data_25309 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; FBP28 WW2 , mutation Y438R ; _BMRB_accession_number 25309 _BMRB_flat_file_name bmr25309.str _Entry_type original _Submission_date 2014-11-03 _Accession_date 2014-11-03 _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 Macias Maria J. . 2 Scheraga Harold . . 3 Sunol David . . 4 Todorovski Toni . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 194 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-08-25 update BMRB 'update entry citation' 2014-11-24 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 25310 'FBP28 WW2 mutant W457F' 25311 'FBP28 WW2 mutant Y446L' 25313 'FBP28 WW2 mutant Y438R DNDC' 25314 'FBP28 WW2 mutant Y238R L453A DNDC' 25315 'FBP28 WW2 mutant Y438R DN' stop_ _Original_release_date 2015-08-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Folding kinetics of WW domains with the united residue force field for bridging microscopic motions and experimental measurements ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25489078 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhou Rui . . 2 Maisuradze Gia G. . 3 Sunol David . . 4 Todorovski Toni . . 5 Macias Maria J. . 6 Xiao Yi . . 7 Scheraga Harold . . 8 Czaplewski Cezary . . 9 Liwo Adam . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 111 _Journal_issue 51 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 18243 _Page_last 18248 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'FBP28 WW2 , mutation Y438R' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $entity 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_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 4058.463 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 37 _Mol_residue_sequence ; GATAVSEWTERKTADGKTYY YNNRTLESTWEKPQELK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 . GLY 2 . ALA 3 . THR 4 . ALA 5 432 VAL 6 433 SER 7 434 GLU 8 435 TRP 9 436 THR 10 437 GLU 11 438 ARG 12 439 LYS 13 440 THR 14 441 ALA 15 442 ASP 16 443 GLY 17 444 LYS 18 445 THR 19 446 TYR 20 447 TYR 21 448 TYR 22 449 ASN 23 450 ASN 24 451 ARG 25 452 THR 26 453 LEU 27 454 GLU 28 455 SER 29 456 THR 30 457 TRP 31 458 GLU 32 459 LYS 33 460 PRO 34 461 GLN 35 462 GLU 36 463 LEU 37 464 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 11007 FBP28WW2 100.00 37 97.30 97.30 1.75e-15 BMRB 11008 FBP28WW2 100.00 37 97.30 97.30 1.75e-15 BMRB 15453 FBP28WW2 100.00 37 97.30 97.30 1.75e-15 BMRB 25313 entity 75.68 28 100.00 100.00 4.86e-10 BMRB 25315 entity 86.49 32 100.00 100.00 6.19e-13 BMRB 4714 "Formin binding WW domain" 100.00 40 97.30 97.30 1.43e-15 PDB 1E0L "Fbp28ww Domain From Mus Musculus" 100.00 37 97.30 97.30 1.75e-15 PDB 2JUP "Fbp28ww2 Domain In Complex With The Pplipppp Peptide" 100.00 37 97.30 97.30 1.75e-15 PDB 2MW9 "Nmr Structure Of Fbp28 Ww2 Y438r Mutant" 100.00 37 100.00 100.00 1.22e-16 PDB 2MWD "Nmr Structure Of Fbp28 Ww2 Mutant Y438r Dndc" 75.68 28 100.00 100.00 4.86e-10 PDB 2MWF "Nmr Structure Of Fbp28 Ww2 Mutant Y438r Dn" 83.78 32 100.00 100.00 