data_4988 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4988 _Entry.Title ; Three Dimensional Solution Structure of Huwentoxin-II BY 2D 1H-NMR ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-04-12 _Entry.Accession_date 2001-04-17 _Entry.Last_release_date 2001-04-17 _Entry.Original_release_date 2001-04-17 _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 Qin Shu . . . . 4988 2 Shan-yun Lu . . . . 4988 3 Xiao-chen Gu . . . . 4988 4 Song-ping Liang . . . . 4988 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4988 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 267 4988 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 . . 2001-05-11 . original BMRB . 4988 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4988 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Three-dimensional Solution Structure Determination of Huwentoxin-II by 2D 1H-NMR ; _Citation.Status submitted _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 . 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 Q. Shu . . . . 4988 1 2 S. Lu . Y. . . 4988 1 3 X. Gu . C. . . 4988 1 4 S. Liang . P. . . 4988 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'disulfide bonds' 4988 1 'insecticidal toxin' 4988 1 neurotoxin 4988 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4988 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 12053191 _Citation.Full_citation ; Q. SHU, S.Y. LU, X.C. GU, S.P. LIANG. Sequence-specific assignment of 1H-NMR resonance and determination of the secondary structure of HWTX-II. Acta Biochim. et Biophys. Sinica 2001,33: 65 ; _Citation.Title ; Sequence-specific Assignment of (1)H-NMR Resonance and Determination of the Secondary Structure of HWTX-II. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao' _Citation.Journal_name_full 'Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica' _Citation.Journal_volume 33 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0582-9879 _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 65 _Citation.Page_last 70 _Citation.Year 2001 _Citation.Details ; Huwentoxin-II (HWTX-II)is an insecticidal peptide purified from the venom of spider Selenocosmia huwena. The structure of this toxin in solution was investigated using 2D-NMR. The complete sequence-specific assignments of proton resonance in the (1)H-NMR spectra of HWTX-II were obtained by analyzing a series of 2D spectrum, including COSY, DQF-COSY, TOCSY and NOESY. All the backbone protons and side chain protons, except epsilonNH(2) protons of Lys residues, were identified by d(alphaN), d(alpha&dgr);, d(NN) and d(betaN) connectivities. The results provide a basis for further determination of the solution conformation of HWTX-II. Furthermore the secondary structure of HWTX-II was determined from NMR data. It contained mainly extended conformation, especially a double-stranded anti-parallel beta-sheet with Trp27--Cys29 and Cys34--Lys36 at the C terminal, and it lacked helix. These characters of the secondary structure of HWTX-II were similar to those spider toxins which structure in solution had been reported. ; 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 . Shu Q. . . . 4988 2 2 . Lu S. Y. . . 4988 2 3 . Gu X. C. . . 4988 2 4 . Liang S. P. . . 4988 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4988 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11298747 _Citation.Full_citation ; Q.SHU,R.H.HUANG,S.P.LIANG Assignment of disulfide bonds of huwentoxin-ii by Edman degradation sequencing and stepwise thiol modification. Eur. J. Biochem. 2001, 268(8):2301-2307 ; _Citation.Title ; Assignment of the disulfide bonds of huwentoxin-II by Edman degradation sequencing and stepwise thiol modification. