data_4995 #Corrected using PDB structure: 1IHQA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 2 A HA 4.24 3.51 # #After reference correction, the following residues still #have a CO chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 4 S C 174.73 166.06 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.17 -0.02 -0.02 -0.47 -0.81 0.08 # #bmr4995.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4995.str file): #HA CA CB CO N HN #N/A -0.02 -0.02 -0.47 -0.81 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.05 +/-0.24 +/-0.28 +/-0.37 +/-0.69 +/-0.13 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.541 0.979 0.996 0.646 0.759 0.382 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.165 0.741 0.823 1.133 2.103 0.387 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution NMR Structure and Folding Dynamics of the N-terminus of a rat Non-muscle Alpha-tropomyosin in an Engineered Chimeric Protein ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Greenfield Norma J. . 2 Huang Yuanpeng Janet . 3 Palm Thomas . . 4 Swapna G.V.T.S. . . 5 Monleon Daniel . . 6 Montelione Gaetano T. . 7 Hitchcock-DeGregori Sarah E. . stop_ _BMRB_accession_number 4995 _BMRB_flat_file_name bmr4995.str _Entry_type new _Submission_date 2001-04-20 _Accession_date 2001-04-20 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 232 '15N chemical shifts' 41 '13C chemical shifts' 160 'coupling constants' 34 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-04-03 update author "Update the Mol_system_name." 2001-10-17 original author "Original release." stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Solution NMR Structure and Folding Dynamics of the N-terminus of a rat Non-muscle Alpha-tropomyosin in an Engineered Chimeric Protein ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 21460866 _PubMed_ID 11575936 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Greenfield Norma J. . 2 Huang Yuanpeng Janet . 3 Palm Thomas . . 4 Swapna G.V.T.S. . . 5 Monleon Daniel . . 6 Montelione Gaetano T. . 7 Hitchcock-DeGregori Sarah E. . stop_ _Journal_abbreviation "J. Mol. Biol." _Journal_volume 312 _Journal_issue 4 _Page_first 833 _Page_last 847 _Year 2001 loop_ _Keyword "tropomyosin" "GCN4" "coiled coil" "triple-resonance" "AutoAssign" "AutoStructure" "alpha-helix" "automatic-assignment" "folding-intermediate" "isoforms" stop_ save_ ################################## # Molecular system description # ################################## save_system_GlyTM1bZip _Saveframe_category molecular_system _Mol_system_name "GlyTM1bZip coiled-coil dimer" _Abbreviation_common GlyTM1bZip _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "GlyTM1bZip subunit A" $GlyTM1bZip "GlyTM1bZip subunit B" $GlyTM1bZip stop_ _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 "GlyTM1bZip subunit A" 1 "GlyTM1bZip subunit B" stop_ loop_ _Biological_function "actin thin-filament regulation" stop_ loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1IHQ ? . stop_ save_ ######################## # Monomeric polymers # ######################## save_GlyTM1bZip _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common GlyTM1bZip _Name_variant . _Abbreviation_common GlyTM1bZip _Molecular_mass 8644 _Mol_thiol_state 'not present' _Details ; Residues 7-35 are a two chained coiled coil. Residues 1-6 are flexible ; ############################## # Polymer residue sequence # ############################## _Ambiguous_sequence_features ; Chimeric peptide. Residues 2-20 are the first 19 residues of short rat alpha tropomyosins encoded by exon 1b. Residues 21-38 are the last 18 C-terminal residues of the yeast transcription factor GCN4. The peptide has an N-terminal glycine. ; ############################## # Polymer residue sequence # ############################## _Residue_count 38 _Mol_residue_sequence ; GAGSSSLEAVRRKIRSLQEQ NYHLENEVARLKKLVGER ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ALA 3 GLY 4 SER 5 SER 6 SER 7 LEU 8 GLU 9 ALA 10 VAL 11 ARG 12 ARG 13 LYS 14 ILE 15 ARG 16 SER 17 LEU 18 GLN 19 GLU 20 GLN 21 ASN 22 TYR 23 HIS 24 LEU 25 GLU 26 ASN 27 GLU 28 VAL 29 ALA 30 ARG 31 LEU 32 LYS 33 LYS 34 LEU 35 VAL 36 GLY 37 GLU 38 ARG stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-04-29 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 1IHQ "A Chain A, Glytm1bzip: A Chimeric PeptideModel Of The N-Terminus Of A Rat Short AlphaTropomyosin With The N-Terminus Encoded By Exon 1b" 100.00 38 100 100 1e-12 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Tissue $GlyTM1bZip Rat 10116 Eukaryota Metazoa Rattus norvegicus non-muscle 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 _Details $GlyTM1bZip 'recombinant technology' . . . . . ; Synthethic gene prepared from oligonucleotides assmebled and amplified using Pfu DNAas polymerase. Cloned into the Vector pPROEX HTa and expressed in E.coli (DH5) ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_GlyTM1bZip_(two-chained) _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Isotopic_labeling $system_GlyTM1bZip 0.6 mM 0.5 . NaCl 100 mM . . "sodium phosphate" 10 mM . . H2O 90 % . . D2O 10 % . . stop_ save_ save_15N-GlyTM1bZip _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $system_GlyTM1bZip . mM 0.5 2.0 "[U-99% 15N]" NaCl 100 mM . . . "sodium phosphate" 10 mM . . . H2O 90 % . . . D2O 10 % . . . stop_ save_ save_15N,13C-GlyTM1bZip _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $system_GlyTM1bZip 0.8 mM "[U-99% 13C; U-99% 15N]" NaCl 100 mM . "sodium phosphate" 10 mM . H2O 90 % . D2O 10 % . stop_ save_ save_GlyTM1bZip_heterodimer _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $system_GlyTM1bZip 1.32 mM . $system_GlyTM1bZip 0.88 mM "[U-99% 13C; U-99% 15N]" NaCl 100 mM . "sodium phosphate" 10 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR _Version 5.3B loop_ _Task "Data Processing" stop_ save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.74 loop_ _Task "Peak Picking" stop_ _Details "T. Goddard and T. Kneller" save_ save_AutoAssign _Saveframe_category software _Name AutoAssign _Version 1.5 loop_ _Task "Automatic Assignments" stop_ _Details ; Zimmerman, D., Kulikowski, C.A, Huang, Y., Reng, W., Tashiro, M., Shimotakahara, S., Chien, C., Powers, R. and Montelione, G.T. J. Mol. Biol. 269, 592-610 In-house developed software for automatically assigning the carbonyl, alpha and beta carbons and backbone nitrogen chemical shifts. ; save_ save_AutoStructure _Saveframe_category software _Name AutoStructure _Version 1.0 loop_ _Task "Automatic Assignments of NOESY peaks" "Structure determination" stop_ _Details ; Y.J. Huang, R. Tejero and G.T. Montelione unpublished In-house developed iterative program for automatic assignments of NOESY cross-peaks and structure determination. ; save_ save_Dyana _Saveframe_category software _Name Dyana _Version 1.5 loop_ _Task "Structure determination using torsion angle dynamics" stop_ _Details ; Guntert, P., Mumenthaler, C. and Wuthrich, K. (1977) J. Mol. Biol. 273, 283-298 ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 15N-1H HSQC 13C-!H HSQC TOCSY NOESY 2QF-COSY HNCO HN(CA)CO CANH H(CA)NH H(CA)(CO)NH (CA)(C0)NH CBCANH CNCA(CO)NH H_HCC(CO)NH-TOCSY C_HCC(CO)NH-TOCSY HCCH-COSY 15N edited PFG NOESY 13C edited PFG NOESY 13C X-filtered NOESY 13C-15N X-filtered NOESY ; _Details ; four channels ; save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 0.1 n/a temperature 281 0.2 K 'ionic strength' 0.12 0.01 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shifts _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $15N,13C-GlyTM1bZip stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "GlyTM1bZip subunit A" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 GLY HA2 H 3.91 0.02 1 2 1 GLY HA3 H 3.91 0.02 1 3 1 GLY C C 169.63 0.05 1 4 1 GLY CA C 43.08 0.05 1 5 2 ALA H H 8.81 0.02 1 6 2 ALA HA H 4.41 0.02 1 7 2 ALA HB H 1.46 0.02 1 8 2 ALA C C 178.03 0.05 1 9 2 ALA CA C 52.48 0.05 1 10 2 ALA CB C 18.88 0.05 1 11 2 ALA N N 123.19 0.05 1 12 3 GLY H H 8.73 0.02 1 13 3 GLY HA2 H 4.05 0.02 1 14 3 GLY HA3 H 4.05 0.02 1 15 3 GLY C C 174.13 0.05 1 16 3 GLY CA C 