 1 27 ? 23.64714 4.65790   13.71579 1.000 22.79747  ? 27  ARG A CZ  1 
ATOM   174 N NH1 . ARG A 1 27 ? 24.31923 5.68438   13.21927 1.000 23.76864  ? 27  ARG A NH1 1 
ATOM   175 N NH2 . ARG A 1 27 ? 22.36896 4.49481   13.38155 1.000 22.72904  ? 27  ARG A NH2 1 
ATOM   176 N N   . TYR A 1 28 ? 22.58052 6.78396   17.02268 1.000 13.57268  ? 28  TYR A N   1 
ATOM   177 C CA  . TYR A 1 28 ? 21.91687 7.79490   16.21228 1.000 13.17263  ? 28  TYR A CA  1 
ATOM   178 C C   . TYR A 1 28 ? 21.85266 9.13082   16.94772 1.000 13.00419  ? 28  TYR A C   1 
ATOM   179 O O   . TYR A 1 28 ? 22.21552 10.18371  16.39952 1.000 14.12275  ? 28  TYR A O   1 
ATOM   180 C CB  . TYR A 1 28 ? 20.51853 7.32763   15.78661 1.000 13.68322  ? 28  TYR A CB  1 
ATOM   181 C CG  . TYR A 1 28 ? 19.81085 8.42779   15.03077 1.000 14.54911  ? 28  TYR A CG  1 
ATOM   182 C CD1 . TYR A 1 28 ? 20.11690 8.68473   13.69626 1.000 16.92571  ? 28  TYR A CD1 1 
ATOM   183 C CD2 . TYR A 1 28 ? 18.89485 9.26647   15.66955 1.000 14.68334  ? 28  TYR A CD2 1 
ATOM   184 C CE1 . TYR A 1 28 ? 19.50706 9.72053   13.01238 1.000 18.45748  ? 28  TYR A CE1 1 
ATOM   185 C CE2 . TYR A 1 28 ? 18.27938 10.31163  14.99464 1.000 16.33091  ? 28  TYR A CE2 1 
ATOM   186 C CZ  . TYR A 1 28 ? 18.58943 10.53169  13.66416 1.000 17.81529  ? 28  TYR A CZ  1 
ATOM   187 O OH  . TYR A 1 28 ? 18.00099 11.56299  12.96419 1.000 20.19716  ? 28  TYR A OH  1 
ATOM   188 N N   . PHE A 1 29 ? 21.38637 9.11310   18.19545 1.000 12.26463  ? 29  PHE A N   1 
ATOM   189 C CA  . PHE A 1 29 ? 21.14041 10.37906  18.86905 1.000 12.54624  ? 29  PHE A CA  1 
ATOM   190 C C   . PHE A 1 29 ? 22.40522 11.04941  19.37472 1.000 12.91207  ? 29  PHE A C   1 
ATOM   191 O O   . PHE A 1 29 ? 22.36855 12.24784  19.67316 1.000 12.88839  ? 29  PHE A O   1 
ATOM   192 C CB  . PHE A 1 29 ? 20.05926 10.23002  19.95264 1.000 12.69626  ? 29  PHE A CB  1 
ATOM   193 C CG  . PHE A 1 29 ? 18.67895 10.20335  19.38532 1.000 12.29095  ? 29  PHE A CG  1 
ATOM   194 C CD1 . PHE A 1 29 ? 18.11226 11.36876  18.89094 1.000 13.98062  ? 29  PHE A CD1 1 
ATOM   195 C CD2 . PHE A 1 29 ? 17.96768 9.00559   19.26192 1.000 12.18567  ? 29  PHE A CD2 1 
ATOM   196 C CE1 . PHE A 1 29 ? 16.86594 11.35482  18.31722 1.000 14.54911  ? 29  PHE A CE1 1 
ATOM   197 C CE2 . PHE A 1 29 ? 16.70975 8.99536   18.69352 1.000 12.63309  ? 29  PHE A CE2 1 
ATOM   198 C CZ  . PHE A 1 29 ? 16.16058 10.16635  18.21301 1.000 13.67269  ? 29  PHE A CZ  1 
ATOM   199 N N   . CYS A 1 30 ? 23.52972 10.33862  19.41247 1.000 13.46214  ? 30  CYS A N   1 
ATOM   200 C CA  . CYS A 1 30 ? 24.77378 10.97898  19.81739 1.000 14.63597  ? 30  CYS A CA  1 
ATOM   201 C C   . CYS A 1 30 ? 25.21200 12.07495  18.86256 1.000 14.86757  ? 30  CYS A C   1 
ATOM   202 O O   . CYS A 1 30 ? 26.08571 12.87196  19.22063 1.000 15.63872  ? 30  CYS A O   1 
ATOM   203 C CB  . CYS A 1 30 ? 25.90315 9.96365   19.88277 1.000 18.18639  ? 30  CYS A CB  1 
ATOM   204 S SG  . CYS A 1 30 ? 25.95468 9.07521   21.37670 1.000 20.28927  ? 30  CYS A SG  1 
ATOM   205 N N   . ARG A 1 31 ? 24.64579 12.13594  17.65528 1.000 15.38869  ? 31  ARG A N   1 
ATOM   206 C CA  . ARG A 1 31 ? 24.99227 13.26096  16.79713 1.000 17.18101  ? 31  ARG A CA  1 
ATOM   207 C C   . ARG A 1 31 ? 24.52625 14.58404  17.38910 1.000 16.32038  ? 31  ARG A C   1 
ATOM   208 O O   . ARG A 1 31 ? 24.98546 15.64587  16.95658 1.000 18.41800  ? 31  ARG A O   1 
ATOM   209 C CB  . ARG A 1 31 ? 24.43744 13.07348  15.38726 1.000 21.44731  ? 31  ARG A CB  1 
ATOM   210 C CG  . ARG A 1 31 ? 22.94850 13.32397  15.25024 1.000 25.43989  ? 31  ARG A CG  1 
ATOM   211 C CD  . ARG A 1 31 ? 22.54570 13.45496  13.78510 1.000 30.61683  ? 31  ARG A CD  1 
ATOM   212 N NE  . ARG A 1 31 ? 22.84565 12.24975  13.02366 1.000 34.20410  ? 31  ARG A NE  1 
ATOM   213 C CZ  . ARG A 1 31 ? 22.66193 12.12652  11.71647 1.000 36.59913  ? 31  ARG A CZ  1 
ATOM   214 N NH1 . ARG A 1 31 ? 22.20335 13.13001  10.98449 1.000 37.06760  ? 31  ARG A NH1 1 
ATOM   215 N NH2 . ARG A 1 31 ? 22.94123 10.96711  11.12807 1.000 37.14130  ? 31  ARG A NH2 1 
ATOM   216 N N   . PHE A 1 32 ? 23.62231 14.54613  18.35518 1.000 13.82008  ? 32  PHE A N   1 
ATOM   217 C CA  . PHE A 1 32 ? 23.11854 15.75427  18.97948 1.000 14.25434  ? 32  PHE A CA  1 
ATOM   218 C C   . PHE A 1 32 ? 23.70494 16.00842  20.35715 1.000 13.96483  ? 32  PHE A C   1 
ATOM   219 O O   . PHE A 1 32 ? 23.32505 16.99356  20.99057 1.000 15.61240  ? 32  PHE A O   1 
ATOM   220 C CB  . PHE A 1 32 ? 21.59524 15.69833  19.06181 1.000 15.07023  ? 32  PHE A CB  1 
ATOM   221 C CG  . PHE A 1 32 ? 20.94162 15.55253  17.72121 1.000 14.94653  ? 32  PHE A CG  1 
ATOM   222 C CD1 . PHE A 1 32 ? 20.83268 16.63601  16.86752 1.000 15.19919  ? 32  PHE A CD1 1 
ATOM   223 C CD2 . PHE A 1 32 ? 20.46013 14.32408  17.29863 1.000 16.87308  ? 32  PHE A CD2 1 
ATOM   224 C CE1 . PHE A 1 32 ? 20.24969 16.49451  15.62448 1.000 16.40986  ? 32  PHE A CE1 1 
ATOM   225 C CE2 . PHE A 1 32 ? 19.86486 14.18737  16.05602 1.000 18.33378  ? 32  PHE A CE2 1 
ATOM   226 C CZ  . PHE A 1 32 ? 19.77025 15.27120  15.22147 1.000 17.58369  ? 32  PHE A CZ  1 
ATOM   227 N N   . GLY A 1 33 ? 24.60749 15.16365  20.83799 1.000 12.72521  ? 33  GLY A N   1 
ATOM   228 C CA  . GLY A 1 33 ? 25.23075 15.39608  22.13015 1.000 13.53583  ? 33  GLY A CA  1 
ATOM   229 C C   . GLY A 1 33 ? 25.55984 14.11035  22.86537 1.000 12.90944  ? 33  GLY A C   1 
ATOM   230 O O   . GLY A 1 33 ? 25.10730 13.01964  22.52471 1.000 13.62532  ? 33  GLY A O   1 
ATOM   231 N N   . ASP A 1 34 ? 26.35545 14.26787  23.92545 1.000 12.28832  ? 34  ASP A N   1 
ATOM   232 C CA  . ASP A 1 34 ? 26.76173 13.14074  24.76189 1.000 12.37254  ? 34  ASP A CA  1 
ATOM   233 C C   . ASP A 1 34 ? 25.55503 12.56561  25.49536 1.000 11.64877  ? 34  ASP A C   1 
ATOM   234 O O   . ASP A 1 34 ? 24.71746 13.31171  26.01304 1.000 12.04355  ? 34  ASP A O   1 
ATOM   235 C CB  . ASP A 1 34 ? 27.77643 13.62266  25.78893 1.000 13.16210  ? 34  ASP A CB  1 
ATOM   236 C CG  . ASP A 1 34 ? 28.93014 14.33767  25.14536 1.000 13.68322  ? 34  ASP A CG  1 
ATOM   237 O OD1 . ASP A 1 34 ? 29.90177 13.66846  24.74353 1.000 14.19644  ? 34  ASP A OD1 1 
ATOM   238 O OD2 . ASP A 1 34 ? 28.85843 15.57753  25.00252 1.000 15.26499  ? 34  ASP A OD2 1 
ATOM   239 N N   . ILE A 1 35 ? 25.48070 11.23645  25.56757 1.000 11.26714  ? 35  ILE A N   1 
ATOM   240 C CA  . ILE A 1 35 ? 24.32267 10.53346  26.11160 1.000 11.30136  ? 35  ILE A CA  1 
ATOM   241 C C   . ILE A 1 35 ? 24.72561 9.75920   27.36613 1.000 11.51717  ? 35  ILE A C   1 
ATOM   242 O O   . ILE A 1 35 ? 25.69115 8.98593   27.34893 1.000 12.60414  ? 35  ILE A O   1 
ATOM   243 C CB  . ILE A 1 35 ? 23.69916 9.62160   25.03957 1.000 12.18830  ? 35  ILE A CB  1 
ATOM   244 C CG1 . ILE A 1 35 ? 22.99291 10.48782  23.98980 1.000 13.84377  ? 35  ILE A CG1 1 
ATOM   245 C CG2 . ILE A 1 35 ? 22.72934 8.61981   25.65095 1.000 12.89891  ? 35  ILE A CG2 1 
ATOM   246 C CD1 . ILE A 1 35 ? 22.52689 9.74442   22.77835 1.000 14.89389  ? 35  ILE A CD1 1 
ATOM   247 N N   . ILE A 1 36 ? 23.96274 9.94396   28.44760 1.000 11.49348  ? 36  ILE A N   1 
ATOM   248 C CA  . ILE A 1 36 ? 24.22892 9.26425   29.71405 1.000 11.91195  ? 36  ILE A CA  1 
ATOM   249 C C   . ILE A 1 36 ? 23.25729 8.13237   30.01635 1.000 12.30411  ? 36  ILE A C   1 
ATOM   250 O O   . ILE A 1 36 ? 23.48573 7.38119   30.97687 1.000 13.82534  ? 36  ILE A O   1 
ATOM   251 C CB  . ILE A 1 36 ? 24.33429 10.24383  30.90512 1.000 13.20685  ? 36  ILE A CB  1 
ATOM   252 C CG1 . ILE A 1 36 ? 23.10742 11.16480  30.98739 1.000 14.74387  ? 36  ILE A CG1 1 
ATOM   253 C CG2 . ILE A 1 36 ? 25.65208 11.02752  30.83492 1.000 14.69387  ? 36  ILE A CG2 1 
ATOM   254 C CD1 . ILE A 1 36 ? 23.02702 11.97349  32.26833 1.000 16.61778  ? 36  ILE A CD1 1 
ATOM   255 N N   . ASP A 1 37 ? 22.19030 7.97768   29.24524 1.000 11.79615  ? 37  ASP A N   1 
ATOM   256 C CA  . ASP A 1 37 ? 21.31128 6.82939   29.40681 1.000 12.55414  ? 37  ASP A CA  1 
ATOM   257 C C   . ASP A 1 37 ? 20.55947 6.62962   28.10507 1.000 12.19620  ? 37  ASP A C   1 
ATOM   258 O O   . ASP A 1 37 ? 20.13334 7.59688   27.47864 1.000 12.51992  ? 37  ASP A O   1 
ATOM   259 C CB  . ASP A 1 37 ? 20.29582 7.03548   30.54171 1.000 14.34383  ? 37  ASP A CB  1 
ATOM   260 C CG  . ASP A 1 37 ? 19.53200 5.76670   30.87929 1.000 18.07059  ? 37  ASP A CG  1 
ATOM   261 O OD1 . ASP A 1 37 ? 20.15811 4.82221   31.38524 1.000 20.71038  ? 37  ASP A OD1 1 
ATOM   262 O OD2 . ASP A 1 37 ? 18.31039 5.70951   30.63368 1.000 19.60761  ? 37  ASP A OD2 1 
ATOM   263 N N   . CYS A 1 38 ? 20.38611 5.37877   27.71049 1.000 12.63046  ? 38  CYS A N   1 
ATOM   264 C CA  . CYS A 1 38 ? 19.59055 5.08953   26.52445 1.000 12.66731  ? 38  CYS A CA  1 
ATOM   265 C C   . CYS A 1 38 ? 19.03401 3.68741   26.65599 1.000 14.34909  ? 38  CYS A C   1 
ATOM   266 O O   . CYS A 1 38 ? 19.79975 2.72140   26.71026 1.000 16.89939  ? 38  CYS A O   1 
ATOM   267 C CB  . CYS A 1 38 ? 20.42242 5.22833   25.25015 1.000 15.25972  ? 38  CYS A CB  1 
ATOM   268 S SG  . CYS A 1 38 ? 19.45290 4.96042   23.75032 1.000 17.19153  ? 38  CYS A SG  1 
ATOM   269 N N   . VAL A 1 39 ? 17.71293 3.57494   26.71233 1.000 13.22527  ? 39  VAL A N   1 
ATOM   270 C CA  . VAL A 1 39 ? 17.06617 2.28208   26.86250 1.000 13.86219  ? 39  VAL A CA  1 
ATOM   271 C C   . VAL A 1 39 ? 15.96329 2.13500   25.83338 1.000 13.17263  ? 39  VAL A C   1 
ATOM   272 O O   . VAL A 1 39 ? 15.29918 3.10603   25.45427 1.000 14.35698  ? 39  VAL A O   1 
ATOM   273 C CB  . VAL A 1 39 ? 16.49619 2.07536   28.27764 1.000 16.26774  ? 39  VAL A CB  1 
ATOM   274 C CG1 . VAL A 1 39 ? 17.61778 2.04828   29.28905 1.000 19.76816  ? 39  VAL A CG1 1 
ATOM   275 C CG2 . VAL A 1 39 ? 15.47898 3.16235   28.61068 1.000 17.14153  ? 39  VAL A CG2 1 
ATOM   276 N N   . VAL A 1 40 ? 15.77789 0.89840   25.38154 1.000 12.69100  ? 40  VAL A N   1 
ATOM   277 C CA  . VAL A 1 40 ? 14.61554 0.48717   24.60790 1.000 12.93839  ? 40  VAL A CA  1 
ATOM   278 C C   . VAL A 1 40 ? 13.77323 -0.38764  25.52217 1.000 13.29633  ? 40  VAL A C   1 
ATOM   279 O O   . VAL A 1 40 ? 14.28337 -1.35163  26.10444 1.000 14.35962  ? 40  VAL A O   1 
ATOM   280 C CB  . VAL A 1 40 ? 15.02122 -0.25130  23.31977 1.000 14.12538  ? 40  VAL A CB  1 
ATOM   281 C CG1 . VAL A 1 40 ? 13.82533 -0.95406  22.70125 1.000 14.47805  ? 40  VAL A CG1 1 
ATOM   282 C CG2 . VAL A 1 40 ? 15.62263 0.72306   22.31816 1.000 16.08088  ? 40  VAL A CG2 1 
ATOM   283 N N   . MET A 1 41 ? 12.50121 -0.02619  25.68841 1.000 13.14894  ? 41  MET A N   1 
ATOM   284 C CA  . MET A 1 41 ? 11.65161 -0.75811  26.61670 1.000 13.87008  ? 41  MET A CA  1 
ATOM   285 C C   . MET A 1 41 ? 11.31365 -2.12477  26.03959 1.000 15.38606  ? 41  MET A C   1 
ATOM   286 O O   . MET A 1 41 ? 10.99016 -2.25415  24.85664 1.000 15.52555  ? 41  MET A O   1 
ATOM   287 C CB  . MET A 1 41 ? 10.37361 0.02896   26.89416 1.000 15.09128  ? 41  MET A CB  1 
ATOM   288 C CG  . MET A 1 41 ? 10.62216 1.42402   27.48015 1.000 17.22575  ? 41  MET A CG  1 
ATOM   289 S SD  . MET A 1 41 ? 11.65499 1.44366   28.96081 1.000 21.43415  ? 41  MET A SD  1 
ATOM   290 C CE  . MET A 1 41 ? 10.63554 0.48790   30.08010 1.000 24.66612  ? 41  MET A CE  1 
ATOM   291 N N   . LYS A 1 42 ? 11.39110 -3.14987  26.88432 1.000 16.32564  ? 42  LYS A N   1 
ATOM   292 C CA  . LYS A 1 42 ? 11.24252 -4.53710  26.46438 1.000 17.84951  ? 42  LYS A CA  1 
ATOM   293 C C   . LYS A 1 42 ? 10.03076 -5.17838  27.13532 1.000 19.01281  ? 42  LYS A C   1 
ATOM   294 O O   . LYS A 1 42 ? 9.67691  -4.85398  28.27653 1.000 18.99701  ? 42  LYS A O   1 
ATOM   295 C CB  . LYS A 1 42 ? 12.47270 -5.37452  26.85945 1.000 20.10504  ? 42  LYS A CB  1 
ATOM   296 C CG  . LYS A 1 42 ? 13.82506 -4.80841  26.47118 1.000 21.77630  ? 42  LYS A CG  1 
ATOM   297 C CD  . LYS A 1 42 ? 13.94973 -4.67668  24.97673 1.000 21.47626  ? 42  LYS A CD  1 
ATOM   298 C CE  . LYS A 1 42 ? 15.41871 -4.50109  24.54217 1.000 20.07346  ? 42  LYS A CE  1 
ATOM   299 N NZ  . LYS A 1 42 ? 16.14391 -3.41924  25.26725 1.000 19.83659  ? 42  LYS A NZ  1 
ATOM   300 N N   . ASN A 1 43 ? 9.41805  -6.12690  26.42865 1.000 21.21307  ? 43  ASN A N   1 
ATOM   301 C CA  . ASN A 1 43 ? 8.34561  -6.91944  27.01119 1.000 26.86112  ? 43  ASN A CA  1 
ATOM   302 C C   . ASN A 1 43 ? 8.91377  -7.80513  28.10952 1.000 31.60116  ? 43  ASN A C   1 
ATOM   303 O O   . ASN A 1 43 ? 9.93486  -8.47099  27.91702 1.000 30.85633  ? 43  ASN A O   1 
ATOM   304 C CB  . ASN A 1 43 ? 7.69717  -7.78424  25.93446 1.000 28.80082  ? 43  ASN A CB  1 
ATOM   305 C CG  . ASN A 1 43 ? 6.56808  -8.63166  26.47546 1.000 31.76170  ? 43  ASN A CG  1 
ATOM   306 O OD1 . ASN A 1 43 ? 6.80028  -9.68144  27.07167 1.000 34.39623  ? 43  ASN A OD1 1 
ATOM   307 N ND2 . ASN A 1 43 ? 5.33737  -8.17692  26.27629 1.000 31.87224  ? 43  ASN A ND2 1 
ATOM   308 N N   . ASN A 1 44 ? 8.24577  -7.81319  29.26458 1.000 37.05181  ? 44  ASN A N   1 
ATOM   309 C CA  . ASN A 1 44 ? 8.77661  -8.52762  30.42110 1.000 43.12359  ? 44  ASN A CA  1 
ATOM   310 C C   . ASN A 1 44 ? 8.89744  -10.02366 30.15180 1.000 45.02382  ? 44  ASN A C   1 
ATOM   311 O O   . ASN A 1 44 ? 9.88025  -10.65646 30.55577 1.000 45.60547  ? 44  ASN A O   1 
ATOM   312 C CB  . ASN A 1 44 ? 7.89545  -8.26333  31.64081 1.000 46.82930  ? 44  ASN A CB  1 
ATOM   313 C CG  . ASN A 1 44 ? 8.70116  -7.94045  32.87807 1.000 49.98757  ? 44  ASN A CG  1 
ATOM   314 O OD1 . ASN A 1 44 ? 9.74495  -8.54383  33.12811 1.000 51.37984  ? 44  ASN A OD1 1 
ATOM   315 N ND2 . ASN A 1 44 ? 8.22608  -6.97550  33.65770 1.000 51.01401  ? 44  ASN A ND2 1 
ATOM   316 N N   . GLU A 1 45 ? 7.91333  -10.60792 29.46730 1.000 46.20554  ? 45  GLU A N   1 
ATOM   317 C CA  . GLU A 1 45 ? 7.92040  -12.05229 29.25600 1.000 47.56623  ? 45  GLU A CA  1 
ATOM   318 C C   . GLU A 1 45 ? 8.84897  -12.45095 28.11452 1.000 45.79496  ? 45  GLU A C   1 
ATOM   319 O O   . GLU A 1 45 ? 9.65949  -13.37352 28.25699 1.000 46.76350  ? 45  GLU A O   1 
ATOM   320 C CB  . GLU A 1 45 ? 6.50054  -12.55937 28.99097 1.000 50.49816  ? 45  GLU A CB  1 
ATOM   321 C CG  . GLU A 1 45 ? 5.48206  -12.14620 30.03770 1.000 53.14058  ? 45  GLU A CG  1 
ATOM   322 C CD  . GLU A 1 45 ? 4.84523  -10.80699 29.72762 1.000 55.52771  ? 45  GLU A CD  1 
ATOM   323 O OE1 . GLU A 1 45 ? 4.11229  -10.71563 28.71926 1.000 56.48309  ? 45  GLU A OE1 1 
ATOM   324 O OE2 . GLU A 1 45 ? 5.08437  -9.84365  30.48515 1.000 56.25148  ? 45  GLU A OE2 1 