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full 'European journal of biochemistry / FEBS' _Citation.Journal_volume 268 _Citation.Journal_issue 8 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0014-2956 _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 2301 _Citation.Page_last 2307 _Citation.Year 2001 _Citation.Details ; A novel strategy combining Edman degradation and thiol modification was developed to assign the three disulfides of huwentoxin-II (HWTX-II), an insecticidal peptide purified from the venom of the spider Selenocosmia huwena. Phenylthiohydantoin (Pth) derivatives of Cys and the elimination product, dehydroalanine (DeltaSer), can be observed in the Cys cycles during Edman degradation of native HWTX-II. The appearance of two products indicates that the disulfides of HWTX-II were split and that the free thiol group of the second half cystine has been generated. Information about the nature of the disulfide bridges of HWTX-II could be obtained from the sequencing signal if the nascent thiols were modified stepwise by 4-vinylpyridine. Using this method the disulfide bridges of HWTX-II were assigned as Cys4-Cys18, Cys8-Cys29 and Cys23-Cys34, which is different from that seen in HWTX-I, a neurotoxic peptide from the same spider. Using this strategy, one can assign the disulfide bonds of small proteins by sequencing and modification n - 1 times, where n is the number of disulfide bonds in the protein. The above assignment of the disulfide bonds of HWTX-II was confirmed by MALDI-TOF MS of tryptic fragments of HWTX-II. Some disulfide interchanging during proteolysis was observed by monitoring the kinetics of proteolysis of HWTX-II by MALDI-TOF MS. ; 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 Q Shu Q. . . . 4988 3 2 R Huang R. . . . 4988 3 3 S Liang S. . . . 4988 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 4988 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10424342 _Citation.Full_citation ; Purification and characterization of huwentoxin-II, a neurotoxic peptide from the venom of the Chinese bird spider Selenocosmia huwena. J. Pept. Res. 1999 May;53(5):486-491 ; _Citation.Title ; Purification and characterization of huwentoxin-II, a neurotoxic peptide from the venom of the Chinese bird spider Selenocosmia huwena. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Pept. Res.' _Citation.Journal_name_full 'The journal of peptide research : official journal of the American Peptide Society' _Citation.Journal_volume 53 _Citation.Journal_issue 5 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1397-002X _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 486 _Citation.Page_last 491 _Citation.Year 1999 _Citation.Details ; A neurotoxic peptide, huwentoxin-II (HWTX-II), was purified from the venom of the Chinese bird spider Selenocosmia huwena by ion exchange chromatography and reversed phase HPLC. The toxin can reversibly paralyse cockroaches for several hours, with an ED50 of 127 +/- 54 microg/g. HWTX-II blocks neuromuscular transmission in an isolated mouse phrenic nerve diaphragm preparation and acts cooperatively to potentiate the activity of huwentoxin-I. The complete amino sequence of HWTX-II was determined and found to consist of 37 amino acid residues, including six Cys residues. There is microheterogeneity (Ile/Gln) in position 10, and mass spectrometry indicated that the two isoproteins have a tendency to dimerize. It was determined by mass spectrometry that the six Cys residues are involved in three disulphide bonds. The sequence of HWTX-II is highly homologous with ESTX, a toxin from the tarantula Eurypefina californicum. ; 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 Q Shu Q. . . . 4988 4 2 'S P' Liang S. P. . . 4988 4 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_HWTX-II _Assembly.Sf_category assembly _Assembly.Sf_framecode system_HWTX-II _Assembly.Entry_ID 4988 _Assembly.ID 1 _Assembly.Name HUWENTOXIN-II _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 4988 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 'HUWENTOXIN-II(Ile, 10)' 1 $HUWENTOXIN-II . . . native . . . . . 4988 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 4 4 SG . 1 . 1 CYS 18 18 SG . . . . . . . . . . . . 4988 1 2 disulfide single . 1 . 1 CYS 8 8 SG . 1 . 1 CYS 29 29 SG . . . . . . . . . . . . 