data_5610 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The Structure of the Carboxyl Terminus of Striated alpha-Tropomyosin in Solution Reveals an Unusual Parallel Arrangement of Interacting alpha-Helices ; _BMRB_accession_number 5610 _BMRB_flat_file_name bmr5610.str _Entry_type original _Submission_date 2002-12-06 _Accession_date 2002-12-09 _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 Swapna G.V.T. . . 3 Huang Yuanpeng . . 4 Palm Thomas . . 5 Graboski Janet . . 6 Montelione Gaetano T. . 7 Hitchcock-DeGregori Sarah E. . stop_ 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" 221 "13C chemical shifts" 162 "15N chemical shifts" 37 "coupling constants" 26 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-02-21 original author 'original release' 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 . _Citation_title ; The Structure of the Carboxyl Terminus of Striated alpha-Tropomyosin in Solution Reveals an Unusual Parallel Arrangement of Interacting alpha-Helices ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12534273 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Greenfield Norma J. . 2 Swapna G.V.T. . . 3 Huang Yuanpeng . . 4 Palm Thomas . . 5 Graboski S. . . 6 Montelione Gaetano T. . 7 Hitchcock-DeGregori Sarah E. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 42 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 614 _Page_last 619 _Year 2003 _Details . loop_ _Keyword 'coiled coil' tropomyosin 'troponin interaction site' stop_ save_ ################################## # Molecular system description # ################################## save_system_TM9a251-284 _Saveframe_category molecular_system _Mol_system_name 'C terminus of rat striated muscle alpha tropomyosin encoded by exon 9a' _Abbreviation_common TM9a251-284 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'tropomyosin peptide fragment, chain 1' $Tm9a251-284 'tropomyosin peptide fragment, chain 2' $Tm9a251-284 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'tropomyosin peptide fragment, chain 1' 1 'tropomyosin peptide fragment, chain 2' stop_ loop_ _Biological_function 'actin regulatory protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Tm9a251-284 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'residues 251-284 of rat striated muscle tropomyosin' _Name_variant N279K _Abbreviation_common Tm9a251-284 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 37 _Mol_residue_sequence ; GCGKSIDDLEDELYAQKLKY KAISEELDHALKDMTSI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLY 2 2 CYS 3 3 GLY 4 251 LYS 5 252 SER 6 253 ILE 7 254 ASP 8 255 ASP 9 256 LEU 10 257 GLU 11 258 ASP 12 259 GLU 13 260 LEU 14 261 TYR 15 262 ALA 16 263 GLN 17 264 LYS 18 265 LEU 19 266 LYS 20 267 TYR 21 268 LYS 22 269 ALA 23 270 ILE 24 271 SER 25 272 GLU 26 273 GLU 27 274 LEU 28 275 ASP 29 276 HIS 30 277 ALA 31 278 LEU 32 279 LYS 33 280 ASP 34 281 MET 35 282 THR 36 283 SER 37 284 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 BMRB 7080 GlyTM9a(251-284) 100.00 37 100.00 100.00 4.88e-16 PDB 1C1G "Crystal Structure Of