45.08 0.05 1 17 3 GLY N N 108.09 0.05 1 18 4 SER H H 8.41 0.02 1 19 4 SER HA H 4.51 0.02 1 20 4 SER HB2 H 3.96 0.02 2 21 4 SER HB3 H 3.89 0.02 2 22 4 SER C C 174.73 0.05 1 23 4 SER CA C 58.38 0.05 1 24 4 SER CB C 63.38 0.05 1 25 4 SER N N 115.19 0.05 1 26 5 SER H H 8.64 0.02 1 27 5 SER HA H 4.53 0.02 1 28 5 SER HB2 H 3.98 0.02 1 29 5 SER HB3 H 3.98 0.02 1 30 5 SER C C 174.93 0.05 1 31 5 SER CA C 58.58 0.05 1 32 5 SER CB C 63.18 0.05 1 33 5 SER N N 117.69 0.05 1 34 6 SER H H 8.45 0.02 1 35 6 SER HA H 4.47 0.02 1 36 6 SER HB2 H 4.09 0.02 2 37 6 SER HB3 H 3.94 0.02 2 38 6 SER C C 174.93 0.05 1 39 6 SER CA C 58.88 0.05 1 40 6 SER CB C 63.28 0.05 1 41 6 SER N N 117.99 0.05 1 42 7 LEU H H 8.44 0.02 1 43 7 LEU HA H 4.21 0.02 1 44 7 LEU HB2 H 1.72 0.02 1 45 7 LEU HB3 H 1.72 0.02 1 46 7 LEU HG H 1.63 0.02 1 47 7 LEU HD1 H 0.95 0.02 1 48 7 LEU HD2 H 0.95 0.02 1 49 7 LEU C C 178.03 0.05 1 50 7 LEU CA C 57.08 0.05 1 51 7 LEU CB C 41.58 0.05 1 52 7 LEU CD1 C 23.68 0.05 2 53 7 LEU CD2 C 30.38 0.05 2 54 7 LEU N N 123.09 0.05 1 55 8 GLU H H 8.35 0.02 1 56 8 GLU HA H 4.05 0.02 1 57 8 GLU HB2 H 2.12 0.02 2 58 8 GLU HB3 H 2.03 0.02 2 59 8 GLU HG2 H 2.36 0.02 1 60 8 GLU HG3 H 2.36 0.02 1 61 8 GLU C C 178.23 0.05 1 62 8 GLU CA C 59.18 0.05 1 63 8 GLU CB C 28.78 0.05 1 64 8 GLU CG C 35.78 0.05 1 65 8 GLU N N 117.99 0.05 1 66 9 ALA H H 8.04 0.02 1 67 9 ALA HA H 4.14 0.02 1 68 9 ALA HB H 1.56 0.02 1 69 9 ALA C C 180.83 0.05 1 70 9 ALA CA C 55.08 0.05 1 71 9 ALA CB C 17.88 0.05 1 72 9 ALA N N 120.89 0.05 1 73 10 VAL H H 8.03 0.02 1 74 10 VAL HA H 3.85 0.02 1 75 10 VAL HB H 2.22 0.02 1 76 10 VAL HG1 H 1.13 0.02 2 77 10 VAL HG2 H 0.99 0.02 2 78 10 VAL C C 177.53 0.05 1 79 10 VAL CA C 65.78 0.05 1 80 10 VAL CB C 31.48 0.05 1 81 10 VAL CG1 C 21.88 0.05 2 82 10 VAL CG2 C 22.18 0.05 2 83 10 VAL N N 117.89 0.05 1 84 11 ARG H H 8.37 0.02 1 85 11 ARG HA H 3.98 0.02 1 86 11 ARG HB2 H 1.92 0.02 1 87 11 ARG HB3 H 1.92 0.02 1 88 11 ARG HG2 H 1.65 0.02 2 89 11 ARG HG3 H 1.80 0.02 2 90 11 ARG HD2 H 3.20 0.02 1 91 11 ARG HD3 H 3.20 0.02 1 92 11 ARG C C 179.13 0.05 1 93 11 ARG CA C 59.68 0.05 1 94 11 ARG CB C 29.88 0.05 1 95 11 ARG CG C 27.88 0.05 1 96 11 ARG CD C 43.38 0.05 1 97 11 ARG N N 119.29 0.05 1 98 12 ARG H H 8.10 0.02 1 99 12 ARG HA H 4.07 0.02 1 100 12 ARG HB2 H 1.98 0.02 1 101 12 ARG HB3 H 1.98 0.02 1 102 12 ARG HG2 H 1.67 0.02 2 103 12 ARG HG3 H 1.87 0.02 2 104 12 ARG HD2 H 3.24 0.02 1 105 12 ARG HD3 H 3.24 0.02 1 106 12 ARG C C 178.33 0.05 1 107 12 ARG CA C 59.28 0.05 1 108 12 ARG CB C 29.88 0.05 1 109 12 ARG CG C 27.58 0.05 1 110 12 ARG CD C 43.18 0.05 1 111 12 ARG N N 118.59 0.05 1 112 13 LYS H H 7.84 0.02 1 113 13 LYS HA H 4.23 0.02 1 114 13 LYS HB2 H 2.11 0.02 2 115 13 LYS HB3 