data_4966 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4966 _Entry.Title ; 1H and 13C Chemical Shift Assignments for Cardiotoxin A3 from Naja Atra at Neutral pH ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-03-06 _Entry.Accession_date 2001-03-06 _Entry.Last_release_date 2001-03-06 _Entry.Original_release_date 2001-03-06 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.0.16 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Source_data_format . _Entry.Source_data_format_version . _Entry.Generated_software_name . _Entry.Generated_software_version . _Entry.Generated_software_ID . _Entry.Generated_software_label . _Entry.Generated_date . _Entry.DOI . _Entry.UUID . _Entry.Related_coordinate_file_name . _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.ORCID _Entry_author.Entry_ID 1 Shih-Che Sue . . . . 4966 2 Harold Jarrell . C. . . 4966 3 Jean-Robert Brisson . . . . 4966 4 Wen-guey Wu . . . . 4966 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4966 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 59 4966 '1H chemical shifts' 432 4966 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 . . 2001-03-09 . original BMRB . 4966 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4966 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 21526408 _Citation.DOI . _Citation.PubMed_ID 11669614 _Citation.Full_citation . _Citation.Title ; Dynamic Characterization of the Water binding loop in the P-type Cardiotoxin: Implication for the role of the bound Water Molecule ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 40 _Citation.Journal_issue 43 _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 12782 _Citation.Page_last 12794 _Citation.Year 2001 _Citation.Details ; This paper describes a comprehensive NMR analysis of the structure and dynamics of P-type cardiotoxin and its bound water by using triple-quantum 17O NMR, NOE/ROE 2D NMR, and 13C T1 relaxation. ; 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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Shih-Che Sue . . . . 4966 1 2 Harold Jarrell . C. . . 4966 1 3 Jean-Robert Brisson . . . . 4966 1 4 Wen-guey Wu . . . . 4966 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID '13C relaxation' 4966 1 '17O NMR' 4966 1 Cardiotoxin 4966 1 'bound water molecule' 4966 1 'order parameter' 4966 1 'residence time' 4966 1 'triple-quantum filtered' 4966 1 'water binding loop' 4966 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4966 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8308891 _Citation.Full_citation ; Bhaskaran R, Huang CC, Chang DK, Yu C. Cardiotoxin III from the Taiwan cobra (Naja naja atra). Determination of structure in solution and comparison with short neurotoxins. J Mol Biol. 1994 Jan 28;235(4):1291-301. ; _Citation.Title ; Cardiotoxin III from the Taiwan cobra (Naja naja atra). Determination of structure in solution and comparison with short neurotoxins. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 235 _Citation.Journal_issue 4 _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 1291 _Citation.Page_last 1301 _Citation.Year 1994 _Citation.Details ; The structure in solution of cardiotoxin III, a membrane toxin purified from the venom of the Taiwan cobra, Naja naja atra, is reported. Sequence-specific assignment of 1H-NMR lines was completed and the NMR data show the presence of a triple and a double-stranded antiparallel beta-sheet. Many NOE cross peaks identified in NOESY spectra were applied as distance constraints based on a hybrid distance geometry/dynamical simulated annealing technique; 20 structures were found within a single family. The average value of atomic RMS differences between the 20 structures and their geometric mean is 0.087 nm for the backbone atoms and 0.152 nm for all heavy atoms; they are 0.055 nm and 0.12 nm, respectively for the segments of secondary structure. In these selected structures the backbone of the polypeptide chain folds such that five strands emerge from a globular head. Three major loops link these strands to form a double and a triple-stranded antiparallel beta-sheet. Comparison of the structures of the toxin in solution with the X-ray crystal structure of its homologous protein, cardiotoxin V4II from Naja mossambica mossambica, showed good agreement between the structures except at segments of the turns. As the functions of short neurotoxins and cardiotoxins are distinct, despite their similar secondary structural patterns and tertiary folding, a comparative analysis has been carried out between cardiotoxin III and short neurotoxins of known structures. We discuss their structural features in order to clarify relationships between their structure and function. ; 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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 R Bhaskaran R. . . . 4966 2 2 'C C' Huang C. C. . . 4966 2 3 'D K' Chang D. K. . . 4966 2 4 C Yu C. . . . 4966 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4966 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8703923 _Citation.Full_citation ; Chiang CM, Chang SL, Lin HJ, Wu WG. The role of acidic amino acid residues in the structural stability of snake cardiotoxins. Biochemistry. 1996 Jul 16;35(28):9177-86. ; _Citation.Title ; The role of acidic amino acid residues in the structural stability of snake cardiotoxins. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume 35 _Citation.Journal_issue 28 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0006-2960 _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 9177 _Citation.Page_last 9186 _Citation.Year 1996 _Citation.Details ; We have recently shown that membrane-related activities of cardiotoxin V from Naja naja atra (CTX A5) are diminished at acidic pH although the overall beta-sheet structure of the molecule is maintained. In order to understand more about the mechanism of inactivation of CTX at acidic pH, we studied the effect of pH and denaturing reagents on the structural stability of CTX. We found, first, pH-induced structural transitions occurred in CTX A5 at two pH values as judged by the CD ellipticity around 195 nm: an increase in the beta-sheet content occurred around pH 4 and followed by a decrease, therein, around pH 2. The pKa of three acidic amino acid residues in CTX A5, i.e., Glu-17, Asp-42, and Asp-59, were determined to be 4.0, 3.2, and below 2.3, respectively, by NMR spectroscopy. The low pKa value of Asp-59 implies salt bridge formation between Lys-2 and Asp-59. Thus, electrostatic