data_4133 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The Structure of the N-terminus of Striated Muscle Alpha-Tropomyosin in a Chimeric Peptide: Solution Nuclear Magnetic Resonance Structure and Circular Dichroism Studies. ; _BMRB_accession_number 4133 _BMRB_flat_file_name bmr4133.str _Entry_type original _Submission_date 1998-04-13 _Accession_date 1998-04-13 _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 Greenfield Norma J. . 2 Montelione Gaetano T. . 3 Farid Ramy S. . 4 Hitchcock-DeGregori Sarah E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 213 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1998-10-01 original author 'Original BMRB release' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 2005-01-21 update BMRB 'Corrected the residue numbering for ASN 20 and ambiguity codes' 2006-04-28 update author 'addition of relationship loop' stop_ loop_ _Related_BMRB_accession_number _Relationship 7080 'Complex of TM1a(1-14)Zip with TM9a(251-284)' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Greenfield, N. J., Montelione, G. T., Farid, R. S. and Hitchcock-DeGregori, S. E., "The Structure of the N-terminus of Striated Muscle Alpha-Tropomyosin in a Chimeric Peptide: Solution Nuclear Magnetic Resonance Structure and Circular Dichroism Studies," Biochemistry 37, 7834-7843 (1998). ; _Citation_title ; The Structure of the N-terminus of Striated Muscle Alpha-Tropomyosin in a Chimeric Peptide: Solution Nuclear Magnetic Resonance Structure and Circular Dichroism Studies. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98263181 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Greenfield Norma J. . 2 Montelione Gaetano T. . 3 Farid Ramy S. . 4 Hitchcock-DeGregori Sarah E. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 37 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7834 _Page_last 7843 _Year 1998 _Details . save_ ################################## # Molecular system description # ################################## save_system_TMZip _Saveframe_category molecular_system _Mol_system_name Tropomyosin_GCN4_chimera _Abbreviation_common TMZip _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TMZip $TMZip stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TMZip _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TMZip _Name_variant Tropomyosin_GCN4_chimera _Abbreviation_common TMZip _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 32 _Mol_residue_sequence ; MDAIKKKMQMLKLDNYHLEN EVARLKKLVGER ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ASP 