4988 1 3 disulfide single . 1 . 1 CYS 23 23 SG . 1 . 1 CYS 34 34 SG . . . . . . . . . . . . 4988 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 1I25 . . . . . . 4988 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID HUWENTOXIN-II system 4988 1 HWTX-II abbreviation 4988 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID neurotoxin 4988 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_HUWENTOXIN-II _Entity.Sf_category entity _Entity.Sf_framecode HUWENTOXIN-II _Entity.Entry_ID 4988 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name Huwentoxin-II _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 ; LFECSFSCEIEKEGDKPCKK KKCKGGWKCKFNMCVKV ; _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 37 _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 4284.3 _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 PDB 1I25 . 'Three Dimensional Solution Structure Of Huwentoxin-Ii By 2d 1h-Nmr' . . . . . 100.00 37 100.00 100.00 1.67e-11 . . . . 4988 1 . no GenBank AAP33076 . 'huwentoxin-II precursor [Ornithoctonus huwena]' . . . . . 100.00 85 100.00 100.00 4.89e-13 . . . . 4988 1 . no GenBank ABY77725 . 'HWTX-IIa precursor [Ornithoctonus huwena]' . . . . . 97.30 85 100.00 100.00 2.00e-12 . . . . 4988 1 . no GenBank ABY77726 . 'HWTX-IIb precursor [Ornithoctonus huwena]' . . . . . 100.00 85 100.00 100.00 4.89e-13 . . . . 4988 1 . no GenBank ABY77727 . 'HWTX-IIc precursor [Ornithoctonus huwena]' . . . . . 97.30 85 100.00 100.00 1.89e-12 . . . . 4988 1 . no GenBank ABY77732 . 'HWTX-VIIIa precursor [Ornithoctonus huwena]' . . . . . 97.30 84 100.00 100.00 2.23e-12 . . . . 4988 1 . no SWISS-PROT P68421 . 'Huwentoxin-7 precursor (Huwentoxin-VII) (HwTx-VII)' . . . . . 100.00 84 100.00 100.00 5.78e-13 . . . . 4988 1 . no SWISS-PROT P82959 . 'Huwentoxin-2 form 1 precursor (Huwentoxin-II) (HwTx-II)' . . . . . 100.00 85 100.00 100.00 4.89e-13 . . . . 4988 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID HWTX-II abbreviation 4988 1 Huwentoxin-II common 4988 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 . 4988 1 2 . PHE . 4988 1 3 . GLU . 4988 1 4 . CYS . 4988 1 5 . SER . 4988 1 6 . PHE . 4988 1 7 . SER . 4988 1 8 . CYS . 4988 1 9 . GLU . 4988 1 10 . ILE . 4988 1 11 . GLU . 4988 1 12 . LYS . 4988 1 13 . GLU . 4988 1 14 . GLY . 4988 1 15 . ASP . 4988 1 16 . LYS . 4988 1 17 . PRO . 4988 1 18 . CYS . 4988 1 19 . LYS . 4988 1 20 . LYS . 4988 1 21 . LYS . 4988 1 22 . LYS . 4988 1 23 . CYS . 4988 1 24 . LYS . 4988 1 25 . GLY . 4988 1 26 . GLY . 4988 1 27 . TRP . 4988 1 28 . LYS . 4988 1 29 . CYS . 4988 1 30 . LYS . 4988 1 31 . PHE . 4988 1 32 . ASN . 4988 1 33 . MET . 4988 1 34 . CYS . 4988 1 35 . VAL . 4988 1 36 . LYS . 4988 1 37 . VAL . 4988 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 4988 1 . PHE 2 2 4988 1 . GLU 3 3 4988 1 . CYS 4 4 4988 1 . SER 5 5 4988 1 . PHE 6 6 4988 1 . SER 7 7 4988 1 . CYS 8 8 4988 1 . GLU 9 9 4988 1 . ILE 10 10 4988 1 . GLU 11 11 4988 1 . LYS 12 12 4988 1 . GLU 13 13 4988 1 . GLY 14 14 4988 1 . ASP 15 15 4988 1 . LYS 16 16 4988 1 . PRO 17 17 4988 1 . CYS 18 18 4988 1 . LYS 19 19 4988 1 . LYS 20 20 4988 1 . LYS 21 21 4988 1 . LYS 22 22 4988 1 . CYS 23 23 4988 1 . LYS 24 24 4988 1 . GLY 25 25 4988 1 . GLY 26 26 4988 1 . TRP 27 27 4988 1 . LYS 28 28 4988 1 . CYS 29 29 4988 1 . LYS 30 30 4988 1 . PHE 31 31 4988 1 . ASN 32 32 4988 1 . MET 33 33 4988 1 . CYS 34 34 4988 1 . VAL 35 35 4988 1 . LYS 36 36 4988 1 . VAL 37 37 4988 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 4988 _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 $HUWENTOXIN-II . 29017 . . 'Selenocosmia huwena' 'Chinese bird spider' . . Eukaryota Metazoa Selenocosmia huwena . . 'venom gland' . . . . . . . . . . 4988 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 4988 _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 $HUWENTOXIN-II . 'purified from the natural source' . . . . . . . . . . . . . . . . 4988 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4988 _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 Huwentoxin-II . . . 