data_4054 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4054 _Entry.Title ; Alpha-Helical Coiled Coil Trimerization Domain of Chicken Cartilage Matrix Protein (Reduced C5-C7 Disulfide Bonds) ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1997-08-07 _Entry.Accession_date 1997-08-08 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Ronald Wiltscheck . . . 4054 2 Richard Kammerer . A. . 4054 3 Sonja Dames . A. . 4054 4 Therese Schulthess . . . 4054 5 Marcel Blommers . J.J. . 4054 6 Jurgen Engel . . . 4054 7 Andrei Alexandrescu . T. . 4054 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4054 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 40 4054 '1H chemical shifts' 202 4054 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 1998-02-25 . reformat BMRB 'converted to NMR-STAR version 2.1' 4054 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4054 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 97406913 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Wiltscheck, R., Kammerer, R. A., Dames, S. A., Schulthess, T., Blommers, M. J.J., Engel, J., and Alexandrescu, A. T., "Heteronuclear NMR Assignments and Secondary Structure of the Coiled Coil Trimerization Domain from Cartilage Matrix Protein in Oxidized and Reduced Forms," Protein Sci. 6, 1734-1745 (1997). ; _Citation.Title ; Heteronuclear NMR Assignments and Secondary Structure of the Coiled Coil Trimerization Domain from Cartilage Matrix Protein in Oxidized and Reduced Forms. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full 'Protein Science' _Citation.Journal_volume 6 _Citation.Journal_issue 8 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 1734 _Citation.Page_last 1745 _Citation.Year 1997 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Ronald Wiltscheck . . . 4054 1 2 Richard Kammerer . A. . 4054 1 3 Sonja Dames . A. . 4054 1 4 Therese Schulthess . . . 4054 1 5 Marcel Blommers . J.J. . 4054 1 6 Jurgen Engel . . . 4054 1 7 Andrei Alexandrescu . T. . 4054 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID alpha-helix 4054 1 'coiled coil' 4054 1 'disulfide bonds' 4054 1 flexibility 4054 1 'heteronuclear NMR' 4054 1 hydrogen-exchange 4054 1 'oligomerization domain' 4054 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_CMPcc _Assembly.Sf_category assembly _Assembly.Sf_framecode CMPcc _Assembly.Entry_ID 4054 _Assembly.ID 1 _Assembly.Name 'Cartilage Matrix Protein' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details ; This molecule is a parallel homo-trimer!! However because of 3-fold symmetry (e.g. magnetic equivalence) the chemical shifts of each of the three monomer chains are equivalent. Cartilage matrix protein is a parallel trimeric coiled coil, linked by inter-monomer disulfide bonds between Cys 5 and Cys 7. The present entry gives NMR data for the protein when the C5-C7 disulfide bonds are broken by a 10-fold excess of DTT per monomer (1 mM protein, 32 mM DTT). ; _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID trimer 4054 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'subunit A' 1 $CMPcc_reduced . . . reduced . . 1 . . 4054 1 2 'subunit B' 1 $CMPcc_reduced . . . reduced . . 1 . . 4054 1 3 'subunit C' 1 $CMPcc_reduced . . . reduced . . 