data_16589 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; peptide_ptha ; _BMRB_accession_number 16589 _BMRB_flat_file_name bmr16589.str _Entry_type original _Submission_date 2009-10-28 _Accession_date 2009-10-28 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details '1.5 repeat peptide of the PthA protein' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Neves 'Jorge Luiz' . . 2 Sforca 'Mauricio Luis' . . 3 Murakami 'Mario Tyago' . . 4 Zeri 'Ana Carolina de Mattos' . . 5 Benedetti 'Celso Eduardo' . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 223 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-05-19 original author . stop_ _Original_release_date 2011-05-19 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'The repeat domain of the type III effector protein PthA shows a TPR-like structure and undergoes conformational changes upon DNA interaction.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20848643 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Murakami 'Mario Tyago' . . 2 Sforca 'Mauricio Luis' . . 3 Neves 'Jorge Luiz' . . 4 Paiva 'Joice Helena' . . 5 Domingues 'Mariane Noronha' . . 6 Pereira 'Andre Luiz Araujo' . . 7 Zeri 'Ana Carolina de Mattos' . . 8 Benedetti 'Celso Eduardo' . . stop_ _Journal_abbreviation Proteins _Journal_name_full Proteins _Journal_volume 78 _Journal_issue 16 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3386 _Page_last 3395 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name PthA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PthA $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 pthA _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 51 _Mol_residue_sequence ; EQVVAIASNIGGKQALETVQ RLLPVLCQAHGLTPEQVVAI ASHDGGKQALE ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 GLN 3 VAL 4 VAL 5 ALA 6 ILE 7 ALA 8 SER 9 ASN 10 ILE 11 GLY 12 GLY 13 LYS 14 GLN 15 ALA 16 LEU 17 GLU 18 THR 19 VAL 20 GLN 21 ARG 22 LEU 23 LEU 24 PRO 25 VAL 26 LEU 27 CYS 28 GLN 29 ALA 30 HIS 31 GLY 32 LEU 33 THR 34 PRO 35 GLU 36 GLN 37 VAL 38 VAL 39 ALA 40 ILE 41 ALA 42 SER 43 HIS 44 ASP 45 GLY 46 GLY 47 LYS 48 GLN 49 ALA 50 LEU 51 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-16 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 PDB 2KQ5 "Solution Nmr Structure Of A Section Of The Repeat Domain Of The Type Iii Effector Protein Ptha" 100.00 51 100.00 100.00 5.63e-26 GB KHL51201 "hypothetical protein XEU66b_23620, partial [Xanthomonas euvesicatoria]" 76.47 74 97.44 100.00 1.18e-16 GB KHL60368 "hypothetical protein XEU83M_22465, partial [Xanthomonas euvesicatoria]" 80.39 73 97.56 97.56 1.38e-16 