data_4930 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4930 _Entry.Title ; 1H and 15N Chemical Shift Assignments for the homodimer of human TFF1 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2000-12-22 _Entry.Accession_date 2000-12-22 _Entry.Last_release_date 2000-12-22 _Entry.Original_release_date 2000-12-22 _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 Mark Williams . A. . . 4930 2 Bruce Westley . R. . . 4930 3 Felicity May . E.B. . . 4930 4 James Feeney . . . . 4930 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4930 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 59 4930 '1H chemical shifts' 386 4930 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 . . 2001-01-04 . original BMRB . 4930 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4930 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 21184346 _Citation.DOI . _Citation.PubMed_ID 11286998 _Citation.Full_citation . _Citation.Title ; The Solution Structure of the Disulphide-linked Homodimer of the Human Trefoil Protein TFF1 ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'FEBS Lett.' _Citation.Journal_name_full . _Citation.Journal_volume 493 _Citation.Journal_issue 2-3 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 70 _Citation.Page_last 74 _Citation.Year 2001 _Citation.Details ; Assignments are based on those derived earlier from a monomeric variant of the protein Polshakov et al. (1995 & 1997) see references ref_1 and ref_2. ; 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 Mark Williams . A. . . 4930 1 2 Bruce Westley . R. . . 4930 1 3 Felicity May . E.B. . . 4930 1 4 James Feeney . . . . 4930 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID TFF1 4930 1 pNR-2 4930 1 ps2 4930 1 trefoil 4930 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4930 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9096235 _Citation.Full_citation ; Polshakov VI, Williams MA, Gargaro AR, Frenkiel TA, Westley BR, Chadwick MP, May FE, Feeney J. High-resolution solution structure of human pNR-2/pS2: a single trefoil motif protein. J Mol Biol. 1997 Mar 28;267(2):418-32. ; _Citation.Title ; High-resolution solution structure of human pNR-2/pS2: a single trefoil motif protein. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 267 _Citation.Journal_issue 2 _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 418 _Citation.Page_last 432 _Citation.Year 1997 _Citation.Details ; pNR-2/pS2 is a 60 residue extracellular protein, which was originally discovered in human breast cancer cells, and subsequently found in other tumours and normal gastric epithelial cells. We have determined the three-dimensional solution structure of a C58S mutant of human pNR-2/pS2 using 639 distance and 137 torsion angle constraints obtained from analysis of multidimensional NMR spectra. A series of simulated annealing calculations resulted in the unambiguous determination of the protein's disulphide bonding pattern and produced a family of 19 structures consistent with the constraints. The peptide contains a single "trefoil" sequence motif, a region of about 40 residues with a characteristic sequence pattern, which has been found, either singly or as a repeat, in about a dozen extracellular proteins. The trefoil domain contains