ATOM   325 N N   . SER A 1 46 ? 8.74772  -11.76479 26.97591 1.000 42.35245  ? 46  SER A N   1 
ATOM   326 C CA  . SER A 1 46 ? 9.46093  -12.17376 25.77326 1.000 38.95730  ? 46  SER A CA  1 
ATOM   327 C C   . SER A 1 46 ? 10.83052 -11.52879 25.62942 1.000 37.02812  ? 46  SER A C   1 
ATOM   328 O O   . SER A 1 46 ? 11.67887 -12.06876 24.90816 1.000 37.01760  ? 46  SER A O   1 
ATOM   329 C CB  . SER A 1 46 ? 8.63317  -11.84030 24.52950 1.000 38.38092  ? 46  SER A CB  1 
ATOM   330 O OG  . SER A 1 46 ? 8.59670  -10.43986 24.31127 1.000 37.70978  ? 46  SER A OG  1 
ATOM   331 N N   . GLY A 1 47 ? 11.06730 -10.39799 26.29024 1.000 34.00408  ? 47  GLY A N   1 
ATOM   332 C CA  . GLY A 1 47 ? 12.29360 -9.65647  26.10655 1.000 31.83803  ? 47  GLY A CA  1 
ATOM   333 C C   . GLY A 1 47 ? 12.36604 -8.85630  24.82660 1.000 29.04822  ? 47  GLY A C   1 
ATOM   334 O O   . GLY A 1 47 ? 13.37705 -8.18050  24.59525 1.000 29.41932  ? 47  GLY A O   1 
ATOM   335 N N   . ARG A 1 48 ? 11.32935 -8.89815  23.99372 1.000 27.65332  ? 48  ARG A N   1 
ATOM   336 C CA  . ARG A 1 48 ? 11.34188 -8.17532  22.73273 1.000 27.10062  ? 48  ARG A CA  1 
ATOM   337 C C   . ARG A 1 48 ? 11.04277 -6.69636  22.94354 1.000 22.20529  ? 48  ARG A C   1 
ATOM   338 O O   . ARG A 1 48 ? 10.30308 -6.30707  23.85063 1.000 21.47626  ? 48  ARG A O   1 
ATOM   339 C CB  . ARG A 1 48 ? 10.31607 -8.76634  21.76544 1.000 32.09859  ? 48  ARG A CB  1 
ATOM   340 C CG  . ARG A 1 48 ? 10.59768 -10.21763 21.38826 1.000 38.09404  ? 48  ARG A CG  1 
ATOM   341 C CD  . ARG A 1 48 ? 9.94355  -10.60289 20.06566 1.000 43.55522  ? 48  ARG A CD  1 
ATOM   342 N NE  . ARG A 1 48 ? 8.54320  -10.98425 20.21372 1.000 48.21104  ? 48  ARG A NE  1 
ATOM   343 C CZ  . ARG A 1 48 ? 8.12863  -12.20687 20.51876 1.000 51.64303  ? 48  ARG A CZ  1 
ATOM   344 N NH1 . ARG A 1 48 ? 8.98429  -13.18800 20.75702 1.000 52.83265  ? 48  ARG A NH1 1 
ATOM   345 N NH2 . ARG A 1 48 ? 6.82281  -12.45145 20.58851 1.000 52.73527  ? 48  ARG A NH2 1 
ATOM   346 N N   . SER A 1 49 ? 11.63129 -5.87257  22.08357 1.000 18.77594  ? 49  SER A N   1 
ATOM   347 C CA  . SER A 1 49 ? 11.36951 -4.44383  22.09952 1.000 17.16258  ? 49  SER A CA  1 
ATOM   348 C C   . SER A 1 49 ? 9.87907  -4.15596  21.97998 1.000 16.38618  ? 49  SER A C   1 
ATOM   349 O O   . SER A 1 49 ? 9.16648  -4.78900  21.19814 1.000 18.28903  ? 49  SER A O   1 
ATOM   350 C CB  . SER A 1 49 ? 12.08828 -3.78011  20.92626 1.000 16.55725  ? 49  SER A CB  1 
ATOM   351 O OG  . SER A 1 49 ? 11.63064 -2.44684  20.79286 1.000 15.03075  ? 49  SER A OG  1 
ATOM   352 N N   . ARG A 1 50 ? 9.42408  -3.16318  22.74027 1.000 15.11234  ? 50  ARG A N   1 
ATOM   353 C CA  . ARG A 1 50 ? 8.07551  -2.62970  22.64648 1.000 15.94665  ? 50  ARG A CA  1 
ATOM   354 C C   . ARG A 1 50 ? 7.97396  -1.47612  21.65196 1.000 15.50975  ? 50  ARG A C   1 
ATOM   355 O O   . ARG A 1 50 ? 6.90374  -0.87045  21.54065 1.000 16.85202  ? 50  ARG A O   1 
ATOM   356 C CB  . ARG A 1 50 ? 7.58693  -2.19364  24.03716 1.000 15.97034  ? 50  ARG A CB  1 
ATOM   357 C CG  . ARG A 1 50 ? 7.54044  -3.34017  25.02703 1.000 16.50987  ? 50  ARG A CG  1 
ATOM   358 C CD  . ARG A 1 50 ? 7.24057  -2.89644  26.44716 1.000 16.54146  ? 50  ARG A CD  1 
ATOM   359 N NE  . ARG A 1 50 ? 5.98704  -2.15682  26.53191 1.000 15.77294  ? 50  ARG A NE  1 
ATOM   360 C CZ  . ARG A 1 50 ? 5.70234  -1.25967  27.46916 1.000 15.25972  ? 50  ARG A CZ  1 
ATOM   361 N NH1 . ARG A 1 50 ? 6.54978  -0.98685  28.45173 1.000 16.13088  ? 50  ARG A NH1 1 
ATOM   362 N NH2 . ARG A 1 50 ? 4.55656  -0.59173  27.39834 1.000 16.10193  ? 50  ARG A NH2 1 
ATOM   363 N N   . GLY A 1 51 ? 9.05662  -1.14785  20.94278 1.000 14.75177  ? 51  GLY A N   1 
ATOM   364 C CA  . GLY A 1 51 ? 9.00357  -0.13977  19.89818 1.000 15.14392  ? 51  GLY A CA  1 
ATOM   365 C C   . GLY A 1 51 ? 9.15481  1.29254   20.36220 1.000 13.93588  ? 51  GLY A C   1 
ATOM   366 O O   . GLY A 1 51 ? 8.83246  2.20782   19.59582 1.000 14.21223  ? 51  GLY A O   1 
ATOM   367 N N   . PHE A 1 52 ? 9.61324  1.52174   21.59348 1.000 13.33844  ? 52  PHE A N   1 
ATOM   368 C CA  . PHE A 1 52 ? 9.88908  2.86916   22.06909 1.000 13.17000  ? 52  PHE A CA  1 
ATOM   369 C C   . PHE A 1 52 ? 10.99876 2.80255   23.10179 1.000 12.58572  ? 52  PHE A C   1 
ATOM   370 O O   . PHE A 1 52 ? 11.28722 1.73822   23.65627 1.000 12.78311  ? 52  PHE A O   1 
ATOM   371 C CB  . PHE A 1 52 ? 8.63507  3.58149   22.60119 1.000 13.61479  ? 52  PHE A CB  1 
ATOM   372 C CG  . PHE A 1 52 ? 8.09889  3.03265   23.90164 1.000 13.28580  ? 52  PHE A CG  1 
ATOM   373 C CD1 . PHE A 1 52 ? 7.27348  1.92172   23.91698 1.000 14.40436  ? 52  PHE A CD1 1 
ATOM   374 C CD2 . PHE A 1 52 ? 8.39287  3.65567   25.10838 1.000 14.18328  ? 52  PHE A CD2 1 
ATOM   375 C CE1 . PHE A 1 52 ? 6.75659  1.43112   25.11525 1.000 16.30985  ? 52  PHE A CE1 1 
ATOM   376 C CE2 . PHE A 1 52 ? 7.86803  3.17967   26.30653 1.000 15.20445  ? 52  PHE A CE2 1 
ATOM   377 C CZ  . PHE A 1 52 ? 7.05442  2.05682   26.30817 1.000 15.55976  ? 52  PHE A CZ  1 
ATOM   378 N N   . GLY A 1 53 ? 11.62595 3.94703   23.33478 1.000 12.11724  ? 53  GLY A N   1 
ATOM   379 C CA  . GLY A 1 53 ? 12.72428 4.03493   24.26722 1.000 12.44623  ? 53  GLY A CA  1 
ATOM   380 C C   . GLY A 1 53 ? 12.88100 5.44242   24.78518 1.000 11.47506  ? 53  GLY A C   1 
ATOM   381 O O   . GLY A 1 53 ? 12.05478 6.31964   24.51754 1.000 11.45927  ? 53  GLY A O   1 
ATOM   382 N N   . PHE A 1 54 ? 13.98309 5.64575   25.50512 1.000 10.94868  ? 54  PHE A N   1 
ATOM   383 C CA  . PHE A 1 54 ? 14.29029 6.93147   26.11207 1.000 11.24609  ? 54  PHE A CA  1 
ATOM   384 C C   . PHE A 1 54 ? 15.77802 7.19802   25.99163 1.000 11.24872  ? 54  PHE A C   1 
ATOM   385 O O   . PHE A 1 54 ? 16.59214 6.30140   26.22874 1.000 12.71995  ? 54  PHE A O   1 
ATOM   386 C CB  . PHE A 1 54 ? 13.91776 6.95450   27.60059 1.000 11.89880  ? 54  PHE A CB  1 
ATOM   387 C CG  . PHE A 1 54 ? 12.45279 6.72278   27.85840 1.000 11.72772  ? 54  PHE A CG  1 
ATOM   388 C CD1 . PHE A 1 54 ? 11.55013 7.78714   27.88966 1.000 11.76720  ? 54  PHE A CD1 1 
ATOM   389 C CD2 . PHE A 1 54 ? 11.97294 5.44412   28.08324 1.000 13.09368  ? 54  PHE A CD2 1 
ATOM   390 C CE1 . PHE A 1 54 ? 10.20003 7.57090   28.11983 1.000 12.57782  ? 54  PHE A CE1 1 
ATOM   391 C CE2 . PHE A 1 54 ? 10.62454 5.24052   28.30381 1.000 13.91483  ? 54  PHE A CE2 1 
ATOM   392 C CZ  . PHE A 1 54 ? 9.74759  6.30426   28.33179 1.000 13.34897  ? 54  PHE A CZ  1 
ATOM   393 N N   . VAL A 1 55 ? 16.11432 8.44066   25.65388 1.000 11.05659  ? 55  VAL A N   1 
ATOM   394 C CA  . VAL A 1 55 ? 17.48811 8.91402   25.55410 1.000 11.76457  ? 55  VAL A CA  1 
ATOM   395 C C   . VAL A 1 55 ? 17.64171 10.05674  26.54769 1.000 11.43558  ? 55  VAL A C   1 
ATOM   396 O O   . VAL A 1 55 ? 16.82779 10.98454  26.54694 1.000 12.78838  ? 55  VAL A O   1 
ATOM   397 C CB  . VAL A 1 55 ? 17.77287 9.41985   24.12669 1.000 13.71480  ? 55  VAL A CB  1 
ATOM   398 C CG1 . VAL A 1 55 ? 19.13715 10.07750  24.05979 1.000 15.25709  ? 55  VAL A CG1 1 
ATOM   399 C CG2 . VAL A 1 55 ? 17.64969 8.28650   23.11970 1.000 16.64673  ? 55  VAL A CG2 1 
ATOM   400 N N   . THR A 1 56 ? 18.68792 10.01301  27.37261 1.000 11.36978  ? 56  THR A N   1 
ATOM   401 C CA  . THR A 1 56 ? 18.99061 11.10928  28.28804 1.000 11.92511  ? 56  THR A CA  1 
ATOM   402 C C   . THR A 1 56 ? 20.31407 11.73907  27.89517 1.000 11.08817  ? 56  THR A C   1 
ATOM   403 O O   . THR A 1 56 ? 21.35425 11.07268  27.92303 1.000 11.59613  ? 56  THR A O   1 
ATOM   404 C CB  . THR A 1 56 ? 19.04163 10.63513  29.73590 1.000 13.72270  ? 56  THR A CB  1 
ATOM   405 O OG1 . THR A 1 56 ? 17.80221 10.00302  30.05665 1.000 14.84652  ? 56  THR A OG1 1 
ATOM   406 C CG2 . THR A 1 56 ? 19.26584 11.81607  30.67088 1.000 14.97811  ? 56  THR A CG2 1 
ATOM   407 N N   . PHE A 1 57 ? 20.26618 13.02265  27.54595 1.000 11.12502  ? 57  PHE A N   1 
ATOM   408 C CA  . PHE A 1 57 ? 21.46905 13.77420  27.24002 1.000 11.53559  ? 57  PHE A CA  1 
ATOM   409 C C   . PHE A 1 57 ? 22.11761 14.29269  28.51174 1.000 11.40926  ? 57  PHE A C   1 
ATOM   410 O O   . PHE A 1 57 ? 21.43778 14.69623  29.45496 1.000 13.43845  ? 57  PHE A O   1 
ATOM   411 C CB  . PHE A 1 57 ? 21.12699 14.94515  26.32149 1.000 12.04355  ? 57  PHE A CB  1 
ATOM   412 C CG  . PHE A 1 57 ? 20.79219 14.52037  24.92219 1.000 11.80668  ? 57  PHE A CG  1 
ATOM   413 C CD1 . PHE A 1 57 ? 21.80243 14.18232  24.03348 1.000 12.50413  ? 57  PHE A CD1 1 
ATOM   414 C CD2 . PHE A 1 57 ? 19.48307 14.42628  24.49934 1.000 13.44898  ? 57  PHE A CD2 1 
ATOM   415 C CE1 . PHE A 1 57 ? 21.51880 13.77042  22.73581 1.000 12.90155  ? 57  PHE A CE1 1 
ATOM   416 C CE2 . PHE A 1 57 ? 19.19127 14.02698  23.20322 1.000 14.48595  ? 57  PHE A CE2 1 
ATOM   417 C CZ  . PHE A 1 57 ? 20.20715 13.69838  22.32606 1.000 14.37804  ? 57  PHE A CZ  1 
ATOM   418 N N   . ALA A 1 58 ? 23.44808 14.28318  28.52133 1.000 12.06724  ? 58  ALA A N   1 
ATOM   419 C CA  . ALA A 1 58 ? 24.18658 14.89430  29.61864 1.000 13.35423  ? 58  ALA A CA  1 
ATOM   420 C C   . ALA A 1 58 ? 23.86443 16.37854  29.73670 1.000 13.56478  ? 58  ALA A C   1 
ATOM   421 O O   . ALA A 1 58 ? 23.76362 16.91528  30.84828 1.000 15.72557  ? 58  ALA A O   1 
ATOM   422 C CB  . ALA A 1 58 ? 25.68092 14.69344  29.38550 1.000 14.80177  ? 58  ALA A CB  1 
ATOM   423 N N   . ASP A 1 59 ? 23.72711 17.06099  28.60013 1.000 13.53057  ? 59  ASP A N   1 
ATOM   424 C CA  . ASP A 1 59 ? 23.45702 18.49259  28.55237 1.000 13.58321  ? 59  ASP A CA  1 
ATOM   425 C C   . ASP A 1 59 ? 22.01688 18.66872  28.10233 1.000 13.74639  ? 59  ASP A C   1 
ATOM   426 O O   . ASP A 1 59 ? 21.69444 18.35459  26.94346 1.000 13.05683  ? 59  ASP A O   1 
ATOM   427 C CB  . ASP A 1 59 ? 24.41543 19.15136  27.55508 1.000 14.40436  ? 59  ASP A CB  1 
ATOM   428 C CG  . ASP A 1 59 ? 24.28056 20.66771  27.49677 1.000 15.24920  ? 59  ASP A CG  1 
ATOM   429 O OD1 . ASP A 1 59 ? 23.19086 21.20191  27.81572 1.000 15.49396  ? 59  ASP A OD1 1 
ATOM   430 O OD2 . ASP A 1 59 ? 25.27699 21.32773  27.11405 1.000 16.49671  ? 59  ASP A OD2 1 
ATOM   431 N N   . PRO A 1 60 ? 21.12466 19.15659  28.97268 1.000 14.55438  ? 60  PRO A N   1 
ATOM   432 C CA  . PRO A 1 60 ? 19.69672 19.19725  28.61886 1.000 14.75703  ? 60  PRO A CA  1 
ATOM   433 C C   . PRO A 1 60 ? 19.36923 20.12170  27.47051 1.000 15.08076  ? 60  PRO A C   1 
ATOM   434 O O   . PRO A 1 60 ? 18.29274 19.97355  26.87339 1.000 15.77558  ? 60  PRO A O   1 
ATOM   435 C CB  . PRO A 1 60 ? 19.02158 19.65348  29.91701 1.000 16.98625  ? 60  PRO A CB  1 
ATOM   436 C CG  . PRO A 1 60 ? 20.09991 20.40022  30.64010 1.000 18.86542  ? 60  PRO A CG  1 
ATOM   437 C CD  . PRO A 1 60 ? 21.35712 19.62733  30.34816 1.000 16.51777  ? 60  PRO A CD  1 
ATOM   438 N N   . THR A 1 61 ? 20.24942 21.07479  27.14772 1.000 15.02285  ? 61  THR A N   1 
ATOM   439 C CA  . THR A 1 61 ? 19.99587 21.94275  26.00743 1.000 16.49145  ? 61  THR A CA  1 
ATOM   440 C C   . THR A 1 61 ? 20.00457 21.17843  24.69082 1.000 16.23879  ? 61  THR A C   1 
ATOM   441 O O   . THR A 1 61 ? 19.51108 21.69215  23.68324 1.000 17.46788  ? 61  THR A O   1 
ATOM   442 C CB  . THR A 1 61 ? 20.98725 23.11360  25.95375 1.000 18.17586  ? 61  THR A CB  1 
ATOM   443 O OG1 . THR A 1 61 ? 22.30968 22.63899  25.66754 1.000 19.32600  ? 61  THR A OG1 1 
ATOM   444 C CG2 . THR A 1 61 ? 20.98914 23.89350  27.26046 1.000 18.88384  ? 61  THR A CG2 1 
ATOM   445 N N   . ASN A 1 62 ? 20.54656 19.95903  24.67076 1.000 15.05707  ? 62  ASN A N   1 
ATOM   446 C CA  . ASN A 1 62 ? 20.57543 19.20313  23.42508 1.000 14.89126  ? 62  ASN A CA  1 
ATOM   447 C C   . ASN A 1 62 ? 19.21973 18.61938  23.03555 1.000 14.04116  ? 62  ASN A C   1 
ATOM   448 O O   . ASN A 1 62 ? 19.03074 18.26172  21.86684 1.000 14.62807  ? 62  ASN A O   1 
ATOM   449 C CB  . ASN A 1 62 ? 21.67227 18.13568  23.46213 1.000 14.27013  ? 62  ASN A CB  1 
ATOM   450 C CG  . ASN A 1 62 ? 23.07069 18.74051  23.50007 1.000 15.42817  ? 62  ASN A CG  1 
ATOM   451 O OD1 . ASN A 1 62 ? 23.99194 18.19332  24.12744 1.000 16.96782  ? 62  ASN A OD1 1 
ATOM   452 N ND2 . ASN A 1 62 ? 23.23705 19.87289  22.82995 1.000 16.21247  ? 62  ASN A ND2 1 
ATOM   453 N N   . VAL A 1 63 ? 18.26192 18.54320  23.95777 1.000 12.93839  ? 63  VAL A N   1 
ATOM   454 C CA  . VAL A 1 63 ? 16.93925 18.04357  23.59159 1.000 13.08841  ? 63  VAL A CA  1 
ATOM   455 C C   . VAL A 1 63 ? 16.32088 18.90448  22.48911 1.000 12.88312  ? 63  VAL A C   1 
ATOM   456 O O   . VAL A 1 63 ? 15.83590 18.38799  21.47285 1.000 13.30423  ? 63  VAL A O   1 
ATOM   457 C CB  . VAL A 1 63 ? 16.03779 17.93139  24.83444 1.000 13.87008  ? 63  VAL A CB  1 
ATOM   458 C CG1 . VAL A 1 63 ? 14.57806 17.69087  24.43440 1.000 15.53607  ? 63  VAL A CG1 1 
ATOM   459 C CG2 . VAL A 1 63 ? 16.53736 16.81478  25.75022 1.000 15.06760  ? 63  VAL A CG2 1 
ATOM   460 N N   . ASN A 1 64 ? 16.33693 20.23082  22.66171 1.000 14.24644  ? 64  ASN A N   1 
ATOM   461 C CA  . ASN A 1 64 ? 15.73931 21.09062  21.64361 1.000 16.33880  ? 64  ASN A CA  1 
ATOM   462 C C   . ASN A 1 64 ? 16.47010 20.97165  20.31763 1.000 15.05180  ? 64  ASN A C   1 
ATOM   463 O O   . ASN A 1 64 ? 15.85538 21.11853  19.25364 1.000 15.48607  ? 64  ASN A O   1 
ATOM   464 C CB  . ASN A 1 64 ? 15.70757 22.55038  22.10001 1.000 20.56826  ? 64  ASN A CB  1 
ATOM   465 C CG  . ASN A 1 64 ? 14.59368 22.83345  23.09234 1.000 26.91112  ? 64  ASN A CG  1 
ATOM   466 O OD1 . ASN A 1 64 ? 13.63578 22.06941  23.20142 1.000 29.15876  ? 64  ASN A OD1 1 
ATOM   467 N ND2 . ASN A 1 64 ? 14.70822 23.94585  23.81086 1.000 29.74830  ? 64  ASN A ND2 1 
ATOM   468 N N   . HIS A 1 65 ? 17.78116 20.72338  20.35880 1.000 14.21223  ? 65  HIS A N   1 
ATOM   469 C CA  . HIS A 1 65 ? 18.52848 20.54374  19.12148 1.000 14.17538  ? 65  HIS A CA  1 
ATOM   470 C C   . HIS A 1 65 ? 18.02160 19.33480  18.33622 1.000 13.47530  ? 65  HIS A C   1 
ATOM   471 O O   . HIS A 1 65 ? 17.90913 19.39077  17.10499 1.000 14.09643  ? 65  HIS A O   1 
ATOM   472 C CB  . HIS A 1 65 ? 20.02230 20.44790  19.41180 1.000 14.67281  ? 65  HIS A CB  1 
ATOM   473 C CG  . HIS A 1 65 ? 20.55081 21.59180  20.21960 1.000 14.88336  ? 65  HIS A CG  1 
ATOM   474 N ND1 . HIS A 1 65 ? 21.80102 21.57008  20.79742 1.000 15.29920  ? 65  HIS A ND1 1 
ATOM   475 C CD2 . HIS A 1 65 ? 20.00655 22.78895  20.54903 1.000 15.13603  ? 65  HIS A CD2 1 
ATOM   476 C CE1 . HIS A 1 65 ? 22.00401 22.69872  21.45314 1.000 14.95179  ? 65  HIS A CE1 1 