1 . . 4054 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID . PDB 1AQ5 . 'A Chain A, High-Resolution Solution Nmr Structure Of The Trimeric Coiled-Coil Domain Of Chicken Cartilage Matrix Protein, 20 Structures' . . . . 4054 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Cartilage Matrix Protein' system 4054 1 CMPcc abbreviation 4054 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_CMPcc_reduced _Entity.Sf_category entity _Entity.Sf_framecode CMPcc_reduced _Entity.Entry_ID 4054 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Coiled Coil domain of Chicken Cartilage Matrix Protein' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; GSHMEEDPCECKSIVKFQTK VEELINTLQQKLEAVAKRIE ALENKII ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 47 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 5386 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details ; Molecule corresponds to the C-terminal domain (residues 451 to 492) of chicken cartilage matrix protein. The molecule is an alpha-helical coiled coil trimer with 3-fold symmetry. Because monomers have equivalent magnetic environments, NMR spectra contain resonances corresponding to the sequence of the monomers. The Swiss-Prot index for CMP is P05099. A separate BMRB deposit has been made for the chemical shifts of the oxidized (native) form of the protein. Inter-chain-disulfide between residue 9 and 11 is broken by 10 fold excess of DTT per monomer The protein contains 4 extra residues that are a cloning artefact. The following numbering scheme has been used: G(-4), S(-3), H(-2), M(-1), E(1), E(2). While the 2nd residue in the protein is Ser, and residue 3 His, these are not found in nature. The wild type protein begins EEAP..., and the extra four residues GSHM have been numbered using negative numbers from the C- to the N-terminus. ; _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 4055 . "Coiled Coil domain of Chicken Cartilage Matrix Protein" . . . . . 100.00 47 100.00 100.00 1.51e-23 . . . . 4054 1 2 no PDB 1AQ5 . "High-Resolution Solution Nmr Structure Of The Trimeric Coiled-Coil Domain Of Chicken Cartilage Matrix Protein, 20 Structures" . . . . . 100.00 47 100.00 100.00 1.51e-23 . . . . 4054 1 3 no EMBL CAA30915 . "cartilage matrix protein [Gallus gallus]" . . . . . 93.62 493 97.73 100.00 4.32e-18 . . . . 4054 1 4 no GB AAA48695 . "cartilage matrix protein, partial [Gallus gallus]" . . . . . 93.62 416 97.73 100.00 1.96e-18 . . . . 4054 1 5 no REF NP_001025546 . "cartilage matrix protein precursor [Gallus gallus]" . . . . . 93.62 493 97.73 100.00 3.91e-18 . . . . 4054 1 6 no SP P05099 . "RecName: Full=Cartilage matrix protein; AltName: Full=Matrilin-1; Flags: Precursor" . . . . . 93.62 493 97.73 100.00 4.32e-18 . . . . 4054 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID CMPcc abbreviation 4054 1 'Coiled Coil domain of Chicken Cartilage Matrix Protein' common 4054 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 -4 GLY . 4054 1 2 -3 SER . 4054 1 3 -2 HIS . 4054 1 4 -1 MET . 4054 1 5 1 GLU . 4054 1 6 2 GLU . 4054 1 7 3 ASP . 4054 1 8 4 PRO . 4054 1 9 5 CYS . 4054 1 10 6 GLU . 4054 1 11 7 CYS . 4054 1 12 8 LYS . 4054 1 13 9 SER . 4054 1 14 10 ILE . 4054 1 15 11 VAL . 4054 1 16 12 LYS . 