3 3 ALA 4 4 ILE 5 5 LYS 6 6 LYS 7 7 LYS 8 8 MET 9 9 GLN 10 10 MET 11 11 LEU 12 12 LYS 13 13 LEU 14 14 ASP 15 15 ASN 16 16 TYR 17 17 HIS 18 18 LEU 19 19 GLU 20 20 ASN 21 21 GLU 22 22 VAL 23 23 ALA 24 24 ARG 25 25 LEU 26 26 LYS 27 27 LYS 28 28 LEU 29 29 VAL 30 30 GLY 31 31 GLU 32 32 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 1IJ0 "Coiled Coil Trimer Gcn4-pvls Ser At Buried D Position" 53.13 34 100.00 100.00 6.24e-02 PDB 1IJ1 "Gcn4-pvlt Coiled-coil Trimer With Threonine At The D(12) Position" 53.13 34 100.00 100.00 6.49e-02 PDB 1TMZ "Tmzip: A Chimeric Peptide Model Of The N-Terminus Of Alpha Tropomyosin, Nmr, 15 Structures" 96.88 32 100.00 100.00 1.76e-11 PDB 2G9J 'Complex Of Tm1a(1-14)zip With Tm9a(251-284): A Model For The Polymerization Domain ("overlap Region") Of Tropomyosin, Northeast' 100.00 33 100.00 100.00 3.49e-12 PDB 2L56 "Nmr Structure Of The Gcn4 Trigger Peptide Refined Using Biased Molecular Dynamics Simulations" 50.00 18 100.00 100.00 3.86e-01 PDB 2OVN "Nmr Structure Of The Gcn4 Trigger Peptide" 53.13 17 100.00 100.00 9.18e-02 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TMZip . . . . . . 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 $TMZip 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TMZip 1 mM . 'Sodium phosphate' 10 mM . NaCl 100 mM . H2O 95 % . D2O 5 % . stop_ 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_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 . n/a temperature 288 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_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 _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 . 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_chemical_shift_assignment_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name TMZip _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 MET H H 8.72 . 1 2 . 1 MET HA H 4.35 . 1 3 . 1 MET HB2 H 2.16 . 2 4 . 1 MET HB3 H 2.09 . 2 5 . 1 MET HG2 H 2.66 . 1 6 . 1 MET HG3 H 2.66 . 1 7 . 2 ASP H H 8.65 . 1 8 . 2 ASP HA H 4.37 . 1 9 . 2 ASP HB2 H 2.67 . 1 10 . 2 ASP HB3 H 2.67 . 1 11 . 3 ALA H H 8.09 . 1 12 . 3 ALA HA H 4.18 . 1 13 . 3 ALA HB H 1.50 . 1 14 . 4 ILE H H 7.79 . 1 15 . 4 ILE HA H 3.90 . 1 16 . 4 ILE HB H 2.03 . 1 17 . 4 ILE HG12 H 1.28 . 2 18 . 4 ILE HG13 H 1.70 . 2 19 . 4 ILE HG2 H 1.03 . 1 20 . 4 ILE HD1 H 0.90 . 1 21 . 5 LYS H H 8.41 . 1 22 . 5 LYS HA H 3.97 . 1 23 . 5 LYS HB2 H 1.95 . 1 24 . 5 LYS HB3 H 1.95 . 1 25 . 5 LYS HG2 H 1.43 . 1 26 . 5 LYS HG3 H 1.43 . 1 27 . 5 LYS HD2 H 1.71 . 