ATOM   477 N NE2 . HIS A 1 65 ? 20.92954 23.45470  21.32095 1.000 15.65714  ? 65  HIS A NE2 1 
ATOM   478 N N   . VAL A 1 66 ? 17.70938 18.23018  19.02541 1.000 12.87786  ? 66  VAL A N   1 
ATOM   479 C CA  . VAL A 1 66 ? 17.09228 17.09399  18.34773 1.000 12.48044  ? 66  VAL A CA  1 
ATOM   480 C C   . VAL A 1 66 ? 15.79677 17.53360  17.68286 1.000 12.15935  ? 66  VAL A C   1 
ATOM   481 O O   . VAL A 1 66 ? 15.54958 17.25634  16.49688 1.000 12.39622  ? 66  VAL A O   1 
ATOM   482 C CB  . VAL A 1 66 ? 16.82258 15.95172  19.34296 1.000 13.06736  ? 66  VAL A CB  1 
ATOM   483 C CG1 . VAL A 1 66 ? 15.99646 14.85559  18.66296 1.000 12.90418  ? 66  VAL A CG1 1 
ATOM   484 C CG2 . VAL A 1 66 ? 18.11746 15.39175  19.92375 1.000 14.65702  ? 66  VAL A CG2 1 
ATOM   485 N N   . LEU A 1 67 ? 14.93594 18.21383  18.44984 1.000 12.76206  ? 67  LEU A N   1 
ATOM   486 C CA  . LEU A 1 67 ? 13.57163 18.47137  18.00202 1.000 13.46477  ? 67  LEU A CA  1 
ATOM   487 C C   . LEU A 1 67 ? 13.54172 19.37980  16.78235 1.000 13.98852  ? 67  LEU A C   1 
ATOM   488 O O   . LEU A 1 67 ? 12.65392 19.24234  15.93462 1.000 15.80979  ? 67  LEU A O   1 
ATOM   489 C CB  . LEU A 1 67 ? 12.75484 19.08413  19.13661 1.000 14.56227  ? 67  LEU A CB  1 
ATOM   490 C CG  . LEU A 1 67 ? 12.68407 18.22204  20.40455 1.000 16.53619  ? 67  LEU A CG  1 
ATOM   491 C CD1 . LEU A 1 67 ? 11.92834 18.95495  21.49245 1.000 18.03111  ? 67  LEU A CD1 1 
ATOM   492 C CD2 . LEU A 1 67 ? 12.04439 16.87154  20.12127 1.000 17.00204  ? 67  LEU A CD2 1 
ATOM   493 N N   . GLN A 1 68 ? 14.49256 20.30650  16.66281 1.000 13.85429  ? 68  GLN A N   1 
ATOM   494 C CA  . GLN A 1 68 ? 14.45812 21.24040  15.55014 1.000 14.87020  ? 68  GLN A CA  1 
ATOM   495 C C   . GLN A 1 68 ? 15.20053 20.74221  14.31696 1.000 13.94904  ? 68  GLN A C   1 
ATOM   496 O O   . GLN A 1 68 ? 15.18662 21.42431  13.28676 1.000 14.16222  ? 68  GLN A O   1 
ATOM   497 C CB  . GLN A 1 68 ? 14.91834 22.62675  15.98587 1.000 18.43905  ? 68  GLN A CB  1 
ATOM   498 C CG  . GLN A 1 68 ? 16.32546 22.72311  16.44234 1.000 21.51311  ? 68  GLN A CG  1 
ATOM   499 C CD  . GLN A 1 68 ? 16.59730 24.05353  17.13465 1.000 22.86064  ? 68  GLN A CD  1 
ATOM   500 O OE1 . GLN A 1 68 ? 15.67435 24.82130  17.43039 1.000 24.04236  ? 68  GLN A OE1 1 
ATOM   501 N NE2 . GLN A 1 68 ? 17.86324 24.33602  17.38667 1.000 21.96053  ? 68  GLN A NE2 1 
ATOM   502 N N   . ASN A 1 69 ? 15.77419 19.54476  14.37030 1.000 12.79101  ? 69  ASN A N   1 
ATOM   503 C CA  . ASN A 1 69 ? 16.55640 19.00341  13.26743 1.000 12.67784  ? 69  ASN A CA  1 
ATOM   504 C C   . ASN A 1 69 ? 15.96053 17.71536  12.71112 1.000 13.82797  ? 69  ASN A C   1 
ATOM   505 O O   . ASN A 1 69 ? 16.68872 16.83009  12.25081 1.000 15.09918  ? 69  ASN A O   1 
ATOM   506 C CB  . ASN A 1 69 ? 18.01618 18.80999  13.67566 1.000 12.99893  ? 69  ASN A CB  1 
ATOM   507 C CG  . ASN A 1 69 ? 18.77147 20.11327  13.72448 1.000 13.37002  ? 69  ASN A CG  1 
ATOM   508 O OD1 . ASN A 1 69 ? 18.84782 20.82627  12.72363 1.000 13.88588  ? 69  ASN A OD1 1 
ATOM   509 N ND2 . ASN A 1 69 ? 19.31075 20.44699  14.89641 1.000 15.39132  ? 69  ASN A ND2 1 
ATOM   510 N N   . GLY A 1 70 ? 14.63564 17.59192  12.75487 1.000 14.44910  ? 70  GLY A N   1 
ATOM   511 C CA  . GLY A 1 70 ? 13.96343 16.45142  12.17731 1.000 15.54397  ? 70  GLY A CA  1 
ATOM   512 C C   . GLY A 1 70 ? 13.67872 16.67349  10.70415 1.000 16.79412  ? 70  GLY A C   1 
ATOM   513 O O   . GLY A 1 70 ? 14.06004 17.69379  10.12309 1.000 18.85752  ? 70  GLY A O   1 
ATOM   514 N N   . PRO A 1 71 ? 13.00205 15.71879  10.06471 1.000 18.17586  ? 71  PRO A N   1 
ATOM   515 C CA  . PRO A 1 71 ? 12.52738 14.45504  10.63607 1.000 18.18113  ? 71  PRO A CA  1 
ATOM   516 C C   . PRO A 1 71 ? 13.67456 13.49272  10.87806 1.000 16.85728  ? 71  PRO A C   1 
ATOM   517 O O   . PRO A 1 71 ? 14.77002 13.64200  10.33760 1.000 18.44695  ? 71  PRO A O   1 
ATOM   518 C CB  . PRO A 1 71 ? 11.57167 13.92499  9.56130  1.000 20.40508  ? 71  PRO A CB  1 
ATOM   519 C CG  . PRO A 1 71 ? 12.15130 14.44814  8.28632  1.000 21.88683  ? 71  PRO A CG  1 
ATOM   520 C CD  . PRO A 1 71 ? 12.68050 15.82407  8.62882  1.000 20.22611  ? 71  PRO A CD  1 
ATOM   521 N N   . HIS A 1 72 ? 13.42744 12.48486  11.70437 1.000 14.91495  ? 72  HIS A N   1 
ATOM   522 C CA  . HIS A 1 72 ? 14.43998 11.51622  12.08526 1.000 14.56754  ? 72  HIS A CA  1 
ATOM   523 C C   . HIS A 1 72 ? 14.02792 10.14461  11.58913 1.000 15.77294  ? 72  HIS A C   1 
ATOM   524 O O   . HIS A 1 72 ? 12.88603 9.72201   11.79917 1.000 16.26248  ? 72  HIS A O   1 
ATOM   525 C CB  . HIS A 1 72 ? 14.56840 11.48141  13.59916 1.000 14.85704  ? 72  HIS A CB  1 
ATOM   526 C CG  . HIS A 1 72 ? 14.95182 12.80274  14.17420 1.000 13.91746  ? 72  HIS A CG  1 
ATOM   527 N ND1 . HIS A 1 72 ? 16.25925 13.23526  14.22359 1.000 15.28078  ? 72  HIS A ND1 1 
ATOM   528 C CD2 . HIS A 1 72 ? 14.19991 13.80557  14.68683 1.000 14.03326  ? 72  HIS A CD2 1 
ATOM   529 C CE1 . HIS A 1 72 ? 16.29608 14.44505  14.75221 1.000 15.77558  ? 72  HIS A CE1 1 
ATOM   530 N NE2 . HIS A 1 72 ? 15.06018 14.81489  15.03872 1.000 14.85441  ? 72  HIS A NE2 1 
ATOM   531 N N   . THR A 1 73 ? 14.95280 9.45865   10.92812 1.000 16.65989  ? 73  THR A N   1 
ATOM   532 C CA  . THR A 1 73 ? 14.72195 8.10556   10.45168 1.000 17.51789  ? 73  THR A CA  1 
ATOM   533 C C   . THR A 1 73 ? 15.77724 7.18389   11.03998 1.000 16.04929  ? 73  THR A C   1 
ATOM   534 O O   . THR A 1 73 ? 16.95050 7.56086   11.17157 1.000 17.89162  ? 73  THR A O   1 
ATOM   535 C CB  . THR A 1 73 ? 14.74163 8.02801   8.92284  1.000 21.47363  ? 73  THR A CB  1 
ATOM   536 O OG1 . THR A 1 73 ? 16.00325 8.48773   8.43734  1.000 26.03470  ? 73  THR A OG1 1 
ATOM   537 C CG2 . THR A 1 73 ? 13.64647 8.88396   8.32634  1.000 22.07370  ? 73  THR A CG2 1 
ATOM   538 N N   . LEU A 1 74 ? 15.34293 5.99004   11.42746 1.000 14.26487  ? 74  LEU A N   1 
ATOM   539 C CA  . LEU A 1 74 ? 16.25053 4.99170   11.97024 1.000 14.13064  ? 74  LEU A CA  1 
ATOM   540 C C   . LEU A 1 74 ? 15.71329 3.62499   11.58238 1.000 13.93588  ? 74  LEU A C   1 
ATOM   541 O O   . LEU A 1 74 ? 14.53610 3.33362   11.82878 1.000 14.37541  ? 74  LEU A O   1 
ATOM   542 C CB  . LEU A 1 74 ? 16.33593 5.12144   13.49387 1.000 14.75177  ? 74  LEU A CB  1 
ATOM   543 C CG  . LEU A 1 74 ? 17.34115 4.22846   14.21830 1.000 15.18866  ? 74  LEU A CG  1 
ATOM   544 C CD1 . LEU A 1 74 ? 18.75304 4.41238   13.66408 1.000 16.49408  ? 74  LEU A CD1 1 
ATOM   545 C CD2 . LEU A 1 74 ? 17.30824 4.53417   15.70190 1.000 16.26774  ? 74  LEU A CD2 1 
ATOM   546 N N   . ASP A 1 75 ? 16.56334 2.81327   10.94787 1.000 14.16222  ? 75  ASP A N   1 
ATOM   547 C CA  . ASP A 1 75 ? 16.16490 1.47579   10.50419 1.000 15.84664  ? 75  ASP A CA  1 
ATOM   548 C C   . ASP A 1 75 ? 14.91719 1.52441   9.62138  1.000 17.33366  ? 75  ASP A C   1 
ATOM   549 O O   . ASP A 1 75 ? 14.04041 0.65931   9.69009  1.000 19.32600  ? 75  ASP A O   1 
ATOM   550 C CB  . ASP A 1 75 ? 15.98361 0.53088   11.69179 1.000 16.02561  ? 75  ASP A CB  1 
ATOM   551 C CG  . ASP A 1 75 ? 17.28524 0.24210   12.40667 1.000 16.66252  ? 75  ASP A CG  1 
ATOM   552 O OD1 . ASP A 1 75 ? 18.35230 0.26400   11.75492 1.000 18.61276  ? 75  ASP A OD1 1 
ATOM   553 O OD2 . ASP A 1 75 ? 17.23520 -0.03967  13.62123 1.000 17.00204  ? 75  ASP A OD2 1 
ATOM   554 N N   . GLY A 1 76 ? 14.84045 2.54370   8.77076  1.000 18.25745  ? 76  GLY A N   1 
ATOM   555 C CA  . GLY A 1 76 ? 13.76354 2.64305   7.80694  1.000 19.94713  ? 76  GLY A CA  1 
ATOM   556 C C   . GLY A 1 76 ? 12.44954 3.16228   8.35122  1.000 20.00240  ? 76  GLY A C   1 
ATOM   557 O O   . GLY A 1 76 ? 11.46270 3.19727   7.60959  1.000 22.86853  ? 76  GLY A O   1 
ATOM   558 N N   . ARG A 1 77 ? 12.39207 3.55235   9.61916  1.000 18.72067  ? 77  ARG A N   1 
ATOM   559 C CA  . ARG A 1 77 ? 11.18586 4.10330   10.21916 1.000 17.88899  ? 77  ARG A CA  1 
ATOM   560 C C   . ARG A 1 77 ? 11.38688 5.58500   10.49506 1.000 16.54935  ? 77  ARG A C   1 
ATOM   561 O O   . ARG A 1 77 ? 12.47256 6.00447   10.90222 1.000 16.56778  ? 77  ARG A O   1 
ATOM   562 C CB  . ARG A 1 77 ? 10.88772 3.41946   11.55827 1.000 20.38402  ? 77  ARG A CB  1 
ATOM   563 C CG  . ARG A 1 77 ? 10.62074 1.92985   11.46953 1.000 25.43989  ? 77  ARG A CG  1 
ATOM   564 C CD  . ARG A 1 77 ? 9.23963  1.65444   10.89488 1.000 31.15374  ? 77  ARG A CD  1 
ATOM   565 N NE  . ARG A 1 77 ? 8.70970  0.37903   11.36451 1.000 36.99654  ? 77  ARG A NE  1 
ATOM   566 C CZ  . ARG A 1 77 ? 7.96594  0.23330   12.45358 1.000 40.62066  ? 77  ARG A CZ  1 
ATOM   567 N NH1 . ARG A 1 77 ? 7.63937  1.26762   13.21264 1.000 41.66289  ? 77  ARG A NH1 1 
ATOM   568 N NH2 . ARG A 1 77 ? 7.53648  -0.97998  12.78826 1.000 41.99714  ? 77  ARG A NH2 1 
ATOM   569 N N   . THR A 1 78 ? 10.33419 6.37492   10.30785 1.000 16.12562  ? 78  THR A N   1 
ATOM   570 C CA  . THR A 1 78 ? 10.32855 7.73800   10.82269 1.000 16.63884  ? 78  THR A CA  1 
ATOM   571 C C   . THR A 1 78 ? 9.99906  7.66120   12.30831 1.000 15.74662  ? 78  THR A C   1 
ATOM   572 O O   . THR A 1 78 ? 8.91688  7.19799   12.68927 1.000 17.38893  ? 78  THR A O   1 
ATOM   573 C CB  . THR A 1 78 ? 9.29724  8.58278   10.07842 1.000 18.86805  ? 78  THR A CB  1 
ATOM   574 O OG1 . THR A 1 78 ? 9.62633  8.64560   8.68342  1.000 21.08411  ? 78  THR A OG1 1 
ATOM   575 C CG2 . THR A 1 78 ? 9.27692  9.99457   10.63410 1.000 19.37338  ? 78  THR A CG2 1 
ATOM   576 N N   . ILE A 1 79 ? 10.93839 8.06356   13.15154 1.000 13.86219  ? 79  ILE A N   1 
ATOM   577 C CA  . ILE A 1 79 ? 10.79220 7.89942   14.58095 1.000 13.61479  ? 79  ILE A CA  1 
ATOM   578 C C   . ILE A 1 79 ? 10.30381 9.20439   15.19041 1.000 13.79113  ? 79  ILE A C   1 
ATOM   579 O O   . ILE A 1 79 ? 10.26291 10.24139  14.53680 1.000 15.33342  ? 79  ILE A O   1 
ATOM   580 C CB  . ILE A 1 79 ? 12.06621 7.32282   15.23568 1.000 13.64111  ? 79  ILE A CB  1 
ATOM   581 C CG1 . ILE A 1 79 ? 13.25400 8.27972   15.07136 1.000 13.84113  ? 79  ILE A CG1 1 
ATOM   582 C CG2 . ILE A 1 79 ? 12.35765 5.95341   14.62060 1.000 13.78850  ? 79  ILE A CG2 1 
ATOM   583 C CD1 . ILE A 1 79 ? 14.52643 7.82092   15.74649 1.000 14.41489  ? 79  ILE A CD1 1 
ATOM   584 N N   . ASP A 1 80 ? 9.93966  9.16917   16.47025 1.000 13.62005  ? 80  ASP A N   1 
ATOM   585 C CA  . ASP A 1 80 ? 9.14756  10.23592  17.07938 1.000 14.00431  ? 80  ASP A CA  1 
ATOM   586 C C   . ASP A 1 80 ? 9.75657  10.68737  18.40034 1.000 12.79101  ? 80  ASP A C   1 
ATOM   587 O O   . ASP A 1 80 ? 9.26434  10.32304  19.47933 1.000 12.63836  ? 80  ASP A O   1 
ATOM   588 C CB  . ASP A 1 80 ? 7.71208  9.74945   17.26989 1.000 16.37302  ? 80  ASP A CB  1 
ATOM   589 C CG  . ASP A 1 80 ? 6.76226  10.84039  17.69695 1.000 19.52339  ? 80  ASP A CG  1 
ATOM   590 O OD1 . ASP A 1 80 ? 7.05419  12.04256  17.50179 1.000 20.92883  ? 80  ASP A OD1 1 
ATOM   591 O OD2 . ASP A 1 80 ? 5.69804  10.47195  18.22319 1.000 21.76314  ? 80  ASP A OD2 1 
ATOM   592 N N   . PRO A 1 81 ? 10.80968 11.50975  18.36126 1.000 13.15947  ? 81  PRO A N   1 
ATOM   593 C CA  . PRO A 1 81 ? 11.37057 12.03349  19.61196 1.000 13.37002  ? 81  PRO A CA  1 
ATOM   594 C C   . PRO A 1 81 ? 10.50298 13.14199  20.18865 1.000 13.09631  ? 81  PRO A C   1 
ATOM   595 O O   . PRO A 1 81 ? 10.03508 14.03227  19.47216 1.000 14.52806  ? 81  PRO A O   1 
ATOM   596 C CB  . PRO A 1 81 ? 12.73772 12.57826  19.18450 1.000 15.05444  ? 81  PRO A CB  1 
ATOM   597 C CG  . PRO A 1 81 ? 12.57982 12.90251  17.75586 1.000 16.68358  ? 81  PRO A CG  1 
ATOM   598 C CD  . PRO A 1 81 ? 11.60651 11.91504  17.18743 1.000 14.62807  ? 81  PRO A CD  1 
ATOM   599 N N   . LYS A 1 82 ? 10.28158 13.07045  21.50464 1.000 12.20936  ? 82  LYS A N   1 
ATOM   600 C CA  . LYS A 1 82 ? 9.48125  14.05552  22.22714 1.000 13.25948  ? 82  LYS A CA  1 
ATOM   601 C C   . LYS A 1 82 ? 10.15556 14.34289  23.55996 1.000 13.31212  ? 82  LYS A C   1 
ATOM   602 O O   . LYS A 1 82 ? 10.63488 13.41428  24.21731 1.000 13.86482  ? 82  LYS A O   1 
ATOM   603 C CB  . LYS A 1 82 ? 8.06022  13.53995  22.51672 1.000 15.35974  ? 82  LYS A CB  1 
ATOM   604 C CG  . LYS A 1 82 ? 7.28777  13.08016  21.29682 1.000 17.06784  ? 82  LYS A CG  1 
ATOM   605 C CD  . LYS A 1 82 ? 5.92698  12.51092  21.68854 1.000 20.33665  ? 82  LYS A CD  1 
ATOM   606 C CE  . LYS A 1 82 ? 4.96033  13.60387  22.11044 1.000 24.40556  ? 82  LYS A CE  1 
ATOM   607 N NZ  . LYS A 1 82 ? 4.63641  14.52945  20.99143 1.000 26.99008  ? 82  LYS A NZ  1 
ATOM   608 N N   . PRO A 1 83 ? 10.17225 15.59295  24.00960 1.000 13.19369  ? 83  PRO A N   1 
ATOM   609 C CA  . PRO A 1 83 ? 10.67378 15.86318  25.36209 1.000 13.95167  ? 83  PRO A CA  1 
ATOM   610 C C   . PRO A 1 83 ? 9.76334  15.21062  26.39057 1.000 13.22790  ? 83  PRO A C   1 
ATOM   611 O O   . PRO A 1 83 ? 8.55710  15.09125  26.18541 1.000 14.84915  ? 83  PRO A O   1 
ATOM   612 C CB  . PRO A 1 83 ? 10.60587 17.39067  25.46053 1.000 15.30447  ? 83  PRO A CB  1 
ATOM   613 C CG  . PRO A 1 83 ? 9.50665  17.77312  24.51357 1.000 17.12311  ? 83  PRO A CG  1 
ATOM   614 C CD  . PRO A 1 83 ? 9.57973  16.78412  23.38153 1.000 14.72282  ? 83  PRO A CD  1 
ATOM   615 N N   . CYS A 1 84 ? 10.34046 14.75355  27.49960 1.000 14.68071  ? 84  CYS A N   1 
ATOM   616 C CA  . CYS A 1 84 ? 9.48493  14.19204  28.53359 1.000 16.30722  ? 84  CYS A CA  1 
ATOM   617 C C   . CYS A 1 84 ? 9.89866  14.67314  29.91277 1.000 16.64410  ? 84  CYS A C   1 
ATOM   618 O O   . CYS A 1 84 ? 11.07321 14.95150  30.16626 1.000 19.62604  ? 84  CYS A O   1 
ATOM   619 C CB  . CYS A 1 84 ? 9.37073  12.66292  28.45951 1.000 18.75225  ? 84  CYS A CB  1 
ATOM   620 S SG  . CYS A 1 84 ? 10.85236 11.70293  28.86247 1.000 21.36835  ? 84  CYS A SG  1 
ATOM   621 N N   . ASN A 1 85 ? 8.90138  14.80056  30.78656 1.000 15.37553  ? 85  ASN A N   1 
ATOM   622 C CA  . ASN A 1 85 ? 9.15598  14.99221  32.20704 1.000 16.43618  ? 85  ASN A CA  1 
ATOM   623 C C   . ASN A 1 85 ? 9.44544  13.62722  32.81660 1.000 15.55713  ? 85  ASN A C   1 
ATOM   624 O O   . ASN A 1 85 ? 8.56834  12.74945  32.78787 1.000 15.83874  ? 85  ASN A O   1 
ATOM   625 C CB  . ASN A 1 85 ? 7.92979  15.61280  32.87207 1.000 19.25231  ? 85  ASN A CB  1 
ATOM   626 C CG  . ASN A 1 85 ? 8.24994  16.28065  34.20896 1.000 21.66576  ? 85  ASN A CG  1 
ATOM   627 O OD1 . ASN A 1 85 ? 9.41403  16.39973  34.59445 1.000 23.59493  ? 85  ASN A OD1 1 
ATOM   628 N ND2 . ASN A 1 85 ? 7.20915  16.72507  34.91863 1.000 23.41070  ? 85  ASN A ND2 1 
ATOM   629 N N   . PRO A 1 86 ? 10.64621 13.39668  33.35466 1.000 15.09655  ? 86  PRO A N   1 