1 $HUWENTOXIN-II . . 4 . . mM . . . . 4988 1 2 'phosphate buffer' . . . . . . . 20 . . mM . . . . 4988 1 3 H2O . . . . . . . 90 . . % . . . . 4988 1 4 D2O . . . . . . . 10 . . % . . . . 4988 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 4988 _Sample.ID 2 _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 Huwentoxin-II . . . 1 $HUWENTOXIN-II . . 4 . . mM . . . . 4988 2 2 'phosphate buffer' . . . . . . . 20 . . mM . . . . 4988 2 3 D2O . . . . . . . 100 . . % . . . . 4988 2 stop_ save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_cond_1 _Sample_condition_list.Entry_ID 4988 _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 'ionic strength' 20 0.02 mM 4988 1 pH 5.4 0.2 n/a 4988 1 pressure 1 . atm 4988 1 temperature 300 1 K 4988 1 stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Software.Sf_category software _Software.Sf_framecode FELIX _Software.Entry_ID 4988 _Software.ID 1 _Software.Type . _Software.Name FELIX _Software.Version 98.0 _Software.DOI . _Software.Details 'Molecular Simulations, Inc.' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 4988 1 stop_ save_ save_X-PLOR _Software.Sf_category software _Software.Sf_framecode X-PLOR _Software.Entry_ID 4988 _Software.ID 2 _Software.Type . _Software.Name X-PLOR _Software.Version 3.851 _Software.DOI . _Software.Details Brunger loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 4988 2 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 4988 _NMR_spectrometer.ID 1 _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 4988 _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 DMX . 500 . . . 4988 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 4988 _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 NOESY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4988 1 2 DQF-COSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4988 1 3 TOCSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4988 1 4 E-COSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4988 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 4988 _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 H 1 TSP 'methyl protons' . . . . ppm 0.00 internal direct . internal cylindrical . . . 4988 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 4988 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_cond_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 NOESY 1 $sample_1 . 4988 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 3.93 0.02 . 1 . . . . . . . . . 4988 1 2 . 1 1 1 1 LEU HB2 H 1 1.56 0.02 . 1 . . . . . . . . . 4988 1 3 . 1 1 1 1 LEU HB3 H 1 1.56 0.02 . 1 . . . . . . . . . 4988 1 4 . 1 1 1 1 LEU HG H 1 1.59 0.02 . 1 . . . . . . . . . 4988 1 5 . 1 1 1 1 LEU HD11 H 1 0.78 0.02 . 2 . . . . . . . . . 4988 1 6 . 1 1 1 1 LEU HD12 H 1 0.78 0.02 . 2 . . . . . . . . . 4988 1 7 . 1 1 1 1 LEU HD13 H 1 0.78 0.02 . 2 . . . . . . . . . 4988 1 8 . 1 1 1 1 LEU HD21 H 1 0.80 0.02 . 2 . . . . . . . . . 4988 1 9 . 1 1 1 1 LEU HD22 H 1 0.80 0.02 . 2 . . . . . . . . . 4988 1 10 . 1 1 1 1 LEU HD23 H 1 0.80 0.02 . 2 . . . . . . . . . 4988 1 11 . 1 1 2 2 PHE H H 1 8.48 0.02 . 1 . . . . . . . . . 4988 1 12 . 1 1 2 2 PHE HA H 1 4.77 0.02 . 1 . . . . . . . . . 4988 1 13 . 1 1 2 2 PHE HB2 H 1 3.00 0.02 . 2 . . . . . . . . . 4988 1 14 . 1 1 2 2 PHE HB3 H 1 3.25 0.02 . 2 . . . . . . . . . 4988 1 15 . 1 1 2 2 PHE HD1 H 1 7.33 0.02 . 1 . . . . . . . . . 4988 1 16 . 1 1 2 2 PHE HD2 H 1 7.33 0.02 . 1 . . . . . . . . . 4988 1 17 . 1 1 2 2 PHE HE1 H 1 7.37 0.02 . 1 . . . . . . . . . 4988 1 18 . 1 1 2 2 PHE HE2 H 1 7.37 0.02 . 1 . . . . . . . . . 4988 1 19 . 1 1 2 2 PHE HZ H 1 7.32 0.02 . 1 . . . . . . . . . 4988 1 20 . 1 1 3 3 GLU H H 1 8.73 0.02 . 1 . . . . . . . . . 4988 1 21 . 1 1 3 3 GLU HA H 1 4.54 0.02 . 1 . . . . . . . . . 4988 1 22 . 1 1 3 3 GLU HB2 H 1 1.96 0.02 . 1 . . . . . . . . . 4988 1 23 . 1 1 3 3 GLU HB3 H 1 1.96 0.02 . 1 . . . . . . . . . 4988 1 24 . 1 1 3 3 GLU HG2 H 1 2.25 0.02 . 2 . . . . . . . . . 4988 1 25 . 1 1 3 3 GLU HG3 H 1 2.57 0.02 . 