data_4995 ####################### # 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 ; _BMRB_accession_number 4995 _BMRB_flat_file_name bmr4995.str _Entry_type original _Submission_date 2001-04-20 _Accession_date 2001-04-20 _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 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_ 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 "13C chemical shifts" 160 "15N chemical shifts" 41 "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_full . _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 _CAS_abstract_code . _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 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 833 _Page_last 847 _Year 2001 _Details . 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_molecular_weight . _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_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_GlyTM1bZip _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common GlyTM1bZip _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 # ############################## _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 . _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 15965 TM1b(1-19)Zip 100.00 38 100.00 100.00 3.07e-16 PDB 1IHQ "Glytm1bzip: A Chimeric Peptide Model Of The N-Terminus Of A Rat Short Alpha Tropomyosin With The N-Terminus Encoded By Exon 1b" 97.37 38 100.00 100.00 2.35e-15 PDB 2K8X "Glytm1b(1-19)zip: A Chimeric Peptide Model Of The N-Terminus Of A Rat Short Alpha-Tropomyosin With The N-Terminus Encoded By Ex" 100.00 38 100.00 100.00 3.07e-16 PDB 3AZD "Crystal Structure Of Tropomyosin N-Terminal Fragment At 0.98a Resolution" 97.37 37 100.00 100.00 2.32e-15 DBJ BAD92278 "TPM1 protein variant [Homo sapiens]" 50.00 303 100.00 100.00 2.29e-01 DBJ BAG11063 "tropomyosin alpha-1 chain [synthetic construct]" 50.00 245 100.00 100.00 1.25e-01 DBJ BAH12832 "unnamed protein product [Homo sapiens]" 50.00 275 100.00 100.00 1.91e-01 DBJ BAH13458 "unnamed protein product [Homo sapiens]" 50.00 248 100.00 100.00 1.17e-01 GB AAA18098 "alpha-tropomyosin 5a [Rattus norvegicus]" 50.00 248 100.00 100.00 1.12e-01 GB AAA18099 "alpha-tropomyosin 5b [Rattus norvegicus]" 50.00 248 100.00 100.00 1.06e-01 GB AAA42253 "brain alpha-tropomyosin (TMBr-2) [Rattus norvegicus]" 50.00 251 100.00 100.00 1.47e-01 GB AAH50473 "TPM1 protein, partial [Homo sapiens]" 50.00 287 100.00 100.00 2.21e-01 GB AAH53545 "Tropomyosin 1 (alpha) [Homo sapiens]" 50.00 245 100.00 100.00 1.20e-01 REF NP_001018008 "tropomyosin alpha-1 chain isoform Tpm1.12br [Homo sapiens]" 50.00 245 100.00 100.00 1.20e-01 REF NP_001029245 "tropomyosin alpha-1 chain isoform Tpm1.8cy [Rattus norvegicus]" 50.00 248 100.00 100.00 1.12e-01 REF NP_001029246 "tropomyosin alpha-1 chain isoform Tpm1.9cy [Rattus norvegicus]" 50.00 248 100.00 100.00 1.06e-01 REF NP_001029247 "tropomyosin alpha-1 chain isoform Tpm1.13 [Rattus norvegicus]" 50.00 248 100.00 100.00 1.14e-01 REF NP_001157724 "tropomyosin alpha-1 chain isoform Tpm1.8cy [Mus musculus]" 50.00 248 100.00 100.00 1.12e-01 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 _Details . 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 _Details . 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 _Details . 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 _Details . 