three disulphide bonds, whose 1-5, 2-4 and 3-6 cysteine pairings form the structure into three closely packed loops with only a small amount of secondary structure, which consists of a short alpha-helix packed against a two-stranded antiparallel beta-sheet. The structure of the domain is very similar to those of the two trefoil domains that occur in porcine spasmolytic polypeptide (PSP), the only member of the trefoil family whose three-dimensional structure has been previously determined. Outside the trefoil domain, which forms the compact "head" of the molecule, the N and C-terminal strands are closely associated, forming an extended "tail", which has some beta-sheet character for part of its length and which becomes more disordered towards the termini as indicated by (15)N{(1)H} NOEs. We have considered the structural implications of the possible formation of a native C58-C58 disulphide-bonded homodimer. Comparison of the surface features of pNR-2/pS2 and PSP, and consideration of the sequences of the other human trefoil domains in the light of these structures, illuminates the possible role of specific residues in ligand/receptor binding. ; 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 'V I' Polshakov V. I. . . 4930 2 2 'M A' Williams M. A. . . 4930 2 3 'A R' Gargaro A. R. . . 4930 2 4 'T A' Frenkiel T. A. . . 4930 2 5 'B R' Westley B. R. . . 4930 2 6 'M P' Chadwick M. P. . . 4930 2 7 'F E' May F. E. . . 4930 2 8 J Feeney J. . . . 4930 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4930 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8521850 _Citation.Full_citation ; Polshakov VI, Frenkiel TA, Westley B, Chadwick M, May F, Carr MD, Feeney J. NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure. Eur J Biochem. 1995 Nov 1;233(3):847-55. ; _Citation.Title ; NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full 'European journal of biochemistry / FEBS' _Citation.Journal_volume 233 _Citation.Journal_issue 3 _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 847 _Citation.Page_last 855 _Citation.Year 1995 _Citation.Details ; NMR spectroscopy measurements have been used to obtain structural information about the pNR-2/pS2 single-domain trefoil peptide. NMR data from 2D (two dimensional) double-quantum-filtered correlation spectroscopy (DQF-COSY), total correlation spectroscopy (TOCSY), NOE spectroscopy (NOESY), rotating frame NOE spectroscopy (ROESY) and 2D 13C-1H heteronuclear single-quantum coherence (HSQC) and 13C-1H HSQC-TOCSY spectra have been analysed to provide essentially complete 1H and 13C sequence-specific assignments for the pNR-2/pS2 protein. From a consideration of the NOE intensities, 3J(NH-alpha CH) coupling constants, 1H and 13C chemical shifts of backbone atoms and amide-proton exchange rates, the pNR-2/pS2 was found to contain two short antiparallel beta-strands (32-35 and 43-46), a short helix (25-30) and a type I beta-turn (11-15). These elements of secondary structure are very similar to those found in the two trefoil domains of pSP for which detailed structural information is already available. Similar 1H chemical shifts were noted for several conserved residues in pNR-2/pS2 and pSP and a characteristic Phe residue with a slowly flipping ring was found