data_5989 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5989 _Entry.Title ; Cytotoxin I from the venom of the Central Asian cobra Naja Oxiana, in aqueous solution ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2003-10-31 _Entry.Accession_date 2003-10-31 _Entry.Last_release_date 2005-05-20 _Entry.Original_release_date 2005-05-20 _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 Maxim Dubinnyi . A. . 5989 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 2 5989 coupling_constants 1 5989 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 842 5989 'coupling constants' 107 5989 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 . . 2005-05-20 2003-10-31 original author . 5989 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5989 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 15584897 _Citation.Full_citation . _Citation.Title ; Interaction of three-finger toxins with phospholipid membranes: comparison of S- and P-type cytotoxins ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biochem. J.' _Citation.Journal_name_full . _Citation.Journal_volume 387 _Citation.Journal_issue 'Pt 3' _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 807 _Citation.Page_last 815 _Citation.Year 2005 _Citation.Details 'Structure determination in aqueous solution and in complex with DPC micelle.' 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 P. Dubovskii . V. . 5989 1 2 D. Lesovoy . M. . 5989 1 3 Maxim Dubinnyi . A. . 5989 1 4 A. Konshina . G. . 5989 1 5 Yuri Utkin . N. . 5989 1 6 R. Efremov . G. . 5989 1 7 Alexander Arseniev . S. . 5989 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'S-type cytotoxin' 5989 1 'tigtly bound water molecule cys/trans isomerisation' 5989 1 stop_ save_ save_ref-1 _Citation.Sf_category citations _Citation.Sf_framecode ref-1 _Citation.Entry_ID 5989 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Grishin E.V., Sukhikh A.P., Adamovich T.B., Ovchinnikov Y.A. "Isolation, properties and sequence determination of the two cytotoxins from the venom of the Middle-Asian cobra Naja Naja oxiana." Bioorg. Khim. 2:1018-1034(1976). ; _Citation.Title . _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _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 . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref-2 _Citation.Sf_category citations _Citation.Sf_framecode ref-2 _Citation.Entry_ID 5989 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Bartles C., Xia T., Billiter M., Guntert P., Wutrich K. "The program XEASY for computer-supported NMR spectral analysis of biological macromolecules" Journal of Biomolecular NMR, 1995, v.5 pp.1-10. ; _Citation.Title . _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _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 . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref-3 _Citation.Sf_category citations _Citation.Sf_framecode ref-3 _Citation.Entry_ID 5989 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 12051947 _Citation.Full_citation ; Herrmann T, Guntert P, Wuthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol. 2002 May 24;319(1):209-27. ; _Citation.Title 'Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 319 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _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 209 _Citation.Page_last 227 _Citation.Year 2002 _Citation.Details ; Combined automated NOE assignment and structure determination module (CANDID) is a new software for efficient NMR structure determination of proteins by automated assignment of the NOESY spectra. CANDID uses an iterative approach with multiple cycles of NOE cross-peak assignment and protein structure calculation using the fast DYANA torsion angle dynamics algorithm, so that the result from each CANDID cycle consists of exhaustive, possibly ambiguous NOE cross-peak assignments in all available spectra and a three-dimensional protein structure represented by a bundle of conformers. The input for the first CANDID cycle consists of the amino acid sequence, the chemical shift list from the sequence-specific resonance assignment, and listings of the cross-peak positions and volumes in one or several two, three or four-dimensional NOESY spectra. The input for the second and subsequent CANDID cycles contains the three-dimensional protein structure from the previous cycle, in addition to the complete input used for the first cycle. CANDID includes two new elements that make it robust with respect to the presence of artifacts in the input data, i.e. network-anchoring and constraint-combination, which have a key role in de novo protein structure determinations for the successful generation of the correct polypeptide fold by the first CANDID cycle. Network-anchoring makes use of the fact that any network of correct NOE cross-peak assignments forms a self-consistent set; the initial, chemical shift-based assignments for each individual NOE cross-peak are therefore weighted by the extent to which they can be embedded into the network formed by all other NOE cross-peak assignments. Constraint-combination reduces the deleterious impact of artifact NOE upper distance constraints in the input for a protein structure calculation by combining the assignments for two or several peaks into a single upper limit distance constraint, which lowers the probability that the presence of an artifact peak will influence the outcome of the structure calculation. CANDID test calculations were performed with NMR data sets of four proteins for which high-quality structures had previously been solved by interactive protocols, and they yielded comparable results to these reference structure determinations with regard to both the residual constraint violations, and the precision and accuracy of the atomic coordinates. The CANDID approach has further been validated by de novo NMR structure determinations of four additional proteins. The experience gained in these calculations shows that once nearly complete sequence-specific resonance assignments are available, the automated CANDID approach results in greatly enhanced efficiency of the NOESY spectral analysis. The fact that the correct fold is obtained in cycle 1 of a de novo structure calculation is the single most important advance achieved with CANDID, when compared with previously proposed automated NOESY assignment methods that do not use network-anchoring and constraint-combination. ; 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 Torsten Herrmann T. . . 5989 4 2 Peter Guntert P. . . 5989 4 3 Kurt Wuthrich K. . . 5989 4 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_CTI _Assembly.Sf_category assembly _Assembly.Sf_framecode system_CTI _Assembly.Entry_ID 5989 _Assembly.ID 1 _Assembly.Name 'Cytotoxin I' _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 'all disulfide bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5989 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 'CTI major form' 1 $CTI . . . native . . . . . 5989 1 2 'CTI minor form' 1 $CTI . . . native . . . . . 5989 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 3 3 SG . 1 . 1 CYS 21 21 SG . . . . . . . . . . 5989 1 2 disulfide single . 1 . 1 CYS 14 14 SG . 1 . 1 CYS 38 38 SG . . . . . . . . . . 5989 1 3 disulfide single . 1 . 1 CYS 42 42 SG . 1 . 1 CYS 53 53 SG . . . . . . . . . . 5989 1 4 disulfide single . 1 . 1 CYS 54 54 SG . 1 . 1 CYS 59 59 SG . . . . . . . . . . 5989 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 yes PDB 1RL5 . . . . . . 5989 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Cytotoxin I' system 5989 1 CTI abbreviation 5989 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'cell lysis' 5989 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_CTI _Entity.Sf_category entity _Entity.Sf_framecode CTI _Entity.Entry_ID 5989 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Cytotocin I' _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 ; LKCNKLVPIAYKTCPEGKNL CYKMFMMSDLTIPVKRGCID VCPKNSLLVKYVCCNTDRCN ; _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 60 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 6821 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 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 PDB 1RL5 . "Nmr Structure With Tightly Bound Water Molecule Of Cytotoxin I From Naja Oxiana In Aqueous Solution (Major Form)" . . . . . 100.00 60 100.00 100.00 1.20e-33 . . . . 5989 1 2 no PDB 1ZAD . "Structure Of Cytotoxin I (Cti) From Naja Oxiana In Complex With Dpc Micelle" . . . . . 100.00 60 100.00 100.00 1.20e-33 . . . . 5989 1 3 no GB AAB24495 . "Vc-1=cytotoxin [Naja oxiana=snakes, venom, Peptide, 59 aa]" . . . . . 100.00 59 98.33 98.33 5.76e-31 . . . . 5989 1 4 no PRF 763620A . "cytotoxin I" . . . . . 100.00 60 100.00 100.00 1.20e-33 . . . . 5989 1 5 no SP P01451 . "RecName: Full=Cytotoxin 1; AltName: Full=Cytotoxin I; Short=CTI [Naja oxiana]" . . . . . 100.00 60 100.00 100.00 1.20e-33 . . . . 5989 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Cytotocin I' common 5989 1 CTI abbreviation 5989 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 . LEU . 5989 1 2 . LYS . 5989 1 3 . CYS . 5989 1 4 . ASN . 5989 1 5 . LYS . 5989 1 6 . LEU . 5989 1 7 . VAL . 5989 1 8 . PRO . 5989 1 9 . ILE . 5989 1 10 . ALA . 5989 1 11 . TYR . 5989 1 12 . LYS . 5989 1 13 . THR . 5989 1 14 . CYS . 5989 1 15 . PRO . 5989 1 16 . GLU . 5989 1 17 . GLY . 5989 1 18 . LYS . 5989 1 19 . ASN . 5989 1 20 . LEU . 5989 1 21 . CYS . 5989 1 22 . TYR . 5989 1 23 . LYS . 5989 1 24 . MET . 5989 1 25 . PHE . 5989 1 26 . MET . 5989 1 27 . MET . 5989 1 28 . SER . 5989 1 29 . ASP . 5989 1 30 . LEU . 5989 1 31 . THR . 5989 1 32 . ILE . 5989 1 33 . PRO . 5989 1 34 . VAL . 5989 1 35 . LYS . 5989 1 36 . ARG . 5989 1 37 . GLY . 5989 1 38 . CYS . 5989 1 39 . ILE . 5989 1 40 . ASP . 5989 1 41 . VAL . 5989 1 42 . CYS . 5989 1 43 . PRO . 5989 1 44 . LYS . 5989 1 45 . ASN . 5989 1 46 . SER . 5989 1 47 . LEU . 5989 1 48 . LEU . 5989 1 49 . VAL . 5989 1 50 . LYS . 5989 1 51 . TYR . 5989 1 52 . VAL . 5989 1 53 . CYS . 5989 1 54 . CYS . 5989 1 55 . ASN . 5989 1 56 . THR . 5989 1 57 . ASP . 5989 1 58 . ARG . 5989 1 59 . CYS . 5989 1 60 . ASN . 