data_26625 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; PH domain of the Arf GAP ASAP1 ; _BMRB_accession_number 26625 _BMRB_flat_file_name bmr26625.str _Entry_type original _Submission_date 2015-08-06 _Accession_date 2015-08-06 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone N and HN assignments for PH domain used in ligand titration experiments' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Li Yifei . . 2 Byrd Andrew . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 99 "13C chemical shifts" 1 "15N chemical shifts" 97 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-07-11 update BMRB 'update entry citation' 2015-09-29 original author 'original release' stop_ _Original_release_date 2015-09-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Molecular Basis for Cooperative Binding of Anionic Phospholipids to the PH Domain of the Arf GAP ASAP1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26365802 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jian Xiaoying . . 2 Tang Wai-Kwan . . 3 Zhai Peng . . 4 Roy Neeladri Sekhar . 5 Luo Ruibai . . 6 Gruschus James M. . 7 Yohe Marielle E. . 8 Chen Pei-Wen . . 9 Li Yifei . . 10 Byrd Andrew . . 11 Xia Di . . 12 Randazzo Paul A. . stop_ _Journal_abbreviation Structure _Journal_volume 23 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1977 _Page_last 1988 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'ASAP1 PH domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ASAP1 PH domain' $ASAP1_PH_domain stop_ _System_molecular_weight 12698.5 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ASAP1_PH_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ASAP1_PH_domain _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 111 _Mol_residue_sequence ; EKKGFLLKKSDGIRKVWQRR KCAVKNGILTISHATSNRQP AKLNLLTCQVKPNAEDKKSF DLISHNRTYHFQAEDEQDYI AWISVLTNSKEEALTMAFRG EQSTGENSLED ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 341 GLU 2 342 LYS 3 343 LYS 4 344 GLY 5 345 PHE 6 346 LEU 7 347 LEU 8 348 LYS 9 349 LYS 10 350 SER 11 351 ASP 12 352 GLY 13 353 ILE 14 354 ARG 15 355 LYS 16 356 VAL 17 357 TRP 18 358 GLN 19 359 ARG 20 360 ARG 21 361 LYS 22 362 CYS 23 363 ALA 24 364 VAL 25 365 LYS 26 366 ASN 27 367 GLY 28 368 ILE 29 369 LEU 30 370 THR 31 371 ILE 32 372 SER 33 373 HIS 34 374 ALA 35 375 THR 36 376 SER 37 377 ASN 38 378 ARG 39 379 GLN 40 380 PRO 41 381 ALA 42 382 LYS 43 383 LEU 44 384 ASN 45 385 LEU 46 386 LEU 47 387 THR 48 388 CYS 49 389 GLN 50 390 VAL 51 391 LYS 52 392 PRO 53 393 ASN 54 394 ALA 55 395 GLU 56 396 ASP 57 397 LYS 58 398 LYS 59 399 SER 60 400 PHE 61 401 ASP 62 402 LEU 63 403 ILE 64 404 SER 65 405 HIS 66 406 ASN 67 407 ARG 68 408 THR 69 409 TYR 70 410 HIS 71 411 PHE 72 412 GLN 73 413 ALA 74 414 GLU 75 415 ASP 76 416 GLU 77 417 GLN 78 418 ASP 79 419 TYR 80 420 ILE 81 421 ALA 82 422 TRP 83 423 ILE 84 424 SER 85 425 VAL 86 426 LEU 87 427 THR 88 428 ASN 89 429 SER 90 430 LYS 91 431 GLU 92 432 GLU 93 433 ALA 94 434 LEU 95 435 THR 96 436 MET 97 437 ALA 98 438 PHE 99 439 ARG 100 440 GLY 101 441 GLU 102 442 GLN 103 443 SER 104 444 THR 105 445 GLY 106 446 GLU 107 447 ASN 108 448 SER 109 449 LEU 110 450 GLU 111 451 ASP 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 _Details $ASAP1_PH_domain human 9606 Eukaryota Metazoa Homo sapiens 'cloned into E. coli' 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 $ASAP1_PH_domain 'recombinant technology' . Escherichia coli . pET19B 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 $ASAP1_PH_domain 250 uM '[U-99% 13C; U-99% 15N]' H2O 90 % 'natural abundance' D2O 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_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _Details . 