interaction may stabilize the three loop structure in addition to the hydrogen bonds between N- and C-termini of CTX molecule. Second, 2,2,2-trifluoroethanol (TFE) and guanidinium chloride (GdmHCI) were found to induce alpha-helical and random coil formation, respectively, in CTX A5 and eight other beta-sheet CTXs. Comparison of the relative potencies of TFE and GdmHCI to induce structural changes suggests that the amino acid residue located at position 17 plays a role in the structural stability. Specifically, CTXs containing negatively charged Glu-17 are least stable. It is suggested that Glu-17 may perturb the interaction between Lys-2 and Asp-59, and thus the overall stability of beta-sheet, in the presence of denaturing reagent. In conclusion, the perturbed structural stability of CTXs may partially explain the lower activity CTX exhibits at acidic pH. A structural model to account for the unfolding and refolding of CTX molecules without the breaking of disulfide bonds is also proposed. ; 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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'C M' Chiang C. M. . . 4966 3 2 'S L' Chang S. L. . . 4966 3 3 'H J' Lin H. J. . . 4966 3 4 'W G' Wu W. G. . . 4966 3 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_CTX_A3 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_CTX_A3 _Assembly.Entry_ID 4966 _Assembly.ID 1 _Assembly.Name 'Cardiotoxin A3' _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 4966 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 'cardiotoxin A3' 1 $CTX_A3 . . . native . . . . . 4966 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_asym_ID_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_asym_ID_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 . . . . . . . . . . . . 4966 1 2 disulfide single . 1 . 1 CYS 14 14 SG . 1 . 1 CYS 38 38 SG . . . . . . . . . . . . 4966 1 3 disulfide single . 1 . 1 CYS 42 42 SG . 1 . 1 CYS 53 53 SG . . . . . . . . . . . . 4966 1 4 disulfide single . 1 . 1 CYS 54 54 SG . 1 . 1 CYS 59 59 SG . . . . . . . . . . . . 4966 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 1I02 . . . . . . 4966 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'CTX A3' abbreviation 4966 1 'Cardiotoxin A3' system 4966 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'depolarization of muscular cell' 4966 1 hemolysis 4966 1 'heparin binding protien' 4966 1 'membrane binding protein' 4966 1 'protein with one bound water' 4966 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_CTX_A3 _Entity.Sf_category entity _Entity.Sf_framecode CTX_A3 _Entity.Entry_ID 4966 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Cardiotoxin A3' _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 ; LKCNKLVPLFYKTCPAGKNL CYKMFMVATPKVPVKRGCID VCPKSSLLVKYVCCNTDRCN ; _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 . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 6741 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 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 . no BMRB 15305 . cardiotoxin_A3 . . . . . 100.00 60 100.00 100.00 9.64e-26 . . . . 4966 1 . no PDB 1H0J . 'Structural Basis Of The Membrane-Induced Cardiotoxin A3 Oligomerization' . . . . . 100.00 60 100.00 100.00 9.64e-26 . . . . 4966 1 . no PDB 1I02 . 'Nmr Structure Of Ctx A3 At Neutral Ph (20 Structures)' . . . . . 100.00 60 100.00 100.00 9.64e-26 . . . . 4966 1 . no PDB 1XT3 . 'Structure Basis Of Venom Citrate-Dependent Heparin Sulfate- Mediated Cell Surface Retention Of Cobra Cardiotoxin A3' . . . . . 100.00 60 100.00 100.00 9.64e-26 . . . . 4966 1 . no PDB 2BHI . 'Crystal Structure Of Taiwan Cobra Cardiotoxin A3 Complexed With Sulfogalactoceramide' . . . . . 100.00 60 100.00 100.00 9.64e-26 . . . . 4966 1 . no PDB 2CRS . 'Cardiotoxin Iii From Taiwan Cobra (Naja Naja Atra) Determination Of Structure In Solution And Comparison With Short Neurotoxins' . . . . . 100.00 60 100.00 100.00 9.64e-26 . . . . 4966 1 . no PDB 2CRT . 'Cardiotoxin Iii From Taiwan Cobra (Naja Naja Atra) Determination Of Structure In Solution And Comparison With Short Neurotoxins' . . . . . 100.00 60 100.00 100.00 9.64e-26 . . . . 4966 1 . no EMBL CAA07686 . 'cardiotoxin 3 precursor protein [Naja atra]' . . . . . 100.00 81 100.00 100.00 3.15e-26 . . . . 4966 1 . no EMBL CAA90963 . 'cardiotoxin 3 [Naja naja]' . . . . . 100.00 81 98.33 98.33 3.32e-25 . . . . 4966 1 . no EMBL CAB42053 . 'cardiotoxin-31 [Naja atra]' . . . . . 100.00 81 98.33 100.00 9.41e-26 . . . . 4966 1 . no EMBL CAB42055 . 'cardiotoxin-3 [Naja atra]' . . . . . 100.00 81 100.00 100.00 2.54e-26 . . . . 4966 1 . no GenBank AAA49386 . cardiotoxin . . . . . 100.00 81 100.00 100.00 2.37e-26 . . . . 4966 1 . no GenBank AAB01541 . 'cardiotoxin III' . . . . . 100.00 81 100.00 100.00 3.15e-26 . . . . 4966 1 . no GenBank AAB18382 . "cardiotoxin 3' [Naja atra]" . . . . . 100.00 81 100.00 100.00 3.15e-26 . . . . 4966 1 . no GenBank AAB18383 . 'cardiotoxin 3a [Naja atra]' . . . . . 100.00 81 98.33 100.00 9.41e-26 . . . . 4966 1 . no GenBank AAB25733 . 'cardiotoxin isoform 3, cytotoxin isoform 3, CTX-3 [Naja naja=Formosan cobra, ssp. atra, venom, Peptide, 60 aa]' . . . . . 100.00 60 100.00 100.00 9.64e-26 . . . . 4966 1 . no PIR JK0222 . 'cytotoxin 10 - monocled cobra' . . . . . 100.00 60 100.00 100.00 9.64e-26 . . . . 4966 1 . no PRF 0406231A . toxin,cardio . . . . . 100.00 60 100.00 100.00 9.64e-26 . . . . 4966 1 . no PRF 2207174B . cardiotoxin:ISOTYPE=III . . . . . 100.00 81 98.33 98.33 3.32e-25 . . . . 4966 1 . no SWISS-PROT O93471 . 'Cardiotoxin-1 precursor (CTX-1) (Ctx1)' . . . . . 100.00 81 98.33 100.00 8.23e-26 . . . . 4966 1 . no SWISS-PROT O93473 . 'Cardiotoxin-4a precursor (CTX-4a) (Ctx4a)' . . . . . 100.00 81 98.33 98.33 1.16e-25 . . . . 4966 1 . no SWISS-PROT P60301 . 'Cardiotoxin-A3 precursor (CTX-A3) (Cardiotoxin 3) (CTX-3) (Cardiotoxin analog III) (CTX III) (Cytotoxin-3)' . . . . . 100.00 81 100.00 100.00 3.15e-26 . . . . 4966 1 . no SWISS-PROT P60302 . 'Cardiotoxin-3 precursor (CTX-3) (Ctx3)' . . . . . 100.00 81 100.00 100.00 3.15e-26 . . . . 4966 1 . no SWISS-PROT P60303 . 'Cytotoxin-4 precursor (Cytotoxin IV)' . . . . . 100.00 81 100.00 100.00 3.15e-26 . . . . 4966 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'CTX A3' abbreviation 4966 1 'Cardiotoxin A3' common 4966 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 . 4966 1 2 . LYS . 4966 1 3 . CYS . 4966 1 4 . ASN . 4966 1 5 . LYS . 4966 1 6 . LEU . 4966 1 7 . VAL . 4966 1 8 . PRO . 4966 1 9 . LEU . 4966 1 10 . PHE . 