ATOM   630 C CA  . PRO A 1 86 ? 11.04526 12.03237  33.72077 1.000 15.28604  ? 86  PRO A CA  1 
ATOM   631 C C   . PRO A 1 86 ? 10.28756 11.49202  34.92097 1.000 15.01759  ? 86  PRO A C   1 
ATOM   632 O O   . PRO A 1 86 ? 9.87798  12.23264  35.82243 1.000 16.28616  ? 86  PRO A O   1 
ATOM   633 C CB  . PRO A 1 86 ? 12.53544 12.17633  34.05563 1.000 16.62568  ? 86  PRO A CB  1 
ATOM   634 C CG  . PRO A 1 86 ? 12.97583 13.41438  33.33574 1.000 18.03637  ? 86  PRO A CG  1 
ATOM   635 C CD  . PRO A 1 86 ? 11.78210 14.33490  33.42673 1.000 16.66516  ? 86  PRO A CD  1 
ATOM   636 N N   . ARG A 1 87 ? 10.12587 10.16522  34.92771 1.000 16.14000  ? 87  ARG A N   1 
ATOM   637 C CA  . ARG A 1 87 ? 9.67250  9.46670   36.11984 1.000 15.69000  ? 87  ARG A CA  1 
ATOM   638 C C   . ARG A 1 87 ? 10.51659 9.91144   37.30156 1.000 16.76000  ? 87  ARG A C   1 
ATOM   639 O O   . ARG A 1 87 ? 11.73865 10.02626  37.19495 1.000 18.12000  ? 87  ARG A O   1 
ATOM   640 C CB  . ARG A 1 87 ? 9.83778  7.95336   35.93237 1.000 16.83000  ? 87  ARG A CB  1 
ATOM   641 C CG  . ARG A 1 87 ? 9.45623  7.12561   37.15259 1.000 17.53000  ? 87  ARG A CG  1 
ATOM   642 C CD  . ARG A 1 87 ? 9.74925  5.63250   36.95574 1.000 18.87000  ? 87  ARG A CD  1 
ATOM   643 N NE  . ARG A 1 87 ? 8.72491  4.91312   36.19813 1.000 19.43000  ? 87  ARG A NE  1 
ATOM   644 C CZ  . ARG A 1 87 ? 7.58518  4.46334   36.71003 1.000 18.25000  ? 87  ARG A CZ  1 
ATOM   645 N NH1 . ARG A 1 87 ? 7.21777  4.75628   37.94575 1.000 19.93000  ? 87  ARG A NH1 1 
ATOM   646 N NH2 . ARG A 1 87 ? 6.79472  3.69959   35.96177 1.000 20.13000  ? 87  ARG A NH2 1 
ATOM   647 N N   . THR A 1 88 ? 9.86571  10.16383  38.42842 1.000 16.75000  ? 88  THR A N   1 
ATOM   648 C CA  . THR A 1 88 ? 10.55256 10.59408  39.63679 1.000 18.87000  ? 88  THR A CA  1 
ATOM   649 C C   . THR A 1 88 ? 10.81178 9.40076   40.55209 1.000 33.89000  ? 88  THR A C   1 
ATOM   650 O O   . THR A 1 88 ? 10.01812 8.45663   40.62206 1.000 23.46000  ? 88  THR A O   1 
ATOM   651 C CB  . THR A 1 88 ? 9.75346  11.67165  40.37441 1.000 23.92000  ? 88  THR A CB  1 
ATOM   652 O OG1 . THR A 1 88 ? 8.39918  11.23895  40.54545 1.000 25.76000  ? 88  THR A OG1 1 
ATOM   653 C CG2 . THR A 1 88 ? 9.76818  12.96890  39.57676 1.000 30.26000  ? 88  THR A CG2 1 
ATOM   654 N N   . LEU A 1 89 ? 11.94018 9.44624   41.24866 1.000 89.67000  ? 89  LEU A N   1 
ATOM   655 C CA  . LEU A 1 89 ? 12.38092 8.35256   42.10071 1.000 105.14000 ? 89  LEU A CA  1 
ATOM   656 C C   . LEU A 1 89 ? 12.32945 8.77535   43.56664 1.000 48.94000  ? 89  LEU A C   1 
ATOM   657 O O   . LEU A 1 89 ? 11.87683 9.87098   43.91171 1.000 62.02000  ? 89  LEU A O   1 
ATOM   658 C CB  . LEU A 1 89 ? 13.78118 7.88335   41.69526 1.000 56.69000  ? 89  LEU A CB  1 
ATOM   659 C CG  . LEU A 1 89 ? 13.97763 7.44423   40.23977 1.000 93.12000  ? 89  LEU A CG  1 
ATOM   660 C CD1 . LEU A 1 89 ? 12.89388 6.46122   39.81257 1.000 69.02000  ? 89  LEU A CD1 1 
ATOM   661 C CD2 . LEU A 1 89 ? 14.03007 8.64257   39.29867 1.000 83.23000  ? 89  LEU A CD2 1 
ATOM   662 N N   . GLN A 1 90 ? 12.79717 7.88419   44.43494 1.000 61.11000  ? 90  GLN A N   1 
ATOM   663 C CA  . GLN A 1 90 ? 12.82673 8.14965   45.86866 1.000 98.25000  ? 90  GLN A CA  1 
ATOM   664 C C   . GLN A 1 90 ? 14.19952 8.66087   46.29123 1.000 116.90000 ? 90  GLN A C   1 
ATOM   665 O O   . GLN A 1 90 ? 15.20200 8.39715   45.62633 1.000 84.44000  ? 90  GLN A O   1 
ATOM   666 C CB  . GLN A 1 90 ? 12.47187 6.88444   46.65245 1.000 45.58000  ? 90  GLN A CB  1 
ATOM   667 C CG  . GLN A 1 90 ? 13.45069 5.73844   46.44829 1.000 91.57000  ? 90  GLN A CG  1 
ATOM   668 C CD  . GLN A 1 90 ? 12.83772 4.38448   46.75024 1.000 119.35000 ? 90  GLN A CD  1 
ATOM   669 O OE1 . GLN A 1 90 ? 11.67086 4.28897   47.12888 1.000 85.59000  ? 90  GLN A OE1 1 
ATOM   670 N NE2 . GLN A 1 90 ? 13.62252 3.32738   46.57664 1.000 64.72000  ? 90  GLN A NE2 1 
HETATM 671 C C1  . GOL B 2 .  ? 27.48787 4.40280   28.84181 1.000 52.46000  ? 101 GOL A C1  1 
HETATM 672 O O1  . GOL B 2 .  ? 28.30035 3.29738   28.57064 1.000 139.30000 ? 101 GOL A O1  1 
HETATM 673 C C2  . GOL B 2 .  ? 26.33319 4.36396   27.82574 1.000 71.23000  ? 101 GOL A C2  1 
HETATM 674 O O2  . GOL B 2 .  ? 25.61690 3.18231   27.88642 1.000 105.19000 ? 101 GOL A O2  1 
HETATM 675 C C3  . GOL B 2 .  ? 25.48705 5.58889   28.18601 1.000 46.67000  ? 101 GOL A C3  1 
HETATM 676 O O3  . GOL B 2 .  ? 24.21163 5.37585   27.63930 1.000 80.64000  ? 101 GOL A O3  1 
HETATM 677 H H11 . GOL B 2 .  ? 27.96195 5.24496   28.75872 1.000 62.97000  ? 101 GOL A H11 1 
HETATM 678 H H12 . GOL B 2 .  ? 27.12583 4.38930   29.74161 1.000 62.97000  ? 101 GOL A H12 1 
HETATM 679 H HO1 . GOL B 2 .  ? 28.42738 3.29825   27.72533 1.000 167.18000 ? 101 GOL A HO1 1 
HETATM 680 H H2  . GOL B 2 .  ? 26.66365 4.41332   26.91510 1.000 85.49000  ? 101 GOL A H2  1 
HETATM 681 H HO2 . GOL B 2 .  ? 25.34650 3.07685   28.68224 1.000 126.25000 ? 101 GOL A HO2 1 
HETATM 682 H H31 . GOL B 2 .  ? 25.92441 6.38461   27.84477 1.000 56.03000  ? 101 GOL A H31 1 
HETATM 683 H H32 . GOL B 2 .  ? 25.48018 5.69378   29.15030 1.000 56.03000  ? 101 GOL A H32 1 
HETATM 684 H HO3 . GOL B 2 .  ? 23.95157 4.61192   27.89584 1.000 96.78000  ? 101 GOL A HO3 1 
HETATM 685 C C1  . GOL C 2 .  ? 11.08830 3.53361   32.88466 1.000 38.93000  ? 102 GOL A C1  1 
HETATM 686 O O1  . GOL C 2 .  ? 10.98038 2.59059   31.87912 1.000 130.01000 ? 102 GOL A O1  1 
HETATM 687 C C2  . GOL C 2 .  ? 11.70330 4.81066   32.25685 1.000 45.91000  ? 102 GOL A C2  1 
HETATM 688 O O2  . GOL C 2 .  ? 11.71355 5.82165   33.18800 1.000 21.94000  ? 102 GOL A O2  1 
HETATM 689 C C3  . GOL C 2 .  ? 13.07169 4.37732   31.76547 1.000 36.70000  ? 102 GOL A C3  1 
HETATM 690 O O3  . GOL C 2 .  ? 13.79461 5.54188   31.42013 1.000 23.82000  ? 102 GOL A O3  1 
HETATM 691 H H11 . GOL C 2 .  ? 11.65087 3.23474   33.61616 1.000 46.74000  ? 102 GOL A H11 1 
HETATM 692 H H12 . GOL C 2 .  ? 10.23109 3.75399   33.28157 1.000 46.74000  ? 102 GOL A H12 1 
HETATM 693 H HO1 . GOL C 2 .  ? 10.47677 2.92697   31.28930 1.000 156.04000 ? 102 GOL A HO1 1 
HETATM 694 H H2  . GOL C 2 .  ? 11.19823 5.15149   31.50210 1.000 55.11000  ? 102 GOL A H2  1 
HETATM 695 H HO2 . GOL C 2 .  ? 12.23753 5.59309   33.82213 1.000 26.35000  ? 102 GOL A HO2 1 
HETATM 696 H H31 . GOL C 2 .  ? 12.95421 3.76598   31.02159 1.000 44.06000  ? 102 GOL A H31 1 
HETATM 697 H H32 . GOL C 2 .  ? 13.49940 3.85459   32.46169 1.000 44.06000  ? 102 GOL A H32 1 
HETATM 698 H HO3 . GOL C 2 .  ? 13.91341 5.97708   32.13182 1.000 28.61000  ? 102 GOL A HO3 1 
HETATM 699 O O   . HOH D 3 .  ? 24.07320 4.71997   25.48738 1.000 24.04000  ? 201 HOH A O   1 
HETATM 700 O O   . HOH D 3 .  ? 23.63331 10.21085  13.93162 1.000 25.89000  ? 202 HOH A O   1 
HETATM 701 O O   . HOH D 3 .  ? 3.79140  -7.83137  30.25585 1.000 52.30000  ? 203 HOH A O   1 
HETATM 702 O O   . HOH D 3 .  ? 13.30728 25.47196  17.12013 1.000 49.60000  ? 204 HOH A O   1 
HETATM 703 O O   . HOH D 3 .  ? 30.422   4.356     27.819   1.000 43.65000  ? 205 HOH A O   1 
HETATM 704 O O   . HOH D 3 .  ? 14.97243 -3.22934  8.55597  1.000 20.65000  ? 206 HOH A O   1 
HETATM 705 O O   . HOH D 3 .  ? 19.17477 2.65607   32.35100 1.000 38.94000  ? 207 HOH A O   1 
HETATM 706 O O   . HOH D 3 .  ? 22.14910 -3.91887  25.88035 1.000 47.48000  ? 208 HOH A O   1 
HETATM 707 O O   . HOH D 3 .  ? 8.87228  13.81657  17.02003 1.000 26.42000  ? 209 HOH A O   1 
HETATM 708 O O   . HOH D 3 .  ? 13.26012 -1.10643  19.22651 1.000 14.50000  ? 210 HOH A O   1 
HETATM 709 O O   . HOH D 3 .  ? 19.32275 6.69649   10.42296 1.000 31.64000  ? 211 HOH A O   1 
HETATM 710 O O   . HOH D 3 .  ? 2.65612  15.64860  22.32191 1.000 44.74000  ? 212 HOH A O   1 
HETATM 711 O O   . HOH D 3 .  ? 27.50883 16.44783  16.92315 1.000 22.19000  ? 213 HOH A O   1 
HETATM 712 O O   . HOH D 3 .  ? 23.85427 24.08523  24.07345 1.000 30.47000  ? 214 HOH A O   1 
HETATM 713 O O   . HOH D 3 .  ? 7.64579  4.58185   12.96626 1.000 23.47000  ? 215 HOH A O   1 
HETATM 714 O O   . HOH D 3 .  ? 10.29795 14.84760  36.57054 1.000 23.03000  ? 216 HOH A O   1 
HETATM 715 O O   . HOH D 3 .  ? 5.33482  7.99955   19.18403 1.000 28.41000  ? 217 HOH A O   1 
HETATM 716 O O   . HOH D 3 .  ? 6.53169  15.96469  24.66742 1.000 15.95000  ? 218 HOH A O   1 
HETATM 717 O O   . HOH D 3 .  ? 26.90634 6.11270   12.67011 1.000 62.45000  ? 219 HOH A O   1 
HETATM 718 O O   . HOH D 3 .  ? 17.27883 -6.44941  17.28633 1.000 22.85000  ? 220 HOH A O   1 
HETATM 719 O O   . HOH D 3 .  ? 20.47659 15.64269  31.78868 1.000 34.97000  ? 221 HOH A O   1 
HETATM 720 O O   . HOH D 3 .  ? 13.17592 6.10549   35.43583 1.000 30.35000  ? 222 HOH A O   1 
HETATM 721 O O   . HOH D 3 .  ? 16.26736 4.71310   32.10627 1.000 26.73000  ? 223 HOH A O   1 
HETATM 722 O O   . HOH D 3 .  ? 14.243   18.641    7.604    1.000 30.07000  ? 224 HOH A O   1 
HETATM 723 O O   . HOH D 3 .  ? 12.41965 19.27817  13.24305 1.000 20.46000  ? 225 HOH A O   1 
HETATM 724 O O   . HOH D 3 .  ? 26.95403 17.27268  25.92239 1.000 17.38000  ? 226 HOH A O   1 
HETATM 725 O O   . HOH D 3 .  ? 17.08979 7.55432   29.05532 1.000 14.77000  ? 227 HOH A O   1 
HETATM 726 O O   . HOH D 3 .  ? 23.43545 -2.46768  17.96899 1.000 14.95000  ? 228 HOH A O   1 
HETATM 727 O O   . HOH D 3 .  ? 22.32674 5.11883   33.00258 1.000 44.90000  ? 229 HOH A O   1 
HETATM 728 O O   . HOH D 3 .  ? 12.21535 -1.33118  10.02752 1.000 24.38000  ? 230 HOH A O   1 
HETATM 729 O O   . HOH D 3 .  ? 17.51147 9.62902   32.74651 1.000 29.49000  ? 231 HOH A O   1 
HETATM 730 O O   . HOH D 3 .  ? 6.48850  -9.40520  22.90326 1.000 45.21000  ? 232 HOH A O   1 
HETATM 731 O O   . HOH D 3 .  ? 27.58325 19.86938  26.84858 1.000 25.18000  ? 233 HOH A O   1 
HETATM 732 O O   . HOH D 3 .  ? 13.46043 12.08229  37.78009 1.000 46.64000  ? 234 HOH A O   1 
HETATM 733 O O   . HOH D 3 .  ? 18.39299 15.02567  11.07416 1.000 36.42000  ? 235 HOH A O   1 
HETATM 734 O O   . HOH D 3 .  ? 25.22405 21.78201  22.77559 1.000 29.88000  ? 236 HOH A O   1 
HETATM 735 O O   . HOH D 3 .  ? 21.08182 25.80783  22.75514 1.000 34.10000  ? 237 HOH A O   1 
HETATM 736 O O   . HOH D 3 .  ? 10.87670 12.45974  13.01299 1.000 18.00000  ? 238 HOH A O   1 
HETATM 737 O O   . HOH D 3 .  ? 23.42230 8.40198   12.04042 1.000 32.28000  ? 239 HOH A O   1 
HETATM 738 O O   . HOH D 3 .  ? 5.69899  14.32219  18.44008 1.000 47.10000  ? 240 HOH A O   1 
HETATM 739 O O   . HOH D 3 .  ? 6.80025  8.18740   14.18133 1.000 29.71000  ? 241 HOH A O   1 
HETATM 740 O O   . HOH D 3 .  ? 25.83444 9.50086   15.19591 1.000 39.43000  ? 242 HOH A O   1 
HETATM 741 O O   . HOH D 3 .  ? 24.52638 16.08289  26.00398 1.000 12.92000  ? 243 HOH A O   1 
HETATM 742 O O   . HOH D 3 .  ? 6.98259  1.31559   17.27133 1.000 25.18000  ? 244 HOH A O   1 
HETATM 743 O O   . HOH D 3 .  ? 18.35814 24.23003  23.69025 1.000 26.08000  ? 245 HOH A O   1 
HETATM 744 O O   . HOH D 3 .  ? 13.51206 2.20234   14.38060 1.000 18.01000  ? 246 HOH A O   1 
HETATM 745 O O   . HOH D 3 .  ? 22.85897 -0.16056  26.16850 1.000 42.53000  ? 247 HOH A O   1 
HETATM 746 O O   . HOH D 3 .  ? 25.99002 3.04737   20.85074 1.000 29.10000  ? 248 HOH A O   1 
HETATM 747 O O   . HOH D 3 .  ? 15.90822 -3.54479  21.10951 1.000 17.97000  ? 249 HOH A O   1 
HETATM 748 O O   . HOH D 3 .  ? 10.37871 12.19978  44.26653 1.000 57.20000  ? 250 HOH A O   1 
HETATM 749 O O   . HOH D 3 .  ? 13.72513 15.65605  30.68664 1.000 18.29000  ? 251 HOH A O   1 
HETATM 750 O O   . HOH D 3 .  ? 8.85411  -2.40392  29.37111 1.000 20.85000  ? 252 HOH A O   1 
HETATM 751 O O   . HOH D 3 .  ? 8.36244  -3.45816  14.94780 1.000 45.87000  ? 253 HOH A O   1 
HETATM 752 O O   . HOH D 3 .  ? 22.59423 15.89769  33.19866 1.000 34.90000  ? 254 HOH A O   1 
HETATM 753 O O   . HOH D 3 .  ? 17.44944 10.82931  10.30012 1.000 23.42000  ? 255 HOH A O   1 
HETATM 754 O O   . HOH D 3 .  ? 2.92910  -0.40066  25.09926 1.000 40.05000  ? 256 HOH A O   1 
HETATM 755 O O   . HOH D 3 .  ? 20.20817 -4.31796  23.01355 1.000 27.16000  ? 257 HOH A O   1 
HETATM 756 O O   . HOH D 3 .  ? 13.49404 23.62906  12.75558 1.000 22.08000  ? 258 HOH A O   1 
HETATM 757 O O   . HOH D 3 .  ? 6.17372  16.76101  21.81766 1.000 45.73000  ? 259 HOH A O   1 
HETATM 758 O O   . HOH D 3 .  ? 13.44242 -6.80927  20.10919 1.000 31.71000  ? 260 HOH A O   1 
HETATM 759 O O   . HOH D 3 .  ? 22.43558 2.18835   25.80196 1.000 38.24000  ? 261 HOH A O   1 
HETATM 760 O O   . HOH D 3 .  ? 16.54150 21.51911  25.25808 1.000 17.35000  ? 262 HOH A O   1 
HETATM 761 O O   . HOH D 3 .  ? 13.39906 8.80456   35.24003 1.000 25.81000  ? 263 HOH A O   1 
HETATM 762 O O   . HOH D 3 .  ? 15.48254 20.77284  28.39251 1.000 48.16000  ? 264 HOH A O   1 
HETATM 763 O O   . HOH D 3 .  ? 16.71637 4.54947   7.98895  1.000 39.45000  ? 265 HOH A O   1 
HETATM 764 O O   . HOH D 3 .  ? 7.595    3.220     33.259   1.000 31.24000  ? 266 HOH A O   1 
HETATM 765 O O   . HOH D 3 .  ? 13.22034 16.98331  27.87549 1.000 23.75000  ? 267 HOH A O   1 
HETATM 766 O O   . HOH D 3 .  ? 19.059   3.797     9.929    1.000 19.78000  ? 268 HOH A O   1 
HETATM 767 O O   . HOH D 3 .  ? 13.70828 11.61101  40.57328 1.000 43.63000  ? 269 HOH A O   1 
HETATM 768 O O   . HOH D 3 .  ? 22.08153 3.45285   29.01336 1.000 23.91000  ? 270 HOH A O   1 
HETATM 769 O O   . HOH D 3 .  ? 28.19176 0.69933   27.31354 1.000 52.89000  ? 271 HOH A O   1 
HETATM 770 O O   . HOH D 3 .  ? 3.98120  -2.84319  24.56071 1.000 29.15000  ? 272 HOH A O   1 
HETATM 771 O O   . HOH D 3 .  ? 11.91993 20.95065  25.24814 1.000 48.26000  ? 273 HOH A O   1 
HETATM 772 O O   . HOH D 3 .  ? 12.63302 -2.83443  29.48905 1.000 25.33000  ? 274 HOH A O   1 
HETATM 773 O O   . HOH D 3 .  ? 17.95563 -3.00442  22.91930 1.000 17.49000  ? 275 HOH A O   1 
HETATM 774 O O   . HOH D 3 .  ? 7.88465  5.03058   9.48173  1.000 29.01000  ? 276 HOH A O   1 
HETATM 775 O O   . HOH D 3 .  ? 5.93661  3.83053   19.72713 1.000 25.07000  ? 277 HOH A O   1 
HETATM 776 O O   . HOH D 3 .  ? 9.59324  -3.96545  12.25663 1.000 27.77000  ? 278 HOH A O   1 
HETATM 777 O O   . HOH D 3 .  ? 6.12072  -5.90144  29.88781 1.000 45.02000  ? 279 HOH A O   1 
HETATM 778 O O   . HOH D 3 .  ? 17.35137 -4.39818  27.75070 1.000 43.94000  ? 280 HOH A O   1 
HETATM 779 O O   . HOH D 3 .  ? 7.09149  -6.54186  22.31694 1.000 40.33000  ? 281 HOH A O   1 
HETATM 780 O O   . HOH D 3 .  ? 12.35510 16.34226  15.45336 1.000 23.17000  ? 282 HOH A O   1 
HETATM 781 O O   . HOH D 3 .  ? 23.560   18.372    33.416   1.000 38.64000  ? 283 HOH A O   1 