H 2.02 0.02 2 116 13 LYS HG2 H 1.54 0.02 1 117 13 LYS HG3 H 1.54 0.02 1 118 13 LYS HD2 H 1.76 0.02 1 119 13 LYS HD3 H 1.76 0.02 1 120 13 LYS HE2 H 2.96 0.02 1 121 13 LYS HE3 H 2.96 0.02 1 122 13 LYS C C 178.33 0.05 1 123 13 LYS CA C 58.78 0.05 1 124 13 LYS CB C 31.78 0.05 1 125 13 LYS CG C 24.58 0.05 1 126 13 LYS CD C 29.18 0.05 1 127 13 LYS CE C 41.68 0.05 1 128 13 LYS N N 121.09 0.05 1 129 14 ILE H H 8.38 0.02 1 130 14 ILE HA H 3.60 0.02 1 131 14 ILE HB H 1.96 0.02 1 132 14 ILE HG12 H 1.81 0.02 2 133 14 ILE HG13 H 1.67 0.02 2 134 14 ILE HG2 H 0.90 0.02 1 135 14 ILE HD1 H 0.96 0.02 1 136 14 ILE C C 176.63 0.05 1 137 14 ILE CA C 65.58 0.05 1 138 14 ILE CB C 37.38 0.05 1 139 14 ILE CG1 C 30.58 0.05 1 140 14 ILE CG2 C 16.28 0.05 1 141 14 ILE CD1 C 13.78 0.05 1 142 14 ILE N N 118.69 0.05 1 143 15 ARG H H 7.79 0.02 1 144 15 ARG HA H 4.24 0.02 1 145 15 ARG HB2 H 1.98 0.02 2 146 15 ARG HB3 H 1.34 0.02 2 147 15 ARG HG2 H 1.83 0.02 2 148 15 ARG HG3 H 1.67 0.02 2 149 15 ARG HD2 H 3.28 0.02 1 150 15 ARG HD3 H 3.28 0.02 1 151 15 ARG C C 178.63 0.05 1 152 15 ARG CA C 59.08 0.05 1 153 15 ARG CB C 29.58 0.05 1 154 15 ARG CG C 27.28 0.05 1 155 15 ARG CD C 43.08 0.05 1 156 15 ARG N N 118.29 0.05 1 157 16 SER H H 8.13 0.02 1 158 16 SER HA H 4.36 0.02 1 159 16 SER HB2 H 4.08 0.02 1 160 16 SER HB3 H 4.08 0.02 1 161 16 SER C C 177.23 0.05 1 162 16 SER CA C 61.28 0.05 1 163 16 SER CB C 62.58 0.05 1 164 16 SER N N 113.49 0.05 1 165 17 LEU H H 8.40 0.02 1 166 17 LEU HA H 4.15 0.02 1 167 17 LEU HB2 H 1.34 0.02 2 168 17 LEU HB3 H 2.13 0.02 2 169 17 LEU HG H 1.87 0.02 1 170 17 LEU HD1 H 0.99 0.02 2 171 17 LEU HD2 H 0.92 0.02 2 172 17 LEU C C 179.13 0.05 1 173 17 LEU CA C 57.68 0.05 1 174 17 LEU CB C 43.18 0.05 1 175 17 LEU CG C 27.38 0.05 1 176 17 LEU CD1 C 27.38 0.05 2 177 17 LEU CD2 C 30.38 0.05 2 178 17 LEU N N 122.09 0.05 1 179 18 GLN H H 8.84 0.02 1 180 18 GLN HA H 4.01 0.02 1 181 18 GLN HB2 H 2.07 0.02 2 182 18 GLN HB3 H 2.42 0.02 2 183 18 GLN HG2 H 2.38 0.02 2 184 18 GLN HG3 H 2.59 0.02 2 185 18 GLN HE21 H 6.89 0.02 2 186 18 GLN HE22 H 7.24 0.02 2 187 18 GLN C C 178.73 0.05 1 188 18 GLN CA C 59.18 0.05 1 189 18 GLN CB C 28.18 0.05 1 190 18 GLN CG C 34.88 0.05 1 191 18 GLN N N 119.09 0.05 1 192 18 GLN NE2 N 111.70 0.05 1 193 19 GLU H H 8.29 0.02 1 194 19 GLU HA H 4.18 0.02 1 195 19 GLU HB2 H 2.27 0.02 2 196 19 GLU HB3 H 2.00 0.02 2 197 19 GLU HG2 H 2.55 0.02 2 198 19 GLU HG3 H 2.35 0.02 2 199 19 GLU C C 179.03 0.05 1 200 19 GLU CA C 59.38 0.05 1 201 19 GLU CB C 28.98 0.05 1 202 19 GLU CG C 36.48 0.05 1 203 19 GLU N N 119.79 0.05 1 204 20 GLN H H 8.36 0.02 1 205 20 GLN HA H 4.32 0.02 1 206 20 GLN HB2 H 2.15 0.02 2 207 20 GLN HB3 H 2.25 0.02 2 208 20 GLN HG2 H 2.48 0.02 2 209 