data_18995 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18995 _Entry.Title ; Structural Insights into Human S100B and Basic Fibroblast Growth Factor (FGF2) Interaction ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2013-02-03 _Entry.Accession_date 2013-02-03 _Entry.Last_release_date 2013-12-16 _Entry.Original_release_date 2013-12-16 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype SOLUTION _Entry.Details 'Human S100B and Basic Fibroblast Growth Factor (FGF2) Interaction' _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Arun Gupta . A. . 18995 2 Chin Yu . . . 18995 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'not applicable' 'not applicable' . 18995 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'S100B, FGF2' . 18995 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18995 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 250 18995 '15N chemical shifts' 81 18995 '1H chemical shifts' 81 18995 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2013-12-16 2013-02-03 original author . 18995 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18995 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 24063890 _Citation.Full_citation . _Citation.Title 'Structural insights into the interaction of human S100B and basic fibroblast growth factor (FGF2): Effects on FGFR1 receptor signaling' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biochim. Biophys. Acta.' _Citation.Journal_name_full . _Citation.Journal_volume 2013 _Citation.Journal_issue 12 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 2606 _Citation.Page_last 2619 _Citation.Year 2013 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Arun Gupta . A. . 18995 1 2 Ruey-Hwang Chou . . . 18995 1 3 Hongchun Li . . . 18995 1 4 Lee-Wei Yang . . . 18995 1 5 Chin Yu . . . 18995 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18995 _Assembly.ID 1 _Assembly.Name 'Human S100B and Basic Fibroblast Growth Factor (FGF2) Interaction' _Assembly.BMRB_code . _Assembly.Number_of_components 3 _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 FGF2_1 1 $FGF2 A . yes native no no . . . 18995 1 2 S100B 2 $S100B B . yes native no no . . . 18995 1 3 FGF2_2 1 $FGF2 C . yes native no no . . . 18995 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_FGF2 _Entity.Sf_category entity _Entity.Sf_framecode FGF2 _Entity.Entry_ID 18995 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name FGF2 _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A,C _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; DPKRLYCKNGGFFLRIHPDG RVDGVREKSDPHIKLQLQAE ERGVVSIKGVSANRYLAMKE DGRLLASKSVTDECFFFERL ESNNYNTYRSRKYTSWYVAL KRTGQYKLGSKTGPGQKAIL FLPMSA ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 126 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all free' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 14422.641 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 4091 . "basic fibroblast Growth Factor" . . . . . 100.00 154 100.00 100.00 3.90e-87 . . . . 18995 1 2 no PDB 1BAS . "Three-Dimensional Structures Of Acidic And Basic Fibroblast Growth Factors" . . . . . 100.00 154 100.00 100.00 3.10e-87 . . . . 18995 1 3 no PDB 1BFB . "Basic Fibroblast Growth Factor Complexed With Heparin Tetramer Fragment" . . . . . 100.00 147 100.00 100.00 6.79e-87 . . . . 18995 1 4 no PDB 1BFC . "Basic Fibroblast Growth Factor Complexed With Heparin Hexamer Fragment" . . . . . 100.00 147 100.00 100.00 6.79e-87 . . . . 18995 1 5 no PDB 1BFF . "The 154 Amino Acid Form Of Human Basic Fibroblast Growth Factor" . . . . . 100.00 129 98.41 98.41 4.43e-86 . . . . 18995 1 6 no PDB 1BFG . "Crystal Structure Of Basic Fibroblast Growth Factor At 1.6 Angstroms Resolution" . . . . . 100.00 146 100.00 100.00 6.71e-87 . . . . 18995 1 7 no PDB 1BLA . "Basic Fibroblast Growth Factor (Fgf-2) Mutant With Cys 78 Replaced By Ser And Cys 96 Replaced By Ser, Nmr" . . . . . 100.00 155 100.00 100.00 3.81e-87 . . . . 18995 1 8 no PDB 1BLD . "Basic Fibroblast Growth Factor (Fgf-2) Mutant With Cys 78 Replaced By Ser And Cys 96 Replaced By Ser, Nmr" . . . . . 100.00 155 100.00 100.00 3.81e-87 . . . . 18995 1 9 no PDB 1CVS . "Crystal Structure Of A Dimeric Fgf2-Fgfr1 Complex" . . . . . 100.00 132 100.00 100.00 1.87e-87 . . . . 18995 1 10 no PDB 1EV2 . "Crystal Structure Of Fgf2 In Complex With The Extracellular Ligand Binding Domain Of Fgf Receptor 2 (Fgfr2)" . . . . . 100.00 132 100.00 100.00 1.87e-87 . . . . 18995 1 11 no PDB 1FGA . "Refinement Of The Structure Of Human Basic Fibroblast Growth Factor At 1.6 Angstroms Resolution And Analysis Of Presumed Hepari" . . . . . 100.00 146 98.41 98.41 2.84e-85 . . . . 18995 1 12 no PDB 1FQ9 . "Crystal Structure Of A Ternary Fgf2-Fgfr1-Heparin Complex" . . . . . 100.00 132 100.00 100.00 1.87e-87 . . . . 18995 1 13 no PDB 1II4 . "Crystal Structure Of Ser252trp Apert Mutant Fgf Receptor 2 (Fgfr2) In Complex With Fgf2" . . . . . 100.00 155 100.00 100.00 3.13e-87 . . . . 18995 1 14 no PDB 1IIL . "Crystal Structure Of Pro253arg Apert Mutant Fgf Receptor 2 (Fgfr2) In Complex With Fgf2" . . . . . 100.00 155 100.00 100.00 3.13e-87 . . . . 18995 1 15 no PDB 2BFH . "Crystal Structure Of Basic Fibroblast Growth Factor At 1.6 Angstroms Resolution" . . . . . 100.00 128 98.41 98.41 5.34e-86 . . . . 18995 1 16 no PDB 2FGF . "Three-Dimensional Structure Of Human Basic Fibroblast Growth Factor, A Structural Homolog Of Interleukin 1beta" . . . . . 100.00 146 98.41 98.41 2.84e-85 . . . . 18995 1 17 no PDB 2M49 . "Structural Insights Into Human S100b And Basic Fibroblast Growth Factor (fgf2) Interaction" . . . . . 100.00 126 100.00 100.00 1.54e-87 . . . . 18995 1 18 no PDB 4FGF . "Refinement Of The Structure Of Human Basic Fibroblast Growth Factor At 1.6 Angstroms Resolution And Analysis Of Presumed Hepari" . . . . . 100.00 146 98.41 98.41 2.84e-85 . . . . 18995 1 19 no PDB 4OEE . "Crystal Structure Analysis Of Fgf2-disaccharide (s3i2) Complex" . . . . . 100.00 155 100.00 100.00 3.13e-87 . . . . 18995 1 20 no PDB 4OEF . "Crystal Structure Analysis Of Fgf2-disaccharide (s6i2) Complex" . . . . . 100.00 155 100.00 100.00 3.13e-87 . . . . 18995 1 21 no PDB 4OEG . "Crystal Structure Analysis Of Fgf2-disaccharide (s9i2) Complex" . . . . . 100.00 155 100.00 100.00 3.13e-87 . . . . 18995 1 22 no DBJ BAG70135 . "heparin-binding growth factor 2 precursor [Homo sapiens]" . . . . . 100.00 155 98.41 98.41 1.56e-85 . . . . 18995 1 23 no DBJ BAG70264 . "heparin-binding growth factor 2 precursor [Homo sapiens]" . . . . . 100.00 155 98.41 98.41 1.56e-85 . . . . 18995 1 24 no EMBL CCO13911 . "SP1-fibroblast growth factor 2 fusion protein [synthetic construct]" . . . . . 100.00 170 98.41 98.41 3.18e-85 . . . . 18995 1 25 no EMBL CCO13913 . "truncated fibroblast growth factor 2, partial [synthetic construct]" . . . . . 100.00 146 98.41 98.41 2.84e-85 . . . . 18995 1 26 no GB AAA31248 . "fibroblast growth factor, partial [Oryctolagus cuniculus]" . . . . . 94.44 137 97.48 98.32 6.80e-79 . . . . 18995 1 27 no GB AAA52448 . "basic fibroblast growth factor [Homo sapiens]" . . . . . 100.00 155 98.41 98.41 1.56e-85 . . . . 18995 1 28 no GB AAA52531 . "basic fibroblast growth factor (ctg start codon); putative [Homo sapiens]" . . . . . 100.00 210 98.41 98.41 3.03e-85 . . . . 18995 1 29 no GB AAA52532 . "21 kd basic fibroblast growth factor (ctg start codon; put.); putative [Homo sapiens]" . . . . . 100.00 196 98.41 98.41 1.92e-85 . . . . 18995 1 30 no GB AAA52533 . "18 kd basic fibroblast growth factor [Homo sapiens]" . . . . . 100.00 155 98.41 98.41 1.56e-85 . . . . 18995 1 31 no REF NP_001103711 . "fibroblast growth factor 2 [Pan troglodytes]" . . . . . 100.00 288 98.41 98.41 1.16e-84 . . . . 18995 1 32 no REF NP_001997 . "fibroblast growth factor 2 [Homo sapiens]" . . . . . 100.00 288 98.41 98.41 1.12e-84 . . . . 18995 1 33 no REF XP_001099284 . "PREDICTED: heparin-binding growth factor 2 [Macaca mulatta]" . . . . . 