in the pNR-2/pS2 variant and in both domains of pSP. The tertiary structures of the domains therefore appear to be very similar in the two proteins and it is likely that the pNR-2/pS2 has the same pattern of disulphide bonds (1-5, 2-4, 3-6) as pSP. Correlation time measurements derived from 1H-1H NOE measurements indicate that the Cys58-->Ser form of the pNR-2/pS2 protein used in this study is monomeric in solution at approximately 2 mM. ; 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 'V I' Polshakov V. I. . . 4930 3 2 'T A' Frenkiel T. A. . . 4930 3 3 B Westley B. . . . 4930 3 4 M Chadwick M. . . . 4930 3 5 F May F. . . . 4930 3 6 'M D' Carr M. D. . . 4930 3 7 J Feeney J. . . . 4930 3 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_TFF1 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_TFF1 _Assembly.Entry_ID 4930 _Assembly.ID 1 _Assembly.Name 'Human Trefoil Factor Family 1 protein homodimer' _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 'disulfide bound and free' _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 dimer 4930 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'subunit 1' 1 $TFF1_monomer . . . native . . 1 . . 4930 1 2 'subunit 2' 1 $TFF1_monomer . . . native . . 1 . . 4930 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 disulphide single . 1 . 1 CYS 7 7 SG . 1 . 1 CYS 33 33 SG . . . . . . . . . . . . 4930 1 2 disulphide single . 1 . 1 CYS 17 17 SG . 1 . 1 CYS 32 32 SG . . . . . . . . . . . . 4930 1 3 disulphide single . 1 . 1 CYS 27 27 SG . 1 . 1 CYS 44 44 SG . . . . . . . . . . . . 4930 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 1PS2 . . . . . 'This structure is a monomeric variant of the molecule here' 4930 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Human Trefoil Factor Family 1 protein homodimer' system 4930 1 TFF1 abbreviation 4930 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'growth factor' 4930 1 motogen 4930 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_TFF1_monomer _Entity.Sf_category entity _Entity.Sf_framecode TFF1_monomer _Entity.Entry_ID 4930 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Trefoil Factor Family 1' _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 ; EAQTETCTVAPRERQNCGFP GVTPSQCANKGCCFDDTVRG VPWCFYPNTIDVPPEEECEF ; _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 'disulfide bound and free' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _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 4933 . 'Trefoil Factor Family 1' . . . . . 100.00 60 98.33 98.33 3.02e-26 . . . . 4930 1 . no PDB 1HI7 . 'Nmr Solution Structure Of The Disulphide-Linked Homodimer Of Human Tff1, 10 Structures' . . . . . 100.00 60 100.00 100.00 7.20e-27 . . . . 4930 1 . no PDB 1PS2 . 'High Resolution Nmr Solution Structure Of Human Ps2, 19 Structures' . . . . . 100.00 60 98.33 98.33 3.02e-26 . . . . 4930 1 . no DBJ BAA95532 . 'trefoil factor, BCE1 [Homo sapiens]' . . . . . 100.00 84 100.00 100.00 3.98e-28 . . . . 4930 1 . no DBJ BAB13729 . 'trefoil factor 1 [Homo sapiens]' . . . . . 100.00 84 100.00 100.00 3.98e-28 . . . . 4930 1 . no EMBL CAA25155 . 'unnamed protein product [Homo sapiens]' . . . . . 100.00 84 100.00 100.00 3.98e-28 . . . . 4930 1 . no EMBL CAA28695 . 'pS2 [Homo sapiens]' . . . . . 