20 GLN HG3 H 2.64 0.02 2 210 20 GLN HE21 H 6.93 0.02 2 211 20 GLN HE22 H 7.48 0.02 2 212 20 GLN C C 177.93 0.05 1 213 20 GLN CA C 58.68 0.05 1 214 20 GLN CB C 28.38 0.05 1 215 20 GLN CG C 33.48 0.05 1 216 20 GLN N N 119.29 0.05 1 217 20 GLN NE2 N 111.20 0.05 1 218 21 ASN H H 8.74 0.02 1 219 21 ASN HA H 4.41 0.02 1 220 21 ASN HB2 H 3.23 0.02 2 221 21 ASN HB3 H 2.78 0.02 2 222 21 ASN HD21 H 6.80 0.02 2 223 21 ASN HD22 H 7.64 0.02 2 224 21 ASN C C 176.23 0.05 1 225 21 ASN CA C 56.78 0.05 1 226 21 ASN CB C 38.28 0.05 1 227 21 ASN N N 119.49 0.05 1 228 21 ASN ND2 N 106.40 0.05 1 229 22 TYR H H 8.15 0.02 1 230 22 TYR HA H 4.45 0.02 1 231 22 TYR HB2 H 3.24 0.02 1 232 22 TYR HB3 H 3.24 0.02 1 233 22 TYR HD1 H 7.09 0.02 1 234 22 TYR HD2 H 7.09 0.02 1 235 22 TYR HE1 H 6.84 0.02 1 236 22 TYR HE2 H 6.84 0.02 1 237 22 TYR C C 177.73 0.05 1 238 22 TYR CA C 60.18 0.05 1 239 22 TYR CB C 37.78 0.05 1 240 22 TYR N N 119.29 0.05 1 241 23 HIS H H 7.94 0.02 1 242 23 HIS HA H 4.44 0.02 1 243 23 HIS HB2 H 3.40 0.02 1 244 23 HIS HB3 H 3.40 0.02 1 245 23 HIS HD2 H 7.14 0.02 1 246 23 HIS HE1 H 7.93 0.02 1 247 23 HIS C C 177.93 0.05 1 248 23 HIS CA C 58.88 0.05 1 249 23 HIS CB C 28.68 0.05 1 250 23 HIS N N 116.89 0.05 1 251 24 LEU H H 8.68 0.02 1 252 24 LEU HA H 3.96 0.02 1 253 24 LEU HB2 H 2.14 0.02 2 254 24 LEU HB3 H 1.36 0.02 2 255 24 LEU HG H 1.98 0.02 1 256 24 LEU HD1 H 1.05 0.02 2 257 24 LEU HD2 H 0.91 0.02 2 258 24 LEU C C 178.43 0.05 1 259 24 LEU CA C 57.98 0.05 1 260 24 LEU CB C 43.38 0.05 1 261 24 LEU CG C 26.98 0.05 1 262 24 LEU CD1 C 26.48 0.05 2 263 24 LEU CD2 C 21.48 0.05 2 264 24 LEU N N 119.89 0.05 1 265 25 GLU H H 8.90 0.02 1 266 25 GLU HA H 3.98 0.02 1 267 25 GLU HB2 H 2.23 0.02 2 268 25 GLU HB3 H 2.00 0.02 2 269 25 GLU HG2 H 2.52 0.02 2 270 25 GLU HG3 H 2.31 0.02 2 271 25 GLU C C 179.93 0.05 1 272 25 GLU CA C 59.68 0.05 1 273 25 GLU CB C 28.88 0.05 1 274 25 GLU CG C 36.38 0.05 1 275 25 GLU N N 118.99 0.05 1 276 26 ASN H H 7.85 0.02 1 277 26 ASN HA H 4.47 0.02 1 278 26 ASN HB2 H 2.81 0.02 2 279 26 ASN HB3 H 2.95 0.02 2 280 26 ASN HD21 H 5.86 0.02 2 281 26 ASN HD22 H 7.51 0.02 2 282 26 ASN C C 177.63 0.05 1 283 26 ASN CA C 55.78 0.05 1 284 26 ASN CB C 37.48 0.05 1 285 26 ASN N N 118.39 0.05 1 286 26 ASN ND2 N 111.60 0.05 1 287 27 GLU H H 8.19 0.02 1 288 27 GLU HA H 4.47 0.02 1 289 27 GLU HB2 H 2.18 0.02 2 290 27 GLU HB3 H 2.06 0.02 2 291 27 GLU HG2 H 2.58 0.02 2 292 27 GLU HG3 H 2.15 0.02 2 293 27 GLU C C 177.73 0.05 1 294 27 GLU CA C 58.38 0.05 1 295 27 GLU CB C 29.98 0.05 1 296 27 GLU CG C 35.68 0.05 1 297 27 GLU N N 123.29 0.05 1 298 28 VAL H H 8.77 0.02 1 299 28 VAL HA H 3.41 0.02 1 300 28 VAL HB H 2.15 0.02 1 301 28 VAL HG1 H 0.92 0.02 2 302 28 VAL HG2 H 