Tropomyosin At 7 Angstroms Resolution In The Spermine-Induced Crystal Form" 91.89 284 97.06 97.06 5.82e-12 PDB 1MV4 "Tm9a251-284: A Peptide Model Of The C-Terminus Of A Rat Striated Alpha Tropomyosin" 100.00 37 100.00 100.00 4.88e-16 PDB 2D3E "Crystal Structure Of The C-Terminal Fragment Of Rabbit Skeletal Alpha-Tropomyosin" 91.89 134 97.06 97.06 3.40e-12 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 37 100.00 100.00 4.88e-16 PDB 2TMA "Tropomyosin Crystal Structure And Muscle Regulation. Appendix. Construction Of An Atomic Model For Tropomyosin And Implications" 91.89 284 97.06 97.06 5.47e-12 PDB 2W49 "Isometrically Contracting Insect Asynchronous Flight Muscle" 91.89 277 97.06 97.06 5.07e-12 PDB 2W4U "Isometrically Contracting Insect Asynchronous Flight Muscle Quick Frozen After A Length Step" 91.89 277 97.06 97.06 5.07e-12 DBJ BAB21978 "unnamed protein product [Mus musculus]" 91.89 284 97.06 97.06 5.76e-12 DBJ BAC36973 "unnamed protein product [Mus musculus]" 91.89 284 97.06 97.06 5.64e-12 DBJ BAC85248 "unnamed protein product [Homo sapiens]" 91.89 217 97.06 97.06 3.83e-12 DBJ BAD86590 "tropomyosin 1 [Bos taurus]" 91.89 284 97.06 97.06 5.19e-12 DBJ BAE40499 "unnamed protein product [Mus musculus]" 91.89 284 97.06 97.06 5.76e-12 EMBL CAA26259 "unnamed protein product [Rattus norvegicus]" 91.89 204 97.06 97.06 3.33e-12 EMBL CAA28393 "unnamed protein product [Coturnix coturnix]" 91.89 284 97.06 97.06 5.14e-12 EMBL CAA34344 "alpha-tropomyosin [Coturnix coturnix]" 91.89 284 97.06 97.06 5.14e-12 EMBL CAA41056 "alpha-tropomyosin of skeletal fast muscle [Gallus gallus]" 91.89 284 97.06 97.06 5.14e-12 EMBL CAA43577 "alpha-skeletal tropomyosin [Xenopus laevis]" 91.89 284 97.06 97.06 7.32e-12 GB AAA18096 "alpha-tropomyosin [Rana temporaria]" 91.89 284 97.06 97.06 6.13e-12 GB AAA21801 "striated-muscle alpha tropomyosin [Rattus norvegicus]" 91.89 284 100.00 100.00 1.04e-12 GB AAA21803 "minor striated-muscle alpha tropomyosin [Rattus norvegicus]" 91.89 294 100.00 100.00 1.32e-12 GB AAA48577 "alpha-tropomyosin [Gallus gallus]" 91.89 284 97.06 97.06 5.14e-12 GB AAA48610 "alpha-tropomyosin [Gallus gallus]" 91.89 284 97.06 97.06 5.30e-12 PRF 1105305B "tropomyosin alpha" 91.89 204 97.06 97.06 3.33e-12 REF NP_001013608 "tropomyosin alpha-1 chain [Bos taurus]" 91.89 284 97.06 97.06 5.19e-12 REF NP_001018005 "tropomyosin alpha-1 chain isoform Tpm1.1st [Homo sapiens]" 91.89 284 97.06 97.06 5.70e-12 REF NP_001029247 "tropomyosin alpha-1 chain isoform Tpm1.13 [Rattus norvegicus]" 91.89 248 97.06 97.06 2.49e-12 REF NP_001090952 "tropomyosin alpha-1 chain [Sus scrofa]" 91.89 284 97.06 97.06 5.30e-12 REF NP_001099158 "tropomyosin alpha-1 chain [Oryctolagus cuniculus]" 91.89 284 97.06 97.06 5.76e-12 SP P04268 "RecName: Full=Tropomyosin alpha-1 chain; AltName: Full=Alpha-tropomyosin; AltName: Full=Tropomyosin-1 [Gallus gallus]" 91.89 284 97.06 97.06 5.14e-12 SP P04692 "RecName: Full=Tropomyosin alpha-1 chain; AltName: Full=Alpha-tropomyosin; AltName: Full=Tropomyosin-1 [Rattus norvegicus]" 91.89 284 97.06 97.06 5.76e-12 SP P09493 "RecName: Full=Tropomyosin alpha-1 chain; AltName: Full=Alpha-tropomyosin; AltName: Full=Tropomyosin-1 [Homo sapiens]" 91.89 284 97.06 97.06 5.70e-12 SP P13105 "RecName: Full=Tropomyosin alpha-1 chain; AltName: Full=Alpha-tropomyosin; AltName: Full=Tropomyosin-1 [Rana temporaria]" 91.89 284 97.06 97.06 6.13e-12 SP P42639 "RecName: Full=Tropomyosin alpha-1 chain; AltName: Full=Alpha-tropomyosin; AltName: Full=Tropomyosin-1 [Sus scrofa]" 91.89 284 97.06 97.06 5.30e-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 _Variant _Tissue $Tm9a251-284 Rat 10116 Eukaryota Metazoa Rattus norvegicus N279K 'striated muscle' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $Tm9a251-284 'recombinant technology' 'E coli' Escherichia coli BL21 DE3 plasmid pSBET-HTb 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 $Tm9a251-284 . mM 0.4 1.2 '[U-98% 15N]' NaCl 100 mM . . . 'Na phosphate' 10 mM . . . stop_ save_ save_Sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Tm9a251-284 . mM 0.4 1.2 '[U-99% 13C; U-98% 15N]' stop_ save_ save_Sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Tm9a251-284 0.4 mM '[U-98% 15N; U-99% 13C]' $Tm9a251-284 0.4 mM . stop_ save_ save_Sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Tm9a251-284 0.8 mM . stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR _Version . loop_ _Task 'data collection' processing stop_ _Details . save_ save_AutoStructure _Saveframe_category software _Name AutoStruct _Version . loop_ _Task 'NOE assignments' 'structural calculations' stop_ _Details ; In house software for automatic structure calculations. (Calls the program DYANA as a subroutine). Huang, Y.J. (2002) Automated determination of protein structures from NMR data by iterative analysis of self-consistent contact patterns. Ph.D. Thesis, Rutgers University, New Brunswick, NJ. ; save_ save_DYANA _Saveframe_category software _Name DYANA _Version . loop_ _Task 'structural calculations' stop_ _Details ; Guntert, P., Mumenthaler, C. and Wuthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273, 283-298. ; save_ save_Sparky _Saveframe_category software _Name SPARKY _Version . loop_ _Task 'peak selection' 'spectra alignments' stop_ _Details ; Goddard, T and Kneller, T. University of California at San Francisco, unpublished. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N-1H_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-1H HSQC' _Sample_label . save_ save_(HA)(CA)CO(CA)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name (HA)(CA)CO(CA)NH _Sample_label . save_ save_HNC0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNC0 _Sample_label . save_ save_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_CBCANH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_CBCA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HA(CA)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name HA(CA)NH _Sample_label . save_ save_HA(CA)(CO)CANH_9 _Saveframe_category NMR_applied_experiment _Experiment_name HA(CA)(CO)CANH _Sample_label . save_ save_CCH-COSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name