100.00 237 98.41 98.41 1.06e-84 . . . . 18995 1 34 no REF XP_002717284 . "PREDICTED: fibroblast growth factor 2 [Oryctolagus cuniculus]" . . . . . 100.00 155 97.62 98.41 3.73e-85 . . . . 18995 1 35 no REF XP_002815172 . "PREDICTED: fibroblast growth factor 2, partial [Pongo abelii]" . . . . . 100.00 322 98.41 98.41 1.84e-84 . . . . 18995 1 36 no SP P09038 . "RecName: Full=Fibroblast growth factor 2; Short=FGF-2; AltName: Full=Basic fibroblast growth factor; Short=bFGF; AltName: Full=" . . . . . 100.00 288 98.41 98.41 1.12e-84 . . . . 18995 1 37 no SP P48799 . "RecName: Full=Fibroblast growth factor 2; Short=FGF-2; AltName: Full=Basic fibroblast growth factor; Short=bFGF; AltName: Full=" . . . . . 94.44 137 97.48 98.32 6.80e-79 . . . . 18995 1 38 no SP Q5IS69 . "RecName: Full=Fibroblast growth factor 2; Short=FGF-2; AltName: Full=Basic fibroblast growth factor; Short=bFGF; AltName: Full=" . . . . . 100.00 288 98.41 98.41 1.16e-84 . . . . 18995 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 1 ASP . 18995 1 2 2 PRO . 18995 1 3 3 LYS . 18995 1 4 4 ARG . 18995 1 5 5 LEU . 18995 1 6 6 TYR . 18995 1 7 7 CYS . 18995 1 8 8 LYS . 18995 1 9 9 ASN . 18995 1 10 10 GLY . 18995 1 11 11 GLY . 18995 1 12 12 PHE . 18995 1 13 13 PHE . 18995 1 14 14 LEU . 18995 1 15 15 ARG . 18995 1 16 16 ILE . 18995 1 17 17 HIS . 18995 1 18 18 PRO . 18995 1 19 19 ASP . 18995 1 20 20 GLY . 18995 1 21 21 ARG . 18995 1 22 22 VAL . 18995 1 23 23 ASP . 18995 1 24 24 GLY . 18995 1 25 25 VAL . 18995 1 26 26 ARG . 18995 1 27 27 GLU . 18995 1 28 28 LYS . 18995 1 29 29 SER . 18995 1 30 30 ASP . 18995 1 31 31 PRO . 18995 1 32 32 HIS . 18995 1 33 33 ILE . 18995 1 34 34 LYS . 18995 1 35 35 LEU . 18995 1 36 36 GLN . 18995 1 37 37 LEU . 18995 1 38 38 GLN . 18995 1 39 39 ALA . 18995 1 40 40 GLU . 18995 1 41 41 GLU . 18995 1 42 42 ARG . 18995 1 43 43 GLY . 18995 1 44 44 VAL . 18995 1 45 45 VAL . 18995 1 46 46 SER . 18995 1 47 47 ILE . 18995 1 48 48 LYS . 18995 1 49 49 GLY . 18995 1 50 50 VAL . 18995 1 51 51 SER . 18995 1 52 52 ALA . 18995 1 53 53 ASN . 18995 1 54 54 ARG . 18995 1 55 55 TYR . 18995 1 56 56 LEU . 18995 1 57 57 ALA . 18995 1 58 58 MET . 18995 1 59 59 LYS . 18995 1 60 60 GLU . 18995 1 61 61 ASP . 18995 1 62 62 GLY . 18995 1 63 63 ARG . 18995 1 64 64 LEU . 18995 1 65 65 LEU . 18995 1 66 66 ALA . 18995 1 67 67 SER . 18995 1 68 68 LYS . 18995 1 69 69 SER . 18995 1 70 70 VAL . 18995 1 71 71 THR . 18995 1 72 72 ASP . 18995 1 73 73 GLU . 18995 1 74 74 CYS . 18995 1 75 75 PHE . 18995 1 76 76 PHE . 18995 1 77 77 PHE . 18995 1 78 78 GLU . 18995 1 79 79 ARG . 18995 1 80 80 LEU . 18995 1 81 81 GLU . 18995 1 82 82 SER . 18995 1 83 83 ASN . 18995 1 84 84 ASN . 18995 1 85 85 TYR . 18995 1 86 86 ASN . 18995 1 87 87 THR . 18995 1 88 88 TYR . 18995 1 89 89 ARG . 18995 1 90 90 SER . 18995 1 91 91 ARG . 18995 1 92 92 LYS . 18995 1 93 93 TYR . 18995 1 94 94 THR . 18995 1 95 95 SER . 18995 1 96 96 TRP . 18995 1 97 97 TYR . 18995 1 98 98 VAL . 18995 1 99 99 ALA . 18995 1 100 100 LEU . 18995 1 101 101 LYS . 18995 1 102 102 ARG . 18995 1 103 103 THR . 18995 1 104 104 GLY . 18995 1 105 105 GLN . 18995 1 106 106 TYR . 18995 1 107 107 LYS . 18995 1 108 108 LEU . 18995 1 109 109 GLY . 18995 1 110 110 SER . 18995 1 111 111 LYS . 18995 1 112 112 THR . 18995 1 113 113 GLY . 18995 1 114 114 PRO . 18995 1 115 115 GLY . 18995 1 116 116 GLN . 18995 1 117 117 LYS . 18995 1 118 118 ALA . 18995 1 119 119 ILE . 18995 1 120 120 LEU . 18995 1 121 121 PHE . 18995 1 122 122 LEU . 18995 1 123 123 PRO . 18995 1 124 124 MET . 18995 1 125 125 SER . 18995 1 126 126 ALA . 18995 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . ASP 1 1 18995 1 . PRO 2 2 18995 1 . LYS 3 3 18995 1 . ARG 4 4 18995 1 . LEU 5 5 18995 1 . TYR 6 6 18995 1 . CYS 7 7 18995 1 . LYS 8 8 18995 1 . ASN 9 9 18995 1 . GLY 10 10 18995 1 . GLY 11 11 18995 1 . PHE 12 12 18995 1 . PHE 13 13 18995 1 . LEU 14 14 18995 1 . ARG 15 15 18995 1 . ILE 16 16 18995 1 . HIS 17 17 18995 1 . PRO 18 18 18995 1 . ASP 19 19 18995 1 . GLY 20 20 18995 1 . ARG 21 21 18995 1 . VAL 22 22 18995 1 . ASP 23 23 18995 1 . GLY 24 24 18995 1 . VAL 25 25 18995 1 . ARG 26 26 18995 1 . GLU 27 27 18995 1 . LYS 28 28 18995 1 . SER 29 29 18995 1 . ASP 30 30 18995 1 . PRO 31 31 18995 1 . HIS 32 32 18995 1 . ILE 33 33 18995 1 . LYS 34 34 18995 1 . LEU 35 35 18995 1 . GLN 36 36 18995 1 . LEU 37 37 18995 1 . GLN 38 38 18995 1 . ALA 39 39 18995 1 . GLU 40 40 18995 1 . GLU 41 41 18995 1 . ARG 42 42 18995 1 . GLY 43 43 18995 1 . VAL 44 44 18995 1 . VAL 45 45 18995 1 . SER 46 46 18995 1 . ILE 47 47 18995 1 . LYS 48 48 18995 1 . GLY 49 49 18995 1 . VAL 50 50 18995 1 . SER 51 51 18995 1 . ALA 52 52 18995 1 . ASN 53 53 18995 1 . ARG 54 54 18995 1 . TYR 55 55 18995 1 . LEU 56 56 18995 1 . ALA 57 57 18995 1 . MET 58 58 18995 1 . LYS 59 59 18995 1 . GLU 60 60 18995 1 . ASP 61 61 18995 1 . GLY 62 62 18995 1 . ARG 63 63 18995 1 . LEU 64 64 18995 1 . LEU 65 65 18995 1 . ALA 66 66 18995 1 . SER 67 67 18995 1 . LYS 68 68 18995 1 . SER 69 69 18995 1 . VAL 70 70 18995 1 . THR 71 71 18995 1 . ASP 72 72 18995 1 . GLU 73 73 18995 1 . CYS 74 74 18995 1 . PHE 75 75 18995 1 . PHE 76 76 18995 1 . PHE 77 77 18995 1 . GLU 78 78 18995 1 . ARG 79 79 18995 1 . LEU 80 80 18995 1 . GLU 81 81 18995 1 . SER 82 82 18995 1 . ASN 83 83 18995 1 . ASN 84 84 18995 1 . TYR 85 85 18995 1 . ASN 86 86 18995 1 . THR 87 87 18995 1 . TYR 88 88 18995 1 . ARG 89 89 18995 1 . SER 90 90 18995 1 . ARG 91 91 18995 1 . LYS 92 92 18995 1 . TYR 93 93 18995 1 . THR 94 94 18995 1 . SER 95 95 18995 1 . TRP 96 96 18995 1 . TYR 97 97 18995 1 . VAL 98 98 18995 1 . ALA 99 99 18995 1 . LEU 100 100 18995 1 . LYS 101 101 18995 1 . ARG 102 102 18995 1 . THR 103 103 18995 1 . GLY 104 104 18995 1 . GLN 105 105 18995 1 . TYR 106 106 18995 1 . LYS 107 107 18995 1 . LEU 108 108 18995 1 . GLY 109 109 18995 1 . SER 110 110 18995 1 . LYS 111 111 18995 1 . THR 112 112 18995 1 . GLY 113 113 18995 1 . PRO 114 114 18995 1 . GLY 115 115 18995 1 . GLN 116 116 18995 1 . LYS 117 117 18995 1 . ALA 118 118 18995 1 . ILE 119 119 18995 1 . LEU 120 120 18995 1 . PHE 121 121 18995 1 . LEU 122 122 18995 1 . PRO 123 123 18995 1 . MET 124 124 18995 1 . SER 125 125 18995 1 . ALA 126 126 18995 1 stop_ save_ save_S100B _Entity.Sf_category entity _Entity.Sf_framecode S100B _Entity.Entry_ID 18995 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name S100B _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID B _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; SELEKAMVALIDVFHQYSGR EGDKHKLKKSELKELINNEL SHFLEEIKEQEVVDKVMETL DNDGDGECDFQEFMAFVAMV TTACHEFFEHESELEKAMVA LIDVFHQYSGREGDKHKLKK SELKELINNELSHFLEEIKE QEVVDKVMETLDNDGDGECD FQEFMAFVAMVTTACHEFFE HE ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 182 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all free' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 21173.836 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-29 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 15923 . "rat S100B" . . . . . 50.00 91 97.80 98.90 8.21e-54 . . . . 18995 2 2 no BMRB 4001 . S100beta . . . . . 50.00 92 97.80 98.90 8.73e-54 . . . . 18995 2 3 no BMRB 4105 . S100B . . . . . 50.00 92 97.80 98.90 8.73e-54 . . . . 18995 2 4 no BMRB 5206 . S100B . . . . . 50.00 92 100.00 100.00 2.18e-55 . . . . 18995 2 5 no BMRB 5895 . S100B . . . . . 50.00 92 97.80 98.90 8.73e-54 . . . . 18995 2 6 no PDB 1B4C . "Solution Structure Of Rat Apo-S100b Using Dipolar Couplings" . . . . . 50.00 92 97.80 98.90 8.73e-54 . . . . 18995 2 7 no PDB 1DT7 . "Solution Structure Of The C-Terminal Negative Regulatory Domain Of P53 In A Complex With Ca2+-Bound S100b(Bb)" . . . . . 50.00 92 97.80 98.90 8.73e-54 . . . . 18995 2 8 no PDB 1MQ1 . "Ca2+-S100b-Trtk-12 Complex" . . . . . 50.00 91 100.00 100.00 2.26e-55 . . . . 18995 2 9 no PDB 1MWN . "Solution Nmr Structure Of S100b Bound To The High-Affinity Target Peptide Trtk-12" . . . . . 