HETATM 782 O O   . HOH D 3 .  ? 13.07705 14.63497  37.46393 1.000 39.10000  ? 284 HOH A O   1 
HETATM 783 O O   . HOH D 3 .  ? 15.51929 8.84787   34.03187 1.000 43.76000  ? 285 HOH A O   1 
HETATM 784 O O   . HOH D 3 .  ? 21.84049 6.31090   11.07040 1.000 39.76000  ? 286 HOH A O   1 
HETATM 785 O O   . HOH D 3 .  ? 10.38245 11.22433  7.36276  1.000 41.20000  ? 287 HOH A O   1 
HETATM 786 O O   . HOH D 3 .  ? 5.57471  1.53533   20.29514 1.000 39.09000  ? 288 HOH A O   1 
HETATM 787 O O   . HOH D 3 .  ? 15.52023 11.66327  8.16329  1.000 42.85000  ? 289 HOH A O   1 
HETATM 788 O O   . HOH D 3 .  ? 4.21617  -2.17294  22.21657 1.000 49.55000  ? 290 HOH A O   1 
HETATM 789 O O   . HOH D 3 .  ? 11.06072 -5.85691  30.81780 1.000 43.96000  ? 291 HOH A O   1 
HETATM 790 O O   . HOH D 3 .  ? 7.67976  15.97801  19.24099 1.000 42.26000  ? 292 HOH A O   1 
HETATM 791 O O   . HOH D 3 .  ? 14.84034 -1.43119  29.11863 1.000 48.04000  ? 293 HOH A O   1 
HETATM 792 O O   . HOH D 3 .  ? 19.20578 -2.05795  29.60179 1.000 56.30000  ? 294 HOH A O   1 
HETATM 793 O O   . HOH D 3 .  ? 15.72505 -5.76951  19.65139 1.000 44.55000  ? 295 HOH A O   1 
HETATM 794 O O   . HOH D 3 .  ? 15.842   27.340    19.647   1.000 50.49000  ? 296 HOH A O   1 
HETATM 795 O O   . HOH D 3 .  ? 8.048    0.538     36.072   1.000 61.39000  ? 297 HOH A O   1 
HETATM 796 O O   . HOH D 3 .  ? 17.07756 24.52771  26.21325 1.000 49.86000  ? 298 HOH A O   1 
HETATM 797 O O   . HOH D 3 .  ? 17.38942 22.84482  28.63002 1.000 38.29000  ? 299 HOH A O   1 
HETATM 798 O O   . HOH D 3 .  ? 10.65806 16.49438  12.59453 1.000 43.01000  ? 300 HOH A O   1 
HETATM 799 O O   . HOH D 3 .  ? 18.00457 25.50125  20.89216 1.000 42.52000  ? 301 HOH A O   1 
HETATM 800 O O   . HOH D 3 .  ? 13.69746 20.62730  26.68212 1.000 48.74000  ? 302 HOH A O   1 
HETATM 801 O O   . HOH D 3 .  ? 26.609   0.955     13.728   1.000 42.25000  ? 303 HOH A O   1 
HETATM 802 O O   . HOH D 3 .  ? 11.873   20.550    8.782    1.000 40.81000  ? 304 HOH A O   1 
HETATM 803 O O   . HOH D 3 .  ? 5.01245  6.84231   16.09294 1.000 43.87000  ? 305 HOH A O   1 
HETATM 804 O O   . HOH D 3 .  ? 9.18650  16.41720  38.59440 1.000 40.11000  ? 306 HOH A O   1 
HETATM 805 O O   . HOH D 3 .  ? 20.25399 9.36007   33.82227 1.000 38.72000  ? 307 HOH A O   1 
HETATM 806 O O   . HOH D 3 .  ? 25.61540 -5.17818  22.98335 1.000 54.63000  ? 308 HOH A O   1 
HETATM 807 O O   . HOH D 3 .  ? 19.98705 -4.93368  25.62581 1.000 55.38000  ? 309 HOH A O   1 
HETATM 808 O O   . HOH D 3 .  ? 17.084   15.941    7.747    1.000 47.45000  ? 310 HOH A O   1 
HETATM 809 O O   . HOH D 3 .  ? 5.56708  6.49916   10.30257 1.000 46.21000  ? 311 HOH A O   1 
HETATM 810 O O   . HOH D 3 .  ? 10.61544 14.53634  14.82836 1.000 26.92000  ? 312 HOH A O   1 
HETATM 811 O O   . HOH D 3 .  ? 3.327    8.590     21.318   1.000 41.26000  ? 313 HOH A O   1 
HETATM 812 O O   . HOH D 3 .  ? 5.39571  8.80005   10.65145 1.000 48.46000  ? 314 HOH A O   1 
HETATM 813 O O   . HOH D 3 .  ? 8.30014  12.87032  8.33505  1.000 37.34000  ? 315 HOH A O   1 
HETATM 814 O O   . HOH D 3 .  ? 13.13144 3.65779   36.84017 1.000 51.92000  ? 316 HOH A O   1 
HETATM 815 O O   . HOH D 3 .  ? 0.28045  -1.61267  26.37624 1.000 55.06000  ? 317 HOH A O   1 
HETATM 816 O O   . HOH D 3 .  ? 8.53699  13.36633  11.61926 1.000 36.29000  ? 318 HOH A O   1 
HETATM 817 O O   . HOH D 3 .  ? 3.26903  2.01177   23.28334 1.000 37.92000  ? 319 HOH A O   1 
HETATM 818 O O   . HOH D 3 .  ? 29.041   6.500     15.775   1.000 46.03000  ? 320 HOH A O   1 
HETATM 819 O O   . HOH D 3 .  ? 18.88391 -6.28095  21.63245 1.000 56.41000  ? 321 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
21  N N   . GLY A 9  ? 0.50460 0.53780 0.60590 -0.30470 -0.04830 -0.03810 9  GLY A N   
22  C CA  . GLY A 9  ? 0.29400 0.32910 0.41850 -0.17780 -0.04080 -0.03710 9  GLY A CA  
23  C C   . GLY A 9  ? 0.17380 0.18680 0.25650 -0.04620 -0.00090 -0.01210 9  GLY A C   
24  O O   . GLY A 9  ? 0.14930 0.15980 0.20720 0.00080  0.00690  0.00230  9  GLY A O   
25  N N   . LYS A 10 ? 0.15820 0.16220 0.21940 -0.02900 0.01140  -0.03580 10 LYS A N   
26  C CA  . LYS A 10 ? 0.15540 0.15440 0.20330 -0.01970 0.00920  -0.02680 10 LYS A CA  
27  C C   . LYS A 10 ? 0.13470 0.13980 0.19110 0.00090  0.01440  -0.02330 10 LYS A C   
28  O O   . LYS A 10 ? 0.14880 0.17440 0.20450 0.01290  0.00230  -0.03660 10 LYS A O   
29  C CB  . LYS A 10 ? 0.17130 0.15860 0.20310 -0.03280 0.01640  -0.01720 10 LYS A CB  
30  C CG  . LYS A 10 ? 0.16540 0.17240 0.18730 -0.01680 0.02030  -0.01260 10 LYS A CG  
31  C CD  . LYS A 10 ? 0.17250 0.17090 0.19090 -0.00510 0.02570  -0.01430 10 LYS A CD  
32  C CE  . LYS A 10 ? 0.18310 0.19450 0.17760 0.01340  0.02030  -0.02710 10 LYS A CE  
33  N NZ  . LYS A 10 ? 0.18520 0.21390 0.17690 0.00520  0.00310  0.00670  10 LYS A NZ  
34  N N   . LEU A 11 ? 0.16050 0.12540 0.18750 -0.00420 0.00580  -0.01610 11 LEU A N   
35  C CA  . LEU A 11 ? 0.20710 0.14710 0.19520 0.00960  -0.00960 -0.00550 11 LEU A CA  
36  C C   . LEU A 11 ? 0.19310 0.12910 0.21200 0.02610  -0.04240 -0.02030 11 LEU A C   
37  O O   . LEU A 11 ? 0.19160 0.11890 0.28930 0.02800  -0.07760 -0.02110 11 LEU A O   
38  C CB  . LEU A 11 ? 0.28120 0.18410 0.22200 0.03410  0.02870  0.01620  11 LEU A CB  
39  C CG  . LEU A 11 ? 0.25800 0.23390 0.25160 0.03310  0.03090  0.05140  11 LEU A CG  
40  C CD1 . LEU A 11 ? 0.24740 0.19050 0.26640 0.02220  -0.01630 0.07710  11 LEU A CD1 
41  C CD2 . LEU A 11 ? 0.25740 0.27680 0.24980 0.04050  0.03600  0.06350  11 LEU A CD2 
42  N N   . PHE A 12 ? 0.17850 0.14370 0.16990 0.01300  -0.00900 -0.02700 12 PHE A N   
43  C CA  . PHE A 12 ? 0.14800 0.15280 0.14620 0.01660  0.00420  0.00210  12 PHE A CA  
44  C C   . PHE A 12 ? 0.15170 0.11190 0.14530 0.01110  0.00300  -0.00790 12 PHE A C   
45  O O   . PHE A 12 ? 0.18810 0.11910 0.16860 0.02460  -0.00210 0.00180  12 PHE A O   
46  C CB  . PHE A 12 ? 0.17030 0.16970 0.16150 0.02430  0.01030  -0.01950 12 PHE A CB  
47  C CG  . PHE A 12 ? 0.16180 0.17180 0.17500 0.03730  0.02260  -0.01780 12 PHE A CG  
48  C CD1 . PHE A 12 ? 0.17560 0.18960 0.18690 0.00260  0.03070  -0.00960 12 PHE A CD1 
49  C CD2 . PHE A 12 ? 0.17060 0.17720 0.19480 0.01920  0.00720  -0.01500 12 PHE A CD2 
50  C CE1 . PHE A 12 ? 0.18620 0.19700 0.18870 0.01800  0.03350  -0.00660 12 PHE A CE1 
51  C CE2 . PHE A 12 ? 0.17650 0.17950 0.21850 0.01850  0.00880  -0.01680 12 PHE A CE2 
52  C CZ  . PHE A 12 ? 0.17150 0.19380 0.20460 0.01030  0.02470  -0.00950 12 PHE A CZ  
53  N N   . VAL A 13 ? 0.14810 0.12150 0.15260 0.00230  0.00280  -0.01670 13 VAL A N   
54  C CA  . VAL A 13 ? 0.14630 0.14000 0.16630 0.00270  0.00260  -0.01730 13 VAL A CA  
55  C C   . VAL A 13 ? 0.15270 0.12690 0.17390 -0.00560 -0.00410 -0.00370 13 VAL A C   
56  O O   . VAL A 13 ? 0.17460 0.12850 0.17600 -0.01130 -0.01110 0.00360  13 VAL A O   
57  C CB  . VAL A 13 ? 0.15660 0.16170 0.16950 -0.00480 0.01450  -0.01550 13 VAL A CB  
58  C CG1 . VAL A 13 ? 0.15980 0.18430 0.16990 0.00090  0.02330  -0.01310 13 VAL A CG1 
59  C CG2 . VAL A 13 ? 0.14780 0.17740 0.19440 -0.01700 -0.00700 -0.01720 13 VAL A CG2 
60  N N   . GLY A 14 ? 0.12940 0.14750 0.17510 -0.01280 -0.01050 -0.00610 14 GLY A N   
61  C CA  . GLY A 14 ? 0.13670 0.15880 0.19060 -0.00860 -0.00530 -0.01120 14 GLY A CA  
62  C C   . GLY A 14 ? 0.14890 0.14400 0.18930 0.00180  -0.01550 -0.01540 14 GLY A C   
63  O O   . GLY A 14 ? 0.17550 0.14820 0.18080 -0.00090 -0.00100 -0.00890 14 GLY A O   
64  N N   . GLY A 15 ? 0.16460 0.15340 0.19650 -0.00040 -0.02200 -0.02560 15 GLY A N   
65  C CA  . GLY A 15 ? 0.16850 0.17510 0.19790 0.01110  -0.01210 -0.03540 15 GLY A CA  
66  C C   . GLY A 15 ? 0.16630 0.17600 0.17680 0.01100  -0.00780 -0.03610 15 GLY A C   
67  O O   . GLY A 15 ? 0.22850 0.21210 0.18050 0.02340  -0.00360 -0.03700 15 GLY A O   
68  N N   . LEU A 16 ? 0.15860 0.15540 0.18400 0.01050  -0.01840 -0.02350 16 LEU A N   
69  C CA  . LEU A 16 ? 0.17240 0.14510 0.19220 0.02990  0.00360  -0.02080 16 LEU A CA  
70  C C   . LEU A 16 ? 0.22430 0.16560 0.21830 0.03460  -0.00130 -0.03150 16 LEU A C   
71  O O   . LEU A 16 ? 0.22510 0.16610 0.24230 0.00280  -0.01930 -0.04260 16 LEU A O   
72  C CB  . LEU A 16 ? 0.18380 0.14160 0.19740 -0.00940 0.00260  -0.02100 16 LEU A CB  
73  C CG  . LEU A 16 ? 0.18460 0.14170 0.20280 -0.01580 -0.00590 -0.02000 16 LEU A CG  
74  C CD1 . LEU A 16 ? 0.18830 0.18500 0.19730 -0.01580 -0.01280 -0.01990 16 LEU A CD1 
75  C CD2 . LEU A 16 ? 0.21700 0.17110 0.21640 -0.05170 -0.00240 -0.00940 16 LEU A CD2 
76  N N   A SER A 17 ? 0.25410 0.18030 0.21550 0.05070  0.00060  -0.03700 17 SER A N   
77  N N   B SER A 17 ? 0.23970 0.18050 0.22020 0.02490  -0.00190 -0.04300 17 SER A N   
78  C CA  A SER A 17 ? 0.27080 0.18290 0.22680 0.04680  -0.00430 -0.04550 17 SER A CA  
79  C CA  B SER A 17 ? 0.24810 0.19110 0.22840 0.00910  -0.00820 -0.05360 17 SER A CA  
80  C C   A SER A 17 ? 0.23870 0.18750 0.23010 0.02870  0.01160  -0.04230 17 SER A C   
81  C C   B SER A 17 ? 0.23760 0.19300 0.23610 0.00510  -0.00500 -0.05230 17 SER A C   
82  O O   A SER A 17 ? 0.19850 0.15850 0.19910 0.01630  0.02200  -0.04220 17 SER A O   
83  O O   B SER A 17 ? 0.22590 0.18390 0.22120 -0.00430 -0.01020 -0.05920 17 SER A O   
84  C CB  A SER A 17 ? 0.28840 0.20630 0.23010 0.06390  -0.00850 -0.03870 17 SER A CB  
85  C CB  B SER A 17 ? 0.25670 0.21270 0.22840 0.00120  -0.00960 -0.05600 17 SER A CB  
86  O OG  A SER A 17 ? 0.27880 0.18840 0.22770 0.06380  0.00600  -0.03910 17 SER A OG  
87  O OG  B SER A 17 ? 0.25910 0.22100 0.22630 -0.00790 -0.00360 -0.06020 17 SER A OG  
88  N N   . TRP A 18 ? 0.22900 0.18900 0.25430 0.00790  -0.00490 -0.05080 18 TRP A N   
89  C CA  . TRP A 18 ? 0.24950 0.18440 0.27790 -0.03590 0.02180  -0.04360 18 TRP A CA  
90  C C   . TRP A 18 ? 0.22680 0.16600 0.24120 -0.01870 0.02300  -0.03650 18 TRP A C   
91  O O   . TRP A 18 ? 0.26570 0.19510 0.23960 -0.01270 0.03180  -0.02290 18 TRP A O   
92  C CB  . TRP A 18 ? 0.31420 0.24420 0.32730 -0.02860 0.02930  -0.03950 18 TRP A CB  
93  C CG  . TRP A 18 ? 0.37940 0.30470 0.36190 -0.02780 0.01910  -0.04530 18 TRP A CG  
94  C CD1 . TRP A 18 ? 0.40590 0.32680 0.37190 -0.04180 0.00130  -0.04850 18 TRP A CD1 
95  C CD2 . TRP A 18 ? 0.43340 0.34480 0.38460 -0.01020 0.01840  -0.04670 18 TRP A CD2 
96  N NE1 . TRP A 18 ? 0.42230 0.34120 0.38620 -0.02630 0.01520  -0.04670 18 TRP A NE1 
97  C CE2 . TRP A 18 ? 0.44070 0.34560 0.39400 -0.01490 0.02180  -0.04740 18 TRP A CE2 
98  C CE3 . TRP A 18 ? 0.46610 0.36290 0.40310 0.01130  0.02430  -0.05020 18 TRP A CE3 
99  C CZ2 . TRP A 18 ? 0.46340 0.36650 0.40820 0.00320  0.03000  -0.04530 18 TRP A CZ2 
100 C CZ3 . TRP A 18 ? 0.48510 0.37430 0.41100 0.01030  0.02530  -0.04480 18 TRP A CZ3 
101 C CH2 . TRP A 18 ? 0.48070 0.37520 0.41370 0.01230  0.02870  -0.04290 18 TRP A CH2 
102 N N   . GLU A 19 ? 0.20840 0.16530 0.21530 -0.00120 0.02890  -0.03080 19 GLU A N   
103 C CA  . GLU A 19 ? 0.21510 0.17670 0.20860 0.00940  0.02890  -0.02570 19 GLU A CA  
104 C C   . GLU A 19 ? 0.19270 0.17550 0.19350 0.00980  0.02100  -0.01010 19 GLU A C   
105 O O   . GLU A 19 ? 0.18730 0.19430 0.23050 0.01790  0.01690  -0.01810 19 GLU A O   
106 C CB  . GLU A 19 ? 0.24890 0.17950 0.22800 -0.01830 0.03380  -0.02870 19 GLU A CB  
107 C CG  . GLU A 19 ? 0.27510 0.19020 0.23990 0.01620  0.01220  -0.01410 19 GLU A CG  
108 C CD  . GLU A 19 ? 0.29420 0.20790 0.22940 0.01840  -0.00390 -0.01140 19 GLU A CD  
109 O OE1 . GLU A 19 ? 0.25700 0.21880 0.22580 0.00270  -0.02260 -0.02320 19 GLU A OE1 
110 O OE2 . GLU A 19 ? 0.32490 0.22230 0.22020 0.01650  0.00360  0.01180  19 GLU A OE2 
111 N N   . THR A 20 ? 0.18930 0.16440 0.17080 0.01170  0.01840  -0.02970 20 THR A N   
112 C CA  . THR A 20 ? 0.19130 0.15470 0.17500 0.01140  0.00970  -0.02650 20 THR A CA  
113 C C   . THR A 20 ? 0.19640 0.14480 0.16700 0.00000  0.01980  -0.01300 20 THR A C   
114 O O   . THR A 20 ? 0.20440 0.15090 0.18140 -0.00640 0.02760  -0.02120 20 THR A O   
115 C CB  . THR A 20 ? 0.19190 0.15550 0.19310 0.00470  -0.00100 -0.00870 20 THR A CB  
116 O OG1 . THR A 20 ? 0.19640 0.19890 0.20180 0.03450  0.00480  -0.00590 20 THR A OG1 
117 C CG2 . THR A 20 ? 0.19010 0.15120 0.21440 0.00980  0.00290  -0.01120 20 THR A CG2 
118 N N   . THR A 21 ? 0.19130 0.14850 0.17810 -0.00650 -0.00790 -0.01610 21 THR A N   
119 C CA  . THR A 21 ? 0.20710 0.13670 0.17510 0.00420  0.00500  -0.02880 21 THR A CA  
120 C C   . THR A 21 ? 0.20120 0.14970 0.16920 0.00460  0.00890  -0.01720 21 THR A C   
121 O O   . THR A 21 ? 0.19450 0.14020 0.17330 0.01200  0.00800  -0.01320 21 THR A O   
122 C CB  . THR A 21 ? 0.21210 0.14400 0.19110 0.00440  0.01860  -0.01380 21 THR A CB  
123 O OG1 . THR A 21 ? 0.18490 0.14660 0.20030 0.01550  0.00290  0.00330  21 THR A OG1 
124 C CG2 . THR A 21 ? 0.23400 0.13600 0.19310 0.01190  -0.00090 -0.02030 21 THR A CG2 
125 N N   . GLN A 22 ? 0.21240 0.16720 0.15860 -0.00680 0.01190  -0.01380 22 GLN A N   
126 C CA  . GLN A 22 ? 0.21320 0.17250 0.16620 -0.02570 0.01350  -0.01910 22 GLN A CA  
127 C C   . GLN A 22 ? 0.20270 0.16360 0.16170 0.02020  0.00190  -0.01390 22 GLN A C   
128 O O   . GLN A 22 ? 0.19650 0.14940 0.17140 0.00070  -0.00160 -0.01370 22 GLN A O   
129 C CB  . GLN A 22 ? 0.24970 0.18820 0.19770 0.00040  -0.00690 -0.01020 22 GLN A CB  
130 C CG  . GLN A 22 ? 0.25950 0.19740 0.21510 0.03310  -0.01740 -0.00030 22 GLN A CG  
131 C CD  . GLN A 22 ? 0.25610 0.22460 0.24230 0.04110  -0.01950 0.01640  22 GLN A CD  
132 O OE1 . GLN A 22 ? 0.25600 0.20180 0.26950 0.05360  -0.03260 0.01340  22 GLN A OE1 
133 N NE2 . GLN A 22 ? 0.28060 0.24270 0.24200 0.04430  -0.04430 0.02560  22 GLN A NE2 
134 N N   . GLU A 23 ? 0.19480 0.14650 0.15770 0.00520  -0.00550 0.00520  23 GLU A N   
135 C CA  . GLU A 23 ? 0.19960 0.15820 0.18040 0.01450  -0.00660 -0.00660 23 GLU A CA  
136 C C   . GLU A 23 ? 0.17620 0.14210 0.18240 0.01260  -0.00040 -0.01700 23 GLU A C   
137 O O   . GLU A 23 ? 0.16620 0.14610 0.18390 0.02290  -0.01090 -0.02590 23 GLU A O   
138 C CB  . GLU A 23 ? 0.23440 0.18850 0.19020 0.03060  -0.01800 0.00030  23 GLU A CB  
139 C CG  . GLU A 23 ? 0.31550 0.23940 0.21460 0.03480  -0.02910 0.01950  23 GLU A CG  
140 C CD  . GLU A 23 ? 0.35740 0.26100 0.21940 0.04660  -0.04610 0.01310  23 GLU A CD  
141 O OE1 . GLU A 23 ? 0.35130 0.21580 0.22090 0.05820  -0.05440 -0.01700 23 GLU A OE1 
142 O OE2 . GLU A 23 ? 0.40450 0.31170 0.24700 0.04730  -0.03230 0.01280  23 GLU A OE2 