2 . . . . . . . . . 4988 1 26 . 1 1 4 4 CYS H H 1 9.60 0.02 . 1 . . . . . . . . . 4988 1 27 . 1 1 4 4 CYS HA H 1 4.31 0.02 . 1 . . . . . . . . . 4988 1 28 . 1 1 4 4 CYS HB2 H 1 2.61 0.02 . 2 . . . . . . . . . 4988 1 29 . 1 1 4 4 CYS HB3 H 1 3.50 0.02 . 2 . . . . . . . . . 4988 1 30 . 1 1 5 5 SER H H 1 9.95 0.02 . 1 . . . . . . . . . 4988 1 31 . 1 1 5 5 SER HA H 1 4.06 0.02 . 1 . . . . . . . . . 4988 1 32 . 1 1 5 5 SER HB2 H 1 3.51 0.02 . 2 . . . . . . . . . 4988 1 33 . 1 1 5 5 SER HB3 H 1 3.81 0.02 . 2 . . . . . . . . . 4988 1 34 . 1 1 6 6 PHE H H 1 9.75 0.02 . 1 . . . . . . . . . 4988 1 35 . 1 1 6 6 PHE HA H 1 4.69 0.02 . 1 . . . . . . . . . 4988 1 36 . 1 1 6 6 PHE HB2 H 1 3.06 0.02 . 2 . . . . . . . . . 4988 1 37 . 1 1 6 6 PHE HB3 H 1 3.19 0.02 . 2 . . . . . . . . . 4988 1 38 . 1 1 6 6 PHE HD1 H 1 7.26 0.02 . 1 . . . . . . . . . 4988 1 39 . 1 1 6 6 PHE HD2 H 1 7.26 0.02 . 1 . . . . . . . . . 4988 1 40 . 1 1 6 6 PHE HE1 H 1 7.36 0.02 . 1 . . . . . . . . . 4988 1 41 . 1 1 6 6 PHE HE2 H 1 7.36 0.02 . 1 . . . . . . . . . 4988 1 42 . 1 1 6 6 PHE HZ H 1 7.44 0.02 . 1 . . . . . . . . . 4988 1 43 . 1 1 7 7 SER H H 1 7.96 0.02 . 1 . . . . . . . . . 4988 1 44 . 1 1 7 7 SER HA H 1 4.48 0.02 . 1 . . . . . . . . . 4988 1 45 . 1 1 7 7 SER HB2 H 1 3.93 0.02 . 1 . . . . . . . . . 4988 1 46 . 1 1 7 7 SER HB3 H 1 3.93 0.02 . 1 . . . . . . . . . 4988 1 47 . 1 1 8 8 CYS H H 1 7.48 0.02 . 1 . . . . . . . . . 4988 1 48 . 1 1 8 8 CYS HA H 1 5.27 0.02 . 1 . . . . . . . . . 4988 1 49 . 1 1 8 8 CYS HB2 H 1 2.57 0.02 . 2 . . . . . . . . . 4988 1 50 . 1 1 8 8 CYS HB3 H 1 3.61 0.02 . 2 . . . . . . . . . 4988 1 51 . 1 1 9 9 GLU H H 1 9.29 0.02 . 1 . . . . . . . . . 4988 1 52 . 1 1 9 9 GLU HA H 1 4.57 0.02 . 1 . . . . . . . . . 4988 1 53 . 1 1 9 9 GLU HB2 H 1 2.20 0.02 . 1 . . . . . . . . . 4988 1 54 . 1 1 9 9 GLU HB3 H 1 2.20 0.02 . 1 . . . . . . . . . 4988 1 55 . 1 1 9 9 GLU HG2 H 1 2.31 0.02 . 1 . . . . . . . . . 4988 1 56 . 1 1 9 9 GLU HG3 H 1 2.31 0.02 . 1 . . . . . . . . . 4988 1 57 . 1 1 10 10 ILE H H 1 8.09 0.02 . 1 . . . . . . . . . 4988 1 58 . 1 1 10 10 ILE HA H 1 4.24 0.02 . 1 . . . . . . . . . 4988 1 59 . 1 1 10 10 ILE HB H 1 2.01 0.02 . 1 . . . . . . . . . 4988 1 60 . 1 1 10 10 ILE HG12 H 1 1.22 0.02 . 2 . . . . . . . . . 4988 1 61 . 1 1 10 10 ILE HG13 H 1 1.55 0.02 . 2 . . . . . . . . . 4988 1 62 . 1 1 10 10 ILE HG21 H 1 1.03 0.02 . 1 . . . . . . . . . 4988 1 63 . 1 1 10 10 ILE HG22 H 1 1.03 0.02 . 1 . . . . . . . . . 4988 1 64 . 1 1 10 10 ILE HG23 H 1 1.03 0.02 . 1 . . . . . . . . . 4988 1 65 . 1 1 10 10 ILE HD11 H 1 0.91 0.02 . 1 . . . . . . . . . 4988 1 66 . 1 1 10 10 ILE HD12 H 1 0.91 0.02 . 1 . . . . . . . . . 4988 1 67 . 1 1 10 10 ILE HD13 H 1 0.91 0.02 . 1 . . . . . . . . . 4988 1 68 . 1 1 11 11 GLU H H 1 8.44 0.02 . 1 . . . . . . . . . 4988 1 69 . 1 1 11 11 GLU HA H 1 4.47 0.02 . 1 . . . . . . . . . 4988 1 70 . 1 1 11 11 GLU HB2 H 1 1.88 0.02 . 2 . . . . . . . . . 4988 1 71 . 1 1 11 11 GLU HB3 H 1 2.79 0.02 . 2 . . . . . . . . . 4988 1 72 . 1 1 11 11 GLU HG2 H 1 2.03 0.02 . 2 . . . . . . . . . 4988 1 73 . 1 1 11 11 GLU HG3 H 1 2.39 0.02 . 2 . . . . . . . . . 4988 1 74 . 1 1 12 12 LYS H H 1 7.80 0.02 . 1 . . . . . . . . . 4988 1 75 . 1 1 12 12 LYS HA H 1 4.92 0.02 . 1 . . . . . . . . . 4988 1 76 . 1 1 12 12 LYS HB2 H 1 1.55 0.02 . 2 . . . . . . . . . 4988 1 77 . 1 1 12 12 LYS HB3 H 1 1.64 0.02 . 2 . . . . . . . . . 4988 1 78 . 1 1 12 12 LYS HG2 H 1 1.09 0.02 . 2 . . . . . . . . . 4988 1 79 . 1 1 12 12 LYS HG3 H 1 1.18 0.02 . 2 . . . . . . . . . 4988 1 80 . 1 1 12 12 LYS HD2 H 1 1.56 0.02 . 1 . . . . . . . . . 4988 1 81 . 1 1 12 12 LYS HD3 H 1 1.56 0.02 . 1 . . . . . . . . . 4988 1 82 . 1 1 12 12 LYS HE2 H 1 2.84 0.02 . 1 . . . . . . . . . 4988 1 83 . 1 1 12 12 LYS HE3 H 1 2.84 0.02 . 1 . . . . . . . . . 4988 1 84 . 1 1 13 13 GLU H H 1 8.45 0.02 . 1 . . . . . . . . . 4988 1 85 . 1 1 13 13 GLU HA H 1 4.49 0.02 . 1 . . . . . . . . . 4988 1 86 . 1 1 13 13 GLU HB2 H 1 2.07 0.02 . 1 . . . . . . . . . 4988 1 87 . 1 1 13 13 GLU HB3 H 1 2.07 0.02 . 