GB KHL63085 "hypothetical protein XEU83M_20550, partial [Xanthomonas euvesicatoria]" 72.55 349 100.00 100.00 8.50e-15 GB KOR38772 "hypothetical protein ADT27_22390, partial [Xanthomonas oryzae]" 68.63 205 97.14 97.14 7.45e-13 GB KOR47463 "hypothetical protein ADT27_08560, partial [Xanthomonas oryzae]" 52.94 84 100.00 100.00 1.55e-07 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $entity 'Xanthomonas axonopodis pv citri' 562 Eubacteria . Xanthomonas citri 306 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 'obtained from a vendor' . Xanthomonas citri 306 . 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 1.0 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' SDS 70 mM 'natural abundance' DTT 1 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' 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 refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _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_COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H COSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _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 . pH pressure 1 . atm temperature 293 . 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 hydrogen' ppm 0 internal direct . . . 1.0 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_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '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 PthA _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 2 2 GLN H H 8.787 . 1 2 2 2 GLN HA H 4.562 . 1 3 2 2 GLN HB2 H 2.050 . 2 4 2 2 GLN HB3 H 2.251 . 2 5 2 2 GLN HE21 H 6.830 . 2 6 2 2 GLN HE22 H 7.460 . 2 7 2 2 GLN HG2 H 2.420 . 2 8 3 3 VAL H H 8.266 . 1 9 3 3 VAL HA H 3.853 . 1 10 3 3 VAL HB H 2.030 . 1 11 3 3 VAL HG1 H 0.983 . 2 12 3 3 VAL HG2 H 1.083 . 2 13 4 4 VAL H H 7.962 . 1 14 4 4 VAL HA H 3.845 . 1 15 4 4 VAL HB H 2.134 . 1 16 4 4 VAL HG1 H 0.968 . 2 17 4 4 VAL HG2 H 1.065 . 2 18 5 5 ALA H H 7.829 . 1 19 5 5 ALA HA H 4.221 . 1 20 5 5 ALA HB H 1.463 . 1 21 6 6 ILE H H 7.863 . 1 22 6 6 ILE HA H 4.127 . 1 23 6 6 ILE HB H 1.936 . 1 24 6 6 ILE HD1 H 0.980 . 1 25 6 6 ILE HG12 H 1.181 . 1 26 7 7 ALA H H 8.221 . 1 27 7 7 ALA HA H 4.118 . 1 28 7 7 ALA HB H 1.469 . 1 29 8 8 SER H H 8.167 . 1 30 8 8 SER HA H 4.288 . 1 31 8 8 SER HB2 H 3.927 . 2 32 8 8 SER HB3 H 3.975 . 2 33 9 9 ASN H H 7.974 . 1 34 9 9 ASN HA H 4.761 . 1 35 9 9 ASN HB2 H 2.840 . 2 36 9 9 ASN HB3 H 2.940 . 2 37 9 9 ASN HD21 H 7.610 . 2 38 9 9 ASN HD22 H 6.920 . 2 39 10 10 ILE H H 7.703 . 1 40 10 10 ILE HA H 4.170 . 1 41 10 10 ILE HB H 1.983 . 1 42 10 10 ILE HD1 H 0.980 . 1 43 10 10 ILE HG12 H 1.295 . 