50.00 92 97.80 98.90 8.73e-54 . . . . 18995 2 10 no PDB 1QLK . "Solution Structure Of Ca(2+)-Loaded Rat S100b (Betabeta) Nmr, 20 Structures" . . . . . 50.00 92 97.80 98.90 8.73e-54 . . . . 18995 2 11 no PDB 1SYM . "3-D Solution Structure Of Reduced Apo-S100b From Rat, Nmr, 20 Structures" . . . . . 50.00 92 97.80 98.90 8.73e-54 . . . . 18995 2 12 no PDB 1UWO . "Calcium Form Of Human S100b, Nmr, 20 Structures" . . . . . 50.00 91 100.00 100.00 2.26e-55 . . . . 18995 2 13 no PDB 1XYD . "Nmr Solution Structure Of Rat Zinc-Calcium-S100b, 20 Structures" . . . . . 50.00 92 97.80 98.90 8.73e-54 . . . . 18995 2 14 no PDB 2H61 . "X-ray Structure Of Human Ca2+-loaded S100b" . . . . . 50.00 92 100.00 100.00 2.18e-55 . . . . 18995 2 15 no PDB 2K7O . "Ca2+-s100b, Refined With Rdcs" . . . . . 50.00 91 97.80 98.90 8.21e-54 . . . . 18995 2 16 no PDB 2M49 . "Structural Insights Into Human S100b And Basic Fibroblast Growth Factor (fgf2) Interaction" . . . . . 50.00 91 100.00 100.00 2.26e-55 . . . . 18995 2 17 no PDB 2PRU . "Nmr Structure Of Human Apos100b At 10c" . . . . . 50.00 91 100.00 100.00 2.26e-55 . . . . 18995 2 18 no PDB 3CZT . "Crystal Structure Of S100b In The Calcium And Zinc Loaded State At Ph 9" . . . . . 50.00 92 100.00 100.00 2.18e-55 . . . . 18995 2 19 no PDB 3D0Y . "Crystal Structure Of S100b In The Calcium And Zinc Loaded State At Ph 6.5" . . . . . 50.00 92 100.00 100.00 2.18e-55 . . . . 18995 2 20 no PDB 3D10 . "Crystal Structure Of S100b In The Calcium And Zinc Loaded State At Ph 10.0" . . . . . 50.00 92 100.00 100.00 2.18e-55 . . . . 18995 2 21 no PDB 3HCM . "Crystal Structure Of Human S100b In Complex With S45" . . . . . 50.00 92 100.00 100.00 2.18e-55 . . . . 18995 2 22 no PDB 4N6I . "X-ray Structure Of Human W61 Peptide-ca(2+)-s100b" . . . . . 50.00 92 100.00 100.00 2.18e-55 . . . . 18995 2 23 no DBJ BAE22214 . "unnamed protein product [Mus musculus]" . . . . . 50.00 92 98.90 98.90 2.73e-54 . . . . 18995 2 24 no DBJ BAE22413 . "unnamed protein product [Mus musculus]" . . . . . 50.00 92 98.90 98.90 2.73e-54 . . . . 18995 2 25 no DBJ BAE36647 . "unnamed protein product [Mus musculus]" . . . . . 50.00 92 98.90 98.90 2.73e-54 . . . . 18995 2 26 no DBJ BAE88979 . "unnamed protein product [Macaca fascicularis]" . . . . . 50.00 92 98.90 100.00 1.17e-54 . . . . 18995 2 27 no DBJ BAG74213 . "S100 calcium binding protein B [synthetic construct]" . . . . . 50.00 92 100.00 100.00 2.18e-55 . . . . 18995 2 28 no EMBL CAA25567 . "unnamed protein product [Rattus norvegicus]" . . . . . 50.00 92 97.80 98.90 8.73e-54 . . . . 18995 2 29 no EMBL CAG46920 . "S100B [Homo sapiens]" . . . . . 50.00 92 100.00 100.00 2.18e-55 . . . . 18995 2 30 no GB AAA03075 . "S100 beta protein [Mus musculus domesticus]" . . . . . 50.00 92 98.90 98.90 2.73e-54 . . . . 18995 2 31 no GB AAA42096 . "S100 protein [Rattus norvegicus]" . . . . . 50.00 92 97.80 98.90 8.73e-54 . . . . 18995 2 32 no GB AAA60367 . "S100 protein beta subunit [Homo sapiens]" . . . . . 50.00 92 100.00 100.00 2.18e-55 . . . . 18995 2 33 no GB AAH01766 . "S100 calcium binding protein B [Homo sapiens]" . . . . . 50.00 92 100.00 100.00 2.18e-55 . . . . 18995 2 34 no GB AAH61178 . "S100 protein, beta polypeptide, neural [Mus musculus]" . . . . . 50.00 92 98.90 98.90 2.73e-54 . . . . 18995 2 35 no PRF 2003367B . "S-100 protein:SUBUNIT=beta" . . . . . 50.00 92 100.00 100.00 2.18e-55 . . . . 18995 2 36 no REF NP_001076199 . "protein S100-B [Oryctolagus cuniculus]" . . . . . 50.00 92 100.00 100.00 2.18e-55 . . . . 18995 2 37 no REF NP_001247455 . "protein S100-B [Macaca mulatta]" . . . . . 50.00 92 98.90 100.00 1.17e-54 . . . . 18995 2 38 no REF NP_001270589 . "uncharacterized protein LOC101925200 [Macaca fascicularis]" . . . . . 50.00 92 98.90 100.00 1.17e-54 . . . . 18995 2 39 no REF NP_006263 . "protein S100-B [Homo sapiens]" . . . . . 50.00 92 100.00 100.00 2.18e-55 . . . . 18995 2 40 no REF NP_033141 . "protein S100-B [Mus musculus]" . . . . . 50.00 92 98.90 98.90 2.73e-54 . . . . 18995 2 41 no SP P04271 . "RecName: Full=Protein S100-B; AltName: Full=S-100 protein beta chain; AltName: Full=S-100 protein subunit beta; AltName: Full=S" . . . . . 50.00 92 100.00 100.00 2.18e-55 . . . . 18995 2 42 no SP P04631 . "RecName: Full=Protein S100-B; AltName: Full=S-100 protein beta chain; AltName: Full=S-100 protein subunit beta; AltName: Full=S" . . . . . 50.00 92 97.80 98.90 8.73e-54 . . . . 18995 2 43 no SP P50114 . "RecName: Full=Protein S100-B; AltName: Full=S-100 protein beta chain; AltName: Full=S-100 protein subunit beta; AltName: Full=S" . . . . . 50.00 92 98.90 98.90 2.73e-54 . . . . 18995 2 44 no SP Q6YNR6 . "RecName: Full=Protein S100-B; AltName: Full=S-100 protein beta chain; AltName: Full=S-100 protein subunit beta; AltName: Full=S" . . . . . 50.00 92 100.00 100.00 2.18e-55 . . . . 18995 2 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 1 SER . 18995 2 2 2 GLU . 18995 2 3 3 LEU . 18995 2 4 4 GLU . 18995 2 5 5 LYS . 18995 2 6 6 ALA . 18995 2 7 7 MET . 18995 2 8 8 VAL . 18995 2 9 9 ALA . 18995 2 10 10 LEU . 18995 2 11 11 ILE . 18995 2 12 12 ASP . 18995 2 13 13 VAL . 18995 2 14 14 PHE . 18995 2 15 15 HIS . 18995 2 16 16 GLN . 18995 2 17 17 TYR . 18995 2 18 18 SER . 18995 2 19 19 GLY . 18995 2 20 20 ARG . 18995 2 21 21 GLU . 18995 2 22 22 GLY . 18995 2 23 23 ASP . 18995 2 24 24 LYS . 18995 2 25 25 HIS . 18995 2 26 26 LYS . 18995 2 27 27 LEU . 18995 2 28 28 LYS . 18995 2 29 29 LYS . 18995 2 30 30 SER . 18995 2 31 31 GLU . 18995 2 32 32 LEU . 18995 2 33 33 LYS . 18995 2 34 34 GLU . 18995 2 35 35 LEU . 18995 2 36 36 ILE . 18995 2 37 37 ASN . 18995 2 38 38 ASN . 18995 2 39 39 GLU . 18995 2 40 40 LEU . 18995 2 41 41 SER . 18995 2 42 42 HIS . 18995 2 43 43 PHE . 18995 2 44 44 LEU . 18995 2 45 45 GLU . 18995 2 46 46 GLU . 18995 2 47 47 ILE . 18995 2 48 48 LYS . 18995 2 49 49 GLU . 18995 2 50 50 GLN . 18995 2 51 51 GLU . 18995 2 52 52 VAL . 18995 2 53 53 VAL . 18995 2 54 54 ASP . 18995 2 55 55 LYS . 18995 2 56 56 VAL . 18995 2 57 57 MET . 18995 2 58 58 GLU . 18995 2 59 59 THR . 18995 2 60 60 LEU . 18995 2 61 61 ASP . 18995 2 62 62 ASN . 18995 2 63 63 ASP . 18995 2 64 64 GLY . 18995 2 65 65 ASP . 18995 2 66 66 GLY . 18995 2 67 67 GLU . 18995 2 68 68 CYS . 18995 2 69 69 ASP . 18995 2 70 70 PHE . 18995 2 71 71 GLN . 18995 2 72 72 GLU . 18995 2 73 73 PHE . 18995 2 74 74 MET . 18995 2 75 75 ALA . 18995 2 76 76 PHE . 18995 2 77 77 VAL . 18995 2 78 78 ALA . 18995 2 79 79 MET . 18995 2 80 80 VAL . 18995 2 81 81 THR . 18995 2 82 82 THR . 18995 2 83 83 ALA . 18995 2 84 84 CYS . 18995 2 85 85 HIS . 18995 2 86 86 GLU . 18995 2 87 87 PHE . 18995 2 88 88 PHE . 18995 2 89 89 GLU . 18995 2 90 90 HIS . 18995 2 91 91 GLU . 18995 2 92 92 SER . 18995 2 93 93 GLU . 18995 2 94 94 LEU . 18995 2 95 95 GLU . 18995 2 96 96 LYS . 18995 2 97 97 ALA . 18995 2 98 98 MET . 18995 2 99 99 VAL . 18995 2 100 100 ALA . 18995 2 101 101 LEU . 18995 2 102 102 ILE . 18995 2 103 103 ASP . 18995 2 104 104 VAL . 18995 2 105 105 PHE . 18995 2 106 106 HIS . 18995 2 107 107 GLN . 18995 2 108 108 TYR . 18995 2 109 109 SER . 18995 2 110 110 GLY . 18995 2 111 111 ARG . 18995 2 112 112 GLU . 18995 2 113 113 GLY . 18995 2 114 114 ASP . 18995 2 115 115 LYS . 18995 2 116 116 HIS . 18995 2 117 117 LYS . 18995 2 118 118 LEU . 18995 2 119 119 LYS . 18995 2 120 120 LYS . 18995 2 121 121 SER . 18995 2 122 122 GLU . 18995 2 123 123 LEU . 18995 2 124 124 LYS . 18995 2 125 125 GLU . 18995 2 126 126 LEU . 18995 2 127 127 ILE . 18995 2 128 128 ASN . 18995 2 129 129 ASN . 18995 2 130 130 GLU . 18995 2 131 131 LEU . 18995 2 132 132 SER . 18995 2 133 133 HIS . 18995 2 134 134 PHE . 18995 2 135 135 LEU . 18995 2 136 136 GLU . 18995 2 137 137 GLU . 18995 2 138 138 ILE . 18995 2 139 139 LYS . 18995 2 140 140 GLU . 18995 2 141 141 GLN . 18995 2 142 142 GLU . 18995 2 143 143 VAL . 18995 2 144 144 VAL . 18995 2 145 145 ASP . 18995 2 146 146 LYS . 