1 . . . . . . . . . 4988 1 88 . 1 1 13 13 GLU HG2 H 1 2.34 0.02 . 1 . . . . . . . . . 4988 1 89 . 1 1 13 13 GLU HG3 H 1 2.34 0.02 . 1 . . . . . . . . . 4988 1 90 . 1 1 14 14 GLY H H 1 9.20 0.02 . 1 . . . . . . . . . 4988 1 91 . 1 1 14 14 GLY HA2 H 1 3.79 0.02 . 2 . . . . . . . . . 4988 1 92 . 1 1 14 14 GLY HA3 H 1 3.98 0.02 . 2 . . . . . . . . . 4988 1 93 . 1 1 15 15 ASP H H 1 8.80 0.02 . 1 . . . . . . . . . 4988 1 94 . 1 1 15 15 ASP HA H 1 4.52 0.02 . 1 . . . . . . . . . 4988 1 95 . 1 1 15 15 ASP HB2 H 1 2.76 0.02 . 2 . . . . . . . . . 4988 1 96 . 1 1 15 15 ASP HB3 H 1 2.87 0.02 . 2 . . . . . . . . . 4988 1 97 . 1 1 16 16 LYS H H 1 7.88 0.02 . 1 . . . . . . . . . 4988 1 98 . 1 1 16 16 LYS HA H 1 4.94 0.02 . 1 . . . . . . . . . 4988 1 99 . 1 1 16 16 LYS HB2 H 1 1.94 0.02 . 1 . . . . . . . . . 4988 1 100 . 1 1 16 16 LYS HB3 H 1 1.94 0.02 . 1 . . . . . . . . . 4988 1 101 . 1 1 16 16 LYS HG2 H 1 1.51 0.02 . 2 . . . . . . . . . 4988 1 102 . 1 1 16 16 LYS HG3 H 1 1.58 0.02 . 2 . . . . . . . . . 4988 1 103 . 1 1 16 16 LYS HD2 H 1 1.77 0.02 . 1 . . . . . . . . . 4988 1 104 . 1 1 16 16 LYS HD3 H 1 1.77 0.02 . 1 . . . . . . . . . 4988 1 105 . 1 1 16 16 LYS HE2 H 1 3.08 0.02 . 1 . . . . . . . . . 4988 1 106 . 1 1 16 16 LYS HE3 H 1 3.08 0.02 . 1 . . . . . . . . . 4988 1 107 . 1 1 17 17 PRO HA H 1 4.92 0.02 . 1 . . . . . . . . . 4988 1 108 . 1 1 17 17 PRO HB2 H 1 1.90 0.02 . 2 . . . . . . . . . 4988 1 109 . 1 1 17 17 PRO HB3 H 1 2.40 0.02 . 2 . . . . . . . . . 4988 1 110 . 1 1 17 17 PRO HG2 H 1 2.00 0.02 . 2 . . . . . . . . . 4988 1 111 . 1 1 17 17 PRO HG3 H 1 2.12 0.02 . 2 . . . . . . . . . 4988 1 112 . 1 1 17 17 PRO HD2 H 1 3.77 0.02 . 2 . . . . . . . . . 4988 1 113 . 1 1 17 17 PRO HD3 H 1 3.98 0.02 . 2 . . . . . . . . . 4988 1 114 . 1 1 18 18 CYS H H 1 7.96 0.02 . 1 . . . . . . . . . 4988 1 115 . 1 1 18 18 CYS HA H 1 4.65 0.02 . 1 . . . . . . . . . 4988 1 116 . 1 1 18 18 CYS HB2 H 1 3.02 0.02 . 2 . . . . . . . . . 4988 1 117 . 1 1 18 18 CYS HB3 H 1 3.06 0.02 . 2 . . . . . . . . . 4988 1 118 . 1 1 19 19 LYS H H 1 8.50 0.02 . 1 . . . . . . . . . 4988 1 119 . 1 1 19 19 LYS HA H 1 4.46 0.02 . 1 . . . . . . . . . 4988 1 120 . 1 1 19 19 LYS HB2 H 1 1.49 0.02 . 2 . . . . . . . . . 4988 1 121 . 1 1 19 19 LYS HB3 H 1 1.61 0.02 . 2 . . . . . . . . . 4988 1 122 . 1 1 19 19 LYS HG2 H 1 1.38 0.02 . 2 . . . . . . . . . 4988 1 123 . 1 1 19 19 LYS HG3 H 1 1.68 0.02 . 2 . . . . . . . . . 4988 1 124 . 1 1 19 19 LYS HD2 H 1 1.49 0.02 . 1 . . . . . . . . . 4988 1 125 . 1 1 19 19 LYS HD3 H 1 1.49 0.02 . 1 . . . . . . . . . 4988 1 126 . 1 1 19 19 LYS HE2 H 1 2.95 0.02 . 1 . . . . . . . . . 4988 1 127 . 1 1 19 19 LYS HE3 H 1 2.95 0.02 . 1 . . . . . . . . . 4988 1 128 . 1 1 20 20 LYS H H 1 8.93 0.02 . 1 . . . . . . . . . 4988 1 129 . 1 1 20 20 LYS HA H 1 3.72 0.02 . 1 . . . . . . . . . 4988 1 130 . 1 1 20 20 LYS HB2 H 1 1.44 0.02 . 1 . . . . . . . . . 4988 1 131 . 1 1 20 20 LYS HB3 H 1 1.44 0.02 . 1 . . . . . . . . . 4988 1 132 . 1 1 20 20 LYS HG2 H 1 1.22 0.02 . 2 . . . . . . . . . 4988 1 133 . 1 1 20 20 LYS HG3 H 1 1.31 0.02 . 2 . . . . . . . . . 4988 1 134 . 1 1 20 20 LYS HD2 H 1 1.60 0.02 . 1 . . . . . . . . . 4988 1 135 . 1 1 20 20 LYS HD3 H 1 1.60 0.02 . 1 . . . . . . . . . 4988 1 136 . 1 1 20 20 LYS HE2 H 1 2.94 0.02 . 1 . . . . . . . . . 4988 1 137 . 1 1 20 20 LYS HE3 H 1 2.94 0.02 . 1 . . . . . . . . . 4988 1 138 . 1 1 21 21 LYS H H 1 8.43 0.02 . 1 . . . . . . . . . 4988 1 139 . 1 1 21 21 LYS HA H 1 4.06 0.02 . 1 . . . . . . . . . 4988 1 140 . 1 1 21 21 LYS HB2 H 1 1.26 0.02 . 2 . . . . . . . . . 4988 1 141 . 1 1 21 21 LYS HB3 H 1 1.41 0.02 . 2 . . . . . . . . . 4988 1 142 . 1 1 21 21 LYS HG2 H 1 1.01 0.02 . 2 . . . . . . . . . 4988 1 143 . 1 1 21 21 LYS HG3 H 1 1.08 0.02 . 2 . . . . . . . . . 4988 1 144 . 1 1 21 21 LYS HD2 H 1 1.30 0.02 . 2 . . . . . . . . . 4988 1 145 . 1 1 21 21 LYS HD3 H 1 1.38 0.02 . 2 . . . . . . . . . 4988 1 146 . 1 1 21 21 LYS HE2 H 1 2.88 0.02 . 1 . . . . . . . . . 4988 1 147 . 1 1 21 21 LYS HE3 H 1 2.88 0.02 . 1 . . . . . . . . . 