5989 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 . LEU 1 1 5989 1 . LYS 2 2 5989 1 . CYS 3 3 5989 1 . ASN 4 4 5989 1 . LYS 5 5 5989 1 . LEU 6 6 5989 1 . VAL 7 7 5989 1 . PRO 8 8 5989 1 . ILE 9 9 5989 1 . ALA 10 10 5989 1 . TYR 11 11 5989 1 . LYS 12 12 5989 1 . THR 13 13 5989 1 . CYS 14 14 5989 1 . PRO 15 15 5989 1 . GLU 16 16 5989 1 . GLY 17 17 5989 1 . LYS 18 18 5989 1 . ASN 19 19 5989 1 . LEU 20 20 5989 1 . CYS 21 21 5989 1 . TYR 22 22 5989 1 . LYS 23 23 5989 1 . MET 24 24 5989 1 . PHE 25 25 5989 1 . MET 26 26 5989 1 . MET 27 27 5989 1 . SER 28 28 5989 1 . ASP 29 29 5989 1 . LEU 30 30 5989 1 . THR 31 31 5989 1 . ILE 32 32 5989 1 . PRO 33 33 5989 1 . VAL 34 34 5989 1 . LYS 35 35 5989 1 . ARG 36 36 5989 1 . GLY 37 37 5989 1 . CYS 38 38 5989 1 . ILE 39 39 5989 1 . ASP 40 40 5989 1 . VAL 41 41 5989 1 . CYS 42 42 5989 1 . PRO 43 43 5989 1 . LYS 44 44 5989 1 . ASN 45 45 5989 1 . SER 46 46 5989 1 . LEU 47 47 5989 1 . LEU 48 48 5989 1 . VAL 49 49 5989 1 . LYS 50 50 5989 1 . TYR 51 51 5989 1 . VAL 52 52 5989 1 . CYS 53 53 5989 1 . CYS 54 54 5989 1 . ASN 55 55 5989 1 . THR 56 56 5989 1 . ASP 57 57 5989 1 . ARG 58 58 5989 1 . CYS 59 59 5989 1 . ASN 60 60 5989 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 5989 _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 $CTI . 8657 organism . 'Naja Naja oxiana' 'Central Asian Cobra' . . Eukaryota Metazoa Naja 'Naja oxiana' . . . . venom . . . . . . . . . . . . . . . . 5989 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 5989 _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 $CTI . 'purified from the natural source' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5989 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5989 _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 'Cytotocin I' . . . 1 $CTI . . 3.0 . . mM . . . . 5989 1 2 KCl . . . . . . . 0.05 . . M . . . . 5989 1 stop_ save_ ####################### # Sample conditions # ####################### save_condition_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode condition_1 _Sample_condition_list.Entry_ID 5989 _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 6.0 0.2 pH 5989 1 temperature 303 1 K 5989 1 'ionic strength' 0.05 0.01 M 5989 1 stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 5989 _Software.ID 1 _Software.Name XWINNMR _Software.Version 3.1a _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'spectral data processing' 5989 1 stop_ save_ save_XEASY _Software.Sf_category software _Software.Sf_framecode XEASY _Software.Entry_ID 5989 _Software.ID 2 _Software.Name XEASY _Software.Version 1.2.11 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'peak picking' 5989 2 'sequence-specific assignment' 5989 2 'manual NOE assignment' 5989 2 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 3 $ref-2 5989 2 stop_ save_ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 5989 _Software.ID 3 _Software.Name CYANA _Software.Version 1.0.6 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'automated NOE assignment' 5989 3 'structure calculation' 5989 3 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 4 $ref-3 5989 3 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5989 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5989 _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 Bruker DRX . 500 . . . 5989 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 5989 _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 DQF-COSY . . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5989 1 2 TOCSY . . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5989 1 3 NOESY . . . . . . . . . . . 1 $sample_1 . . . 1 $condition_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5989 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5989 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . 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 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 5989 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_CTI_1H_Shifts_major _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode CTI_1H_Shifts_major _Assigned_chem_shift_list.Entry_ID 5989 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $condition_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _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_1 . 5989 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 1 1 LEU HA H 1 4.184 0.005 . 1 . . . . . . . . 5989 1 2 . 1 1 1 1 LEU HB2 H 1 1.568 0.002 . 2 . . . . . . . . 5989 1 3 . 1 1 1 1 LEU HD11 H 1 0.772 0.004 . 1 . . . . . . . . 5989 1 4 . 1 1 1 1 LEU HD12 H 1 0.772 0.004 . 1 . . . . . . . . 5989 1 5 . 1 1 1 1 LEU HD13 H 1 0.772 0.004 . 1 . . . . . . . . 5989 1 6 . 1 1 1 1 LEU HD21 H 1 0.853 0.005 . 1 . . . . . . . . 5989 1 7 . 1 1 1 1 LEU HD22 H 1 0.853 0.005 . 1 . . . . . . . . 5989 1 8 . 1 1 1 1 LEU HD23 H 1 0.853 0.005 . 1 . . . . . . . . 5989 1 9 . 1 1 1 1 LEU HG H 1 1.508 0.005 . 1 . . . . . . . . 5989 1 10 . 1 1 2 2 LYS H H 1 8.590 0.002 . 1 . . . . . . . . 5989 1 11 . 1 1 2 2 LYS HA H 1 5.391 0.016 . 1 . . . . . . . . 5989 1 12 . 1 1 2 2 LYS HB2 H 1 1.323 0.002 . 1 . . . . . . . . 5989 1 13 . 1 1 2 2 LYS HB3 H 1 1.172 0.118 . 1 . . . . . . . . 5989 1 14 . 1 1 2 2 LYS HG2 H 1 1.120 0.000 . 2 . . . . . . . . 5989 1 15 . 1 1 2 2 LYS HD2 H 1 1.204 0.004 . 2 . . . . . . . . 5989 1 16 . 1 1 2 2 LYS HE2 H 1 2.820 0.000 . 2 . . . . . . . . 5989 1 17 . 1 1 3 3 CYS H H 1 8.819 0.000 . 1 . . . . . . . . 5989 1 18 . 1 1 3 3 CYS HA H 1 5.146 0.005 . 1 . . . . . . . . 5989 1 19 . 1 1 3 3 CYS HB2 H 1 2.492 0.003 . 1 . . . . . . . . 5989 1 20 . 1 1 3 3 CYS HB3 H 1 2.844 0.000 . 1 . . . . . . . . 5989 1 21 . 1 1 4 4 ASN H H 1 9.695 0.000 . 1 . . . . . . . . 5989 1 22 . 1 1 4 4 ASN HA H 1 4.949 0.007 . 1 . . . . . . . . 5989 1 23 . 1 1 4 4 ASN HB2 H 1 2.299 0.001 . 1 . . . . . . . . 5989 1 24 . 1 1 4 4 ASN HB3 H 1 2.710 0.002 . 1 . . . . . . . . 5989 1 25 . 1 1 4 4 ASN HD21 H 1 7.572 0.000 . 1 . . . . . . . . 5989 1 26 . 1 1 4 4 ASN HD22 H 1 6.643 0.003 . 1 . . . . . . . . 5989 1 27 . 1 1 5 5 LYS H H 1 7.915 0.005 . 1 . . . . . . . . 5989 1 28 . 1 1 5 5 LYS HA H 1 4.245 0.005 . 1 . . . . . . . . 5989 1 29 . 1 1 5 5 LYS HB2 H 1 1.552 0.000 . 1 . . . . . . . . 5989 1 30 . 1 1 5 5 LYS HB3 H 1 2.088 0.001 . 1 . . . . . . . . 5989 1 31 . 1 1 5 5 LYS HG2 H 1 1.254 0.007 . 2 . . . . . . . . 5989 1 32 . 1 1 5 5 LYS HD2 H 1 1.379 0.004 . 2 . . . . . . . . 5989 1 33 . 1 1 5 5 LYS HE2 H 1 2.888 0.005 . 2 . . . . . . . . 5989 1 34 . 1 1 6 6 LEU H H 1 8.173 0.001 . 1 . . . . . . . . 5989 1 35 . 1 1 6 6 LEU HA H 1 3.675 0.000 . 1 . . . . . . . . 5989 1 36 . 1 1 6 6 LEU HB2 H 1 1.652 0.000 . 1 . . . . . . . . 5989 1 37 . 1 1 6 6 LEU HB3 H 1 1.792 0.000 . 1 . . . . . . . . 5989 1 38 . 1 1 6 6 LEU HD11 H 1 0.701 0.003 . 1 . . . . . . . . 5989 1 39 . 1 1 6 6 LEU HD12 H 1 0.701 0.003 . 1 . . . . . . . . 5989 1 40 . 1 1 6 6 LEU HD13 H 1 0.701 0.003 . 1 . . . . . . . . 5989 1 41 . 1 1 6 6 LEU HD21 H 1 0.876 0.001 . 1 . . . . . . . . 5989 1 42 . 1 1 6 6 LEU HD22 H 1 0.876 0.001 . 1 . . . . . . . . 5989 1 43 . 1 1 6 6 LEU HD23 H 1 0.876 0.001 . 1 . . . . . . . . 5989 1 44 . 1 1 6 6 LEU HG H 1 1.547 0.000 . 1 . . . . . . . . 5989 1 45 . 1 1 7 7 VAL H H 1 7.548 0.000 . 1 . . . . . . . . 5989 1 46 . 1 1 7 7 VAL HA H 1 4.471 0.006 . 1 . . . . . . . . 5989 1 47 . 1 1 7 7 VAL HB H 1 2.123 0.005 . 1 . . . . . . . . 5989 1 48 . 1 1 7 7 VAL HG11 H 1 0.974 0.000 . 1 . . . . . . . . 5989 1 49 . 1 1 7 7 VAL HG12 H 1 0.974 0.000 . 1 . . . . . . . . 5989 1 50 . 1 1 7 7 VAL HG13 H 1 0.974 0.000 . 1 . . . . . . . . 5989 1 51 . 1 1 7 7 VAL HG21 H 1 1.004 0.004 . 1 . . . . . . . . 5989 1 52 . 1 1 7 7 VAL HG22 H 1 1.004 0.004 . 1 . . . . . . . . 5989 1 53 . 1 1 7 7 VAL HG23 H 1 1.004 0.004 . 1 . . . . . . . . 5989 1 54 . 1 1 8 8 PRO HA H 1 4.536 0.002 . 1 . . . . . . . . 5989 1 55 . 1 1 8 8 PRO HB2 H 1 1.856 0.005 . 1 . . . . . . . . 5989 1 56 . 1 1 8 8 PRO HB3 H 1 2.245 0.004 . 1 . . . . . . . . 5989 1 57 . 1 1 8 8 PRO HG2 H 1 1.920 0.000 . 1 . . . . . . . . 5989 1 58 . 1 1 8 8 PRO HG3 H 1 1.986 0.002 . 1 . . . . . . . . 5989 1 59 . 1 1 8 8 PRO HD2 H 1 3.835 0.000 . 1 . . . . . . . . 5989 1 60 . 1 1 8 8 PRO HD3 H 1 3.979 0.000 . 1 . . . . . . . . 5989 1 61 . 1 1 9 9 ILE H H 1 7.060 0.000 . 1 . . . . . . . . 5989 1 62 . 1 1 9 9 ILE HA H 1 4.190 0.000 . 1 . . . . . . . . 5989 1 63 . 1 1 9 9 ILE HB H 1 2.070 0.003 . 1 . . . . . . . . 5989 1 64 . 1 1 9 9 ILE HG12 H 1 1.093 0.000 . 1 . . . . . . . . 5989 1 65 . 1 1 9 9 ILE HG13 H 1 1.001 0.001 . 1 . . . . . . . . 5989 1 66 . 1 1 9 9 ILE HG21 H 1 0.910 0.004 . 1 . . . . . . . . 5989 1 67 . 1 1 9 9 ILE HG22 H 1 0.910 0.004 . 1 . . . . . . . . 5989 1 68 . 1 1 9 9 ILE HG23 H 1 0.910 0.004 . 1 . . . . . . . . 5989 1 69 . 1 1 9 9 ILE HD11 H 1 1.331 0.000 . 1 . . . . . . . . 5989 1 70 . 1 1 9 9 ILE HD12 H 1 1.331 0.000 . 1 . . . . . . . . 5989 1 71 . 1 1 9 9 ILE HD13 H 1 1.331 0.000 . 1 . . . . . . . . 5989 1 72 . 1 1 10 10 ALA H H 1 7.871 0.000 . 1 . . . . . . . . 5989 1 73 . 1 1 10 10 ALA HA H 1 4.624 0.004 . 1 . . . . . . . . 5989 1 74 . 1 1 10 10 ALA HB1 H 1 1.376 0.002 . 1 . . . . . . . . 5989 1 75 . 1 1 10 10 ALA HB2 H 1 1.376 0.002 . 1 . . . . . . . . 5989 1 76 . 1 1 10 10 ALA HB3 H 1 1.376 0.002 . 1 . . . . . . . . 5989 1 77 . 1 1 11 11 TYR H H 1 7.845 0.000 . 1 . . . . . . . . 5989 1 78 . 1 1 11 11 TYR HA H 1 5.317 0.005 . 1 . . . . . . . . 5989 1 79 . 1 1 11 11 TYR HB2 H 1 2.700 0.004 . 1 . . . . . . . . 5989 1 80 . 1 1 11 11 TYR HB3 H 1 2.837 0.003 . 1 . . . . . . . . 5989 1 81 . 1 1 11 11 TYR HD1 H 1 6.734 0.001 . 2 . . . . . . . . 5989 1 82 . 1 1 11 11 TYR HE1 H 1 6.793 0.002 . 2 . . . . . . . . 5989 1 83 . 1 1 12 12 LYS H H 1 8.982 0.105 . 1 . . . . . . . . 5989 1 84 . 1 1 12 12 LYS HA H 1 4.770 0.000 . 1 . . . . . . . . 5989 1 85 . 1 1 12 12 LYS HB2 H 1 1.730 0.000 . 1 . . . . . . . . 5989 1 86 . 1 1 12 12 LYS HB3 H 1 1.432 0.000 . 1 . . . . . . . . 5989 1 87 . 1 1 12 12 LYS HG2 H 1 1.280 0.000 . 1 . . . . . . . . 5989 1 88 . 1 1 12 12 LYS HG3 H 1 1.410 0.000 . 1 . . . . . . . . 5989 1 89 . 1 1 12 12 LYS HD2 H 1 1.710 0.000 . 2 . . . . . . . . 5989 1 90 . 1 1 12 12 LYS HE2 H 1 3.010 0.000 . 2 . . . . . . . . 5989 1 91 . 1 1 13 13 THR H H 1 8.726 0.001 . 1 . . . . . . . . 5989 1 92 . 1 1 13 13 THR HA H 1 4.666 0.002 . 1 . . . . . . . . 5989 1 93 . 1 1 13 13 THR HB H 1 4.074 0.005 . 1 . . . . . . . . 5989 1 94 . 1 1 13 13 THR HG21 H 1 1.270 0.009 . 1 . . . . . . . . 5989 1 95 . 1 1 13 13 THR HG22 H 1 1.270 0.009 . 1 . . . . . . . . 5989 1 96 . 1 1 13 13 THR HG23 H 1 1.270 0.009 . 1 . . . . . . . . 5989 1 97 . 1 1 14 14 CYS H H 1 9.143 0.000 . 1 . . . . . . . . 5989 1 98 . 1 1 14 14 CYS HA H 1 4.987 0.006 . 1 . . . . . . . . 5989 1 99 . 1 1 14 14 CYS HB2 H 1 2.842 0.003 . 1 . . . . . . . . 5989 1 100 . 1 1 14 14 CYS HB3 H 1 3.527 0.008 . 