100.00 84 100.00 100.00 3.98e-28 . . . . 4930 1 . no EMBL CAA36254 . 'pS2 protein [Homo sapiens]' . . . . . 100.00 84 100.00 100.00 3.98e-28 . . . . 4930 1 . no GenBank AAA52402 . 'estrogen receptor' . . . . . 100.00 83 100.00 100.00 4.78e-28 . . . . 4930 1 . no GenBank AAH32811 . 'Trefoil factor 1 [Homo sapiens]' . . . . . 100.00 84 100.00 100.00 3.98e-28 . . . . 4930 1 . no GenBank AAX36234 . 'trefoil factor 1 [synthetic construct]' . . . . . 100.00 84 100.00 100.00 3.98e-28 . . . . 4930 1 . no GenBank AAX36702 . 'trefoil factor 1 [synthetic construct]' . . . . . 100.00 85 100.00 100.00 3.07e-28 . . . . 4930 1 . no GenBank AAX41076 . 'trefoil factor 1 [synthetic construct]' . . . . . 100.00 84 100.00 100.00 3.98e-28 . . . . 4930 1 . no PRF 1502207A . 'pS2 protein' . . . . . 100.00 84 100.00 100.00 3.98e-28 . . . . 4930 1 . no PRF 1716375A . 'estrogen-regulated protein pNR-2' . . . . . 100.00 84 100.00 100.00 3.98e-28 . . . . 4930 1 . no REF NP_003216 . 'trefoil factor 1 precursor [Homo sapiens]' . . . . . 100.00 84 100.00 100.00 3.98e-28 . . . . 4930 1 . no SWISS-PROT P04155 . 'Trefoil factor 1 precursor (pS2 protein) (HP1.A) (Breast cancer estrogen-inducible protein) (PNR-2)' . . . . . 100.00 84 100.00 100.00 3.98e-28 . . . . 4930 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID TFF1 abbreviation 4930 1 'Trefoil Factor Family 1' common 4930 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 . GLU . 4930 1 2 . ALA . 4930 1 3 . GLN . 4930 1 4 . THR . 4930 1 5 . GLU . 4930 1 6 . THR . 4930 1 7 . CYS . 4930 1 8 . THR . 4930 1 9 . VAL . 4930 1 10 . ALA . 4930 1 11 . PRO . 4930 1 12 . ARG . 4930 1 13 . GLU . 4930 1 14 . ARG . 4930 1 15 . GLN . 4930 1 16 . ASN . 4930 1 17 . CYS . 4930 1 18 . GLY . 4930 1 19 . PHE . 4930 1 20 . PRO . 4930 1 21 . GLY . 4930 1 22 . VAL . 4930 1 23 . THR . 4930 1 24 . PRO . 4930 1 25 . SER . 4930 1 26 . GLN . 4930 1 27 . CYS . 4930 1 28 . ALA . 4930 1 29 . ASN . 4930 1 30 . LYS . 4930 1 31 . GLY . 4930 1 32 . CYS . 4930 1 33 . CYS . 4930 1 34 . PHE . 4930 1 35 . ASP . 4930 1 36 . ASP . 4930 1 37 . THR . 4930 1 38 . VAL . 4930 1 39 . ARG . 4930 1 40 . GLY . 4930 1 41 . VAL . 4930 1 42 . PRO . 4930 1 43 . TRP . 4930 1 44 . CYS . 4930 1 45 . PHE . 4930 1 46 . TYR . 4930 1 47 . PRO . 4930 1 48 . ASN . 4930 1 49 . THR . 4930 1 50 . ILE . 4930 1 51 . ASP . 4930 1 52 . VAL . 4930 1 53 . PRO . 4930 1 54 . PRO . 4930 1 55 . GLU . 4930 1 56 . GLU . 4930 1 57 . GLU . 4930 1 58 . CYS . 4930 1 59 . GLU . 4930 1 60 . PHE . 4930 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 . GLU 1 1 4930 1 . ALA 2 2 4930 1 . GLN 3 3 4930 1 . THR 4 4 4930 1 . GLU 5 5 4930 1 . THR 6 6 4930 1 . CYS 7 7 4930 1 . THR 8 8 4930 1 . VAL 9 9 4930 1 . ALA 10 10 4930 1 . PRO 11 11 4930 1 . ARG 12 12 4930 1 . GLU 13 13 4930 1 . ARG 14 14 4930 1 . GLN 15 15 4930 1 . ASN 16 16 4930 1 . CYS 17 17 4930 1 . GLY 18 18 4930 1 . PHE 19 19 4930 1 . PRO 20 20 4930 1 . GLY 21 21 4930 1 . VAL 22 22 4930 1 . THR 23 23 4930 1 . PRO 24 24 4930 1 . SER 25 25 4930 1 . GLN 26 26 4930 1 . CYS 27 27 4930 1 . ALA 28 28 4930 1 . ASN 29 29 4930 1 . LYS 30 30 4930 1 . GLY 31 31 4930 1 . CYS 32 32 4930 1 . CYS 33 33 4930 1 . PHE 34 34 4930 1 . ASP 35 35 4930 1 . ASP 36 36 4930 1 . THR 37 37 4930 1 . VAL 38 38 4930 1 . ARG 39 39 4930 