4988 1 148 . 1 1 22 22 LYS H H 1 8.24 0.02 . 1 . . . . . . . . . 4988 1 149 . 1 1 22 22 LYS HA H 1 4.34 0.02 . 1 . . . . . . . . . 4988 1 150 . 1 1 22 22 LYS HB2 H 1 1.69 0.02 . 2 . . . . . . . . . 4988 1 151 . 1 1 22 22 LYS HB3 H 1 1.75 0.02 . 2 . . . . . . . . . 4988 1 152 . 1 1 22 22 LYS HG2 H 1 1.42 0.02 . 2 . . . . . . . . . 4988 1 153 . 1 1 22 22 LYS HG3 H 1 1.52 0.02 . 2 . . . . . . . . . 4988 1 154 . 1 1 22 22 LYS HD2 H 1 1.69 0.02 . 1 . . . . . . . . . 4988 1 155 . 1 1 22 22 LYS HD3 H 1 1.69 0.02 . 1 . . . . . . . . . 4988 1 156 . 1 1 22 22 LYS HE2 H 1 3.04 0.02 . 1 . . . . . . . . . 4988 1 157 . 1 1 22 22 LYS HE3 H 1 3.04 0.02 . 1 . . . . . . . . . 4988 1 158 . 1 1 23 23 CYS H H 1 8.89 0.02 . 1 . . . . . . . . . 4988 1 159 . 1 1 23 23 CYS HA H 1 4.66 0.02 . 1 . . . . . . . . . 4988 1 160 . 1 1 23 23 CYS HB2 H 1 2.55 0.02 . 2 . . . . . . . . . 4988 1 161 . 1 1 23 23 CYS HB3 H 1 3.10 0.02 . 2 . . . . . . . . . 4988 1 162 . 1 1 24 24 LYS H H 1 8.56 0.02 . 1 . . . . . . . . . 4988 1 163 . 1 1 24 24 LYS HA H 1 4.18 0.02 . 1 . . . . . . . . . 4988 1 164 . 1 1 24 24 LYS HB2 H 1 1.38 0.02 . 2 . . . . . . . . . 4988 1 165 . 1 1 24 24 LYS HB3 H 1 1.72 0.02 . 2 . . . . . . . . . 4988 1 166 . 1 1 24 24 LYS HG2 H 1 1.30 0.02 . 1 . . . . . . . . . 4988 1 167 . 1 1 24 24 LYS HG3 H 1 1.30 0.02 . 1 . . . . . . . . . 4988 1 168 . 1 1 24 24 LYS HD2 H 1 1.36 0.02 . 2 . . . . . . . . . 4988 1 169 . 1 1 24 24 LYS HD3 H 1 1.44 0.02 . 2 . . . . . . . . . 4988 1 170 . 1 1 24 24 LYS HE2 H 1 2.71 0.02 . 1 . . . . . . . . . 4988 1 171 . 1 1 24 24 LYS HE3 H 1 2.71 0.02 . 1 . . . . . . . . . 4988 1 172 . 1 1 25 25 GLY H H 1 8.50 0.02 . 1 . . . . . . . . . 4988 1 173 . 1 1 25 25 GLY HA2 H 1 3.84 0.02 . 2 . . . . . . . . . 4988 1 174 . 1 1 25 25 GLY HA3 H 1 4.05 0.02 . 2 . . . . . . . . . 4988 1 175 . 1 1 26 26 GLY H H 1 8.96 0.02 . 1 . . . . . . . . . 4988 1 176 . 1 1 26 26 GLY HA2 H 1 3.70 0.02 . 2 . . . . . . . . . 4988 1 177 . 1 1 26 26 GLY HA3 H 1 4.43 0.02 . 2 . . . . . . . . . 4988 1 178 . 1 1 27 27 TRP H H 1 8.74 0.02 . 1 . . . . . . . . . 4988 1 179 . 1 1 27 27 TRP HA H 1 5.27 0.02 . 1 . . . . . . . . . 4988 1 180 . 1 1 27 27 TRP HB2 H 1 2.96 0.02 . 2 . . . . . . . . . 4988 1 181 . 1 1 27 27 TRP HB3 H 1 3.55 0.02 . 2 . . . . . . . . . 4988 1 182 . 1 1 27 27 TRP HD1 H 1 7.13 0.02 . 1 . . . . . . . . . 4988 1 183 . 1 1 27 27 TRP HE1 H 1 10.38 0.02 . 1 . . . . . . . . . 4988 1 184 . 1 1 27 27 TRP HE3 H 1 7.15 0.02 . 1 . . . . . . . . . 4988 1 185 . 1 1 27 27 TRP HZ2 H 1 7.52 0.02 . 1 . . . . . . . . . 4988 1 186 . 1 1 27 27 TRP HZ3 H 1 7.17 0.02 . 1 . . . . . . . . . 4988 1 187 . 1 1 27 27 TRP HH2 H 1 7.27 0.02 . 1 . . . . . . . . . 4988 1 188 . 1 1 28 28 LYS H H 1 9.69 0.02 . 1 . . . . . . . . . 4988 1 189 . 1 1 28 28 LYS HA H 1 4.75 0.02 . 1 . . . . . . . . . 4988 1 190 . 1 1 28 28 LYS HB2 H 1 1.66 0.02 . 2 . . . . . . . . . 4988 1 191 . 1 1 28 28 LYS HB3 H 1 1.72 0.02 . 2 . . . . . . . . . 4988 1 192 . 1 1 28 28 LYS HG2 H 1 1.28 0.02 . 2 . . . . . . . . . 4988 1 193 . 1 1 28 28 LYS HG3 H 1 1.34 0.02 . 2 . . . . . . . . . 4988 1 194 . 1 1 28 28 LYS HD2 H 1 1.64 0.02 . 1 . . . . . . . . . 4988 1 195 . 1 1 28 28 LYS HD3 H 1 1.64 0.02 . 1 . . . . . . . . . 4988 1 196 . 1 1 28 28 LYS HE2 H 1 2.91 0.02 . 1 . . . . . . . . . 4988 1 197 . 1 1 28 28 LYS HE3 H 1 2.91 0.02 . 1 . . . . . . . . . 4988 1 198 . 1 1 29 29 CYS H H 1 8.90 0.02 . 1 . . . . . . . . . 4988 1 199 . 1 1 29 29 CYS HA H 1 5.07 0.02 . 1 . . . . . . . . . 4988 1 200 . 1 1 29 29 CYS HB2 H 1 3.01 0.02 . 2 . . . . . . . . . 4988 1 201 . 1 1 29 29 CYS HB3 H 1 3.10 0.02 . 2 . . . . . . . . . 4988 1 202 . 1 1 30 30 LYS H H 1 9.68 0.02 . 1 . . . . . . . . . 4988 1 203 . 1 1 30 30 LYS HA H 1 4.41 0.02 . 1 . . . . . . . . . 4988 1 204 . 1 1 30 30 LYS HB2 H 1 1.52 0.02 . 2 . . . . . . . . . 4988 1 205 . 1 1 30 30 LYS HB3 H 1 1.66 0.02 . 2 . . . . . . . . . 4988 1 206 . 1 1 30 30 LYS HG2 H 1 1.01 0.02 . 2 . . . . . . . . . 4988 1 207 . 1 1 30 30 LYS HG3 H 1 1.14 0.02 . 2 . . . . . . . . . 4988 1 208 . 