4054 1 17 13 PHE . 4054 1 18 14 GLN . 4054 1 19 15 THR . 4054 1 20 16 LYS . 4054 1 21 17 VAL . 4054 1 22 18 GLU . 4054 1 23 19 GLU . 4054 1 24 20 LEU . 4054 1 25 21 ILE . 4054 1 26 22 ASN . 4054 1 27 23 THR . 4054 1 28 24 LEU . 4054 1 29 25 GLN . 4054 1 30 26 GLN . 4054 1 31 27 LYS . 4054 1 32 28 LEU . 4054 1 33 29 GLU . 4054 1 34 30 ALA . 4054 1 35 31 VAL . 4054 1 36 32 ALA . 4054 1 37 33 LYS . 4054 1 38 34 ARG . 4054 1 39 35 ILE . 4054 1 40 36 GLU . 4054 1 41 37 ALA . 4054 1 42 38 LEU . 4054 1 43 39 GLU . 4054 1 44 40 ASN . 4054 1 45 41 LYS . 4054 1 46 42 ILE . 4054 1 47 43 ILE . 4054 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . GLY 1 1 4054 1 . SER 2 2 4054 1 . HIS 3 3 4054 1 . MET 4 4 4054 1 . GLU 5 5 4054 1 . GLU 6 6 4054 1 . ASP 7 7 4054 1 . PRO 8 8 4054 1 . CYS 9 9 4054 1 . GLU 10 10 4054 1 . CYS 11 11 4054 1 . LYS 12 12 4054 1 . SER 13 13 4054 1 . ILE 14 14 4054 1 . VAL 15 15 4054 1 . LYS 16 16 4054 1 . PHE 17 17 4054 1 . GLN 18 18 4054 1 . THR 19 19 4054 1 . LYS 20 20 4054 1 . VAL 21 21 4054 1 . GLU 22 22 4054 1 . GLU 23 23 4054 1 . LEU 24 24 4054 1 . ILE 25 25 4054 1 . ASN 26 26 4054 1 . THR 27 27 4054 1 . LEU 28 28 4054 1 . GLN 29 29 4054 1 . GLN 30 30 4054 1 . LYS 31 31 4054 1 . LEU 32 32 4054 1 . GLU 33 33 4054 1 . ALA 34 34 4054 1 . VAL 35 35 4054 1 . ALA 36 36 4054 1 . LYS 37 37 4054 1 . ARG 38 38 4054 1 . ILE 39 39 4054 1 . GLU 40 40 4054 1 . ALA 41 41 4054 1 . LEU 42 42 4054 1 . GLU 43 43 4054 1 . ASN 44 44 4054 1 . LYS 45 45 4054 1 . ILE 46 46 4054 1 . ILE 47 47 4054 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 4054 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $CMPcc_reduced . 9031 organism . 'Gallus gallus' chicken . . Eukaryota Metazoa Gallus gallus . . . endoskeleton 'cartilage matrix' . . . . . . . . . . . . . . . . 4054 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 4054 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $CMPcc_reduced . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21(DE3) . . . . . . . . . . . . plasmid . . pET-15b . . . synthetic . . 4054 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_CMPcc_reduced _Sample.Sf_category sample _Sample.Sf_framecode sample_CMPcc_reduced _Sample.Entry_ID 4054 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'Coiled Coil domain of Chicken Cartilage Matrix Protein' [U-15N] . . 1 $CMPcc_reduced . . 1 . . mM . . . . 4054 1 2 DTT . . . . . . . 32 . . mM . . . . 4054 1 3 NaCl . . . . . . . 150 . . mM . . . . 4054 1 stop_ save_ ####################### # Sample conditions # ####################### save_experimental_conditions_CMPcc_reduced _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode experimental_conditions_CMPcc_reduced _Sample_condition_list.Entry_ID 4054 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 5.8 0.1 pH 4054 1 pressure 1 . atm 4054 1 temperature 373 1 K 4054 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_one _NMR_spectrometer.Entry_ID 4054 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX600 _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4054 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer_one Bruker AMX600 . 600 . . . 4054 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 4054 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 . . . . . . . . . . . . 