1 . . . . . . . . 5989 1 101 . 1 1 15 15 PRO HA H 1 4.625 0.001 . 1 . . . . . . . . 5989 1 102 . 1 1 15 15 PRO HB2 H 1 2.414 0.003 . 1 . . . . . . . . 5989 1 103 . 1 1 15 15 PRO HB3 H 1 1.971 0.005 . 1 . . . . . . . . 5989 1 104 . 1 1 15 15 PRO HG2 H 1 1.927 0.000 . 1 . . . . . . . . 5989 1 105 . 1 1 15 15 PRO HG3 H 1 2.184 0.003 . 1 . . . . . . . . 5989 1 106 . 1 1 15 15 PRO HD2 H 1 3.447 0.003 . 1 . . . . . . . . 5989 1 107 . 1 1 15 15 PRO HD3 H 1 3.995 0.005 . 1 . . . . . . . . 5989 1 108 . 1 1 16 16 GLU H H 1 8.572 0.000 . 1 . . . . . . . . 5989 1 109 . 1 1 16 16 GLU HA H 1 4.032 0.003 . 1 . . . . . . . . 5989 1 110 . 1 1 16 16 GLU HB2 H 1 1.961 0.000 . 1 . . . . . . . . 5989 1 111 . 1 1 16 16 GLU HB3 H 1 2.311 0.004 . 1 . . . . . . . . 5989 1 112 . 1 1 16 16 GLU HG2 H 1 2.012 0.000 . 2 . . . . . . . . 5989 1 113 . 1 1 17 17 GLY H H 1 8.894 0.000 . 1 . . . . . . . . 5989 1 114 . 1 1 17 17 GLY HA2 H 1 3.679 0.001 . 1 . . . . . . . . 5989 1 115 . 1 1 17 17 GLY HA3 H 1 4.301 0.003 . 1 . . . . . . . . 5989 1 116 . 1 1 18 18 LYS H H 1 7.613 0.000 . 1 . . . . . . . . 5989 1 117 . 1 1 18 18 LYS HA H 1 4.297 0.002 . 1 . . . . . . . . 5989 1 118 . 1 1 18 18 LYS HB2 H 1 1.936 0.000 . 2 . . . . . . . . 5989 1 119 . 1 1 18 18 LYS HG2 H 1 1.101 0.007 . 2 . . . . . . . . 5989 1 120 . 1 1 18 18 LYS HD2 H 1 1.360 0.000 . 1 . . . . . . . . 5989 1 121 . 1 1 18 18 LYS HD3 H 1 1.410 0.000 . 1 . . . . . . . . 5989 1 122 . 1 1 18 18 LYS HE2 H 1 2.960 0.000 . 2 . . . . . . . . 5989 1 123 . 1 1 18 18 LYS HZ1 H 1 7.700 0.000 . 1 . . . . . . . . 5989 1 124 . 1 1 18 18 LYS HZ2 H 1 7.700 0.000 . 1 . . . . . . . . 5989 1 125 . 1 1 18 18 LYS HZ3 H 1 7.700 0.000 . 1 . . . . . . . . 5989 1 126 . 1 1 19 19 ASN H H 1 7.929 0.000 . 1 . . . . . . . . 5989 1 127 . 1 1 19 19 ASN HA H 1 4.945 0.002 . 1 . . . . . . . . 5989 1 128 . 1 1 19 19 ASN HB2 H 1 3.017 0.000 . 1 . . . . . . . . 5989 1 129 . 1 1 19 19 ASN HB3 H 1 2.656 0.002 . 1 . . . . . . . . 5989 1 130 . 1 1 19 19 ASN HD21 H 1 7.488 0.000 . 1 . . . . . . . . 5989 1 131 . 1 1 19 19 ASN HD22 H 1 7.024 0.000 . 1 . . . . . . . . 5989 1 132 . 1 1 20 20 LEU H H 1 8.224 0.003 . 1 . . . . . . . . 5989 1 133 . 1 1 20 20 LEU HA H 1 4.858 0.008 . 1 . . . . . . . . 5989 1 134 . 1 1 20 20 LEU HB2 H 1 1.681 0.005 . 1 . . . . . . . . 5989 1 135 . 1 1 20 20 LEU HB3 H 1 1.391 0.001 . 1 . . . . . . . . 5989 1 136 . 1 1 20 20 LEU HD11 H 1 0.754 0.007 . 1 . . . . . . . . 5989 1 137 . 1 1 20 20 LEU HD12 H 1 0.754 0.007 . 1 . . . . . . . . 5989 1 138 . 1 1 20 20 LEU HD13 H 1 0.754 0.007 . 1 . . . . . . . . 5989 1 139 . 1 1 20 20 LEU HD21 H 1 0.892 0.006 . 1 . . . . . . . . 5989 1 140 . 1 1 20 20 LEU HD22 H 1 0.892 0.006 . 1 . . . . . . . . 5989 1 141 . 1 1 20 20 LEU HD23 H 1 0.892 0.006 . 1 . . . . . . . . 5989 1 142 . 1 1 20 20 LEU HG H 1 1.517 0.000 . 1 . . . . . . . . 5989 1 143 . 1 1 21 21 CYS H H 1 9.020 0.004 . 1 . . . . . . . . 5989 1 144 . 1 1 21 21 CYS HA H 1 6.108 0.000 . 1 . . . . . . . . 5989 1 145 . 1 1 21 21 CYS HB2 H 1 2.974 0.000 . 1 . . . . . . . . 5989 1 146 . 1 1 21 21 CYS HB3 H 1 3.040 0.000 . 1 . . . . . . . . 5989 1 147 . 1 1 22 22 TYR H H 1 8.967 0.000 . 1 . . . . . . . . 5989 1 148 . 1 1 22 22 TYR HA H 1 6.095 0.000 . 1 . . . . . . . . 5989 1 149 . 1 1 22 22 TYR HB2 H 1 3.123 0.000 . 1 . . . . . . . . 5989 1 150 . 1 1 22 22 TYR HB3 H 1 2.982 0.000 . 1 . . . . . . . . 5989 1 151 . 1 1 22 22 TYR HD1 H 1 6.839 0.003 . 2 . . . . . . . . 5989 1 152 . 1 1 22 22 TYR HE1 H 1 6.607 0.003 . 2 . . . . . . . . 5989 1 153 . 1 1 23 23 LYS H H 1 9.062 0.000 . 1 . . . . . . . . 5989 1 154 . 1 1 23 23 LYS HA H 1 4.859 0.007 . 1 . . . . . . . . 5989 1 155 . 1 1 23 23 LYS HB2 H 1 1.505 0.007 . 1 . . . . . . . . 5989 1 156 . 1 1 23 23 LYS HB3 H 1 1.659 0.002 . 1 . . . . . . . . 5989 1 157 . 1 1 23 23 LYS HG2 H 1 1.423 0.008 . 2 . . . . . . . . 5989 1 158 . 1 1 23 23 LYS HD2 H 1 1.756 0.000 . 2 . . . . . . . . 5989 1 159 . 1 1 23 23 LYS HE2 H 1 3.060 0.000 . 2 . . . . . . . . 5989 1 160 . 1 1 23 23 LYS HZ1 H 1 7.860 0.000 . 1 . . . . . . . . 5989 1 161 . 1 1 23 23 LYS HZ2 H 1 7.860 0.000 . 1 . . . . . . . . 5989 1 162 . 1 1 23 23 LYS HZ3 H 1 7.860 0.000 . 1 . . . . . . . . 5989 1 163 . 1 1 24 24 MET H H 1 8.297 0.004 . 1 . . . . . . . . 5989 1 164 . 1 1 24 24 MET HA H 1 5.151 0.005 . 1 . . . . . . . . 5989 1 165 . 1 1 24 24 MET HB2 H 1 1.787 0.000 . 1 . . . . . . . . 5989 1 166 . 1 1 24 24 MET HB3 H 1 1.693 0.004 . 1 . . . . . . . . 5989 1 167 . 1 1 24 24 MET HG2 H 1 1.317 0.007 . 1 . . . . . . . . 5989 1 168 . 1 1 24 24 MET HG3 H 1 1.546 0.007 . 1 . . . . . . . . 5989 1 169 . 1 1 24 24 MET HE1 H 1 2.080 0.000 . 1 . . . . . . . . 5989 1 170 . 1 1 24 24 MET HE2 H 1 2.080 0.000 . 1 . . . . . . . . 5989 1 171 . 1 1 24 24 MET HE3 H 1 2.080 0.000 . 1 . . . . . . . . 5989 1 172 . 1 1 25 25 PHE H H 1 9.508 0.003 . 1 . . . . . . . . 5989 1 173 . 1 1 25 25 PHE HA H 1 4.862 0.005 . 1 . . . . . . . . 5989 1 174 . 1 1 25 25 PHE HB2 H 1 2.491 0.003 . 1 . . . . . . . . 5989 1 175 . 1 1 25 25 PHE HB3 H 1 3.396 0.004 . 1 . . . . . . . . 5989 1 176 . 1 1 25 25 PHE HD1 H 1 7.082 0.004 . 2 . . . . . . . . 5989 1 177 . 1 1 25 25 PHE HE1 H 1 6.941 0.002 . 2 . . . . . . . . 5989 1 178 . 1 1 25 25 PHE HZ H 1 7.188 0.002 . 1 . . . . . . . . 5989 1 179 . 1 1 26 26 MET H H 1 9.304 0.005 . 1 . . . . . . . . 5989 1 180 . 1 1 26 26 MET HA H 1 5.114 0.005 . 1 . . . . . . . . 5989 1 181 . 1 1 26 26 MET HB2 H 1 2.033 0.005 . 1 . . . . . . . . 5989 1 182 . 1 1 26 26 MET HB3 H 1 2.352 0.003 . 1 . . . . . . . . 5989 1 183 . 1 1 26 26 MET HG2 H 1 2.632 0.007 . 1 . . . . . . . . 5989 1 184 . 1 1 26 26 MET HG3 H 1 2.865 0.003 . 1 . . . . . . . . 5989 1 185 . 1 1 26 26 MET HE1 H 1 1.860 0.000 . 1 . . . . . . . . 5989 1 186 . 1 1 26 26 MET HE2 H 1 1.860 0.000 . 1 . . . . . . . . 5989 1 187 . 1 1 26 26 MET HE3 H 1 1.860 0.000 . 1 . . . . . . . . 5989 1 188 . 1 1 27 27 MET H H 1 8.371 0.000 . 1 . . . . . . . . 5989 1 189 . 1 1 27 27 MET HA H 1 4.157 0.005 . 1 . . . . . . . . 5989 1 190 . 1 1 27 27 MET HB2 H 1 1.916 0.004 . 1 . . . . . . . . 5989 1 191 . 1 1 27 27 MET HB3 H 1 2.030 0.003 . 1 . . . . . . . . 5989 1 192 . 1 1 27 27 MET HG2 H 1 2.119 0.000 . 1 . . . . . . . . 5989 1 193 . 1 1 27 27 MET HG3 H 1 2.643 0.004 . 1 . . . . . . . . 5989 1 194 . 1 1 27 27 MET HE1 H 1 2.080 0.000 . 1 . . . . . . . . 5989 1 195 . 1 1 27 27 MET HE2 H 1 2.080 0.000 . 1 . . . . . . . . 5989 1 196 . 1 1 27 27 MET HE3 H 1 2.080 0.000 . 1 . . . . . . . . 5989 1 197 . 1 1 28 28 SER H H 1 7.664 0.000 . 1 . . . . . . . . 5989 1 198 . 1 1 28 28 SER HA H 1 4.206 0.003 . 1 . . . . . . . . 5989 1 199 . 1 1 28 28 SER HB2 H 1 3.810 0.007 . 1 . . . . . . . . 5989 1 200 . 1 1 28 28 SER HB3 H 1 4.067 0.005 . 1 . . . . . . . . 5989 1 201 . 1 1 29 29 ASP H H 1 7.944 0.000 . 1 . . . . . . . . 5989 1 202 . 1 1 29 29 ASP HA H 1 4.672 0.004 . 1 . . . . . . . . 5989 1 203 . 1 1 29 29 ASP HB2 H 1 2.705 0.005 . 1 . . . . . . . . 5989 1 204 . 1 1 29 29 ASP HB3 H 1 2.904 0.009 . 1 . . . . . . . . 5989 1 205 . 1 1 30 30 LEU H H 1 8.792 0.000 . 1 . . . . . . . . 5989 1 206 . 1 1 30 30 LEU HA H 1 4.039 0.000 . 1 . . . . . . . . 5989 1 207 . 1 1 30 30 LEU HB2 H 1 1.483 0.000 . 1 . . . . . . . . 5989 1 208 . 1 1 30 30 LEU HB3 H 1 1.320 0.000 . 1 . . . . . . . . 5989 1 209 . 1 1 30 30 LEU HD11 H 1 0.677 0.001 . 1 . . . . . . . . 5989 1 210 . 1 1 30 30 LEU HD12 H 1 0.677 0.001 . 1 . . . . . . . . 5989 1 211 . 1 1 30 30 LEU HD13 H 1 0.677 0.001 . 1 . . . . . . . . 5989 1 212 . 1 1 30 30 LEU HD21 H 1 0.830 0.000 . 1 . . . . . . . . 5989 1 213 . 1 1 30 30 LEU HD22 H 1 0.830 0.000 . 1 . . . . . . . . 5989 1 214 . 1 1 30 30 LEU HD23 H 1 0.830 0.000 . 1 . . . . . . . . 5989 1 215 . 1 1 30 30 LEU HG H 1 1.630 0.000 . 1 . . . . . . . . 5989 1 216 . 1 1 31 31 THR H H 1 8.693 0.000 . 1 . . . . . . . . 5989 1 217 . 1 1 31 31 THR HA H 1 4.418 0.004 . 1 . . . . . . . . 5989 1 218 . 1 1 31 31 THR HB H 1 4.321 0.002 . 1 . . . . . . . . 5989 1 219 . 1 1 31 31 THR HG21 H 1 1.196 0.002 . 1 . . . . . . . . 5989 1 220 . 1 1 31 31 THR HG22 H 1 1.196 0.002 . 1 . . . . . . . . 5989 1 221 . 1 1 31 31 THR HG23 H 1 1.196 0.002 . 1 . . . . . . . . 5989 1 222 . 1 1 32 32 ILE H H 1 7.117 0.000 . 1 . . . . . . . . 5989 1 223 . 1 1 32 32 ILE HA H 1 4.871 0.003 . 1 . . . . . . . . 5989 1 224 . 1 1 32 32 ILE HB H 1 1.881 0.000 . 1 . . . . . . . . 5989 1 225 . 1 1 32 32 ILE HG21 H 1 0.900 0.000 . 1 . . . . . . . . 5989 1 226 . 1 1 32 32 ILE HG22 H 1 0.900 0.000 . 1 . . . . . . . . 5989 1 227 . 1 1 32 32 ILE HG23 H 1 0.900 0.000 . 1 . . . . . . . . 5989 1 228 . 1 1 32 32 ILE HG12 H 1 1.170 0.000 . 1 . . . . . . . . 5989 1 229 . 1 1 32 32 ILE HG13 H 1 1.210 0.000 . 1 . . . . . . . . 5989 1 230 . 1 1 32 32 ILE HD11 H 1 1.633 0.005 . 1 . . . . . . . . 5989 1 231 . 1 1 32 32 ILE HD12 H 1 1.633 0.005 . 1 . . . . . . . . 5989 1 232 . 1 1 32 32 ILE HD13 H 1 1.633 0.005 . 1 . . . . . . . . 5989 1 233 . 1 1 33 33 PRO HA H 1 4.054 0.010 . 1 . . . . . . . . 5989 1 234 . 1 1 33 33 PRO HB2 H 1 1.215 0.006 . 1 . . . . . . . . 5989 1 235 . 1 1 33 33 PRO HB3 H 1 1.498 0.005 . 1 . . . . . . . . 5989 1 236 . 1 1 33 33 PRO HG2 H 1 1.658 0.002 . 1 . . . . . . . . 5989 1 237 . 1 1 33 33 PRO HG3 H 1 1.910 0.000 . 1 . . . . . . . . 5989 1 238 . 1 1 33 33 PRO HD2 H 1 3.858 0.003 . 1 . . . . . . . . 5989 1 239 . 1 1 33 33 PRO HD3 H 1 3.948 0.003 . 1 . . . . . . . . 5989 1 240 . 1 1 34 34 VAL H H 1 8.747 0.004 . 1 . . . . . . . . 5989 1 241 . 1 1 34 34 VAL HA H 1 4.425 0.001 . 1 . . . . . . . . 5989 1 242 . 1 1 34 34 VAL HB H 1 2.295 0.003 . 1 . . . . . . . . 5989 1 243 . 1 1 34 34 VAL HG11 H 1 0.832 0.006 . 1 . . . . . . . . 5989 1 244 . 1 1 34 34 VAL HG12 H 1 0.832 0.006 . 1 . . . . . . . . 5989 1 245 . 1 1 34 34 VAL HG13 H 1 0.832 0.006 . 1 . . . . . . . . 5989 1 246 . 1 1 34 34 VAL HG21 H 1 1.032 0.002 . 1 . . . . . . . . 5989 1 247 . 1 1 34 34 VAL HG22 H 1 1.032 0.002 . 1 . . . . . . . . 5989 1 248 . 1 1 34 34 VAL HG23 H 1 1.032 0.002 . 1 . . . . . . . . 5989 1 249 . 1 1 35 35 LYS H H 1 7.355 0.005 . 1 . . . . . . . . 5989 1 250 . 1 1 35 35 LYS HA H 1 4.560 0.003 . 1 . . . . . . . . 5989 1 251 . 1 1 35 35 LYS HB2 H 1 1.727 0.005 . 1 . . . . . . . . 5989 1 252 . 1 1 35 35 LYS HB3 H 1 1.978 0.011 . 1 . . . . . . . . 5989 1 253 . 1 1 35 35 LYS HG2 H 1 1.550 0.000 . 1 . . . . . . . . 5989 1 254 . 1 1 35 35 LYS HG3 H 1 1.633 0.000 . 1 . . . . . . . . 5989 1 255 . 1 1 35 35 LYS HD2 H 1 1.790 0.000 . 1 . . . . . . . . 5989 1 256 . 1 1 35 35 LYS HD3 H 1 1.856 0.000 . 1 . . . . . . . . 5989 1 257 . 