2.97e-12 PDB 2RLY "Fbp28ww2 Domain In Complex With Ptppplpp Peptide" 100.00 37 97.30 97.30 1.75e-15 PDB 2RM0 "Fbp28ww2 Domain In Complex With A Ppplipppp Peptide" 100.00 37 97.30 97.30 1.75e-15 GB EGW05321 "Transcription elongation regulator 1 [Cricetulus griseus]" 100.00 414 97.30 97.30 7.10e-15 GB EHB12574 "Transcription elongation regulator 1-like protein [Heterocephalus glaber]" 100.00 967 97.30 97.30 1.80e-14 GB ELW66441 "Transcription elongation regulator 1, partial [Tupaia chinensis]" 100.00 1001 97.30 97.30 1.36e-14 GB EQB78163 "transcription elongation regulator 1 isoform 1 [Camelus ferus]" 100.00 797 97.30 97.30 1.95e-14 GB KFQ71484 "Transcription elongation regulator 1, partial [Phaethon lepturus]" 100.00 686 97.30 97.30 2.24e-14 REF XP_004697122 "PREDICTED: transcription elongation regulator 1 [Echinops telfairi]" 100.00 1004 97.30 97.30 1.67e-14 REF XP_006977759 "PREDICTED: transcription elongation regulator 1 [Peromyscus maniculatus bairdii]" 100.00 1057 97.30 97.30 1.29e-14 REF XP_007653449 "PREDICTED: uncharacterized protein LOC100076344 [Ornithorhynchus anatinus]" 100.00 774 97.30 97.30 1.49e-14 REF XP_008253407 "PREDICTED: transcription elongation regulator 1 isoform X9 [Oryctolagus cuniculus]" 100.00 770 97.30 97.30 2.51e-14 REF XP_008926141 "PREDICTED: transcription elongation regulator 1 [Manacus vitellinus]" 100.00 814 97.30 97.30 1.86e-14 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity 'house mouse' 10090 Eukaryota Metazoa Mus musculus 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 $entity 'recombinant technology' . Escherichia coli . pGAT2 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 $entity 0.7 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' 'sodium azide' 1 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Vendor _Address _Electronic_address 'Bartels et al.' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version . loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ 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 Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _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 pH 6.5 . pH pressure 1 . atm temperature 285 . 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 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_ _Software_label $XEASY stop_ loop_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H NOESY' 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 entity _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 1 432 5 VAL H H 8.046 0.000 . 2 432 5 VAL HA H 3.904 0.003 . 3 432 5 VAL HB H 1.851 0.004 . 4 432 5 VAL HG1 H 0.728 0.000 . 5 432 5 VAL HG2 H 0.728 0.000 . 6 433 6 SER H H 8.240 0.000 . 7 433 6 SER HA H 4.287 0.000 . 8 433 6 SER HB2 H 3.798 0.000 . 9 433 6 SER HB3 H 3.691 0.000 . 10 434 7 GLU H H 8.659 0.000 . 11 434 7 GLU HA H 4.008 0.000 . 12 434 7 GLU HB2 H 1.710 0.000 . 13 434 7 GLU HB3 H 1.619 0.000 . 14 434 7 GLU HG2 H 1.861 0.004 . 15 434 7 GLU HG3 H 1.803 0.000 . 16 435 8 TRP H H 8.112 0.001 . 17 435 8 TRP HA H 5.073 0.000 . 