1 $sample_CMPcc_reduced . . . 1 $experimental_conditions_CMPcc_reduced . . . 1 $NMR_spectrometer_one . . . . . . . . . . . . . . . . 4054 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_CMPcc_reduced _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_CMPcc_reduced _Chem_shift_reference.Entry_ID 4054 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details ; DSS in water as described in Wishart D.S., Bigam C.G., Yao J., Abildgaard F., Dyson H.J., Oldfield E., Markley J.L., Sykes B.D. 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J. Biomol. NMR 6, 135-140 (1995). ; loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS . . . . . ppm 0.000 . indirect 0.251449528 . . . . . . . . . 4054 1 H 1 DSS . . . . . ppm 0.000 . direct . . . . . . . . . . 4054 1 N 15 DSS . . . . . ppm 0.000 . indirect 0.101329118 . . . . . . . . . 4054 1 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_CMPcc_reduced _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_assignment_CMPcc_reduced _Assigned_chem_shift_list.Entry_ID 4054 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $experimental_conditions_CMPcc_reduced _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_CMPcc_reduced _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_CMPcc_reduced . 4054 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 6 6 GLU HA H 1 4.29 . . 1 . . . . . . . . 4054 1 2 . 1 1 7 7 ASP H H 1 8.26 . . 1 . . . . . . . . 4054 1 3 . 1 1 7 7 ASP HA H 1 4.89 . . 1 . . . . . . . . 4054 1 4 . 1 1 7 7 ASP HB2 H 1 2.78 . . 2 . . . . . . . . 4054 1 5 . 1 1 7 7 ASP HB3 H 1 2.56 . . 2 . . . . . . . . 4054 1 6 . 1 1 7 7 ASP N N 15 122.9 . . 1 . . . . . . . . 4054 1 7 . 1 1 9 9 CYS H H 1 8.13 . . 1 . . . . . . . . 4054 1 8 . 1 1 9 9 CYS HA H 1 4.35 . . 1 . . . . . . . . 4054 1 9 . 1 1 9 9 CYS HB2 H 1 3.62 . . 2 . . . . . . . . 4054 1 10 . 1 1 9 9 CYS N N 15 115.4 . . 1 . . . . . . . . 4054 1 11 . 1 1 10 10 GLU H H 1 8.33 . . 1 . . . . . . . . 4054 1 12 . 1 1 10 10 GLU HA H 1 4.29 . . 1 . . . . . . . . 4054 1 13 . 1 1 10 10 GLU HB2 H 1 1.97 . . 2 . . . . . . . . 4054 1 14 . 1 1 10 10 GLU HB3 H 1 2.11 . . 2 . . . . . . . . 4054 1 15 . 1 1 10 10 GLU HG2 H 1 2.28 . . 1 . . . . . . . . 4054 1 16 . 1 1 10 10 GLU N N 15 121.6 . . 1 . . . . . . . . 4054 1 17 . 1 1 11 11 CYS H H 1 8.41 . . 1 . . . . . . . . 4054 1 18 . 1 1 11 11 CYS HA H 1 4.40 . . 1 . . . . . . . . 4054 1 19 . 1 1 11 11 CYS HB2 H 1 2.99 . . 2 . . . . . . . . 4054 1 20 . 1 1 11 11 CYS HB3 H 1 3.83 . . 2 . . . . . . . . 4054 1 21 . 1 1 11 11 CYS N N 15 118.0 . . 1 . . . . . . . . 4054 1 22 . 1 1 12 12 LYS H H 1 8.25 . . 1 . . . . . . . . 4054 1 23 . 1 1 12 12 LYS HA H 1 4.24 . . 1 . . . . . . . . 4054 1 24 . 1 1 12 12 LYS N N 15 122.2 . . 1 . . . . . . . . 4054 1 25 . 1 1 13 13 SER H H 1 8.20 . . 1 . . . . . . . . 4054 1 26 . 1 1 13 13 SER HA H 1 4.11 . . 1 . . . . . . . . 4054 1 27 . 1 1 13 13 SER HB2 H 1 2.99 . . 2 . . . . . . . . 4054 1 28 . 1 1 13 13 SER N N 15 119.7 . . 1 . . . . . . . . 4054 1 29 . 1 1 14 14 ILE H H 1 7.67 . . 1 . . . . . . . . 4054 1 30 . 1 1 14 14 ILE HA H 1 3.80 . . 1 . . . . . . . . 4054 1 31 . 1 1 14 14 ILE HB H 1 2.10 . . 1 . . . . . . . . 4054 1 32 . 