18995 2 147 147 VAL . 18995 2 148 148 MET . 18995 2 149 149 GLU . 18995 2 150 150 THR . 18995 2 151 151 LEU . 18995 2 152 152 ASP . 18995 2 153 153 ASN . 18995 2 154 154 ASP . 18995 2 155 155 GLY . 18995 2 156 156 ASP . 18995 2 157 157 GLY . 18995 2 158 158 GLU . 18995 2 159 159 CYS . 18995 2 160 160 ASP . 18995 2 161 161 PHE . 18995 2 162 162 GLN . 18995 2 163 163 GLU . 18995 2 164 164 PHE . 18995 2 165 165 MET . 18995 2 166 166 ALA . 18995 2 167 167 PHE . 18995 2 168 168 VAL . 18995 2 169 169 ALA . 18995 2 170 170 MET . 18995 2 171 171 VAL . 18995 2 172 172 THR . 18995 2 173 173 THR . 18995 2 174 174 ALA . 18995 2 175 175 CYS . 18995 2 176 176 HIS . 18995 2 177 177 GLU . 18995 2 178 178 PHE . 18995 2 179 179 PHE . 18995 2 180 180 GLU . 18995 2 181 181 HIS . 18995 2 182 182 GLU . 18995 2 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . SER 1 1 18995 2 . GLU 2 2 18995 2 . LEU 3 3 18995 2 . GLU 4 4 18995 2 . LYS 5 5 18995 2 . ALA 6 6 18995 2 . MET 7 7 18995 2 . VAL 8 8 18995 2 . ALA 9 9 18995 2 . LEU 10 10 18995 2 . ILE 11 11 18995 2 . ASP 12 12 18995 2 . VAL 13 13 18995 2 . PHE 14 14 18995 2 . HIS 15 15 18995 2 . GLN 16 16 18995 2 . TYR 17 17 18995 2 . SER 18 18 18995 2 . GLY 19 19 18995 2 . ARG 20 20 18995 2 . GLU 21 21 18995 2 . GLY 22 22 18995 2 . ASP 23 23 18995 2 . LYS 24 24 18995 2 . HIS 25 25 18995 2 . LYS 26 26 18995 2 . LEU 27 27 18995 2 . LYS 28 28 18995 2 . LYS 29 29 18995 2 . SER 30 30 18995 2 . GLU 31 31 18995 2 . LEU 32 32 18995 2 . LYS 33 33 18995 2 . GLU 34 34 18995 2 . LEU 35 35 18995 2 . ILE 36 36 18995 2 . ASN 37 37 18995 2 . ASN 38 38 18995 2 . GLU 39 39 18995 2 . LEU 40 40 18995 2 . SER 41 41 18995 2 . HIS 42 42 18995 2 . PHE 43 43 18995 2 . LEU 44 44 18995 2 . GLU 45 45 18995 2 . GLU 46 46 18995 2 . ILE 47 47 18995 2 . LYS 48 48 18995 2 . GLU 49 49 18995 2 . GLN 50 50 18995 2 . GLU 51 51 18995 2 . VAL 52 52 18995 2 . VAL 53 53 18995 2 . ASP 54 54 18995 2 . LYS 55 55 18995 2 . VAL 56 56 18995 2 . MET 57 57 18995 2 . GLU 58 58 18995 2 . THR 59 59 18995 2 . LEU 60 60 18995 2 . ASP 61 61 18995 2 . ASN 62 62 18995 2 . ASP 63 63 18995 2 . GLY 64 64 18995 2 . ASP 65 65 18995 2 . GLY 66 66 18995 2 . GLU 67 67 18995 2 . CYS 68 68 18995 2 . ASP 69 69 18995 2 . PHE 70 70 18995 2 . GLN 71 71 18995 2 . GLU 72 72 18995 2 . PHE 73 73 18995 2 . MET 74 74 18995 2 . ALA 75 75 18995 2 . PHE 76 76 18995 2 . VAL 77 77 18995 2 . ALA 78 78 18995 2 . MET 79 79 18995 2 . VAL 80 80 18995 2 . THR 81 81 18995 2 . THR 82 82 18995 2 . ALA 83 83 18995 2 . CYS 84 84 18995 2 . HIS 85 85 18995 2 . GLU 86 86 18995 2 . PHE 87 87 18995 2 . PHE 88 88 18995 2 . GLU 89 89 18995 2 . HIS 90 90 18995 2 . GLU 91 91 18995 2 . SER 92 92 18995 2 . GLU 93 93 18995 2 . LEU 94 94 18995 2 . GLU 95 95 18995 2 . LYS 96 96 18995 2 . ALA 97 97 18995 2 . MET 98 98 18995 2 . VAL 99 99 18995 2 . ALA 100 100 18995 2 . LEU 101 101 18995 2 . ILE 102 102 18995 2 . ASP 103 103 18995 2 . VAL 104 104 18995 2 . PHE 105 105 18995 2 . HIS 106 106 18995 2 . GLN 107 107 18995 2 . TYR 108 108 18995 2 . SER 109 109 18995 2 . GLY 110 110 18995 2 . ARG 111 111 18995 2 . GLU 112 112 18995 2 . GLY 113 113 18995 2 . ASP 114 114 18995 2 . LYS 115 115 18995 2 . HIS 116 116 18995 2 . LYS 117 117 18995 2 . LEU 118 118 18995 2 . LYS 119 119 18995 2 . LYS 120 120 18995 2 . SER 121 121 18995 2 . GLU 122 122 18995 2 . LEU 123 123 18995 2 . LYS 124 124 18995 2 . GLU 125 125 18995 2 . LEU 126 126 18995 2 . ILE 127 127 18995 2 . ASN 128 128 18995 2 . ASN 129 129 18995 2 . GLU 130 130 18995 2 . LEU 131 131 18995 2 . SER 132 132 18995 2 . HIS 133 133 18995 2 . PHE 134 134 18995 2 . LEU 135 135 18995 2 . GLU 136 136 18995 2 . GLU 137 137 18995 2 . ILE 138 138 18995 2 . LYS 139 139 18995 2 . GLU 140 140 18995 2 . GLN 141 141 18995 2 . GLU 142 142 18995 2 . VAL 143 143 18995 2 . VAL 144 144 18995 2 . ASP 145 145 18995 2 . LYS 146 146 18995 2 . VAL 147 147 18995 2 . MET 148 148 18995 2 . GLU 149 149 18995 2 . THR 150 150 18995 2 . LEU 151 151 18995 2 . ASP 152 152 18995 2 . ASN 153 153 18995 2 . ASP 154 154 18995 2 . GLY 155 155 18995 2 . ASP 156 156 18995 2 . GLY 157 157 18995 2 . GLU 158 158 18995 2 . CYS 159 159 18995 2 . ASP 160 160 18995 2 . PHE 161 161 18995 2 . GLN 162 162 18995 2 . GLU 163 163 18995 2 . PHE 164 164 18995 2 . MET 165 165 18995 2 . ALA 166 166 18995 2 . PHE 167 167 18995 2 . VAL 168 168 18995 2 . ALA 169 169 18995 2 . MET 170 170 18995 2 . VAL 171 171 18995 2 . THR 172 172 18995 2 . THR 173 173 18995 2 . ALA 174 174 18995 2 . CYS 175 175 18995 2 . HIS 176 176 18995 2 . GLU 177 177 18995 2 . PHE 178 178 18995 2 . PHE 179 179 18995 2 . GLU 180 180 18995 2 . HIS 181 181 18995 2 . GLU 182 182 18995 2 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 18995 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $FGF2 . 9606 plasmid . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18995 1 2 2 $S100B . 9606 plasmid . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 18995 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 18995 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $FGF2 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli 'BL21 (DE3)' . . . . . . . . . . . . . . . pET(20b)+ . . . . . . 18995 1 2 2 $S100B . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli 'BL21 (DE3)' . . . . . . . . . . . . . . . pET(20b)+ . . . . . . 18995 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18995 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O/10% D2O' _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 S100B '[U-100% 13C; U-100% 15N]' . . 2 $S100B . . 1.2 . . mM . . . . 18995 1 2 TRIS 'natural abundance' . . . . . . 20 . . mM . . . . 18995 1 3 'ammonium sulfate' 'natural abundance' . . . . . . 50 . . mM . . . . 18995 1 4 'calcium chloride' 'natural abundance' . . . . . . 5 . . mM . . . . 18995 1 5 DTT 'natural abundance' . . . . . . 5 . . mM . . . . 18995 1 6 'sodium azide' 'natural abundance' . . . . . . 0.01 . . % . . . . 18995 1 7 H2O 'natural abundance' . . . . . . 90 . . % . . . . 18995 1 8 D2O 'natural abundance' . . . . . . 10 . . % . . . . 18995 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 18995 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.050 . M 18995 1 pH 7.2 . pH 18995 1 pressure 1 . atm 18995 1 temperature 298 . K 18995 1 stop_ save_ ############################ # Computer software used # ############################ save_VNMRJ _Software.Sf_category software _Software.Sf_framecode VNMRJ _Software.Entry_ID 18995 _Software.ID 1 _Software.Name VNMRJ _Software.Version 3.2 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Varian . . 18995 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 18995 1 processing 18995 1 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 18995 _Software.ID 2 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 18995 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 18995 2 'data analysis' 18995 2 'peak picking' 18995 2 stop_ save_ save_HADDOCK _Software.Sf_category software _Software.Sf_framecode HADDOCK _Software.Entry_ID 18995 _Software.ID 3 _Software.Name HADDOCK _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Alexandre Bonvin' . . 18995 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 18995 3 'structure solution' 18995 3 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 18995 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model INOVA _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 700 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 18995 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 Varian INOVA . 700 . . . 