18 435 8 TRP HB2 H 2.917 0.000 . 19 435 8 TRP HB3 H 2.716 0.000 . 20 435 8 TRP HD1 H 6.988 0.001 . 21 435 8 TRP HE1 H 10.057 0.000 . 22 435 8 TRP HE3 H 7.103 0.000 . 23 435 8 TRP HZ2 H 7.300 0.000 . 24 435 8 TRP HZ3 H 6.701 0.000 . 25 435 8 TRP HH2 H 6.839 0.000 . 26 436 9 THR H H 9.310 0.000 . 27 436 9 THR HA H 4.543 0.000 . 28 436 9 THR HB H 3.889 0.000 . 29 436 9 THR HG2 H 1.093 0.000 . 30 437 10 GLU H H 8.558 0.000 . 31 437 10 GLU HA H 4.160 0.000 . 32 437 10 GLU HB2 H 1.708 0.000 . 33 437 10 GLU HG2 H 1.758 0.000 . 34 438 11 ARG H H 8.486 0.003 . 35 438 11 ARG HA H 4.165 0.000 . 36 438 11 ARG HB2 H 1.054 0.004 . 37 438 11 ARG HB3 H 0.947 0.004 . 38 438 11 ARG HG2 H -0.276 0.000 . 39 438 11 ARG HD2 H 2.588 0.000 . 40 438 11 ARG HD3 H 2.416 0.000 . 41 438 11 ARG HE H 7.831 0.000 . 42 439 12 LYS H H 7.957 0.396 . 43 439 12 LYS HA H 5.311 0.000 . 44 439 12 LYS HB2 H 1.443 0.000 . 45 439 12 LYS HB3 H 1.386 0.000 . 46 439 12 LYS HG2 H 1.112 0.000 . 47 439 12 LYS HD2 H 1.324 0.000 . 48 439 12 LYS HD3 H 1.223 0.004 . 49 439 12 LYS HE2 H 2.648 0.000 . 50 440 13 THR H H 9.140 0.000 . 51 440 13 THR HA H 4.627 0.000 . 52 440 13 THR HB H 4.449 0.000 . 53 440 13 THR HG2 H 1.318 0.001 . 54 441 14 ALA H H 9.086 0.000 . 55 441 14 ALA HA H 3.971 0.003 . 56 441 14 ALA HB H 1.275 0.000 . 57 442 15 ASP H H 7.881 0.000 . 58 442 15 ASP HA H 4.477 0.000 . 59 442 15 ASP HB2 H 2.648 0.000 . 60 442 15 ASP HB3 H 2.449 0.004 . 61 443 16 GLY H H 7.783 0.000 . 62 443 16 GLY HA2 H 3.426 0.004 . 63 443 16 GLY HA3 H 3.973 0.001 . 64 444 17 LYS H H 7.831 0.000 . 65 444 17 LYS HA H 4.355 0.000 . 66 444 17 LYS HB2 H 1.834 0.001 . 67 444 17 LYS HG2 H 1.138 0.000 . 68 444 17 LYS HD2 H 1.344 0.000 . 69 444 17 LYS HD3 H 1.257 0.000 . 70 444 17 LYS HE2 H 2.563 0.000 . 71 445 18 THR H H 8.631 0.000 . 72 445 18 THR HA H 4.687 0.000 . 73 445 18 THR HB H 3.753 0.000 . 74 445 18 THR HG2 H 0.714 0.002 . 75 446 19 TYR H H 8.531 0.003 . 76 446 19 TYR HA H 4.328 0.002 . 77 446 19 TYR HB2 H 2.084 0.000 . 78 446 19 TYR HD2 H 6.554 0.000 . 79 446 19 TYR HE2 H 6.147 0.000 . 80 447 20 TYR H H 8.692 0.000 . 81 447 20 TYR HA H 4.911 0.002 . 82 447 20 TYR HB2 H 2.476 0.003 . 83 447 20 TYR HB3 H 2.408 0.009 . 84 447 20 TYR HD1 H 6.484 0.001 . 85 447 20 TYR HE1 H 6.479 0.000 . 86 448 21 TYR H H 9.076 0.000 . 87 448 21 TYR HA H 5.346 0.002 . 88 448 21 TYR HB2 H 2.441 0.004 . 89 448 21 TYR HB3 H 2.408 0.000 . 90 448 21 TYR HD1 H 6.690 0.003 . 91 448 21 TYR HE1 H 6.384 0.000 . 92 449 22 ASN H H 7.976 0.000 . 93 449 22 ASN HA H 4.036 0.000 . 94 449 22 ASN HB2 H 2.105 0.000 . 95 449 22 ASN HB3 H -0.151 0.000 . 96 449 22 ASN HD21 H 4.228 0.000 . 97 449 22 ASN HD22 H 7.043 0.000 . 98 450 23 ASN H H 8.329 0.002 . 99 450 23 ASN HA H 3.948 0.000 . 100 450 23 ASN HB2 H 2.541 0.000 . 101 450 23 ASN HB3 H 2.479 0.000 . 102 450 23 ASN HD21 H 7.209 0.004 . 103 450 23 ASN HD22 H 6.846 0.000 . 104 451 24 ARG H H 8.322 0.000 . 105 451 24 ARG HA H 4.066 0.000 . 106 451 24 ARG HB2 H 1.702 0.000 . 107 451 24 ARG HB3 H 1.390 0.000 . 