CCH-COSY _Sample_label . save_ save_HCCH-COSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _Sample_label . save_ save_2QF-COSY_12 _Saveframe_category NMR_applied_experiment _Experiment_name 2QF-COSY _Sample_label . save_ save_15N_Edited_NOESY_13 _Saveframe_category NMR_applied_experiment _Experiment_name '15N Edited NOESY' _Sample_label . save_ save_13C_Edited_NOESY_14 _Saveframe_category NMR_applied_experiment _Experiment_name '13C Edited NOESY' _Sample_label . save_ save_13C_X-Filtered_NOESY_15 _Saveframe_category NMR_applied_experiment _Experiment_name '13C X-Filtered NOESY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_Condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.12 0.01 M pH 6.5 0.1 n/a temperature 183 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $Sample_1 $Sample_2 $Sample_3 $Sample_4 stop_ _Sample_conditions_label $Condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'tropomyosin peptide fragment, chain 1' _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 GLY HA2 H 3.88 0.02 2 2 . 1 GLY HA3 H 3.881 0.02 2 3 . 1 GLY C C 174.7 0.05 1 4 . 1 GLY CA C 43.37 0.05 1 5 . 2 CYS H H 8.425 0.02 1 6 . 2 CYS HA H 4.878 0.02 1 7 . 2 CYS HB2 H 3.301 0.02 2 8 . 2 CYS HB3 H 2.827 0.02 2 9 . 2 CYS C C 175.7 0.05 1 10 . 2 CYS CA C 54.74 0.05 1 11 . 2 CYS CB C 40.88 0.05 1 12 . 2 CYS N N 119 0.05 1 13 . 3 GLY H H 8.657 0.02 1 14 . 3 GLY HA2 H 3.88 0.02 1 15 . 3 GLY HA3 H 4.091 0.02 1 16 . 3 GLY C C 173.7 0.05 1 17 . 3 GLY CA C 45.09 0.05 1 18 . 3 GLY N N 111.5 0.05 1 19 . 4 LYS H H 8.225 0.02 1 20 . 4 LYS HA H 3.929 0.02 1 21 . 4 LYS HB2 H 1.75 0.02 2 22 . 4 LYS HB3 H 1.981 0.02 2 23 . 4 LYS HG2 H 1.385 0.02 1 24 . 4 LYS HG3 H 1.385 0.02 1 25 . 4 LYS HD2 H 1.615 0.02 2 26 . 4 LYS HD3 H 1.411 0.02 2 27 . 4 LYS HE2 H 2.755 0.02 2 28 . 4 LYS HE3 H 2.889 0.02 2 29 . 4 LYS C C 176.9 0.05 1 30 . 4 LYS CA C 58.16 0.05 1 31 . 4 LYS CB C 33.86 0.05 1 32 . 4 LYS CG C 25.14 0.05 1 33 . 4 LYS CD C 30 0.05 1 34 . 4 LYS CE C 42.04 0.05 1 35 . 4 LYS N N 121.6 0.05 1 36 . 5 SER H H 8.301 0.02 1 37 . 5 SER HA H 4.316 0.02 1 38 . 5 SER HB2 H 3.681 0.02 2 39 . 5 SER HB3 H 3.899 0.02 2 40 . 5 SER CA C 62.48 0.05 1 41 . 5 SER CB C 62.25 0.05 1 42 . 5 SER N N 114.6 0.05 1 43 . 6 ILE H H 8.175 0.02 1 44 . 6 ILE HA H 3.631 0.02 1 45 . 6 ILE HB H 1.68 0.02 1 46 . 6 ILE HG12 H 1.018 0.02 2 47 . 6 ILE HG13 H 1.581 0.02 2 48 . 6 ILE HG2 H 0.8201 0.02 1 49 . 6 ILE HD1 H 0.854 0.02 1 50 . 6 ILE CA C 64.4 0.05 1 51 . 6 ILE CB C 37.63 0.05 1 52 . 6 ILE CG1 C 29.28 0.05 1 53 . 6 ILE CG2 C 17.37 0.05 1 54 . 6 ILE CD1 C 12.78 0.05 1 55 . 6 ILE N N 119.4 0.05 1 56 . 7 ASP H H 8.833 0.02 1 57 . 7 ASP HA H 4.233 0.02 1 58 . 7 ASP HB2 H 2.697 0.02 2 59 . 7 ASP HB3 H 2.906 0.02 2 60 . 7 ASP CA C 57.33 0.05 1 61 . 7 ASP CB C 40.11 0.05 1 62 . 7 ASP N N 119.7 0.05 1 63 . 8 ASP H H 8.348 0.02 1 64 . 8 ASP HA H 4.363 0.02 1 65 . 8 ASP HB2 H 2.848 0.02 2 66 . 8 ASP HB3 H 2.523 0.02 2 67 . 8 ASP CA C 57.19 0.05 1 68 . 8 ASP CB C 40.02 0.05 1 69 . 8 ASP N N 119.1 0.05 1 70 . 9 LEU H H 7.702 0.02 1 71 . 9 LEU HA H 4.123 0.02 1 72 . 