1 1 35 35 LYS HE2 H 1 3.054 0.002 . 2 . . . . . . . . 5989 1 258 . 1 1 35 35 LYS HZ1 H 1 7.530 0.000 . 1 . . . . . . . . 5989 1 259 . 1 1 35 35 LYS HZ2 H 1 7.530 0.000 . 1 . . . . . . . . 5989 1 260 . 1 1 35 35 LYS HZ3 H 1 7.530 0.000 . 1 . . . . . . . . 5989 1 261 . 1 1 36 36 ARG H H 1 8.224 0.011 . 1 . . . . . . . . 5989 1 262 . 1 1 36 36 ARG HA H 1 4.400 0.009 . 1 . . . . . . . . 5989 1 263 . 1 1 36 36 ARG HB2 H 1 1.034 0.000 . 1 . . . . . . . . 5989 1 264 . 1 1 36 36 ARG HB3 H 1 1.496 0.004 . 1 . . . . . . . . 5989 1 265 . 1 1 36 36 ARG HG2 H 1 1.390 0.003 . 1 . . . . . . . . 5989 1 266 . 1 1 36 36 ARG HG3 H 1 1.550 0.004 . 1 . . . . . . . . 5989 1 267 . 1 1 36 36 ARG HD2 H 1 3.037 0.008 . 2 . . . . . . . . 5989 1 268 . 1 1 36 36 ARG HE H 1 7.862 0.000 . 1 . . . . . . . . 5989 1 269 . 1 1 37 37 GLY H H 1 6.506 0.004 . 1 . . . . . . . . 5989 1 270 . 1 1 37 37 GLY HA2 H 1 3.873 0.006 . 1 . . . . . . . . 5989 1 271 . 1 1 37 37 GLY HA3 H 1 4.154 0.009 . 1 . . . . . . . . 5989 1 272 . 1 1 38 38 CYS H H 1 8.666 0.003 . 1 . . . . . . . . 5989 1 273 . 1 1 38 38 CYS HA H 1 5.968 0.004 . 1 . . . . . . . . 5989 1 274 . 1 1 38 38 CYS HB2 H 1 3.461 0.005 . 1 . . . . . . . . 5989 1 275 . 1 1 38 38 CYS HB3 H 1 2.930 0.009 . 1 . . . . . . . . 5989 1 276 . 1 1 39 39 ILE H H 1 9.830 0.867 . 1 . . . . . . . . 5989 1 277 . 1 1 39 39 ILE HA H 1 4.416 0.006 . 1 . . . . . . . . 5989 1 278 . 1 1 39 39 ILE HB H 1 1.733 0.008 . 1 . . . . . . . . 5989 1 279 . 1 1 39 39 ILE HG21 H 1 0.571 0.005 . 1 . . . . . . . . 5989 1 280 . 1 1 39 39 ILE HG22 H 1 0.571 0.005 . 1 . . . . . . . . 5989 1 281 . 1 1 39 39 ILE HG23 H 1 0.571 0.005 . 1 . . . . . . . . 5989 1 282 . 1 1 39 39 ILE HG12 H 1 1.200 0.000 . 1 . . . . . . . . 5989 1 283 . 1 1 39 39 ILE HG13 H 1 1.430 0.000 . 1 . . . . . . . . 5989 1 284 . 1 1 39 39 ILE HD11 H 1 0.412 0.005 . 1 . . . . . . . . 5989 1 285 . 1 1 39 39 ILE HD12 H 1 0.412 0.005 . 1 . . . . . . . . 5989 1 286 . 1 1 39 39 ILE HD13 H 1 0.412 0.005 . 1 . . . . . . . . 5989 1 287 . 1 1 40 40 ASP H H 1 8.725 0.000 . 1 . . . . . . . . 5989 1 288 . 1 1 40 40 ASP HA H 1 4.880 0.004 . 1 . . . . . . . . 5989 1 289 . 1 1 40 40 ASP HB2 H 1 2.796 0.005 . 2 . . . . . . . . 5989 1 290 . 1 1 41 41 VAL H H 1 7.744 0.003 . 1 . . . . . . . . 5989 1 291 . 1 1 41 41 VAL HA H 1 4.018 0.003 . 1 . . . . . . . . 5989 1 292 . 1 1 41 41 VAL HB H 1 1.730 0.002 . 1 . . . . . . . . 5989 1 293 . 1 1 41 41 VAL HG11 H 1 0.754 0.001 . 1 . . . . . . . . 5989 1 294 . 1 1 41 41 VAL HG12 H 1 0.754 0.001 . 1 . . . . . . . . 5989 1 295 . 1 1 41 41 VAL HG13 H 1 0.754 0.001 . 1 . . . . . . . . 5989 1 296 . 1 1 41 41 VAL HG21 H 1 0.763 0.002 . 1 . . . . . . . . 5989 1 297 . 1 1 41 41 VAL HG22 H 1 0.763 0.002 . 1 . . . . . . . . 5989 1 298 . 1 1 41 41 VAL HG23 H 1 0.763 0.002 . 1 . . . . . . . . 5989 1 299 . 1 1 42 42 CYS H H 1 8.877 0.003 . 1 . . . . . . . . 5989 1 300 . 1 1 42 42 CYS HA H 1 4.461 0.002 . 1 . . . . . . . . 5989 1 301 . 1 1 42 42 CYS HB2 H 1 2.756 0.003 . 1 . . . . . . . . 5989 1 302 . 1 1 42 42 CYS HB3 H 1 3.108 0.008 . 1 . . . . . . . . 5989 1 303 . 1 1 43 43 PRO HA H 1 4.081 0.000 . 1 . . . . . . . . 5989 1 304 . 1 1 43 43 PRO HB2 H 1 1.872 0.000 . 1 . . . . . . . . 5989 1 305 . 1 1 43 43 PRO HB3 H 1 0.741 0.006 . 1 . . . . . . . . 5989 1 306 . 1 1 43 43 PRO HG2 H 1 0.547 0.005 . 1 . . . . . . . . 5989 1 307 . 1 1 43 43 PRO HG3 H 1 1.233 0.000 . 1 . . . . . . . . 5989 1 308 . 1 1 43 43 PRO HD2 H 1 2.333 0.006 . 1 . . . . . . . . 5989 1 309 . 1 1 43 43 PRO HD3 H 1 3.885 0.005 . 1 . . . . . . . . 5989 1 310 . 1 1 44 44 LYS H H 1 7.921 0.000 . 1 . . . . . . . . 5989 1 311 . 1 1 44 44 LYS HA H 1 4.212 0.001 . 1 . . . . . . . . 5989 1 312 . 1 1 44 44 LYS HB2 H 1 1.711 0.002 . 1 . . . . . . . . 5989 1 313 . 1 1 44 44 LYS HB3 H 1 1.861 0.002 . 1 . . . . . . . . 5989 1 314 . 1 1 44 44 LYS HG2 H 1 1.557 0.000 . 2 . . . . . . . . 5989 1 315 . 1 1 44 44 LYS HE2 H 1 3.058 0.010 . 2 . . . . . . . . 5989 1 316 . 1 1 44 44 LYS HZ1 H 1 7.510 0.000 . 1 . . . . . . . . 5989 1 317 . 1 1 44 44 LYS HZ2 H 1 7.510 0.000 . 1 . . . . . . . . 5989 1 318 . 1 1 44 44 LYS HZ3 H 1 7.510 0.000 . 1 . . . . . . . . 5989 1 319 . 1 1 45 45 ASN H H 1 8.429 0.001 . 1 . . . . . . . . 5989 1 320 . 1 1 45 45 ASN HA H 1 4.957 0.007 . 1 . . . . . . . . 5989 1 321 . 1 1 45 45 ASN HB2 H 1 2.873 0.007 . 1 . . . . . . . . 5989 1 322 . 1 1 45 45 ASN HB3 H 1 3.258 0.000 . 1 . . . . . . . . 5989 1 323 . 1 1 45 45 ASN HD21 H 1 7.692 0.002 . 1 . . . . . . . . 5989 1 324 . 1 1 45 45 ASN HD22 H 1 7.371 0.001 . 1 . . . . . . . . 5989 1 325 . 1 1 46 46 SER H H 1 9.004 0.000 . 1 . . . . . . . . 5989 1 326 . 1 1 46 46 SER HA H 1 5.026 0.001 . 1 . . . . . . . . 5989 1 327 . 1 1 46 46 SER HB2 H 1 4.457 0.003 . 1 . . . . . . . . 5989 1 328 . 1 1 46 46 SER HB3 H 1 3.982 0.004 . 1 . . . . . . . . 5989 1 329 . 1 1 47 47 LEU H H 1 8.368 0.001 . 1 . . . . . . . . 5989 1 330 . 1 1 47 47 LEU HA H 1 4.296 0.003 . 1 . . . . . . . . 5989 1 331 . 1 1 47 47 LEU HB2 H 1 1.940 0.003 . 1 . . . . . . . . 5989 1 332 . 1 1 47 47 LEU HB3 H 1 1.633 0.000 . 1 . . . . . . . . 5989 1 333 . 1 1 47 47 LEU HD11 H 1 0.935 0.000 . 1 . . . . . . . . 5989 1 334 . 1 1 47 47 LEU HD12 H 1 0.935 0.000 . 1 . . . . . . . . 5989 1 335 . 1 1 47 47 LEU HD13 H 1 0.935 0.000 . 1 . . . . . . . . 5989 1 336 . 1 1 47 47 LEU HD21 H 1 0.964 0.000 . 1 . . . . . . . . 5989 1 337 . 1 1 47 47 LEU HD22 H 1 0.964 0.000 . 1 . . . . . . . . 5989 1 338 . 1 1 47 47 LEU HD23 H 1 0.964 0.000 . 1 . . . . . . . . 5989 1 339 . 1 1 47 47 LEU HG H 1 1.760 0.001 . 1 . . . . . . . . 5989 1 340 . 1 1 48 48 LEU H H 1 8.242 0.000 . 1 . . . . . . . . 5989 1 341 . 1 1 48 48 LEU HA H 1 4.499 0.001 . 1 . . . . . . . . 5989 1 342 . 1 1 48 48 LEU HB2 H 1 1.748 0.000 . 1 . . . . . . . . 5989 1 343 . 1 1 48 48 LEU HB3 H 1 1.667 0.002 . 1 . . . . . . . . 5989 1 344 . 1 1 48 48 LEU HD11 H 1 0.892 0.000 . 1 . . . . . . . . 5989 1 345 . 1 1 48 48 LEU HD12 H 1 0.892 0.000 . 1 . . . . . . . . 5989 1 346 . 1 1 48 48 LEU HD13 H 1 0.892 0.000 . 1 . . . . . . . . 5989 1 347 . 1 1 48 48 LEU HD21 H 1 0.960 0.000 . 1 . . . . . . . . 5989 1 348 . 1 1 48 48 LEU HD22 H 1 0.960 0.000 . 1 . . . . . . . . 5989 1 349 . 1 1 48 48 LEU HD23 H 1 0.960 0.000 . 1 . . . . . . . . 5989 1 350 . 1 1 49 49 VAL H H 1 7.549 0.001 . 1 . . . . . . . . 5989 1 351 . 1 1 49 49 VAL HA H 1 5.081 0.000 . 1 . . . . . . . . 5989 1 352 . 1 1 49 49 VAL HB H 1 1.878 0.003 . 1 . . . . . . . . 5989 1 353 . 1 1 49 49 VAL HG11 H 1 0.832 0.003 . 1 . . . . . . . . 5989 1 354 . 1 1 49 49 VAL HG12 H 1 0.832 0.003 . 1 . . . . . . . . 5989 1 355 . 1 1 49 49 VAL HG13 H 1 0.832 0.003 . 1 . . . . . . . . 5989 1 356 . 1 1 49 49 VAL HG21 H 1 0.903 0.003 . 1 . . . . . . . . 5989 1 357 . 1 1 49 49 VAL HG22 H 1 0.903 0.003 . 1 . . . . . . . . 5989 1 358 . 1 1 49 49 VAL HG23 H 1 0.903 0.003 . 1 . . . . . . . . 5989 1 359 . 1 1 50 50 LYS H H 1 8.788 0.002 . 1 . . . . . . . . 5989 1 360 . 1 1 50 50 LYS HA H 1 4.810 0.000 . 1 . . . . . . . . 5989 1 361 . 1 1 50 50 LYS HB2 H 1 1.799 0.006 . 1 . . . . . . . . 5989 1 362 . 1 1 50 50 LYS HB3 H 1 1.638 0.004 . 1 . . . . . . . . 5989 1 363 . 1 1 50 50 LYS HG2 H 1 1.223 0.000 . 2 . . . . . . . . 5989 1 364 . 1 1 50 50 LYS HD2 H 1 1.497 0.000 . 2 . . . . . . . . 5989 1 365 . 1 1 50 50 LYS HE2 H 1 2.877 0.002 . 2 . . . . . . . . 5989 1 366 . 1 1 50 50 LYS HZ1 H 1 7.630 0.000 . 1 . . . . . . . . 5989 1 367 . 1 1 50 50 LYS HZ2 H 1 7.630 0.000 . 1 . . . . . . . . 5989 1 368 . 1 1 50 50 LYS HZ3 H 1 7.630 0.000 . 1 . . . . . . . . 5989 1 369 . 1 1 51 51 TYR H H 1 9.289 0.006 . 1 . . . . . . . . 5989 1 370 . 1 1 51 51 TYR HA H 1 5.332 0.004 . 1 . . . . . . . . 5989 1 371 . 1 1 51 51 TYR HB2 H 1 2.982 0.004 . 1 . . . . . . . . 5989 1 372 . 1 1 51 51 TYR HB3 H 1 2.755 0.006 . 1 . . . . . . . . 5989 1 373 . 1 1 51 51 TYR HD1 H 1 6.840 0.002 . 2 . . . . . . . . 5989 1 374 . 1 1 51 51 TYR HE1 H 1 6.468 0.000 . 2 . . . . . . . . 5989 1 375 . 1 1 52 52 VAL H H 1 8.981 0.005 . 1 . . . . . . . . 5989 1 376 . 1 1 52 52 VAL HA H 1 4.575 0.005 . 1 . . . . . . . . 5989 1 377 . 1 1 52 52 VAL HB H 1 2.091 0.007 . 1 . . . . . . . . 5989 1 378 . 1 1 52 52 VAL HG11 H 1 1.078 0.004 . 1 . . . . . . . . 5989 1 379 . 1 1 52 52 VAL HG12 H 1 1.078 0.004 . 1 . . . . . . . . 5989 1 380 . 1 1 52 52 VAL HG13 H 1 1.078 0.004 . 1 . . . . . . . . 5989 1 381 . 1 1 52 52 VAL HG21 H 1 1.163 0.002 . 1 . . . . . . . . 5989 1 382 . 1 1 52 52 VAL HG22 H 1 1.163 0.002 . 1 . . . . . . . . 5989 1 383 . 1 1 52 52 VAL HG23 H 1 1.163 0.002 . 1 . . . . . . . . 5989 1 384 . 1 1 53 53 CYS H H 1 9.535 0.005 . 1 . . . . . . . . 5989 1 385 . 1 1 53 53 CYS HA H 1 5.893 0.004 . 1 . . . . . . . . 5989 1 386 . 1 1 53 53 CYS HB2 H 1 3.099 0.003 . 1 . . . . . . . . 5989 1 387 . 1 1 53 53 CYS HB3 H 1 3.804 0.003 . 1 . . . . . . . . 5989 1 388 . 1 1 54 54 CYS H H 1 9.190 0.002 . 1 . . . . . . . . 5989 1 389 . 1 1 54 54 CYS HA H 1 5.114 0.002 . 1 . . . . . . . . 5989 1 390 . 1 1 54 54 CYS HB2 H 1 3.440 0.004 . 1 . . . . . . . . 5989 1 391 . 1 1 54 54 CYS HB3 H 1 3.649 0.003 . 1 . . . . . . . . 5989 1 392 . 1 1 55 55 ASN H H 1 8.579 0.001 . 1 . . . . . . . . 5989 1 393 . 1 1 55 55 ASN HA H 1 5.154 0.007 . 1 . . . . . . . . 5989 1 394 . 1 1 55 55 ASN HB2 H 1 2.655 0.003 . 1 . . . . . . . . 5989 1 395 . 1 1 55 55 ASN HB3 H 1 3.384 0.002 . 1 . . . . . . . . 5989 1 396 . 1 1 55 55 ASN HD21 H 1 6.728 0.002 . 1 . . . . . . . . 5989 1 397 . 1 1 55 55 ASN HD22 H 1 7.536 0.005 . 1 . . . . . . . . 5989 1 398 . 1 1 56 56 THR H H 1 7.590 0.006 . 1 . . . . . . . . 5989 1 399 . 1 1 56 56 THR HA H 1 4.717 0.000 . 1 . . . . . . . . 5989 1 400 . 1 1 56 56 THR HB H 1 4.297 0.000 . 1 . . . . . . . . 5989 1 401 . 1 1 56 56 THR HG21 H 1 1.206 0.000 . 1 . . . . . . . . 5989 1 402 . 1 1 56 56 THR HG22 H 1 1.206 0.000 . 1 . . . . . . . . 5989 1 403 . 1 1 56 56 THR HG23 H 1 1.206 0.000 . 1 . . . . . . . . 5989 1 404 . 1 1 57 57 ASP H H 1 8.232 0.000 . 1 . . . . . . . . 5989 1 405 . 1 1 57 57 ASP HA H 1 4.817 0.004 . 1 . . . . . . . . 5989 1 406 . 1 1 57 57 ASP HB2 H 1 2.493 0.005 . 1 . . . . . . . . 5989 1 407 . 1 1 57 57 ASP HB3 H 1 2.272 0.005 . 1 . . . . . . . . 5989 1 408 . 1 1 58 58 ARG H H 1 9.657 0.003 . 1 . . . . . . . . 5989 1 409 . 1 1 58 58 ARG HA H 1 3.397 0.006 . 1 . . . . . . . . 5989 1 410 . 1 1 58 58 ARG HB2 H 1 1.798 0.001 . 1 . . . . . . . . 5989 1 411 . 1 1 58 58 ARG HB3 H 1 2.185 0.002 . 1 . . . . . . . . 5989 1 412 . 1 1 58 58 ARG HG2 H 1 1.321 0.000 . 1 . . . . . . . . 5989 1 413 . 1 1 58 58 ARG HG3 H 1 1.370 0.000 . 1 . . . . . . . . 