4966 1 11 . TYR . 4966 1 12 . LYS . 4966 1 13 . THR . 4966 1 14 . CYS . 4966 1 15 . PRO . 4966 1 16 . ALA . 4966 1 17 . GLY . 4966 1 18 . LYS . 4966 1 19 . ASN . 4966 1 20 . LEU . 4966 1 21 . CYS . 4966 1 22 . TYR . 4966 1 23 . LYS . 4966 1 24 . MET . 4966 1 25 . PHE . 4966 1 26 . MET . 4966 1 27 . VAL . 4966 1 28 . ALA . 4966 1 29 . THR . 4966 1 30 . PRO . 4966 1 31 . LYS . 4966 1 32 . VAL . 4966 1 33 . PRO . 4966 1 34 . VAL . 4966 1 35 . LYS . 4966 1 36 . ARG . 4966 1 37 . GLY . 4966 1 38 . CYS . 4966 1 39 . ILE . 4966 1 40 . ASP . 4966 1 41 . VAL . 4966 1 42 . CYS . 4966 1 43 . PRO . 4966 1 44 . LYS . 4966 1 45 . SER . 4966 1 46 . SER . 4966 1 47 . LEU . 4966 1 48 . LEU . 4966 1 49 . VAL . 4966 1 50 . LYS . 4966 1 51 . TYR . 4966 1 52 . VAL . 4966 1 53 . CYS . 4966 1 54 . CYS . 4966 1 55 . ASN . 4966 1 56 . THR . 4966 1 57 . ASP . 4966 1 58 . ARG . 4966 1 59 . CYS . 4966 1 60 . ASN . 4966 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 4966 1 . LYS 2 2 4966 1 . CYS 3 3 4966 1 . ASN 4 4 4966 1 . LYS 5 5 4966 1 . LEU 6 6 4966 1 . VAL 7 7 4966 1 . PRO 8 8 4966 1 . LEU 9 9 4966 1 . PHE 10 10 4966 1 . TYR 11 11 4966 1 . LYS 12 12 4966 1 . THR 13 13 4966 1 . CYS 14 14 4966 1 . PRO 15 15 4966 1 . ALA 16 16 4966 1 . GLY 17 17 4966 1 . LYS 18 18 4966 1 . ASN 19 19 4966 1 . LEU 20 20 4966 1 . CYS 21 21 4966 1 . TYR 22 22 4966 1 . LYS 23 23 4966 1 . MET 24 24 4966 1 . PHE 25 25 4966 1 . MET 26 26 4966 1 . VAL 27 27 4966 1 . ALA 28 28 4966 1 . THR 29 29 4966 1 . PRO 30 30 4966 1 . LYS 31 31 4966 1 . VAL 32 32 4966 1 . PRO 33 33 4966 1 . VAL 34 34 4966 1 . LYS 35 35 4966 1 . ARG 36 36 4966 1 . GLY 37 37 4966 1 . CYS 38 38 4966 1 . ILE 39 39 4966 1 . ASP 40 40 4966 1 . VAL 41 41 4966 1 . CYS 42 42 4966 1 . PRO 43 43 4966 1 . LYS 44 44 4966 1 . SER 45 45 4966 1 . SER 46 46 4966 1 . LEU 47 47 4966 1 . LEU 48 48 4966 1 . VAL 49 49 4966 1 . LYS 50 50 4966 1 . TYR 51 51 4966 1 . VAL 52 52 4966 1 . CYS 53 53 4966 1 . CYS 54 54 4966 1 . ASN 55 55 4966 1 . THR 56 56 4966 1 . ASP 57 57 4966 1 . ARG 58 58 4966 1 . CYS 59 59 4966 1 . ASN 60 60 4966 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 4966 _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.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.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $CTX_A3 . 8656 . . 'cobra naja atra' 'Taiwan cobra' . . Eukaryota Metazoa cobra 'naja atra' . . . . . . . . . venom . . ; Cobra Venom were purchased from Sigma. Further purification by open column and HPLC was proceeded to get pure cardiotoxin A3 compound. ; 4966 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 4966 _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_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.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $CTX_A3 . 'purified from the natural source' . . . . . . . . . . . . . . . 'purified from cobra venom' 4966 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4966 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details '10mM phosphate buffer was added to maintain the pH value at 6.0.' _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 'Cardiotoxin A3' . . . 1 $CTX_A3 . . 5 . . mM . . . . 4966 1 2 'phosphate buffer' . . . . . . . 10 . . mM . . . . 4966 1 stop_ save_ ####################### # Sample conditions # ####################### save_CTX_A3_condition _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode CTX_A3_condition _Sample_condition_list.Entry_ID 4966 _Sample_condition_list.ID 1 _Sample_condition_list.Details ; There is no indication of protein aggregation or degradation as judged by the 1H NMR spectral quailty during the experimental (25C, up to week) and storage time (4C, up to months). The assignments of 13C have been collected from the natural abundance nucleii. ; 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 'ionic strength' 0.03 0.005 M 4966 1 pH 5.96 0.05 n/a 4966 1 pressure 1.013 . atm 4966 1 temperature 300 0.5 K 4966 1 stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 4966 _Software.ID 1 _Software.Type . _Software.Name XWINNMR _Software.Version 2.01 _Software.DOI . _Software.Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_1 _NMR_spectrometer.Entry_ID 4966 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer BRUKER _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_2 _NMR_spectrometer.Entry_ID 4966 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer BRUKER _NMR_spectrometer.Model DMX _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 4966 _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_1 BRUKER DRX . 600 . . . 4966 1 2 NMR_spectrometer_2 BRUKER DMX . 500 . . . 4966 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 4966 _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 COSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4966 1 2 NOESY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4966 1 3 TOCSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4966 1 4 HSQC . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4966 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 4966 _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.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . 4966 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . 4966 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_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 4966 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $CTX_A3_condition _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 ; The chemical Shift of Cardiotoxin A3 at pH 3.0 have been determinted in 1994. But it was later demonstrated that the assignments were based on at least 9 wrongly assigned signals out of the 60 amino acid residues. The correct assignment of all proton resonance were achieved now at pH 6.0 and 27C. ; _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 COSY 1 $sample_1 . 4966 1 2 NOESY 1 $sample_1 . 4966 1 3 TOCSY 1 $sample_1 . 4966 1 4 HSQC 1 $sample_1 . 4966 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.Ambiguity_set_ID _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 4.175 0.01 . 1 . . . . . . . . . 4966 1 2 . 1 1 1 1 LEU HB2 H 1 1.595 0.01 . 1 . . . . . . . . . 4966 1 3 . 1 1 1 1 LEU HB3 H 1 1.536 0.01 . 1 . . . . . . . . . 4966 1 4 . 1 1 1 1 LEU HG H 1 1.580 0.01 . 1 . . . . . . . . . 4966 1 5 . 1 1 1 1 LEU HD11 H 1 0.844 0.01 . 2 . . . . . . . . . 4966 1 6 . 1 1 1 1 LEU HD12 H 1 0.844 0.01 . 2 . . . . . . . . . 4966 1 7 . 1 1 1 1 LEU HD13 H 1 0.844 0.01 . 2 . . . . . . . . . 4966 1 8 . 