9 LEU HB2 H 2.005 0.02 2 73 . 9 LEU HB3 H 1.344 0.02 2 74 . 9 LEU HG H 1.714 0.02 2 75 . 9 LEU HD1 H 0.8336 0.02 2 76 . 9 LEU HD2 H 0.9235 0.02 2 77 . 9 LEU C C 179.2 0.05 1 78 . 9 LEU CA C 57.79 0.05 1 79 . 9 LEU CB C 43.13 0.05 1 80 . 9 LEU CG C 27.96 0.05 1 81 . 9 LEU CD1 C 24.18 0.05 1 82 . 9 LEU CD2 C 26.82 0.05 1 83 . 9 LEU N N 122.7 0.05 1 84 . 10 GLU H H 8.857 0.02 1 85 . 10 GLU HA H 4.079 0.02 1 86 . 10 GLU HB2 H 2.157 0.02 2 87 . 10 GLU HB3 H 1.998 0.02 2 88 . 10 GLU HG2 H 2.205 0.02 2 89 . 10 GLU HG3 H 2.477 0.02 2 90 . 10 GLU C C 180.7 0.05 1 91 . 10 GLU CA C 59.99 0.05 1 92 . 10 GLU CB C 28.97 0.05 1 93 . 10 GLU CG C 36.38 0.05 1 94 . 10 GLU N N 119.9 0.05 1 95 . 11 ASP H H 8.314 0.02 1 96 . 11 ASP HA H 4.539 0.02 1 97 . 11 ASP HB2 H 2.691 0.02 2 98 . 11 ASP HB3 H 2.894 0.02 2 99 . 11 ASP C C 179.3 0.05 1 100 . 11 ASP CA C 57.57 0.05 1 101 . 11 ASP CB C 40.2 0.05 1 102 . 11 ASP N N 121.4 0.05 1 103 . 12 GLU H H 8.174 0.02 1 104 . 12 GLU HA H 4.136 0.02 1 105 . 12 GLU HB2 H 2.176 0.02 2 106 . 12 GLU HB3 H 2.1 0.02 2 107 . 12 GLU HG2 H 2.233 0.02 2 108 . 12 GLU HG3 H 2.446 0.02 2 109 . 12 GLU C C 179.6 0.05 1 110 . 12 GLU CA C 59.51 0.05 1 111 . 12 GLU CB C 29.39 0.05 1 112 . 12 GLU CG C 36.45 0.05 1 113 . 12 GLU N N 123.1 0.05 1 114 . 13 LEU H H 8.857 0.02 1 115 . 13 LEU HA H 3.93 0.02 1 116 . 13 LEU HB2 H 1.632 0.02 2 117 . 13 LEU HB3 H 1.834 0.02 2 118 . 13 LEU HG H 1.552 0.02 2 119 . 13 LEU HD1 H 0.8566 0.02 2 120 . 13 LEU HD2 H 0.8654 0.02 2 121 . 13 LEU C C 178.5 0.05 1 122 . 13 LEU CA C 58.27 0.05 1 123 . 13 LEU CB C 41.77 0.05 1 124 . 13 LEU CG C 27.32 0.05 1 125 . 13 LEU CD1 C 24.12 0.05 1 126 . 13 LEU CD2 C 25.17 0.05 1 127 . 13 LEU N N 122.1 0.05 1 128 . 14 TYR H H 8.346 0.02 1 129 . 14 TYR HA H 4.12 0.02 1 130 . 14 TYR HB2 H 3.183 0.02 1 131 . 14 TYR HB3 H 3.183 0.02 1 132 . 14 TYR HD1 H 7.153 0.02 1 133 . 14 TYR HD2 H 7.153 0.02 1 134 . 14 TYR HE1 H 6.788 0.02 1 135 . 14 TYR HE2 H 6.788 0.02 1 136 . 14 TYR C C 178 0.05 1 137 . 14 TYR CA C 61.56 0.05 1 138 . 14 TYR CB C 37.97 0.05 1 139 . 14 TYR CD1 C 132.5 0.05 1 140 . 14 TYR CD2 C 132.5 0.05 1 141 . 14 TYR CE1 C 117.3 0.05 1 142 . 14 TYR CE2 C 117.3 0.05 1 143 . 14 TYR N N 120.9 0.05 1 144 . 15 ALA H H 8.123 0.02 1 145 . 15 ALA HA H 3.958 0.02 1 146 . 15 ALA HB H 1.51 0.02 1 147 . 15 ALA C C 181.6 0.05 1 148 . 15 ALA CA C 55.11 0.05 1 149 . 15 ALA CB C 17.8 0.05 1 150 . 15 ALA N N 120.9 0.05 1 151 . 16 GLN H H 8.494 0.02 1 152 . 16 GLN HA H 3.795 0.02 1 153 . 16 GLN HB2 H 2.172 0.02 1 154 . 16 GLN HB3 H 2.172 0.02 1 155 . 16 GLN HG2 H 2.336 0.02 1 156 . 16 GLN HG3 H 2.336 0.02 1 157 . 16 GLN HE21 H 6.468 0.02 2 158 . 16 GLN HE22 H 7.7 0.02 2 159 . 16 GLN C C 177.8 0.05 1 160 . 16 GLN CA C 58.19 0.05 1 161 . 16 GLN CB C 27.81 0.05 1 162 . 16 GLN CG C 33.36 0.05 1 163 . 16 GLN N N 118.9 0.05 1 164 . 16 GLN NE2 N 112.5 0.05 1 165 . 17 LYS H H 8.468 0.02 1 166 . 17 LYS HA H 4 0.02 1 167 . 17 LYS HB2 H 1.868 0.02 2 168 . 17 LYS HB3 H 1.913 0.02 2 169 . 17 LYS HG2 H 1.235 0.02 2 170 . 17 LYS HG3 H 1.43 0.02 2 171 . 17 LYS HD2 H 1.593 0.02 2 172 . 