data_4889 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H and 15N Chemical Shift Assignment of c-Src SH3 complexed with RLP2 ligand in high salt solution ; _BMRB_accession_number 4889 _BMRB_flat_file_name bmr4889.str _Entry_type original _Submission_date 2000-10-30 _Accession_date 2000-10-30 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wang Chunyu . . 2 Pawley Norma H. . 3 Nicholson Linda K. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 70 "15N chemical shifts" 70 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-01-23 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4888 'c-Src SH3 monomer' stop_ _Original_release_date 2002-01-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The Role of Backbone Motions in Ligand Binding to the c-Src SH3 Domain' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21555253 _PubMed_ID 11697910 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wang Chunyu . . 2 Pawley Norma H. . 3 Nicholson Linda K. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 313 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 873 _Page_last 887 _Year 2001 _Details . save_ ################################## # Molecular system description # ################################## save_SH3-RLP2_complex _Saveframe_category molecular_system _Mol_system_name 'c-Src SH3 RLP2 peptide complex' _Abbreviation_common 'SH3-RLP2 complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'c-Src SH3' $SH3 RLP2 $RLP2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'binds proline rich motifs' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SH3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Src Homology 3 domain' _Abbreviation_common SH3 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 72 _Mol_residue_sequence ; AGGVTTFVALYDYESRTETD LSFKKGERLQIVNNTEGDWW LAHSLTTGQTGYIPSNYVAP SDSIQAEGIHRD ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 GLY 3 GLY 4 VAL 5 THR 6 THR 7 PHE 8 VAL 9 ALA 10 LEU 11 TYR 12 ASP 13 TYR 14 GLU 15 SER 16 ARG 17 THR 18 GLU 19 THR 20 ASP 21 LEU 22 SER 23 PHE 24 LYS 25 LYS 26 GLY 27 GLU 28 ARG 29 LEU 30 GLN 31 ILE 32 VAL 33 ASN 34 ASN 35 THR 36 GLU 37 GLY 38 ASP 39 TRP 40 TRP 41 LEU 42 ALA 43 HIS 44 SER 45 LEU 46 THR 47 THR 48 GLY 49 GLN 50 THR 51 GLY 52 TYR 53 ILE 54 PRO 55 SER 56 ASN 57 TYR 58 VAL 59 ALA 60 PRO 61 SER 62 ASP 63 SER 64 ILE 65 GLN 66 ALA 67 GLU 68 GLY 69 ILE 70 HIS 71 ARG 72 ASP stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value SWISS-PROT P00526 'Tyrosine-protein kinase transforming protein Src (pp60v-src) (p60-Src) (v-Src)' 93.06 526 98.51 98.51 5.10e-31 SWISS-PROT P12931 'Proto-oncogene tyrosine-protein kinase Src (pp60c-src) (p60-Src) (c-Src)' 93.06 536 98.51 100.00 5.97e-32 SWISS-PROT P00524 'Tyrosine-protein kinase transforming protein Src (pp60v-src) (p60-Src) (v-Src)' 93.06 526 100.00 100.00 2.72e-32 SWISS-PROT P00525 'Tyrosine-protein kinase transforming