1 1 1 1 LEU HD21 H 1 0.777 0.01 . 2 . . . . . . . . . 4966 1 9 . 1 1 1 1 LEU HD22 H 1 0.777 0.01 . 2 . . . . . . . . . 4966 1 10 . 1 1 1 1 LEU HD23 H 1 0.777 0.01 . 2 . . . . . . . . . 4966 1 11 . 1 1 1 1 LEU CA C 13 52.260 0.15 . 1 . . . . . . . . . 4966 1 12 . 1 1 2 2 LYS H H 1 8.638 0.01 . 1 . . . . . . . . . 4966 1 13 . 1 1 2 2 LYS HA H 1 5.483 0.01 . 1 . . . . . . . . . 4966 1 14 . 1 1 2 2 LYS HB2 H 1 1.417 0.01 . 1 . . . . . . . . . 4966 1 15 . 1 1 2 2 LYS HB3 H 1 1.417 0.01 . 1 . . . . . . . . . 4966 1 16 . 1 1 2 2 LYS HG2 H 1 1.255 0.01 . 1 . . . . . . . . . 4966 1 17 . 1 1 2 2 LYS HG3 H 1 1.255 0.01 . 1 . . . . . . . . . 4966 1 18 . 1 1 2 2 LYS HE2 H 1 2.864 0.01 . 1 . . . . . . . . . 4966 1 19 . 1 1 2 2 LYS HE3 H 1 2.864 0.01 . 1 . . . . . . . . . 4966 1 20 . 1 1 2 2 LYS CA C 13 51.867 0.15 . 1 . . . . . . . . . 4966 1 21 . 1 1 3 3 CYS H H 1 8.861 0.01 . 1 . . . . . . . . . 4966 1 22 . 1 1 3 3 CYS HA H 1 5.164 0.01 . 1 . . . . . . . . . 4966 1 23 . 1 1 3 3 CYS HB2 H 1 2.867 0.01 . 2 . . . . . . . . . 4966 1 24 . 1 1 3 3 CYS HB3 H 1 2.470 0.01 . 2 . . . . . . . . . 4966 1 25 . 1 1 3 3 CYS CA C 13 49.495 0.15 . 1 . . . . . . . . . 4966 1 26 . 1 1 4 4 ASN H H 1 9.676 0.01 . 1 . . . . . . . . . 4966 1 27 . 1 1 4 4 ASN HA H 1 5.077 0.01 . 1 . . . . . . . . . 4966 1 28 . 1 1 4 4 ASN HB2 H 1 2.771 0.01 . 2 . . . . . . . . . 4966 1 29 . 1 1 4 4 ASN HB3 H 1 2.325 0.01 . 2 . . . . . . . . . 4966 1 30 . 1 1 4 4 ASN HD21 H 1 7.711 0.01 . 2 . . . . . . . . . 4966 1 31 . 1 1 4 4 ASN HD22 H 1 6.557 0.01 . 2 . . . . . . . . . 4966 1 32 . 1 1 4 4 ASN CA C 13 52.225 0.15 . 1 . . . . . . . . . 4966 1 33 . 1 1 5 5 LYS H H 1 8.009 0.01 . 1 . . . . . . . . . 4966 1 34 . 1 1 5 5 LYS HA H 1 4.266 0.01 . 1 . . . . . . . . . 4966 1 35 . 1 1 5 5 LYS HB2 H 1 1.620 0.01 . 1 . . . . . . . . . 4966 1 36 . 1 1 5 5 LYS HB3 H 1 1.620 0.01 . 1 . . . . . . . . . 4966 1 37 . 1 1 5 5 LYS HG2 H 1 1.401 0.01 . 2 . . . . . . . . . 4966 1 38 . 1 1 5 5 LYS HG3 H 1 1.261 0.01 . 2 . . . . . . . . . 4966 1 39 . 1 1 5 5 LYS HD2 H 1 2.206 0.01 . 1 . . . . . . . . . 4966 1 40 . 1 1 5 5 LYS HD3 H 1 2.206 0.01 . 1 . . . . . . . . . 4966 1 41 . 1 1 5 5 LYS HE2 H 1 2.919 0.01 . 1 . . . . . . . . . 4966 1 42 . 1 1 5 5 LYS HE3 H 1 2.919 0.01 . 1 . . . . . . . . . 4966 1 43 . 1 1 5 5 LYS CA C 13 52.828 0.15 . 1 . . . . . . . . . 4966 1 44 . 1 1 6 6 LEU H H 1 8.338 0.01 . 1 . . . . . . . . . 4966 1 45 . 1 1 6 6 LEU HA H 1 3.677 0.01 . 1 . . . . . . . . . 4966 1 46 . 1 1 6 6 LEU HB2 H 1 1.672 0.01 . 2 . . . . . . . . . 4966 1 47 . 1 1 6 6 LEU HB3 H 1 1.597 0.01 . 2 . . . . . . . . . 4966 1 48 . 1 1 6 6 LEU HG H 1 1.828 0.01 . 1 . . . . . . . . . 4966 1 49 . 1 1 6 6 LEU HD11 H 1 0.876 0.01 . 1 . . . . . . . . . 4966 1 50 . 1 1 6 6 LEU HD12 H 1 0.876 0.01 . 1 . . . . . . . . . 4966 1 51 . 1 1 6 6 LEU HD13 H 1 0.876 0.01 . 1 . . . . . . . . . 4966 1 52 . 1 1 6 6 LEU HD21 H 1 0.720 0.01 . 1 . . . . . . . . . 4966 1 53 . 1 1 6 6 LEU HD22 H 1 0.720 0.01 . 1 . . . . . . . . . 4966 1 54 . 1 1 6 6 LEU HD23 H 1 0.720 0.01 . 1 . . . . . . . . . 4966 1 55 . 1 1 6 6 LEU CA C 13 56.869 0.15 . 1 . . . . . . . . . 4966 1 56 . 1 1 7 7 VAL H H 1 7.654 0.01 . 1 . . . . . . . . . 4966 1 57 . 1 1 7 7 VAL HA H 1 4.422 0.01 . 1 . . . . . . . . . 4966 1 58 . 1 1 7 7 VAL HB H 1 2.276 0.01 . 1 . . . . . . . . . 4966 1 59 . 1 1 7 7 VAL HG11 H 1 1.053 0.01 . 1 . . . . . . . . . 4966 1 60 . 1 1 7 7 VAL HG12 H 1 1.053 0.01 . 1 . . . . . . . . . 4966 1 61 . 1 1 7 7 VAL HG13 H 1 1.053 0.01 . 1 . . . . . . . . . 4966 1 62 . 1 1 7 7 VAL HG21 H 1 1.053 0.01 . 1 . . . . . . . . . 4966 1 63 . 1 1 7 7 VAL HG22 H 1 1.053 0.01 . 1 . . . . . . . . . 4966 1 64 . 1 1 7 7 VAL HG23 H 1 1.053 0.01 . 1 . . . . . . . . . 4966 1 65 . 1 1 7 7 VAL CA C 13 57.482 0.15 . 1 . . . . . . . . . 4966 1 66 . 1 1 8 8 PRO HA H 1 4.544 0.01 . 1 . . . . . . . . . 4966 1 67 . 1 1 8 8 PRO HB2 H 1 2.173 0.01 . 2 . . . . . . . . . 4966 1 68 . 1 1 8 8 PRO HB3 H 1 1.984 0.01 . 2 . . . . . . . . . 4966 1 69 . 1 1 8 8 PRO HG2 H 1 1.842 0.01 . 1 . . . . . . . . . 4966 1 70 . 1 1 8 8 PRO HG3 H 1 1.842 0.01 . 1 . . . . . . . . . 4966 1 71 . 1 1 8 8 PRO HD2 H 1 4.052 0.01 . 2 . . . . . . . . . 4966 1 72 . 1 1 8 8 PRO HD3 H 1 3.845 0.01 . 2 . . . . . . . . . 4966 1 73 . 1 1 8 8 PRO CA C 13 63.358 0.15 . 1 . . . . . . . . . 4966 1 74 . 1 1 9 9 LEU H H 1 6.625 0.01 . 1 . . . . . . . . . 4966 1 75 . 1 1 9 9 LEU HA H 1 3.959 0.01 . 1 . . . . . . . . . 4966 1 76 . 1 1 9 9 LEU HB2 H 1 1.033 0.01 . 1 . . . . . . . . . 4966 1 77 . 1 1 9 9 LEU HB3 H 1 1.033 0.01 . 1 . . . . . . . . . 4966 1 78 . 1 1 9 9 LEU HG H 1 1.333 0.01 . 1 . . . . . . . . . 4966 1 79 . 1 1 9 9 LEU HD11 H 1 0.757 0.01 . 2 . . . . . . . . . 4966 1 80 . 1 1 9 9 LEU HD12 H 1 0.757 0.01 . 2 . . . . . . . . . 4966 1 81 . 1 1 9 9 LEU HD13 H 1 0.757 0.01 . 2 . . . . . . . . . 4966 1 82 . 1 1 9 9 LEU HD21 H 1 0.719 0.01 . 2 . . . . . . . . . 4966 1 83 . 1 1 9 9 LEU HD22 H 1 0.719 0.01 . 2 . . . . . . . . . 4966 1 84 . 1 1 9 9 LEU HD23 H 1 0.719 0.01 . 2 . . . . . . . . . 4966 1 85 . 1 1 9 9 LEU CA C 13 54.089 0.15 . 1 . . . . . . . . . 4966 1 86 . 1 1 10 10 PHE H H 1 8.139 0.01 . 1 . . . . . . . . . 4966 1 87 . 1 1 10 10 PHE HA H 1 4.858 0.01 . 1 . . . . . . . . . 4966 1 88 . 1 1 10 10 PHE HB2 H 1 3.228 0.01 . 2 . . . . . . . . . 4966 1 89 . 1 1 10 10 PHE HB3 H 1 2.858 0.01 . 2 . . . . . . . . . 4966 1 90 . 1 1 10 10 PHE HD1 H 1 7.289 0.01 . 1 . . . . . . . . . 4966 1 91 . 1 1 10 10 PHE HD2 H 1 7.289 0.01 . 1 . . . . . . . . . 4966 1 92 . 1 1 10 10 PHE HE1 H 1 7.352 0.01 . 1 . . . . . . . . . 4966 1 93 . 1 1 10 10 PHE HE2 H 1 7.352 0.01 . 1 . . . . . . . . . 4966 1 94 . 1 1 10 10 PHE HZ H 1 7.324 0.01 . 1 . . . . . . . . . 4966 1 95 . 1 1 10 10 PHE CA C 13 53.465 0.15 . 1 . . . . . . . . . 4966 1 96 . 1 1 11 11 TYR H H 1 8.206 0.01 . 1 . . . . . . . . . 4966 1 97 . 1 1 11 11 TYR HA H 1 5.443 0.01 . 1 . . . . . . . . . 4966 1 98 . 1 1 11 11 TYR HB2 H 1 2.928 0.01 . 2 . . . . . . . . . 4966 1 99 . 1 1 11 11 TYR HB3 H 1 2.686 0.01 . 2 . . . . . . . . . 4966 1 100 . 1 1 11 11 TYR HD1 H 1 6.750 0.01 . 1 . . . . . . . . . 4966 1 101 . 1 1 11 11 TYR HD2 H 1 6.750 0.01 . 1 . . . . . . . . . 4966 1 102 . 1 1 11 11 TYR HE1 H 1 6.806 0.01 . 1 . . . . . . . . . 4966 1 103 . 1 1 11 11 TYR HE2 H 1 6.806 0.01 . 1 . . . . . . . . . 4966 1 104 . 1 1 11 11 TYR CA C 13 53.309 0.15 . 1 . . . . . . . . . 4966 1 105 . 1 1 12 12 LYS H H 1 9.085 0.01 . 1 . . . . . . . . . 4966 1 106 . 1 1 12 12 LYS HA H 1 4.829 0.01 . 1 . . . . . . . . . 4966 1 107 . 1 1 12 12 LYS HB2 H 1 1.707 0.01 . 1 . . . . . . . . . 