1 . GLY 40 40 4930 1 . VAL 41 41 4930 1 . PRO 42 42 4930 1 . TRP 43 43 4930 1 . CYS 44 44 4930 1 . PHE 45 45 4930 1 . TYR 46 46 4930 1 . PRO 47 47 4930 1 . ASN 48 48 4930 1 . THR 49 49 4930 1 . ILE 50 50 4930 1 . ASP 51 51 4930 1 . VAL 52 52 4930 1 . PRO 53 53 4930 1 . PRO 54 54 4930 1 . GLU 55 55 4930 1 . GLU 56 56 4930 1 . GLU 57 57 4930 1 . CYS 58 58 4930 1 . GLU 59 59 4930 1 . PHE 60 60 4930 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 4930 _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 $TFF1_monomer . 9606 . . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . 'Breast, Stomach' epithelial . 'Mcf-7, Uacl' . . . . . TFF1 . 4930 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 4930 _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 $TFF1_monomer . 'recombinant technology' 'Escherichia coli' 'E. Coli' . . Escherichia coli BL21(DE3) . . plasmid . . 'Pezz18 (Pharmacia)' . . . 4930 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4930 _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 'Trefoil Factor Family 1' 'U-95% 15N' . . 1 $TFF1_monomer . . 2 . . mM . . . . 4930 1 2 'sodium phosphate' . . . . . . . 5 . . mM . . . . 4930 1 stop_ save_ ####################### # Sample conditions # ####################### save_cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode cond_1 _Sample_condition_list.Entry_ID 4930 _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' 0.01 0.003 M 4930 1 pH 5.9 0.2 n/a 4930 1 temperature 298 1 K 4930 1 stop_ save_ save_cond_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode cond_2 _Sample_condition_list.Entry_ID 4930 _Sample_condition_list.ID 2 _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' 0.01 0.003 M 4930 2 pH 5.9 0.2 n/a 4930 2 temperature 283 1 K 4930 2 stop_ 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 4930 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model UNITY _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 4930 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model 'UNITY PLUS' _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 4930 _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 Varian UNITY . 600 . . . 4930 1 2 NMR_spectrometer_2 Varian 'UNITY PLUS' . 500 . . . 4930 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 4930 _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 TOCSY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4930 1 2 NOESY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4930 1 3 ROESY . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4930 1 4 '15N-1H HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4930 1 5 '15N-1H HSQC-NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4930 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 4930 _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 DSS 'methyl protons' . . . . ppm 0.0 internal direct . . . . . . 4930 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . 4930 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 4930 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $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 TOCSY 1 $sample_1 . 4930 1 2 NOESY 1 $sample_1 . 4930 1 3 ROESY 1 $sample_1 . 4930 1 4 '15N-1H HSQC' 1 $sample_1 . 4930 1 5 '15N-1H HSQC-NOESY' 1 $sample_1 . 