data_25683 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; FBP28 WW T456Y ; _BMRB_accession_number 25683 _BMRB_flat_file_name bmr25683.str _Entry_type original _Submission_date 2015-07-01 _Accession_date 2015-07-01 _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 Medina Jordi . . 2 Macias Maria J. . 3 Martin-Malpartida Pau . . 4 Scheraga Harold A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 214 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-08-12 update BMRB 'update entry citation' 2015-10-19 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 25678 L453D 25679 L453E 25680 L453W 25681 E454Y 25682 T456D stop_ _Original_release_date 2015-10-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Preventing fibril formation of a protein by selective mutation ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26483482 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Maisuradze Gia G. . 2 Medina Jordi . . 3 Kachlishvili Khatuna . . 4 Krupa Pawel . . 5 Mozolewska Magdalena . . 6 Martin-Malpartida Pau . . 7 Maisuradze Luka . . 8 Macias Maria J. . 9 Scheraga Harold A. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 112 _Journal_issue 44 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 13549 _Page_last 13554 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name T456Y _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 4426.829 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 37 _Mol_residue_sequence ; GATAVSEWTEYKTADGKTYY YNNRTLESYWEKPQELK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 428 GLY 2 429 ALA 3 430 THR 4 431 ALA 5 432 VAL 6 433 SER 7 434 GLU 8 435 TRP 9 436 THR 10 437 GLU 11 438 TYR 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 TYR 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 . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity 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 $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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $entity . uM 500 1000 'natural abundance' 'sodium phosphate' 25 mM . . 'natural abundance' 'sodium chloride' 100 mM . . 'natural abundance' H2O 90 % . . 'natural abundance' D2O 10 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_ARIA _Saveframe_category software _Name ARIA _Version . loop_ _Vendor _Address _Electronic_address "Linge, O'Donoghue and Nilges" . . stop_ loop_ _Task 'data analysis' 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_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_CNSSOLVE _Saveframe_category software _Name CNSSOLVE _Version . loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task 'structure solution' 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 5.8 . 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_ _Experiment_label '2D 1H-1H NOESY' '2D 1H-1H TOCSY' 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 1 1 GLY HA2 H 3.720 0.010 2 2 1 1 GLY HA3 H 3.605 0.010 2 3 2 2 ALA H H 8.084 0.010 1 4 2 2 ALA HA H 4.151 0.010 1 5 2 2 ALA HB H 1.177 0.010 1 6 3 3 THR H H 8.025 0.010 1 7 3 3 THR HA H 4.104 0.010 1 8 3 3 THR HB H 3.992 0.010 1 9 3 3 THR HG2 H 1.000 0.010 1 10 4 4 ALA H H 8.168 0.010 1 11 4 4 ALA HA H 4.150 0.010 1 12 4 4 ALA HB H 1.175 0.010 1 13 5 5 VAL H H 8.028 0.010 1 14 5 5 VAL HA H 3.896 0.010 1 