18995 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 18995 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18995 1 2 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18995 1 3 '3D HN(CO)CA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18995 1 4 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18995 1 5 '3D HCACO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18995 1 6 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18995 1 7 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18995 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 18995 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 TSP 'methyl protons' . . . . ppm 0.00 na indirect 0.251449530 . . . . . . . . . 18995 1 H 1 TSP 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 18995 1 N 15 TSP 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 18995 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 18995 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-15N HSQC' . . . 18995 1 2 '3D HNCA' . . . 18995 1 3 '3D HN(CO)CA' . . . 18995 1 4 '3D HNCO' . . . 18995 1 5 '3D HCACO' . . . 18995 1 6 '3D CBCA(CO)NH' . . . 18995 1 7 '3D HNCACB' . . . 18995 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 2 2 1 1 SER C C 13 174.260 0.20 0.990 1 . . . B 1 SER C . 18995 1 2 . 2 2 1 1 SER CA C 13 57.700 0.20 1.000 1 . . . B 1 SER CA . 18995 1 3 . 2 2 1 1 SER CB C 13 65.500 0.20 1.000 1 . . . B 1 SER CB . 18995 1 4 . 2 2 2 2 GLU H H 1 9.267 0.02 0.990 1 . . . B 2 GLU H . 18995 1 5 . 2 2 2 2 GLU CA C 13 60.100 0.20 0.635 1 . . . B 2 GLU CA . 18995 1 6 . 2 2 2 2 GLU CB C 13 29.300 0.20 0.629 1 . . . B 2 GLU CB . 18995 1 7 . 2 2 2 2 GLU N N 15 120.641 0.20 0.990 1 . . . B 2 GLU N . 18995 1 8 . 2 2 3 3 LEU C C 13 177.352 0.20 1.000 1 . . . B 3 LEU C . 18995 1 9 . 2 2 3 3 LEU CA C 13 58.400 0.20 1.000 1 . . . B 3 LEU CA . 18995 1 10 . 2 2 3 3 LEU CB C 13 42.400 0.20 1.000 1 . . . B 3 LEU CB . 18995 1 11 . 2 2 4 4 GLU H H 1 8.237 0.02 1.000 1 . . . B 4 GLU H . 18995 1 12 . 2 2 4 4 GLU C C 13 178.536 0.20 1.000 1 . . . B 4 GLU C . 18995 1 13 . 2 2 4 4 GLU CA C 13 59.900 0.20 1.000 1 . . . B 4 GLU CA . 18995 1 14 . 2 2 4 4 GLU CB C 13 30.000 0.20 1.000 1 . . . B 4 GLU CB . 18995 1 15 . 2 2 4 4 GLU N N 15 120.469 0.20 1.000 1 . . . B 4 GLU N . 18995 1 16 . 2 2 5 5 LYS H H 1 8.729 0.02 1.000 1 . . . B 5 LYS H . 18995 1 17 . 2 2 5 5 LYS C C 13 179.518 0.20 1.000 1 . . . B 5 LYS C . 18995 1 18 . 2 2 5 5 LYS CA C 13 60.400 0.20 1.000 1 . . . B 5 LYS CA . 18995 1 19 . 2 2 5 5 LYS CB C 13 32.900 0.20 1.000 1 . . . B 5 LYS CB . 18995 1 20 . 2 2 5 5 LYS CE C 13 42.100 0.20 0.161 1 . . . B 5 LYS CE . 18995 1 21 . 2 2 5 5 LYS N N 15 117.682 0.20 1.000 1 . . . B 5 LYS N . 18995 1 22 . 2 2 6 6 ALA H H 1 8.084 0.02 1.000 1 . . . B 6 ALA H . 18995 1 23 . 2 2 6 6 ALA CA C 13 55.300 0.20 1.000 1 . . . B 6 ALA CA . 18995 1 24 . 2 2 6 6 ALA N N 15 124.152 0.20 1.000 1 . . . B 6 ALA N . 18995 1 25 . 2 2 8 8 VAL C C 13 177.294 0.20 1.000 1 . . . B 8 VAL C . 18995 1 26 . 2 2 8 8 VAL CA C 13 66.900 0.20 1.000 1 . . . B 8 VAL CA . 18995 1 27 . 2 2 8 8 VAL CB C 13 32.000 0.20 1.000 1 . . . B 8 VAL CB . 18995 1 28 . 2 2 9 9 ALA H H 1 8.050 0.02 1.000 1 . . . B 9 ALA H . 18995 1 29 . 2 2 9 9 ALA C C 13 178.639 0.20 1.000 1 . . . B 9 ALA C . 18995 1 30 . 2 2 9 9 ALA CA C 13 55.400 0.20 1.000 1 . . . B 9 ALA CA . 18995 1 31 . 2 2 9 9 ALA CB C 13 18.400 0.20 1.000 1 . . . B 9 ALA CB . 18995 1 32 . 2 2 9 9 ALA N N 15 122.839 0.20 1.000 1 . . . B 9 ALA N . 18995 1 33 . 2 2 10 10 LEU H H 1 8.179 0.02 1.000 1 . . . B 10 LEU H . 18995 1 34 . 2 2 10 10 LEU C C 13 178.381 0.20 1.000 1 . . . B 10 LEU C . 18995 1 35 . 2 2 10 10 LEU CA C 13 59.100 0.20 1.000 1 . . . B 10 LEU CA . 18995 1 36 . 2 2 10 10 LEU CB C 13 42.500 0.20 1.000 1 . . . B 10 LEU CB . 18995 1 37 . 2 2 10 10 LEU N N 15 117.815 0.20 1.000 1 . . . B 10 LEU N . 18995 1 38 . 2 2 11 11 ILE H H 1 7.666 0.02 1.000 1 . . . B 11 ILE H . 18995 1 39 . 2 2 11 11 ILE C C 13 177.860 0.20 1.000 1 . . . B 11 ILE C . 18995 1 40 . 2 2 11 11 ILE CA C 13 65.100 0.20 1.000 1 . . . B 11 ILE CA . 18995 1 41 . 2 2 11 11 ILE N N 15 118.370 0.20 1.000 1 . . . B 11 ILE N . 18995 1 42 . 2 2 12 12 ASP H H 1 8.719 0.02 1.000 1 . . . B 12 ASP H . 18995 1 43 . 2 2 12 12 ASP C C 13 179.459 0.20 1.000 1 . . . B 12 ASP C . 18995 1 44 . 2 2 12 12 ASP CA C 13 58.100 0.20 1.000 1 . . . B 12 ASP CA . 18995 1 45 . 2 2 12 12 ASP CB C 13 40.900 0.20 1.000 1 . . . B 12 ASP CB . 18995 1 46 . 2 2 12 12 ASP N N 15 122.812 0.20 1.000 1 . . . B 12 ASP N . 18995 1 47 . 2 2 13 13 VAL H H 1 8.929 0.02 1.000 1 . . . B 13 VAL H . 18995 1 48 . 2 2 13 13 VAL C C 13 177.167 0.20 1.000 1 . . . B 13 VAL C . 18995 1 49 . 2 2 13 13 VAL CA C 13 66.700 0.20 1.000 1 . . . B 13 VAL CA . 18995 1 50 . 2 2 13 13 VAL N N 15 121.403 0.20 1.000 1 . . . B 13 VAL N . 18995 1 51 . 2 2 14 14 PHE H H 1 8.058 0.02 1.000 1 . . . B 14 PHE H . 18995 1 52 . 2 2 14 14 PHE C C 13 177.234 0.20 1.000 1 . . . B 14 PHE C . 18995 1 53 . 2 2 14 14 PHE CA C 13 63.200 0.20 1.000 1 . . . B 14 PHE CA . 18995 1 54 . 2 2 14 14 PHE CB C 13 39.400 0.20 1.000 1 . . . B 14 PHE CB . 18995 1 55 . 2 2 14 14 PHE N N 15 120.152 0.20 1.000 1 . . . B 14 PHE N . 18995 1 56 . 2 2 15 15 HIS H H 1 8.239 0.02 1.000 1 . . . B 15 HIS H . 18995 1 57 . 2 2 15 15 HIS C C 13 178.154 0.20 1.000 1 . . . B 15 HIS C . 18995 1 58 . 2 2 15 15 HIS CA C 13 58.400 0.20 1.000 1 . . . B 15 HIS CA . 18995 1 59 . 2 2 15 15 HIS CB C 13 29.000 0.20 1.000 1 . . . B 15 HIS CB . 18995 1 60 . 2 2 15 15 HIS N N 15 116.727 0.20 1.000 1 . . . B 15 HIS N . 18995 1 61 . 2 2 16 16 GLN H H 1 8.363 0.02 1.000 1 . . . B 16 GLN H . 18995 1 62 . 2 2 16 16 GLN C C 13 177.482 0.20 1.000 1 . . . B 16 GLN C . 18995 1 63 . 2 2 16 16 GLN CA C 13 58.900 0.20 1.000 1 . . . B 16 GLN CA . 18995 1 64 . 2 2 16 16 GLN CB C 13 28.300 0.20 1.000 1 . . . B 16 GLN CB . 18995 1 65 . 2 2 16 16 GLN N N 15 122.963 0.20 1.000 1 . . . B 16 GLN N . 18995 1 66 . 2 2 17 17 TYR H H 1 7.264 0.02 1.000 1 . . . B 17 TYR H . 18995 1 67 . 2 2 17 17 TYR C C 13 176.106 0.20 1.000 1 . . . B 17 TYR C . 18995 1 68 . 2 2 17 17 TYR CA C 13 61.300 0.20 1.000 1 . . . B 17 TYR CA . 18995 1 69 . 2 2 17 17 TYR CB C 13 40.400 0.20 1.000 1 . . . B 17 TYR CB . 18995 1 70 . 2 2 17 17 TYR N N 15 116.073 0.20 1.000 1 . . . B 17 TYR N . 18995 1 71 . 2 2 18 18 SER H H 1 9.228 0.02 1.000 1 . . . B 18 SER H . 18995 1 72 . 2 2 18 18 SER C C 13 177.339 0.20 1.000 1 . . . B 18 SER C . 18995 1 73 . 2 2 18 18 SER CA C 13 62.100 0.20 1.000 1 . . . B 18 SER CA . 18995 1 74 . 2 2 18 18 SER N N 15 116.120 0.20 1.000 1 . . . B 18 SER N . 18995 1 75 . 2 2 19 19 GLY H H 1 7.758 0.02 1.000 1 . . . B 19 GLY H . 18995 1 76 . 2 2 19 19 GLY C C 13 173.303 0.20 1.000 1 . . . B 19 GLY C . 18995 1 77 . 2 2 19 19 GLY CA C 13 45.700 0.20 1.000 1 . . . B 19 GLY CA . 18995 1 78 . 2 2 19 19 GLY N N 15 110.664 0.20 1.000 1 . . . B 19 GLY N . 18995 1 79 . 2 2 20 20 ARG H H 1 7.135 0.02 1.000 1 . . . B 20 ARG H . 18995 1 80 . 2 2 20 20 ARG C C 13 177.097 0.20 1.000 1 . . . B 20 ARG C . 18995 1 81 . 2 2 20 20 ARG CA C 13 60.100 0.20 1.000 1 . . . B 20 ARG CA . 18995 1 82 . 2 2 20 20 ARG CB C 13 31.000 0.20 1.000 1 . . . B 20 ARG CB . 18995 1 83 . 2 2 20 20 ARG CD C 13 43.300 0.20 0.155 1 . . . B 20 ARG CD . 18995 1 84 . 2 2 20 20 ARG N N 15 121.554 0.20 1.000 1 . . . B 20 ARG N . 18995 1 85 . 2 2 21 21 GLU H H 1 9.468 0.02 1.000 1 . . . B 21 GLU H . 18995 1 86 . 2 2 21 21 GLU C C 13 175.055 0.20 0.998 1 . . . B 21 GLU C . 18995 1 87 . 2 2 21 21 GLU CA C 13 55.600 0.20 1.000 1 . . . B 21 GLU CA . 18995 1 88 . 2 2 21 21 GLU CB C 13 35.700 0.20 1.000 1 . . . B 21 GLU CB . 18995 1 89 . 2 2 21 21 GLU N N 15 116.519 0.20 1.000 1 . . . B 21 GLU N . 18995 1 90 . 2 2 23 23 ASP H H 1 8.115 0.02 1.000 1 . . . B 23 ASP H . 18995 1 91 . 2 2 23 23 ASP C C 13 178.957 0.20 1.000 1 . . . B 23 ASP C . 18995 1 92 . 2 2 23 23 ASP CA C 13 55.500 0.20 1.000 1 . . . B 23 ASP CA . 18995 1 93 . 2 2 24 24 LYS C C 13 176.539 0.20 1.000 1 . . . B 24 LYS C . 18995 1 94 . 2 2 24 24 LYS CA C 13 58.200 0.20 1.000 1 . . . B 24 LYS CA . 18995 1 95 . 2 2 24 24 LYS CB C 13 31.700 0.20 1.000 1 . . . B 24 LYS CB . 18995 1 96 . 2 2 24 24 LYS CE C 13 42.100 0.20 0.161 1 . . . B 24 LYS CE . 18995 1 97 . 