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_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '20 mM Tris buffer' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 150 . mM pH 7.4 . 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 na 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' '3D HNCACB' '3D CBCA(CO)NH' 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 'ASAP1 PH domain' _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 1 341 1 GLU H H 8.2840 . 1 2 341 1 GLU N N 122.7000 . 1 3 342 2 LYS H H 7.8291 . 1 4 342 2 LYS N N 120.8000 . 1 5 343 3 LYS H H 8.4700 . 1 6 343 3 LYS N N 125.0000 . 1 7 344 4 GLY H H 8.9282 . 1 8 344 4 GLY N N 110.9000 . 1 9 345 5 PHE H H 9.3330 . 1 10 346 6 LEU H H 8.8331 . 1 11 346 6 LEU N N 120.6000 . 1 12 347 7 LEU H H 8.5645 . 1 13 347 7 LEU N N 118.8000 . 1 14 348 8 LYS H H 9.5101 . 1 15 348 8 LYS N N 123.4000 . 1 16 350 10 SER H H 8.9130 . 1 17 350 10 SER N N 123.8000 . 1 18 352 12 GLY H H 7.9000 . 1 19 352 12 GLY N N 108.0000 . 1 20 353 13 ILE H H 8.4255 . 1 21 353 13 ILE CA C 63.3700 . 1 22 354 14 ARG H H 8.015 . 1 23 354 14 ARG N N 120.354 . 1 24 355 15 LYS H H 8.9098 . 1 25 355 15 LYS N N 124.0799 . 1 26 356 16 VAL H H 8.0090 . 1 27 356 16 VAL N N 117.8000 . 1 28 357 17 TRP H H 8.6461 . 1 29 357 17 TRP N N 123.9000 . 1 30 358 18 GLN H H 8.6904 . 1 31 358 18 GLN N N 121.8000 . 1 32 359 19 ARG H H 9.0760 . 1 33 359 19 ARG N N 126.2000 . 1 34 360 20 ARG H H 9.5617 . 1 35 360 20 ARG N N 126.8000 . 1 36 361 21 LYS H H 8.8436 . 1 37 361 21 LYS N N 124.5486 . 1 38 362 22 CYS H H 8.8436 . 1 39 362 22 CYS N N 124.6000 . 1 40 363 23 ALA H H 8.6921 . 1 41 363 23 ALA N N 123.1000 . 1 42 364 24 VAL H H 9.2754 . 1 43 364 24 VAL N N 121.7362 . 1 44 365 25 LYS H H 8.3026 . 1 45 365 25 LYS N N 125.9548 . 1 46 366 26 ASN H H 7.7775 . 1 47 366 26 ASN N N 120.3299 . 1 48 367 27 GLY H H 8.4230 . 1 49 367 27 GLY N N 102.1000 . 1 50 368 28 ILE H H 7.7780 . 1 51 368 28 ILE N N 120.5000 . 1 52 369 29 LEU H H 9.0210 . 1 53 369 29 LEU N N 130.4000 . 1 54 370 30 THR H H 9.7350 . 1 55 370 30 THR N N 123.6000 . 1 56 371 31 ILE H H 9.0710 . 1 57 371 31 ILE N N 126.7000 . 1 58 372 32 SER H H 8.9260 . 1 59 372 32 SER N N 123.5000 . 1 60 373 33 HIS H H 8.9800 . 1 61 373 33 HIS N N 122.8860 . 1 62 378 38 ARG H H 7.6752 . 1 63 378 38 ARG N N 118.4510 . 1 64 381 41 ALA H H 8.2554 . 1 65 381 41 ALA N N 123.7000 . 1 66 382 42 LYS H H 8.3646 . 1 67 382 42 LYS N N 120.1000 . 1 68 383 43 LEU H H 9.3384 . 1 69 383 43 LEU N N 125.0000 . 1 70 384 44 ASN H H 8.9200 . 1 71 384 44 ASN N N 122.3000 . 1 72 385 45 LEU H H 8.9055 . 1 73 385 45 LEU N N 127.4000 . 1 74 386 46 LEU H H 8.4490 . 1 75 386 46 LEU N N 118.1000 . 1 76 387 47 THR H H 7.5401 . 1 77 387 47 THR N N 104.8000 . 1 78 388 48 CYS H H 7.3839 . 1 79 388 48 CYS N N 117.8000 . 1 80 389 49 GLN H H 8.8420 . 1 81 389 49 GLN N N 120.3000 . 1 82 390 50 VAL H H 8.9206 . 1 83 390 50 VAL N N 125.1000 . 1 84 391 51 LYS H H 9.3730 . 1 85 391 51 LYS N N 128.7000 . 1 86 393 53 ASN H H 8.4100 . 1 87 393 53 ASN N N 122.8000 . 1 88 394 54 ALA H H 8.7221 . 1 89 394 54 ALA N N 126.4000 . 