1 1 30 30 LYS HD2 H 1 1.54 0.02 . 1 . . . . . . . . . 4988 1 209 . 1 1 30 30 LYS HD3 H 1 1.54 0.02 . 1 . . . . . . . . . 4988 1 210 . 1 1 30 30 LYS HE2 H 1 2.76 0.02 . 1 . . . . . . . . . 4988 1 211 . 1 1 30 30 LYS HE3 H 1 2.76 0.02 . 1 . . . . . . . . . 4988 1 212 . 1 1 31 31 PHE H H 1 9.10 0.02 . 1 . . . . . . . . . 4988 1 213 . 1 1 31 31 PHE HA H 1 4.34 0.02 . 1 . . . . . . . . . 4988 1 214 . 1 1 31 31 PHE HB2 H 1 3.26 0.02 . 2 . . . . . . . . . 4988 1 215 . 1 1 31 31 PHE HB3 H 1 3.32 0.02 . 2 . . . . . . . . . 4988 1 216 . 1 1 31 31 PHE HD1 H 1 7.30 0.02 . 1 . . . . . . . . . 4988 1 217 . 1 1 31 31 PHE HD2 H 1 7.30 0.02 . 1 . . . . . . . . . 4988 1 218 . 1 1 31 31 PHE HE1 H 1 7.41 0.02 . 1 . . . . . . . . . 4988 1 219 . 1 1 31 31 PHE HE2 H 1 7.41 0.02 . 1 . . . . . . . . . 4988 1 220 . 1 1 31 31 PHE HZ H 1 7.35 0.02 . 1 . . . . . . . . . 4988 1 221 . 1 1 32 32 ASN H H 1 8.76 0.02 . 1 . . . . . . . . . 4988 1 222 . 1 1 32 32 ASN HA H 1 4.29 0.02 . 1 . . . . . . . . . 4988 1 223 . 1 1 32 32 ASN HB2 H 1 2.56 0.02 . 2 . . . . . . . . . 4988 1 224 . 1 1 32 32 ASN HB3 H 1 3.65 0.02 . 2 . . . . . . . . . 4988 1 225 . 1 1 32 32 ASN HD21 H 1 7.29 0.02 . 2 . . . . . . . . . 4988 1 226 . 1 1 32 32 ASN HD22 H 1 7.89 0.02 . 2 . . . . . . . . . 4988 1 227 . 1 1 33 33 MET H H 1 7.90 0.02 . 1 . . . . . . . . . 4988 1 228 . 1 1 33 33 MET HA H 1 5.06 0.02 . 1 . . . . . . . . . 4988 1 229 . 1 1 33 33 MET HB2 H 1 2.13 0.02 . 1 . . . . . . . . . 4988 1 230 . 1 1 33 33 MET HB3 H 1 2.13 0.02 . 1 . . . . . . . . . 4988 1 231 . 1 1 33 33 MET HG2 H 1 2.68 0.02 . 2 . . . . . . . . . 4988 1 232 . 1 1 33 33 MET HG3 H 1 2.76 0.02 . 2 . . . . . . . . . 4988 1 233 . 1 1 33 33 MET HE1 H 1 2.16 0.02 . 1 . . . . . . . . . 4988 1 234 . 1 1 33 33 MET HE2 H 1 2.16 0.02 . 1 . . . . . . . . . 4988 1 235 . 1 1 33 33 MET HE3 H 1 2.16 0.02 . 1 . . . . . . . . . 4988 1 236 . 1 1 34 34 CYS H H 1 9.27 0.02 . 1 . . . . . . . . . 4988 1 237 . 1 1 34 34 CYS HA H 1 5.37 0.02 . 1 . . . . . . . . . 4988 1 238 . 1 1 34 34 CYS HB2 H 1 2.91 0.02 . 2 . . . . . . . . . 4988 1 239 . 1 1 34 34 CYS HB3 H 1 3.04 0.02 . 2 . . . . . . . . . 4988 1 240 . 1 1 35 35 VAL H H 1 9.87 0.02 . 1 . . . . . . . . . 4988 1 241 . 1 1 35 35 VAL HA H 1 4.80 0.02 . 1 . . . . . . . . . 4988 1 242 . 1 1 35 35 VAL HB H 1 2.18 0.02 . 1 . . . . . . . . . 4988 1 243 . 1 1 35 35 VAL HG11 H 1 1.00 0.02 . 2 . . . . . . . . . 4988 1 244 . 1 1 35 35 VAL HG12 H 1 1.00 0.02 . 2 . . . . . . . . . 4988 1 245 . 1 1 35 35 VAL HG13 H 1 1.00 0.02 . 2 . . . . . . . . . 4988 1 246 . 1 1 35 35 VAL HG21 H 1 1.07 0.02 . 2 . . . . . . . . . 4988 1 247 . 1 1 35 35 VAL HG22 H 1 1.07 0.02 . 2 . . . . . . . . . 4988 1 248 . 1 1 35 35 VAL HG23 H 1 1.07 0.02 . 2 . . . . . . . . . 4988 1 249 . 1 1 36 36 LYS H H 1 8.13 0.02 . 1 . . . . . . . . . 4988 1 250 . 1 1 36 36 LYS HA H 1 3.30 0.02 . 1 . . . . . . . . . 4988 1 251 . 1 1 36 36 LYS HB2 H 1 0.40 0.02 . 2 . . . . . . . . . 4988 1 252 . 1 1 36 36 LYS HB3 H 1 1.23 0.02 . 2 . . . . . . . . . 4988 1 253 . 1 1 36 36 LYS HG2 H 1 0.54 0.02 . 2 . . . . . . . . . 4988 1 254 . 1 1 36 36 LYS HG3 H 1 0.74 0.02 . 2 . . . . . . . . . 4988 1 255 . 1 1 36 36 LYS HD2 H 1 1.15 0.02 . 1 . . . . . . . . . 4988 1 256 . 1 1 36 36 LYS HD3 H 1 1.15 0.02 . 1 . . . . . . . . . 4988 1 257 . 1 1 36 36 LYS HE2 H 1 2.79 0.02 . 1 . . . . . . . . . 4988 1 258 . 1 1 36 36 LYS HE3 H 1 2.79 0.02 . 1 . . . . . . . . . 4988 1 259 . 1 1 37 37 VAL H H 1 7.58 0.02 . 1 . . . . . . . . . 4988 1 260 . 1 1 37 37 VAL HA H 1 3.82 0.02 . 1 . . . . . . . . . 4988 1 261 . 1 1 37 37 VAL HB H 1 1.96 0.02 . 1 . . . . . . . . . 4988 1 262 . 1 1 37 37 VAL HG11 H 1 0.76 0.02 . 2 . . . . . . . . . 4988 1 263 . 1 1 37 37 VAL HG12 H 1 0.76 0.02 . 2 . . . . . . . . . 4988 1 264 . 1 1 37 37 VAL HG13 H 1 0.76 0.02 . 2 . . . . . . . . . 4988 1 265 . 1 1 37 37 VAL HG21 H 1 0.85 0.02 . 2 . . . . . . . . . 4988 1 266 . 1 1 37 37 VAL HG22 H 1 0.85 0.02 . 2 . . . . . . . . . 4988 1 267 . 1 1 37 37 VAL HG23 H 1 0.85 0.02 . 2 . . . . . . . . . 4988 1 stop_ save_