4966 1 108 . 1 1 12 12 LYS HB3 H 1 1.707 0.01 . 1 . . . . . . . . . 4966 1 109 . 1 1 12 12 LYS HG2 H 1 1.384 0.01 . 2 . . . . . . . . . 4966 1 110 . 1 1 12 12 LYS HG3 H 1 1.196 0.01 . 2 . . . . . . . . . 4966 1 111 . 1 1 12 12 LYS HD2 H 1 1.859 0.01 . 1 . . . . . . . . . 4966 1 112 . 1 1 12 12 LYS HD3 H 1 1.859 0.01 . 1 . . . . . . . . . 4966 1 113 . 1 1 12 12 LYS CA C 13 51.549 0.15 . 1 . . . . . . . . . 4966 1 114 . 1 1 13 13 THR H H 1 8.869 0.01 . 1 . . . . . . . . . 4966 1 115 . 1 1 13 13 THR HA H 1 4.712 0.01 . 1 . . . . . . . . . 4966 1 116 . 1 1 13 13 THR HB H 1 4.072 0.01 . 1 . . . . . . . . . 4966 1 117 . 1 1 13 13 THR HG21 H 1 1.277 0.01 . 1 . . . . . . . . . 4966 1 118 . 1 1 13 13 THR HG22 H 1 1.277 0.01 . 1 . . . . . . . . . 4966 1 119 . 1 1 13 13 THR HG23 H 1 1.277 0.01 . 1 . . . . . . . . . 4966 1 120 . 1 1 13 13 THR CA C 13 60.720 0.15 . 1 . . . . . . . . . 4966 1 121 . 1 1 14 14 CYS H H 1 9.179 0.01 . 1 . . . . . . . . . 4966 1 122 . 1 1 14 14 CYS HA H 1 4.995 0.01 . 1 . . . . . . . . . 4966 1 123 . 1 1 14 14 CYS HB2 H 1 3.549 0.01 . 2 . . . . . . . . . 4966 1 124 . 1 1 14 14 CYS HB3 H 1 2.835 0.01 . 2 . . . . . . . . . 4966 1 125 . 1 1 14 14 CYS CA C 13 49.552 0.15 . 1 . . . . . . . . . 4966 1 126 . 1 1 15 15 PRO HA H 1 4.635 0.01 . 1 . . . . . . . . . 4966 1 127 . 1 1 15 15 PRO HB2 H 1 2.419 0.01 . 2 . . . . . . . . . 4966 1 128 . 1 1 15 15 PRO HB3 H 1 2.194 0.01 . 2 . . . . . . . . . 4966 1 129 . 1 1 15 15 PRO HG2 H 1 1.982 0.01 . 2 . . . . . . . . . 4966 1 130 . 1 1 15 15 PRO HG3 H 1 1.903 0.01 . 2 . . . . . . . . . 4966 1 131 . 1 1 15 15 PRO HD2 H 1 3.458 0.01 . 2 . . . . . . . . . 4966 1 132 . 1 1 15 15 PRO HD3 H 1 4.106 0.01 . 2 . . . . . . . . . 4966 1 133 . 1 1 15 15 PRO CA C 13 59.919 0.15 . 1 . . . . . . . . . 4966 1 134 . 1 1 16 16 ALA H H 1 8.473 0.01 . 1 . . . . . . . . . 4966 1 135 . 1 1 16 16 ALA HA H 1 4.121 0.01 . 1 . . . . . . . . . 4966 1 136 . 1 1 16 16 ALA HB1 H 1 1.380 0.01 . 1 . . . . . . . . . 4966 1 137 . 1 1 16 16 ALA HB2 H 1 1.380 0.01 . 1 . . . . . . . . . 4966 1 138 . 1 1 16 16 ALA HB3 H 1 1.380 0.01 . 1 . . . . . . . . . 4966 1 139 . 1 1 16 16 ALA CA C 13 51.467 0.15 . 1 . . . . . . . . . 4966 1 140 . 1 1 17 17 GLY H H 1 8.799 0.01 . 1 . . . . . . . . . 4966 1 141 . 1 1 17 17 GLY HA2 H 1 4.272 0.01 . 2 . . . . . . . . . 4966 1 142 . 1 1 17 17 GLY HA3 H 1 3.675 0.01 . 2 . . . . . . . . . 4966 1 143 . 1 1 17 17 GLY CA C 13 42.586 0.15 . 1 . . . . . . . . . 4966 1 144 . 1 1 18 18 LYS H H 1 7.589 0.01 . 1 . . . . . . . . . 4966 1 145 . 1 1 18 18 LYS HA H 1 4.288 0.01 . 1 . . . . . . . . . 4966 1 146 . 1 1 18 18 LYS HB2 H 1 1.381 0.01 . 1 . . . . . . . . . 4966 1 147 . 1 1 18 18 LYS HB3 H 1 1.381 0.01 . 1 . . . . . . . . . 4966 1 148 . 1 1 18 18 LYS HG2 H 1 1.060 0.01 . 1 . . . . . . . . . 4966 1 149 . 1 1 18 18 LYS HG3 H 1 1.060 0.01 . 1 . . . . . . . . . 4966 1 150 . 1 1 18 18 LYS HD2 H 1 1.919 0.01 . 1 . . . . . . . . . 4966 1 151 . 1 1 18 18 LYS HD3 H 1 1.919 0.01 . 1 . . . . . . . . . 4966 1 152 . 1 1 18 18 LYS HE2 H 1 2.958 0.01 . 1 . . . . . . . . . 4966 1 153 . 1 1 18 18 LYS HE3 H 1 2.958 0.01 . 1 . . . . . . . . . 4966 1 154 . 1 1 18 18 LYS CA C 13 53.416 0.15 . 1 . . . . . . . . . 4966 1 155 . 1 1 19 19 ASN H H 1 7.946 0.01 . 1 . . . . . . . . . 4966 1 156 . 1 1 19 19 ASN HA H 1 4.958 0.01 . 1 . . . . . . . . . 4966 1 157 . 1 1 19 19 ASN HB2 H 1 3.029 0.01 . 2 . . . . . . . . . 4966 1 158 . 1 1 19 19 ASN HB3 H 1 2.647 0.01 . 2 . . . . . . . . . 4966 1 159 . 1 1 19 19 ASN HD21 H 1 7.522 0.01 . 2 . . . . . . . . . 4966 1 160 . 1 1 19 19 ASN HD22 H 1 6.986 0.01 . 2 . . . . . . . . . 4966 1 161 . 1 1 19 19 ASN CA C 13 50.709 0.15 . 1 . . . . . . . . . 4966 1 162 . 1 1 20 20 LEU H H 1 8.225 0.01 . 1 . . . . . . . . . 4966 1 163 . 1 1 20 20 LEU HA H 1 4.852 0.01 . 1 . . . . . . . . . 4966 1 164 . 1 1 20 20 LEU HB2 H 1 1.712 0.01 . 2 . . . . . . . . . 4966 1 165 . 1 1 20 20 LEU HB3 H 1 1.527 0.01 . 2 . . . . . . . . . 4966 1 166 . 1 1 20 20 LEU HG H 1 1.378 0.01 . 1 . . . . . . . . . 4966 1 167 . 1 1 20 20 LEU HD11 H 1 0.880 0.01 . 2 . . . . . . . . . 4966 1 168 . 1 1 20 20 LEU HD12 H 1 0.880 0.01 . 2 . . . . . . . . . 4966 1 169 . 1 1 20 20 LEU HD13 H 1 0.880 0.01 . 2 . . . . . . . . . 4966 1 170 . 1 1 20 20 LEU HD21 H 1 0.736 0.01 . 2 . . . . . . . . . 4966 1 171 . 1 1 20 20 LEU HD22 H 1 0.736 0.01 . 2 . . . . . . . . . 4966 1 172 . 1 1 20 20 LEU HD23 H 1 0.736 0.01 . 2 . . . . . . . . . 4966 1 173 . 1 1 21 21 CYS H H 1 9.050 0.01 . 1 . . . . . . . . . 4966 1 174 . 1 1 21 21 CYS HA H 1 6.133 0.01 . 1 . . . . . . . . . 4966 1 175 . 1 1 21 21 CYS HB2 H 1 3.054 0.01 . 2 . . . . . . . . . 4966 1 176 . 1 1 21 21 CYS HB3 H 1 2.982 0.01 . 2 . . . . . . . . . 4966 1 177 . 1 1 21 21 CYS CA C 13 49.516 0.15 . 1 . . . . . . . . . 4966 1 178 . 1 1 22 22 TYR H H 1 8.960 0.01 . 1 . . . . . . . . . 4966 1 179 . 1 1 22 22 TYR HA H 1 6.099 0.01 . 1 . . . . . . . . . 4966 1 180 . 1 1 22 22 TYR HB2 H 1 3.114 0.01 . 2 . . . . . . . . . 4966 1 181 . 1 1 22 22 TYR HB3 H 1 2.947 0.01 . 2 . . . . . . . . . 4966 1 182 . 1 1 22 22 TYR HD1 H 1 6.624 0.01 . 1 . . . . . . . . . 4966 1 183 . 1 1 22 22 TYR HD2 H 1 6.624 0.01 . 1 . . . . . . . . . 4966 1 184 . 1 1 22 22 TYR HE1 H 1 6.733 0.01 . 1 . . . . . . . . . 4966 1 185 . 1 1 22 22 TYR HE2 H 1 6.733 0.01 . 1 . . . . . . . . . 4966 1 186 . 1 1 22 22 TYR CA C 13 53.829 0.15 . 1 . . . . . . . . . 4966 1 187 . 1 1 23 23 LYS H H 1 9.080 0.01 . 1 . . . . . . . . . 4966 1 188 . 1 1 23 23 LYS HA H 1 4.948 0.01 . 1 . . . . . . . . . 4966 1 189 . 1 1 23 23 LYS HB2 H 1 1.710 0.01 . 1 . . . . . . . . . 4966 1 190 . 1 1 23 23 LYS HB3 H 1 1.710 0.01 . 1 . . . . . . . . . 4966 1 191 . 1 1 23 23 LYS HG2 H 1 1.512 0.01 . 1 . . . . . . . . . 4966 1 192 . 1 1 23 23 LYS HG3 H 1 1.512 0.01 . 1 . . . . . . . . . 4966 1 193 . 1 1 23 23 LYS HD2 H 1 1.854 0.01 . 1 . . . . . . . . . 4966 1 194 . 1 1 23 23 LYS HD3 H 1 1.854 0.01 . 1 . . . . . . . . . 4966 1 195 . 1 1 23 23 LYS CA C 13 52.981 0.15 . 1 . . . . . . . . . 4966 1 196 . 1 1 24 24 MET H H 1 8.460 0.01 . 1 . . . . . . . . . 4966 1 197 . 1 1 24 24 MET HA H 1 5.229 0.01 . 1 . . . . . . . . . 4966 1 198 . 1 1 24 24 MET HB2 H 1 1.798 0.01 . 2 . . . . . . . . . 4966 1 199 . 1 1 24 24 MET HB3 H 1 1.621 0.01 . 2 . . . . . . . . . 4966 1 200 . 1 1 24 24 MET HG2 H 1 1.346 0.01 . 1 . . . . . . . . . 4966 1 201 . 1 1 24 24 MET HG3 H 1 1.346 0.01 . 1 . . . . . . . . . 4966 1 202 . 1 1 24 24 MET CA C 13 51.324 0.15 . 1 . . . . . . . . . 4966 1 203 . 1 1 25 25 PHE H H 1 9.095 0.01 . 1 . . . . . . . . . 4966 1 204 . 