1 44 10 10 ILE HG2 H 0.880 . 1 45 11 11 GLY H H 8.349 . 1 46 11 11 GLY HA2 H 3.870 . 2 47 12 12 GLY H H 8.360 . 1 48 12 12 GLY HA2 H 3.944 . 2 49 13 13 LYS H H 8.163 . 1 50 13 13 LYS HA H 4.141 . 1 51 13 13 LYS HB2 H 1.861 . 2 52 13 13 LYS HD2 H 1.711 . 2 53 13 13 LYS HE2 H 3.000 . 2 54 13 13 LYS HG2 H 1.461 . 2 55 13 13 LYS HZ H 7.500 . 1 56 14 14 GLN H H 7.984 . 1 57 14 14 GLN HA H 4.096 . 1 58 14 14 GLN HB2 H 2.120 . 2 59 15 15 ALA H H 7.977 . 1 60 15 15 ALA HA H 4.264 . 1 61 15 15 ALA HB H 1.422 . 1 62 16 16 LEU H H 8.093 . 1 63 16 16 LEU HA H 4.239 . 1 64 16 16 LEU HB2 H 1.860 . 2 65 16 16 LEU HD1 H 0.938 . 2 66 16 16 LEU HD2 H 1.006 . 2 67 16 16 LEU HG H 1.860 . 1 68 17 17 GLU H H 8.233 . 1 69 17 17 GLU HA H 4.178 . 1 70 17 17 GLU HB2 H 2.068 . 2 71 17 17 GLU HB3 H 2.126 . 2 72 17 17 GLU HG2 H 2.389 . 2 73 18 18 THR H H 8.031 . 1 74 18 18 THR HA H 4.283 . 1 75 18 18 THR HB H 4.255 . 1 76 18 18 THR HG2 H 1.424 . 1 77 19 19 VAL H H 7.959 . 1 78 19 19 VAL HA H 3.783 . 1 79 19 19 VAL HB H 1.985 . 1 80 19 19 VAL HG1 H 0.967 . 2 81 19 19 VAL HG2 H 1.011 . 2 82 20 20 GLN H H 8.268 . 1 83 20 20 GLN HA H 3.958 . 1 84 20 20 GLN HB2 H 2.210 . 2 85 20 20 GLN HG2 H 2.388 . 2 86 21 21 ARG H H 7.691 . 1 87 21 21 ARG HA H 4.226 . 1 88 21 21 ARG HB2 H 1.797 . 2 89 21 21 ARG HB3 H 1.985 . 2 90 21 21 ARG HD2 H 3.330 . 2 91 21 21 ARG HD3 H 3.237 . 2 92 21 21 ARG HE H 7.328 . 1 93 21 21 ARG HG2 H 1.692 . 2 94 22 22 LEU H H 7.890 . 1 95 22 22 LEU HA H 4.664 . 1 96 22 22 LEU HB2 H 1.952 . 2 97 22 22 LEU HB3 H 1.967 . 2 98 22 22 LEU HG H 1.520 . 1 99 23 23 LEU H H 7.800 . 1 100 23 23 LEU HA H 4.738 . 1 101 23 23 LEU HB2 H 1.740 . 2 102 23 23 LEU HB3 H 1.630 . 2 103 23 23 LEU HD1 H 0.886 . 2 104 23 23 LEU HD2 H 0.945 . 2 105 23 23 LEU HG H 1.470 . 1 106 24 24 PRO HA H 3.960 . 1 107 24 24 PRO HB2 H 2.305 . 2 108 24 24 PRO HD2 H 3.589 . 2 109 24 24 PRO HD3 H 3.698 . 2 110 24 24 PRO HG2 H 2.141 . 2 111 25 25 VAL H H 7.109 . 1 112 25 25 VAL HA H 3.826 . 1 113 25 25 VAL HB H 2.354 . 1 114 25 25 VAL HG1 H 1.015 . 2 115 25 25 VAL HG2 H 1.130 . 2 116 26 26 LEU H H 8.059 . 1 117 26 26 LEU HA H 4.208 . 1 118 26 26 LEU HB2 H 1.700 . 2 119 26 26 LEU HD1 H 0.962 . 2 120 26 26 LEU HD2 H 0.930 . 2 121 26 26 LEU HG H 1.609 . 1 122 27 27 CYS H H 7.830 . 1 123 27 27 CYS HA H 4.390 . 1 124 27 27 CYS HB2 H 3.235 . 2 125 27 27 CYS HB3 H 3.350 . 2 126 28 28 GLN H H 8.066 . 1 127 28 28 GLN HA H 4.297 . 1 128 28 28 GLN HB2 H 2.140 . 2 129 28 28 GLN HE21 H 6.828 . 2 130 28 28 GLN HE22 H 7.523 . 2 131 28 28 GLN HG2 H 2.405 . 2 132 29 29 ALA H H 8.042 . 1 133 29 29 ALA HA H 4.193 . 1 134 29 29 ALA HB H 1.435 . 