15 5 5 VAL HB H 1.858 0.010 1 16 5 5 VAL HG1 H 0.747 0.010 2 17 5 5 VAL HG2 H 0.732 0.010 2 18 6 6 SER H H 8.212 0.010 1 19 6 6 SER HA H 4.294 0.010 1 20 6 6 SER HB2 H 3.820 0.001 2 21 6 6 SER HB3 H 3.706 0.001 2 22 7 7 GLU H H 8.569 0.010 1 23 7 7 GLU HA H 3.918 0.010 1 24 7 7 GLU HB2 H 1.639 0.003 2 25 7 7 GLU HB3 H 1.628 0.010 2 26 7 7 GLU HG2 H 1.687 0.010 2 27 7 7 GLU HG3 H 1.676 0.010 2 28 8 8 TRP H H 7.924 0.010 1 29 8 8 TRP HA H 5.252 0.010 1 30 8 8 TRP HB2 H 2.907 0.010 2 31 8 8 TRP HB3 H 2.835 0.003 2 32 8 8 TRP HD1 H 7.064 0.010 1 33 8 8 TRP HE1 H 10.088 0.010 1 34 8 8 TRP HE3 H 7.092 0.010 1 35 8 8 TRP HZ2 H 7.217 0.010 1 36 8 8 TRP HZ3 H 6.618 0.010 1 37 8 8 TRP HH2 H 6.858 0.002 1 38 9 9 THR H H 9.391 0.002 1 39 9 9 THR HA H 4.330 0.010 1 40 9 9 THR HB H 3.686 0.001 1 41 9 9 THR HG2 H 0.632 0.010 1 42 10 10 GLU H H 8.381 0.010 1 43 10 10 GLU HA H 4.263 0.010 1 44 10 10 GLU HB2 H 1.625 0.010 2 45 10 10 GLU HB3 H 1.611 0.010 2 46 10 10 GLU HG2 H 1.578 0.010 2 47 11 11 TYR H H 8.311 0.010 1 48 11 11 TYR HA H 4.356 0.010 1 49 11 11 TYR HB2 H 2.311 0.010 2 50 11 11 TYR HB3 H 0.958 0.010 2 51 11 11 TYR HD1 H 6.624 0.010 3 52 11 11 TYR HE1 H 6.341 0.010 3 53 12 12 LYS H H 8.003 0.002 1 54 12 12 LYS HA H 5.275 0.010 1 55 12 12 LYS HB2 H 1.429 0.010 2 56 12 12 LYS HB3 H 1.151 0.010 2 57 12 12 LYS HG2 H 1.489 0.010 2 58 12 12 LYS HG3 H 1.348 0.010 2 59 12 12 LYS HD2 H 1.299 0.010 2 60 12 12 LYS HD3 H 1.284 0.010 2 61 12 12 LYS HE2 H 2.676 0.010 2 62 13 13 THR H H 9.101 0.010 1 63 13 13 THR HA H 4.465 0.001 1 64 13 13 THR HB H 4.447 0.010 1 65 13 13 THR HG2 H 1.344 0.002 1 66 14 14 ALA H H 7.822 0.010 1 67 14 14 ALA HA H 3.977 0.010 1 68 14 14 ALA HB H 1.264 0.010 1 69 15 15 ASP H H 7.910 0.010 1 70 15 15 ASP HA H 4.475 0.010 1 71 15 15 ASP HB2 H 2.659 0.010 2 72 15 15 ASP HB3 H 2.466 0.010 2 73 16 16 GLY H H 7.817 0.010 1 74 16 16 GLY HA2 H 3.444 0.010 2 75 16 16 GLY HA3 H 3.977 0.010 2 76 17 17 LYS H H 7.760 0.002 1 77 17 17 LYS HA H 4.363 0.001 1 78 17 17 LYS HB2 H 1.792 0.010 2 79 17 17 LYS HB3 H 1.784 0.010 2 80 17 17 LYS HG2 H 1.158 0.010 2 81 17 17 LYS HG3 H 1.139 0.010 2 82 17 17 LYS HD2 H 1.315 0.001 2 83 17 17 LYS HD3 H 1.214 0.010 2 84 17 17 LYS HE2 H 2.513 0.010 2 85 18 18 THR H H 8.531 0.010 1 86 18 18 THR HA H 4.807 0.010 1 87 18 18 THR HB H 3.721 0.010 1 88 18 18 THR HG2 H 0.673 0.010 1 89 19 19 TYR H H 8.575 0.010 1 90 19 19 TYR HA H 4.616 0.003 1 91 19 19 TYR HB2 H 2.260 0.010 2 92 19 19 TYR HB3 H 2.121 0.010 2 93 19 19 TYR HD2 H 6.526 0.010 3 94 19 19 TYR HE2 H 6.143 0.001 3 95 20 20 TYR H H 8.820 0.001 1 96 20 20 TYR HA H 4.836 0.010 1 97 20 20 TYR HB2 H 2.622 0.010 2 98 20 20 TYR HB3 H 2.454 0.010 2 99 20 20 TYR HD1 H 7.219 0.010 3 100 20 20 TYR HE1 H 6.530 0.010 3 101 21 21 TYR H H 9.355 0.010 1 102 21 21 TYR HA H 5.294 0.010 1 103 21 21 TYR HB2 H 2.886 0.002 2 104 21 21 TYR HB3 H 2.716 0.010 2 105 21 21 TYR HD2 H 6.849 0.010 3 106 21 21 TYR HE2 H 6.434 0.001 3 107 22 22 ASN H H 8.224 0.010 1 108 22 22 ASN HA H 4.179 0.010 1 109 22 22 ASN HB2 H 2.493 0.010 2 110 22 22 ASN HB3 H 0.812 0.010 2 111 22 22 ASN HD21 H 7.216 0.010 2 112 22 22 ASN HD22 H 7.091 0.010 2 113 23 23 ASN H H 8.494 0.001 1 114 23 23 ASN HA H 4.014 0.002 1 115 23 23 ASN HB2 H 2.530 0.010 2 116 23 23 ASN HB3 H 2.498 0.010 2 117 23 23 ASN