2 2 24 24 LYS N N 15 131.954 0.20 1.000 1 . . . B 24 LYS N . 18995 1 98 . 2 2 25 25 HIS H H 1 9.589 0.02 1.000 1 . . . B 25 HIS H . 18995 1 99 . 2 2 25 25 HIS C C 13 172.815 0.20 1.000 1 . . . B 25 HIS C . 18995 1 100 . 2 2 25 25 HIS CA C 13 55.500 0.20 1.000 1 . . . B 25 HIS CA . 18995 1 101 . 2 2 25 25 HIS CB C 13 30.800 0.20 1.000 1 . . . B 25 HIS CB . 18995 1 102 . 2 2 25 25 HIS N N 15 119.313 0.20 1.000 1 . . . B 25 HIS N . 18995 1 103 . 2 2 26 26 LYS H H 1 7.095 0.02 1.000 1 . . . B 26 LYS H . 18995 1 104 . 2 2 26 26 LYS C C 13 174.608 0.20 1.000 1 . . . B 26 LYS C . 18995 1 105 . 2 2 26 26 LYS CA C 13 55.400 0.20 1.000 1 . . . B 26 LYS CA . 18995 1 106 . 2 2 26 26 LYS CB C 13 39.100 0.20 1.000 1 . . . B 26 LYS CB . 18995 1 107 . 2 2 26 26 LYS CE C 13 42.100 0.20 0.161 1 . . . B 26 LYS CE . 18995 1 108 . 2 2 26 26 LYS N N 15 115.394 0.20 1.000 1 . . . B 26 LYS N . 18995 1 109 . 2 2 27 27 LEU H H 1 9.595 0.02 1.000 1 . . . B 27 LEU H . 18995 1 110 . 2 2 27 27 LEU C C 13 175.637 0.20 1.000 1 . . . B 27 LEU C . 18995 1 111 . 2 2 27 27 LEU CA C 13 52.800 0.20 1.000 1 . . . B 27 LEU CA . 18995 1 112 . 2 2 27 27 LEU CB C 13 43.700 0.20 1.000 1 . . . B 27 LEU CB . 18995 1 113 . 2 2 27 27 LEU N N 15 126.263 0.20 1.000 1 . . . B 27 LEU N . 18995 1 114 . 2 2 28 28 LYS H H 1 9.711 0.02 1.000 1 . . . B 28 LYS H . 18995 1 115 . 2 2 28 28 LYS C C 13 177.395 0.20 1.000 1 . . . B 28 LYS C . 18995 1 116 . 2 2 28 28 LYS CA C 13 55.200 0.20 1.000 1 . . . B 28 LYS CA . 18995 1 117 . 2 2 28 28 LYS CB C 13 33.000 0.20 1.000 1 . . . B 28 LYS CB . 18995 1 118 . 2 2 28 28 LYS CE C 13 42.100 0.20 0.161 1 . . . B 28 LYS CE . 18995 1 119 . 2 2 28 28 LYS N N 15 124.436 0.20 1.000 1 . . . B 28 LYS N . 18995 1 120 . 2 2 29 29 LYS H H 1 9.084 0.02 1.000 1 . . . B 29 LYS H . 18995 1 121 . 2 2 29 29 LYS C C 13 177.400 0.20 1.000 1 . . . B 29 LYS C . 18995 1 122 . 2 2 29 29 LYS CA C 13 62.700 0.20 1.000 1 . . . B 29 LYS CA . 18995 1 123 . 2 2 29 29 LYS CB C 13 32.500 0.20 1.000 1 . . . B 29 LYS CB . 18995 1 124 . 2 2 29 29 LYS CE C 13 42.100 0.20 0.161 1 . . . B 29 LYS CE . 18995 1 125 . 2 2 29 29 LYS N N 15 121.980 0.20 1.000 1 . . . B 29 LYS N . 18995 1 126 . 2 2 30 30 SER H H 1 8.267 0.02 1.000 1 . . . B 30 SER H . 18995 1 127 . 2 2 30 30 SER C C 13 176.950 0.20 1.000 1 . . . B 30 SER C . 18995 1 128 . 2 2 30 30 SER CA C 13 61.100 0.20 1.000 1 . . . B 30 SER CA . 18995 1 129 . 2 2 30 30 SER CB C 13 61.300 0.20 1.000 1 . . . B 30 SER CB . 18995 1 130 . 2 2 30 30 SER N N 15 111.519 0.20 1.000 1 . . . B 30 SER N . 18995 1 131 . 2 2 31 31 GLU H H 1 6.603 0.02 1.000 1 . . . B 31 GLU H . 18995 1 132 . 2 2 31 31 GLU C C 13 179.463 0.20 1.000 1 . . . B 31 GLU C . 18995 1 133 . 2 2 31 31 GLU CA C 13 60.100 0.20 1.000 1 . . . B 31 GLU CA . 18995 1 134 . 2 2 31 31 GLU CB C 13 29.200 0.20 1.000 1 . . . B 31 GLU CB . 18995 1 135 . 2 2 31 31 GLU N N 15 123.792 0.20 1.000 1 . . . B 31 GLU N . 18995 1 136 . 2 2 32 32 LEU H H 1 8.936 0.02 1.000 1 . . . B 32 LEU H . 18995 1 137 . 2 2 32 32 LEU C C 13 176.995 0.20 1.000 1 . . . B 32 LEU C . 18995 1 138 . 2 2 32 32 LEU CA C 13 57.900 0.20 1.000 1 . . . B 32 LEU CA . 18995 1 139 . 2 2 32 32 LEU CB C 13 42.300 0.20 1.000 1 . . . B 32 LEU CB . 18995 1 140 . 2 2 32 32 LEU N N 15 121.954 0.20 1.000 1 . . . B 32 LEU N . 18995 1 141 . 2 2 33 33 LYS H H 1 8.390 0.02 1.000 1 . . . B 33 LYS H . 18995 1 142 . 2 2 33 33 LYS C C 13 176.714 0.20 1.000 1 . . . B 33 LYS C . 18995 1 143 . 2 2 33 33 LYS CA C 13 60.500 0.20 1.000 1 . . . B 33 LYS CA . 18995 1 144 . 2 2 33 33 LYS CB C 13 32.900 0.20 1.000 1 . . . B 33 LYS CB . 18995 1 145 . 2 2 33 33 LYS CE C 13 42.100 0.20 0.161 1 . . . B 33 LYS CE . 18995 1 146 . 2 2 33 33 LYS N N 15 118.576 0.20 1.000 1 . . . B 33 LYS N . 18995 1 147 . 2 2 34 34 GLU H H 1 7.326 0.02 1.000 1 . . . B 34 GLU H . 18995 1 148 . 2 2 34 34 GLU C C 13 177.689 0.20 1.000 1 . . . B 34 GLU C . 18995 1 149 . 2 2 34 34 GLU CA C 13 59.400 0.20 1.000 1 . . . B 34 GLU CA . 18995 1 150 . 2 2 34 34 GLU CB C 13 29.400 0.20 1.000 1 . . . B 34 GLU CB . 18995 1 151 . 2 2 34 34 GLU N N 15 116.152 0.20 1.000 1 . . . B 34 GLU N . 18995 1 152 . 2 2 35 35 LEU H H 1 7.978 0.02 1.000 1 . . . B 35 LEU H . 18995 1 153 . 2 2 35 35 LEU C C 13 178.845 0.20 1.000 1 . . . B 35 LEU C . 18995 1 154 . 2 2 35 35 LEU CA C 13 59.800 0.20 1.000 1 . . . B 35 LEU CA . 18995 1 155 . 2 2 35 35 LEU CB C 13 42.000 0.20 1.000 1 . . . B 35 LEU CB . 18995 1 156 . 2 2 35 35 LEU N N 15 123.632 0.20 1.000 1 . . . B 35 LEU N . 18995 1 157 . 2 2 36 36 ILE H H 1 8.470 0.02 1.000 1 . . . B 36 ILE H . 18995 1 158 . 2 2 36 36 ILE C C 13 178.328 0.20 1.000 1 . . . B 36 ILE C . 18995 1 159 . 2 2 36 36 ILE CA C 13 66.300 0.20 1.000 1 . . . B 36 ILE CA . 18995 1 160 . 2 2 36 36 ILE CB C 13 38.700 0.20 1.000 1 . . . B 36 ILE CB . 18995 1 161 . 2 2 36 36 ILE N N 15 121.271 0.20 1.000 1 . . . B 36 ILE N . 18995 1 162 . 2 2 37 37 ASN H H 1 8.336 0.02 1.000 1 . . . B 37 ASN H . 18995 1 163 . 2 2 37 37 ASN C C 13 177.052 0.20 1.000 1 . . . B 37 ASN C . 18995 1 164 . 2 2 37 37 ASN CA C 13 54.800 0.20 1.000 1 . . . B 37 ASN CA . 18995 1 165 . 2 2 37 37 ASN CB C 13 37.500 0.20 1.000 1 . . . B 37 ASN CB . 18995 1 166 . 2 2 37 37 ASN N N 15 118.242 0.20 1.000 1 . . . B 37 ASN N . 18995 1 167 . 2 2 38 38 ASN H H 1 8.213 0.02 1.000 1 . . . B 38 ASN H . 18995 1 168 . 2 2 38 38 ASN C C 13 176.578 0.20 1.000 1 . . . B 38 ASN C . 18995 1 169 . 2 2 38 38 ASN CA C 13 55.200 0.20 1.000 1 . . . B 38 ASN CA . 18995 1 170 . 2 2 38 38 ASN CB C 13 40.800 0.20 1.000 1 . . . B 38 ASN CB . 18995 1 171 . 2 2 38 38 ASN N N 15 114.845 0.20 1.000 1 . . . B 38 ASN N . 18995 1 172 . 2 2 39 39 GLU H H 1 8.522 0.02 1.000 1 . . . B 39 GLU H . 18995 1 173 . 2 2 39 39 GLU C C 13 177.689 0.20 1.000 1 . . . B 39 GLU C . 18995 1 174 . 2 2 39 39 GLU CA C 13 55.200 0.20 1.000 1 . . . B 39 GLU CA . 18995 1 175 . 2 2 39 39 GLU CB C 13 31.300 0.20 1.000 1 . . . B 39 GLU CB . 18995 1 176 . 2 2 39 39 GLU N N 15 113.797 0.20 1.000 1 . . . B 39 GLU N . 18995 1 177 . 2 2 40 40 LEU H H 1 7.552 0.02 1.000 1 . . . B 40 LEU H . 18995 1 178 . 2 2 40 40 LEU C C 13 177.212 0.20 1.000 1 . . . B 40 LEU C . 18995 1 179 . 2 2 40 40 LEU CA C 13 54.100 0.20 1.000 1 . . . B 40 LEU CA . 18995 1 180 . 2 2 40 40 LEU CB C 13 42.700 0.20 1.000 1 . . . B 40 LEU CB . 18995 1 181 . 2 2 40 40 LEU N N 15 119.982 0.20 1.000 1 . . . B 40 LEU N . 18995 1 182 . 2 2 41 41 SER H H 1 7.592 0.02 1.000 1 . . . B 41 SER H . 18995 1 183 . 2 2 41 41 SER C C 13 175.688 0.20 1.000 1 . . . B 41 SER C . 18995 1 184 . 2 2 41 41 SER CA C 13 60.800 0.20 1.000 1 . . . B 41 SER CA . 18995 1 185 . 2 2 41 41 SER CB C 13 64.100 0.20 1.000 1 . . . B 41 SER CB . 18995 1 186 . 2 2 41 41 SER N N 15 114.635 0.20 1.000 1 . . . B 41 SER N . 18995 1 187 . 2 2 42 42 HIS H H 1 10.406 0.02 1.000 1 . . . B 42 HIS H . 18995 1 188 . 2 2 42 42 HIS C C 13 175.523 0.20 1.000 1 . . . B 42 HIS C . 18995 1 189 . 2 2 42 42 HIS CA C 13 58.700 0.20 1.000 1 . . . B 42 HIS CA . 18995 1 190 . 2 2 42 42 HIS CB C 13 28.600 0.20 1.000 1 . . . B 42 HIS CB . 18995 1 191 . 2 2 42 42 HIS N N 15 122.397 0.20 1.000 1 . . . B 42 HIS N . 18995 1 192 . 2 2 43 43 PHE H H 1 7.785 0.02 1.000 1 . . . B 43 PHE H . 18995 1 193 . 2 2 43 43 PHE C C 13 177.431 0.20 1.000 1 . . . B 43 PHE C . 18995 1 194 . 2 2 43 43 PHE CA C 13 58.800 0.20 1.000 1 . . . B 43 PHE CA . 18995 1 195 . 2 2 43 43 PHE N N 15 117.618 0.20 1.000 1 . . . B 43 PHE N . 18995 1 196 . 2 2 44 44 LEU H H 1 8.533 0.02 1.000 1 . . . B 44 LEU H . 18995 1 197 . 2 2 44 44 LEU C C 13 175.829 0.20 1.000 1 . . . B 44 LEU C . 18995 1 198 . 2 2 44 44 LEU CA C 13 53.800 0.20 1.000 1 . . . B 44 LEU CA . 18995 1 199 . 2 2 44 44 LEU CB C 13 45.000 0.20 1.000 1 . . . B 44 LEU CB . 18995 1 200 . 2 2 44 44 LEU N N 15 120.185 0.20 1.000 1 . . . B 44 LEU N . 18995 1 201 . 2 2 45 45 GLU H H 1 8.130 0.02 1.000 1 . . . B 45 GLU H . 18995 1 202 . 2 2 45 45 GLU C C 13 175.060 0.20 1.000 1 . . . B 45 GLU C . 