4930 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 GLU HA H 1 4.05 0.01 . 1 . . . . . . . . . 4930 1 2 . 1 1 1 1 GLU HB2 H 1 2.14 0.01 . 2 . . . . . . . . . 4930 1 3 . 1 1 1 1 GLU HB3 H 1 2.08 0.01 . 2 . . . . . . . . . 4930 1 4 . 1 1 1 1 GLU HG2 H 1 2.40 0.01 . 1 . . . . . . . . . 4930 1 5 . 1 1 1 1 GLU HG3 H 1 2.40 0.01 . 1 . . . . . . . . . 4930 1 6 . 1 1 2 2 ALA H H 1 8.80 0.01 . 1 . . . . . . . . . 4930 1 7 . 1 1 2 2 ALA HA H 1 4.38 0.01 . 1 . . . . . . . . . 4930 1 8 . 1 1 2 2 ALA HB1 H 1 1.39 0.01 . 1 . . . . . . . . . 4930 1 9 . 1 1 2 2 ALA HB2 H 1 1.39 0.01 . 1 . . . . . . . . . 4930 1 10 . 1 1 2 2 ALA HB3 H 1 1.39 0.01 . 1 . . . . . . . . . 4930 1 11 . 1 1 2 2 ALA N N 15 125.7 0.05 . 1 . . . . . . . . . 4930 1 12 . 1 1 3 3 GLN H H 1 8.53 0.01 . 1 . . . . . . . . . 4930 1 13 . 1 1 3 3 GLN HA H 1 4.54 0.01 . 1 . . . . . . . . . 4930 1 14 . 1 1 3 3 GLN HB2 H 1 2.13 0.01 . 1 . . . . . . . . . 4930 1 15 . 1 1 3 3 GLN HB3 H 1 2.00 0.01 . 1 . . . . . . . . . 4930 1 16 . 1 1 3 3 GLN HG2 H 1 2.40 0.01 . 1 . . . . . . . . . 4930 1 17 . 1 1 3 3 GLN HG3 H 1 2.40 0.01 . 1 . . . . . . . . . 4930 1 18 . 1 1 3 3 GLN HE21 H 1 7.59 0.01 . 2 . . . . . . . . . 4930 1 19 . 1 1 3 3 GLN HE22 H 1 6.85 0.01 . 2 . . . . . . . . . 4930 1 20 . 1 1 3 3 GLN N N 15 120.0 0.05 . 1 . . . . . . . . . 4930 1 21 . 1 1 3 3 GLN NE2 N 15 112.25 0.05 . 1 . . . . . . . . . 4930 1 22 . 1 1 4 4 THR H H 1 8.37 0.01 . 1 . . . . . . . . . 4930 1 23 . 1 1 4 4 THR HA H 1 4.80 0.01 . 1 . . . . . . . . . 4930 1 24 . 1 1 4 4 THR HB H 1 4.38 0.01 . 1 . . . . . . . . . 4930 1 25 . 1 1 4 4 THR HG21 H 1 1.20 0.01 . 1 . . . . . . . . . 4930 1 26 . 1 1 4 4 THR HG22 H 1 1.20 0.01 . 1 . . . . . . . . . 4930 1 27 . 1 1 4 4 THR HG23 H 1 1.20 0.01 . 1 . . . . . . . . . 4930 1 28 . 1 1 4 4 THR N N 15 114.65 0.05 . 1 . . . . . . . . . 4930 1 29 . 1 1 5 5 GLU H H 1 8.56 0.01 . 1 . . . . . . . . . 4930 1 30 . 1 1 5 5 GLU HA H 1 4.73 0.01 . 1 . . . . . . . . . 4930 1 31 . 1 1 5 5 GLU HB2 H 1 2.04 0.01 . 1 . . . . . . . . . 4930 1 32 . 1 1 5 5 GLU HB3 H 1 1.98 0.01 . 1 . . . . . . . . . 4930 1 33 . 1 1 5 5 GLU HG2 H 1 2.28 0.01 . 1 . . . . . . . . . 4930 1 34 . 1 1 5 5 GLU HG3 H 1 2.28 0.01 . 1 . . . . . . . . . 4930 1 35 . 1 1 5 5 GLU N N 15 122.35 0.05 . 1 . . . . . . . . . 4930 1 36 . 1 1 6 6 THR H H 1 8.34 0.01 . 1 . . . . . . . . . 4930 1 37 . 1 1 6 6 THR HA H 1 4.62 0.01 . 1 . . . . . . . . . 4930 1 38 . 1 1 6 6 THR HB H 1 4.23 0.01 . 1 . . . . . . . . . 4930 1 39 . 1 1 6 6 THR HG21 H 1 1.23 0.01 . 1 . . . . . . . . . 4930 1 40 . 1 1 6 6 THR HG22 H 1 1.23 0.01 . 1 . . . . . . . . . 4930 1 41 . 1 1 6 6 THR HG23 H 1 1.23 0.01 . 1 . . . . . . . . . 4930 1 42 . 1 1 6 6 THR N N 15 112.6 0.05 . 1 . . . . . . . . . 4930 1 43 . 1 1 7 7 CYS H H 1 8.24 0.01 . 1 . . . . . . . . . 4930 1 44 . 1 1 7 7 CYS HA H 1 5.30 0.01 . 1 . . . . . . . . . 4930 1 45 . 1 1 7 7 CYS HB2 H 1 3.50 0.01 . 1 . . . . . . . . . 4930 1 46 . 1 1 7 7 CYS HB3 H 1 2.81 0.01 . 1 . . . . . . . . . 4930 1 47 . 1 1 7 7 CYS N N 15 118.3 0.05 . 1 . . . . . . . . . 4930 1 48 . 1 1 8 8 THR H H 1 8.11 0.01 . 1 . . . . . . . . . 4930 1 49 . 1 1 8 8 THR HA H 1 4.28 0.01 . 1 . . . . . . . . . 4930 1 50 . 1 1 8 8 THR HB H 1 4.36 0.01 . 1 . . . . . . . . . 4930 1 51 . 1 1 8 8 THR HG21 H 1 1.20 0.01 . 