data_15551 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H and 15N Chemical Shift Assignments for Dok1 PTB domain ; _BMRB_accession_number 15551 _BMRB_flat_file_name bmr15551.str _Entry_type original _Submission_date 2007-11-09 _Accession_date 2007-11-09 _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 Oxley Camilla L. . 2 Vakonakis Ioannis . . 3 Wegener Kate L. . 4 Campbell Iain D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 119 "15N chemical shifts" 113 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-11-08 update author 'Change 89 GLN HE21 110.727 to NE2, 104 GLN HE21 111.331 to NE2' 2012-03-26 update author 'Update chemical shift table and residue in entity' 2009-02-05 update author 'Update chemical shift table and residue in entity' 2008-07-07 update BMRB 'complete entry citation' 2008-01-09 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; An integrin phosphorylation switch: the effect of beta3 integrin tail phosphorylation on DOK1 and talin binding. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18156175 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Oxley Camilla L. . 2 Anthis Nicholas J. . 3 Lowe Edward D. . 4 Vakonakis Ioannis . . 5 Campbell Iain D. . 6 Wegener Kate L. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 283 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5420 _Page_last 5426 _Year 2008 _Details . loop_ _Keyword Dok1 'integrin activation' 'integrin cytoplasmic tail' 'phosphotyrosine binding domains' talin stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Dok1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Dok1 $Dok1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Dok1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Dok1 _Molecular_mass 12087.7 _Mol_thiol_state 'all free' loop_ _Biological_function 'adaptor protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 108 _Mol_residue_sequence ; GPLGSQFWVTVQRTEAAERC GLHGSYVLRVEAERLTLLTV GAQSQILEPLLSWWYTLLRR YGRDKVMFSFEAGRRCPSGP GTFTFQTAQGNDIFQAVETA IHRQKAQG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 149 GLY 2 150 PRO 3 151 LEU 4 152 GLY 5 153 SER 6 154 GLN 7 155 PHE 8 156 TRP 9 157 VAL 10 158 THR 11 159 VAL 12 160 GLN 13 161 ARG 14 162 THR 15 163 GLU 16 164 ALA 17 165 ALA 18 166 GLU 19 167 ARG 20 168 CYS 21 169 GLY 22 170 LEU 23 171 HIS 24 172 GLY 25 173 SER 26 174 TYR 27 175 VAL 28 176 LEU 29 177 ARG 30 178 VAL 31 179 GLU 32 180 ALA 33 181 GLU 34 182 ARG 35 183 LEU 36 184 THR 37 185 LEU 38 186 LEU 39 187 THR 40 188 VAL 41 189 GLY 42 190 ALA 43 191 GLN 44 192 SER 45 193 GLN 46 194 ILE 47 195 LEU 48 196 GLU 49 197 PRO 50 198 LEU 51 199 LEU 52 200 SER 53 201 TRP 54 202 TRP 55 203 TYR 56 204 THR 57 205 LEU 58 206 LEU 59 207 ARG 60 208 ARG 61 209 TYR 62 210 GLY 63 211 ARG 64 212 ASP 65 213 LYS 66 214 VAL 67 215 MET 68 216 PHE 69 217 SER 70 218 PHE 71 219 GLU 72 220 ALA 73 221 GLY 74 222 ARG 75 223 ARG 76 224 CYS 77 225 PRO 78 226 SER 79 227 GLY 80 228 PRO 81 229 GLY 82 230 THR 83 231 PHE 84 232 THR 85 233 PHE 86 234 GLN 87 235 THR 88 236 ALA 89 237 GLN 90 238 GLY 91 239 ASN 92 240 ASP 93 241 ILE 94 242 PHE 95 243 GLN 96 244 ALA 97 245 VAL 98 246 GLU 99 247 THR 100 248 