17 LYS HD3 H 1.618 0.02 2 173 . 17 LYS HE2 H 2.826 0.02 2 174 . 17 LYS HE3 H 2.739 0.02 2 175 . 17 LYS C C 180.2 0.05 1 176 . 17 LYS CA C 60.17 0.05 1 177 . 17 LYS CB C 31.95 0.05 1 178 . 17 LYS CG C 26.47 0.05 1 179 . 17 LYS CD C 29.49 0.05 1 180 . 17 LYS CE C 42.11 0.05 1 181 . 17 LYS N N 122.5 0.05 1 182 . 18 LEU H H 7.866 0.02 1 183 . 18 LEU HA H 4.009 0.02 1 184 . 18 LEU HB2 H 1.733 0.02 2 185 . 18 LEU HB3 H 1.416 0.02 2 186 . 18 LEU HG H 1.379 0.02 2 187 . 18 LEU HD1 H 0.6978 0.02 2 188 . 18 LEU HD2 H 0.7183 0.02 2 189 . 18 LEU C C 180.6 0.05 1 190 . 18 LEU CA C 58.05 0.05 1 191 . 18 LEU CB C 41.47 0.05 1 192 . 18 LEU CG C 26.52 0.05 1 193 . 18 LEU CD1 C 22.76 0.05 1 194 . 18 LEU CD2 C 25.21 0.05 1 195 . 18 LEU N N 121.3 0.05 1 196 . 19 LYS H H 7.841 0.02 1 197 . 19 LYS HA H 4.113 0.02 1 198 . 19 LYS HB2 H 1.796 0.02 2 199 . 19 LYS HB3 H 1.966 0.02 2 200 . 19 LYS HG2 H 1.384 0.02 1 201 . 19 LYS HG3 H 1.384 0.02 1 202 . 19 LYS HD2 H 1.366 0.02 2 203 . 19 LYS HD3 H 1.4 0.02 2 204 . 19 LYS HE2 H 2.607 0.02 1 205 . 19 LYS HE3 H 2.607 0.02 1 206 . 19 LYS C C 179.5 0.05 1 207 . 19 LYS CA C 59.53 0.05 1 208 . 19 LYS CB C 32.22 0.05 1 209 . 19 LYS CG C 24.9 0.05 1 210 . 19 LYS CD C 29.35 0.05 1 211 . 19 LYS CE C 41.49 0.05 1 212 . 19 LYS N N 121.3 0.05 1 213 . 20 TYR H H 8.388 0.02 1 214 . 20 TYR HA H 4.201 0.02 1 215 . 20 TYR HB2 H 3.199 0.02 2 216 . 20 TYR HB3 H 3.418 0.02 2 217 . 20 TYR HD1 H 7.007 0.02 1 218 . 20 TYR HD2 H 7.007 0.02 1 219 . 20 TYR HE1 H 6.711 0.02 1 220 . 20 TYR HE2 H 6.711 0.02 1 221 . 20 TYR C C 177.4 0.05 1 222 . 20 TYR CA C 61.79 0.05 1 223 . 20 TYR CB C 38.09 0.05 1 224 . 20 TYR CD1 C 132.1 0.05 1 225 . 20 TYR CD2 C 132.1 0.05 1 226 . 20 TYR CE1 C 117.6 0.05 1 227 . 20 TYR CE2 C 117.6 0.05 1 228 . 20 TYR N N 121.3 0.05 1 229 . 21 LYS H H 8.191 0.02 1 230 . 21 LYS HA H 3.961 0.02 1 231 . 21 LYS HB2 H 1.797 0.02 2 232 . 21 LYS HB3 H 1.962 0.02 2 233 . 21 LYS HG2 H 1.393 0.02 2 234 . 21 LYS HG3 H 1.525 0.02 2 235 . 21 LYS HD2 H 1.64 0.02 2 236 . 21 LYS HD3 H 1.709 0.02 2 237 . 21 LYS HE2 H 2.952 0.02 1 238 . 21 LYS HE3 H 2.952 0.02 1 239 . 21 LYS C C 179.3 0.05 1 240 . 21 LYS CA C 59.46 0.05 1 241 . 21 LYS CB C 32.4 0.05 1 242 . 21 LYS CG C 24.77 0.05 1 243 . 21 LYS CD C 29.56 0.05 1 244 . 21 LYS CE C 42.29 0.05 1 245 . 21 LYS N N 121.6 0.05 1 246 . 22 ALA H H 7.717 0.02 1 247 . 22 ALA HA H 4.174 0.02 1 248 . 22 ALA HB H 1.5 0.02 1 249 . 22 ALA C C 181 0.05 1 250 . 22 ALA CA C 55.19 0.05 1 251 . 22 ALA CB C 17.95 0.05 1 252 . 22 ALA N N 120.1 0.05 1 253 . 23 ILE H H 7.996 0.02 1 254 . 23 ILE HA H 4.12 0.02 1 255 . 23 ILE HB H 1.818 0.02 1 256 . 23 ILE HG12 H 1.167 0.02 2 257 . 23 ILE HG13 H 1.474 0.02 2 258 . 23 ILE HG2 H 0.7767 0.02 1 259 . 23 ILE HD1 H 0.6049 0.02 1 260 . 23 ILE C C 177.3 0.05 1 261 . 23 ILE CA C 63.79 0.05 1 262 . 23 ILE CB C 36.98 0.05 1 263 . 23 ILE CG1 C 29.49 0.05 1 264 . 23 ILE CG2 C 18.43 0.05 1 265 . 23 ILE CD1 C 12.81 0.05 1 266 . 23 ILE N N 119.4 0.05 1 267 . 24 SER H H 8.196 0.02 1 268 . 24 SER HA H 4.19 0.02 1 269 . 24 SER HB2 H 3.687 0.02 2 270 . 