143 N N   . ASN A 24 ? 0.16630 0.14370 0.15950 0.01860  -0.00700 -0.02250 24 ASN A N   
144 C CA  . ASN A 24 ? 0.18780 0.14470 0.14700 0.01360  -0.00610 -0.02200 24 ASN A CA  
145 C C   . ASN A 24 ? 0.16360 0.13400 0.14990 -0.00360 0.00200  -0.01470 24 ASN A C   
146 O O   . ASN A 24 ? 0.18250 0.13100 0.15440 -0.00160 0.00870  -0.02080 24 ASN A O   
147 C CB  . ASN A 24 ? 0.22620 0.15250 0.14170 0.02360  -0.00080 -0.03430 24 ASN A CB  
148 C CG  . ASN A 24 ? 0.21080 0.16180 0.16700 0.02230  -0.00660 -0.03370 24 ASN A CG  
149 O OD1 . ASN A 24 ? 0.24000 0.15410 0.18320 -0.00030 0.00300  -0.00190 24 ASN A OD1 
150 N ND2 . ASN A 24 ? 0.22390 0.21460 0.18330 0.03330  -0.00780 -0.03170 24 ASN A ND2 
151 N N   . LEU A 25 ? 0.16310 0.13100 0.14950 0.01090  0.00740  -0.01880 25 LEU A N   
152 C CA  . LEU A 25 ? 0.15720 0.12380 0.16840 -0.00560 0.00570  -0.01560 25 LEU A CA  
153 C C   . LEU A 25 ? 0.14920 0.12570 0.15880 -0.00130 0.01230  -0.01280 25 LEU A C   
154 O O   . LEU A 25 ? 0.15770 0.12810 0.17350 0.00670  0.00380  -0.02350 25 LEU A O   
155 C CB  . LEU A 25 ? 0.16280 0.14840 0.17540 0.00210  0.00080  -0.01060 25 LEU A CB  
156 C CG  . LEU A 25 ? 0.16520 0.12990 0.19480 0.00030  0.00380  -0.01880 25 LEU A CG  
157 C CD1 . LEU A 25 ? 0.18500 0.15570 0.21260 0.03100  -0.00300 -0.01620 25 LEU A CD1 
158 C CD2 . LEU A 25 ? 0.17620 0.14930 0.19380 -0.02220 0.01630  -0.01120 25 LEU A CD2 
159 N N   . SER A 26 ? 0.15280 0.15680 0.16800 0.00160  -0.02520 -0.01290 26 SER A N   
160 C CA  . SER A 26 ? 0.16860 0.16530 0.17040 -0.00410 -0.02270 -0.00940 26 SER A CA  
161 C C   . SER A 26 ? 0.16680 0.16110 0.18750 0.00150  -0.01940 0.01060  26 SER A C   
162 O O   . SER A 26 ? 0.18850 0.16760 0.20610 -0.02670 -0.03890 0.00180  26 SER A O   
163 C CB  . SER A 26 ? 0.19060 0.19820 0.18470 -0.01140 -0.05020 -0.01460 26 SER A CB  
164 O OG  . SER A 26 ? 0.22350 0.22580 0.22840 -0.04000 -0.06030 -0.00970 26 SER A OG  
165 N N   . ARG A 27 ? 0.15940 0.17770 0.20410 0.00740  0.00110  -0.00870 27 ARG A N   
166 C CA  . ARG A 27 ? 0.17290 0.18360 0.21030 0.00750  0.00920  0.00410  27 ARG A CA  
167 C C   . ARG A 27 ? 0.16160 0.18320 0.20250 -0.01320 -0.00910 0.00180  27 ARG A C   
168 O O   . ARG A 27 ? 0.18390 0.19140 0.23740 -0.02260 0.00610  0.02080  27 ARG A O   
169 C CB  . ARG A 27 ? 0.17750 0.20730 0.23310 0.01190  0.03560  0.00940  27 ARG A CB  
170 C CG  . ARG A 27 ? 0.20630 0.24290 0.25690 0.01700  0.05120  0.00250  27 ARG A CG  
171 C CD  . ARG A 27 ? 0.23570 0.25950 0.27780 0.00520  0.03120  0.00670  27 ARG A CD  
172 N NE  . ARG A 27 ? 0.28070 0.26150 0.27720 0.01300  0.02480  0.02000  27 ARG A NE  
173 C CZ  . ARG A 27 ? 0.32460 0.26680 0.27480 0.00460  0.03400  0.03550  27 ARG A CZ  
174 N NH1 . ARG A 27 ? 0.34990 0.27680 0.27640 -0.01120 0.06510  0.03400  27 ARG A NH1 
175 N NH2 . ARG A 27 ? 0.33480 0.24440 0.28440 0.02010  0.02340  0.04010  27 ARG A NH2 
176 N N   . TYR A 28 ? 0.16310 0.17390 0.17870 0.01220  -0.00740 -0.01650 28 TYR A N   
177 C CA  . TYR A 28 ? 0.16820 0.17240 0.15990 0.00580  -0.01380 -0.00990 28 TYR A CA  
178 C C   . TYR A 28 ? 0.16850 0.16430 0.16130 -0.00300 0.00110  0.01470  28 TYR A C   
179 O O   . TYR A 28 ? 0.19940 0.16800 0.16920 -0.00130 0.02330  0.00640  28 TYR A O   
180 C CB  . TYR A 28 ? 0.17610 0.18510 0.15870 -0.00630 -0.02530 -0.00440 28 TYR A CB  
181 C CG  . TYR A 28 ? 0.17890 0.21270 0.16120 0.01190  -0.00450 0.00480  28 TYR A CG  
182 C CD1 . TYR A 28 ? 0.21900 0.25760 0.16650 0.04330  -0.00960 -0.00650 28 TYR A CD1 
183 C CD2 . TYR A 28 ? 0.16830 0.20220 0.18740 -0.00230 -0.00570 0.01330  28 TYR A CD2 
184 C CE1 . TYR A 28 ? 0.24240 0.26900 0.18990 0.06580  0.01710  0.02280  28 TYR A CE1 
185 C CE2 . TYR A 28 ? 0.19570 0.23010 0.19470 0.00500  0.00840  0.03030  28 TYR A CE2 
186 C CZ  . TYR A 28 ? 0.22830 0.25290 0.19570 0.05020  0.00970  0.04020  28 TYR A CZ  
187 O OH  . TYR A 28 ? 0.26220 0.28120 0.22400 0.06560  0.00020  0.05610  28 TYR A OH  
188 N N   . PHE A 29 ? 0.15140 0.15760 0.15700 -0.00420 -0.00030 -0.01470 29 PHE A N   
189 C CA  . PHE A 29 ? 0.15620 0.16270 0.15780 -0.00010 0.00520  -0.01090 29 PHE A CA  
190 C C   . PHE A 29 ? 0.17110 0.16040 0.15910 -0.00910 0.00820  -0.01290 29 PHE A C   
191 O O   . PHE A 29 ? 0.17810 0.15160 0.16000 -0.02530 0.00400  -0.00760 29 PHE A O   
192 C CB  . PHE A 29 ? 0.15860 0.15730 0.16650 -0.00880 0.01440  -0.01260 29 PHE A CB  
193 C CG  . PHE A 29 ? 0.14370 0.13850 0.18480 -0.00770 0.00500  -0.00850 29 PHE A CG  
194 C CD1 . PHE A 29 ? 0.16960 0.13950 0.22210 0.01450  0.00710  0.00540  29 PHE A CD1 
195 C CD2 . PHE A 29 ? 0.13980 0.13640 0.18680 -0.02000 0.01490  -0.01760 29 PHE A CD2 
196 C CE1 . PHE A 29 ? 0.16700 0.15830 0.22750 0.00950  0.00650  0.00200  29 PHE A CE1 
197 C CE2 . PHE A 29 ? 0.16490 0.13590 0.17920 0.00190  0.00370  -0.01240 29 PHE A CE2 
198 C CZ  . PHE A 29 ? 0.16620 0.14030 0.21300 0.00660  0.00680  -0.01240 29 PHE A CZ  
199 N N   . CYS A 30 ? 0.15510 0.18590 0.17050 -0.02770 -0.01540 -0.01660 30 CYS A N   
200 C CA  . CYS A 30 ? 0.15830 0.20660 0.19120 -0.01180 -0.01830 0.00400  30 CYS A CA  
201 C C   . CYS A 30 ? 0.15970 0.22020 0.18500 -0.02540 0.00440  -0.03260 30 CYS A C   
202 O O   . CYS A 30 ? 0.15340 0.24250 0.19830 -0.04000 -0.00040 -0.02910 30 CYS A O   
203 C CB  . CYS A 30 ? 0.20040 0.23850 0.25210 -0.05350 -0.05610 0.02010  30 CYS A CB  
204 S SG  . CYS A 30 ? 0.23370 0.24280 0.29440 -0.02000 -0.03260 0.01260  30 CYS A SG  
205 N N   . ARG A 31 ? 0.18460 0.22780 0.17230 -0.04750 0.02060  -0.03810 31 ARG A N   
206 C CA  . ARG A 31 ? 0.22480 0.25490 0.17310 -0.06170 0.01610  -0.03720 31 ARG A CA  
207 C C   . ARG A 31 ? 0.21410 0.24060 0.16540 -0.07940 0.01700  0.00100  31 ARG A C   
208 O O   . ARG A 31 ? 0.25370 0.25530 0.19080 -0.09290 0.04470  0.01510  31 ARG A O   
209 C CB  . ARG A 31 ? 0.28920 0.32690 0.19880 -0.04110 -0.00210 -0.06150 31 ARG A CB  
210 C CG  . ARG A 31 ? 0.35110 0.38690 0.22860 -0.04050 -0.02830 -0.10580 31 ARG A CG  
211 C CD  . ARG A 31 ? 0.41830 0.46610 0.27890 -0.02300 -0.04740 -0.12910 31 ARG A CD  
212 N NE  . ARG A 31 ? 0.47070 0.51380 0.31510 -0.01850 -0.04880 -0.14710 31 ARG A NE  
213 C CZ  . ARG A 31 ? 0.51500 0.54540 0.33020 -0.01740 -0.03990 -0.15850 31 ARG A CZ  
214 N NH1 . ARG A 31 ? 0.52580 0.55300 0.32960 -0.01640 -0.03810 -0.16650 31 ARG A NH1 
215 N NH2 . ARG A 31 ? 0.52320 0.55330 0.33470 -0.01930 -0.04500 -0.16540 31 ARG A NH2 
216 N N   . PHE A 32 ? 0.16660 0.21210 0.14640 -0.03330 0.00160  0.03410  32 PHE A N   
217 C CA  . PHE A 32 ? 0.18110 0.19260 0.16790 -0.03010 -0.01200 0.02700  32 PHE A CA  
218 C C   . PHE A 32 ? 0.18030 0.17540 0.17490 -0.01020 -0.02100 0.01670  32 PHE A C   
219 O O   . PHE A 32 ? 0.23220 0.16340 0.19760 0.01550  -0.04130 0.01600  32 PHE A O   
220 C CB  . PHE A 32 ? 0.19110 0.20680 0.17470 -0.02690 -0.02270 0.02210  32 PHE A CB  
221 C CG  . PHE A 32 ? 0.18100 0.21250 0.17440 -0.02910 -0.00710 0.03350  32 PHE A CG  
222 C CD1 . PHE A 32 ? 0.18250 0.21930 0.17570 -0.01900 0.00050  0.05160  32 PHE A CD1 
223 C CD2 . PHE A 32 ? 0.21470 0.23110 0.19530 -0.05160 -0.05210 0.02300  32 PHE A CD2 
224 C CE1 . PHE A 32 ? 0.19950 0.23730 0.18670 -0.02170 -0.01920 0.06640  32 PHE A CE1 
225 C CE2 . PHE A 32 ? 0.22140 0.26180 0.21340 -0.03260 -0.04560 0.03170  32 PHE A CE2 
226 C CZ  . PHE A 32 ? 0.20580 0.26170 0.20060 -0.02580 -0.02310 0.04760  32 PHE A CZ  
227 N N   . GLY A 33 ? 0.14160 0.17340 0.16850 -0.01460 -0.01110 0.00720  33 GLY A N   
228 C CA  . GLY A 33 ? 0.17190 0.17010 0.17230 -0.01730 -0.03630 0.00580  33 GLY A CA  
229 C C   . GLY A 33 ? 0.15520 0.17080 0.16450 -0.00740 0.00640  -0.00880 33 GLY A C   
230 O O   . GLY A 33 ? 0.17730 0.17370 0.16670 -0.01630 -0.00630 -0.01320 33 GLY A O   
231 N N   . ASP A 34 ? 0.13790 0.16350 0.16550 -0.01250 -0.00090 -0.00240 34 ASP A N   
232 C CA  . ASP A 34 ? 0.13920 0.15560 0.17530 -0.01830 -0.01690 -0.00770 34 ASP A CA  
233 C C   . ASP A 34 ? 0.13460 0.14850 0.15950 -0.00360 -0.01870 -0.01960 34 ASP A C   
234 O O   . ASP A 34 ? 0.14290 0.14780 0.16690 -0.00470 0.00470  -0.00990 34 ASP A O   
235 C CB  . ASP A 34 ? 0.13170 0.17640 0.19200 -0.02380 -0.00450 -0.00810 34 ASP A CB  
236 C CG  . ASP A 34 ? 0.15700 0.17060 0.19230 -0.02370 0.00610  -0.04300 34 ASP A CG  
237 O OD1 . ASP A 34 ? 0.14810 0.18330 0.20800 -0.00810 -0.01440 -0.02260 34 ASP A OD1 
238 O OD2 . ASP A 34 ? 0.17110 0.19330 0.21560 -0.03230 0.02730  -0.02020 34 ASP A OD2 
239 N N   . ILE A 35 ? 0.13720 0.14100 0.14990 -0.00820 -0.00350 -0.00630 35 ILE A N   
240 C CA  . ILE A 35 ? 0.13950 0.14170 0.14820 -0.01370 -0.01620 0.00190  35 ILE A CA  
241 C C   . ILE A 35 ? 0.14500 0.13410 0.15850 0.00390  -0.01660 -0.00050 35 ILE A C   
242 O O   . ILE A 35 ? 0.15650 0.15560 0.16680 0.01040  -0.00400 0.00570  35 ILE A O   
243 C CB  . ILE A 35 ? 0.15630 0.15420 0.15260 -0.02310 -0.00220 0.00000  35 ILE A CB  
244 C CG1 . ILE A 35 ? 0.17620 0.19530 0.15450 -0.03170 -0.01270 0.00350  35 ILE A CG1 
245 C CG2 . ILE A 35 ? 0.15050 0.16820 0.17140 -0.03800 -0.00650 -0.00630 35 ILE A CG2 
246 C CD1 . ILE A 35 ? 0.18730 0.23440 0.14420 -0.03500 -0.01980 -0.00740 35 ILE A CD1 
247 N N   . ILE A 36 ? 0.15830 0.13720 0.14120 -0.01560 -0.01510 0.00200  36 ILE A N   
248 C CA  . ILE A 36 ? 0.15560 0.15310 0.14390 -0.00710 -0.01650 0.00400  36 ILE A CA  
249 C C   . ILE A 36 ? 0.14600 0.16160 0.15990 -0.00760 -0.01250 0.01240  36 ILE A C   
250 O O   . ILE A 36 ? 0.16860 0.18440 0.17230 -0.01390 -0.02690 0.02500  36 ILE A O   
251 C CB  . ILE A 36 ? 0.17070 0.16830 0.16280 0.00560  -0.00980 -0.01310 36 ILE A CB  
252 C CG1 . ILE A 36 ? 0.20790 0.16710 0.18520 0.03720  -0.01000 -0.02060 36 ILE A CG1 
253 C CG2 . ILE A 36 ? 0.19640 0.17440 0.18750 -0.03060 -0.03060 -0.00380 36 ILE A CG2 
254 C CD1 . ILE A 36 ? 0.23180 0.20470 0.19490 0.03480  -0.00150 -0.03820 36 ILE A CD1 
255 N N   . ASP A 37 ? 0.14780 0.13580 0.16460 -0.00680 -0.02090 -0.00730 37 ASP A N   
256 C CA  . ASP A 37 ? 0.15090 0.14440 0.18170 -0.00220 -0.00720 0.00570  37 ASP A CA  
257 C C   . ASP A 37 ? 0.15100 0.12950 0.18290 -0.00920 -0.01230 0.00690  37 ASP A C   
258 O O   . ASP A 37 ? 0.17420 0.12600 0.17550 0.00040  -0.01090 0.00220  37 ASP A O   
259 C CB  . ASP A 37 ? 0.16110 0.17860 0.20530 -0.04150 -0.01870 0.02690  37 ASP A CB  
260 C CG  . ASP A 37 ? 0.20190 0.22530 0.25940 -0.03940 -0.03310 0.03860  37 ASP A CG  
261 O OD1 . ASP A 37 ? 0.24590 0.23730 0.30370 -0.02780 -0.03960 0.04320  37 ASP A OD1 
262 O OD2 . ASP A 37 ? 0.22280 0.23150 0.29070 -0.03970 -0.02260 0.04730  37 ASP A OD2 
263 N N   . CYS A 38 ? 0.15390 0.13700 0.18900 -0.00300 -0.01080 0.00450  38 CYS A N   
264 C CA  . CYS A 38 ? 0.16150 0.12460 0.19520 -0.00230 -0.00620 -0.01590 38 CYS A CA  
265 C C   . CYS A 38 ? 0.17840 0.12420 0.24260 0.02480  -0.03020 -0.00670 38 CYS A C   
266 O O   . CYS A 38 ? 0.18050 0.14250 0.31910 0.00800  -0.03110 -0.00450 38 CYS A O   
267 C CB  . CYS A 38 ? 0.19160 0.18910 0.19910 0.00690  -0.00500 -0.04030 38 CYS A CB  
268 S SG  . CYS A 38 ? 0.22610 0.22270 0.20440 0.02710  -0.01280 -0.05930 38 CYS A SG  
269 N N   . VAL A 39 ? 0.15690 0.12440 0.22120 0.00330  -0.01830 -0.01280 39 VAL A N   
270 C CA  . VAL A 39 ? 0.18740 0.12190 0.21740 -0.00690 -0.02800 0.00220  39 VAL A CA  
271 C C   . VAL A 39 ? 0.17190 0.11280 0.21580 -0.00190 -0.02330 -0.00640 39 VAL A C   
272 O O   . VAL A 39 ? 0.18610 0.11370 0.24570 0.01670  -0.02900 -0.01270 39 VAL A O   
273 C CB  . VAL A 39 ? 0.22010 0.16900 0.22900 -0.01590 -0.01130 0.01080  39 VAL A CB  
274 C CG1 . VAL A 39 ? 0.27800 0.23040 0.24270 -0.00660 -0.02900 0.01390  39 VAL A CG1 
275 C CG2 . VAL A 39 ? 0.23760 0.18950 0.22420 -0.00210 0.01490  0.00040  39 VAL A CG2 
276 N N   . VAL A 40 ? 0.16630 0.11660 0.19930 -0.00190 -0.00350 -0.00560 40 VAL A N   
277 C CA  . VAL A 40 ? 0.18300 0.11670 0.19190 -0.01940 0.00850  -0.01630 40 VAL A CA  
278 C C   . VAL A 40 ? 0.18720 0.11880 0.19920 0.00240  -0.00190 -0.00060 40 VAL A C   
279 O O   . VAL A 40 ? 0.19950 0.13120 0.21490 0.00780  0.00100  0.01830  40 VAL A O   
280 C CB  . VAL A 40 ? 0.20460 0.12800 0.20410 -0.02480 0.01830  -0.02470 40 VAL A CB  
281 C CG1 . VAL A 40 ? 0.21850 0.15760 0.17400 -0.03510 0.01850  -0.02070 40 VAL A CG1 
282 C CG2 . VAL A 40 ? 0.22930 0.16690 0.21480 -0.00970 0.02510  -0.01190 40 VAL A CG2 
283 N N   . MET A 41 ? 0.17700 0.12630 0.19630 -0.01080 0.01410  -0.00870 41 MET A N   
284 C CA  . MET A 41 ? 0.19650 0.11870 0.21180 -0.01470 0.03750  0.00380  41 MET A CA  
285 C C   . MET A 41 ? 0.23040 0.12470 0.22950 -0.02610 0.04350  0.00290  41 MET A C   
286 O O   . MET A 41 ? 0.21870 0.13930 0.23190 -0.02560 0.02090  -0.00480 41 MET A O   
287 C CB  . MET A 41 ? 0.21760 0.14050 0.21530 -0.01290 0.04060  -0.00920 41 MET A CB  
288 C CG  . MET A 41 ? 0.27990 0.16100 0.21360 -0.00920 -0.00310 -0.00320 41 MET A CG  
289 S SD  . MET A 41 ? 0.39880 0.17660 0.23900 -0.02270 -0.04460 -0.01520 41 MET A SD  
290 C CE  . MET A 41 ? 0.44000 0.23730 0.25990 -0.02710 -0.02640 -0.01300 41 MET A CE  
291 N N   . LYS A 42 ? 0.23870 0.12820 0.25340 -0.02580 0.04780  0.01920  42 LYS A N   
292 C CA  . LYS A 42 ? 0.25500 0.12600 0.29720 -0.02180 0.05520  0.03210  42 LYS A CA  
293 C C   . LYS A 42 ? 0.26560 0.13490 0.32190 -0.01570 0.04990  0.04600  42 LYS A C   
294 O O   . LYS A 42 ? 0.25630 0.15660 0.30890 -0.02130 0.05100  0.03500  42 LYS A O   
295 C CB  . LYS A 42 ? 0.27230 0.16770 0.32390 -0.01550 0.05710  0.00470  42 LYS A CB  
296 C CG  . LYS A 42 ? 0.29660 0.19570 0.33510 -0.02060 0.06470  -0.00390 42 LYS A CG  
297 C CD  . LYS A 42 ? 0.29230 0.19450 0.32920 -0.02650 0.05370  0.00860  42 LYS A CD  
298 C CE  . LYS A 42 ? 0.26320 0.16950 0.33000 -0.02470 0.06570  -0.00470 42 LYS A CE  
299 N NZ  . LYS A 42 ? 0.25670 0.16740 0.32960 0.01500  0.04080  -0.00210 42 LYS A NZ  
300 N N   . ASN A 43 ? 0.27820 0.15700 0.37080 -0.05560 0.04010  0.04660  43 ASN A N   
301 C CA  . ASN A 43 ? 0.36330 0.21020 0.44710 -0.09220 0.02740  0.06370  43 ASN A CA  
302 C C   . ASN A 43 ? 0.46910 0.23320 0.49840 -0.08250 0.02340  0.09310  43 ASN A C   
303 O O   . ASN A 43 ? 0.47280 0.20360 0.49600 -0.07710 0.01340  0.11720  43 ASN A O   
304 C CB  . ASN A 43 ? 0.36750 0.24990 0.47690 -0.13260 0.01420  0.05720  43 ASN A CB  
305 C CG  . ASN A 43 ? 0.38880 0.30580 0.51220 -0.12350 -0.00080 0.04660  43 ASN A CG  
306 O OD1 . ASN A 43 ? 0.42820 0.34660 0.53210 -0.09170 -0.01230 0.03660  43 ASN A OD1 
307 N ND2 . ASN A 43 ? 0.38480 0.30920 0.51700 -0.13820 0.00260  0.05880  43 ASN A ND2 