1 1 25 25 PHE HA H 1 4.943 0.01 . 1 . . . . . . . . . 4966 1 205 . 1 1 25 25 PHE HB2 H 1 2.902 0.01 . 1 . . . . . . . . . 4966 1 206 . 1 1 25 25 PHE HB3 H 1 2.902 0.01 . 1 . . . . . . . . . 4966 1 207 . 1 1 25 25 PHE HD1 H 1 6.907 0.01 . 1 . . . . . . . . . 4966 1 208 . 1 1 25 25 PHE HD2 H 1 6.907 0.01 . 1 . . . . . . . . . 4966 1 209 . 1 1 25 25 PHE HE1 H 1 7.108 0.01 . 1 . . . . . . . . . 4966 1 210 . 1 1 25 25 PHE HE2 H 1 7.108 0.01 . 1 . . . . . . . . . 4966 1 211 . 1 1 25 25 PHE HZ H 1 7.236 0.01 . 1 . . . . . . . . . 4966 1 212 . 1 1 25 25 PHE CA C 13 53.575 0.15 . 1 . . . . . . . . . 4966 1 213 . 1 1 26 26 MET H H 1 9.432 0.01 . 1 . . . . . . . . . 4966 1 214 . 1 1 26 26 MET HA H 1 5.106 0.01 . 1 . . . . . . . . . 4966 1 215 . 1 1 26 26 MET HB2 H 1 2.273 0.01 . 2 . . . . . . . . . 4966 1 216 . 1 1 26 26 MET HB3 H 1 2.134 0.01 . 2 . . . . . . . . . 4966 1 217 . 1 1 26 26 MET HG2 H 1 2.838 0.01 . 2 . . . . . . . . . 4966 1 218 . 1 1 26 26 MET HG3 H 1 2.624 0.01 . 2 . . . . . . . . . 4966 1 219 . 1 1 26 26 MET CA C 13 51.379 0.15 . 1 . . . . . . . . . 4966 1 220 . 1 1 27 27 VAL H H 1 8.149 0.01 . 1 . . . . . . . . . 4966 1 221 . 1 1 27 27 VAL HA H 1 3.546 0.01 . 1 . . . . . . . . . 4966 1 222 . 1 1 27 27 VAL HB H 1 1.942 0.01 . 1 . . . . . . . . . 4966 1 223 . 1 1 27 27 VAL HG11 H 1 0.981 0.01 . 2 . . . . . . . . . 4966 1 224 . 1 1 27 27 VAL HG12 H 1 0.981 0.01 . 2 . . . . . . . . . 4966 1 225 . 1 1 27 27 VAL HG13 H 1 0.981 0.01 . 2 . . . . . . . . . 4966 1 226 . 1 1 27 27 VAL HG21 H 1 0.903 0.01 . 2 . . . . . . . . . 4966 1 227 . 1 1 27 27 VAL HG22 H 1 0.903 0.01 . 2 . . . . . . . . . 4966 1 228 . 1 1 27 27 VAL HG23 H 1 0.903 0.01 . 2 . . . . . . . . . 4966 1 229 . 1 1 27 27 VAL CA C 13 63.763 0.15 . 1 . . . . . . . . . 4966 1 230 . 1 1 28 28 ALA H H 1 8.470 0.01 . 1 . . . . . . . . . 4966 1 231 . 1 1 28 28 ALA HA H 1 4.238 0.01 . 1 . . . . . . . . . 4966 1 232 . 1 1 28 28 ALA HB1 H 1 1.491 0.01 . 1 . . . . . . . . . 4966 1 233 . 1 1 28 28 ALA HB2 H 1 1.491 0.01 . 1 . . . . . . . . . 4966 1 234 . 1 1 28 28 ALA HB3 H 1 1.491 0.01 . 1 . . . . . . . . . 4966 1 235 . 1 1 28 28 ALA CA C 13 51.723 0.15 . 1 . . . . . . . . . 4966 1 236 . 1 1 29 29 THR H H 1 7.425 0.01 . 1 . . . . . . . . . 4966 1 237 . 1 1 29 29 THR HA H 1 4.824 0.01 . 1 . . . . . . . . . 4966 1 238 . 1 1 29 29 THR HB H 1 4.310 0.01 . 1 . . . . . . . . . 4966 1 239 . 1 1 29 29 THR HG21 H 1 1.199 0.01 . 1 . . . . . . . . . 4966 1 240 . 1 1 29 29 THR HG22 H 1 1.199 0.01 . 1 . . . . . . . . . 4966 1 241 . 1 1 29 29 THR HG23 H 1 1.199 0.01 . 1 . . . . . . . . . 4966 1 242 . 1 1 29 29 THR CA C 13 55.557 0.15 . 1 . . . . . . . . . 4966 1 243 . 1 1 30 30 PRO HA H 1 4.278 0.01 . 1 . . . . . . . . . 4966 1 244 . 1 1 30 30 PRO HB2 H 1 2.043 0.01 . 1 . . . . . . . . . 4966 1 245 . 1 1 30 30 PRO HB3 H 1 2.043 0.01 . 1 . . . . . . . . . 4966 1 246 . 1 1 30 30 PRO HG2 H 1 1.748 0.01 . 1 . . . . . . . . . 4966 1 247 . 1 1 30 30 PRO HG3 H 1 1.748 0.01 . 1 . . . . . . . . . 4966 1 248 . 1 1 30 30 PRO HD2 H 1 3.580 0.01 . 1 . . . . . . . . . 4966 1 249 . 1 1 30 30 PRO HD3 H 1 3.580 0.01 . 1 . . . . . . . . . 4966 1 250 . 1 1 30 30 PRO CA C 13 62.313 0.15 . 1 . . . . . . . . . 4966 1 251 . 1 1 31 31 LYS H H 1 8.306 0.01 . 1 . . . . . . . . . 4966 1 252 . 1 1 31 31 LYS HA H 1 4.110 0.01 . 1 . . . . . . . . . 4966 1 253 . 1 1 31 31 LYS HB2 H 1 1.960 0.01 . 2 . . . . . . . . . 4966 1 254 . 1 1 31 31 LYS HB3 H 1 1.823 0.01 . 2 . . . . . . . . . 4966 1 255 . 1 1 31 31 LYS HG2 H 1 1.638 0.01 . 1 . . . . . . . . . 4966 1 256 . 1 1 31 31 LYS HG3 H 1 1.638 0.01 . 1 . . . . . . . . . 4966 1 257 . 1 1 31 31 LYS HD2 H 1 1.429 0.01 . 2 . . . . . . . . . 4966 1 258 . 1 1 31 31 LYS HD3 H 1 1.335 0.01 . 2 . . . . . . . . . 4966 1 259 . 1 1 31 31 LYS CA C 13 55.167 0.15 . 1 . . . . . . . . . 4966 1 260 . 1 1 32 32 VAL H H 1 7.565 0.01 . 1 . . . . . . . . . 4966 1 261 . 1 1 32 32 VAL HA H 1 4.638 0.01 . 1 . . . . . . . . . 4966 1 262 . 1 1 32 32 VAL HB H 1 2.162 0.01 . 1 . . . . . . . . . 4966 1 263 . 1 1 32 32 VAL HG11 H 1 0.978 0.01 . 2 . . . . . . . . . 4966 1 264 . 1 1 32 32 VAL HG12 H 1 0.978 0.01 . 2 . . . . . . . . . 4966 1 265 . 1 1 32 32 VAL HG13 H 1 0.978 0.01 . 2 . . . . . . . . . 4966 1 266 . 1 1 32 32 VAL HG21 H 1 0.920 0.01 . 2 . . . . . . . . . 4966 1 267 . 1 1 32 32 VAL HG22 H 1 0.920 0.01 . 2 . . . . . . . . . 4966 1 268 . 1 1 32 32 VAL HG23 H 1 0.920 0.01 . 2 . . . . . . . . . 4966 1 269 . 1 1 32 32 VAL CA C 13 56.863 0.15 . 1 . . . . . . . . . 4966 1 270 . 1 1 33 33 PRO HA H 1 4.331 0.01 . 1 . . . . . . . . . 4966 1 271 . 1 1 33 33 PRO HB2 H 1 2.037 0.01 . 2 . . . . . . . . . 4966 1 272 . 1 1 33 33 PRO HB3 H 1 1.795 0.01 . 2 . . . . . . . . . 4966 1 273 . 1 1 33 33 PRO HG2 H 1 1.673 0.01 . 1 . . . . . . . . . 4966 1 274 . 1 1 33 33 PRO HG3 H 1 1.673 0.01 . 1 . . . . . . . . . 4966 1 275 . 1 1 33 33 PRO HD2 H 1 3.934 0.01 . 2 . . . . . . . . . 4966 1 276 . 1 1 33 33 PRO HD3 H 1 3.836 0.01 . 2 . . . . . . . . . 4966 1 277 . 1 1 33 33 PRO CA C 13 60.743 0.15 . 1 . . . . . . . . . 4966 1 278 . 1 1 34 34 VAL H H 1 8.868 0.01 . 1 . . . . . . . . . 4966 1 279 . 1 1 34 34 VAL HA H 1 4.309 0.01 . 1 . . . . . . . . . 4966 1 280 . 1 1 34 34 VAL HB H 1 2.139 0.01 . 1 . . . . . . . . . 4966 1 281 . 1 1 34 34 VAL HG11 H 1 1.050 0.01 . 2 . . . . . . . . . 4966 1 282 . 1 1 34 34 VAL HG12 H 1 1.050 0.01 . 2 . . . . . . . . . 4966 1 283 . 1 1 34 34 VAL HG13 H 1 1.050 0.01 . 2 . . . . . . . . . 4966 1 284 . 1 1 34 34 VAL HG21 H 1 0.961 0.01 . 2 . . . . . . . . . 4966 1 285 . 1 1 34 34 VAL HG22 H 1 0.961 0.01 . 2 . . . . . . . . . 4966 1 286 . 1 1 34 34 VAL HG23 H 1 0.961 0.01 . 2 . . . . . . . . . 4966 1 287 . 1 1 34 34 VAL CA C 13 59.892 0.15 . 1 . . . . . . . . . 4966 1 288 . 1 1 35 35 LYS H H 1 7.389 0.01 . 1 . . . . . . . . . 4966 1 289 . 1 1 35 35 LYS HA H 1 4.629 0.01 . 1 . . . . . . . . . 4966 1 290 . 1 1 35 35 LYS HB2 H 1 1.716 0.01 . 2 . . . . . . . . . 4966 1 291 . 1 1 35 35 LYS HB3 H 1 1.578 0.01 . 2 . . . . . . . . . 4966 1 292 . 1 1 35 35 LYS HG2 H 1 1.853 0.01 . 1 . . . . . . . . . 4966 1 293 . 1 1 35 35 LYS HG3 H 1 1.853 0.01 . 1 . . . . . . . . . 4966 1 294 . 1 1 35 35 LYS HD2 H 1 2.048 0.01 . 1 . . . . . . . . . 4966 1 295 . 1 1 35 35 LYS HD3 H 1 2.048 0.01 . 1 . . . . . . . . . 4966 1 296 . 1 1 35 35 LYS HE2 H 1 3.090 0.01 . 1 . . . . . . . . . 4966 1 297 . 1 1 35 35 LYS HE3 H 1 3.090 0.01 . 1 . . . . . . . . . 4966 1 298 . 1 1 35 35 LYS CA C 13 53.902 0.15 . 1 . . . . . . . . . 4966 1 299 . 1 1 36 36 ARG H H 1 8.364 0.01 . 1 . . . . . . . . . 4966 1 300 . 