5989 1 414 . 1 1 58 58 ARG HE H 1 7.850 0.000 . 1 . . . . . . . . 5989 1 415 . 1 1 59 59 CYS H H 1 7.598 0.004 . 1 . . . . . . . . 5989 1 416 . 1 1 59 59 CYS HA H 1 4.464 0.003 . 1 . . . . . . . . 5989 1 417 . 1 1 59 59 CYS HB2 H 1 3.363 0.000 . 1 . . . . . . . . 5989 1 418 . 1 1 59 59 CYS HB3 H 1 3.651 0.002 . 1 . . . . . . . . 5989 1 419 . 1 1 60 60 ASN H H 1 9.024 0.000 . 1 . . . . . . . . 5989 1 420 . 1 1 60 60 ASN HA H 1 4.369 0.004 . 1 . . . . . . . . 5989 1 421 . 1 1 60 60 ASN HB2 H 1 2.722 0.003 . 1 . . . . . . . . 5989 1 422 . 1 1 60 60 ASN HB3 H 1 2.327 0.007 . 1 . . . . . . . . 5989 1 423 . 1 1 60 60 ASN HD21 H 1 7.398 0.006 . 1 . . . . . . . . 5989 1 424 . 1 1 60 60 ASN HD22 H 1 7.518 0.000 . 1 . . . . . . . . 5989 1 stop_ save_ save_CTI_1H_Shifts_minor _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode CTI_1H_Shifts_minor _Assigned_chem_shift_list.Entry_ID 5989 _Assigned_chem_shift_list.ID 2 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $condition_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _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_1 . 5989 2 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 . 2 1 1 1 LEU HA H 1 4.184 0.005 . 1 . . . . . . . . 5989 2 2 . 2 1 1 1 LEU HB2 H 1 1.568 0.002 . 2 . . . . . . . . 5989 2 3 . 2 1 1 1 LEU HD11 H 1 0.772 0.004 . 1 . . . . . . . . 5989 2 4 . 2 1 1 1 LEU HD12 H 1 0.772 0.004 . 1 . . . . . . . . 5989 2 5 . 2 1 1 1 LEU HD13 H 1 0.772 0.004 . 1 . . . . . . . . 5989 2 6 . 2 1 1 1 LEU HD21 H 1 0.853 0.005 . 1 . . . . . . . . 5989 2 7 . 2 1 1 1 LEU HD22 H 1 0.853 0.005 . 1 . . . . . . . . 5989 2 8 . 2 1 1 1 LEU HD23 H 1 0.853 0.005 . 1 . . . . . . . . 5989 2 9 . 2 1 1 1 LEU HG H 1 1.508 0.005 . 1 . . . . . . . . 5989 2 10 . 2 1 2 2 LYS H H 1 8.619 0.000 . 1 . . . . . . . . 5989 2 11 . 2 1 2 2 LYS HA H 1 5.391 0.000 . 1 . . . . . . . . 5989 2 12 . 2 1 2 2 LYS HB2 H 1 1.420 0.000 . 2 . . . . . . . . 5989 2 13 . 2 1 2 2 LYS HG2 H 1 1.120 0.000 . 2 . . . . . . . . 5989 2 14 . 2 1 2 2 LYS HD2 H 1 1.204 0.000 . 2 . . . . . . . . 5989 2 15 . 2 1 2 2 LYS HE2 H 1 2.820 0.000 . 2 . . . . . . . . 5989 2 16 . 2 1 3 3 CYS H H 1 8.659 0.001 . 1 . . . . . . . . 5989 2 17 . 2 1 3 3 CYS HA H 1 5.130 0.000 . 1 . . . . . . . . 5989 2 18 . 2 1 3 3 CYS HB2 H 1 2.562 0.002 . 1 . . . . . . . . 5989 2 19 . 2 1 3 3 CYS HB3 H 1 2.938 0.000 . 1 . . . . . . . . 5989 2 20 . 2 1 4 4 ASN H H 1 9.647 0.000 . 1 . . . . . . . . 5989 2 21 . 2 1 4 4 ASN HA H 1 5.042 0.002 . 1 . . . . . . . . 5989 2 22 . 2 1 4 4 ASN HB2 H 1 2.246 0.000 . 1 . . . . . . . . 5989 2 23 . 2 1 4 4 ASN HB3 H 1 2.572 0.000 . 1 . . . . . . . . 5989 2 24 . 2 1 4 4 ASN HD21 H 1 7.452 0.000 . 1 . . . . . . . . 5989 2 25 . 2 1 4 4 ASN HD22 H 1 6.672 0.000 . 1 . . . . . . . . 5989 2 26 . 2 1 5 5 LYS H H 1 7.961 0.001 . 1 . . . . . . . . 5989 2 27 . 2 1 5 5 LYS HA H 1 4.568 0.000 . 1 . . . . . . . . 5989 2 28 . 2 1 5 5 LYS HB2 H 1 1.457 0.000 . 1 . . . . . . . . 5989 2 29 . 2 1 5 5 LYS HB3 H 1 1.900 0.000 . 1 . . . . . . . . 5989 2 30 . 2 1 5 5 LYS HG2 H 1 1.378 0.000 . 2 . . . . . . . . 5989 2 31 . 2 1 5 5 LYS HD2 H 1 1.379 0.000 . 2 . . . . . . . . 5989 2 32 . 2 1 5 5 LYS HE2 H 1 2.888 0.000 . 2 . . . . . . . . 5989 2 33 . 2 1 6 6 LEU H H 1 8.218 0.000 . 1 . . . . . . . . 5989 2 34 . 2 1 6 6 LEU HA H 1 4.381 0.000 . 1 . . . . . . . . 5989 2 35 . 2 1 6 6 LEU HB2 H 1 1.652 0.000 . 1 . . . . . . . . 5989 2 36 . 2 1 6 6 LEU HB3 H 1 1.792 0.000 . 1 . . . . . . . . 5989 2 37 . 2 1 6 6 LEU HD11 H 1 0.701 0.000 . 1 . . . . . . . . 5989 2 38 . 2 1 6 6 LEU HD12 H 1 0.701 0.000 . 1 . . . . . . . . 5989 2 39 . 2 1 6 6 LEU HD13 H 1 0.701 0.000 . 1 . . . . . . . . 5989 2 40 . 2 1 6 6 LEU HD21 H 1 0.876 0.000 . 1 . . . . . . . . 5989 2 41 . 2 1 6 6 LEU HD22 H 1 0.876 0.000 . 1 . . . . . . . . 5989 2 42 . 2 1 6 6 LEU HD23 H 1 0.876 0.000 . 1 . . . . . . . . 5989 2 43 . 2 1 6 6 LEU HG H 1 1.547 0.000 . 1 . . . . . . . . 5989 2 44 . 2 1 7 7 VAL H H 1 8.025 0.000 . 1 . . . . . . . . 5989 2 45 . 2 1 7 7 VAL HA H 1 4.109 0.000 . 1 . . . . . . . . 5989 2 46 . 2 1 7 7 VAL HB H 1 2.048 0.000 . 1 . . . . . . . . 5989 2 47 . 2 1 7 7 VAL HG11 H 1 0.956 0.000 . 1 . . . . . . . . 5989 2 48 . 2 1 7 7 VAL HG12 H 1 0.956 0.000 . 1 . . . . . . . . 5989 2 49 . 2 1 7 7 VAL HG13 H 1 0.956 0.000 . 1 . . . . . . . . 5989 2 50 . 2 1 7 7 VAL HG21 H 1 1.003 0.000 . 1 . . . . . . . . 5989 2 51 . 2 1 7 7 VAL HG22 H 1 1.003 0.000 . 1 . . . . . . . . 5989 2 52 . 2 1 7 7 VAL HG23 H 1 1.003 0.000 . 1 . . . . . . . . 5989 2 53 . 2 1 8 8 PRO HA H 1 4.715 0.000 . 1 . . . . . . . . 5989 2 54 . 2 1 8 8 PRO HB2 H 1 2.159 0.001 . 1 . . . . . . . . 5989 2 55 . 2 1 8 8 PRO HB3 H 1 2.360 0.001 . 1 . . . . . . . . 5989 2 56 . 2 1 8 8 PRO HG2 H 1 1.684 0.001 . 1 . . . . . . . . 5989 2 57 . 2 1 8 8 PRO HG3 H 1 2.018 0.001 . 1 . . . . . . . . 5989 2 58 . 2 1 8 8 PRO HD2 H 1 3.455 0.000 . 1 . . . . . . . . 5989 2 59 . 2 1 8 8 PRO HD3 H 1 3.600 0.000 . 1 . . . . . . . . 5989 2 60 . 2 1 9 9 ILE H H 1 8.360 0.000 . 1 . . . . . . . . 5989 2 61 . 2 1 9 9 ILE HA H 1 4.045 0.000 . 1 . . . . . . . . 5989 2 62 . 2 1 9 9 ILE HB H 1 2.105 0.000 . 1 . . . . . . . . 5989 2 63 . 2 1 9 9 ILE HG21 H 1 0.910 0.000 . 1 . . . . . . . . 5989 2 64 . 2 1 9 9 ILE HG22 H 1 0.910 0.000 . 1 . . . . . . . . 5989 2 65 . 2 1 9 9 ILE HG23 H 1 0.910 0.000 . 1 . . . . . . . . 5989 2 66 . 2 1 9 9 ILE HG12 H 1 0.858 0.000 . 2 . . . . . . . . 5989 2 67 . 2 1 9 9 ILE HD11 H 1 1.331 0.000 . 1 . . . . . . . . 5989 2 68 . 2 1 9 9 ILE HD12 H 1 1.331 0.000 . 1 . . . . . . . . 5989 2 69 . 2 1 9 9 ILE HD13 H 1 1.331 0.000 . 1 . . . . . . . . 5989 2 70 . 2 1 10 10 ALA H H 1 8.174 0.000 . 1 . . . . . . . . 5989 2 71 . 2 1 10 10 ALA HA H 1 4.277 0.000 . 1 . . . . . . . . 5989 2 72 . 2 1 10 10 ALA HB1 H 1 1.389 0.000 . 1 . . . . . . . . 5989 2 73 . 2 1 10 10 ALA HB2 H 1 1.389 0.000 . 1 . . . . . . . . 5989 2 74 . 2 1 10 10 ALA HB3 H 1 1.389 0.000 . 1 . . . . . . . . 5989 2 75 . 2 1 11 11 TYR H H 1 7.413 0.000 . 1 . . . . . . . . 5989 2 76 . 2 1 11 11 TYR HA H 1 5.058 0.000 . 1 . . . . . . . . 5989 2 77 . 2 1 11 11 TYR HB2 H 1 2.618 0.002 . 1 . . . . . . . . 5989 2 78 . 2 1 11 11 TYR HB3 H 1 3.184 0.000 . 1 . . . . . . . . 5989 2 79 . 2 1 11 11 TYR HD1 H 1 6.772 0.000 . 2 . . . . . . . . 5989 2 80 . 2 1 11 11 TYR HE1 H 1 6.772 0.000 . 2 . . . . . . . . 5989 2 81 . 2 1 12 12 LYS H H 1 8.714 0.000 . 1 . . . . . . . . 5989 2 82 . 2 1 12 12 LYS HA H 1 4.707 0.000 . 1 . . . . . . . . 5989 2 83 . 2 1 12 12 LYS HB2 H 1 1.670 0.000 . 1 . . . . . . . . 5989 2 84 . 2 1 12 12 LYS HB3 H 1 1.463 0.000 . 1 . . . . . . . . 5989 2 85 . 2 1 12 12 LYS HG2 H 1 1.280 0.000 . 1 . . . . . . . . 5989 2 86 . 2 1 12 12 LYS HG3 H 1 1.410 0.000 . 1 . . . . . . . . 5989 2 87 . 2 1 12 12 LYS HD2 H 1 1.730 0.000 . 2 . . . . . . . . 5989 2 88 . 2 1 12 12 LYS HE2 H 1 3.010 0.000 . 2 . . . . . . . . 5989 2 89 . 2 1 13 13 THR H H 1 8.685 0.000 . 1 . . . . . . . . 5989 2 90 . 2 1 13 13 THR HA H 1 4.605 0.000 . 1 . . . . . . . . 5989 2 91 . 2 1 13 13 THR HB H 1 4.068 0.000 . 1 . . . . . . . . 5989 2 92 . 2 1 13 13 THR HG21 H 1 1.281 0.000 . 1 . . . . . . . . 5989 2 93 . 2 1 13 13 THR HG22 H 1 1.281 0.000 . 1 . . . . . . . . 5989 2 94 . 2 1 13 13 THR HG23 H 1 1.281 0.000 . 1 . . . . . . . . 5989 2 95 . 2 1 14 14 CYS H H 1 9.234 0.001 . 1 . . . . . . . . 5989 2 96 . 2 1 14 14 CYS HA H 1 4.989 0.002 . 1 . . . . . . . . 5989 2 97 . 2 1 14 14 CYS HB2 H 1 2.837 0.000 . 1 . . . . . . . . 5989 2 98 . 2 1 14 14 CYS HB3 H 1 3.497 0.000 . 1 . . . . . . . . 5989 2 99 . 2 1 15 15 PRO HA H 1 4.611 0.000 . 1 . . . . . . . . 5989 2 100 . 2 1 15 15 PRO HB2 H 1 2.415 0.000 . 1 . . . . . . . . 5989 2 101 . 2 1 15 15 PRO HB3 H 1 1.971 0.000 . 1 . . . . . . . . 5989 2 102 . 2 1 15 15 PRO HG2 H 1 1.918 0.000 . 1 . . . . . . . . 5989 2 103 . 2 1 15 15 PRO HG3 H 1 2.183 0.000 . 1 . . . . . . . . 5989 2 104 . 2 1 15 15 PRO HD2 H 1 3.457 0.000 . 1 . . . . . . . . 5989 2 105 . 2 1 15 15 PRO HD3 H 1 3.989 0.000 . 1 . . . . . . . . 5989 2 106 . 2 1 16 16 GLU H H 1 8.551 0.000 . 1 . . . . . . . . 5989 2 107 . 2 1 16 16 GLU HA H 1 4.023 0.000 . 1 . . . . . . . . 5989 2 108 . 2 1 16 16 GLU HB2 H 1 1.950 0.000 . 1 . . . . . . . . 5989 2 109 . 2 1 16 16 GLU HB3 H 1 2.026 0.000 . 1 . . . . . . . . 5989 2 110 . 2 1 16 16 GLU HG2 H 1 2.296 0.000 . 2 . . . . . . . . 5989 2 111 . 2 1 17 17 GLY H H 1 8.929 0.000 . 1 . . . . . . . . 5989 2 112 . 2 1 17 17 GLY HA2 H 1 3.695 0.000 . 1 . . . . . . . . 5989 2 113 . 2 1 17 17 GLY HA3 H 1 4.306 0.000 . 1 . . . . . . . . 5989 2 114 . 2 1 18 18 LYS H H 1 7.634 0.000 . 1 . . . . . . . . 5989 2 115 . 2 1 18 18 LYS HA H 1 4.300 0.007 . 1 . . . . . . . . 5989 2 116 . 2 1 18 18 LYS HB2 H 1 1.936 0.000 . 2 . . . . . . . . 5989 2 117 . 2 1 18 18 LYS HG2 H 1 1.101 0.000 . 2 . . . . . . . . 5989 2 118 . 2 1 18 18 LYS HD2 H 1 1.358 0.000 . 1 . . . . . . . . 5989 2 119 . 2 1 18 18 LYS HD3 H 1 1.415 0.000 . 1 . . . . . . . . 5989 2 120 . 2 1 18 18 LYS HE2 H 1 2.960 0.000 . 2 . . . . . . . . 5989 2 121 . 2 1 18 18 LYS HZ1 H 1 7.700 0.000 . 1 . . . . . . . . 5989 2 122 . 2 1 18 18 LYS HZ2 H 1 7.700 0.000 . 1 . . . . . . . . 5989 2 123 . 2 1 18 18 LYS HZ3 H 1 7.700 0.000 . 1 . . . . . . . . 5989 2 124 . 2 1 19 19 ASN H H 1 7.960 0.000 . 1 . . . . . . . . 5989 2 125 . 2 1 19 19 ASN HA H 1 4.936 0.000 . 1 . . . . . . . . 5989 2 126 . 2 1 19 19 ASN HB2 H 1 3.010 0.000 . 1 . . . . . . . . 5989 2 127 . 2 1 19 19 ASN HB3 H 1 2.660 0.000 . 1 . . . . . . . . 5989 2 128 . 2 1 19 19 ASN HD21 H 1 7.488 0.000 . 1 . . . . . . . . 5989 2 129 . 2 1 19 19 ASN HD22 H 1 7.024 0.000 . 1 . . . . . . . . 5989 2 130 . 2 1 20 20 LEU H H 1 8.253 0.000 . 1 . . . . . . . . 5989 2 131 . 2 1 20 20 LEU HA H 1 4.844 0.000 . 1 . . . . . . . . 5989 2 132 . 2 1 20 20 LEU HB2 H 1 1.674 0.000 . 1 . . . . . . . . 5989 2 133 . 2 1 20 20 LEU HB3 H 1 1.392 0.000 . 1 . . . . . . . . 5989 2 134 . 2 1 20 20 LEU HD11 H 1 0.754 0.000 . 1 . . . . . . . . 5989 2 135 . 2 1 20 20 LEU HD12 H 1 0.754 0.000 . 1 . . . . . . . . 5989 2 136 . 2 1 20 20 LEU HD13 H 1 0.754 0.000 . 1 . . . . . . . . 5989 2 137 . 2 1 20 20 LEU HD21 H 1 0.892 0.000 . 1 . . . . . . . . 5989 2 138 . 2 1 20 20 LEU HD22 H 1 0.892 0.000 . 1 . . . . . . . . 5989 2 139 . 2 1 20 20 LEU HD23 H 1 0.892 0.000 . 1 . . . . . . . . 5989 2 140 . 2 1 20 20 LEU HG H 1 1.515 0.000 . 1 . . . . . . . . 5989 2 141 . 2 1 21 21 CYS H H 1 8.982 0.000 . 1 . . . . . . . . 5989 2 142 . 2 1 21 21 CYS HA H 1 6.117 0.000 . 1 . . . . . . . . 5989 2 143 . 2 1 21 21 CYS HB2 H 1 2.974 0.000 . 