1 . . . . . . . . . 4930 1 52 . 1 1 8 8 THR HG22 H 1 1.20 0.01 . 1 . . . . . . . . . 4930 1 53 . 1 1 8 8 THR HG23 H 1 1.20 0.01 . 1 . . . . . . . . . 4930 1 54 . 1 1 8 8 THR N N 15 119.05 0.05 . 1 . . . . . . . . . 4930 1 55 . 1 1 9 9 VAL H H 1 7.43 0.01 . 1 . . . . . . . . . 4930 1 56 . 1 1 9 9 VAL HA H 1 4.07 0.01 . 1 . . . . . . . . . 4930 1 57 . 1 1 9 9 VAL HB H 1 1.72 0.01 . 1 . . . . . . . . . 4930 1 58 . 1 1 9 9 VAL HG11 H 1 0.93 0.01 . 1 . . . . . . . . . 4930 1 59 . 1 1 9 9 VAL HG12 H 1 0.93 0.01 . 1 . . . . . . . . . 4930 1 60 . 1 1 9 9 VAL HG13 H 1 0.93 0.01 . 1 . . . . . . . . . 4930 1 61 . 1 1 9 9 VAL HG21 H 1 1.14 0.01 . 1 . . . . . . . . . 4930 1 62 . 1 1 9 9 VAL HG22 H 1 1.14 0.01 . 1 . . . . . . . . . 4930 1 63 . 1 1 9 9 VAL HG23 H 1 1.14 0.01 . 1 . . . . . . . . . 4930 1 64 . 1 1 9 9 VAL N N 15 127.2 0.05 . 1 . . . . . . . . . 4930 1 65 . 1 1 10 10 ALA H H 1 9.07 0.01 . 1 . . . . . . . . . 4930 1 66 . 1 1 10 10 ALA HA H 1 4.35 0.01 . 1 . . . . . . . . . 4930 1 67 . 1 1 10 10 ALA HB1 H 1 1.33 0.01 . 1 . . . . . . . . . 4930 1 68 . 1 1 10 10 ALA HB2 H 1 1.33 0.01 . 1 . . . . . . . . . 4930 1 69 . 1 1 10 10 ALA HB3 H 1 1.33 0.01 . 1 . . . . . . . . . 4930 1 70 . 1 1 10 10 ALA N N 15 133.85 0.05 . 1 . . . . . . . . . 4930 1 71 . 1 1 11 11 PRO HA H 1 3.51 0.01 . 1 . . . . . . . . . 4930 1 72 . 1 1 11 11 PRO HB2 H 1 2.08 0.01 . 1 . . . . . . . . . 4930 1 73 . 1 1 11 11 PRO HB3 H 1 2.01 0.01 . 1 . . . . . . . . . 4930 1 74 . 1 1 11 11 PRO HG2 H 1 2.24 0.01 . 2 . . . . . . . . . 4930 1 75 . 1 1 11 11 PRO HG3 H 1 1.76 0.01 . 2 . . . . . . . . . 4930 1 76 . 1 1 11 11 PRO HD2 H 1 3.85 0.01 . 1 . . . . . . . . . 4930 1 77 . 1 1 11 11 PRO HD3 H 1 3.73 0.01 . 1 . . . . . . . . . 4930 1 78 . 1 1 12 12 ARG H H 1 8.61 0.01 . 1 . . . . . . . . . 4930 1 79 . 1 1 12 12 ARG HA H 1 4.11 0.01 . 1 . . . . . . . . . 4930 1 80 . 1 1 12 12 ARG HB2 H 1 1.86 0.01 . 1 . . . . . . . . . 4930 1 81 . 1 1 12 12 ARG HB3 H 1 1.86 0.01 . 1 . . . . . . . . . 4930 1 82 . 1 1 12 12 ARG HG2 H 1 1.61 0.01 . 1 . . . . . . . . . 4930 1 83 . 1 1 12 12 ARG HG3 H 1 1.61 0.01 . 1 . . . . . . . . . 4930 1 84 . 1 1 12 12 ARG HD2 H 1 3.17 0.01 . 1 . . . . . . . . . 4930 1 85 . 1 1 12 12 ARG HD3 H 1 3.17 0.01 . 1 . . . . . . . . . 4930 1 86 . 1 1 12 12 ARG HE H 1 7.29 0.01 . 1 . . . . . . . . . 4930 1 87 . 1 1 12 12 ARG N N 15 113.05 0.05 . 1 . . . . . . . . . 4930 1 88 . 1 1 13 13 GLU H H 1 8.01 0.01 . 1 . . . . . . . . . 4930 1 89 . 1 1 13 13 GLU HA H 1 4.38 0.01 . 1 . . . . . . . . . 4930 1 90 . 1 1 13 13 GLU HB2 H 1 2.25 0.01 . 1 . . . . . . . . . 4930 1 91 . 1 1 13 13 GLU HB3 H 1 1.89 0.01 . 1 . . . . . . . . . 4930 1 92 . 1 1 13 13 GLU HG2 H 1 2.20 0.01 . 1 . . . . . . . . . 4930 1 93 . 1 1 13 13 GLU HG3 H 1 2.20 0.01 . 1 . . . . . . . . . 4930 1 94 . 1 1 13 13 GLU N N 15 116.5 0.05 . 1 . . . . . . . . . 4930 1 95 . 1 1 14 14 ARG H H 1 7.00 0.01 . 1 . . . . . . . . . 4930 1 96 . 1 1 14 14 ARG HA H 1 4.18 0.01 . 1 . . . . . . . . . 4930 1 97 . 1 1 14 14 ARG HB2 H 1 1.20 0.01 . 1 . . . . . . . . . 4930 1 98 . 1 1 14 14 ARG HB3 H 1 1.52 0.01 . 1 . . . . . . . . . 4930 1 99 . 1 1 14 14 ARG HG2 H 1 1.60 0.01 . 1 . . . . . . . . . 4930 1 100 . 1 1 14 14 ARG HG3 H 1 0.37 0.01 . 1 . . . . . . . . . 4930 1 101 . 1 1 14 14 ARG HD2 H 1 1.78 0.01 . 