108 451 24 ARG HG2 H 1.231 0.000 . 109 451 24 ARG HG3 H 1.036 0.000 . 110 451 24 ARG HD2 H 3.049 0.000 . 111 451 24 ARG HD3 H 2.784 0.000 . 112 451 24 ARG HE H 7.830 0.000 . 113 451 24 ARG HH11 H 6.582 0.003 . 114 451 24 ARG HH12 H 6.582 0.003 . 115 452 25 THR H H 7.740 0.000 . 116 452 25 THR HA H 3.762 0.000 . 117 452 25 THR HB H 3.977 0.000 . 118 452 25 THR HG2 H 0.702 0.001 . 119 453 26 LEU H H 7.656 0.000 . 120 453 26 LEU HA H 3.513 0.000 . 121 453 26 LEU HB2 H 1.868 0.003 . 122 453 26 LEU HB3 H 1.496 0.000 . 123 453 26 LEU HG H 1.065 0.000 . 124 453 26 LEU HD1 H 0.629 0.004 . 125 453 26 LEU HD2 H 0.549 0.000 . 126 454 27 GLU H H 6.933 0.000 . 127 454 27 GLU HA H 4.057 0.000 . 128 454 27 GLU HB2 H 1.680 0.000 . 129 454 27 GLU HB3 H 1.533 0.000 . 130 454 27 GLU HG2 H 2.023 0.000 . 131 454 27 GLU HG3 H 1.879 0.000 . 132 455 28 SER H H 8.216 0.000 . 133 455 28 SER HA H 5.784 0.000 . 134 455 28 SER HB2 H 3.460 0.000 . 135 456 29 THR H H 9.230 0.000 . 136 456 29 THR HA H 4.578 0.000 . 137 456 29 THR HB H 3.711 0.975 . 138 456 29 THR HG2 H 0.947 0.000 . 139 457 30 TRP H H 8.382 0.000 . 140 457 30 TRP HA H 4.726 0.000 . 141 457 30 TRP HB2 H 3.457 0.000 . 142 457 30 TRP HB3 H 2.944 0.000 . 143 457 30 TRP HD1 H 7.171 0.000 . 144 457 30 TRP HE1 H 9.908 0.000 . 145 457 30 TRP HE3 H 7.856 0.000 . 146 457 30 TRP HZ2 H 7.101 0.004 . 147 457 30 TRP HZ3 H 6.675 0.000 . 148 457 30 TRP HH2 H 6.825 0.000 . 149 458 31 GLU H H 7.937 0.000 . 150 458 31 GLU HA H 4.197 0.000 . 151 458 31 GLU HB2 H 1.578 0.000 . 152 458 31 GLU HG2 H 1.932 0.000 . 153 459 32 LYS H H 8.237 0.000 . 154 459 32 LYS HA H 2.527 0.000 . 155 459 32 LYS HB2 H 2.612 0.000 . 156 459 32 LYS HB3 H 2.247 0.435 . 157 459 32 LYS HG2 H 0.818 0.000 . 158 459 32 LYS HG3 H 0.278 0.000 . 159 459 32 LYS HD2 H 1.233 0.002 . 160 459 32 LYS HD3 H 1.098 0.001 . 161 459 32 LYS HE2 H 1.969 0.000 . 162 460 33 PRO HA H 3.704 0.000 . 163 460 33 PRO HB2 H 1.086 0.000 . 164 460 33 PRO HB3 H 0.843 0.000 . 165 460 33 PRO HG2 H 0.058 0.000 . 166 460 33 PRO HG3 H -0.070 0.000 . 167 460 33 PRO HD2 H 2.533 0.000 . 168 460 33 PRO HD3 H 1.972 0.000 . 169 461 34 GLN H H 8.352 0.000 . 170 461 34 GLN HA H 3.536 0.001 . 171 461 34 GLN HB2 H 1.796 0.004 . 172 461 34 GLN HB3 H 1.733 0.004 . 173 461 34 GLN HG2 H 2.134 0.000 . 174 461 34 GLN HE21 H 7.395 0.000 . 175 461 34 GLN HE22 H 6.703 0.000 . 176 462 35 GLU H H 8.885 0.000 . 177 462 35 GLU HA H 3.910 0.003 . 178 462 35 GLU HB2 H 1.848 0.004 . 179 462 35 GLU HB3 H 1.768 0.004 . 180 462 35 GLU HG2 H 2.112 0.000 . 181 463 36 LEU H H 7.317 0.000 . 182 463 36 LEU HA H 4.222 0.000 . 183 463 36 LEU HB2 H 1.408 0.003 . 184 463 36 LEU HB3 H 1.147 0.004 . 185 463 36 LEU HG H 1.048 0.004 . 186 463 36 LEU HD1 H 0.677 0.000 . 187 463 36 LEU HD2 H 0.595 0.001 . 188 464 37 LYS H H 7.414 0.000 . 189 464 37 LYS HA H 3.734 0.000 . 190 464 37 LYS HB2 H 1.493 0.004 . 191 464 37 LYS HB3 H 1.391 0.000 . 192 464 37 LYS HG2 H 1.014 0.004 . 193 464 37 LYS HD2 H 1.165 0.000 . 194 464 37 LYS HE2 H 1.581 0.000 . stop_ save_