1 . . . . . . . . 5989 2 144 . 2 1 21 21 CYS HB3 H 1 3.139 0.000 . 1 . . . . . . . . 5989 2 145 . 2 1 22 22 TYR H H 1 9.136 0.000 . 1 . . . . . . . . 5989 2 146 . 2 1 22 22 TYR HA H 1 6.105 0.000 . 1 . . . . . . . . 5989 2 147 . 2 1 22 22 TYR HB2 H 1 3.129 0.000 . 1 . . . . . . . . 5989 2 148 . 2 1 22 22 TYR HB3 H 1 3.018 0.000 . 1 . . . . . . . . 5989 2 149 . 2 1 22 22 TYR HD1 H 1 6.679 0.000 . 2 . . . . . . . . 5989 2 150 . 2 1 22 22 TYR HE1 H 1 6.621 0.000 . 2 . . . . . . . . 5989 2 151 . 2 1 23 23 LYS H H 1 9.088 0.000 . 1 . . . . . . . . 5989 2 152 . 2 1 23 23 LYS HA H 1 4.869 0.000 . 1 . . . . . . . . 5989 2 153 . 2 1 23 23 LYS HB2 H 1 1.508 0.000 . 1 . . . . . . . . 5989 2 154 . 2 1 23 23 LYS HB3 H 1 1.656 0.000 . 1 . . . . . . . . 5989 2 155 . 2 1 23 23 LYS HG2 H 1 1.435 0.000 . 2 . . . . . . . . 5989 2 156 . 2 1 23 23 LYS HD2 H 1 1.756 0.000 . 2 . . . . . . . . 5989 2 157 . 2 1 23 23 LYS HE2 H 1 3.070 0.000 . 2 . . . . . . . . 5989 2 158 . 2 1 23 23 LYS HZ1 H 1 7.860 0.000 . 1 . . . . . . . . 5989 2 159 . 2 1 23 23 LYS HZ2 H 1 7.860 0.000 . 1 . . . . . . . . 5989 2 160 . 2 1 23 23 LYS HZ3 H 1 7.860 0.000 . 1 . . . . . . . . 5989 2 161 . 2 1 24 24 MET H H 1 8.320 0.000 . 1 . . . . . . . . 5989 2 162 . 2 1 24 24 MET HA H 1 5.165 0.000 . 1 . . . . . . . . 5989 2 163 . 2 1 24 24 MET HB2 H 1 1.788 0.001 . 1 . . . . . . . . 5989 2 164 . 2 1 24 24 MET HB3 H 1 1.696 0.001 . 1 . . . . . . . . 5989 2 165 . 2 1 24 24 MET HG2 H 1 1.324 0.001 . 1 . . . . . . . . 5989 2 166 . 2 1 24 24 MET HG3 H 1 1.558 0.000 . 1 . . . . . . . . 5989 2 167 . 2 1 24 24 MET HE1 H 1 2.080 0.000 . 1 . . . . . . . . 5989 2 168 . 2 1 24 24 MET HE2 H 1 2.080 0.000 . 1 . . . . . . . . 5989 2 169 . 2 1 24 24 MET HE3 H 1 2.080 0.000 . 1 . . . . . . . . 5989 2 170 . 2 1 25 25 PHE H H 1 9.545 0.001 . 1 . . . . . . . . 5989 2 171 . 2 1 25 25 PHE HA H 1 4.870 0.000 . 1 . . . . . . . . 5989 2 172 . 2 1 25 25 PHE HB2 H 1 2.506 0.000 . 1 . . . . . . . . 5989 2 173 . 2 1 25 25 PHE HB3 H 1 3.397 0.000 . 1 . . . . . . . . 5989 2 174 . 2 1 25 25 PHE HD1 H 1 7.082 0.000 . 2 . . . . . . . . 5989 2 175 . 2 1 25 25 PHE HE1 H 1 6.941 0.000 . 2 . . . . . . . . 5989 2 176 . 2 1 25 25 PHE HZ H 1 7.188 0.000 . 1 . . . . . . . . 5989 2 177 . 2 1 26 26 MET H H 1 9.255 0.000 . 1 . . . . . . . . 5989 2 178 . 2 1 26 26 MET HA H 1 5.110 0.000 . 1 . . . . . . . . 5989 2 179 . 2 1 26 26 MET HB2 H 1 2.036 0.000 . 1 . . . . . . . . 5989 2 180 . 2 1 26 26 MET HB3 H 1 2.349 0.000 . 1 . . . . . . . . 5989 2 181 . 2 1 26 26 MET HG2 H 1 2.635 0.000 . 1 . . . . . . . . 5989 2 182 . 2 1 26 26 MET HG3 H 1 2.868 0.000 . 1 . . . . . . . . 5989 2 183 . 2 1 26 26 MET HE1 H 1 1.860 0.000 . 1 . . . . . . . . 5989 2 184 . 2 1 26 26 MET HE2 H 1 1.860 0.000 . 1 . . . . . . . . 5989 2 185 . 2 1 26 26 MET HE3 H 1 1.860 0.000 . 1 . . . . . . . . 5989 2 186 . 2 1 27 27 MET H H 1 8.371 0.000 . 1 . . . . . . . . 5989 2 187 . 2 1 27 27 MET HA H 1 4.157 0.005 . 1 . . . . . . . . 5989 2 188 . 2 1 27 27 MET HB2 H 1 1.916 0.004 . 1 . . . . . . . . 5989 2 189 . 2 1 27 27 MET HB3 H 1 2.030 0.003 . 1 . . . . . . . . 5989 2 190 . 2 1 27 27 MET HG2 H 1 2.119 0.000 . 1 . . . . . . . . 5989 2 191 . 2 1 27 27 MET HG3 H 1 2.643 0.004 . 1 . . . . . . . . 5989 2 192 . 2 1 27 27 MET HE1 H 1 2.080 0.000 . 1 . . . . . . . . 5989 2 193 . 2 1 27 27 MET HE2 H 1 2.080 0.000 . 1 . . . . . . . . 5989 2 194 . 2 1 27 27 MET HE3 H 1 2.080 0.000 . 1 . . . . . . . . 5989 2 195 . 2 1 28 28 SER H H 1 7.664 0.000 . 1 . . . . . . . . 5989 2 196 . 2 1 28 28 SER HA H 1 4.206 0.003 . 1 . . . . . . . . 5989 2 197 . 2 1 28 28 SER HB2 H 1 3.810 0.007 . 1 . . . . . . . . 5989 2 198 . 2 1 28 28 SER HB3 H 1 4.067 0.005 . 1 . . . . . . . . 5989 2 199 . 2 1 29 29 ASP H H 1 7.961 0.000 . 1 . . . . . . . . 5989 2 200 . 2 1 29 29 ASP HA H 1 4.643 0.001 . 1 . . . . . . . . 5989 2 201 . 2 1 29 29 ASP HB2 H 1 2.651 0.000 . 1 . . . . . . . . 5989 2 202 . 2 1 29 29 ASP HB3 H 1 2.907 0.000 . 1 . . . . . . . . 5989 2 203 . 2 1 30 30 LEU H H 1 8.826 0.000 . 1 . . . . . . . . 5989 2 204 . 2 1 30 30 LEU HA H 1 4.050 0.001 . 1 . . . . . . . . 5989 2 205 . 2 1 30 30 LEU HB2 H 1 1.635 0.000 . 1 . . . . . . . . 5989 2 206 . 2 1 30 30 LEU HB3 H 1 1.493 0.000 . 1 . . . . . . . . 5989 2 207 . 2 1 30 30 LEU HD11 H 1 0.677 0.000 . 1 . . . . . . . . 5989 2 208 . 2 1 30 30 LEU HD12 H 1 0.677 0.000 . 1 . . . . . . . . 5989 2 209 . 2 1 30 30 LEU HD13 H 1 0.677 0.000 . 1 . . . . . . . . 5989 2 210 . 2 1 30 30 LEU HD21 H 1 0.830 0.000 . 1 . . . . . . . . 5989 2 211 . 2 1 30 30 LEU HD22 H 1 0.830 0.000 . 1 . . . . . . . . 5989 2 212 . 2 1 30 30 LEU HD23 H 1 0.830 0.000 . 1 . . . . . . . . 5989 2 213 . 2 1 30 30 LEU HG H 1 1.640 0.000 . 1 . . . . . . . . 5989 2 214 . 2 1 31 31 THR H H 1 8.677 0.000 . 1 . . . . . . . . 5989 2 215 . 2 1 31 31 THR HA H 1 4.416 0.000 . 1 . . . . . . . . 5989 2 216 . 2 1 31 31 THR HB H 1 4.329 0.000 . 1 . . . . . . . . 5989 2 217 . 2 1 31 31 THR HG21 H 1 1.179 0.000 . 1 . . . . . . . . 5989 2 218 . 2 1 31 31 THR HG22 H 1 1.179 0.000 . 1 . . . . . . . . 5989 2 219 . 2 1 31 31 THR HG23 H 1 1.179 0.000 . 1 . . . . . . . . 5989 2 220 . 2 1 32 32 ILE H H 1 7.116 0.000 . 1 . . . . . . . . 5989 2 221 . 2 1 32 32 ILE HA H 1 4.875 0.000 . 1 . . . . . . . . 5989 2 222 . 2 1 32 32 ILE HB H 1 1.887 0.000 . 1 . . . . . . . . 5989 2 223 . 2 1 32 32 ILE HG21 H 1 1.210 0.000 . 1 . . . . . . . . 5989 2 224 . 2 1 32 32 ILE HG22 H 1 1.210 0.000 . 1 . . . . . . . . 5989 2 225 . 2 1 32 32 ILE HG23 H 1 1.210 0.000 . 1 . . . . . . . . 5989 2 226 . 2 1 32 32 ILE HG12 H 1 0.903 0.000 . 2 . . . . . . . . 5989 2 227 . 2 1 32 32 ILE HD11 H 1 1.619 0.000 . 1 . . . . . . . . 5989 2 228 . 2 1 32 32 ILE HD12 H 1 1.619 0.000 . 1 . . . . . . . . 5989 2 229 . 2 1 32 32 ILE HD13 H 1 1.619 0.000 . 1 . . . . . . . . 5989 2 230 . 2 1 33 33 PRO HA H 1 4.054 0.010 . 1 . . . . . . . . 5989 2 231 . 2 1 33 33 PRO HB2 H 1 1.215 0.006 . 1 . . . . . . . . 5989 2 232 . 2 1 33 33 PRO HB3 H 1 1.498 0.005 . 1 . . . . . . . . 5989 2 233 . 2 1 33 33 PRO HG2 H 1 1.658 0.002 . 1 . . . . . . . . 5989 2 234 . 2 1 33 33 PRO HG3 H 1 1.910 0.000 . 1 . . . . . . . . 5989 2 235 . 2 1 33 33 PRO HD2 H 1 3.858 0.003 . 1 . . . . . . . . 5989 2 236 . 2 1 33 33 PRO HD3 H 1 3.948 0.003 . 1 . . . . . . . . 5989 2 237 . 2 1 34 34 VAL H H 1 8.726 0.000 . 1 . . . . . . . . 5989 2 238 . 2 1 34 34 VAL HA H 1 4.366 0.000 . 1 . . . . . . . . 5989 2 239 . 2 1 34 34 VAL HB H 1 2.240 0.000 . 1 . . . . . . . . 5989 2 240 . 2 1 34 34 VAL HG11 H 1 0.862 0.000 . 1 . . . . . . . . 5989 2 241 . 2 1 34 34 VAL HG12 H 1 0.862 0.000 . 1 . . . . . . . . 5989 2 242 . 2 1 34 34 VAL HG13 H 1 0.862 0.000 . 1 . . . . . . . . 5989 2 243 . 2 1 34 34 VAL HG21 H 1 1.027 0.000 . 1 . . . . . . . . 5989 2 244 . 2 1 34 34 VAL HG22 H 1 1.027 0.000 . 1 . . . . . . . . 5989 2 245 . 2 1 34 34 VAL HG23 H 1 1.027 0.000 . 1 . . . . . . . . 5989 2 246 . 2 1 35 35 LYS H H 1 7.378 0.000 . 1 . . . . . . . . 5989 2 247 . 2 1 35 35 LYS HA H 1 4.567 0.000 . 1 . . . . . . . . 5989 2 248 . 2 1 35 35 LYS HB2 H 1 1.714 0.000 . 1 . . . . . . . . 5989 2 249 . 2 1 35 35 LYS HB3 H 1 1.997 0.000 . 1 . . . . . . . . 5989 2 250 . 2 1 35 35 LYS HG2 H 1 1.531 0.000 . 1 . . . . . . . . 5989 2 251 . 2 1 35 35 LYS HG3 H 1 1.606 0.000 . 1 . . . . . . . . 5989 2 252 . 2 1 35 35 LYS HD2 H 1 1.811 0.000 . 1 . . . . . . . . 5989 2 253 . 2 1 35 35 LYS HD3 H 1 1.870 0.000 . 1 . . . . . . . . 5989 2 254 . 2 1 35 35 LYS HE2 H 1 3.052 0.000 . 2 . . . . . . . . 5989 2 255 . 2 1 35 35 LYS HZ1 H 1 7.530 0.000 . 1 . . . . . . . . 5989 2 256 . 2 1 35 35 LYS HZ2 H 1 7.530 0.000 . 1 . . . . . . . . 5989 2 257 . 2 1 35 35 LYS HZ3 H 1 7.530 0.000 . 1 . . . . . . . . 5989 2 258 . 2 1 36 36 ARG H H 1 8.297 0.000 . 1 . . . . . . . . 5989 2 259 . 2 1 36 36 ARG HA H 1 4.421 0.000 . 1 . . . . . . . . 5989 2 260 . 2 1 36 36 ARG HB2 H 1 1.308 0.000 . 1 . . . . . . . . 5989 2 261 . 2 1 36 36 ARG HB3 H 1 1.684 0.000 . 1 . . . . . . . . 5989 2 262 . 2 1 36 36 ARG HG2 H 1 1.554 0.000 . 1 . . . . . . . . 5989 2 263 . 2 1 36 36 ARG HG3 H 1 0.857 0.000 . 1 . . . . . . . . 5989 2 264 . 2 1 36 36 ARG HD2 H 1 2.741 0.000 . 2 . . . . . . . . 5989 2 265 . 2 1 36 36 ARG HE H 1 7.996 0.000 . 1 . . . . . . . . 5989 2 266 . 2 1 37 37 GLY H H 1 6.796 0.000 . 1 . . . . . . . . 5989 2 267 . 2 1 37 37 GLY HA2 H 1 3.941 0.000 . 1 . . . . . . . . 5989 2 268 . 2 1 37 37 GLY HA3 H 1 4.280 0.000 . 1 . . . . . . . . 5989 2 269 . 2 1 38 38 CYS H H 1 8.660 0.000 . 1 . . . . . . . . 5989 2 270 . 2 1 38 38 CYS HA H 1 5.968 0.000 . 1 . . . . . . . . 5989 2 271 . 2 1 38 38 CYS HB2 H 1 3.461 0.000 . 1 . . . . . . . . 5989 2 272 . 2 1 38 38 CYS HB3 H 1 2.949 0.000 . 1 . . . . . . . . 5989 2 273 . 2 1 39 39 ILE H H 1 9.802 0.000 . 1 . . . . . . . . 5989 2 274 . 2 1 39 39 ILE HA H 1 4.395 0.000 . 1 . . . . . . . . 5989 2 275 . 2 1 39 39 ILE HB H 1 1.733 0.000 . 1 . . . . . . . . 5989 2 276 . 2 1 39 39 ILE HG21 H 1 0.571 0.000 . 1 . . . . . . . . 5989 2 277 . 2 1 39 39 ILE HG22 H 1 0.571 0.000 . 1 . . . . . . . . 5989 2 278 . 2 1 39 39 ILE HG23 H 1 0.571 0.000 . 1 . . . . . . . . 5989 2 279 . 2 1 39 39 ILE HG12 H 1 1.200 0.000 . 1 . . . . . . . . 5989 2 280 . 2 1 39 39 ILE HG13 H 1 1.430 0.000 . 1 . . . . . . . . 5989 2 281 . 2 1 39 39 ILE HD11 H 1 0.412 0.000 . 1 . . . . . . . . 5989 2 282 . 2 1 39 39 ILE HD12 H 1 0.412 0.000 . 1 . . . . . . . . 5989 2 283 . 2 1 39 39 ILE HD13 H 1 0.412 0.000 . 1 . . . . . . . . 5989 2 284 . 2 1 40 40 ASP H H 1 8.777 0.000 . 1 . . . . . . . . 5989 2 285 . 2 1 40 40 ASP HA H 1 4.894 0.000 . 1 . . . . . . . . 5989 2 286 . 2 1 40 40 ASP HB2 H 1 2.802 0.001 . 2 . . . . . . . . 5989 2 287 . 2 1 41 41 VAL H H 1 7.617 0.000 . 1 . . . . . . . . 5989 2 288 . 2 1 41 41 VAL HA H 1 4.029 0.000 . 1 . . . . . . . . 5989 2 289 . 2 1 41 41 VAL HB H 1 1.720 0.000 . 1 . . . . . . . . 5989 2 290 . 2 1 41 41 VAL HG11 H 1 0.770 0.000 . 2 . . . . . . . . 5989 2 291 . 2 1 41 41 VAL HG12 H 1 0.770 0.000 . 2 . . . . . . . . 5989 2 292 . 2 1 41 41 VAL HG13 H 1 0.770 0.000 . 2 . . . . . . . . 5989 2 293 . 2 1 42 42 CYS H H 1 8.877 0.003 . 1 . . . . . . . . 5989 2 294 . 2 1 42 42 CYS HA H 1 4.461 0.002 . 1 . . . . . . . . 5989 2 295 . 2 1 42 42 CYS HB2 H 1 2.756 0.003 . 1 . . . . . . . . 5989 2 296 . 2 1 42 42 CYS HB3 H 1 3.108 0.008 . 1 . . . . . . . . 5989 2 297 . 2 1 43 43 PRO HA H 1 4.092 0.000 . 1 . . . . . . . . 5989 2 298 . 2 1 43 43 PRO HB2 H 1 1.905 0.000 . 1 . . . . . . . . 5989 2 299 . 2 1 43 43 PRO HB3 H 1 0.749 0.000 . 1 . . . . . . . . 5989 2 300 . 2 1 43 43 PRO HG2 H 1 0.547 0.000 . 