18995 1 203 . 2 2 45 45 GLU CA C 13 56.600 0.20 1.000 1 . . . B 45 GLU CA . 18995 1 204 . 2 2 45 45 GLU CB C 13 30.600 0.20 1.000 1 . . . B 45 GLU CB . 18995 1 205 . 2 2 45 45 GLU N N 15 121.499 0.20 1.000 1 . . . B 45 GLU N . 18995 1 206 . 2 2 46 46 GLU H H 1 8.123 0.02 1.000 1 . . . B 46 GLU H . 18995 1 207 . 2 2 46 46 GLU C C 13 176.861 0.20 1.000 1 . . . B 46 GLU C . 18995 1 208 . 2 2 46 46 GLU CA C 13 56.800 0.20 1.000 1 . . . B 46 GLU CA . 18995 1 209 . 2 2 46 46 GLU CB C 13 30.700 0.20 1.000 1 . . . B 46 GLU CB . 18995 1 210 . 2 2 46 46 GLU N N 15 122.480 0.20 1.000 1 . . . B 46 GLU N . 18995 1 211 . 2 2 47 47 ILE H H 1 9.897 0.02 1.000 1 . . . B 47 ILE H . 18995 1 212 . 2 2 47 47 ILE C C 13 175.931 0.20 1.000 1 . . . B 47 ILE C . 18995 1 213 . 2 2 47 47 ILE CA C 13 62.100 0.20 1.000 1 . . . B 47 ILE CA . 18995 1 214 . 2 2 47 47 ILE CB C 13 38.600 0.20 1.000 1 . . . B 47 ILE CB . 18995 1 215 . 2 2 47 47 ILE N N 15 127.680 0.20 1.000 1 . . . B 47 ILE N . 18995 1 216 . 2 2 48 48 LYS H H 1 9.077 0.02 1.000 1 . . . B 48 LYS H . 18995 1 217 . 2 2 48 48 LYS C C 13 175.896 0.20 1.000 1 . . . B 48 LYS C . 18995 1 218 . 2 2 48 48 LYS CA C 13 56.600 0.20 1.000 1 . . . B 48 LYS CA . 18995 1 219 . 2 2 48 48 LYS CB C 13 34.700 0.20 1.000 1 . . . B 48 LYS CB . 18995 1 220 . 2 2 48 48 LYS CE C 13 42.100 0.20 0.161 1 . . . B 48 LYS CE . 18995 1 221 . 2 2 48 48 LYS N N 15 126.846 0.20 1.000 1 . . . B 48 LYS N . 18995 1 222 . 2 2 49 49 GLU H H 1 7.636 0.02 1.000 1 . . . B 49 GLU H . 18995 1 223 . 2 2 49 49 GLU C C 13 179.470 0.20 1.000 1 . . . B 49 GLU C . 18995 1 224 . 2 2 49 49 GLU CA C 13 55.600 0.20 1.000 1 . . . B 49 GLU CA . 18995 1 225 . 2 2 49 49 GLU CB C 13 31.800 0.20 1.000 1 . . . B 49 GLU CB . 18995 1 226 . 2 2 49 49 GLU N N 15 118.747 0.20 1.000 1 . . . B 49 GLU N . 18995 1 227 . 2 2 50 50 GLN H H 1 9.041 0.02 1.000 1 . . . B 50 GLN H . 18995 1 228 . 2 2 50 50 GLN C C 13 176.883 0.20 1.000 1 . . . B 50 GLN C . 18995 1 229 . 2 2 50 50 GLN CA C 13 58.500 0.20 1.000 1 . . . B 50 GLN CA . 18995 1 230 . 2 2 50 50 GLN CB C 13 28.400 0.20 1.000 1 . . . B 50 GLN CB . 18995 1 231 . 2 2 50 50 GLN N N 15 125.850 0.20 1.000 1 . . . B 50 GLN N . 18995 1 232 . 2 2 51 51 GLU H H 1 9.352 0.02 1.000 1 . . . B 51 GLU H . 18995 1 233 . 2 2 51 51 GLU C C 13 178.262 0.20 1.000 1 . . . B 51 GLU C . 18995 1 234 . 2 2 51 51 GLU CA C 13 59.700 0.20 1.000 1 . . . B 51 GLU CA . 18995 1 235 . 2 2 51 51 GLU CB C 13 29.300 0.20 1.000 1 . . . B 51 GLU CB . 18995 1 236 . 2 2 51 51 GLU N N 15 117.404 0.20 1.000 1 . . . B 51 GLU N . 18995 1 237 . 2 2 52 52 VAL H H 1 7.247 0.02 1.000 1 . . . B 52 VAL H . 18995 1 238 . 2 2 52 52 VAL C C 13 177.677 0.20 1.000 1 . . . B 52 VAL C . 18995 1 239 . 2 2 52 52 VAL CA C 13 66.100 0.20 1.000 1 . . . B 52 VAL CA . 18995 1 240 . 2 2 52 52 VAL CB C 13 31.700 0.20 1.000 1 . . . B 52 VAL CB . 18995 1 241 . 2 2 52 52 VAL N N 15 118.888 0.20 1.000 1 . . . B 52 VAL N . 18995 1 242 . 2 2 53 53 VAL H H 1 7.264 0.02 1.000 1 . . . B 53 VAL H . 18995 1 243 . 2 2 53 53 VAL C C 13 176.742 0.20 1.000 1 . . . B 53 VAL C . 18995 1 244 . 2 2 53 53 VAL CA C 13 66.200 0.20 1.000 1 . . . B 53 VAL CA . 18995 1 245 . 2 2 53 53 VAL CB C 13 31.600 0.20 1.000 1 . . . B 53 VAL CB . 18995 1 246 . 2 2 53 53 VAL N N 15 119.906 0.20 1.000 1 . . . B 53 VAL N . 18995 1 247 . 2 2 54 54 ASP H H 1 8.524 0.02 1.000 1 . . . B 54 ASP H . 18995 1 248 . 2 2 54 54 ASP C C 13 178.291 0.20 1.000 1 . . . B 54 ASP C . 18995 1 249 . 2 2 54 54 ASP CA C 13 58.200 0.20 1.000 1 . . . B 54 ASP CA . 18995 1 250 . 2 2 54 54 ASP CB C 13 40.000 0.20 1.000 1 . . . B 54 ASP CB . 18995 1 251 . 2 2 54 54 ASP N N 15 121.483 0.20 1.000 1 . . . B 54 ASP N . 18995 1 252 . 2 2 55 55 LYS H H 1 7.580 0.02 1.000 1 . . . B 55 LYS H . 18995 1 253 . 2 2 55 55 LYS C C 13 179.054 0.20 1.000 1 . . . B 55 LYS C . 18995 1 254 . 2 2 55 55 LYS CA C 13 58.900 0.20 1.000 1 . . . B 55 LYS CA . 18995 1 255 . 2 2 55 55 LYS CB C 13 32.200 0.20 1.000 1 . . . B 55 LYS CB . 18995 1 256 . 2 2 55 55 LYS CE C 13 42.100 0.20 0.161 1 . . . B 55 LYS CE . 18995 1 257 . 2 2 55 55 LYS N N 15 120.875 0.20 1.000 1 . . . B 55 LYS N . 18995 1 258 . 2 2 56 56 VAL H H 1 8.279 0.02 1.000 1 . . . B 56 VAL H . 18995 1 259 . 2 2 56 56 VAL C C 13 178.221 0.20 1.000 1 . . . B 56 VAL C . 18995 1 260 . 2 2 56 56 VAL CA C 13 67.000 0.20 1.000 1 . . . B 56 VAL CA . 18995 1 261 . 2 2 56 56 VAL CB C 13 31.700 0.20 1.000 1 . . . B 56 VAL CB . 18995 1 262 . 2 2 56 56 VAL N N 15 121.960 0.20 1.000 1 . . . B 56 VAL N . 18995 1 263 . 2 2 57 57 MET H H 1 8.467 0.02 1.000 1 . . . B 57 MET H . 18995 1 264 . 2 2 57 57 MET C C 13 176.888 0.20 1.000 1 . . . B 57 MET C . 18995 1 265 . 2 2 57 57 MET CA C 13 57.900 0.20 1.000 1 . . . B 57 MET CA . 18995 1 266 . 2 2 57 57 MET CB C 13 32.900 0.20 1.000 1 . . . B 57 MET CB . 18995 1 267 . 2 2 57 57 MET N N 15 118.815 0.20 1.000 1 . . . B 57 MET N . 18995 1 268 . 2 2 58 58 GLU H H 1 8.073 0.02 1.000 1 . . . B 58 GLU H . 18995 1 269 . 2 2 58 58 GLU C C 13 178.510 0.20 1.000 1 . . . B 58 GLU C . 18995 1 270 . 2 2 58 58 GLU CA C 13 59.400 0.20 1.000 1 . . . B 58 GLU CA . 18995 1 271 . 2 2 58 58 GLU CB C 13 29.800 0.20 1.000 1 . . . B 58 GLU CB . 18995 1 272 . 2 2 58 58 GLU N N 15 117.894 0.20 1.000 1 . . . B 58 GLU N . 18995 1 273 . 2 2 59 59 THR H H 1 7.739 0.02 1.000 1 . . . B 59 THR H . 18995 1 274 . 2 2 59 59 THR C C 13 174.778 0.20 1.000 1 . . . B 59 THR C . 18995 1 275 . 2 2 59 59 THR CA C 13 65.600 0.20 1.000 1 . . . B 59 THR CA . 18995 1 276 . 2 2 59 59 THR CB C 13 69.600 0.20 1.000 1 . . . B 59 THR CB . 18995 1 277 . 2 2 59 59 THR N N 15 113.244 0.20 1.000 1 . . . B 59 THR N . 18995 1 278 . 2 2 60 60 LEU H H 1 7.643 0.02 1.000 1 . . . B 60 LEU H . 18995 1 279 . 2 2 60 60 LEU C C 13 177.561 0.20 1.000 1 . . . B 60 LEU C . 18995 1 280 . 2 2 60 60 LEU CA C 13 55.600 0.20 1.000 1 . . . B 60 LEU CA . 18995 1 281 . 2 2 60 60 LEU CB C 13 43.300 0.20 1.000 1 . . . B 60 LEU CB . 18995 1 282 . 2 2 60 60 LEU N N 15 119.636 0.20 1.000 1 . . . B 60 LEU N . 18995 1 283 . 2 2 61 61 ASP H H 1 7.984 0.02 1.000 1 . . . B 61 ASP H . 18995 1 284 . 2 2 61 61 ASP C C 13 175.915 0.20 1.000 1 . . . B 61 ASP C . 18995 1 285 . 2 2 61 61 ASP CA C 13 54.600 0.20 1.000 1 . . . B 61 ASP CA . 18995 1 286 . 2 2 61 61 ASP CB C 13 40.100 0.20 1.000 1 . . . B 61 ASP CB . 18995 1 287 . 2 2 61 61 ASP N N 15 117.424 0.20 1.000 1 . . . B 61 ASP N . 18995 1 288 . 2 2 62 62 ASN H H 1 9.032 0.02 1.000 1 . . . B 62 ASN H . 18995 1 289 . 2 2 62 62 ASN C C 13 175.905 0.20 1.000 1 . . . B 62 ASN C . 18995 1 290 . 2 2 62 62 ASN CA C 13 54.900 0.20 1.000 1 . . . B 62 ASN CA . 18995 1 291 . 2 2 62 62 ASN CB C 13 40.400 0.20 1.000 1 . . . B 62 ASN CB . 18995 1 292 . 2 2 62 62 ASN N N 15 127.650 0.20 1.000 1 . . . B 62 ASN N . 18995 1 293 . 2 2 63 63 ASP H H 1 8.302 0.02 1.000 1 . . . B 63 ASP H . 18995 1 294 . 2 2 63 63 ASP C C 13 177.604 0.20 1.000 1 . . . B 63 ASP C . 18995 1 295 . 2 2 63 63 ASP CA C 13 53.400 0.20 1.000 1 . . . B 63 ASP CA . 18995 1 296 . 2 2 63 63 ASP CB C 13 40.200 0.20 1.000 1 . . . B 63 ASP CB . 18995 1 297 . 2 2 63 63 ASP N N 15 116.676 0.20 1.000 1 . . . B 63 ASP N . 18995 1 298 . 2 2 64 64 GLY H H 1 7.681 0.02 1.000 1 . . . B 64 GLY H . 18995 1 299 . 2 2 64 64 GLY C C 13 174.834 0.20 1.000 1 . . . B 64 GLY C . 18995 1 300 . 2 2 64 64 GLY CA C 13 47.700 0.20 1.000 1 . . . B 64 GLY CA . 18995 1 301 . 2 2 64 64 GLY N N 15 109.334 0.20 1.000 1 . . . B 64 GLY N . 18995 1 302 . 2 2 65 65 ASP H H 1 8.386 0.02 1.000 1 . . . B 65 ASP H . 18995 1 303 . 2 2 65 65 ASP C C 13 177.010 0.20 1.000 1 . . . B 65 ASP C . 18995 1 304 . 2 2 65 65 ASP CA C 13 53.800 0.20 1.000 1 . . . B 65 ASP CA . 18995 1 305 . 2 2 65 65 ASP CB C 13 40.300 0.20 1.000 1 . . . B 65 ASP CB . 18995 1 306 . 2 2 65 65 ASP N N 15 120.960 0.20 1.000 1 . . . B 65 ASP N . 18995 1 307 . 2 2 66 66 GLY H H 1 10.212 0.02 1.000 1 . . . B 66 GLY H . 