1 135 30 30 HIS H H 7.784 . 1 136 30 30 HIS HA H 4.660 . 1 137 30 30 HIS HB2 H 3.056 . 2 138 30 30 HIS HB3 H 3.503 . 2 139 30 30 HIS HD2 H 7.549 . 1 140 30 30 HIS HE2 H 8.762 . 1 141 31 31 GLY H H 7.919 . 1 142 31 31 GLY HA2 H 4.121 . 2 143 32 32 LEU H H 7.861 . 1 144 32 32 LEU HA H 4.589 . 1 145 33 33 THR H H 7.871 . 1 146 33 33 THR HA H 4.381 . 1 147 33 33 THR HB H 4.334 . 1 148 33 33 THR HG2 H 1.248 . 1 149 34 34 PRO HA H 3.760 . 1 150 34 34 PRO HB2 H 2.350 . 2 151 34 34 PRO HD2 H 3.535 . 2 152 34 34 PRO HD3 H 3.631 . 2 153 34 34 PRO HG2 H 2.179 . 2 154 35 35 GLU H H 8.233 . 1 155 35 35 GLU HA H 4.211 . 1 156 35 35 GLU HB2 H 2.067 . 2 157 35 35 GLU HB3 H 2.126 . 2 158 35 35 GLU HG2 H 2.391 . 2 159 36 36 GLN H H 8.761 . 1 160 36 36 GLN HA H 4.540 . 1 161 36 36 GLN HB2 H 2.016 . 2 162 36 36 GLN HB3 H 2.185 . 2 163 36 36 GLN HG2 H 2.373 . 2 164 37 37 VAL H H 8.275 . 1 165 37 37 VAL HA H 3.800 . 1 166 37 37 VAL HB H 2.210 . 1 167 37 37 VAL HG1 H 1.081 . 2 168 37 37 VAL HG2 H 0.986 . 2 169 38 38 VAL H H 7.888 . 1 170 38 38 VAL HA H 3.928 . 1 171 38 38 VAL HG1 H 0.891 . 2 172 38 38 VAL HG2 H 0.948 . 2 173 39 39 ALA H H 8.019 . 1 174 39 39 ALA HA H 4.234 . 1 175 39 39 ALA HB H 1.423 . 1 176 40 40 ILE H H 7.861 . 1 177 40 40 ILE HA H 4.133 . 1 178 40 40 ILE HB H 1.733 . 1 179 40 40 ILE HD1 H 0.892 . 1 180 40 40 ILE HG12 H 1.132 . 1 181 40 40 ILE HG13 H 1.632 . 1 182 40 40 ILE HG2 H 0.945 . 1 183 41 41 ALA H H 8.221 . 1 184 41 41 ALA HA H 4.118 . 1 185 41 41 ALA HB H 1.469 . 1 186 42 42 SER H H 8.542 . 1 187 42 42 SER HA H 4.351 . 1 188 42 42 SER HB2 H 3.866 . 2 189 42 42 SER HB3 H 3.894 . 2 190 43 43 HIS H H 8.021 . 1 191 43 43 HIS HA H 4.658 . 1 192 43 43 HIS HB2 H 3.314 . 2 193 43 43 HIS HB3 H 3.444 . 2 194 43 43 HIS HD2 H 7.439 . 1 195 43 43 HIS HE2 H 8.649 . 1 196 44 44 ASP H H 8.305 . 1 197 44 44 ASP HA H 4.759 . 1 198 44 44 ASP HB2 H 2.932 . 2 199 44 44 ASP HB3 H 3.007 . 2 200 45 45 GLY H H 8.266 . 1 201 45 45 GLY HA2 H 3.857 . 2 202 46 46 GLY H H 8.244 . 1 203 46 46 GLY HA2 H 3.975 . 2 204 47 47 LYS H H 8.166 . 1 205 47 47 LYS HA H 4.150 . 1 206 47 47 LYS HB2 H 1.861 . 2 207 47 47 LYS HD2 H 1.791 . 2 208 47 47 LYS HE2 H 3.000 . 2 209 47 47 LYS HG2 H 1.461 . 2 210 47 47 LYS HZ H 7.500 . 1 211 48 48 GLN H H 8.311 . 1 212 48 48 GLN HA H 4.146 . 1 213 49 49 ALA H H 7.930 . 1 214 49 49 ALA HA H 4.265 . 1 215 49 49 ALA HB H 1.440 . 1 216 50 50 LEU H H 7.810 . 1 217 50 50 LEU HA H 4.324 . 1 218 50 50 LEU HB2 H 1.734 . 2 219 50 50 LEU HD1 H 0.942 . 2 220 50 50 LEU HD2 H 0.887 . 2 221 50 50 LEU HG H 1.631 . 1 222 51 51 GLU H H 7.871 . 1 223 51 51 GLU HA H 4.350 . 1 stop_ save_