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_ _Details . 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 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N-1H_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-1H HSQC' _Sample_label . save_ save_13C-!H_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-!H HSQC' _Sample_label . save_ save_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . save_ save_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_2QF-COSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name 2QF-COSY _Sample_label . save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_CANH_8 _Saveframe_category NMR_applied_experiment _Experiment_name CANH _Sample_label . save_ save_H(CA)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name H(CA)NH _Sample_label . save_ save_H(CA)(CO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name H(CA)(CO)NH _Sample_label . save_ save_(CA)(C0)NH_11 _Saveframe_category NMR_applied_experiment _Experiment_name (CA)(C0)NH _Sample_label . save_ save_CBCANH_12 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_CNCA(CO)NH_13 _Saveframe_category NMR_applied_experiment _Experiment_name CNCA(CO)NH _Sample_label . save_ save_H_HCC(CO)NH-TOCSY_14 _Saveframe_category NMR_applied_experiment _Experiment_name H_HCC(CO)NH-TOCSY _Sample_label . save_ save_C_HCC(CO)NH-TOCSY_15 _Saveframe_category NMR_applied_experiment _Experiment_name C_HCC(CO)NH-TOCSY _Sample_label . save_ save_HCCH-COSY_16 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _Sample_label . save_ save_15N_edited_PFG_NOESY_17 _Saveframe_category NMR_applied_experiment _Experiment_name '15N edited PFG NOESY' _Sample_label . save_ save_13C_edited_PFG_NOESY_18 _Saveframe_category NMR_applied_experiment _Experiment_name '13C edited PFG NOESY' _Sample_label . save_ save_13C_X-filtered_NOESY_19 _Saveframe_category NMR_applied_experiment _Experiment_name '13C X-filtered NOESY' _Sample_label . save_ save_13C-15N_X-filtered_NOESY_20 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-15N X-filtered NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-1H HSQC' _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-!H HSQC' _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 2QF-COSY _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name CANH _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name H(CA)NH _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name H(CA)(CO)NH _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name (CA)(C0)NH _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_13 _Saveframe_category NMR_applied_experiment _Experiment_name CNCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_14 _Saveframe_category NMR_applied_experiment _Experiment_name H_HCC(CO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_15 _Saveframe_category NMR_applied_experiment _Experiment_name C_HCC(CO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_16 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_17 _Saveframe_category NMR_applied_experiment _Experiment_name '15N edited PFG NOESY' _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_18 _Saveframe_category NMR_applied_experiment _Experiment_name '13C edited PFG NOESY' _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_19 _Saveframe_category NMR_applied_experiment _Experiment_name '13C X-filtered NOESY' _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ save_NMR_spec_expt__0_20 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-15N X-filtered NOESY' _BMRB_pulse_sequence_accession_number . _Details 'four channels' save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . 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 _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 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 # # # # 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_shifts _Saveframe_category assigned_chemical_shifts _Details . 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' _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 3.91 0.02 1 2 . 1 GLY HA3 H 3.91 0.02 1 3 . 1 GLY C C 170.1 0.05 1 4 . 1 GLY CA C 43.1 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 178.5 0.05 1 9 . 2 ALA CA C 52.5 0.05 1 10 . 2 ALA CB C 18.9 0.05 1 11 . 2 ALA N N 124 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 174.6 0.05 1 16 . 3 GLY CA C 45.1 0.05 1 17 . 3 GLY N N 108.9 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 175.2 0.05 1 23 . 4 SER CA C 58.4 0.05 1 24 . 4 SER CB C 63.4 0.05 1 25 . 4 SER N N 116 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 175.4 0.05 1 31 . 5 SER CA C 58.6 0.05 1 32 . 5 SER CB C 63.2 0.05 1 33 . 5 SER N N 118.5 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 175.4 0.05 1 39 . 6 SER CA C 58.9 0.05 1 40 . 6 SER CB C 63.3 0.05 1 41 . 6 SER N N 118.8 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 178.5 0.05 1 50 . 7 LEU CA C 57.1 0.05 1 51 . 7 LEU CB C 41.6 0.05 1 52 . 7 LEU CD1 C 23.7 0.05 2 53 . 7 LEU CD2 C 30.4 0.05 2 54 . 7 LEU N N 123.9 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 178.7 0.05 1 62 . 8 GLU CA C 59.2 0.05 1 63 . 8 GLU CB C 28.8 0.05 1 64 . 8 GLU CG C 35.8 0.05 1 65 . 8 GLU N N 118.8 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 181.3 0.05 1 70 . 9 ALA CA C 55.1 0.05 1 71 . 9 ALA CB C 17.9 0.05 1 72 . 9 ALA N N 121.7 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 178 0.05 1 79 . 10 VAL CA C 65.8 0.05 1 80 . 10 VAL CB C 31.5 0.05 1 81 . 10 VAL CG1 C 21.9 0.05 2 82 . 10 VAL CG2 C 22.2 0.05 2 83 . 10 VAL N N 118.7 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 1.8 0.02 2 90 . 11 ARG HD2 H 3.2 0.02 1 91 . 11 ARG HD3 H 3.2 0.02 1 92 . 11 ARG C C 179.6 0.05 1 93 . 11 ARG CA C 59.7 0.05 1 94 . 11 ARG CB C 29.9 0.05 1 95 . 11 ARG CG C 27.9 0.05 1 96 . 11 ARG CD C 43.4 0.05 1 97 . 11 ARG N N 120.1 0.05 1 98 . 12 ARG H H 8.1 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 178.8 0.05 1 107 . 12 ARG CA C 59.3 0.05 1 108 . 12 ARG CB C 29.9 0.05 1 109 . 12 ARG CG C 27.6 0.05 1 110 . 12 ARG CD C 43.2 0.05 1 111 . 12 ARG N N 119.4 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 178.8 0.05 1 123 . 13 LYS CA C 58.8 0.05 1 124 . 13 LYS CB C 31.8 0.05 1 125 . 13 LYS CG C 24.6 0.05 1 126 . 13 LYS CD C 29.2 0.05 1 127 . 13 LYS CE C 41.7 0.05 1 128 . 13 LYS N N 121.9 0.05 1 129 . 14 ILE H H 8.38 0.02 1 130 . 14 ILE HA H 3.6 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 0.9 0.02 1 135 . 14 ILE HD1 H 0.96 0.02 1 136 . 14 ILE C C 177.1 0.05 1 137 . 14 ILE CA C 65.6 0.05 1 138 . 14 ILE CB C 37.4 0.05 1 139 . 14 ILE CG1 C 30.6 0.05 1 140 . 14 ILE CG2 C 16.3 0.05 1 141 . 14 ILE CD1 C 13.8 0.05 1 142 . 14 ILE N N 119.5 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 179.1 0.05 1 152 . 