1 28 . 5 LYS HD3 H 1.71 . 1 29 . 5 LYS HE2 H 2.96 . 1 30 . 5 LYS HE3 H 2.96 . 1 31 . 6 LYS H H 7.90 . 1 32 . 6 LYS HA H 4.16 . 1 33 . 6 LYS HB2 H 1.94 . 2 34 . 6 LYS HB3 H 1.61 . 2 35 . 6 LYS HG2 H 0.97 . 2 36 . 6 LYS HG3 H 0.90 . 2 37 . 6 LYS HD2 H 1.72 . 2 38 . 6 LYS HD3 H 1.35 . 2 39 . 6 LYS HE2 H 3.03 . 1 40 . 6 LYS HE3 H 3.03 . 1 41 . 7 LYS H H 7.84 . 1 42 . 7 LYS HA H 4.61 . 1 43 . 7 LYS HB2 H 1.95 . 2 44 . 7 LYS HB3 H 2.04 . 2 45 . 7 LYS HG2 H 1.52 . 1 46 . 7 LYS HG3 H 1.52 . 1 47 . 7 LYS HD2 H 1.73 . 1 48 . 7 LYS HD3 H 1.73 . 1 49 . 7 LYS HE2 H 2.98 . 1 50 . 7 LYS HE3 H 2.98 . 1 51 . 8 MET H H 8.73 . 1 52 . 8 MET HA H 4.06 . 1 53 . 8 MET HB2 H 2.27 . 1 54 . 8 MET HB3 H 2.27 . 1 55 . 8 MET HG2 H 2.47 . 2 56 . 8 MET HG3 H 2.62 . 2 57 . 9 GLN H H 8.12 . 1 58 . 9 GLN HA H 4.06 . 1 59 . 9 GLN HB2 H 2.09 . 2 60 . 9 GLN HB3 H 2.26 . 2 61 . 9 GLN HG2 H 2.48 . 2 62 . 9 GLN HG3 H 2.55 . 2 63 . 9 GLN HE21 H 6.98 . 2 64 . 9 GLN HE22 H 7.47 . 2 65 . 10 MET H H 7.96 . 1 66 . 10 MET HA H 4.27 . 1 67 . 10 MET HB2 H 2.29 . 2 68 . 10 MET HB3 H 2.23 . 2 69 . 10 MET HG2 H 2.69 . 2 70 . 10 MET HG3 H 2.83 . 2 71 . 11 LEU H H 8.21 . 1 72 . 11 LEU HA H 4.21 . 1 73 . 11 LEU HB2 H 1.50 . 2 74 . 11 LEU HB3 H 2.03 . 2 75 . 11 LEU HG H 1.82 . 1 76 . 11 LEU HD1 H 0.95 . 2 77 . 11 LEU HD2 H 1.00 . 2 78 . 12 LYS H H 8.44 . 1 79 . 12 LYS HA H 3.98 . 1 80 . 12 LYS HB2 H 1.93 . 1 81 . 12 LYS HB3 H 1.93 . 1 82 . 12 LYS HG2 H 1.48 . 1 83 . 12 LYS HG3 H 1.48 . 1 84 . 12 LYS HD2 H 1.72 . 1 85 . 12 LYS HD3 H 1.72 . 1 86 . 12 LYS HE2 H 3.03 . 1 87 . 12 LYS HE3 H 3.03 . 1 88 . 13 LEU H H 7.90 . 1 89 . 13 LEU HA H 4.23 . 1 90 . 13 LEU HB2 H 1.81 . 2 91 . 13 LEU HB3 H 1.87 . 2 92 . 13 LEU HG H 1.73 . 1 93 . 13 LEU HD1 H 0.95 . 1 94 . 13 LEU HD2 H 0.95 . 1 95 . 14 ASP H H 8.41 . 1 96 . 14 ASP HA H 4.49 . 1 97 . 14 ASP HB2 H 2.67 . 2 98 . 14 ASP HB3 H 2.91 . 2 99 . 15 ASN H H 8.57 . 1 100 . 15 ASN HA H 4.38 . 1 101 . 15 ASN HB2 H 2.85 . 2 102 . 15 ASN HB3 H 3.30 . 2 103 . 15 ASN HD21 H 7.99 . 2 104 . 15 ASN HD22 H 7.02 . 2 105 . 16 TYR H H 8.17 . 1 106 . 16 TYR HA H 4.43 . 1 107 . 16 TYR HB2 H 3.26 . 2 108 . 16 TYR HB3 H 3.30 . 2 109 . 16 TYR HD1 H 7.11 . 1 110 . 16 TYR HD2 H 7.11 . 1 111 . 16 TYR HE1 H 6.87 . 1 112 . 16 TYR HE2 H 6.87 . 1 113 . 17 HIS H H 8.30 . 1 114 . 17 HIS HA H 4.44 . 1 115 . 17 HIS HB2 H 3.45 . 1 116 . 17 HIS HB3 H 3.45 . 1 117 . 17 HIS HD2 H 7.34 . 1 118 . 17 HIS HE1 H 8.43 . 1 119 . 18 LEU H H 8.81 . 1 120 . 18 LEU HA H 3.99 . 1 121 . 18 LEU HB2 H 1.35 . 2 122 . 18 LEU HB3 H 2.15 . 