18995 1 308 . 2 2 66 66 GLY C C 13 172.343 0.20 1.000 1 . . . B 66 GLY C . 18995 1 309 . 2 2 66 66 GLY CA C 13 45.900 0.20 1.000 1 . . . B 66 GLY CA . 18995 1 310 . 2 2 66 66 GLY N N 15 113.875 0.20 1.000 1 . . . B 66 GLY N . 18995 1 311 . 2 2 67 67 GLU H H 1 7.949 0.02 1.000 1 . . . B 67 GLU H . 18995 1 312 . 2 2 67 67 GLU C C 13 174.711 0.20 1.000 1 . . . B 67 GLU C . 18995 1 313 . 2 2 67 67 GLU CA C 13 55.200 0.20 1.000 1 . . . B 67 GLU CA . 18995 1 314 . 2 2 67 67 GLU CB C 13 34.400 0.20 1.000 1 . . . B 67 GLU CB . 18995 1 315 . 2 2 67 67 GLU N N 15 118.701 0.20 1.000 1 . . . B 67 GLU N . 18995 1 316 . 2 2 68 68 CYS H H 1 9.486 0.02 1.000 1 . . . B 68 CYS H . 18995 1 317 . 2 2 68 68 CYS C C 13 174.411 0.20 1.000 1 . . . B 68 CYS C . 18995 1 318 . 2 2 68 68 CYS CA C 13 57.000 0.20 1.000 1 . . . B 68 CYS CA . 18995 1 319 . 2 2 68 68 CYS CB C 13 28.100 0.20 1.000 1 . . . B 68 CYS CB . 18995 1 320 . 2 2 68 68 CYS N N 15 124.753 0.20 1.000 1 . . . B 68 CYS N . 18995 1 321 . 2 2 69 69 ASP H H 1 9.911 0.02 1.000 1 . . . B 69 ASP H . 18995 1 322 . 2 2 69 69 ASP C C 13 175.307 0.20 1.000 1 . . . B 69 ASP C . 18995 1 323 . 2 2 69 69 ASP CA C 13 53.300 0.20 1.000 1 . . . B 69 ASP CA . 18995 1 324 . 2 2 69 69 ASP CB C 13 40.600 0.20 1.000 1 . . . B 69 ASP CB . 18995 1 325 . 2 2 69 69 ASP N N 15 132.376 0.20 1.000 1 . . . B 69 ASP N . 18995 1 326 . 2 2 70 70 PHE H H 1 9.075 0.02 1.000 1 . . . B 70 PHE H . 18995 1 327 . 2 2 70 70 PHE C C 13 176.482 0.20 1.000 1 . . . B 70 PHE C . 18995 1 328 . 2 2 70 70 PHE CA C 13 62.900 0.20 1.000 1 . . . B 70 PHE CA . 18995 1 329 . 2 2 70 70 PHE CB C 13 39.100 0.20 1.000 1 . . . B 70 PHE CB . 18995 1 330 . 2 2 70 70 PHE N N 15 119.131 0.20 1.000 1 . . . B 70 PHE N . 18995 1 331 . 2 2 71 71 GLN H H 1 8.047 0.02 1.000 1 . . . B 71 GLN H . 18995 1 332 . 2 2 71 71 GLN C C 13 179.517 0.20 1.000 1 . . . B 71 GLN C . 18995 1 333 . 2 2 71 71 GLN CA C 13 60.100 0.20 1.000 1 . . . B 71 GLN CA . 18995 1 334 . 2 2 71 71 GLN CB C 13 28.200 0.20 1.000 1 . . . B 71 GLN CB . 18995 1 335 . 2 2 71 71 GLN N N 15 119.323 0.20 1.000 1 . . . B 71 GLN N . 18995 1 336 . 2 2 72 72 GLU H H 1 9.061 0.02 1.000 1 . . . B 72 GLU H . 18995 1 337 . 2 2 72 72 GLU C C 13 179.337 0.20 1.000 1 . . . B 72 GLU C . 18995 1 338 . 2 2 72 72 GLU CA C 13 58.900 0.20 1.000 1 . . . B 72 GLU CA . 18995 1 339 . 2 2 72 72 GLU CB C 13 30.300 0.20 1.000 1 . . . B 72 GLU CB . 18995 1 340 . 2 2 72 72 GLU N N 15 123.228 0.20 1.000 1 . . . B 72 GLU N . 18995 1 341 . 2 2 73 73 PHE H H 1 8.863 0.02 1.000 1 . . . B 73 PHE H . 18995 1 342 . 2 2 73 73 PHE C C 13 176.497 0.20 1.000 1 . . . B 73 PHE C . 18995 1 343 . 2 2 73 73 PHE CA C 13 60.800 0.20 1.000 1 . . . B 73 PHE CA . 18995 1 344 . 2 2 73 73 PHE CB C 13 39.700 0.20 1.000 1 . . . B 73 PHE CB . 18995 1 345 . 2 2 73 73 PHE N N 15 123.155 0.20 1.000 1 . . . B 73 PHE N . 18995 1 346 . 2 2 74 74 MET H H 1 8.217 0.02 1.000 1 . . . B 74 MET H . 18995 1 347 . 2 2 74 74 MET C C 13 178.476 0.20 1.000 1 . . . B 74 MET C . 18995 1 348 . 2 2 74 74 MET CA C 13 56.200 0.20 1.000 1 . . . B 74 MET CA . 18995 1 349 . 2 2 74 74 MET CB C 13 30.400 0.20 1.000 1 . . . B 74 MET CB . 18995 1 350 . 2 2 74 74 MET N N 15 119.622 0.20 1.000 1 . . . B 74 MET N . 18995 1 351 . 2 2 75 75 ALA H H 1 7.490 0.02 1.000 1 . . . B 75 ALA H . 18995 1 352 . 2 2 75 75 ALA C C 13 180.129 0.20 1.000 1 . . . B 75 ALA C . 18995 1 353 . 2 2 75 75 ALA CA C 13 55.200 0.20 1.000 1 . . . B 75 ALA CA . 18995 1 354 . 2 2 75 75 ALA N N 15 123.073 0.20 1.000 1 . . . B 75 ALA N . 18995 1 355 . 2 2 76 76 PHE H H 1 7.676 0.02 1.000 1 . . . B 76 PHE H . 18995 1 356 . 2 2 76 76 PHE C C 13 176.365 0.20 1.000 1 . . . B 76 PHE C . 18995 1 357 . 2 2 76 76 PHE CA C 13 59.800 0.20 1.000 1 . . . B 76 PHE CA . 18995 1 358 . 2 2 76 76 PHE CB C 13 38.600 0.20 1.000 1 . . . B 76 PHE CB . 18995 1 359 . 2 2 76 76 PHE N N 15 122.171 0.20 1.000 1 . . . B 76 PHE N . 18995 1 360 . 2 2 77 77 VAL H H 1 8.498 0.02 1.000 1 . . . B 77 VAL H . 18995 1 361 . 2 2 77 77 VAL C C 13 179.175 0.20 1.000 1 . . . B 77 VAL C . 18995 1 362 . 2 2 77 77 VAL CA C 13 66.800 0.20 1.000 1 . . . B 77 VAL CA . 18995 1 363 . 2 2 77 77 VAL CB C 13 31.200 0.20 1.000 1 . . . B 77 VAL CB . 18995 1 364 . 2 2 77 77 VAL N N 15 119.765 0.20 1.000 1 . . . B 77 VAL N . 18995 1 365 . 2 2 78 78 ALA H H 1 8.193 0.02 1.000 1 . . . B 78 ALA H . 18995 1 366 . 2 2 78 78 ALA C C 13 178.630 0.20 1.000 1 . . . B 78 ALA C . 18995 1 367 . 2 2 78 78 ALA CA C 13 56.100 0.20 1.000 1 . . . B 78 ALA CA . 18995 1 368 . 2 2 78 78 ALA CB C 13 18.300 0.20 1.000 1 . . . B 78 ALA CB . 18995 1 369 . 2 2 78 78 ALA N N 15 123.880 0.20 1.000 1 . . . B 78 ALA N . 18995 1 370 . 2 2 79 79 MET H H 1 7.883 0.02 1.000 1 . . . B 79 MET H . 18995 1 371 . 2 2 79 79 MET C C 13 178.430 0.20 1.000 1 . . . B 79 MET C . 18995 1 372 . 2 2 79 79 MET CA C 13 59.500 0.20 1.000 1 . . . B 79 MET CA . 18995 1 373 . 2 2 79 79 MET CB C 13 32.800 0.20 1.000 1 . . . B 79 MET CB . 18995 1 374 . 2 2 79 79 MET N N 15 120.537 0.20 1.000 1 . . . B 79 MET N . 18995 1 375 . 2 2 80 80 VAL H H 1 8.299 0.02 1.000 1 . . . B 80 VAL H . 18995 1 376 . 2 2 80 80 VAL CA C 13 66.200 0.20 0.716 1 . . . B 80 VAL CA . 18995 1 377 . 2 2 80 80 VAL N N 15 120.374 0.20 1.000 1 . . . B 80 VAL N . 18995 1 378 . 2 2 82 82 THR C C 13 175.144 0.20 1.000 1 . . . B 82 THR C . 18995 1 379 . 2 2 82 82 THR CA C 13 65.800 0.20 1.000 1 . . . B 82 THR CA . 18995 1 380 . 2 2 83 83 ALA H H 1 7.587 0.02 1.000 1 . . . B 83 ALA H . 18995 1 381 . 2 2 83 83 ALA C C 13 178.574 0.20 1.000 1 . . . B 83 ALA C . 18995 1 382 . 2 2 83 83 ALA CA C 13 53.900 0.20 1.000 1 . . . B 83 ALA CA . 18995 1 383 . 2 2 83 83 ALA CB C 13 19.000 0.20 1.000 1 . . . B 83 ALA CB . 18995 1 384 . 2 2 83 83 ALA N N 15 123.244 0.20 1.000 1 . . . B 83 ALA N . 18995 1 385 . 2 2 84 84 CYS H H 1 7.788 0.02 1.000 1 . . . B 84 CYS H . 18995 1 386 . 2 2 84 84 CYS CA C 13 59.800 0.20 0.630 1 . . . B 84 CYS CA . 18995 1 387 . 2 2 84 84 CYS CB C 13 27.900 0.20 0.478 1 . . . B 84 CYS CB . 18995 1 388 . 2 2 84 84 CYS N N 15 116.910 0.20 1.000 1 . . . B 84 CYS N . 18995 1 389 . 2 2 86 86 GLU CA C 13 58.600 0.20 1.000 1 . . . B 86 GLU CA . 18995 1 390 . 2 2 86 86 GLU CB C 13 29.400 0.20 1.000 1 . . . B 86 GLU CB . 18995 1 391 . 2 2 87 87 PHE H H 1 7.838 0.02 1.000 1 . . . B 87 PHE H . 18995 1 392 . 2 2 87 87 PHE C C 13 175.597 0.20 1.000 1 . . . B 87 PHE C . 18995 1 393 . 2 2 87 87 PHE CA C 13 59.100 0.20 1.000 1 . . . B 87 PHE CA . 18995 1 394 . 2 2 87 87 PHE CB C 13 39.400 0.20 1.000 1 . . . B 87 PHE CB . 18995 1 395 . 2 2 87 87 PHE N N 15 118.550 0.20 1.000 1 . . . B 87 PHE N . 18995 1 396 . 2 2 88 88 PHE H H 1 7.718 0.02 1.000 1 . . . B 88 PHE H . 18995 1 397 . 2 2 88 88 PHE C C 13 175.241 0.20 1.000 1 . . . B 88 PHE C . 18995 1 398 . 2 2 88 88 PHE CA C 13 58.200 0.20 1.000 1 . . . B 88 PHE CA . 18995 1 399 . 2 2 88 88 PHE CB C 13 39.700 0.20 1.000 1 . . . B 88 PHE CB . 18995 1 400 . 2 2 88 88 PHE N N 15 118.438 0.20 1.000 1 . . . B 88 PHE N . 18995 1 401 . 2 2 89 89 GLU H H 1 7.959 0.02 1.000 1 . . . B 89 GLU H . 18995 1 402 . 2 2 89 89 GLU C C 13 175.437 0.20 1.000 1 . . . B 89 GLU C . 18995 1 403 . 2 2 89 89 GLU CA C 13 56.600 0.20 1.000 1 . . . B 89 GLU CA . 18995 1 404 . 2 2 89 89 GLU CB C 13 30.300 0.20 1.000 1 . . . B 89 GLU CB . 18995 1 405 . 2 2 89 89 GLU N N 15 121.366 0.20 1.000 1 . . . B 89 GLU N . 18995 1 406 . 2 2 90 90 HIS H H 1 8.116 0.02 1.000 1 . . . B 90 HIS H . 18995 1 407 . 2 2 90 90 HIS C C 13 173.652 0.20 1.000 1 . . . B 90 HIS C . 18995 1 408 . 2 2 90 90 HIS CA C 13 55.800 0.20 1.000 1 . . . B 90 HIS CA . 18995 1 409 . 2 2 90 90 HIS CB C 13 30.100 0.20 1.000 1 . . . B 90 HIS CB . 18995 1 410 . 2 2 90 90 HIS N N 15 120.349 0.20 1.000 1 . . . B 90 HIS N . 18995 1 411 . 2 2 91 91 GLU H H 1 8.235 0.02 1.000 1 . . . B 91 GLU H . 18995 1 412 . 2 2 91 91 GLU N N 15 127.965 0.20 1.000 1 . . . B 91 GLU N . 18995 1 stop_ save_