308 N N   . ASN A 44 ? 0.56670 0.29380 0.54730 -0.06000 0.02570  0.10560  44 ASN A N   
309 C CA  . ASN A 44 ? 0.67270 0.36530 0.60050 -0.01580 0.01890  0.09390  44 ASN A CA  
310 C C   . ASN A 44 ? 0.70540 0.37790 0.62740 -0.02490 0.03740  0.10340  44 ASN A C   
311 O O   . ASN A 44 ? 0.70880 0.38770 0.63630 -0.02490 0.03550  0.11170  44 ASN A O   
312 C CB  . ASN A 44 ? 0.73750 0.41870 0.62310 0.02780  -0.00320 0.07090  44 ASN A CB  
313 C CG  . ASN A 44 ? 0.78930 0.46580 0.64420 0.06630  -0.01710 0.04840  44 ASN A CG  
314 O OD1 . ASN A 44 ? 0.81150 0.48940 0.65130 0.07380  -0.02080 0.04280  44 ASN A OD1 
315 N ND2 . ASN A 44 ? 0.80490 0.48090 0.65250 0.08080  -0.02020 0.03890  44 ASN A ND2 
316 N N   . GLU A 45 ? 0.73590 0.37620 0.64350 -0.04000 0.05860  0.09680  45 GLU A N   
317 C CA  . GLU A 45 ? 0.76640 0.38230 0.65860 -0.04720 0.07350  0.08320  45 GLU A CA  
318 C C   . GLU A 45 ? 0.76720 0.33500 0.63780 -0.06130 0.07400  0.09540  45 GLU A C   
319 O O   . GLU A 45 ? 0.79190 0.34220 0.64270 -0.06390 0.07870  0.11170  45 GLU A O   
320 C CB  . GLU A 45 ? 0.78820 0.43790 0.69260 -0.04430 0.08540  0.05420  45 GLU A CB  
321 C CG  . GLU A 45 ? 0.80760 0.48980 0.72170 -0.04510 0.09460  0.02810  45 GLU A CG  
322 C CD  . GLU A 45 ? 0.82710 0.53640 0.74630 -0.05010 0.09990  0.00270  45 GLU A CD  
323 O OE1 . GLU A 45 ? 0.83620 0.55580 0.75410 -0.05140 0.10070  -0.00430 45 GLU A OE1 
324 O OE2 . GLU A 45 ? 0.83180 0.55040 0.75510 -0.05190 0.10220  -0.00710 45 GLU A OE2 
325 N N   . SER A 46 ? 0.73200 0.27000 0.60720 -0.08310 0.06790  0.09040  46 SER A N   
326 C CA  . SER A 46 ? 0.68700 0.21530 0.57790 -0.07830 0.05200  0.06450  46 SER A CA  
327 C C   . SER A 46 ? 0.65350 0.20680 0.54660 -0.02230 0.03450  0.06270  46 SER A C   
328 O O   . SER A 46 ? 0.66080 0.19550 0.55020 0.01330  0.02780  0.06370  46 SER A O   
329 C CB  . SER A 46 ? 0.67190 0.20690 0.57950 -0.10930 0.04620  0.03370  46 SER A CB  
330 O OG  . SER A 46 ? 0.64600 0.20860 0.57820 -0.12730 0.03910  0.01600  46 SER A OG  
331 N N   . GLY A 47 ? 0.60220 0.17780 0.51200 0.00140  0.02550  0.05980  47 GLY A N   
332 C CA  . GLY A 47 ? 0.55100 0.17930 0.47940 0.01730  0.02850  0.04350  47 GLY A CA  
333 C C   . GLY A 47 ? 0.50310 0.14980 0.45080 0.01310  0.03430  0.01430  47 GLY A C   
334 O O   . GLY A 47 ? 0.49210 0.17430 0.45140 0.02780  0.02610  -0.00090 47 GLY A O   
335 N N   . ARG A 48 ? 0.47920 0.14370 0.42780 -0.00470 0.04820  0.00330  48 ARG A N   
336 C CA  . ARG A 48 ? 0.46770 0.15480 0.40720 -0.00090 0.03320  -0.00640 48 ARG A CA  
337 C C   . ARG A 48 ? 0.36810 0.13810 0.33750 -0.01200 0.04720  -0.01210 48 ARG A C   
338 O O   . ARG A 48 ? 0.35810 0.14150 0.31640 -0.02720 0.05200  0.00830  48 ARG A O   
339 C CB  . ARG A 48 ? 0.56530 0.19280 0.46150 -0.02510 0.00560  -0.01700 48 ARG A CB  
340 C CG  . ARG A 48 ? 0.65650 0.27280 0.51810 -0.04890 -0.00740 -0.01580 48 ARG A CG  
341 C CD  . ARG A 48 ? 0.73610 0.35040 0.56840 -0.06410 -0.01490 -0.00610 48 ARG A CD  
342 N NE  . ARG A 48 ? 0.80660 0.41270 0.61250 -0.06960 -0.02000 0.00300  48 ARG A NE  
343 C CZ  . ARG A 48 ? 0.85810 0.45860 0.64550 -0.06680 -0.02420 0.01120  48 ARG A CZ  
344 N NH1 . ARG A 48 ? 0.87930 0.47240 0.65570 -0.06250 -0.02350 0.01390  48 ARG A NH1 
345 N NH2 . ARG A 48 ? 0.87080 0.47670 0.65620 -0.06730 -0.02620 0.01360  48 ARG A NH2 
346 N N   . SER A 49 ? 0.29910 0.12860 0.28570 -0.03970 0.04160  -0.02430 49 SER A N   
347 C CA  . SER A 49 ? 0.24490 0.15530 0.25190 -0.02710 0.03090  -0.01490 49 SER A CA  
348 C C   . SER A 49 ? 0.23010 0.15020 0.24230 -0.04650 0.01220  -0.02430 49 SER A C   
349 O O   . SER A 49 ? 0.25140 0.17980 0.26370 -0.06290 0.00420  -0.02320 49 SER A O   
350 C CB  . SER A 49 ? 0.23950 0.16740 0.22220 -0.02730 0.03520  -0.00330 49 SER A CB  
351 O OG  . SER A 49 ? 0.20440 0.16150 0.20520 -0.01650 0.02410  -0.01080 49 SER A OG  
352 N N   . ARG A 50 ? 0.21600 0.13790 0.22030 -0.02140 0.03850  -0.01980 50 ARG A N   
353 C CA  . ARG A 50 ? 0.22560 0.14950 0.23080 -0.02840 0.02550  -0.02540 50 ARG A CA  
354 C C   . ARG A 50 ? 0.19910 0.16270 0.22750 -0.04290 0.01140  -0.01960 50 ARG A C   
355 O O   . ARG A 50 ? 0.20470 0.18080 0.25480 -0.03950 0.00430  -0.01130 50 ARG A O   
356 C CB  . ARG A 50 ? 0.23250 0.13900 0.23530 -0.03650 0.03900  -0.01080 50 ARG A CB  
357 C CG  . ARG A 50 ? 0.23870 0.15040 0.23820 -0.03880 0.04530  -0.00330 50 ARG A CG  
358 C CD  . ARG A 50 ? 0.22860 0.16100 0.23890 -0.00820 0.05930  -0.00020 50 ARG A CD  
359 N NE  . ARG A 50 ? 0.20680 0.15240 0.24010 -0.00520 0.06580  -0.00370 50 ARG A NE  
360 C CZ  . ARG A 50 ? 0.19350 0.15150 0.23480 -0.00510 0.04630  0.01270  50 ARG A CZ  
361 N NH1 . ARG A 50 ? 0.22740 0.16170 0.22380 -0.02320 0.03740  0.02490  50 ARG A NH1 
362 N NH2 . ARG A 50 ? 0.19390 0.16390 0.25400 -0.00280 0.04860  0.00720  50 ARG A NH2 
363 N N   . GLY A 51 ? 0.20430 0.15900 0.19720 -0.04450 0.01500  -0.01470 51 GLY A N   
364 C CA  . GLY A 51 ? 0.21430 0.16760 0.19350 -0.04090 -0.00080 -0.00550 51 GLY A CA  
365 C C   . GLY A 51 ? 0.18440 0.16000 0.18510 -0.03420 -0.00190 0.00690  51 GLY A C   
366 O O   . GLY A 51 ? 0.18370 0.17450 0.18180 -0.02110 -0.00200 0.01000  51 GLY A O   
367 N N   . PHE A 52 ? 0.16790 0.14430 0.19460 -0.03280 0.00770  -0.00110 52 PHE A N   
368 C CA  . PHE A 52 ? 0.16710 0.13920 0.19410 -0.01300 -0.00380 -0.00680 52 PHE A CA  
369 C C   . PHE A 52 ? 0.16710 0.13250 0.17860 -0.01110 0.00810  0.00490  52 PHE A C   
370 O O   . PHE A 52 ? 0.17840 0.13210 0.17520 -0.02540 0.00650  0.01510  52 PHE A O   
371 C CB  . PHE A 52 ? 0.17780 0.14340 0.19610 -0.01980 0.00910  -0.00330 52 PHE A CB  
372 C CG  . PHE A 52 ? 0.16110 0.14350 0.20020 -0.01310 0.00290  0.00080  52 PHE A CG  
373 C CD1 . PHE A 52 ? 0.19510 0.15050 0.20170 -0.02520 0.00930  0.01150  52 PHE A CD1 
374 C CD2 . PHE A 52 ? 0.17910 0.15630 0.20350 -0.00660 0.01320  0.00570  52 PHE A CD2 
375 C CE1 . PHE A 52 ? 0.23540 0.16290 0.22140 -0.02910 0.03740  -0.01160 52 PHE A CE1 
376 C CE2 . PHE A 52 ? 0.20620 0.15870 0.21280 -0.01680 0.02150  0.00480  52 PHE A CE2 
377 C CZ  . PHE A 52 ? 0.21270 0.15770 0.22080 -0.02920 0.03820  -0.00130 52 PHE A CZ  
378 N N   . GLY A 53 ? 0.16510 0.12380 0.17150 -0.01400 -0.00520 0.00730  53 GLY A N   
379 C CA  . GLY A 53 ? 0.16970 0.13200 0.17120 -0.01220 -0.01450 0.00540  53 GLY A CA  
380 C C   . GLY A 53 ? 0.15180 0.12390 0.16030 0.00280  0.00360  0.01640  53 GLY A C   
381 O O   . GLY A 53 ? 0.14560 0.13810 0.15170 -0.00810 -0.00000 0.00870  53 GLY A O   
382 N N   . PHE A 54 ? 0.14470 0.11510 0.15620 -0.00870 -0.00080 0.00310  54 PHE A N   
383 C CA  . PHE A 54 ? 0.16050 0.11020 0.15660 -0.00920 0.00520  -0.01550 54 PHE A CA  
384 C C   . PHE A 54 ? 0.14980 0.10500 0.17260 0.01000  -0.01050 -0.00170 54 PHE A C   
385 O O   . PHE A 54 ? 0.14990 0.11280 0.22060 0.00270  -0.00580 0.01890  54 PHE A O   
386 C CB  . PHE A 54 ? 0.15710 0.15230 0.14270 0.00520  -0.00600 -0.00530 54 PHE A CB  
387 C CG  . PHE A 54 ? 0.15420 0.14600 0.14540 0.00110  0.00290  0.00070  54 PHE A CG  
388 C CD1 . PHE A 54 ? 0.14280 0.15940 0.14490 0.01190  0.00560  -0.01300 54 PHE A CD1 
389 C CD2 . PHE A 54 ? 0.16440 0.16520 0.16790 -0.01580 0.01540  0.00340  54 PHE A CD2 
390 C CE1 . PHE A 54 ? 0.15520 0.15750 0.16520 -0.00690 0.01370  0.00720  54 PHE A CE1 
391 C CE2 . PHE A 54 ? 0.16970 0.16570 0.19330 -0.00830 0.01070  0.01130  54 PHE A CE2 
392 C CZ  . PHE A 54 ? 0.16690 0.15530 0.18500 0.00760  0.01570  0.01840  54 PHE A CZ  
393 N N   . VAL A 55 ? 0.14300 0.10770 0.16940 -0.00980 -0.02010 -0.00280 55 VAL A N   
394 C CA  . VAL A 55 ? 0.14640 0.13130 0.16930 -0.02730 -0.00580 0.00350  55 VAL A CA  
395 C C   . VAL A 55 ? 0.14090 0.11920 0.17440 -0.01320 -0.02140 -0.00430 55 VAL A C   
396 O O   . VAL A 55 ? 0.15210 0.13920 0.19460 0.00990  -0.03200 -0.00730 55 VAL A O   
397 C CB  . VAL A 55 ? 0.17800 0.17070 0.17240 -0.03210 0.00700  -0.00260 55 VAL A CB  
398 C CG1 . VAL A 55 ? 0.17840 0.20340 0.19790 -0.03050 0.01770  0.01570  55 VAL A CG1 
399 C CG2 . VAL A 55 ? 0.25700 0.18740 0.18810 -0.02630 0.01590  -0.02070 55 VAL A CG2 
400 N N   . THR A 56 ? 0.14240 0.13260 0.15700 -0.01370 -0.00060 -0.00520 56 THR A N   
401 C CA  . THR A 56 ? 0.14460 0.14900 0.15950 -0.02240 0.00240  0.00490  56 THR A CA  
402 C C   . THR A 56 ? 0.13870 0.12600 0.15660 0.00250  -0.01440 -0.00380 56 THR A C   
403 O O   . THR A 56 ? 0.13700 0.13530 0.16830 -0.00040 -0.01870 -0.00490 56 THR A O   
404 C CB  . THR A 56 ? 0.17690 0.17510 0.16940 -0.03000 0.00190  0.00040  56 THR A CB  
405 O OG1 . THR A 56 ? 0.17010 0.19760 0.19640 -0.01130 -0.00640 0.01050  56 THR A OG1 
406 C CG2 . THR A 56 ? 0.20250 0.18950 0.17710 -0.01280 0.00640  -0.00800 56 THR A CG2 
407 N N   . PHE A 57 ? 0.14520 0.12050 0.15700 -0.00380 -0.01010 -0.00310 57 PHE A N   
408 C CA  . PHE A 57 ? 0.13640 0.14340 0.15850 -0.00200 -0.01570 -0.00230 57 PHE A CA  
409 C C   . PHE A 57 ? 0.14350 0.13740 0.15260 -0.00860 -0.00430 0.00480  57 PHE A C   
410 O O   . PHE A 57 ? 0.16590 0.18960 0.15510 -0.01800 0.00300  -0.02080 57 PHE A O   
411 C CB  . PHE A 57 ? 0.15650 0.14080 0.16030 0.00400  -0.01520 -0.00470 57 PHE A CB  
412 C CG  . PHE A 57 ? 0.14260 0.15100 0.15500 0.00490  -0.00710 0.00620  57 PHE A CG  
413 C CD1 . PHE A 57 ? 0.15790 0.16210 0.15510 -0.01210 -0.01460 0.01150  57 PHE A CD1 
414 C CD2 . PHE A 57 ? 0.17080 0.18910 0.15110 -0.00270 -0.02930 0.00870  57 PHE A CD2 
415 C CE1 . PHE A 57 ? 0.17730 0.15990 0.15300 -0.00350 -0.00810 0.00930  57 PHE A CE1 
416 C CE2 . PHE A 57 ? 0.18260 0.21160 0.15620 0.00410  -0.03880 0.00650  57 PHE A CE2 
417 C CZ  . PHE A 57 ? 0.19760 0.18380 0.16490 -0.00400 -0.01930 0.00350  57 PHE A CZ  
418 N N   . ALA A 58 ? 0.14400 0.15180 0.16270 -0.00320 -0.02390 0.00950  58 ALA A N   
419 C CA  . ALA A 58 ? 0.17070 0.16270 0.17400 -0.02120 -0.02760 -0.00690 58 ALA A CA  
420 C C   . ALA A 58 ? 0.18840 0.15380 0.17320 -0.02490 -0.02290 -0.01610 58 ALA A C   
421 O O   . ALA A 58 ? 0.23980 0.17040 0.18730 -0.02490 -0.01290 -0.02810 58 ALA A O   
422 C CB  . ALA A 58 ? 0.16450 0.20650 0.19140 -0.01320 -0.02040 0.00110  58 ALA A CB  
423 N N   . ASP A 59 ? 0.18880 0.14340 0.18190 -0.01340 -0.03510 0.00410  59 ASP A N   
424 C CA  . ASP A 59 ? 0.17380 0.14820 0.19410 -0.01030 -0.02010 -0.00220 59 ASP A CA  
425 C C   . ASP A 59 ? 0.17390 0.15250 0.19590 -0.00640 -0.02080 -0.00870 59 ASP A C   
426 O O   . ASP A 59 ? 0.16620 0.15050 0.17940 0.00580  -0.00680 0.00160  59 ASP A O   
427 C CB  . ASP A 59 ? 0.18260 0.15210 0.21260 -0.00270 -0.00840 0.00120  59 ASP A CB  
428 C CG  . ASP A 59 ? 0.18580 0.15150 0.24210 -0.01050 -0.00950 0.01690  59 ASP A CG  
429 O OD1 . ASP A 59 ? 0.19090 0.14830 0.24950 -0.01340 -0.01570 0.00650  59 ASP A OD1 
430 O OD2 . ASP A 59 ? 0.21060 0.15260 0.26360 -0.01970 -0.00110 0.01520  59 ASP A OD2 
431 N N   . PRO A 60 ? 0.17220 0.18700 0.19380 -0.01640 -0.01360 -0.02240 60 PRO A N   
432 C CA  . PRO A 60 ? 0.17440 0.18770 0.19860 -0.02140 -0.01070 -0.02670 60 PRO A CA  
433 C C   . PRO A 60 ? 0.17790 0.17880 0.21630 -0.00040 -0.01400 -0.02960 60 PRO A C   
434 O O   . PRO A 60 ? 0.16950 0.21400 0.21590 -0.00900 -0.01110 -0.02190 60 PRO A O   
435 C CB  . PRO A 60 ? 0.21390 0.22870 0.20280 -0.01800 -0.00340 -0.03510 60 PRO A CB  
436 C CG  . PRO A 60 ? 0.22690 0.26370 0.22620 0.00090  0.00000  -0.04800 60 PRO A CG  
437 C CD  . PRO A 60 ? 0.20340 0.22770 0.19650 0.00860  -0.00970 -0.04240 60 PRO A CD  
438 N N   . THR A 61 ? 0.18010 0.16200 0.22870 -0.00170 0.00330  -0.01350 61 THR A N   
439 C CA  . THR A 61 ? 0.18830 0.18370 0.25460 -0.01100 -0.01320 0.02320  61 THR A CA  
440 C C   . THR A 61 ? 0.18740 0.18680 0.24280 0.01490  -0.00970 0.04040  61 THR A C   
441 O O   . THR A 61 ? 0.19610 0.20860 0.25900 0.02480  -0.01060 0.05620  61 THR A O   
442 C CB  . THR A 61 ? 0.20450 0.18840 0.29770 -0.01120 -0.01340 0.02290  61 THR A CB  
443 O OG1 . THR A 61 ? 0.22120 0.19810 0.31500 -0.03570 -0.00480 0.03460  61 THR A OG1 
444 C CG2 . THR A 61 ? 0.23280 0.16730 0.31740 -0.01280 -0.01810 0.00450  61 THR A CG2 
445 N N   . ASN A 62 ? 0.16340 0.18520 0.22350 0.00450  -0.00820 0.02560  62 ASN A N   
446 C CA  . ASN A 62 ? 0.16830 0.19430 0.20320 0.00790  -0.01590 0.02290  62 ASN A CA  
447 C C   . ASN A 62 ? 0.15980 0.19340 0.18030 0.01290  0.01140  0.03030  62 ASN A C   
448 O O   . ASN A 62 ? 0.17310 0.21480 0.16790 0.01000  0.00230  0.02500  62 ASN A O   
449 C CB  . ASN A 62 ? 0.14710 0.20270 0.19240 0.00410  -0.00530 0.03890  62 ASN A CB  
450 C CG  . ASN A 62 ? 0.16110 0.22640 0.19870 0.01340  -0.00110 0.05450  62 ASN A CG  
451 O OD1 . ASN A 62 ? 0.16440 0.25520 0.22510 0.01030  -0.01220 0.04200  62 ASN A OD1 
452 N ND2 . ASN A 62 ? 0.15580 0.23610 0.22410 -0.00860 -0.01790 0.06660  62 ASN A ND2 
453 N N   . VAL A 63 ? 0.14720 0.17180 0.17260 0.00110  0.01010  0.01620  63 VAL A N   
454 C CA  . VAL A 63 ? 0.15100 0.16930 0.17700 0.00100  0.01460  0.01000  63 VAL A CA  
455 C C   . VAL A 63 ? 0.15500 0.15740 0.17710 -0.00230 0.00020  0.00370  63 VAL A C   
456 O O   . VAL A 63 ? 0.16800 0.17280 0.16470 -0.00810 0.00250  0.02730  63 VAL A O   
457 C CB  . VAL A 63 ? 0.16220 0.18120 0.18360 -0.00520 -0.00110 0.00110  63 VAL A CB  
458 C CG1 . VAL A 63 ? 0.17710 0.20140 0.21180 0.00240  -0.01010 -0.01220 63 VAL A CG1 
459 C CG2 . VAL A 63 ? 0.17820 0.19280 0.20150 0.00730  -0.00200 0.02960  63 VAL A CG2 
460 N N   . ASN A 64 ? 0.19080 0.16510 0.18540 0.01170  -0.01710 0.00770  64 ASN A N   
461 C CA  . ASN A 64 ? 0.24930 0.16370 0.20780 0.01640  -0.00770 0.01670  64 ASN A CA  
462 C C   . ASN A 64 ? 0.22480 0.15180 0.19530 -0.00850 -0.02050 0.01720  64 ASN A C   
463 O O   . ASN A 64 ? 0.23900 0.16440 0.18500 -0.00510 -0.02820 0.02070  64 ASN A O   
464 C CB  . ASN A 64 ? 0.31840 0.19590 0.26720 0.03490  0.01420  0.00100  64 ASN A CB  
465 C CG  . ASN A 64 ? 0.41660 0.26710 0.33880 0.01270  0.01230  -0.01690 64 ASN A CG  
466 O OD1 . ASN A 64 ? 0.43670 0.30630 0.36490 -0.00030 0.02350  -0.01950 64 ASN A OD1 
467 N ND2 . ASN A 64 ? 0.47170 0.29170 0.36690 0.01470  0.00950  -0.01660 64 ASN A ND2 
468 N N   . HIS A 65 ? 0.20100 0.13750 0.20150 -0.02420 -0.00710 0.01190  65 HIS A N   
469 C CA  . HIS A 65 ? 0.19870 0.15090 0.18900 -0.02790 0.00070  0.01720  65 HIS A CA  
470 C C   . HIS A 65 ? 0.20010 0.14310 0.16880 -0.04070 -0.00240 0.02380  65 HIS A C   
471 O O   . HIS A 65 ? 0.21700 0.16640 0.15220 -0.04290 -0.00060 0.02920  65 HIS A O   