1 1 36 36 ARG HA H 1 4.423 0.01 . 1 . . . . . . . . . 4966 1 301 . 1 1 36 36 ARG HB2 H 1 1.625 0.01 . 2 . . . . . . . . . 4966 1 302 . 1 1 36 36 ARG HB3 H 1 1.511 0.01 . 2 . . . . . . . . . 4966 1 303 . 1 1 36 36 ARG HG2 H 1 1.054 0.01 . 1 . . . . . . . . . 4966 1 304 . 1 1 36 36 ARG HG3 H 1 1.054 0.01 . 1 . . . . . . . . . 4966 1 305 . 1 1 36 36 ARG HD2 H 1 3.142 0.01 . 2 . . . . . . . . . 4966 1 306 . 1 1 36 36 ARG HD3 H 1 2.884 0.01 . 2 . . . . . . . . . 4966 1 307 . 1 1 36 36 ARG HE H 1 8.416 0.01 . 1 . . . . . . . . . 4966 1 308 . 1 1 36 36 ARG CA C 13 53.410 0.15 . 1 . . . . . . . . . 4966 1 309 . 1 1 37 37 GLY H H 1 6.466 0.01 . 1 . . . . . . . . . 4966 1 310 . 1 1 37 37 GLY HA2 H 1 4.364 0.01 . 2 . . . . . . . . . 4966 1 311 . 1 1 37 37 GLY HA3 H 1 3.808 0.01 . 2 . . . . . . . . . 4966 1 312 . 1 1 37 37 GLY CA C 13 44.044 0.15 . 1 . . . . . . . . . 4966 1 313 . 1 1 38 38 CYS H H 1 9.260 0.01 . 1 . . . . . . . . . 4966 1 314 . 1 1 38 38 CYS HA H 1 5.987 0.01 . 1 . . . . . . . . . 4966 1 315 . 1 1 38 38 CYS HB2 H 1 3.578 0.01 . 2 . . . . . . . . . 4966 1 316 . 1 1 38 38 CYS HB3 H 1 2.910 0.01 . 2 . . . . . . . . . 4966 1 317 . 1 1 38 38 CYS CA C 13 53.763 0.15 . 1 . . . . . . . . . 4966 1 318 . 1 1 39 39 ILE H H 1 9.937 0.01 . 1 . . . . . . . . . 4966 1 319 . 1 1 39 39 ILE HA H 1 4.458 0.01 . 1 . . . . . . . . . 4966 1 320 . 1 1 39 39 ILE HB H 1 1.734 0.01 . 1 . . . . . . . . . 4966 1 321 . 1 1 39 39 ILE HG12 H 1 1.371 0.01 . 1 . . . . . . . . . 4966 1 322 . 1 1 39 39 ILE HG13 H 1 1.371 0.01 . 1 . . . . . . . . . 4966 1 323 . 1 1 39 39 ILE HG21 H 1 0.580 0.01 . 1 . . . . . . . . . 4966 1 324 . 1 1 39 39 ILE HG22 H 1 0.580 0.01 . 1 . . . . . . . . . 4966 1 325 . 1 1 39 39 ILE HG23 H 1 0.580 0.01 . 1 . . . . . . . . . 4966 1 326 . 1 1 39 39 ILE HD11 H 1 0.451 0.01 . 1 . . . . . . . . . 4966 1 327 . 1 1 39 39 ILE HD12 H 1 0.451 0.01 . 1 . . . . . . . . . 4966 1 328 . 1 1 39 39 ILE HD13 H 1 0.451 0.01 . 1 . . . . . . . . . 4966 1 329 . 1 1 39 39 ILE CA C 13 53.763 0.15 . 1 . . . . . . . . . 4966 1 330 . 1 1 40 40 ASP H H 1 8.744 0.01 . 1 . . . . . . . . . 4966 1 331 . 1 1 40 40 ASP HA H 1 4.897 0.01 . 1 . . . . . . . . . 4966 1 332 . 1 1 40 40 ASP HB2 H 1 2.793 0.01 . 1 . . . . . . . . . 4966 1 333 . 1 1 40 40 ASP HB3 H 1 2.793 0.01 . 1 . . . . . . . . . 4966 1 334 . 1 1 40 40 ASP CA C 13 52.253 0.15 . 1 . . . . . . . . . 4966 1 335 . 1 1 41 41 VAL H H 1 7.737 0.01 . 1 . . . . . . . . . 4966 1 336 . 1 1 41 41 VAL HA H 1 4.018 0.01 . 1 . . . . . . . . . 4966 1 337 . 1 1 41 41 VAL HB H 1 1.732 0.01 . 1 . . . . . . . . . 4966 1 338 . 1 1 41 41 VAL HG11 H 1 0.765 0.01 . 1 . . . . . . . . . 4966 1 339 . 1 1 41 41 VAL HG12 H 1 0.765 0.01 . 1 . . . . . . . . . 4966 1 340 . 1 1 41 41 VAL HG13 H 1 0.765 0.01 . 1 . . . . . . . . . 4966 1 341 . 1 1 41 41 VAL HG21 H 1 0.765 0.01 . 1 . . . . . . . . . 4966 1 342 . 1 1 41 41 VAL HG22 H 1 0.765 0.01 . 1 . . . . . . . . . 4966 1 343 . 1 1 41 41 VAL HG23 H 1 0.765 0.01 . 1 . . . . . . . . . 4966 1 344 . 1 1 41 41 VAL CA C 13 58.018 0.15 . 1 . . . . . . . . . 4966 1 345 . 1 1 42 42 CYS H H 1 8.912 0.01 . 1 . . . . . . . . . 4966 1 346 . 1 1 42 42 CYS HA H 1 4.466 0.01 . 1 . . . . . . . . . 4966 1 347 . 1 1 42 42 CYS HB2 H 1 3.090 0.01 . 2 . . . . . . . . . 4966 1 348 . 1 1 42 42 CYS HB3 H 1 2.764 0.01 . 2 . . . . . . . . . 4966 1 349 . 1 1 42 42 CYS CA C 13 52.513 0.15 . 1 . . . . . . . . . 4966 1 350 . 1 1 43 43 PRO HA H 1 4.059 0.01 . 1 . . . . . . . . . 4966 1 351 . 1 1 43 43 PRO HB2 H 1 1.751 0.01 . 2 . . . . . . . . . 4966 1 352 . 1 1 43 43 PRO HB3 H 1 0.370 0.01 . 2 . . . . . . . . . 4966 1 353 . 1 1 43 43 PRO HG2 H 1 1.247 0.01 . 2 . . . . . . . . . 4966 1 354 . 1 1 43 43 PRO HG3 H 1 0.561 0.01 . 2 . . . . . . . . . 4966 1 355 . 1 1 43 43 PRO HD2 H 1 3.931 0.01 . 2 . . . . . . . . . 4966 1 356 . 1 1 43 43 PRO HD3 H 1 2.493 0.01 . 2 . . . . . . . . . 4966 1 357 . 1 1 43 43 PRO CA C 13 59.698 0.15 . 1 . . . . . . . . . 4966 1 358 . 1 1 44 44 LYS H H 1 8.029 0.01 . 1 . . . . . . . . . 4966 1 359 . 1 1 44 44 LYS HA H 1 4.201 0.01 . 1 . . . . . . . . . 4966 1 360 . 1 1 44 44 LYS HB2 H 1 1.727 0.01 . 1 . . . . . . . . . 4966 1 361 . 1 1 44 44 LYS HB3 H 1 1.727 0.01 . 1 . . . . . . . . . 4966 1 362 . 1 1 44 44 LYS HG2 H 1 1.565 0.01 . 1 . . . . . . . . . 4966 1 363 . 1 1 44 44 LYS HG3 H 1 1.565 0.01 . 1 . . . . . . . . . 4966 1 364 . 1 1 44 44 LYS HD2 H 1 1.834 0.01 . 1 . . . . . . . . . 4966 1 365 . 1 1 44 44 LYS HD3 H 1 1.834 0.01 . 1 . . . . . . . . . 4966 1 366 . 1 1 44 44 LYS HE2 H 1 3.042 0.01 . 1 . . . . . . . . . 4966 1 367 . 1 1 44 44 LYS HE3 H 1 3.042 0.01 . 1 . . . . . . . . . 4966 1 368 . 1 1 44 44 LYS CA C 13 54.034 0.15 . 1 . . . . . . . . . 4966 1 369 . 1 1 45 45 SER H H 1 8.582 0.01 . 1 . . . . . . . . . 4966 1 370 . 1 1 45 45 SER HA H 1 4.775 0.01 . 1 . . . . . . . . . 4966 1 371 . 1 1 45 45 SER HB2 H 1 4.410 0.01 . 2 . . . . . . . . . 4966 1 372 . 1 1 45 45 SER HB3 H 1 4.032 0.01 . 2 . . . . . . . . . 4966 1 373 . 1 1 45 45 SER CA C 13 57.682 0.15 . 1 . . . . . . . . . 4966 1 374 . 1 1 46 46 SER H H 1 9.436 0.01 . 1 . . . . . . . . . 4966 1 375 . 1 1 46 46 SER HA H 1 5.004 0.01 . 1 . . . . . . . . . 4966 1 376 . 1 1 46 46 SER HB2 H 1 4.472 0.01 . 2 . . . . . . . . . 4966 1 377 . 1 1 46 46 SER HB3 H 1 3.974 0.01 . 2 . . . . . . . . . 4966 1 378 . 1 1 46 46 SER CA C 13 53.928 0.15 . 1 . . . . . . . . . 4966 1 379 . 1 1 47 47 LEU H H 1 8.269 0.01 . 1 . . . . . . . . . 4966 1 380 . 1 1 47 47 LEU HA H 1 4.232 0.01 . 1 . . . . . . . . . 4966 1 381 . 1 1 47 47 LEU HB2 H 1 1.763 0.01 . 1 . . . . . . . . . 4966 1 382 . 1 1 47 47 LEU HB3 H 1 1.763 0.01 . 1 . . . . . . . . . 4966 1 383 . 1 1 47 47 LEU HG H 1 1.639 0.01 . 1 . . . . . . . . . 4966 1 384 . 1 1 47 47 LEU HD11 H 1 0.948 0.01 . 1 . . . . . . . . . 4966 1 385 . 1 1 47 47 LEU HD12 H 1 0.948 0.01 . 1 . . . . . . . . . 4966 1 386 . 1 1 47 47 LEU HD13 H 1 0.948 0.01 . 1 . . . . . . . . . 4966 1 387 . 1 1 47 47 LEU HD21 H 1 0.948 0.01 . 1 . . . . . . . . . 4966 1 388 . 1 1 47 47 LEU HD22 H 1 0.948 0.01 . 1 . . . . . . . . . 4966 1 389 . 1 1 47 47 LEU HD23 H 1 0.948 0.01 . 1 . . . . . . . . . 4966 1 390 . 1 1 47 47 LEU CA C 13 55.029 0.15 . 1 . . . . . . . . . 4966 1 391 . 1 1 48 48 LEU H H 1 8.084 0.01 . 1 . . . . . . . . . 4966 1 392 . 1 1 48 48 LEU HA H 1 4.545 0.01 . 1 . . . . . . . . . 4966 1 393 . 1 1 48 48 LEU HB2 H 1 1.748 0.01 . 1 . . . . . . . . . 4966 1 394 . 1 1 48 48 LEU HB3 H 1 1.748 0.01 . 1 . . . . . . . . . 4966 1 395 . 1 1 48 48 LEU HG H 1 1.657 0.01 . 1 . . . . . . . . . 4966 1 396 . 