1 1 14 14 ILE N N 15 121.4 . . 1 . . . . . . . . 4054 1 33 . 1 1 15 15 VAL H H 1 7.88 . . 1 . . . . . . . . 4054 1 34 . 1 1 15 15 VAL HA H 1 4.12 . . 1 . . . . . . . . 4054 1 35 . 1 1 15 15 VAL HB H 1 1.93 . . 1 . . . . . . . . 4054 1 36 . 1 1 15 15 VAL HG11 H 1 1.02 . . 2 . . . . . . . . 4054 1 37 . 1 1 15 15 VAL HG12 H 1 1.02 . . 2 . . . . . . . . 4054 1 38 . 1 1 15 15 VAL HG13 H 1 1.02 . . 2 . . . . . . . . 4054 1 39 . 1 1 15 15 VAL N N 15 121.2 . . 1 . . . . . . . . 4054 1 40 . 1 1 16 16 LYS H H 1 8.01 . . 1 . . . . . . . . 4054 1 41 . 1 1 16 16 LYS HA H 1 4.39 . . 1 . . . . . . . . 4054 1 42 . 1 1 16 16 LYS N N 15 122.8 . . 1 . . . . . . . . 4054 1 43 . 1 1 17 17 PHE H H 1 7.87 . . 1 . . . . . . . . 4054 1 44 . 1 1 17 17 PHE HA H 1 4.17 . . 1 . . . . . . . . 4054 1 45 . 1 1 17 17 PHE HB2 H 1 3.37 . . 2 . . . . . . . . 4054 1 46 . 1 1 17 17 PHE HB3 H 1 3.16 . . 2 . . . . . . . . 4054 1 47 . 1 1 17 17 PHE HD1 H 1 7.31 . . 3 . . . . . . . . 4054 1 48 . 1 1 17 17 PHE N N 15 120.4 . . 1 . . . . . . . . 4054 1 49 . 1 1 18 18 GLN H H 1 8.46 . . 1 . . . . . . . . 4054 1 50 . 1 1 18 18 GLN HA H 1 3.59 . . 1 . . . . . . . . 4054 1 51 . 1 1 18 18 GLN HB2 H 1 1.93 . . 2 . . . . . . . . 4054 1 52 . 1 1 18 18 GLN N N 15 118.6 . . 1 . . . . . . . . 4054 1 53 . 1 1 19 19 THR H H 1 7.95 . . 1 . . . . . . . . 4054 1 54 . 1 1 19 19 THR HA H 1 4.01 . . 1 . . . . . . . . 4054 1 55 . 1 1 19 19 THR HB H 1 4.22 . . 1 . . . . . . . . 4054 1 56 . 1 1 19 19 THR HG21 H 1 1.26 . . 1 . . . . . . . . 4054 1 57 . 1 1 19 19 THR HG22 H 1 1.26 . . 1 . . . . . . . . 4054 1 58 . 1 1 19 19 THR HG23 H 1 1.26 . . 1 . . . . . . . . 4054 1 59 . 1 1 19 19 THR N N 15 113.3 . . 1 . . . . . . . . 4054 1 60 . 1 1 20 20 LYS H H 1 7.68 . . 1 . . . . . . . . 4054 1 61 . 1 1 20 20 LYS HA H 1 4.12 . . 1 . . . . . . . . 4054 1 62 . 1 1 20 20 LYS HB2 H 1 1.96 . . 2 . . . . . . . . 4054 1 63 . 1 1 20 20 LYS N N 15 122.6 . . 1 . . . . . . . . 4054 1 64 . 1 1 21 21 VAL H H 1 8.18 . . 1 . . . . . . . . 4054 1 65 . 1 1 21 21 VAL HA H 1 3.52 . . 1 . . . . . . . . 4054 1 66 . 1 1 21 21 VAL HB H 1 2.00 . . 1 . . . . . . . . 4054 1 67 . 1 1 21 21 VAL HG11 H 1 0.88 . . 2 . . . . . . . . 4054 1 68 . 1 1 21 21 VAL HG12 H 1 0.88 . . 2 . . . . . . . . 4054 1 69 . 1 1 21 21 VAL HG13 H 1 0.88 . . 2 . . . . . . . . 4054 1 70 . 1 1 21 21 VAL HG21 H 1 0.67 . . 2 . . . . . . . . 4054 1 71 . 1 1 21 21 VAL HG22 H 1 0.67 . . 2 . . . . . . . . 4054 1 72 . 1 1 21 21 VAL HG23 H 1 0.67 . . 2 . . . . . . . . 4054 1 73 . 1 1 21 21 VAL N N 15 118.5 . . 1 . . . . . . . . 4054 1 74 . 1 1 22 22 GLU H H 1 8.28 . . 1 . . . . . . . . 4054 1 75 . 1 1 22 22 GLU HA H 1 3.84 . . 1 . . . . . . . . 4054 1 76 . 1 1 22 22 GLU HB2 H 1 2.07 . . 2 . . . . . . . . 4054 1 77 . 1 1 22 22 GLU N N 15 119.5 . . 1 . . . . . . . . 4054 1 78 . 1 1 23 23 GLU H H 1 7.87 . . 1 . . . . . . . . 4054 1 79 . 1 1 23 23 GLU HA H 1 4.12 . . 1 . . . . . . . . 4054 1 80 . 1 1 23 23 GLU HB2 H 1 2.21 . . 2 . . . . . . . . 4054 1 81 . 1 1 23 23 GLU HG2 H 1 2.46 . . 1 . . . . . . . . 4054 1 82 . 1 1 23 23 GLU N N 15 119.4 . . 1 . . . . . . . . 4054 1 83 . 1 1 24 24 LEU H H 1 8.13 . . 1 . . . . . . . . 4054 1 84 . 1 1 24 24 LEU HA H 1 4.11 . . 1 . . . . . . . . 4054 1 85 . 1 1 24 24 LEU HB2 H 1 1.44 . . 