protein Src (pp60v-src) (p60-Src) (v-Src)' 93.06 526 100.00 100.00 2.72e-32 REF NP_955616 'pp60 SRC [Rous sarcoma virus]' 93.06 525 98.51 98.51 5.05e-31 SWISS-PROT P00523 'Proto-oncogene tyrosine-protein kinase Src (pp60c-src) (p60-Src) (c-Src)' 93.06 533 100.00 100.00 2.91e-32 REF NP_056888 'p60 src [Rous sarcoma virus]' 93.06 526 98.51 98.51 5.10e-31 REF NP_938033 'proto-oncogene tyrosine-protein kinase SRC [Homo sapiens]' 93.06 536 98.51 100.00 5.97e-32 REF NP_001020566 'Rous sarcoma oncogene isoform 2 [Mus musculus]' 93.06 535 98.51 100.00 6.07e-32 REF NP_005408 'proto-oncogene tyrosine-protein kinase SRC [Homo sapiens]' 93.06 536 98.51 100.00 5.97e-32 GenBank AAA49078 pp60c-scr 93.06 193 100.00 100.00 2.18e-32 GenBank AAA60584 'pp60 c-src-1 protein' 93.06 536 98.51 100.00 5.97e-32 GenBank AAA42571 'src-p60 phoshoprotein [Rous sarcoma virus]' 93.06 204 98.51 98.51 6.60e-31 GenBank AAA42583 'p66-src protein' 93.06 587 100.00 100.00 3.93e-32 EMBL CAC34523 'v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog (avian) [Homo sapiens]' 93.06 536 98.51 100.00 5.97e-32 GenBank AAA42565 'src-p60 phosphoprotein' 93.06 526 100.00 100.00 2.72e-32 EMBL CAA36156 'src protein [Avian sarcoma virus]' 93.06 587 100.00 100.00 3.93e-32 EMBL CAA37004 'v-3src-1 [Rous sarcoma virus]' 93.06 526 98.51 98.51 4.46e-31 EMBL CAA23696 'pp60-c-src protein [Gallus gallus]' 93.06 533 100.00 100.00 2.91e-32 EMBL CAA33404 'unnamed protein product [Rous sarcoma virus]' 93.06 526 98.51 98.51 4.53e-31 PDB 2SRC 'Crystal Structure Of Human Tyrosine-Protein Kinase C-Src, In Complex With Amp-Pnp' 88.89 452 98.44 100.00 5.01e-30 DBJ BAE26865 'unnamed protein product [Mus musculus]' 93.06 535 98.51 100.00 5.97e-32 PDB 2H8H 'Src Kinase In Complex With A Quinazoline Inhibitor' 93.06 535 98.51 100.00 5.92e-32 PDB 2PTK 'Chicken Src Tyrosine Kinase' 91.67 453 100.00 100.00 1.22e-31 PDB 1SRM '1h And 15n Assignments And Secondary Structure Of The Src Sh3 Domain' 84.72 64 100.00 100.00 2.73e-28 PDB 1Y57 'Structure Of Unphosphorylated C-Src In Complex With An Inhibitor' 88.89 452 98.44 100.00 5.14e-30 PDB 1RLQ 'Two Binding Orientations For Peptides To Src Sh3 Domain: Development Of A General Model For Sh3-Ligand Interactions' 84.72 64 100.00 100.00 2.73e-28 PDB 1SRL '1h And 15n Assignments And Secondary Structure Of The Src Sh3 Domain' 84.72 64 100.00 100.00 2.73e-28 PDB 1QWF 'C-Src Sh3 Domain Complexed With Ligand Vsl12' 83.33 64 100.00 100.00 8.14e-28 PDB 1RLP 'Two Binding Orientations For Peptides To Src Sh3 Domain: Development Of A General Model For Sh3-Ligand Interactions' 84.72 64 100.00 100.00 2.73e-28 PDB 1PRM 'Two Binding Orientations For Peptides To Src Sh3 Domain: Development Of A General Model For Sh3-Ligand Interactions' 84.72 64 100.00 100.00 2.73e-28 PDB 1QWE 'C-Src Sh3 Domain Complexed With Ligand App12' 83.33 64 100.00 100.00 8.14e-28 PDB 1NLP 'Structure Of Signal Transduction