ALA 101 249 ILE 102 250 HIS 103 251 ARG 104 252 GLN 105 253 LYS 106 254 ALA 107 255 GLN 108 256 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 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 BMRB 19672 Dok1_PTB_domain 93.52 101 99.01 99.01 5.25e-65 PDB 2V76 "Crystal Structure Of The Human Dok1 Ptb Domain" 99.07 107 99.07 99.07 8.16e-70 DBJ BAD96603 "docking protein 1 variant [Homo sapiens]" 97.22 481 99.05 99.05 1.14e-64 DBJ BAG51595 "unnamed protein product [Homo sapiens]" 97.22 481 99.05 99.05 1.02e-64 DBJ BAG58893 "unnamed protein product [Homo sapiens]" 97.22 470 99.05 99.05 4.56e-65 DBJ BAJ17765 "docking protein 1, 62kDa [synthetic construct]" 97.22 481 99.05 99.05 9.38e-65 GB AAB88182 "similar to GAP binding protein p62do [Homo sapiens]" 97.22 509 99.05 99.05 1.24e-64 GB AAC51127 "GAP binding protein p62dok [Homo sapiens]" 97.22 481 99.05 99.05 9.38e-65 GB AAI14441 "Docking protein 1, 62kDa (downstream of tyrosine kinase 1) [Homo sapiens]" 97.22 481 99.05 99.05 9.38e-65 GB AAX93224 "unknown [Homo sapiens]" 97.22 481 99.05 99.05 9.38e-65 GB AIC48651 "DOK1, partial [synthetic construct]" 97.22 481 99.05 99.05 9.38e-65 REF NP_001184189 "docking protein 1 isoform 2 [Homo sapiens]" 97.22 342 99.05 99.05 1.90e-66 REF NP_001372 "docking protein 1 isoform 1 [Homo sapiens]" 97.22 481 99.05 99.05 9.38e-65 REF XP_001111248 "PREDICTED: docking protein 1 isoform 2 [Macaca mulatta]" 97.22 475 97.14 98.10 7.67e-64 REF XP_001161802 "PREDICTED: docking protein 1 isoform X1 [Pan troglodytes]" 97.22 481 99.05 99.05 9.99e-65 REF XP_002757635 "PREDICTED: docking protein 1 isoform X1 [Callithrix jacchus]" 97.22 478 97.14 98.10 1.14e-63 SP Q99704 "RecName: Full=Docking protein 1; AltName: Full=Downstream of tyrosine kinase 1; AltName: Full=p62(dok); AltName: Full=pp62" 97.22 481 99.05 99.05 9.38e-65 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Dok1 Human 9606 Eukaryota Metazoa Homo sapiens 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 $Dok1 'recombinant technology' . Escherichia coli . 'pGEX 6P2' 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 $Dok1 1 mM '[U-100% 13C; U-100% 15N]' PBS 50 mM . NaCl 100 mM 'natural abundance' DTT 10 mM 'natural abundance' D2O 5 % . Azide 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer 'Home build' _Model 'Home build' _Field_strength 600 _Details 'Home build consoles controlled by GE/Bruker Omega software & computers' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 6.1 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Dok1 _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 1 151 3 LEU H H 8.492 . 1 2 151 3 LEU N N 121.589 . 1 3 152 4 GLY H H 8.042 . 1 4 152 4 GLY N N 108.377 . 1 5 153 5 SER H H 8.072 . 1 6 153 5 SER N N 115.642 . 1 7 154 6 GLN H H 7.835 . 1 8 154 6 GLN HE21 H 7.37 . 2 9 154 6 GLN HE22 H 6.712 . 2 10 154 6 GLN N N 119.418 . 1 11 154 6 GLN NE2 N 110.345 . 1 12 155 7 PHE H H 8.692 . 1 13 155 7 PHE N N 119.875 . 1 14 156 8 TRP H H 9.483 . 1 15 156 8 TRP HE1 H 10.025 . 1 16 156 8 TRP N N 126.666 . 1 17 156 8 TRP NE1 N 128.149 . 1 18 157 9 VAL H H 9.333 . 1 19 157 9 VAL N N 118.931 . 1 20 158 10 THR H H 8.037 . 1 21 158 10 THR N N 115.313 . 