2 . . . . . . . . 4054 1 86 . 1 1 24 24 LEU HD11 H 1 0.91 . . 2 . . . . . . . . 4054 1 87 . 1 1 24 24 LEU HD12 H 1 0.91 . . 2 . . . . . . . . 4054 1 88 . 1 1 24 24 LEU HD13 H 1 0.91 . . 2 . . . . . . . . 4054 1 89 . 1 1 24 24 LEU N N 15 121.3 . . 1 . . . . . . . . 4054 1 90 . 1 1 25 25 ILE H H 1 8.56 . . 1 . . . . . . . . 4054 1 91 . 1 1 25 25 ILE HA H 1 3.62 . . 1 . . . . . . . . 4054 1 92 . 1 1 25 25 ILE HB H 1 2.03 . . 1 . . . . . . . . 4054 1 93 . 1 1 25 25 ILE HG12 H 1 1.05 . . 2 . . . . . . . . 4054 1 94 . 1 1 25 25 ILE HD11 H 1 0.74 . . 1 . . . . . . . . 4054 1 95 . 1 1 25 25 ILE HD12 H 1 0.74 . . 1 . . . . . . . . 4054 1 96 . 1 1 25 25 ILE HD13 H 1 0.74 . . 1 . . . . . . . . 4054 1 97 . 1 1 25 25 ILE N N 15 119.4 . . 1 . . . . . . . . 4054 1 98 . 1 1 26 26 ASN H H 1 8.33 . . 1 . . . . . . . . 4054 1 99 . 1 1 26 26 ASN HA H 1 4.50 . . 1 . . . . . . . . 4054 1 100 . 1 1 26 26 ASN HB2 H 1 2.99 . . 2 . . . . . . . . 4054 1 101 . 1 1 26 26 ASN HB3 H 1 2.88 . . 2 . . . . . . . . 4054 1 102 . 1 1 26 26 ASN N N 15 119.5 . . 1 . . . . . . . . 4054 1 103 . 1 1 27 27 THR H H 1 8.23 . . 1 . . . . . . . . 4054 1 104 . 1 1 27 27 THR HA H 1 4.01 . . 1 . . . . . . . . 4054 1 105 . 1 1 27 27 THR HB H 1 4.39 . . 1 . . . . . . . . 4054 1 106 . 1 1 27 27 THR HG21 H 1 1.30 . . 1 . . . . . . . . 4054 1 107 . 1 1 27 27 THR HG22 H 1 1.30 . . 1 . . . . . . . . 4054 1 108 . 1 1 27 27 THR HG23 H 1 1.30 . . 1 . . . . . . . . 4054 1 109 . 1 1 27 27 THR N N 15 116.8 . . 1 . . . . . . . . 4054 1 110 . 1 1 28 28 LEU H H 1 8.03 . . 1 . . . . . . . . 4054 1 111 . 1 1 28 28 LEU HA H 1 4.01 . . 1 . . . . . . . . 4054 1 112 . 1 1 28 28 LEU HB2 H 1 2.04 . . 2 . . . . . . . . 4054 1 113 . 1 1 28 28 LEU HB3 H 1 1.44 . . 2 . . . . . . . . 4054 1 114 . 1 1 28 28 LEU HG H 1 1.93 . . 1 . . . . . . . . 4054 1 115 . 1 1 28 28 LEU HD11 H 1 0.91 . . 2 . . . . . . . . 4054 1 116 . 1 1 28 28 LEU HD12 H 1 0.91 . . 2 . . . . . . . . 4054 1 117 . 1 1 28 28 LEU HD13 H 1 0.91 . . 2 . . . . . . . . 4054 1 118 . 1 1 28 28 LEU N N 15 122.9 . . 1 . . . . . . . . 4054 1 119 . 1 1 29 29 GLN H H 1 8.72 . . 1 . . . . . . . . 4054 1 120 . 1 1 29 29 GLN HA H 1 3.90 . . 1 . . . . . . . . 4054 1 121 . 1 1 29 29 GLN HB2 H 1 2.24 . . 2 . . . . . . . . 4054 1 122 . 1 1 29 29 GLN HG2 H 1 2.50 . . 2 . . . . . . . . 4054 1 123 . 1 1 29 29 GLN HG3 H 1 2.35 . . 2 . . . . . . . . 4054 1 124 . 1 1 29 29 GLN N N 15 118.6 . . 1 . . . . . . . . 4054 1 125 . 1 1 30 30 GLN H H 1 8.01 . . 1 . . . . . . . . 4054 1 126 . 1 1 30 30 GLN HA H 1 4.11 . . 1 . . . . . . . . 4054 1 127 . 1 1 30 30 GLN HB2 H 1 2.25 . . 2 . . . . . . . . 4054 1 128 . 1 1 30 30 GLN HG2 H 1 2.64 . . 2 . . . . . . . . 4054 1 129 . 1 1 30 30 GLN HG3 H 1 2.46 . . 2 . . . . . . . . 4054 1 130 . 1 1 30 30 GLN N N 15 118.7 . . 1 . . . . . . . . 4054 1 131 . 1 1 31 31 LYS H H 1 8.16 . . 1 . . . . . . . . 4054 1 132 . 1 1 31 31 LYS HA H 1 4.15 . . 1 . . . . . . . . 4054 1 133 . 1 1 31 31 LYS HB2 H 1 2.14 . . 2 . . . . . . . . 4054 1 134 . 1 1 31 31 LYS HB3 H 1 2.03 . . 2 . . . . . . . . 4054 1 135 . 1 1 31 31 LYS N N 15 121.1 . . 1 . . . . . . . . 4054 1 136 . 1 1 32 32 LEU H H 1 8.55 . . 1 . . . . . . . . 4054 1 137 . 1 1 32 32 LEU HA H 1 4.05 . . 1 . . . . . . . . 4054 1 138 . 1 1 32 32 LEU HB2 H 1 1.93 . . 