Protein, Nmr, Minimized Average Structure' 83.33 64 100.00 100.00 8.14e-28 PDB 1PRL 'Two Binding Orientations For Peptides To Src Sh3 Domain: Development Of A General Model For Sh3-Ligand Interactions' 84.72 64 100.00 100.00 2.73e-28 PDB 1KSW 'Structure Of Human C-Src Tyrosine Kinase (Thr338gly Mutant) In Complex With N6-Benzyl Adp' 88.89 452 98.44 100.00 5.27e-30 PDB 1NLO 'Structure Of Signal Transduction Protein, Nmr, Minimized Average Structure' 83.33 64 100.00 100.00 8.14e-28 BMRB 4888 'Src Homology 3 domain' 100.00 72 100.00 100.00 4.24e-35 PDB 1FMK 'Crystal Structure Of Human Tyrosine-Protein Kinase C-Src' 88.89 452 98.44 100.00 5.01e-30 stop_ save_ save_RLP2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common RLP2 _Abbreviation_common RLP2 _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 9 _Mol_residue_sequence RALPPLPRY loop_ _Residue_seq_code _Residue_label 1 ARG 2 ALA 3 LEU 4 PRO 5 PRO 6 LEU 7 PRO 8 ARG 9 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SH3 chicken 9031 Eukaryota Metazoa . . $RLP2 . . . . . . stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $SH3 'recombinant technology' . . . . . $RLP2 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SH3 1 mM [U-15N] $RLP2 4 eq . 'sodium phosphate' 50 mM . 'sodium sulphate' 200 mM . DTT 10 mM . pepstatin 5 mg/ml . EDTA 50 uM . benzamidine 10 ug/ml . chloramphenicol 50 uM . stop_ save_ ############################ # Computer software used # ############################ save_NMRpipe _Saveframe_category software _Name NMRpipe _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.2 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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_sh3_rlp2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'c-Src SH3' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 ALA H H 8.26 0.02 1 2 . 1 ALA N N 125.21 0.2 1 3 . 2 GLY H H 8.3 0.02 1 4 . 2 GLY N N 107.08 0.2 1 5 . 3 GLY H H 8.18 0.02 1 6 . 3 GLY N N 107.51 0.2 1 7 . 4 VAL H H 7.95 0.02 1 8 . 4 VAL N N 118.97 0.2 1 9 . 5 THR H H 8.42 0.02 1 10 . 5 THR N N 118.13 0.2 1 11 . 6 THR H H 8.24 0.02 1 12 . 6 THR N N 118.53 0.2 1 13 . 7 PHE H H 9.43 0.02 1 14 . 7 PHE N N 127.11 0.2 1 15 . 8 VAL H H 9.53 0.02 1 16 . 8 VAL N N 118.82 0.2 1 17 . 9 ALA H H 8.42 0.02 1 18 . 9 ALA N N 126.97 0.2 1 19 . 10 LEU H H 9.37 0.02 1 20 . 10 LEU N N 126.27 0.2 1 21 . 11 TYR H H 7.22 0.02 1 22 . 11 TYR N N 110.83 0.2 1 23 . 12 ASP H H 8.33 0.02 1 24 . 12 ASP N N 117.31 0.2 1 25 . 13 TYR H H 8.55 0.02 1 26 . 13 TYR N N 120.3 0.2 1 27 . 14 GLU H H 7.47 0.02 1 28 . 14 GLU N N 127.97 0.2 1 29 . 15 SER H H 8.17 0.02 1 30 . 15 SER N N 117.7 0.2 1 31 . 16 ARG H H 8.82 0.02 1 32 . 16 ARG N N 123.39 0.2 1 33 . 17 THR H H 8 0.02 1 34 . 17 THR N N 113.36 0.2 1 35 . 18 GLU H H 9.01 0.02 1 36 . 18 GLU N N 122.83 0.2 1 37 . 19 THR H H 7.45 0.02 1 38 . 19 THR N N 103.8 0.2 1 39 . 20 ASP H H 7.49 0.02 1 40 . 