472 C CB  . HIS A 65 ? 0.20080 0.16140 0.19530 -0.02860 0.01300  0.01810  65 HIS A CB  
473 C CG  . HIS A 65 ? 0.21790 0.15120 0.19640 -0.02740 -0.00130 0.01650  65 HIS A CG  
474 N ND1 . HIS A 65 ? 0.21850 0.17150 0.19130 -0.03720 -0.01350 0.01700  65 HIS A ND1 
475 C CD2 . HIS A 65 ? 0.21020 0.16590 0.19900 -0.04310 -0.01640 0.02020  65 HIS A CD2 
476 C CE1 . HIS A 65 ? 0.20850 0.17210 0.18750 -0.03600 -0.00820 0.01700  65 HIS A CE1 
477 N NE2 . HIS A 65 ? 0.21560 0.17730 0.20200 -0.02120 -0.00560 0.01400  65 HIS A NE2 
478 N N   . VAL A 66 ? 0.18220 0.13300 0.17410 -0.02900 0.01170  0.01770  66 VAL A N   
479 C CA  . VAL A 66 ? 0.16120 0.12770 0.18530 -0.01870 0.00340  0.01800  66 VAL A CA  
480 C C   . VAL A 66 ? 0.14920 0.14500 0.16780 -0.02020 0.01300  0.01890  66 VAL A C   
481 O O   . VAL A 66 ? 0.17900 0.13280 0.15920 -0.01430 0.00030  0.01830  66 VAL A O   
482 C CB  . VAL A 66 ? 0.16720 0.13620 0.19310 -0.01650 0.00340  0.03620  66 VAL A CB  
483 C CG1 . VAL A 66 ? 0.19050 0.12960 0.17020 -0.02210 0.01520  0.01870  66 VAL A CG1 
484 C CG2 . VAL A 66 ? 0.17170 0.17170 0.21350 0.01300  -0.01170 0.05840  66 VAL A CG2 
485 N N   . LEU A 67 ? 0.16850 0.14790 0.16850 -0.01130 0.01650  0.01820  67 LEU A N   
486 C CA  . LEU A 67 ? 0.16740 0.16850 0.17570 -0.00660 0.02330  0.01580  67 LEU A CA  
487 C C   . LEU A 67 ? 0.18380 0.15680 0.19090 -0.00380 0.00780  0.03260  67 LEU A C   
488 O O   . LEU A 67 ? 0.20620 0.18130 0.21320 -0.01010 -0.03520 0.03110  67 LEU A O   
489 C CB  . LEU A 67 ? 0.17690 0.18680 0.18960 -0.00730 0.04580  0.01510  67 LEU A CB  
490 C CG  . LEU A 67 ? 0.21190 0.21580 0.20060 -0.01770 0.03050  0.01030  67 LEU A CG  
491 C CD1 . LEU A 67 ? 0.23410 0.24870 0.20230 -0.02020 0.04380  -0.00140 67 LEU A CD1 
492 C CD2 . LEU A 67 ? 0.22770 0.20220 0.21610 -0.02010 0.03420  0.01960  67 LEU A CD2 
493 N N   . GLN A 68 ? 0.18970 0.14610 0.19060 0.01230  0.00440  0.02850  68 GLN A N   
494 C CA  . GLN A 68 ? 0.21710 0.15320 0.19470 -0.01020 0.01210  0.04210  68 GLN A CA  
495 C C   . GLN A 68 ? 0.17810 0.15970 0.19220 -0.00100 0.00870  0.03280  68 GLN A C   
496 O O   . GLN A 68 ? 0.19230 0.15050 0.19530 0.01020  0.01180  0.04180  68 GLN A O   
497 C CB  . GLN A 68 ? 0.28340 0.18260 0.23460 -0.03150 0.00800  0.04820  68 GLN A CB  
498 C CG  . GLN A 68 ? 0.31670 0.22100 0.27970 -0.01600 0.00040  0.04250  68 GLN A CG  
499 C CD  . GLN A 68 ? 0.31650 0.23750 0.31460 -0.02780 -0.01330 0.02310  68 GLN A CD  
500 O OE1 . GLN A 68 ? 0.31320 0.27000 0.33030 -0.04440 -0.03650 0.02210  68 GLN A OE1 
501 N NE2 . GLN A 68 ? 0.29360 0.22530 0.31550 -0.02910 -0.00470 0.00430  68 GLN A NE2 
502 N N   . ASN A 69 ? 0.17140 0.13550 0.17910 -0.00490 0.00280  0.01800  69 ASN A N   
503 C CA  . ASN A 69 ? 0.17430 0.13450 0.17290 -0.01160 -0.00560 0.01250  69 ASN A CA  
504 C C   . ASN A 69 ? 0.20870 0.13620 0.18050 -0.01970 -0.00970 0.03360  69 ASN A C   
505 O O   . ASN A 69 ? 0.21890 0.15510 0.19970 -0.00010 0.00660  0.01560  69 ASN A O   
506 C CB  . ASN A 69 ? 0.17170 0.14910 0.17310 -0.02160 0.00110  0.02730  69 ASN A CB  
507 C CG  . ASN A 69 ? 0.17320 0.18040 0.15440 -0.03350 0.01110  0.02080  69 ASN A CG  
508 O OD1 . ASN A 69 ? 0.18900 0.18540 0.15320 -0.02040 0.01970  0.02730  69 ASN A OD1 
509 N ND2 . ASN A 69 ? 0.21650 0.20460 0.16370 -0.05670 0.00140  0.00970  69 ASN A ND2 
510 N N   . GLY A 70 ? 0.20670 0.15530 0.18700 -0.03180 -0.01430 0.03820  70 GLY A N   
511 C CA  . GLY A 70 ? 0.24050 0.16170 0.18840 -0.04790 -0.03140 0.03420  70 GLY A CA  
512 C C   . GLY A 70 ? 0.28040 0.15650 0.20120 -0.05690 -0.06260 0.05170  70 GLY A C   
513 O O   . GLY A 70 ? 0.33130 0.16480 0.22040 -0.05810 -0.05110 0.05280  70 GLY A O   
514 N N   . PRO A 71 ? 0.31240 0.17810 0.20010 -0.05590 -0.08750 0.04560  71 PRO A N   
515 C CA  . PRO A 71 ? 0.29140 0.18740 0.21200 -0.04920 -0.08140 0.03820  71 PRO A CA  
516 C C   . PRO A 71 ? 0.27150 0.17220 0.19680 -0.03760 -0.03640 0.02760  71 PRO A C   
517 O O   . PRO A 71 ? 0.29120 0.18570 0.22400 -0.03690 -0.01000 0.04700  71 PRO A O   
518 C CB  . PRO A 71 ? 0.33520 0.21550 0.22460 -0.05610 -0.10170 0.04270  71 PRO A CB  
519 C CG  . PRO A 71 ? 0.37160 0.23290 0.22710 -0.07380 -0.09190 0.03540  71 PRO A CG  
520 C CD  . PRO A 71 ? 0.35490 0.20560 0.20800 -0.07150 -0.08650 0.03920  71 PRO A CD  
521 N N   . HIS A 72 ? 0.25040 0.14060 0.17570 -0.01620 -0.03320 0.01800  72 HIS A N   
522 C CA  . HIS A 72 ? 0.23520 0.14150 0.17680 -0.00700 -0.02610 0.00630  72 HIS A CA  
523 C C   . HIS A 72 ? 0.26050 0.15550 0.18330 -0.00990 -0.01860 0.00490  72 HIS A C   
524 O O   . HIS A 72 ? 0.27270 0.16810 0.17710 -0.01630 -0.02090 -0.00170 72 HIS A O   
525 C CB  . HIS A 72 ? 0.24840 0.14300 0.17310 -0.02080 -0.03390 -0.00140 72 HIS A CB  
526 C CG  . HIS A 72 ? 0.21720 0.13750 0.17410 -0.02750 -0.01850 0.01600  72 HIS A CG  
527 N ND1 . HIS A 72 ? 0.22000 0.16740 0.19320 -0.02860 -0.02510 0.03300  72 HIS A ND1 
528 C CD2 . HIS A 72 ? 0.22350 0.13610 0.17360 -0.01450 -0.00350 0.03000  72 HIS A CD2 
529 C CE1 . HIS A 72 ? 0.23470 0.16700 0.19770 -0.04040 -0.03300 0.02740  72 HIS A CE1 
530 N NE2 . HIS A 72 ? 0.24490 0.14810 0.17140 -0.03720 -0.01230 0.04780  72 HIS A NE2 
531 N N   . THR A 73 ? 0.27220 0.16010 0.20070 0.00910  -0.03220 -0.00540 73 THR A N   
532 C CA  . THR A 73 ? 0.27930 0.18180 0.20450 0.02160  -0.04480 -0.01660 73 THR A CA  
533 C C   . THR A 73 ? 0.23670 0.17330 0.19980 0.01250  -0.04760 -0.01310 73 THR A C   
534 O O   . THR A 73 ? 0.25870 0.17910 0.24200 -0.00400 -0.03720 -0.00410 73 THR A O   
535 C CB  . THR A 73 ? 0.34230 0.25300 0.22060 0.03870  -0.02640 -0.01670 73 THR A CB  
536 O OG1 . THR A 73 ? 0.39550 0.33050 0.26320 0.02600  -0.01420 -0.01550 73 THR A OG1 
537 C CG2 . THR A 73 ? 0.36110 0.26780 0.20980 0.06900  -0.02620 -0.00800 73 THR A CG2 
538 N N   . LEU A 74 ? 0.22530 0.15020 0.16650 0.02620  -0.03270 -0.01580 74 LEU A N   
539 C CA  . LEU A 74 ? 0.20520 0.15870 0.17300 0.03330  -0.03440 -0.02160 74 LEU A CA  
540 C C   . LEU A 74 ? 0.19510 0.16350 0.17090 0.02660  -0.01840 -0.02390 74 LEU A C   
541 O O   . LEU A 74 ? 0.19040 0.18580 0.17000 0.01860  -0.02510 -0.02410 74 LEU A O   
542 C CB  . LEU A 74 ? 0.21330 0.16650 0.18070 0.00570  -0.05130 -0.03300 74 LEU A CB  
543 C CG  . LEU A 74 ? 0.20110 0.18040 0.19560 0.00560  -0.03940 -0.01550 74 LEU A CG  
544 C CD1 . LEU A 74 ? 0.19350 0.20780 0.22540 0.01830  -0.02700 -0.01320 74 LEU A CD1 
545 C CD2 . LEU A 74 ? 0.24420 0.18550 0.18840 -0.00600 -0.04150 -0.01940 74 LEU A CD2 
546 N N   . ASP A 75 ? 0.20980 0.15940 0.16890 0.02150  -0.00580 -0.02310 75 ASP A N   
547 C CA  . ASP A 75 ? 0.24870 0.17240 0.18100 0.02760  -0.02390 -0.01120 75 ASP A CA  
548 C C   . ASP A 75 ? 0.25160 0.19720 0.20980 0.03210  -0.03140 -0.03430 75 ASP A C   
549 O O   . ASP A 75 ? 0.27060 0.21480 0.24890 0.02470  -0.02350 -0.04060 75 ASP A O   
550 C CB  . ASP A 75 ? 0.25310 0.17810 0.17770 0.03960  -0.02380 -0.00110 75 ASP A CB  
551 C CG  . ASP A 75 ? 0.24080 0.20410 0.18820 0.05740  0.01860  0.01330  75 ASP A CG  
552 O OD1 . ASP A 75 ? 0.25850 0.23700 0.21170 0.06660  0.03630  0.02600  75 ASP A OD1 
553 O OD2 . ASP A 75 ? 0.22990 0.23130 0.18480 0.05470  0.02450  0.01280  75 ASP A OD2 
554 N N   . GLY A 76 ? 0.26050 0.23080 0.20240 0.07390  -0.04890 -0.04090 76 GLY A N   
555 C CA  . GLY A 76 ? 0.27310 0.27420 0.21060 0.07670  -0.06490 -0.05150 76 GLY A CA  
556 C C   . GLY A 76 ? 0.26830 0.26930 0.22240 0.08010  -0.06990 -0.05310 76 GLY A C   
557 O O   . GLY A 76 ? 0.29540 0.33100 0.24250 0.08930  -0.06700 -0.05880 76 GLY A O   
558 N N   . ARG A 77 ? 0.25380 0.22070 0.23680 0.03630  -0.03890 -0.05610 77 ARG A N   
559 C CA  . ARG A 77 ? 0.23690 0.20780 0.23500 0.03210  -0.05260 -0.03820 77 ARG A CA  
560 C C   . ARG A 77 ? 0.22710 0.19000 0.21170 0.03900  -0.04220 -0.04190 77 ARG A C   
561 O O   . ARG A 77 ? 0.21210 0.19600 0.22140 0.02500  -0.05470 -0.04310 77 ARG A O   
562 C CB  . ARG A 77 ? 0.29480 0.21060 0.26910 0.01830  -0.05250 -0.02510 77 ARG A CB  
563 C CG  . ARG A 77 ? 0.38650 0.25960 0.32050 -0.01550 -0.05820 -0.04140 77 ARG A CG  
564 C CD  . ARG A 77 ? 0.48900 0.31630 0.37840 -0.05920 -0.07040 -0.04450 77 ARG A CD  
565 N NE  . ARG A 77 ? 0.58750 0.38630 0.43190 -0.06250 -0.06710 -0.04030 77 ARG A NE  
566 C CZ  . ARG A 77 ? 0.65120 0.42420 0.46800 -0.07980 -0.07560 -0.04680 77 ARG A CZ  
567 N NH1 . ARG A 77 ? 0.67180 0.43230 0.47890 -0.08370 -0.08670 -0.05800 77 ARG A NH1 
568 N NH2 . ARG A 77 ? 0.67480 0.43730 0.48360 -0.08700 -0.07870 -0.04910 77 ARG A NH2 
569 N N   . THR A 78 ? 0.21900 0.19020 0.20350 0.03670  -0.03570 -0.03120 78 THR A N   
570 C CA  . THR A 78 ? 0.22400 0.19410 0.21410 0.05950  -0.03470 -0.02450 78 THR A CA  
571 C C   . THR A 78 ? 0.19840 0.19280 0.20710 0.02610  -0.02080 -0.02230 78 THR A C   
572 O O   . THR A 78 ? 0.20040 0.23930 0.22100 0.00910  -0.03370 -0.01800 78 THR A O   
573 C CB  . THR A 78 ? 0.27450 0.21870 0.22370 0.06310  -0.05210 -0.02100 78 THR A CB  
574 O OG1 . THR A 78 ? 0.30910 0.26510 0.22690 0.06000  -0.05910 -0.00040 78 THR A OG1 
575 C CG2 . THR A 78 ? 0.29580 0.20360 0.23670 0.05170  -0.06690 -0.01670 78 THR A CG2 
576 N N   . ILE A 79 ? 0.19140 0.15680 0.17850 -0.00070 -0.02190 -0.00890 79 ILE A N   
577 C CA  . ILE A 79 ? 0.19290 0.13990 0.18450 -0.00500 -0.02110 -0.00490 79 ILE A CA  
578 C C   . ILE A 79 ? 0.20470 0.12950 0.18980 -0.01240 -0.01500 0.00450  79 ILE A C   
579 O O   . ILE A 79 ? 0.24090 0.14560 0.19610 0.00420  0.01250  0.01290  79 ILE A O   
580 C CB  . ILE A 79 ? 0.18310 0.13300 0.20220 -0.01080 -0.01170 -0.00200 79 ILE A CB  
581 C CG1 . ILE A 79 ? 0.16860 0.15430 0.20300 -0.01080 0.00250  0.00470  79 ILE A CG1 
582 C CG2 . ILE A 79 ? 0.20340 0.12910 0.19140 0.01170  -0.00730 -0.00320 79 ILE A CG2 
583 C CD1 . ILE A 79 ? 0.18080 0.17540 0.19150 0.00190  -0.00280 0.00650  79 ILE A CD1 
584 N N   . ASP A 80 ? 0.18140 0.14770 0.18840 0.00810  -0.00820 -0.00060 80 ASP A N   
585 C CA  . ASP A 80 ? 0.16070 0.16430 0.20710 0.00980  -0.00630 -0.01600 80 ASP A CA  
586 C C   . ASP A 80 ? 0.16040 0.14940 0.17620 0.00760  0.00930  -0.00250 80 ASP A C   
587 O O   . ASP A 80 ? 0.15690 0.14710 0.17620 0.00170  -0.00420 0.00340  80 ASP A O   
588 C CB  . ASP A 80 ? 0.16530 0.20520 0.25160 0.01320  -0.01210 -0.03090 80 ASP A CB  
589 C CG  . ASP A 80 ? 0.17910 0.26860 0.29410 0.00860  -0.00020 -0.03640 80 ASP A CG  
590 O OD1 . ASP A 80 ? 0.21800 0.27050 0.30670 0.05520  -0.01340 -0.02420 80 ASP A OD1 
591 O OD2 . ASP A 80 ? 0.18290 0.31990 0.32410 0.01100  0.02150  -0.03740 80 ASP A OD2 
592 N N   . PRO A 81 ? 0.17430 0.14800 0.17770 -0.00290 0.01370  0.00210  81 PRO A N   
593 C CA  . PRO A 81 ? 0.18210 0.14480 0.18110 -0.00880 0.03080  -0.01240 81 PRO A CA  
594 C C   . PRO A 81 ? 0.18070 0.13150 0.18540 0.00470  0.01460  0.00530  81 PRO A C   
595 O O   . PRO A 81 ? 0.20490 0.14510 0.20200 0.01140  0.00760  0.01830  81 PRO A O   
596 C CB  . PRO A 81 ? 0.20500 0.18320 0.18380 -0.03410 0.01510  0.01800  81 PRO A CB  
597 C CG  . PRO A 81 ? 0.22020 0.22620 0.18750 -0.04750 0.01920  0.01450  81 PRO A CG  
598 C CD  . PRO A 81 ? 0.19980 0.17780 0.17820 -0.02000 0.01990  -0.00030 81 PRO A CD  
599 N N   . LYS A 82 ? 0.16190 0.13570 0.16630 0.00820  0.00560  -0.00410 82 LYS A N   
600 C CA  . LYS A 82 ? 0.15980 0.15020 0.19380 0.02380  -0.00170 -0.01530 82 LYS A CA  
601 C C   . LYS A 82 ? 0.16750 0.13890 0.19940 0.03230  0.00810  -0.01230 82 LYS A C   
602 O O   . LYS A 82 ? 0.18400 0.14020 0.20260 0.04060  -0.03080 -0.01580 82 LYS A O   
603 C CB  . LYS A 82 ? 0.18520 0.18050 0.21790 0.02880  0.00350  -0.01770 82 LYS A CB  
604 C CG  . LYS A 82 ? 0.19590 0.20850 0.24410 0.00940  0.00450  0.00210  82 LYS A CG  
605 C CD  . LYS A 82 ? 0.24370 0.25130 0.27770 0.03610  0.00360  0.01320  82 LYS A CD  
606 C CE  . LYS A 82 ? 0.31550 0.31140 0.30040 0.04470  -0.00080 0.04100  82 LYS A CE  
607 N NZ  . LYS A 82 ? 0.36000 0.35060 0.31490 0.05010  0.01660  0.05640  82 LYS A NZ  
608 N N   . PRO A 83 ? 0.17070 0.12970 0.20090 0.01600  0.02560  -0.00740 83 PRO A N   
609 C CA  . PRO A 83 ? 0.17010 0.16140 0.19860 -0.00000 0.01680  -0.01680 83 PRO A CA  
610 C C   . PRO A 83 ? 0.14460 0.15390 0.20410 -0.01600 -0.00570 -0.01080 83 PRO A C   
611 O O   . PRO A 83 ? 0.16310 0.17020 0.23090 -0.01660 0.01050  0.01510  83 PRO A O   
612 C CB  . PRO A 83 ? 0.19490 0.16030 0.22630 -0.00880 0.00390  -0.02010 83 PRO A CB  
613 C CG  . PRO A 83 ? 0.25700 0.17180 0.22180 -0.00570 0.03100  -0.00830 83 PRO A CG  
614 C CD  . PRO A 83 ? 0.22320 0.12830 0.20790 -0.01230 0.04360  -0.00010 83 PRO A CD  
615 N N   . CYS A 84 ? 0.17180 0.17850 0.20750 -0.02400 0.00690  0.00170  84 CYS A N   
616 C CA  . CYS A 84 ? 0.20390 0.19380 0.22190 -0.03190 0.00250  0.00740  84 CYS A CA  
617 C C   . CYS A 84 ? 0.16860 0.24920 0.21460 -0.05730 0.00230  -0.01750 84 CYS A C   
618 O O   . CYS A 84 ? 0.18570 0.32740 0.23260 -0.06640 -0.00010 -0.01600 84 CYS A O   
619 C CB  . CYS A 84 ? 0.22440 0.21950 0.26860 -0.00440 -0.01340 0.03600  84 CYS A CB  
620 S SG  . CYS A 84 ? 0.22630 0.26870 0.31690 0.02010  0.02320  0.04010  84 CYS A SG  
621 N N   . ASN A 85 ? 0.17720 0.21230 0.19470 -0.04300 0.01380  -0.02350 85 ASN A N   
622 C CA  . ASN A 85 ? 0.21310 0.20220 0.20920 -0.01830 0.00410  -0.03370 85 ASN A CA  
623 C C   . ASN A 85 ? 0.19030 0.19600 0.20480 -0.01550 -0.00390 -0.01510 85 ASN A C   
624 O O   . ASN A 85 ? 0.18260 0.20170 0.21750 -0.04110 -0.02840 -0.01670 85 ASN A O   
625 C CB  . ASN A 85 ? 0.23030 0.24180 0.25940 -0.00010 0.02520  -0.04170 85 ASN A CB  
626 C CG  . ASN A 85 ? 0.22700 0.29220 0.30400 0.01100  0.04940  -0.04900 85 ASN A CG  
627 O OD1 . ASN A 85 ? 0.27080 0.30490 0.32080 -0.00660 0.04540  -0.05680 85 ASN A OD1 
628 N ND2 . ASN A 85 ? 0.23510 0.32740 0.32700 0.03010  0.04500  -0.04200 85 ASN A ND2 
629 N N   . PRO A 86 ? 0.17370 0.19670 0.20320 -0.01750 -0.00040 -0.01660 86 PRO A N   
630 C CA  . PRO A 86 ? 0.16380 0.20530 0.21170 0.00230  0.00920  0.00490  86 PRO A CA  
631 C C   . PRO A 86 ? 0.15420 0.21290 0.20350 0.01730  0.00270  -0.00510 86 PRO A C   
632 O O   . PRO A 86 ? 0.17890 0.22970 0.21020 0.03670  0.00730  -0.01800 86 PRO A O   
633 C CB  . PRO A 86 ? 0.17330 0.22940 0.22900 -0.01130 0.00240  -0.00560 86 PRO A CB  
634 C CG  . PRO A 86 ? 0.19620 0.24390 0.24520 -0.02260 0.00980  -0.00840 86 PRO A CG  
635 C CD  . PRO A 86 ? 0.16920 0.22730 0.23670 -0.03180 0.00500  -0.01620 86 PRO A CD  
# 