24 SER HB3 H 3.865 0.02 2 271 . 24 SER C C 177.4 0.05 1 272 . 24 SER CA C 61.81 0.05 1 273 . 24 SER CB C 62.29 0.05 1 274 . 24 SER N N 118.8 0.05 1 275 . 25 GLU H H 8.219 0.02 1 276 . 25 GLU HA H 4.055 0.02 1 277 . 25 GLU HB2 H 1.967 0.02 2 278 . 25 GLU HB3 H 2.15 0.02 2 279 . 25 GLU HG2 H 2.195 0.02 2 280 . 25 GLU HG3 H 2.443 0.02 2 281 . 25 GLU C C 179 0.05 1 282 . 25 GLU CA C 59.3 0.05 1 283 . 25 GLU CB C 29.05 0.05 1 284 . 25 GLU CG C 36.55 0.05 1 285 . 25 GLU N N 121.5 0.05 1 286 . 26 GLU H H 7.745 0.02 1 287 . 26 GLU HA H 4.023 0.02 1 288 . 26 GLU HB2 H 2.164 0.02 2 289 . 26 GLU HB3 H 2.077 0.02 2 290 . 26 GLU HG2 H 2.404 0.02 2 291 . 26 GLU HG3 H 2.19 0.02 2 292 . 26 GLU C C 179.9 0.05 1 293 . 26 GLU CA C 59.54 0.05 1 294 . 26 GLU CB C 29.51 0.05 1 295 . 26 GLU CG C 36.36 0.05 1 296 . 26 GLU N N 121.1 0.05 1 297 . 27 LEU H H 8.541 0.02 1 298 . 27 LEU HA H 4.043 0.02 1 299 . 27 LEU HB2 H 1.229 0.02 2 300 . 27 LEU HB3 H 1.981 0.02 2 301 . 27 LEU HG H 1.563 0.02 2 302 . 27 LEU HD1 H 0.8601 0.02 2 303 . 27 LEU HD2 H 0.7404 0.02 2 304 . 27 LEU C C 177.6 0.05 1 305 . 27 LEU CA C 57.91 0.05 1 306 . 27 LEU CB C 41.08 0.05 1 307 . 27 LEU CG C 26.97 0.05 1 308 . 27 LEU CD1 C 25.47 0.05 1 309 . 27 LEU CD2 C 23.04 0.05 1 310 . 27 LEU N N 122.3 0.05 1 311 . 28 ASP H H 8.028 0.02 1 312 . 28 ASP HA H 4.276 0.02 1 313 . 28 ASP HB2 H 2.681 0.02 2 314 . 28 ASP HB3 H 2.6 0.02 2 315 . 28 ASP C C 179 0.05 1 316 . 28 ASP CA C 57.54 0.05 1 317 . 28 ASP CB C 40.8 0.05 1 318 . 28 ASP N N 118.9 0.05 1 319 . 29 HIS H H 7.98 0.02 1 320 . 29 HIS HA H 4.3 0.02 1 321 . 29 HIS HB2 H 3.28 0.02 1 322 . 29 HIS HB3 H 3.28 0.02 1 323 . 29 HIS HD2 H 7.291 0.02 2 324 . 29 HIS HE1 H 8.478 0.02 2 325 . 29 HIS C C 176.6 0.05 1 326 . 29 HIS CA C 58.18 0.05 1 327 . 29 HIS CB C 28.36 0.05 1 328 . 29 HIS CD2 C 119.2 0.05 1 329 . 29 HIS CE1 C 135.8 0.05 2 330 . 29 HIS N N 115.7 0.05 1 331 . 30 ALA H H 8.174 0.02 1 332 . 30 ALA HA H 4.133 0.02 1 333 . 30 ALA HB H 1.417 0.02 1 334 . 30 ALA C C 179.7 0.05 1 335 . 30 ALA CA C 54.57 0.05 1 336 . 30 ALA CB C 18.02 0.05 1 337 . 30 ALA N N 122.7 0.05 1 338 . 31 LEU H H 8.203 0.02 1 339 . 31 LEU HA H 4.17 0.02 1 340 . 31 LEU HB2 H 1.455 0.02 2 341 . 31 LEU HB3 H 1.781 0.02 2 342 . 31 LEU HG H 1.746 0.02 2 343 . 31 LEU HD1 H 0.8464 0.02 2 344 . 31 LEU HD2 H 0.8181 0.02 2 345 . 31 LEU C C 179.3 0.05 1 346 . 31 LEU CA C 56.37 0.05 1 347 . 31 LEU CB C 41.71 0.05 1 348 . 31 LEU CG C 26.76 0.05 1 349 . 31 LEU CD1 C 25.29 0.05 1 350 . 31 LEU CD2 C 22.26 0.05 1 351 . 31 LEU N N 116.9 0.05 1 352 . 32 LYS H H 7.755 0.02 1 353 . 32 LYS HA H 4.117 0.02 1 354 . 32 LYS HB2 H 1.799 0.02 1 355 . 32 LYS HB3 H 1.799 0.02 1 356 . 32 LYS HG2 H 1.395 0.02 2 357 . 32 LYS HG3 H 1.528 0.02 2 358 . 32 LYS HD2 H 1.594 0.02 2 359 . 32 LYS HD3 H 1.38 0.02 2 360 . 32 LYS HE2 H 2.92 0.02 1 361 . 32 LYS HE3 H 2.92 0.02 1 362 . 32 LYS C C 177.6 0.05 1 363 . 32 LYS CA C 57.82 0.05 1 364 . 32 LYS CB C 32.61 0.05 1 365 . 32 LYS CG C 24.98 0.05 1 366 . 32 LYS CD C 29.1 0.05 1 367 . 32 LYS CE C 42 0.05 1 368 . 32 LYS N N 120 0.05 1 369 . 