data_3036 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Effect of Trifluoroethanol on Protein Secondary Structure: An NMR and CD Study Using a Synthetic Actin Peptide ; _BMRB_accession_number 3036 _BMRB_flat_file_name bmr3036.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _Entry_origination BMRB _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 Sonnichsen F. D. . 2 'Van Eyk' Jennifer . . 3 Hodges Robert S. . 4 Sykes Brian D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 124 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Sonnichsen, F.D., Van Eyk, Jennifer, Hodges, Robert S., Sykes, Brian D., "Effect of Trifluoroethanol on Protein Secondary Structure: An NMR and CD Study Using a Synthetic Actin Peptide," Biochemistry 31 (37), 8790-8798 (1992). ; _Citation_title ; Effect of Trifluoroethanol on Protein Secondary Structure: An NMR and CD Study Using a Synthetic Actin Peptide ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sonnichsen F. D. . 2 'Van Eyk' Jennifer . . 3 Hodges Robert S. . 4 Sykes Brian D. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 31 _Journal_issue 37 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 8790 _Page_last 8798 _Year 1992 _Details . save_ ################################## # Molecular system description # ################################## save_system_actin _Saveframe_category molecular_system _Mol_system_name actin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label actin $actin stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_actin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common actin _Name_variant 'residues 1-28' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 27 _Mol_residue_sequence ; XEDETTALVADNGSGLVKAG FAGDDAP ; loop_ _Residue_seq_code _Residue_label 1 X 2 GLU 3 ASP 4 GLU 5 THR 6 THR 7 ALA 8 LEU 9 VAL 10 ALA 11 ASP 12 ASN 13 GLY 14 SER 15 GLY 16 LEU 17 VAL 18 LYS 19 ALA 20 GLY 21 PHE 22 ALA 23 GLY 24 ASP 25 ASP 26 ALA 27 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 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 GB KFR04036 "Actin, alpha cardiac muscle 1, partial [Opisthocomus hoazin]" 55.56 364 100.00 100.00 2.26e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $actin . . . . . . 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 $actin 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.05 . na temperature 278 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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 DSS H . CH3 ppm 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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name actin _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 GLU H H 8.62 . 1 2 . 2 GLU HA H 4.32 . 1 3 . 2 GLU HB2 H 2.2 . 2 4 . 2 GLU HB3 H 2.17 . 2 5 . 2 GLU HG2 H 2.58 . 1 6 . 2 GLU HG3 H 2.58 . 1 7 . 3 ASP H H 8.46 . 1 8 . 3 ASP HA H 4.62 . 1 9 . 3 ASP HB2 H 3 . 1 10 . 3 ASP HB3 H 3 . 1 11 . 4 GLU H H 8.16 . 1 12 . 4 GLU HA H 4.23 . 