1 22 159 11 VAL H H 9.027 . 1 23 159 11 VAL N N 128.198 . 1 24 160 12 GLN H H 8.459 . 1 25 160 12 GLN HE21 H 7.194 . 2 26 160 12 GLN HE22 H 6.816 . 2 27 160 12 GLN N N 128.255 . 1 28 160 12 GLN NE2 N 111.436 . 1 29 161 13 ARG H H 8.644 . 1 30 161 13 ARG N N 124.998 . 1 31 162 14 THR H H 7.089 . 1 32 162 14 THR N N 115.721 . 1 33 163 15 GLU H H 9.139 . 1 34 163 15 GLU N N 122.806 . 1 35 164 16 ALA H H 8.336 . 1 36 164 16 ALA N N 120.99 . 1 37 165 17 ALA H H 7.079 . 1 38 165 17 ALA N N 119.335 . 1 39 166 18 GLU H H 8.189 . 1 40 166 18 GLU N N 117.389 . 1 41 167 19 ARG H H 8.34 . 1 42 167 19 ARG N N 122.587 . 1 43 168 20 CYS H H 7.664 . 1 44 168 20 CYS N N 113.427 . 1 45 169 21 GLY H H 7.887 . 1 46 169 21 GLY N N 109.315 . 1 47 170 22 LEU H H 8.276 . 1 48 170 22 LEU N N 118.091 . 1 49 171 23 HIS H H 8.912 . 1 50 171 23 HIS N N 119.97 . 1 51 172 24 GLY H H 9.33 . 1 52 172 24 GLY N N 113.477 . 1 53 173 25 SER H H 8.189 . 1 54 173 25 SER N N 117.002 . 1 55 174 26 TYR H H 8.979 . 1 56 174 26 TYR N N 120.459 . 1 57 175 27 VAL H H 8.282 . 1 58 175 27 VAL N N 118.409 . 1 59 176 28 LEU H H 9.418 . 1 60 176 28 LEU N N 129.254 . 1 61 177 29 ARG H H 9.841 . 1 62 177 29 ARG N N 128.619 . 1 63 178 30 VAL H H 8.926 . 1 64 178 30 VAL N N 128.836 . 1 65 179 31 GLU H H 8.215 . 1 66 179 31 GLU N N 125.568 . 1 67 180 32 ALA H H 8.725 . 1 68 180 32 ALA N N 121.807 . 1 69 181 33 GLU H H 8.377 . 1 70 181 33 GLU N N 108.665 . 1 71 182 34 ARG H H 6.683 . 1 72 182 34 ARG N N 116.878 . 1 73 183 35 LEU H H 7.655 . 1 74 183 35 LEU N N 117.403 . 1 75 184 36 THR H H 9.142 . 1 76 184 36 THR N N 119.716 . 1 77 185 37 LEU H H 9.352 . 1 78 185 37 LEU N N 129.724 . 1 79 186 38 LEU H H 9.996 . 1 80 186 38 LEU N N 127.095 . 1 81 187 39 THR H H 8.689 . 1 82 187 39 THR N N 113.589 . 1 83 188 40 VAL H H 8.103 . 1 84 188 40 VAL N N 122.067 . 1 85 189 41 GLY H H 8.842 . 1 86 189 41 GLY N N 115.287 . 1 87 190 42 ALA H H 8.731 . 1 88 190 42 ALA N N 125.713 . 1 89 191 43 GLN H H 8.368 . 1 90 191 43 GLN HE21 H 7.565 . 2 91 191 43 GLN HE22 H 6.882 . 2 92 191 43 GLN N N 114.847 . 1 93 191 43 GLN NE2 N 112.453 . 1 94 192 44 SER H H 8.271 . 1 95 192 44 SER N N 113.997 . 1 96 193 45 GLN H H 8.384 . 1 97 193 45 GLN HE21 H 7.488 . 2 98 193 45 GLN HE22 H 6.874 . 2 99 193 45 GLN N N 117.051 . 1 100 193 45 GLN NE2 N 112.875 . 1 101 194 46 ILE H H 8.01 . 1 102 194 46 ILE N N 119.181 . 1 103 195 47 LEU H H 8.396 . 1 104 195 47 LEU N N 125.735 . 1 105 198 50 LEU H H 9.334 . 1 106 198 50 LEU N N 125.335 . 1 107 199 51 LEU H H 7.17 . 1 108 199 51 LEU N N 117.312 . 1 109 200 52 SER H H 7.48 . 1 110 200 52 SER N N 112.636 . 1 111 201 53 TRP H H 9.496 . 1 112 201 53 TRP HE1 H 9.28 . 1 113 201 53 TRP N N 123.482 . 1 114 201 53 TRP NE1 N 127.434 . 1 115 203 55 TYR H H 7.508 . 1 116 203 55 TYR N N 123.79 . 1 117 204 56 THR H H 8.04 . 1 118 204 56 THR N N 106.758 . 1 119 205 57 LEU H H 7.558 . 1 120 205 57 LEU N N 118.458 . 1 121 206 58 LEU H H 7.503 . 1 122 206 58 LEU N N 119.642 . 1 123 207 59 ARG H H 9.093 . 1 124 207 59 ARG N N 121.191 . 1 125 208 60 ARG H H 7.541 . 1 126 208 60 ARG N N 111.778 . 1 127 209 61 TYR H H 7.843 . 1 128 209 61 TYR N N 115.834 . 