1 90 395 55 GLU H H 8.4536 . 1 91 395 55 GLU N N 116.8000 . 1 92 396 56 ASP H H 7.7629 . 1 93 396 56 ASP N N 117.8000 . 1 94 397 57 LYS H H 8.1460 . 1 95 397 57 LYS N N 119.2000 . 1 96 398 58 LYS H H 8.0580 . 1 97 398 58 LYS N N 113.9000 . 1 98 399 59 SER H H 8.4100 . 1 99 399 59 SER N N 116.9000 . 1 100 400 60 PHE H H 8.6372 . 1 101 400 60 PHE N N 118.0000 . 1 102 401 61 ASP H H 9.0133 . 1 103 401 61 ASP N N 120.7000 . 1 104 402 62 LEU H H 9.2732 . 1 105 402 62 LEU N N 121.9000 . 1 106 403 63 ILE H H 9.2017 . 1 107 403 63 ILE N N 125.6000 . 1 108 404 64 SER H H 8.9796 . 1 109 404 64 SER N N 124.0000 . 1 110 407 67 ARG H H 7.7111 . 1 111 407 67 ARG N N 119.5000 . 1 112 408 68 THR H H 8.2720 . 1 113 408 68 THR N N 118.7000 . 1 114 409 69 TYR H H 9.2045 . 1 115 409 69 TYR N N 127.0000 . 1 116 410 70 HIS H H 8.7110 . 1 117 410 70 HIS N N 122.6000 . 1 118 411 71 PHE H H 8.8035 . 1 119 411 71 PHE N N 120.9000 . 1 120 412 72 GLN H H 9.1113 . 1 121 412 72 GLN N N 119.6000 . 1 122 413 73 ALA H H 8.9173 . 1 123 413 73 ALA N N 127.1000 . 1 124 414 74 GLU H H 9.9643 . 1 125 414 74 GLU N N 118.1000 . 1 126 415 75 ASP H H 7.5972 . 1 127 415 75 ASP N N 111.3000 . 1 128 416 76 GLU H H 9.1100 . 1 129 416 76 GLU N N 120.0000 . 1 130 417 77 GLN H H 8.4545 . 1 131 417 77 GLN N N 119.8000 . 1 132 418 78 ASP H H 9.1270 . 1 133 418 78 ASP N N 122.7000 . 1 134 419 79 TYR H H 8.2835 . 1 135 419 79 TYR N N 120.1000 . 1 136 420 80 ILE H H 7.7837 . 9 137 420 80 ILE N N 118.4000 . 9 138 421 81 ALA H H 7.7467 . 1 139 421 81 ALA N N 122.5000 . 1 140 422 82 TRP H H 8.7510 . 1 141 422 82 TRP N N 118.8000 . 1 142 423 83 ILE H H 8.3350 . 1 143 423 83 ILE N N 117.8000 . 1 144 424 84 SER H H 8.0174 . 1 145 424 84 SER N N 116.5000 . 1 146 425 85 VAL H H 7.9547 . 9 147 425 85 VAL N N 120.5000 . 9 148 426 86 LEU H H 8.5642 . 1 149 426 86 LEU N N 121.6000 . 1 150 427 87 THR H H 7.8700 . 1 151 427 87 THR N N 112.7000 . 1 152 428 88 ASN H H 8.4300 . 1 153 428 88 ASN N N 121.2000 . 1 154 429 89 SER H H 8.6430 . 1 155 429 89 SER N N 115.5000 . 1 156 430 90 LYS H H 7.7448 . 1 157 430 90 LYS N N 119.7000 . 1 158 431 91 GLU H H 7.7880 . 9 159 431 91 GLU N N 118.5000 . 9 160 432 92 GLU H H 8.4240 . 1 161 432 92 GLU N N 120.6000 . 1 162 433 93 ALA H H 8.2220 . 1 163 433 93 ALA N N 122.6000 . 1 164 434 94 LEU H H 8.1114 . 1 165 434 94 LEU N N 119.8000 . 1 166 435 95 THR H H 7.9433 . 1 167 435 95 THR N N 112.9000 . 1 168 436 96 MET H H 7.9487 . 9 169 436 96 MET N N 120.5000 . 9 170 437 97 ALA H H 8.0190 . 1 171 437 97 ALA N N 123.1000 . 1 172 438 98 PHE H H 8.0770 . 1 173 438 98 PHE N N 118.5000 . 1 174 439 99 ARG H H 8.0906 . 1 175 439 99 ARG N N 121.6000 . 1 176 440 100 GLY H H 7.9159 . 1 177 440 100 GLY N N 108.7000 . 1 178 441 101 GLU H H 8.3087 . 1 179 441 101 GLU N N 120.6000 . 1 180 442 102 GLN H H 8.4650 . 1 181 442 102 GLN N N 121.1000 . 1 182 444 104 THR H H 8.3060 . 1 183 444 104 THR N N 115.3000 . 1 184 445 105 GLY H H 8.4130 . 1 185 445 105 GLY N N 110.8000 . 1 186 446 106 GLU H H 8.3510 . 1 187 446 106 GLU N N 120.6000 . 1 188 447 107 ASN H H 8.5643 . 1 189 447 107 ASN N N 118.9237 . 1 190 448 108 SER H H 8.3360 . 1 191 448 108 SER N N 116.5000 . 1 192 449 109 LEU H H 8.3154 . 1 193 449 109 LEU N N 123.8000 . 1 194 450 110 GLU H H 8.3230 . 1 195 450 110 GLU N N 121.5000 . 1 196 451 111 ASP H H 7.9704 . 1 197 451 111 ASP N N 126.9000 . 1 stop_ save_