1.07 0.02 2 303 28 VAL C C 177.13 0.05 1 304 28 VAL CA C 67.58 0.05 1 305 28 VAL CB C 31.38 0.05 1 306 28 VAL CG1 C 23.08 0.05 2 307 28 VAL CG2 C 25.28 0.05 2 308 28 VAL N N 119.59 0.05 1 309 29 ALA H H 7.83 0.02 1 310 29 ALA HA H 4.05 0.02 1 311 29 ALA HB H 1.53 0.02 1 312 29 ALA C C 180.03 0.05 1 313 29 ALA CA C 54.98 0.05 1 314 29 ALA CB C 17.78 0.05 1 315 29 ALA N N 119.09 0.05 1 316 30 ARG H H 8.06 0.02 1 317 30 ARG HA H 4.00 0.02 1 318 30 ARG HB2 H 1.91 0.02 2 319 30 ARG HB3 H 2.19 0.02 2 320 30 ARG HG2 H 1.64 0.02 2 321 30 ARG HG3 H 1.36 0.02 2 322 30 ARG HD2 H 3.48 0.02 2 323 30 ARG HD3 H 3.01 0.02 2 324 30 ARG C C 179.23 0.05 1 325 30 ARG CA C 58.98 0.05 1 326 30 ARG CB C 30.58 0.05 1 327 30 ARG CG C 27.28 0.05 1 328 30 ARG CD C 42.38 0.05 1 329 30 ARG N N 119.29 0.05 1 330 31 LEU H H 8.55 0.02 1 331 31 LEU HA H 4.02 0.02 1 332 31 LEU HB2 H 2.01 0.02 2 333 31 LEU HB3 H 1.37 0.02 2 334 31 LEU HG H 1.68 0.02 1 335 31 LEU HD1 H 0.86 0.02 2 336 31 LEU HD2 H 0.97 0.02 2 337 31 LEU C C 178.83 0.05 1 338 31 LEU CA C 57.48 0.05 1 339 31 LEU CB C 43.68 0.05 1 340 31 LEU CG C 27.38 0.05 1 341 31 LEU CD1 C 23.48 0.05 2 342 31 LEU CD2 C 27.48 0.05 2 343 31 LEU N N 120.19 0.05 1 344 32 LYS H H 9.10 0.02 1 345 32 LYS HA H 3.85 0.02 1 346 32 LYS HB2 H 1.87 0.02 1 347 32 LYS HB3 H 1.87 0.02 1 348 32 LYS HG2 H 1.35 0.02 2 349 32 LYS HG3 H 1.81 0.02 2 350 32 LYS HD2 H 1.66 0.02 2 351 32 LYS HD3 H 1.50 0.02 2 352 32 LYS HE2 H 2.85 0.02 1 353 32 LYS HE3 H 2.85 0.02 1 354 32 LYS C C 179.13 0.05 1 355 32 LYS CA C 60.78 0.05 1 356 32 LYS CB C 32.28 0.05 1 357 32 LYS CG C 27.38 0.05 1 358 32 LYS CD C 29.58 0.05 1 359 32 LYS CE C 41.58 0.05 1 360 32 LYS N N 118.09 0.05 1 361 33 LYS H H 7.44 0.02 1 362 33 LYS HA H 4.16 0.02 1 363 33 LYS HB2 H 1.93 0.02 2 364 33 LYS HB3 H 2.00 0.02 2 365 33 LYS HG2 H 1.62 0.02 2 366 33 LYS HG3 H 1.48 0.02 2 367 33 LYS HD2 H 1.74 0.02 1 368 33 LYS HD3 H 1.74 0.02 1 369 33 LYS HE2 H 3.01 0.02 1 370 33 LYS HE3 H 3.01 0.02 1 371 33 LYS C C 178.73 0.05 1 372 33 LYS CA C 58.68 0.05 1 373 33 LYS CB C 31.98 0.05 1 374 33 LYS CG C 25.18 0.05 1 375 33 LYS CD C 29.08 0.05 1 376 33 LYS CE C 41.68 0.05 1 377 33 LYS N N 116.89 0.05 1 378 34 LEU H H 7.50 0.02 1 379 34 LEU HA H 4.22 0.02 1 380 34 LEU HB2 H 1.67 0.02 2 381 34 LEU HB3 H 2.11 0.02 2 382 34 LEU HG H 1.87 0.02 1 383 34 LEU HD1 H 0.93 0.02 2 384 34 LEU HD2 H 1.00 0.02 2 385 34 LEU C C 178.83 0.05 1 386 34 LEU CA C 57.08 0.05 1 387 34 LEU CB C 42.38 0.05 1 388 34 LEU CG C 26.78 0.05 1 389 34 LEU CD1 C 22.88 0.05 2 390 34 LEU CD2 C 25.18 0.05 2 391 34 LEU N N 118.09 0.05 1 392 35 VAL H H 7.85 0.02 1 393 35 VAL HA H 4.11 0.02 1 394 35 VAL HB H 2.28 0.02 1 395 35 VAL HG1 H 0.97 0.02 2 396 35 VAL