2 . . . . . . . . 4054 1 139 . 1 1 32 32 LEU HB3 H 1 1.72 . . 2 . . . . . . . . 4054 1 140 . 1 1 32 32 LEU HD11 H 1 0.91 . . 1 . . . . . . . . 4054 1 141 . 1 1 32 32 LEU HD12 H 1 0.91 . . 1 . . . . . . . . 4054 1 142 . 1 1 32 32 LEU HD13 H 1 0.91 . . 1 . . . . . . . . 4054 1 143 . 1 1 32 32 LEU N N 15 121.5 . . 1 . . . . . . . . 4054 1 144 . 1 1 33 33 GLU H H 1 8.12 . . 1 . . . . . . . . 4054 1 145 . 1 1 33 33 GLU HA H 1 4.08 . . 1 . . . . . . . . 4054 1 146 . 1 1 33 33 GLU HB2 H 1 2.15 . . 2 . . . . . . . . 4054 1 147 . 1 1 33 33 GLU HG2 H 1 2.43 . . 1 . . . . . . . . 4054 1 148 . 1 1 33 33 GLU HG3 H 1 2.32 . . 2 . . . . . . . . 4054 1 149 . 1 1 33 33 GLU N N 15 119.8 . . 1 . . . . . . . . 4054 1 150 . 1 1 34 34 ALA H H 1 7.71 . . 1 . . . . . . . . 4054 1 151 . 1 1 34 34 ALA HA H 1 4.19 . . 1 . . . . . . . . 4054 1 152 . 1 1 34 34 ALA HB1 H 1 1.58 . . 1 . . . . . . . . 4054 1 153 . 1 1 34 34 ALA HB2 H 1 1.58 . . 1 . . . . . . . . 4054 1 154 . 1 1 34 34 ALA HB3 H 1 1.58 . . 1 . . . . . . . . 4054 1 155 . 1 1 34 34 ALA N N 15 121.4 . . 1 . . . . . . . . 4054 1 156 . 1 1 35 35 VAL H H 1 8.08 . . 1 . . . . . . . . 4054 1 157 . 1 1 35 35 VAL HA H 1 3.73 . . 1 . . . . . . . . 4054 1 158 . 1 1 35 35 VAL HB H 1 2.32 . . 1 . . . . . . . . 4054 1 159 . 1 1 35 35 VAL HG11 H 1 1.09 . . 2 . . . . . . . . 4054 1 160 . 1 1 35 35 VAL HG12 H 1 1.09 . . 2 . . . . . . . . 4054 1 161 . 1 1 35 35 VAL HG13 H 1 1.09 . . 2 . . . . . . . . 4054 1 162 . 1 1 35 35 VAL HG21 H 1 0.91 . . 2 . . . . . . . . 4054 1 163 . 1 1 35 35 VAL HG22 H 1 0.91 . . 2 . . . . . . . . 4054 1 164 . 1 1 35 35 VAL HG23 H 1 0.91 . . 2 . . . . . . . . 4054 1 165 . 1 1 35 35 VAL N N 15 118.0 . . 1 . . . . . . . . 4054 1 166 . 1 1 36 36 ALA H H 1 8.47 . . 1 . . . . . . . . 4054 1 167 . 1 1 36 36 ALA HA H 1 3.97 . . 1 . . . . . . . . 4054 1 168 . 1 1 36 36 ALA HB1 H 1 1.54 . . 1 . . . . . . . . 4054 1 169 . 1 1 36 36 ALA HB2 H 1 1.54 . . 1 . . . . . . . . 4054 1 170 . 1 1 36 36 ALA HB3 H 1 1.54 . . 1 . . . . . . . . 4054 1 171 . 1 1 36 36 ALA N N 15 123.5 . . 1 . . . . . . . . 4054 1 172 . 1 1 37 37 LYS H H 1 7.90 . . 1 . . . . . . . . 4054 1 173 . 1 1 37 37 LYS HA H 1 4.12 . . 1 . . . . . . . . 4054 1 174 . 1 1 37 37 LYS HB2 H 1 1.97 . . 2 . . . . . . . . 4054 1 175 . 1 1 37 37 LYS N N 15 117.7 . . 1 . . . . . . . . 4054 1 176 . 1 1 38 38 ARG H H 1 7.65 . . 1 . . . . . . . . 4054 1 177 . 1 1 38 38 ARG HA H 1 4.15 . . 1 . . . . . . . . 4054 1 178 . 1 1 38 38 ARG HB2 H 1 2.04 . . 2 . . . . . . . . 4054 1 179 . 1 1 38 38 ARG N N 15 120.4 . . 1 . . . . . . . . 4054 1 180 . 1 1 39 39 ILE H H 1 8.11 . . 1 . . . . . . . . 4054 1 181 . 1 1 39 39 ILE HA H 1 3.73 . . 1 . . . . . . . . 4054 1 182 . 1 1 39 39 ILE HB H 1 1.93 . . 1 . . . . . . . . 4054 1 183 . 1 1 39 39 ILE HG12 H 1 1.76 . . 2 . . . . . . . . 4054 1 184 . 1 1 39 39 ILE HG21 H 1 0.91 . . 1 . . . . . . . . 4054 1 185 . 1 1 39 39 ILE HG22 H 1 0.91 . . 1 . . . . . . . . 4054 1 186 . 1 1 39 39 ILE HG23 H 1 0.91 . . 1 . . . . . . . . 4054 1 187 . 1 1 39 39 ILE HD11 H 1 0.88 . . 1 . . . . . . . . 4054 1 188 . 1 1 39 39 ILE HD12 H 1 0.88 . . 1 . . . . . . . . 4054 1 189 . 1 1 39 39 ILE HD13 H 1 0.88 . . 1 . . . . . . . . 4054 1 190 . 1 1 39 39 ILE N N 15 120.2 . . 