1 . . . . . . . . 5989 2 301 . 2 1 43 43 PRO HG3 H 1 1.220 0.000 . 1 . . . . . . . . 5989 2 302 . 2 1 43 43 PRO HD2 H 1 2.354 0.000 . 1 . . . . . . . . 5989 2 303 . 2 1 43 43 PRO HD3 H 1 3.915 0.000 . 1 . . . . . . . . 5989 2 304 . 2 1 44 44 LYS H H 1 7.856 0.000 . 1 . . . . . . . . 5989 2 305 . 2 1 44 44 LYS HA H 1 4.206 0.000 . 1 . . . . . . . . 5989 2 306 . 2 1 44 44 LYS HB2 H 1 1.714 0.000 . 1 . . . . . . . . 5989 2 307 . 2 1 44 44 LYS HB3 H 1 1.847 0.000 . 1 . . . . . . . . 5989 2 308 . 2 1 44 44 LYS HG2 H 1 1.553 0.000 . 2 . . . . . . . . 5989 2 309 . 2 1 44 44 LYS HE2 H 1 3.041 0.000 . 2 . . . . . . . . 5989 2 310 . 2 1 44 44 LYS HZ1 H 1 7.510 0.000 . 1 . . . . . . . . 5989 2 311 . 2 1 44 44 LYS HZ2 H 1 7.510 0.000 . 1 . . . . . . . . 5989 2 312 . 2 1 44 44 LYS HZ3 H 1 7.510 0.000 . 1 . . . . . . . . 5989 2 313 . 2 1 45 45 ASN H H 1 8.423 0.001 . 1 . . . . . . . . 5989 2 314 . 2 1 45 45 ASN HA H 1 4.960 0.001 . 1 . . . . . . . . 5989 2 315 . 2 1 45 45 ASN HB2 H 1 2.881 0.000 . 1 . . . . . . . . 5989 2 316 . 2 1 45 45 ASN HB3 H 1 3.257 0.000 . 1 . . . . . . . . 5989 2 317 . 2 1 45 45 ASN HD21 H 1 7.692 0.000 . 1 . . . . . . . . 5989 2 318 . 2 1 45 45 ASN HD22 H 1 7.371 0.000 . 1 . . . . . . . . 5989 2 319 . 2 1 46 46 SER H H 1 9.047 0.000 . 1 . . . . . . . . 5989 2 320 . 2 1 46 46 SER HA H 1 5.041 0.001 . 1 . . . . . . . . 5989 2 321 . 2 1 46 46 SER HB2 H 1 4.481 0.000 . 1 . . . . . . . . 5989 2 322 . 2 1 46 46 SER HB3 H 1 3.993 0.000 . 1 . . . . . . . . 5989 2 323 . 2 1 47 47 LEU H H 1 8.341 0.000 . 1 . . . . . . . . 5989 2 324 . 2 1 47 47 LEU HA H 1 4.283 0.001 . 1 . . . . . . . . 5989 2 325 . 2 1 47 47 LEU HB2 H 1 1.931 0.000 . 1 . . . . . . . . 5989 2 326 . 2 1 47 47 LEU HB3 H 1 1.632 0.000 . 1 . . . . . . . . 5989 2 327 . 2 1 47 47 LEU HD11 H 1 0.935 0.000 . 1 . . . . . . . . 5989 2 328 . 2 1 47 47 LEU HD12 H 1 0.935 0.000 . 1 . . . . . . . . 5989 2 329 . 2 1 47 47 LEU HD13 H 1 0.935 0.000 . 1 . . . . . . . . 5989 2 330 . 2 1 47 47 LEU HD21 H 1 0.964 0.000 . 1 . . . . . . . . 5989 2 331 . 2 1 47 47 LEU HD22 H 1 0.964 0.000 . 1 . . . . . . . . 5989 2 332 . 2 1 47 47 LEU HD23 H 1 0.964 0.000 . 1 . . . . . . . . 5989 2 333 . 2 1 47 47 LEU HG H 1 1.758 0.000 . 1 . . . . . . . . 5989 2 334 . 2 1 48 48 LEU H H 1 8.216 0.000 . 1 . . . . . . . . 5989 2 335 . 2 1 48 48 LEU HA H 1 4.497 0.000 . 1 . . . . . . . . 5989 2 336 . 2 1 48 48 LEU HB2 H 1 1.748 0.000 . 1 . . . . . . . . 5989 2 337 . 2 1 48 48 LEU HB3 H 1 1.667 0.000 . 1 . . . . . . . . 5989 2 338 . 2 1 48 48 LEU HD11 H 1 0.882 0.000 . 1 . . . . . . . . 5989 2 339 . 2 1 48 48 LEU HD12 H 1 0.882 0.000 . 1 . . . . . . . . 5989 2 340 . 2 1 48 48 LEU HD13 H 1 0.882 0.000 . 1 . . . . . . . . 5989 2 341 . 2 1 48 48 LEU HD21 H 1 0.958 0.000 . 1 . . . . . . . . 5989 2 342 . 2 1 48 48 LEU HD22 H 1 0.958 0.000 . 1 . . . . . . . . 5989 2 343 . 2 1 48 48 LEU HD23 H 1 0.958 0.000 . 1 . . . . . . . . 5989 2 344 . 2 1 49 49 VAL H H 1 7.515 0.000 . 1 . . . . . . . . 5989 2 345 . 2 1 49 49 VAL HA H 1 5.051 0.000 . 1 . . . . . . . . 5989 2 346 . 2 1 49 49 VAL HB H 1 1.860 0.000 . 1 . . . . . . . . 5989 2 347 . 2 1 49 49 VAL HG11 H 1 0.819 0.000 . 1 . . . . . . . . 5989 2 348 . 2 1 49 49 VAL HG12 H 1 0.819 0.000 . 1 . . . . . . . . 5989 2 349 . 2 1 49 49 VAL HG13 H 1 0.819 0.000 . 1 . . . . . . . . 5989 2 350 . 2 1 49 49 VAL HG21 H 1 0.895 0.000 . 1 . . . . . . . . 5989 2 351 . 2 1 49 49 VAL HG22 H 1 0.895 0.000 . 1 . . . . . . . . 5989 2 352 . 2 1 49 49 VAL HG23 H 1 0.895 0.000 . 1 . . . . . . . . 5989 2 353 . 2 1 50 50 LYS H H 1 8.812 0.000 . 1 . . . . . . . . 5989 2 354 . 2 1 50 50 LYS HA H 1 4.804 0.000 . 1 . . . . . . . . 5989 2 355 . 2 1 50 50 LYS HB2 H 1 1.793 0.000 . 1 . . . . . . . . 5989 2 356 . 2 1 50 50 LYS HB3 H 1 1.608 0.000 . 1 . . . . . . . . 5989 2 357 . 2 1 50 50 LYS HG2 H 1 1.220 0.000 . 2 . . . . . . . . 5989 2 358 . 2 1 50 50 LYS HD2 H 1 1.521 0.000 . 2 . . . . . . . . 5989 2 359 . 2 1 50 50 LYS HE2 H 1 2.867 0.000 . 2 . . . . . . . . 5989 2 360 . 2 1 50 50 LYS HZ1 H 1 7.630 0.000 . 1 . . . . . . . . 5989 2 361 . 2 1 50 50 LYS HZ2 H 1 7.630 0.000 . 1 . . . . . . . . 5989 2 362 . 2 1 50 50 LYS HZ3 H 1 7.630 0.000 . 1 . . . . . . . . 5989 2 363 . 2 1 51 51 TYR H H 1 9.251 0.000 . 1 . . . . . . . . 5989 2 364 . 2 1 51 51 TYR HA H 1 5.385 0.000 . 1 . . . . . . . . 5989 2 365 . 2 1 51 51 TYR HB2 H 1 2.989 0.000 . 1 . . . . . . . . 5989 2 366 . 2 1 51 51 TYR HB3 H 1 2.785 0.001 . 1 . . . . . . . . 5989 2 367 . 2 1 51 51 TYR HD1 H 1 6.894 0.000 . 2 . . . . . . . . 5989 2 368 . 2 1 51 51 TYR HE1 H 1 6.554 0.000 . 2 . . . . . . . . 5989 2 369 . 2 1 52 52 VAL H H 1 9.022 0.000 . 1 . . . . . . . . 5989 2 370 . 2 1 52 52 VAL HA H 1 4.577 0.000 . 1 . . . . . . . . 5989 2 371 . 2 1 52 52 VAL HB H 1 2.092 0.000 . 1 . . . . . . . . 5989 2 372 . 2 1 52 52 VAL HG11 H 1 1.071 0.000 . 1 . . . . . . . . 5989 2 373 . 2 1 52 52 VAL HG12 H 1 1.071 0.000 . 1 . . . . . . . . 5989 2 374 . 2 1 52 52 VAL HG13 H 1 1.071 0.000 . 1 . . . . . . . . 5989 2 375 . 2 1 52 52 VAL HG21 H 1 1.162 0.000 . 1 . . . . . . . . 5989 2 376 . 2 1 52 52 VAL HG22 H 1 1.162 0.000 . 1 . . . . . . . . 5989 2 377 . 2 1 52 52 VAL HG23 H 1 1.162 0.000 . 1 . . . . . . . . 5989 2 378 . 2 1 53 53 CYS H H 1 9.495 0.000 . 1 . . . . . . . . 5989 2 379 . 2 1 53 53 CYS HA H 1 5.870 0.001 . 1 . . . . . . . . 5989 2 380 . 2 1 53 53 CYS HB2 H 1 3.087 0.000 . 1 . . . . . . . . 5989 2 381 . 2 1 53 53 CYS HB3 H 1 3.810 0.000 . 1 . . . . . . . . 5989 2 382 . 2 1 54 54 CYS H H 1 9.227 0.000 . 1 . . . . . . . . 5989 2 383 . 2 1 54 54 CYS HA H 1 5.113 0.000 . 1 . . . . . . . . 5989 2 384 . 2 1 54 54 CYS HB2 H 1 3.443 0.000 . 1 . . . . . . . . 5989 2 385 . 2 1 54 54 CYS HB3 H 1 3.658 0.000 . 1 . . . . . . . . 5989 2 386 . 2 1 55 55 ASN H H 1 8.547 0.000 . 1 . . . . . . . . 5989 2 387 . 2 1 55 55 ASN HA H 1 5.177 0.000 . 1 . . . . . . . . 5989 2 388 . 2 1 55 55 ASN HB2 H 1 2.639 0.000 . 1 . . . . . . . . 5989 2 389 . 2 1 55 55 ASN HB3 H 1 3.372 0.000 . 1 . . . . . . . . 5989 2 390 . 2 1 55 55 ASN HD21 H 1 6.728 0.000 . 1 . . . . . . . . 5989 2 391 . 2 1 55 55 ASN HD22 H 1 7.536 0.000 . 1 . . . . . . . . 5989 2 392 . 2 1 56 56 THR H H 1 7.590 0.006 . 1 . . . . . . . . 5989 2 393 . 2 1 56 56 THR HA H 1 4.717 0.000 . 1 . . . . . . . . 5989 2 394 . 2 1 56 56 THR HB H 1 4.297 0.000 . 1 . . . . . . . . 5989 2 395 . 2 1 56 56 THR HG21 H 1 1.206 0.000 . 1 . . . . . . . . 5989 2 396 . 2 1 56 56 THR HG22 H 1 1.206 0.000 . 1 . . . . . . . . 5989 2 397 . 2 1 56 56 THR HG23 H 1 1.206 0.000 . 1 . . . . . . . . 5989 2 398 . 2 1 57 57 ASP H H 1 8.232 0.000 . 1 . . . . . . . . 5989 2 399 . 2 1 57 57 ASP HA H 1 4.817 0.004 . 1 . . . . . . . . 5989 2 400 . 2 1 57 57 ASP HB2 H 1 2.493 0.005 . 1 . . . . . . . . 5989 2 401 . 2 1 57 57 ASP HB3 H 1 2.272 0.005 . 1 . . . . . . . . 5989 2 402 . 2 1 58 58 ARG H H 1 9.649 0.000 . 1 . . . . . . . . 5989 2 403 . 2 1 58 58 ARG HA H 1 3.397 0.000 . 1 . . . . . . . . 5989 2 404 . 2 1 58 58 ARG HB2 H 1 1.798 0.000 . 1 . . . . . . . . 5989 2 405 . 2 1 58 58 ARG HB3 H 1 2.192 0.000 . 1 . . . . . . . . 5989 2 406 . 2 1 58 58 ARG HG2 H 1 1.321 0.000 . 1 . . . . . . . . 5989 2 407 . 2 1 58 58 ARG HG3 H 1 1.370 0.000 . 1 . . . . . . . . 5989 2 408 . 2 1 58 58 ARG HE H 1 7.850 0.000 . 1 . . . . . . . . 5989 2 409 . 2 1 59 59 CYS H H 1 7.583 0.000 . 1 . . . . . . . . 5989 2 410 . 2 1 59 59 CYS HA H 1 4.465 0.000 . 1 . . . . . . . . 5989 2 411 . 2 1 59 59 CYS HB2 H 1 3.365 0.000 . 1 . . . . . . . . 5989 2 412 . 2 1 59 59 CYS HB3 H 1 3.649 0.000 . 1 . . . . . . . . 5989 2 413 . 2 1 60 60 ASN H H 1 8.956 0.000 . 1 . . . . . . . . 5989 2 414 . 2 1 60 60 ASN HA H 1 4.382 0.000 . 1 . . . . . . . . 5989 2 415 . 2 1 60 60 ASN HB2 H 1 2.774 0.000 . 1 . . . . . . . . 5989 2 416 . 2 1 60 60 ASN HB3 H 1 2.310 0.000 . 1 . . . . . . . . 5989 2 417 . 2 1 60 60 ASN HD21 H 1 7.563 0.000 . 1 . . . . . . . . 5989 2 418 . 2 1 60 60 ASN HD22 H 1 7.752 0.000 . 1 . . . . . . . . 5989 2 stop_ save_ ######################## # Coupling constants # ######################## save_J_values_1 _Coupling_constant_list.Sf_category coupling_constants _Coupling_constant_list.Sf_framecode J_values_1 _Coupling_constant_list.Entry_ID 5989 _Coupling_constant_list.ID 1 _Coupling_constant_list.Sample_condition_list_ID 1 _Coupling_constant_list.Sample_condition_list_label $condition_1 _Coupling_constant_list.Spectrometer_frequency_1H 500 _Coupling_constant_list.Details . _Coupling_constant_list.Text_data_format . _Coupling_constant_list.Text_data . loop_ _Coupling_constant_experiment.Experiment_ID _Coupling_constant_experiment.Experiment_name _Coupling_constant_experiment.Sample_ID _Coupling_constant_experiment.Sample_label _Coupling_constant_experiment.Sample_state _Coupling_constant_experiment.Entry_ID _Coupling_constant_experiment.Coupling_constant_list_ID . . 1 $sample_1 . 5989 1 stop_ loop_ _Coupling_constant.ID _Coupling_constant.Code _Coupling_constant.Assembly_atom_ID_1 _Coupling_constant.Entity_assembly_ID_1 _Coupling_constant.Entity_ID_1 _Coupling_constant.Comp_index_ID_1 _Coupling_constant.Seq_ID_1 _Coupling_constant.Comp_ID_1 _Coupling_constant.Atom_ID_1 _Coupling_constant.Atom_type_1 _Coupling_constant.Atom_isotope_number_1 _Coupling_constant.Ambiguity_code_1 _Coupling_constant.Assembly_atom_ID_2 _Coupling_constant.Entity_assembly_ID_2 _Coupling_constant.Entity_ID_2 _Coupling_constant.Comp_index_ID_2 _Coupling_constant.Seq_ID_2 _Coupling_constant.Comp_ID_2 _Coupling_constant.Atom_ID_2 _Coupling_constant.Atom_type_2 _Coupling_constant.Atom_isotope_number_2 _Coupling_constant.Ambiguity_code_2 _Coupling_constant.Val _Coupling_constant.Val_min _Coupling_constant.Val_max _Coupling_constant.Val_err _Coupling_constant.Resonance_ID_1 _Coupling_constant.Resonance_ID_2 _Coupling_constant.Auth_entity_assembly_ID_1 _Coupling_constant.Auth_seq_ID_1 _Coupling_constant.Auth_comp_ID_1 _Coupling_constant.Auth_atom_ID_1 _Coupling_constant.Auth_entity_assembly_ID_2 _Coupling_constant.Auth_seq_ID_2 _Coupling_constant.Auth_comp_ID_2 _Coupling_constant.Auth_atom_ID_2 _Coupling_constant.Details _Coupling_constant.Entry_ID _Coupling_constant.Coupling_constant_list_ID 1 3JHNHA . 1 1 2 2 LYS H H 1 . . 1 1 2 2 LYS HA H 1 . 9.2 . . 0.4 . . . . . . . . . . . 5989 1 2 3JHNHA . 1 1 3 3 CYS H H 1 . . 1 1 3 3 CYS HA H 1 . 10.5 . . 0.4 . . . . . . . . . . . 5989 1 3 3JHNHA . 1 1 5 5 LYS H H 1 . . 1 1 5 5 LYS HA H 1 . 7.9 . . 0.4 . . . . . . . . . . . 5989 1 4 3JHNHA . 1 1 6 6 LEU H H 1 . . 1 1 6 6 LEU HA H 1 . 