1 13 . 4 GLU HB2 H 2.21 . 1 14 . 4 GLU HB3 H 2.21 . 1 15 . 4 GLU HG2 H 2.57 . 1 16 . 4 GLU HG3 H 2.57 . 1 17 . 5 THR H H 8.12 . 1 18 . 5 THR HA H 4.04 . 1 19 . 5 THR HB H 4.32 . 1 20 . 5 THR HG2 H 1.33 . 1 21 . 6 THR H H 7.89 . 1 22 . 6 THR HA H 3.97 . 1 23 . 6 THR HB H 4.32 . 1 24 . 6 THR HG2 H 1.32 . 1 25 . 7 ALA H H 7.74 . 1 26 . 7 ALA HA H 4.13 . 1 27 . 7 ALA HB H 1.55 . 1 28 . 8 LEU H H 7.98 . 1 29 . 8 LEU HA H 4.2 . 1 30 . 8 LEU HB2 H 1.99 . 2 31 . 8 LEU HB3 H 1.71 . 2 32 . 8 LEU HG H 1.85 . 1 33 . 8 LEU HD1 H .98 . 1 34 . 8 LEU HD2 H .98 . 1 35 . 9 VAL H H 8.14 . 1 36 . 9 VAL HA H 3.8 . 1 37 . 9 VAL HB H 2.26 . 1 38 . 9 VAL HG1 H 1.13 . 2 39 . 9 VAL HG2 H 1.02 . 2 40 . 10 ALA H H 8.46 . 1 41 . 10 ALA HA H 4.22 . 1 42 . 10 ALA HB H 1.54 . 1 43 . 11 ASP H H 8.53 . 1 44 . 11 ASP HA H 4.66 . 1 45 . 11 ASP HB2 H 3.12 . 2 46 . 11 ASP HB3 H 3.03 . 2 47 . 12 ASN H H 8.31 . 1 48 . 12 ASN HA H 4.7 . 1 49 . 12 ASN HB2 H 3 . 2 50 . 12 ASN HB3 H 2.94 . 2 51 . 12 ASN HD21 H 7.63 . 2 52 . 12 ASN HD22 H 6.6 . 2 53 . 13 GLY H H 8.63 . 1 54 . 13 GLY HA2 H 4.04 . 1 55 . 13 GLY HA3 H 4.04 . 1 56 . 14 SER H H 8.23 . 1 57 . 14 SER HA H 4.3 . 1 58 . 14 SER HB2 H 4.08 . 1 59 . 14 SER HB3 H 4.08 . 1 60 . 15 GLY H H 8.27 . 1 61 . 15 GLY HA2 H 3.96 . 2 62 . 15 GLY HA3 H 3.97 . 2 63 . 16 LEU H H 7.82 . 1 64 . 16 LEU HA H 4.28 . 1 65 . 16 LEU HB2 H 1.93 . 2 66 . 16 LEU HB3 H 1.66 . 2 67 . 16 LEU HG H 1.77 . 1 68 . 16 LEU HD1 H .99 . 2 69 . 16 LEU HD2 H .92 . 2 70 . 17 VAL H H 7.74 . 1 71 . 17 VAL HA H 3.84 . 1 72 . 17 VAL HB H 2.23 . 1 73 . 17 VAL HG1 H 1.09 . 2 74 . 17 VAL HG2 H 1.02 . 2 75 . 18 LYS H H 8.07 . 1 76 . 18 LYS HA H 4.17 . 1 77 . 18 LYS HB2 H 1.98 . 2 78 . 18 LYS HB3 H 1.67 . 2 79 . 18 LYS HG2 H 1.51 . 1 80 . 18 LYS HG3 H 1.51 . 1 81 . 18 LYS HD2 H 1.75 . 1 82 . 18 LYS HD3 H 1.75 . 1 83 . 18 LYS HE2 H 3.01 . 1 84 . 18 LYS HE3 H 3.01 . 1 85 . 18 LYS HZ H 7.59 . 1 86 . 19 ALA H H 8.07 . 1 87 . 19 ALA HA H 4.26 . 1 88 . 19 ALA HB H 1.54 . 1 89 . 20 GLY H H 8.05 . 1 90 . 20 GLY HA2 H 3.96 . 1 91 . 20 GLY HA3 H 3.96 . 1 92 . 21 PHE H H 7.97 . 1 93 . 21 PHE HA H 4.63 . 1 94 . 21 PHE HB2 H 3.28 . 2 95 . 21 PHE HB3 H 3.17 . 2 96 . 21 PHE HD1 H 7.35 . 1 97 . 21 PHE HD2 H 7.35 . 1 98 . 21 PHE HE1 H 7.35 . 1 99 . 21 PHE HE2 H 7.35 . 1 100 . 21 PHE HZ H 7.35 . 1 101 . 22 ALA H H 8.15 . 1 102 . 22 ALA HA H 4.28 . 1 103 . 22 ALA HB H 1.5 . 1 104 . 23 GLY H H 7.79 . 1 105 . 23 GLY HA2 H 3.94 . 2 106 . 23 GLY HA3 H 3.96 . 2 107 . 24 ASP H H 8.04 . 1 108 . 24 ASP HA H 4.76 . 1 109 . 24 ASP HB2 H 3.01 . 2 110 . 24 ASP HB3 H 2.99 . 2 111 . 25 ASP H H 8.2 . 1 112 . 25 ASP HA H 4.83 . 1 113 . 25 ASP HB2 H 2.98 . 2 114 . 25 ASP HB3 H 2.9 . 2 115 . 26 ALA H H 7.71 . 1 116 . 26 ALA HA H 4.59 . 1 117 . 26 ALA HB H 1.44 . 1 118 . 27 PRO HA H 4.45 . 1 119 . 27 PRO HB2 H 2.32 . 2 120 . 27 PRO HB3 H 1.96 . 2 121 . 27 PRO HG2 H 2.13 . 2 122 . 27 PRO HG3 H 2.06 . 2 123 . 27 PRO HD2 H 3.81 . 2 124 . 27 PRO HD3 H 3.64 . 2 stop_ save_