HD21 H 7.128 0.010 2 118 23 23 ASN HD22 H 7.084 0.010 2 119 24 24 ARG H H 8.352 0.010 1 120 24 24 ARG HA H 4.106 0.010 1 121 24 24 ARG HB2 H 1.759 0.002 2 122 24 24 ARG HB3 H 1.257 0.010 2 123 24 24 ARG HG2 H 1.456 0.010 2 124 24 24 ARG HG3 H 1.100 0.010 2 125 24 24 ARG HD2 H 3.042 0.010 2 126 24 24 ARG HD3 H 2.805 0.010 2 127 24 24 ARG HE H 7.721 0.010 1 128 25 25 THR H H 7.881 0.010 1 129 25 25 THR HA H 3.851 0.004 1 130 25 25 THR HB H 4.040 0.010 1 131 25 25 THR HG2 H 0.760 0.010 1 132 26 26 LEU H H 7.764 0.010 1 133 26 26 LEU HA H 3.572 0.003 1 134 26 26 LEU HB2 H 1.895 0.010 2 135 26 26 LEU HB3 H 1.476 0.010 2 136 26 26 LEU HG H 1.102 0.002 1 137 26 26 LEU HD1 H 0.646 0.004 2 138 26 26 LEU HD2 H 0.595 0.010 2 139 27 27 GLU H H 6.840 0.001 1 140 27 27 GLU HA H 4.132 0.002 1 141 27 27 GLU HB2 H 1.666 0.004 2 142 27 27 GLU HB3 H 1.533 0.010 2 143 27 27 GLU HG2 H 2.007 0.001 2 144 27 27 GLU HG3 H 1.912 0.002 2 145 28 28 SER H H 7.943 0.001 1 146 28 28 SER HA H 5.562 0.010 1 147 28 28 SER HB2 H 3.378 0.010 2 148 28 28 SER HB3 H 3.348 0.010 2 149 29 29 TYR H H 9.218 0.010 1 150 29 29 TYR HA H 4.627 0.001 1 151 29 29 TYR HB2 H 3.179 0.010 2 152 29 29 TYR HB3 H 2.580 0.010 2 153 29 29 TYR HD2 H 7.094 0.001 3 154 29 29 TYR HE2 H 6.605 0.003 3 155 30 30 TRP H H 8.718 0.010 1 156 30 30 TRP HA H 4.794 0.010 1 157 30 30 TRP HB2 H 3.390 0.010 2 158 30 30 TRP HB3 H 2.982 0.010 2 159 30 30 TRP HD1 H 7.176 0.010 1 160 30 30 TRP HE1 H 9.951 0.010 1 161 30 30 TRP HE3 H 7.826 0.010 1 162 30 30 TRP HZ2 H 7.118 0.010 1 163 30 30 TRP HZ3 H 6.666 0.010 1 164 30 30 TRP HH2 H 6.835 0.001 1 165 31 31 GLU H H 7.604 0.010 1 166 31 31 GLU HA H 4.304 0.010 1 167 31 31 GLU HB2 H 1.696 0.010 2 168 31 31 GLU HB3 H 1.648 0.010 2 169 31 31 GLU HG2 H 2.019 0.010 2 170 31 31 GLU HG3 H 2.003 0.010 2 171 32 32 LYS H H 8.167 0.010 1 172 32 32 LYS HA H 2.839 0.002 1 173 32 32 LYS HB2 H 0.973 0.010 2 174 32 32 LYS HB3 H 0.857 0.010 2 175 32 32 LYS HG2 H 0.400 0.010 2 176 32 32 LYS HG3 H 0.111 0.010 2 177 32 32 LYS HE2 H 2.768 0.010 2 178 32 32 LYS HZ H 6.510 0.002 1 179 33 33 PRO HA H 3.809 0.010 1 180 33 33 PRO HB2 H 1.464 0.010 2 181 33 33 PRO HB3 H 1.067 0.010 2 182 33 33 PRO HG2 H 0.477 0.001 2 183 33 33 PRO HG3 H 0.120 0.010 2 184 33 33 PRO HD2 H 2.751 0.010 2 185 33 33 PRO HD3 H 2.244 0.010 2 186 34 34 GLN H H 8.329 0.010 1 187 34 34 GLN HA H 3.650 0.010 1 188 34 34 GLN HB2 H 1.750 0.010 2 189 34 34 GLN HB3 H 1.702 0.010 2 190 34 34 GLN HG2 H 2.117 0.010 2 191 34 34 GLN HE21 H 7.405 0.010 2 192 34 34 GLN HE22 H 6.690 0.003 2 193 35 35 GLU H H 8.711 0.010 1 194 35 35 GLU HA H 3.941 0.010 1 195 35 35 GLU HB2 H 1.792 0.010 2 196 35 35 GLU HB3 H 1.694 0.010 2 197 35 35 GLU HG2 H 2.031 0.010 2 198 35 35 GLU HG3 H 2.016 0.010 2 199 36 36 LEU H H 7.602 0.010 1 200 36 36 LEU HA H 4.129 0.010 1 201 36 36 LEU HB2 H 1.307 0.010 2 202 36 36 LEU HB3 H 1.053 0.010 2 203 36 36 LEU HG H 1.080 0.010 1 204 36 36 LEU HD1 H 0.564 0.010 2 205 36 36 LEU HD2 H 0.480 0.010 2 206 37 37 LYS H H 7.502 0.010 1 207 37 37 LYS HA H 3.786 0.010 1 208 37 37 LYS HB2 H 1.569 0.010 2 209 37 37 LYS HB3 H 1.465 0.010 2 210 37 37 LYS HG2 H 1.142 0.010 2 211 37 37 LYS HG3 H 1.037 0.010 2 212 37 37 LYS HD2 H 1.385 0.002 2 213 37 37 LYS HE2 H 2.939 0.473 2 214 37 37 LYS HZ H 7.436 0.010 1 stop_ save_