3.6 . . 0.4 . . . . . . . . . . . 5989 1 5 3JHNHA . 1 1 7 7 VAL H H 1 . . 1 1 7 7 VAL HA H 1 . 8.3 . . 0.4 . . . . . . . . . . . 5989 1 6 3JHNHA . 1 1 9 9 ILE H H 1 . . 1 1 9 9 ILE HA H 1 . 8.5 . . 0.4 . . . . . . . . . . . 5989 1 7 3JHNHA . 1 1 10 10 ALA H H 1 . . 1 1 10 10 ALA HA H 1 . 6.2 . . 0.4 . . . . . . . . . . . 5989 1 8 3JHNHA . 1 1 11 11 TYR H H 1 . . 1 1 11 11 TYR HA H 1 . 9.0 . . 0.4 . . . . . . . . . . . 5989 1 9 3JHNHA . 1 1 12 12 LYS H H 1 . . 1 1 12 12 LYS HA H 1 . 9.9 . . 0.4 . . . . . . . . . . . 5989 1 10 3JHNHA . 1 1 13 13 THR H H 1 . . 1 1 13 13 THR HA H 1 . 9.0 . . 0.4 . . . . . . . . . . . 5989 1 11 3JHNHA . 1 1 14 14 CYS H H 1 . . 1 1 14 14 CYS HA H 1 . 5.3 . . 0.4 . . . . . . . . . . . 5989 1 12 3JHNHA . 1 1 16 16 GLU H H 1 . . 1 1 16 16 GLU HA H 1 . 4.2 . . 0.4 . . . . . . . . . . . 5989 1 13 3JHNHA . 1 1 18 18 LYS H H 1 . . 1 1 18 18 LYS HA H 1 . 8.6 . . 0.4 . . . . . . . . . . . 5989 1 14 3JHNHA . 1 1 19 19 ASN H H 1 . . 1 1 19 19 ASN HA H 1 . 9.7 . . 0.4 . . . . . . . . . . . 5989 1 15 3JHNHA . 1 1 20 20 LEU H H 1 . . 1 1 20 20 LEU HA H 1 . 8.5 . . 0.4 . . . . . . . . . . . 5989 1 16 3JHNHA . 1 1 22 22 TYR H H 1 . . 1 1 22 22 TYR HA H 1 . 10.0 . . 0.4 . . . . . . . . . . . 5989 1 17 3JHNHA . 1 1 21 21 CYS H H 1 . . 1 1 21 21 CYS HA H 1 . 10.4 . . 0.4 . . . . . . . . . . . 5989 1 18 3JHNHA . 1 1 23 23 LYS H H 1 . . 1 1 23 23 LYS HA H 1 . 3.6 . . 0.4 . . . . . . . . . . . 5989 1 19 3JHNHA . 1 1 24 24 MET H H 1 . . 1 1 24 24 MET HA H 1 . 9.8 . . 0.4 . . . . . . . . . . . 5989 1 20 3JHNHA . 1 1 25 25 PHE H H 1 . . 1 1 25 25 PHE HA H 1 . 9.0 . . 0.4 . . . . . . . . . . . 5989 1 21 3JHNHA . 1 1 26 26 MET H H 1 . . 1 1 26 26 MET HA H 1 . 7.4 . . 0.4 . . . . . . . . . . . 5989 1 22 3JHNHA . 1 1 27 27 MET H H 1 . . 1 1 27 27 MET HA H 1 . 5.5 . . 0.4 . . . . . . . . . . . 5989 1 23 3JHNHA . 1 1 28 28 SER H H 1 . . 1 1 28 28 SER HA H 1 . 5.3 . . 0.4 . . . . . . . . . . . 5989 1 24 3JHNHA . 1 1 29 29 ASP H H 1 . . 1 1 29 29 ASP HA H 1 . 5.6 . . 0.4 . . . . . . . . . . . 5989 1 25 3JHNHA . 1 1 30 30 LEU H H 1 . . 1 1 30 30 LEU HA H 1 . 6.5 . . 0.4 . . . . . . . . . . . 5989 1 26 3JHNHA . 1 1 31 31 THR H H 1 . . 1 1 31 31 THR HA H 1 . 7.0 . . 1.0 . . . . . . . . . . . 5989 1 27 3JHNHA . 1 1 34 34 VAL H H 1 . . 1 1 34 34 VAL HA H 1 . 10.1 . . 0.4 . . . . . . . . . . . 5989 1 28 3JHNHA . 1 1 36 36 ARG H H 1 . . 1 1 36 36 ARG HA H 1 . 8.1 . . 0.4 . . . . . . . . . . . 5989 1 29 3JHNHA . 1 1 38 38 CYS H H 1 . . 1 1 38 38 CYS HA H 1 . 9.7 . . 0.4 . . . . . . . . . . . 5989 1 30 3JHNHA . 1 1 39 39 ILE H H 1 . . 1 1 39 39 ILE HA H 1 . 7.5 . . 0.4 . . . . . . . . . . . 5989 1 31 3JHNHA . 1 1 40 40 ASP H H 1 . . 1 1 40 40 ASP HA H 1 . 8.0 . . 0.4 . . . . . . . . . . . 5989 1 32 3JHNHA . 1 1 41 41 VAL H H 1 . . 1 1 41 41 VAL HA H 1 . 10.5 . . 0.4 . . . . . . . . . . . 5989 1 33 3JHNHA . 1 1 42 42 CYS H H 1 . . 1 1 42 42 CYS HA H 1 . 5.7 . . 0.4 . . . . . . . . . . . 5989 1 34 3JHNHA . 1 1 44 44 LYS H H 1 . . 1 1 44 44 LYS HA H 1 . 5.8 . . 0.4 . . . . . . . . . . . 5989 1 35 3JHNHA . 1 1 45 45 ASN H H 1 . . 1 1 45 45 ASN HA H 1 . 6.3 . . 0.4 . . . . . . . . . . . 5989 1 36 3JHNHA . 1 1 46 46 SER H H 1 . . 1 1 46 46 SER HA H 1 . 8.3 . . 0.4 . . . . . . . . . . . 5989 1 37 3JHNHA . 1 1 47 47 LEU H H 1 . . 1 1 47 47 LEU HA H 1 . 6.5 . . 1.0 . . . . . . . . . . . 5989 1 38 3JHNHA . 1 1 48 48 LEU H H 1 . . 1 1 48 48 LEU HA H 1 . 8.8 . . 0.4 . . . . . . . . . . . 5989 1 39 3JHNHA . 1 1 49 49 VAL H H 1 . . 1 1 49 49 VAL HA H 1 . 10.3 . . 0.4 . . . . . . . . . . . 5989 1 40 3JHNHA . 1 1 51 51 TYR H H 1 . . 1 1 51 51 TYR HA H 1 . 10.4 . . 0.4 . . . . . . . . . . . 5989 1 41 3JHNHA . 1 1 52 52 VAL H H 1 . . 1 1 52 52 VAL HA H 1 . 8.9 . . 0.4 . . . . . . . . . . . 5989 1 42 3JHNHA . 1 1 53 53 CYS H H 1 . . 1 1 53 53 CYS HA H 1 . 9.7 . . 0.4 . . . . . . . . . . . 5989 1 43 3JHNHA . 1 1 54 54 CYS H H 1 . . 1 1 54 54 CYS HA H 1 . 7.4 . . 0.4 . . . . . . . . . . . 5989 1 44 3JHNHA . 1 1 55 55 ASN H H 1 . . 1 1 55 55 ASN HA H 1 . 9.3 . . 0.4 . . . . . . . . . . . 5989 1 45 3JHNHA . 1 1 56 56 THR H H 1 . . 1 1 56 56 THR HA H 1 . 9.4 . . 0.4 . . . . . . . . . . . 5989 1 46 3JHNHA . 1 1 58 58 ARG H H 1 . . 1 1 58 58 ARG HA H 1 . 9.2 . . 0.4 . . . . . . . . . . . 5989 1 47 3JHNHA . 1 1 60 60 ASN H H 1 . . 1 1 60 60 ASN HA H 1 . 8.4 . . 0.4 . . . . . . . . . . . 5989 1 48 3JHAHB . 1 1 2 2 LYS HA H 1 . . 1 1 2 2 LYS HB2 H 1 . 11.7 . . 0.8 . . . . . . . . . . . 5989 1 49 3JHAHB . 1 1 3 3 CYS HA H 1 . . 1 1 3 3 CYS HB2 H 1 . 12.3 . . 0.5 . . . . . . . . . . . 5989 1 50 3JHAHB . 1 1 4 4 ASN HA H 1 . . 1 1 4 4 ASN HB2 H 1 . 12.4 . . 0.5 . . . . . . . . . . . 5989 1 51 3JHAHB . 1 1 5 5 LYS HA H 1 . . 1 1 5 5 LYS HB2 H 1 . 13.2 . . 0.5 . . . . . . . . . . . 5989 1 52 3JHAHB . 1 1 6 6 LEU HA H 1 . . 1 1 6 6 LEU HB3 H 1 . 11.6 . . 0.5 . . . . . . . . . . . 5989 1 53 3JHAHB . 1 1 7 7 VAL HA H 1 . . 1 1 7 7 VAL HB H 1 . 10.1 . . 0.5 . . . . . . . . . . . 5989 1 54 3JHAHB . 1 1 8 8 PRO HA H 1 . . 1 1 8 8 PRO HB2 H 1 . 8.5 . . 0.5 . . . . . . . . . . . 5989 1 55 3JHAHB . 1 1 9 9 ILE HA H 1 . . 1 1 9 9 ILE HB H 1 . 5.2 . . 0.5 . . . . . . . . . . . 5989 1 56 3JHAHB . 1 1 11 11 TYR HA H 1 . . 1 1 11 11 TYR HB2 H 1 . 4.4 . . 0.5 . . . . . . . . . . . 5989 1 57 3JHAHB . 1 1 13 13 THR HA H 1 . . 1 1 13 13 THR HB H 1 . 9.4 . . 0.5 . . . . . . . . . . . 5989 1 58 3JHAHB . 1 1 14 14 CYS HA H 1 . . 1 1 14 14 CYS HB2 H 1 . 13.5 . . 0.5 . . . . . . . . . . . 5989 1 59 3JHAHB . 1 1 15 15 PRO HA H 1 . . 1 1 15 15 PRO HB3 H 1 . 9.5 . . 1.0 . . . . . . . . . . . 5989 1 60 3JHAHB . 1 1 15 15 PRO HA H 1 . . 1 1 15 15 PRO HB2 H 1 . 5.5 . . 1.0 . . . . . . . . . . . 5989 1 61 3JHAHB . 1 1 16 16 GLU HA H 1 . . 1 1 16 16 GLU HB2 H 1 . 12.5 . . 0.5 . . . . . . . . . . . 5989 1 62 3JHAHB . 1 1 19 19 ASN HA H 1 . . 1 1 19 19 ASN HB3 H 1 . 11.5 . . 0.5 . . . . . . . . . . . 5989 1 63 3JHAHB . 1 1 19 19 ASN HA H 1 . . 1 1 19 19 ASN HB2 H 1 . 4.7 . . 0.5 . . . . . . . . . . . 5989 1 64 3JHAHB . 1 1 20 20 LEU HA H 1 . . 1 1 20 20 LEU HB2 H 1 . 12.4 . . 0.5 . . . . . . . . . . . 5989 1 65 3JHAHB . 1 1 21 21 CYS HA H 1 . . 1 1 21 21 CYS HB2 H 1 . 12.8 . . 1.0 . . . . . . . . . . . 5989 1 66 3JHAHB . 1 1 23 23 LYS HA H 1 . . 1 1 23 23 LYS HB2 H 1 . 4.9 . . 0.5 . . . . . . . . . . . 5989 1 67 3JHAHB . 1 1 24 24 MET HA H 1 . . 1 1 24 24 MET HB2 H 1 . 12.0 . . 0.5 . . . . . . . . . . . 5989 1 68 3JHAHB . 1 1 25 25 PHE HA H 1 . . 1 1 25 25 PHE HB2 H 1 . 12.7 . . 0.5 . . . . . . . . . . . 5989 1 69 3JHAHB . 1 1 26 26 MET HA H 1 . . 1 1 26 26 MET HB2 H 1 . 13.7 . . 0.5 . . . . . . . . . . . 5989 1 70 3JHAHB . 1 1 27 27 MET HA H 1 . . 1 1 27 27 MET HB2 H 1 . 11.5 . . 0.5 . . . . . . . . . . . 5989 1 71 3JHAHB . 1 1 29 29 ASP HA H 1 . . 1 1 29 29 ASP HB3 H 1 . 12.4 . . 0.5 . . . . . . . . . . . 5989 1 72 3JHAHB . 1 1 30 30 LEU HA H 1 . . 1 1 30 30 LEU HB2 H 1 . 13.1 . . 0.5 . . . . . . . . . . . 5989 1 73 3JHAHB . 1 1 31 31 THR HA H 1 . . 1 1 31 31 THR HB H 1 . 5.3 . . 0.5 . . . . . . . . . . . 5989 1 74 3JHAHB . 1 1 32 32 ILE HA H 1 . . 1 1 32 32 ILE HB H 1 . 9.8 . . 0.5 . . . . . . . . . . . 5989 1 75 3JHAHB . 1 1 34 34 VAL HA H 1 . . 1 1 34 34 VAL HB H 1 . 5.1 . . 0.5 . . . . . . . . . . . 5989 1 76 3JHAHB . 1 1 35 35 LYS HA H 1 . . 1 1 35 35 LYS HB2 H 1 . 11.7 . . 0.5 . . . . . . . . . . . 5989 1 77 3JHAHB . 1 1 35 35 LYS HA H 1 . . 1 1 35 35 LYS HB3 H 1 . 5.0 . . 0.5 . . . . . . . . . . . 5989 1 78 3JHAHB . 1 1 36 36 ARG HA H 1 . . 1 1 36 36 ARG HB2 H 1 . 10.9 . . 1.0 . . . . . . . . . . . 5989 1 79 3JHAHB . 1 1 38 38 CYS HA H 1 . . 1 1 38 38 CYS HB3 H 1 . 3.5 . . 0.5 . . . . . . . . . . . 5989 1 80 3JHAHB . 1 1 38 38 CYS HA H 1 . . 1 1 38 38 CYS HB2 H 1 . 12.4 . . 0.5 . . . . . . . . . . . 5989 1 81 3JHAHB . 1 1 39 39 ILE HA H 1 . . 1 1 39 39 ILE HB H 1 . 2.0 . . 0.5 . . . . . . . . . . . 5989 1 82 3JHAHB . 1 1 41 41 VAL HA H 1 . . 1 1 41 41 VAL HB H 1 . 8.9 . . 0.5 . . . . . . . . . . . 5989 1 83 3JHAHB . 1 1 42 42 CYS HA H 1 . . 1 1 42 42 CYS HB3 H 1 . 11.2 . . 0.5 . . . . . . . . . . . 5989 1 84 3JHAHB . 1 1 43 43 PRO HA H 1 . . 1 1 43 43 PRO HB3 H 1 . 9.4 . . 0.5 . . . . . . . . . . . 5989 1 85 3JHAHB . 1 1 43 43 PRO HA H 1 . . 1 1 43 43 PRO HB2 H 1 . 8.8 . . 0.5 . . . . . . . . . . . 5989 1 86 3JHAHB . 1 1 44 44 LYS HA H 1 . . 1 1 44 44 LYS HB2 H 1 . 11.9 . . 0.5 . . . . . . . . . . . 5989 1 87 3JHAHB . 1 1 45 45 ASN HA H 1 . . 1 1 45 45 ASN HB2 H 1 . 11.8 . . 0.5 . . . . . . . . . . . 5989 1 88 3JHAHB . 1 1 46 46 SER HA H 1 . . 1 1 46 46 SER HB3 H 1 . 3.2 . . 1.0 . . . . . . . . . . . 5989 1 89 3JHAHB . 1 1 46 46 SER HA H 1 . . 1 1 46 46 SER HB2 H 1 . 3.2 . . 0.5 . . . . . . . . . . . 5989 1 90 3JHAHB . 1 1 47 47 LEU HA H 1 . . 1 1 47 47 LEU HB2 H 1 . 13.2 . . 0.5 . . . . . . . . . . . 5989 1 91 3JHAHB . 1 1 48 48 LEU HA H 1 . . 1 1 48 48 LEU HB3 H 1 . 4.3 . . 0.5 . . . . . . . . . . . 5989 1 92 3JHAHB . 1 1 48 48 LEU HA H 1 . . 1 1 48 48 LEU HB2 H 1 . 12.0 . . 0.5 . . . . . . . . . . . 5989 1 93 3JHAHB . 1 1 49 49 VAL HA H 1 . . 1 1 49 49 VAL HB H 1 . 6.2 . . 0.5 . . . . . . . . . . . 5989 1 94 3JHAHB . 1 1 50 50 LYS HA H 1 . . 1 1 50 50 LYS HB3 H 1 . 12.4 . . 0.5 . . . . . . . . . . . 5989 1 95 3JHAHB . 1 1 51 51 TYR HA H 1 . . 1 1 51 51 TYR HB2 H 1 . 12.1 . . 0.5 . . . . . . . . . . . 5989 1 96 3JHAHB . 1 1 52 52 VAL HA H 1 . . 1 1 52 52 VAL HB H 1 . 10.6 . . 0.5 . . . . . . . . . . . 5989 1 97 3JHAHB . 1 1 53 53 CYS HA H 1 . . 1 1 53 53 CYS HB2 H 1 . 12.4 . . 0.5 . . . . . . . . . . . 5989 1 98 3JHAHB . 1 1 53 53 CYS HA H 1 . . 1 1 53 53 CYS HB3 H 1 . 4.0 . . 0.5 . . . . . . . . . . . 5989 1 99 3JHAHB . 1 1 54 54 CYS HA H 1 . . 1 1 54 54 CYS HB2 H 1 . 5.1 . . 0.5 . . . . . . . . . . . 5989 1 100 3JHAHB . 1 1 55 55 ASN HA H 1 . . 1 1 55 55 ASN HB2 H 1 . 3.3 . . 0.5 . . . . . . . . . . . 5989 1 101 3JHAHB . 1 1 55 55 ASN HA H 1 . . 1 1 55 55 ASN HB3 H 1 . 4.4 . . 0.5 . . . . . . . . . . . 5989 1 102 3JHAHB . 1 1 57 57 ASP HA H 1 . . 1 1 57 57 ASP HB2 H 1 . 11.0 . . 0.5 . . . . . . . . . . . 5989 1 103 3JHAHB . 1 1 58 58 ARG HA H 1 . . 1 1 58 58 ARG HB2 H 1 . 12.8 . . 0.5 . . . . . . . . . . . 5989 1 104 3JHAHB . 1 1 59 59 CYS HA H 1 . . 1 1 59 59 CYS HB2 H 1 . 2.6 . . 0.5 . . . . . . . . . . . 5989 1 105 3JHAHB . 1 1 59 59 CYS HA H 1 . . 1 1 59 59 CYS HB3 H 1 . 4.0 . . 0.5 . . . . . . . . . . . 5989 1 106 3JHAHB . 1 1 60 60 ASN HA H 1 . . 1 1 60 60 ASN HB3 H 1 . 3.9 . . 1.0 . . . . . . . . . . . 5989 1 107 3JHAHB . 1 1 60 60 ASN HA H 1 . . 1 1 60 60 ASN HB2 H 1 . 3.6 . . 1.0 . . . . . . . . . . . 5989 1 stop_ save_