1 1 48 48 LEU HD11 H 1 0.947 0.01 . 2 . . . . . . . . . 4966 1 397 . 1 1 48 48 LEU HD12 H 1 0.947 0.01 . 2 . . . . . . . . . 4966 1 398 . 1 1 48 48 LEU HD13 H 1 0.947 0.01 . 2 . . . . . . . . . 4966 1 399 . 1 1 48 48 LEU HD21 H 1 0.878 0.01 . 2 . . . . . . . . . 4966 1 400 . 1 1 48 48 LEU HD22 H 1 0.878 0.01 . 2 . . . . . . . . . 4966 1 401 . 1 1 48 48 LEU HD23 H 1 0.878 0.01 . 2 . . . . . . . . . 4966 1 402 . 1 1 48 48 LEU CA C 13 53.483 0.15 . 1 . . . . . . . . . 4966 1 403 . 1 1 49 49 VAL H H 1 7.538 0.01 . 1 . . . . . . . . . 4966 1 404 . 1 1 49 49 VAL HA H 1 4.810 0.01 . 1 . . . . . . . . . 4966 1 405 . 1 1 49 49 VAL HB H 1 1.900 0.01 . 1 . . . . . . . . . 4966 1 406 . 1 1 49 49 VAL HG11 H 1 0.882 0.01 . 2 . . . . . . . . . 4966 1 407 . 1 1 49 49 VAL HG12 H 1 0.882 0.01 . 2 . . . . . . . . . 4966 1 408 . 1 1 49 49 VAL HG13 H 1 0.882 0.01 . 2 . . . . . . . . . 4966 1 409 . 1 1 49 49 VAL HG21 H 1 0.763 0.01 . 2 . . . . . . . . . 4966 1 410 . 1 1 49 49 VAL HG22 H 1 0.763 0.01 . 2 . . . . . . . . . 4966 1 411 . 1 1 49 49 VAL HG23 H 1 0.763 0.01 . 2 . . . . . . . . . 4966 1 412 . 1 1 49 49 VAL CA C 13 58.462 0.15 . 1 . . . . . . . . . 4966 1 413 . 1 1 50 50 LYS H H 1 8.729 0.01 . 1 . . . . . . . . . 4966 1 414 . 1 1 50 50 LYS HA H 1 4.813 0.01 . 1 . . . . . . . . . 4966 1 415 . 1 1 50 50 LYS HB2 H 1 1.349 0.01 . 1 . . . . . . . . . 4966 1 416 . 1 1 50 50 LYS HB3 H 1 1.349 0.01 . 1 . . . . . . . . . 4966 1 417 . 1 1 50 50 LYS HG2 H 1 1.225 0.01 . 2 . . . . . . . . . 4966 1 418 . 1 1 50 50 LYS HG3 H 1 1.148 0.01 . 2 . . . . . . . . . 4966 1 419 . 1 1 50 50 LYS HD2 H 1 1.664 0.01 . 1 . . . . . . . . . 4966 1 420 . 1 1 50 50 LYS HD3 H 1 1.664 0.01 . 1 . . . . . . . . . 4966 1 421 . 1 1 50 50 LYS HE2 H 1 2.923 0.01 . 2 . . . . . . . . . 4966 1 422 . 1 1 50 50 LYS HE3 H 1 2.842 0.01 . 2 . . . . . . . . . 4966 1 423 . 1 1 50 50 LYS CA C 13 51.534 0.15 . 1 . . . . . . . . . 4966 1 424 . 1 1 51 51 TYR H H 1 8.324 0.01 . 1 . . . . . . . . . 4966 1 425 . 1 1 51 51 TYR HA H 1 5.293 0.01 . 1 . . . . . . . . . 4966 1 426 . 1 1 51 51 TYR HB2 H 1 2.831 0.01 . 2 . . . . . . . . . 4966 1 427 . 1 1 51 51 TYR HB3 H 1 2.635 0.01 . 2 . . . . . . . . . 4966 1 428 . 1 1 51 51 TYR HD1 H 1 6.733 0.01 . 1 . . . . . . . . . 4966 1 429 . 1 1 51 51 TYR HD2 H 1 6.733 0.01 . 1 . . . . . . . . . 4966 1 430 . 1 1 51 51 TYR HE1 H 1 6.465 0.01 . 1 . . . . . . . . . 4966 1 431 . 1 1 51 51 TYR HE2 H 1 6.465 0.01 . 1 . . . . . . . . . 4966 1 432 . 1 1 51 51 TYR CA C 13 54.788 0.15 . 1 . . . . . . . . . 4966 1 433 . 1 1 52 52 VAL H H 1 8.953 0.01 . 1 . . . . . . . . . 4966 1 434 . 1 1 52 52 VAL HA H 1 4.556 0.01 . 1 . . . . . . . . . 4966 1 435 . 1 1 52 52 VAL HB H 1 2.092 0.01 . 1 . . . . . . . . . 4966 1 436 . 1 1 52 52 VAL HG11 H 1 1.149 0.01 . 2 . . . . . . . . . 4966 1 437 . 1 1 52 52 VAL HG12 H 1 1.149 0.01 . 2 . . . . . . . . . 4966 1 438 . 1 1 52 52 VAL HG13 H 1 1.149 0.01 . 2 . . . . . . . . . 4966 1 439 . 1 1 52 52 VAL HG21 H 1 1.069 0.01 . 2 . . . . . . . . . 4966 1 440 . 1 1 52 52 VAL HG22 H 1 1.069 0.01 . 2 . . . . . . . . . 4966 1 441 . 1 1 52 52 VAL HG23 H 1 1.069 0.01 . 2 . . . . . . . . . 4966 1 442 . 1 1 52 52 VAL CA C 13 59.688 0.15 . 1 . . . . . . . . . 4966 1 443 . 1 1 53 53 CYS H H 1 9.471 0.01 . 1 . . . . . . . . . 4966 1 444 . 1 1 53 53 CYS HA H 1 5.912 0.01 . 1 . . . . . . . . . 4966 1 445 . 1 1 53 53 CYS HB2 H 1 3.803 0.01 . 2 . . . . . . . . . 4966 1 446 . 1 1 53 53 CYS HB3 H 1 3.078 0.01 . 2 . . . . . . . . . 4966 1 447 . 1 1 53 53 CYS CA C 13 52.609 0.15 . 1 . . . . . . . . . 4966 1 448 . 1 1 54 54 CYS H H 1 9.166 0.01 . 1 . . . . . . . . . 4966 1 449 . 1 1 54 54 CYS HA H 1 5.117 0.01 . 1 . . . . . . . . . 4966 1 450 . 1 1 54 54 CYS HB2 H 1 3.650 0.01 . 2 . . . . . . . . . 4966 1 451 . 1 1 54 54 CYS HB3 H 1 3.440 0.01 . 2 . . . . . . . . . 4966 1 452 . 1 1 54 54 CYS CA C 13 52.872 0.15 . 1 . . . . . . . . . 4966 1 453 . 1 1 55 55 ASN H H 1 8.595 0.01 . 1 . . . . . . . . . 4966 1 454 . 1 1 55 55 ASN HA H 1 5.167 0.01 . 1 . . . . . . . . . 4966 1 455 . 1 1 55 55 ASN HB2 H 1 3.402 0.01 . 2 . . . . . . . . . 4966 1 456 . 1 1 55 55 ASN HB3 H 1 2.656 0.01 . 2 . . . . . . . . . 4966 1 457 . 1 1 55 55 ASN HD21 H 1 6.740 0.01 . 2 . . . . . . . . . 4966 1 458 . 1 1 55 55 ASN HD22 H 1 7.542 0.01 . 2 . . . . . . . . . 4966 1 459 . 1 1 55 55 ASN CA C 13 50.689 0.15 . 1 . . . . . . . . . 4966 1 460 . 1 1 56 56 THR H H 1 7.584 0.01 . 1 . . . . . . . . . 4966 1 461 . 1 1 56 56 THR HA H 1 4.706 0.01 . 1 . . . . . . . . . 4966 1 462 . 1 1 56 56 THR HG21 H 1 1.204 0.01 . 1 . . . . . . . . . 4966 1 463 . 1 1 56 56 THR HG22 H 1 1.204 0.01 . 1 . . . . . . . . . 4966 1 464 . 1 1 56 56 THR HG23 H 1 1.204 0.01 . 1 . . . . . . . . . 4966 1 465 . 1 1 56 56 THR CA C 13 57.714 0.15 . 1 . . . . . . . . . 4966 1 466 . 1 1 57 57 ASP H H 1 8.228 0.01 . 1 . . . . . . . . . 4966 1 467 . 1 1 57 57 ASP HA H 1 4.856 0.01 . 1 . . . . . . . . . 4966 1 468 . 1 1 57 57 ASP HB2 H 1 2.500 0.01 . 2 . . . . . . . . . 4966 1 469 . 1 1 57 57 ASP HB3 H 1 2.274 0.01 . 2 . . . . . . . . . 4966 1 470 . 1 1 57 57 ASP CA C 13 51.632 0.15 . 1 . . . . . . . . . 4966 1 471 . 1 1 58 58 ARG H H 1 9.666 0.01 . 1 . . . . . . . . . 4966 1 472 . 1 1 58 58 ARG HA H 1 3.407 0.01 . 1 . . . . . . . . . 4966 1 473 . 1 1 58 58 ARG HB2 H 1 1.781 0.01 . 2 . . . . . . . . . 4966 1 474 . 1 1 58 58 ARG HB3 H 1 1.372 0.01 . 2 . . . . . . . . . 4966 1 475 . 1 1 58 58 ARG HG2 H 1 0.756 0.01 . 1 . . . . . . . . . 4966 1 476 . 1 1 58 58 ARG HG3 H 1 0.756 0.01 . 1 . . . . . . . . . 4966 1 477 . 1 1 58 58 ARG HD2 H 1 2.207 0.01 . 1 . . . . . . . . . 4966 1 478 . 1 1 58 58 ARG HD3 H 1 2.207 0.01 . 1 . . . . . . . . . 4966 1 479 . 1 1 58 58 ARG CA C 13 55.729 0.15 . 1 . . . . . . . . . 4966 1 480 . 1 1 59 59 CYS H H 1 7.572 0.01 . 1 . . . . . . . . . 4966 1 481 . 1 1 59 59 CYS HA H 1 4.473 0.01 . 1 . . . . . . . . . 4966 1 482 . 1 1 59 59 CYS HB2 H 1 3.642 0.01 . 2 . . . . . . . . . 4966 1 483 . 1 1 59 59 CYS HB3 H 1 3.363 0.01 . 2 . . . . . . . . . 4966 1 484 . 1 1 59 59 CYS CA C 13 54.011 0.15 . 1 . . . . . . . . . 4966 1 485 . 1 1 60 60 ASN H H 1 9.136 0.01 . 1 . . . . . . . . . 4966 1 486 . 1 1 60 60 ASN HA H 1 4.387 0.01 . 1 . . . . . . . . . 4966 1 487 . 1 1 60 60 ASN HB2 H 1 2.732 0.01 . 2 . . . . . . . . . 4966 1 488 . 1 1 60 60 ASN HB3 H 1 2.357 0.01 . 2 . . . . . . . . . 4966 1 489 . 1 1 60 60 ASN HD21 H 1 7.485 0.01 . 2 . . . . . . . . . 4966 1 490 . 1 1 60 60 ASN HD22 H 1 7.642 0.01 . 2 . . . . . . . . . 4966 1 491 . 1 1 60 60 ASN CA C 13 52.342 0.15 . 1 . . . . . . . . . 4966 1 stop_ save_