15 ARG CA C 59.1 0.05 1 153 . 15 ARG CB C 29.6 0.05 1 154 . 15 ARG CG C 27.3 0.05 1 155 . 15 ARG CD C 43.1 0.05 1 156 . 15 ARG N N 119.1 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 177.7 0.05 1 162 . 16 SER CA C 61.3 0.05 1 163 . 16 SER CB C 62.6 0.05 1 164 . 16 SER N N 114.3 0.05 1 165 . 17 LEU H H 8.4 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 179.6 0.05 1 173 . 17 LEU CA C 57.7 0.05 1 174 . 17 LEU CB C 43.2 0.05 1 175 . 17 LEU CG C 27.4 0.05 1 176 . 17 LEU CD1 C 27.4 0.05 2 177 . 17 LEU CD2 C 30.4 0.05 2 178 . 17 LEU N N 122.9 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 179.2 0.05 1 188 . 18 GLN CA C 59.2 0.05 1 189 . 18 GLN CB C 28.2 0.05 1 190 . 18 GLN CG C 34.9 0.05 1 191 . 18 GLN N N 119.9 0.05 1 192 . 18 GLN NE2 N 111.7 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 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 179.5 0.05 1 200 . 19 GLU CA C 59.4 0.05 1 201 . 19 GLU CB C 29 0.05 1 202 . 19 GLU CG C 36.5 0.05 1 203 . 19 GLU N N 120.6 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 178.4 0.05 1 213 . 20 GLN CA C 58.7 0.05 1 214 . 20 GLN CB C 28.4 0.05 1 215 . 20 GLN CG C 33.5 0.05 1 216 . 20 GLN N N 120.1 0.05 1 217 . 20 GLN NE2 N 111.2 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 6.8 0.02 2 223 . 21 ASN HD22 H 7.64 0.02 2 224 . 21 ASN C C 176.7 0.05 1 225 . 21 ASN CA C 56.8 0.05 1 226 . 21 ASN CB C 38.3 0.05 1 227 . 21 ASN N N 120.3 0.05 1 228 . 21 ASN ND2 N 106.4 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 178.2 0.05 1 238 . 22 TYR CA C 60.2 0.05 1 239 . 22 TYR CB C 37.8 0.05 1 240 . 22 TYR N N 120.1 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 3.4 0.02 1 244 . 23 HIS HB3 H 3.4 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 178.4 0.05 1 248 . 23 HIS CA C 58.9 0.05 1 249 . 23 HIS CB C 28.7 0.05 1 250 . 23 HIS N N 117.7 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 178.9 0.05 1 259 . 24 LEU CA C 58 0.05 1 260 . 24 LEU CB C 43.4 0.05 1 261 . 24 LEU CG C 27 0.05 1 262 . 24 LEU CD1 C 26.5 0.05 2 263 . 24 LEU CD2 C 21.5 0.05 2 264 . 24 LEU N N 120.7 0.05 1 265 . 25 GLU H H 8.9 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 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 180.4 0.05 1 272 . 25 GLU CA C 59.7 0.05 1 273 . 25 GLU CB C 28.9 0.05 1 274 . 25 GLU CG C 36.4 0.05 1 275 . 25 GLU N N 119.8 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 178.1 0.05 1 283 . 26 ASN CA C 55.8 0.05 1 284 . 26 ASN CB C 37.5 0.05 1 285 . 26 ASN N N 119.2 0.05 1 286 . 26 ASN ND2 N 111.6 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 178.2 0.05 1 294 . 27 GLU CA C 58.4 0.05 1 295 . 27 GLU CB C 30 0.05 1 296 . 27 GLU CG C 35.7 0.05 1 297 . 27 GLU N N 124.1 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 177.6 0.05 1 304 . 28 VAL CA C 67.6 0.05 1 305 . 28 VAL CB C 31.4 0.05 1 306 . 28 VAL CG1 C 23.1 0.05 2 307 . 28 VAL CG2 C 25.3 0.05 2 308 . 28 VAL N N 120.4 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 180.5 0.05 1 313 . 29 ALA CA C 55 0.05 1 314 . 29 ALA CB C 17.8 0.05 1 315 . 29 ALA N N 119.9 0.05 1 316 . 30 ARG H H 8.06 0.02 1 317 . 30 ARG HA H 4 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 179.7 0.05 1 325 . 30 ARG CA C 59 0.05 1 326 . 30 ARG CB C 30.6 0.05 1 327 . 30 ARG CG C 27.3 0.05 1 328 . 30 ARG CD C 42.4 0.05 1 329 . 