33 ASP H H 8.141 0.02 1 370 . 33 ASP HA H 4.551 0.02 1 371 . 33 ASP HB2 H 2.635 0.02 2 372 . 33 ASP HB3 H 2.724 0.02 2 373 . 33 ASP C C 177.1 0.05 1 374 . 33 ASP CA C 55.15 0.05 1 375 . 33 ASP CB C 40.55 0.05 1 376 . 33 ASP N N 120.2 0.05 1 377 . 34 MET H H 8.065 0.02 1 378 . 34 MET HA H 4.452 0.02 1 379 . 34 MET HB2 H 2.067 0.02 2 380 . 34 MET HB3 H 2.147 0.02 2 381 . 34 MET HG2 H 2.544 0.02 2 382 . 34 MET HG3 H 2.647 0.02 2 383 . 34 MET HE H 2.049 0.02 1 384 . 34 MET C C 176.9 0.05 1 385 . 34 MET CA C 56.03 0.05 1 386 . 34 MET CB C 32.71 0.05 1 387 . 34 MET CG C 31.78 0.05 1 388 . 34 MET CE C 16.81 0.05 1 389 . 34 MET N N 120 0.05 1 390 . 35 THR H H 8.121 0.02 1 391 . 35 THR HA H 4.328 0.02 1 392 . 35 THR HB H 4.224 0.02 1 393 . 35 THR HG2 H 1.203 0.02 1 394 . 35 THR C C 174.7 0.05 1 395 . 35 THR CA C 62.29 0.05 1 396 . 35 THR CB C 69.88 0.05 1 397 . 35 THR CG2 C 21.52 0.05 1 398 . 35 THR N N 114.1 0.05 1 399 . 36 SER H H 8.253 0.02 1 400 . 36 SER HA H 4.5 0.02 1 401 . 36 SER HB2 H 3.945 0.02 2 402 . 36 SER HB3 H 3.845 0.02 2 403 . 36 SER C C 173.7 0.05 1 404 . 36 SER CA C 58.23 0.05 1 405 . 36 SER CB C 63.82 0.05 1 406 . 36 SER N N 119.1 0.05 1 407 . 37 ILE H H 7.783 0.02 1 408 . 37 ILE HA H 4.045 0.02 1 409 . 37 ILE HB H 1.803 0.02 1 410 . 37 ILE HG12 H 1.367 0.02 2 411 . 37 ILE HG13 H 1.109 0.02 2 412 . 37 ILE HG2 H 0.8508 0.02 1 413 . 37 ILE HD1 H 0.8253 0.02 1 414 . 37 ILE C C 181.4 0.05 1 415 . 37 ILE CA C 62.98 0.05 1 416 . 37 ILE CB C 39.37 0.05 1 417 . 37 ILE CG1 C 27.13 0.05 1 418 . 37 ILE CG2 C 17.9 0.05 1 419 . 37 ILE CD1 C 13.54 0.05 1 420 . 37 ILE N N 126.8 0.05 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants _Saveframe_category coupling_constants _Details . loop_ _Sample_label $Sample_1 $Sample_2 $Sample_3 $Sample_4 stop_ _Sample_conditions_label $Condition_1 _Spectrometer_frequency_1H . _Mol_system_component_name 'tropomyosin peptide fragment, chain 1' _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _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_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 5 SER HA 5 SER H 6.6 . . . 2 3JHNHA 11 ASP HA 11 ASP H 6.6 . . . 3 3JHNHA 12 GLU HA 12 GLU H 6.8 . . . 4 3JHNHA 13 LEU HA 13 LEU H 5.5 . . . 5 3JHNHA 14 TYR HA 14 TYR H 7.3 . . . 6 3JHNHA 15 ALA HA 15 ALA H 4.7 . . . 7 3JHNHA 17 LYS HA 17 LYS H 6.1 . . . 8 3JHNHA 18 LEU HA 18 LEU H 5.8 . . . 9 3JHNHA 19 LYS HA 19 LYS H 5.0 . . . 10 3JHNHA 20 TYR HA 20 TYR H 5.6 . . . 11 3JHNHA 22 ALA HA 22 ALA H 1.3 . . . 12 3JHNHA 23 ILE HA 23 ILE H 5.1 . . . 13 3JHNHA 24 SER HA 24 SER H 3.6 . . . 14 3JHNHA 25 GLU HA 25 GLU H 5.6 . . . 15 3JHNHA 26 GLU HA 26 GLU H 6.4 . . . 16 3JHNHA 27 LEU HA 27 LEU H 6.1 . . . 17 3JHNHA 28 ASP HA 28 ASP H 5.2 . . . 18 3JHNHA 29 HIS HA 29 HIS H 6.3 . . . 19 3JHNHA 30 ALA HA 30 ALA H 4.5 . . . 20 3JHNHA 31 LEU HA 31 LEU H 6.7 . . . 21 3JHNHA 32 LYS HA 32 LYS H 5.6 . . . 22 3JHNHA 33 ASP HA 33 ASP H 5.1 . . . 23 3JHNHA 34 MET HA 34 MET H 7.3 . . . 24 3JHNHA 35 THR HA 35 THR H 6.0 . . . 25 3JHNHA 36 SER HA 36 SER H 6.4 . . . 26 3JHNHA 37 ILE HA 37 ILE H 7.7 . . . stop_ save_