1 129 210 62 GLY H H 8.972 . 1 130 210 62 GLY N N 107.087 . 1 131 211 63 ARG H H 8.239 . 1 132 211 63 ARG N N 115.563 . 1 133 212 64 ASP H H 8.883 . 1 134 212 64 ASP N N 122.647 . 1 135 213 65 LYS H H 8.143 . 1 136 213 65 LYS N N 115.247 . 1 137 214 66 VAL H H 8.929 . 1 138 214 66 VAL N N 112.24 . 1 139 215 67 MET H H 8.381 . 1 140 215 67 MET N N 120.814 . 1 141 216 68 PHE H H 8.848 . 1 142 216 68 PHE N N 118.786 . 1 143 217 69 SER H H 8.316 . 1 144 217 69 SER N N 121.782 . 1 145 218 70 PHE H H 8.624 . 1 146 218 70 PHE N N 118.008 . 1 147 219 71 GLU H H 8.478 . 1 148 219 71 GLU N N 119.192 . 1 149 220 72 ALA H H 9.743 . 1 150 220 72 ALA N N 131.141 . 1 151 221 73 GLY H H 8.365 . 1 152 221 73 GLY N N 109.35 . 1 153 222 74 ARG H H 8.959 . 1 154 222 74 ARG N N 117.108 . 1 155 223 75 ARG H H 8.576 . 1 156 223 75 ARG N N 115.506 . 1 157 224 76 CYS H H 7.603 . 1 158 224 76 CYS N N 118.443 . 1 159 226 78 SER H H 8.148 . 1 160 226 78 SER N N 108.978 . 1 161 227 79 GLY H H 8.123 . 1 162 227 79 GLY N N 111.488 . 1 163 229 81 GLY H H 7.988 . 1 164 229 81 GLY N N 104.962 . 1 165 230 82 THR H H 8.064 . 1 166 230 82 THR N N 116.463 . 1 167 231 83 PHE H H 8.811 . 1 168 231 83 PHE N N 128.195 . 1 169 232 84 THR H H 9.423 . 1 170 232 84 THR N N 120.304 . 1 171 233 85 PHE H H 9.375 . 1 172 233 85 PHE N N 123.584 . 1 173 234 86 GLN H H 9.747 . 1 174 234 86 GLN HE21 H 8.18 . 2 175 234 86 GLN HE22 H 7.388 . 2 176 234 86 GLN N N 123.979 . 1 177 234 86 GLN NE2 N 113.915 . 1 178 235 87 THR H H 8.419 . 1 179 235 87 THR N N 122.015 . 1 180 236 88 ALA H H 9.092 . 1 181 236 88 ALA N N 129.832 . 1 182 237 89 GLN H H 9.529 . 1 183 237 89 GLN NE2 N 110.727 . 1 184 237 89 GLN N N 120.86 . 1 185 238 90 GLY H H 9.169 . 1 186 238 90 GLY N N 111.664 . 1 187 239 91 ASN H H 9.109 . 1 188 239 91 ASN HD21 H 7.885 . 2 189 239 91 ASN HD22 H 7.01 . 2 190 239 91 ASN N N 118.781 . 1 191 239 91 ASN ND2 N 114.618 . 1 192 240 92 ASP H H 7.667 . 1 193 240 92 ASP N N 120.615 . 1 194 241 93 ILE H H 7.804 . 1 195 241 93 ILE N N 121.036 . 1 196 242 94 PHE H H 8.307 . 1 197 242 94 PHE N N 118.669 . 1 198 243 95 GLN H H 8.492 . 1 199 243 95 GLN HE21 H 7.41 . 2 200 243 95 GLN HE22 H 6.991 . 2 201 243 95 GLN N N 116.219 . 1 202 243 95 GLN NE2 N 111.951 . 1 203 244 96 ALA H H 7.891 . 1 204 244 96 ALA N N 123.735 . 1 205 245 97 VAL H H 8.368 . 1 206 245 97 VAL N N 122.577 . 1 207 246 98 GLU H H 8.341 . 1 208 246 98 GLU N N 118.601 . 1 209 247 99 THR H H 8.166 . 1 210 247 99 THR N N 115.438 . 1 211 248 100 ALA H H 7.705 . 1 212 248 100 ALA N N 125.015 . 1 213 249 101 ILE H H 8.387 . 1 214 249 101 ILE N N 119.585 . 1 215 250 102 HIS H H 8.114 . 1 216 250 102 HIS N N 117.697 . 1 217 251 103 ARG H H 7.935 . 1 218 251 103 ARG N N 119.149 . 1 219 252 104 GLN H H 7.956 . 1 220 252 104 GLN NE2 N 111.331 . 2 221 252 104 GLN N N 119.746 . 1 222 253 105 LYS H H 8.114 . 1 223 253 105 LYS N N 120.42 . 1 224 254 106 ALA H H 8.07 . 1 225 254 106 ALA N N 123.897 . 1 226 255 107 GLN H H 8.165 . 1 227 255 107 GLN HE21 H 7.575 . 2 228 255 107 GLN HE22 H 6.867 . 2 229 255 107 GLN N N 118.96 . 1 230 255 107 GLN NE2 N 112.597 . 1 231 256 108 GLY H H 7.972 . 1 232 256 108 GLY N N 116.028 . 1 stop_ save_