HG2 H 1.03 0.02 2 397 35 VAL C C 176.43 0.05 1 398 35 VAL CA C 62.68 0.05 1 399 35 VAL CB C 32.08 0.05 1 400 35 VAL CG1 C 21.58 0.05 1 401 35 VAL CG2 C 21.58 0.05 1 402 35 VAL N N 113.09 0.05 1 403 36 GLY H H 7.92 0.02 1 404 36 GLY HA2 H 3.92 0.02 2 405 36 GLY HA3 H 4.13 0.02 2 406 36 GLY C C 174.23 0.05 1 407 36 GLY CA C 45.48 0.05 1 408 36 GLY N N 108.39 0.05 1 409 37 GLU H H 8.01 0.02 1 410 37 GLU HA H 4.40 0.02 1 411 37 GLU HB2 H 2.07 0.02 2 412 37 GLU HB3 H 1.78 0.02 2 413 37 GLU HG2 H 2.29 0.02 1 414 37 GLU HG3 H 2.29 0.02 1 415 37 GLU C C 175.03 0.05 1 416 37 GLU CA C 55.88 0.05 1 417 37 GLU CB C 31.18 0.05 1 418 37 GLU CG C 36.38 0.05 1 419 37 GLU N N 119.99 0.05 1 420 38 ARG H H 8.09 0.02 1 421 38 ARG HA H 4.16 0.02 1 422 38 ARG HB2 H 1.74 0.02 2 423 38 ARG HB3 H 1.86 0.02 2 424 38 ARG HG2 H 1.34 0.02 2 425 38 ARG HG3 H 1.66 0.02 2 426 38 ARG HD2 H 3.22 0.02 2 427 38 ARG HD3 H 2.94 0.02 2 428 38 ARG C C 180.73 0.05 1 429 38 ARG CA C 57.18 0.05 1 430 38 ARG CB C 31.18 0.05 1 431 38 ARG CG C 27.38 0.05 1 432 38 ARG CD C 42.38 0.05 1 433 38 ARG N N 126.69 0.05 1 stop_ save_ ######################## # Coupling constants # ######################## save_GlyTM1bZip,_H_values _Saveframe_category coupling_constants _Details ; Residues G1: No amide A2 - two low intensity E20 degenerate with R11 N21 degenerate with V28 ; loop_ _Sample_label $15N,13C-GlyTM1bZip stop_ _Sample_conditions_label $conditions_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name "GlyTM1bZip subunit A" loop_ _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_value_error 3JHNHA 3 GLY H 3 GLY HA 6 0.1 3JHNHA 4 SER H 4 SER HA 6 0.1 3JHNHA 5 SER H 5 SER HA 5.4 0.1 3JHNHA 6 SER H 6 SER HA 4.5 0.1 3JHNHA 7 LEU H 7 LEU HA 4.6 0.1 3JHNHA 8 GLU H 8 GLU HA 4.3 0.1 3JHNHA 9 ALA H 9 ALA HA 4 0.1 3JHNHA 10 VAL H 10 VAL HA 5.1 0.1 3JHNHA 11 ARG H 11 ARG HA 4 0.1 3JHNHA 12 ARG H 12 ARG HA 5 0.1 3JHNHA 13 LYS H 13 LYS HA 4.6 0.1 3JHNHA 14 ILE H 14 ILE HA 4.8 0.1 3JHNHA 15 ARG H 15 ARG HA 4.4 0.1 3JHNHA 16 SER H 16 SER HA 4 0.1 3JHNHA 17 LEU H 17 LEU HA 5.1 0.1 3JHNHA 18 GLN H 18 GLN HA 4.3 0.1 3JHNHA 19 GLU H 19 GLU HA 4.4 0.1 3JHNHA 22 TYR H 22 TYR HA 4.9 0.1 3JHNHA 23 HIS H 23 HIS HA 4.5 0.1 3JHNHA 24 LEU H 24 LEU HA 4.5 0.1 3JHNHA 25 GLU H 25 GLU HA 4 0.1 3JHNHA 26 ASN H 26 ASN HA 4 0.1 3JHNHA 27 GLU H 27 GLU HA 3.8 0.1 3JHNHA 28 VAL H 28 VAL HA 3 0.1 3JHNHA 29 ALA H 29 ALA HA 3 0.1 3JHNHA 30 ARG H 30 ARG HA 3 0.1 3JHNHA 31 LEU H 31 LEU HA 4.9 0.1 3JHNHA 32 LYS H 32 LYS HA 4 0.1 3JHNHA 33 LYS H 33 LYS HA 5 0.1 3JHNHA 34 LEU H 34 LEU HA 1 0.1 3JHNHA 35 VAL H 35 VAL HA 6.7 0.1 3JHNHA 36 GLY H 36 GLY HA 5.6 0.1 3JHNHA 37 GLU H 37 GLU HA 7.9 0.1 3JHNHA 38 ARG H 38 ARG HA 7.3 0.1 stop_ save_