20 ASP N N 123.52 0.2 1 41 . 21 LEU H H 9.03 0.02 1 42 . 21 LEU N N 125.08 0.2 1 43 . 22 SER H H 7.92 0.02 1 44 . 22 SER N N 117.04 0.2 1 45 . 23 PHE H H 8.58 0.02 1 46 . 23 PHE N N 116.6 0.2 1 47 . 24 LYS H H 8.67 0.02 1 48 . 24 LYS N N 119.64 0.2 1 49 . 25 LYS H H 9.2 0.02 1 50 . 25 LYS N N 120.86 0.2 1 51 . 26 GLY H H 9.07 0.02 1 52 . 26 GLY N N 114.28 0.2 1 53 . 27 GLU H H 8.36 0.02 1 54 . 27 GLU N N 123.58 0.2 1 55 . 28 ARG H H 8.1 0.02 1 56 . 28 ARG N N 121.89 0.2 1 57 . 29 LEU H H 9.2 0.02 1 58 . 29 LEU N N 123.63 0.2 1 59 . 30 GLN H H 9.16 0.02 1 60 . 30 GLN N N 122.31 0.2 1 61 . 31 ILE H H 9.09 0.02 1 62 . 31 ILE N N 126.05 0.2 1 63 . 32 VAL H H 8.8 0.02 1 64 . 32 VAL N N 128.17 0.2 1 65 . 33 ASN H H 7.75 0.02 1 66 . 33 ASN N N 115.27 0.2 1 67 . 34 ASN H H 8.32 0.02 1 68 . 34 ASN N N 123 0.2 1 69 . 35 THR H H 8.02 0.02 1 70 . 35 THR N N 108.37 0.2 1 71 . 36 GLU H H 8.61 0.02 1 72 . 36 GLU N N 121.93 0.2 1 73 . 37 GLY H H 8.12 0.02 1 74 . 37 GLY N N 107.9 0.2 1 75 . 38 ASP H H 8.44 0.02 1 76 . 38 ASP N N 117.69 0.2 1 77 . 39 TRP H H 8.18 0.02 1 78 . 39 TRP N N 121.5 0.2 1 79 . 40 TRP H H 8.74 0.02 1 80 . 40 TRP N N 125.3 0.2 1 81 . 41 LEU H H 8.9 0.02 1 82 . 41 LEU N N 125.54 0.2 1 83 . 42 ALA H H 9.18 0.02 1 84 . 42 ALA N N 131.66 0.2 1 85 . 43 HIS H H 9.18 0.02 1 86 . 43 HIS N N 117.37 0.2 1 87 . 44 SER H H 8.82 0.02 1 88 . 44 SER N N 119.58 0.2 1 89 . 45 LEU H H 8.84 0.02 1 90 . 45 LEU N N 130.04 0.2 1 91 . 46 THR H H 8.37 0.02 1 92 . 46 THR N N 115.19 0.2 1 93 . 47 THR H H 8.27 0.02 1 94 . 47 THR N N 107.78 0.2 1 95 . 48 GLY H H 7.82 0.02 1 96 . 48 GLY N N 110.1 0.2 1 97 . 49 GLN H H 7.45 0.02 1 98 . 49 GLN N N 118.65 0.2 1 99 . 50 THR H H 8.57 0.02 1 100 . 50 THR N N 116.44 0.2 1 101 . 51 GLY H H 9.08 0.02 1 102 . 51 GLY N N 111.96 0.2 1 103 . 52 TYR H H 9.09 0.02 1 104 . 52 TYR N N 119.27 0.2 1 105 . 53 ILE H H 9.59 0.02 1 106 . 53 ILE N N 111.34 0.2 1 107 . 55 SER H H 6.91 0.02 1 108 . 55 SER N N 119.72 0.2 1 109 . 56 ASN H H 8.25 0.02 1 110 . 56 ASN N N 114.65 0.2 1 111 . 57 TYR H H 7.85 0.02 1 112 . 57 TYR N N 119.55 0.2 1 113 . 58 VAL H H 7.06 0.02 1 114 . 58 VAL N N 107.21 0.2 1 115 . 59 ALA H H 8.74 0.02 1 116 . 59 ALA N N 121.39 0.2 1 117 . 61 SER H H 8.28 0.02 1 118 . 61 SER N N 117.25 0.2 1 119 . 62 ASP H H 8.29 0.02 1 120 . 62 ASP N N 120.08 0.2 1 121 . 63 SER H H 7.91 0.02 1 122 . 63 SER N N 114.27 0.2 1 123 . 64 ILE H H 8.05 0.02 1 124 . 64 ILE N N 122.22 0.2 1 125 . 65 GLN H H 8.36 0.02 1 126 . 65 GLN N N 123.1 0.2 1 127 . 66 ALA H H 8.07 0.02 1 128 . 66 ALA N N 124.23 0.2 1 129 . 67 GLU H H 8.17 0.02 1 130 . 67 GLU N N 119.4 0.2 1 131 . 68 GLY H H 8.28 0.02 1 132 . 68 GLY N N 108.17 0.2 1 133 . 69 ILE H H 7.68 0.02 1 134 . 69 ILE N N 119.07 0.2 1 135 . 70 HIS H H 8.46 0.02 1 136 . 70 HIS N N 123.41 0.2 1 137 . 71 ARG H H 8.3 0.02 1 138 . 71 ARG N N 124.05 0.2 1 139 . 72 ASP H H 8.03 0.02 1 140 . 72 ASP N N 127.53 0.2 1 stop_ save_