2 123 . 18 LEU HG H 1.94 . 1 124 . 18 LEU HD1 H 0.88 . 2 125 . 18 LEU HD2 H 1.00 . 2 126 . 19 GLU H H 8.95 . 1 127 . 19 GLU HA H 3.93 . 1 128 . 19 GLU HB2 H 2.02 . 2 129 . 19 GLU HB3 H 2.25 . 2 130 . 19 GLU HG2 H 2.53 . 1 131 . 19 GLU HG3 H 2.53 . 1 132 . 20 ASN H H 7.87 . 1 133 . 20 ASN HA H 4.46 . 1 134 . 20 ASN HB2 H 2.76 . 2 135 . 20 ASN HB3 H 2.91 . 2 136 . 20 ASN HD21 H 5.76 . 2 137 . 20 ASN HD22 H 7.46 . 2 138 . 21 GLU H H 8.15 . 1 139 . 21 GLU HA H 4.51 . 1 140 . 21 GLU HB2 H 2.02 . 2 141 . 21 GLU HB3 H 2.22 . 2 142 . 22 VAL H H 8.77 . 1 143 . 22 VAL HA H 3.41 . 1 144 . 22 VAL HB H 2.15 . 1 145 . 22 VAL HG1 H 0.91 . 2 146 . 22 VAL HG2 H 1.06 . 2 147 . 23 ALA H H 7.83 . 1 148 . 23 ALA HA H 4.04 . 1 149 . 23 ALA HB H 1.51 . 1 150 . 24 ARG H H 8.03 . 1 151 . 24 ARG HA H 3.99 . 1 152 . 24 ARG HB2 H 1.90 . 2 153 . 24 ARG HB3 H 2.19 . 2 154 . 24 ARG HG2 H 1.35 . 2 155 . 24 ARG HG3 H 1.67 . 2 156 . 24 ARG HD2 H 3.03 . 2 157 . 24 ARG HD3 H 3.48 . 2 158 . 25 LEU H H 8.55 . 1 159 . 25 LEU HA H 4.00 . 1 160 . 25 LEU HB2 H 1.38 . 2 161 . 25 LEU HB3 H 2.01 . 2 162 . 25 LEU HG H 1.70 . 1 163 . 25 LEU HD1 H 0.84 . 2 164 . 25 LEU HD2 H 0.96 . 2 165 . 26 LYS H H 9.10 . 1 166 . 26 LYS HA H 3.85 . 1 167 . 26 LYS HB2 H 1.85 . 1 168 . 26 LYS HB3 H 1.85 . 1 169 . 26 LYS HG2 H 1.34 . 1 170 . 26 LYS HG3 H 1.34 . 1 171 . 26 LYS HD2 H 1.51 . 2 172 . 26 LYS HD3 H 1.67 . 2 173 . 26 LYS HE2 H 2.85 . 1 174 . 26 LYS HE3 H 2.85 . 1 175 . 27 LYS H H 7.44 . 1 176 . 27 LYS HA H 4.17 . 1 177 . 27 LYS HB2 H 1.92 . 2 178 . 27 LYS HB3 H 2.00 . 2 179 . 27 LYS HG2 H 1.49 . 2 180 . 27 LYS HG3 H 1.62 . 2 181 . 27 LYS HD2 H 1.73 . 1 182 . 27 LYS HD3 H 1.73 . 1 183 . 27 LYS HE2 H 3.00 . 1 184 . 27 LYS HE3 H 3.00 . 1 185 . 28 LEU H H 7.51 . 1 186 . 28 LEU HA H 4.22 . 1 187 . 28 LEU HB2 H 1.66 . 2 188 . 28 LEU HB3 H 2.10 . 2 189 . 28 LEU HG H 1.84 . 1 190 . 28 LEU HD1 H 0.93 . 2 191 . 28 LEU HD2 H 0.99 . 2 192 . 29 VAL H H 7.83 . 1 193 . 29 VAL HA H 4.11 . 1 194 . 29 VAL HB H 2.27 . 1 195 . 29 VAL HG1 H 0.96 . 2 196 . 29 VAL HG2 H 1.02 . 2 197 . 30 GLY H H 7.92 . 1 198 . 30 GLY HA2 H 3.92 . 2 199 . 30 GLY HA3 H 4.12 . 2 200 . 31 GLU H H 8.02 . 1 201 . 31 GLU HA H 4.40 . 1 202 . 31 GLU HB2 H 1.78 . 2 203 . 31 GLU HB3 H 2.06 . 2 204 . 31 GLU HG2 H 2.27 . 1 205 . 31 GLU HG3 H 2.27 . 1 206 . 32 ARG H H 8.04 . 1 207 . 32 ARG HA H 4.15 . 1 208 . 32 ARG HB2 H 1.71 . 2 209 . 32 ARG HB3 H 1.87 . 2 210 . 32 ARG HG2 H 1.35 . 2 211 . 32 ARG HG3 H 1.63 . 2 212 . 32 ARG HD2 H 3.00 . 2 213 . 32 ARG HD3 H 3.22 . 2 stop_ save_