1 . . . . . . . . 4054 1 191 . 1 1 40 40 GLU H H 1 7.97 . . 1 . . . . . . . . 4054 1 192 . 1 1 40 40 GLU HA H 1 4.11 . . 1 . . . . . . . . 4054 1 193 . 1 1 40 40 GLU HB2 H 1 2.14 . . 2 . . . . . . . . 4054 1 194 . 1 1 40 40 GLU N N 15 121.8 . . 1 . . . . . . . . 4054 1 195 . 1 1 41 41 ALA H H 1 7.53 . . 1 . . . . . . . . 4054 1 196 . 1 1 41 41 ALA HA H 1 4.18 . . 1 . . . . . . . . 4054 1 197 . 1 1 41 41 ALA HB1 H 1 1.51 . . 1 . . . . . . . . 4054 1 198 . 1 1 41 41 ALA HB2 H 1 1.51 . . 1 . . . . . . . . 4054 1 199 . 1 1 41 41 ALA HB3 H 1 1.51 . . 1 . . . . . . . . 4054 1 200 . 1 1 41 41 ALA N N 15 119.2 . . 1 . . . . . . . . 4054 1 201 . 1 1 42 42 LEU H H 1 7.43 . . 1 . . . . . . . . 4054 1 202 . 1 1 42 42 LEU HA H 1 4.08 . . 1 . . . . . . . . 4054 1 203 . 1 1 42 42 LEU HB2 H 1 2.04 . . 2 . . . . . . . . 4054 1 204 . 1 1 42 42 LEU HB3 H 1 1.47 . . 2 . . . . . . . . 4054 1 205 . 1 1 42 42 LEU HD11 H 1 0.88 . . 2 . . . . . . . . 4054 1 206 . 1 1 42 42 LEU HD12 H 1 0.88 . . 2 . . . . . . . . 4054 1 207 . 1 1 42 42 LEU HD13 H 1 0.88 . . 2 . . . . . . . . 4054 1 208 . 1 1 42 42 LEU N N 15 118.2 . . 1 . . . . . . . . 4054 1 209 . 1 1 43 43 GLU H H 1 8.52 . . 1 . . . . . . . . 4054 1 210 . 1 1 43 43 GLU HA H 1 3.87 . . 1 . . . . . . . . 4054 1 211 . 1 1 43 43 GLU HB2 H 1 2.32 . . 2 . . . . . . . . 4054 1 212 . 1 1 43 43 GLU HB3 H 1 1.97 . . 2 . . . . . . . . 4054 1 213 . 1 1 43 43 GLU HG2 H 1 2.53 . . 1 . . . . . . . . 4054 1 214 . 1 1 43 43 GLU HG3 H 1 2.25 . . 2 . . . . . . . . 4054 1 215 . 1 1 43 43 GLU N N 15 118.6 . . 1 . . . . . . . . 4054 1 216 . 1 1 44 44 ASN H H 1 7.63 . . 1 . . . . . . . . 4054 1 217 . 1 1 44 44 ASN HA H 1 4.64 . . 1 . . . . . . . . 4054 1 218 . 1 1 44 44 ASN HB2 H 1 2.85 . . 2 . . . . . . . . 4054 1 219 . 1 1 44 44 ASN N N 15 113.8 . . 1 . . . . . . . . 4054 1 220 . 1 1 45 45 LYS H H 1 7.56 . . 1 . . . . . . . . 4054 1 221 . 1 1 45 45 LYS HA H 1 4.36 . . 1 . . . . . . . . 4054 1 222 . 1 1 45 45 LYS HB2 H 1 1.93 . . 2 . . . . . . . . 4054 1 223 . 1 1 45 45 LYS HG2 H 1 1.51 . . 2 . . . . . . . . 4054 1 224 . 1 1 45 45 LYS HD2 H 1 1.65 . . 2 . . . . . . . . 4054 1 225 . 1 1 45 45 LYS N N 15 118.3 . . 1 . . . . . . . . 4054 1 226 . 1 1 46 46 ILE H H 1 7.51 . . 1 . . . . . . . . 4054 1 227 . 1 1 46 46 ILE HA H 1 4.26 . . 1 . . . . . . . . 4054 1 228 . 1 1 46 46 ILE HB H 1 1.93 . . 1 . . . . . . . . 4054 1 229 . 1 1 46 46 ILE HG12 H 1 1.26 . . 2 . . . . . . . . 4054 1 230 . 1 1 46 46 ILE HG21 H 1 0.91 . . 1 . . . . . . . . 4054 1 231 . 1 1 46 46 ILE HG22 H 1 0.91 . . 1 . . . . . . . . 4054 1 232 . 1 1 46 46 ILE HG23 H 1 0.91 . . 1 . . . . . . . . 4054 1 233 . 1 1 46 46 ILE N N 15 118.3 . . 1 . . . . . . . . 4054 1 234 . 1 1 47 47 ILE H H 1 7.41 . . 1 . . . . . . . . 4054 1 235 . 1 1 47 47 ILE HA H 1 4.05 . . 1 . . . . . . . . 4054 1 236 . 1 1 47 47 ILE HB H 1 1.86 . . 1 . . . . . . . . 4054 1 237 . 1 1 47 47 ILE HG12 H 1 1.48 . . 2 . . . . . . . . 4054 1 238 . 1 1 47 47 ILE HG13 H 1 1.19 . . 2 . . . . . . . . 4054 1 239 . 1 1 47 47 ILE HG21 H 1 0.91 . . 1 . . . . . . . . 4054 1 240 . 1 1 47 47 ILE HG22 H 1 0.91 . . 1 . . . . . . . . 4054 1 241 . 1 1 47 47 ILE HG23 H 1 0.91 . . 1 . . . . . . . . 4054 1 242 . 1 1 47 47 ILE N N 15 127.6 . . 1 . . . . . . . . 4054 1 stop_ save_