30 ARG N N 120.1 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 179.3 0.05 1 338 . 31 LEU CA C 57.5 0.05 1 339 . 31 LEU CB C 43.7 0.05 1 340 . 31 LEU CG C 27.4 0.05 1 341 . 31 LEU CD1 C 23.5 0.05 2 342 . 31 LEU CD2 C 27.5 0.05 2 343 . 31 LEU N N 121 0.05 1 344 . 32 LYS H H 9.1 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 1.5 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 179.6 0.05 1 355 . 32 LYS CA C 60.8 0.05 1 356 . 32 LYS CB C 32.3 0.05 1 357 . 32 LYS CG C 27.4 0.05 1 358 . 32 LYS CD C 29.6 0.05 1 359 . 32 LYS CE C 41.6 0.05 1 360 . 32 LYS N N 118.9 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 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 179.2 0.05 1 372 . 33 LYS CA C 58.7 0.05 1 373 . 33 LYS CB C 32 0.05 1 374 . 33 LYS CG C 25.2 0.05 1 375 . 33 LYS CD C 29.1 0.05 1 376 . 33 LYS CE C 41.7 0.05 1 377 . 33 LYS N N 117.7 0.05 1 378 . 34 LEU H H 7.5 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 0.02 2 385 . 34 LEU C C 179.3 0.05 1 386 . 34 LEU CA C 57.1 0.05 1 387 . 34 LEU CB C 42.4 0.05 1 388 . 34 LEU CG C 26.8 0.05 1 389 . 34 LEU CD1 C 22.9 0.05 2 390 . 34 LEU CD2 C 25.2 0.05 2 391 . 34 LEU N N 118.9 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 176.9 0.05 1 398 . 35 VAL CA C 62.7 0.05 1 399 . 35 VAL CB C 32.1 0.05 1 400 . 35 VAL CG1 C 21.6 0.05 1 401 . 35 VAL CG2 C 21.6 0.05 1 402 . 35 VAL N N 113.9 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 174.7 0.05 1 407 . 36 GLY CA C 45.5 0.05 1 408 . 36 GLY N N 109.2 0.05 1 409 . 37 GLU H H 8.01 0.02 1 410 . 37 GLU HA H 4.4 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 175.5 0.05 1 416 . 37 GLU CA C 55.9 0.05 1 417 . 37 GLU CB C 31.2 0.05 1 418 . 37 GLU CG C 36.4 0.05 1 419 . 37 GLU N N 120.8 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 181.2 0.05 1 429 . 38 ARG CA C 57.2 0.05 1 430 . 38 ARG CB C 31.2 0.05 1 431 . 38 ARG CG C 27.4 0.05 1 432 . 38 ARG CD C 42.4 0.05 1 433 . 38 ARG N N 127.5 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' _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 3 GLY H 3 GLY HA 6 . . 0.1 2 3JHNHA 4 SER H 4 SER HA 6 . . 0.1 3 3JHNHA 5 SER H 5 SER HA 5.4 . . 0.1 4 3JHNHA 6 SER H 6 SER HA 4.5 . . 0.1 5 3JHNHA 7 LEU H 7 LEU HA 4.6 . . 0.1 6 3JHNHA 8 GLU H 8 GLU HA 4.3 . . 0.1 7 3JHNHA 9 ALA H 9 ALA HA 4 . . 0.1 8 3JHNHA 10 VAL H 10 VAL HA 5.1 . . 0.1 9 3JHNHA 11 ARG H 11 ARG HA 4 . . 0.1 10 3JHNHA 12 ARG H 12 ARG HA 5 . . 0.1 11 3JHNHA 13 LYS H 13 LYS HA 4.6 . . 0.1 12 3JHNHA 14 ILE H 14 ILE HA 4.8 . . 0.1 13 3JHNHA 15 ARG H 15 ARG HA 4.4 . . 0.1 14 3JHNHA 16 SER H 16 SER HA 4 . . 0.1 15 3JHNHA 17 LEU H 17 LEU HA 5.1 . . 0.1 16 3JHNHA 18 GLN H 18 GLN HA 4.3 . . 0.1 17 3JHNHA 19 GLU H 19 GLU HA 4.4 . . 0.1 18 3JHNHA 22 TYR H 22 TYR HA 4.9 . . 0.1 19 3JHNHA 23 HIS H 23 HIS HA 4.5 . . 0.1 20 3JHNHA 24 LEU H 24 LEU HA 4.5 . . 0.1 21 3JHNHA 25 GLU H 25 GLU HA 4 . . 0.1 22 3JHNHA 26 ASN H 26 ASN HA 4 . . 0.1 23 3JHNHA 27 GLU H 27 GLU HA 3.8 . . 0.1 24 3JHNHA 28 VAL H 28 VAL HA 3 . . 0.1 25 3JHNHA 29 ALA H 29 ALA HA 3 . . 0.1 26 3JHNHA 30 ARG H 30 ARG HA 3 . . 0.1 27 3JHNHA 31 LEU H 31 LEU HA 4.9 . . 0.1 28 3JHNHA 32 LYS H 32 LYS HA 4 . . 0.1 29 3JHNHA 33 LYS H 33 LYS HA 5 . . 0.1 30 3JHNHA 34 LEU H 34 LEU HA 1 . . 0.1 31 3JHNHA 35 VAL H 35 VAL HA 6.7 . . 0.1 32 3JHNHA 36 GLY H 36 GLY HA 5.6 . . 0.1 33 3JHNHA 37 GLU H 37 GLU HA 7.9 . . 0.1 34 3JHNHA 38 ARG H 38 ARG HA 7.3 . . 0.1 stop_ save_