1 . . . . . . . . . 4930 1 102 . 1 1 14 14 ARG HD3 H 1 2.30 0.01 . 1 . . . . . . . . . 4930 1 103 . 1 1 14 14 ARG HE H 1 5.54 0.01 . 1 . . . . . . . . . 4930 1 104 . 1 1 14 14 ARG HH11 H 1 6.74 0.01 . 1 . . . . . . . . . 4930 1 105 . 1 1 14 14 ARG HH12 H 1 6.74 0.01 . 1 . . . . . . . . . 4930 1 106 . 1 1 14 14 ARG HH21 H 1 7.13 0.01 . 2 . . . . . . . . . 4930 1 107 . 1 1 14 14 ARG HH22 H 1 7.40 0.01 . 2 . . . . . . . . . 4930 1 108 . 1 1 14 14 ARG N N 15 119.55 0.05 . 1 . . . . . . . . . 4930 1 109 . 1 1 15 15 GLN H H 1 9.94 0.01 . 1 . . . . . . . . . 4930 1 110 . 1 1 15 15 GLN HA H 1 4.63 0.01 . 1 . . . . . . . . . 4930 1 111 . 1 1 15 15 GLN HB2 H 1 2.31 0.01 . 1 . . . . . . . . . 4930 1 112 . 1 1 15 15 GLN HB3 H 1 2.31 0.01 . 1 . . . . . . . . . 4930 1 113 . 1 1 15 15 GLN HG2 H 1 2.57 0.01 . 2 . . . . . . . . . 4930 1 114 . 1 1 15 15 GLN HG3 H 1 2.45 0.01 . 2 . . . . . . . . . 4930 1 115 . 1 1 15 15 GLN HE21 H 1 6.84 0.01 . 2 . . . . . . . . . 4930 1 116 . 1 1 15 15 GLN HE22 H 1 7.45 0.01 . 2 . . . . . . . . . 4930 1 117 . 1 1 15 15 GLN N N 15 124.6 0.05 . 1 . . . . . . . . . 4930 1 118 . 1 1 15 15 GLN NE2 N 15 112.55 0.05 . 1 . . . . . . . . . 4930 1 119 . 1 1 16 16 ASN H H 1 9.05 0.01 . 1 . . . . . . . . . 4930 1 120 . 1 1 16 16 ASN HA H 1 4.49 0.01 . 1 . . . . . . . . . 4930 1 121 . 1 1 16 16 ASN HB2 H 1 2.99 0.01 . 1 . . . . . . . . . 4930 1 122 . 1 1 16 16 ASN HB3 H 1 2.78 0.01 . 1 . . . . . . . . . 4930 1 123 . 1 1 16 16 ASN HD21 H 1 6.72 0.01 . 2 . . . . . . . . . 4930 1 124 . 1 1 16 16 ASN HD22 H 1 7.81 0.01 . 2 . . . . . . . . . 4930 1 125 . 1 1 16 16 ASN N N 15 121.4 0.05 . 1 . . . . . . . . . 4930 1 126 . 1 1 16 16 ASN ND2 N 15 114.35 0.05 . 1 . . . . . . . . . 4930 1 127 . 1 1 17 17 CYS H H 1 9.27 0.01 . 1 . . . . . . . . . 4930 1 128 . 1 1 17 17 CYS HA H 1 4.49 0.01 . 1 . . . . . . . . . 4930 1 129 . 1 1 17 17 CYS HB2 H 1 2.60 0.01 . 1 . . . . . . . . . 4930 1 130 . 1 1 17 17 CYS HB3 H 1 1.48 0.01 . 1 . . . . . . . . . 4930 1 131 . 1 1 17 17 CYS N N 15 126.10 0.05 . 1 . . . . . . . . . 4930 1 132 . 1 1 18 18 GLY H H 1 8.03 0.01 . 1 . . . . . . . . . 4930 1 133 . 1 1 18 18 GLY HA2 H 1 4.23 0.01 . 1 . . . . . . . . . 4930 1 134 . 1 1 18 18 GLY HA3 H 1 3.35 0.01 . 1 . . . . . . . . . 4930 1 135 . 1 1 18 18 GLY N N 15 106.9 0.05 . 1 . . . . . . . . . 4930 1 136 . 1 1 19 19 PHE H H 1 6.48 0.01 . 1 . . . . . . . . . 4930 1 137 . 1 1 19 19 PHE HA H 1 5.01 0.01 . 1 . . . . . . . . . 4930 1 138 . 1 1 19 19 PHE HB2 H 1 3.29 0.01 . 1 . . . . . . . . . 4930 1 139 . 1 1 19 19 PHE HB3 H 1 3.14 0.01 . 1 . . . . . . . . . 4930 1 140 . 1 1 19 19 PHE HD1 H 1 7.03 0.01 . 1 . . . . . . . . . 4930 1 141 . 1 1 19 19 PHE HD2 H 1 7.03 0.01 . 1 . . . . . . . . . 4930 1 142 . 1 1 19 19 PHE HE1 H 1 7.25 0.01 . 1 . . . . . . . . . 4930 1 143 . 1 1 19 19 PHE HE2 H 1 7.25 0.01 . 1 . . . . . . . . . 4930 1 144 . 1 1 19 19 PHE HZ H 1 7.24 0.01 . 1 . . . . . . . . . 4930 1 145 . 1 1 19 19 PHE N N 15 117.2 0.05 . 1 . . . . . . . . . 4930 1 146 . 1 1 20 20 PRO HA H 1 4.30 0.01 . 1 . . . . . . . . . 4930 1 147 . 1 1 20 20 PRO HB2 H 1 2.30 0.01 . 1 . . . . . . . . . 4930 1 148 . 1 1 20 20 PRO HB3 H 1 2.00 0.01 . 1 . . . . . . . . . 4930 1 149 . 1 1 20 20 PRO HG2 H 1 2.20 0.01 . 1 . . . . . . . . . 4930 1 150 . 1 1 20 20 PRO HG3 H 1 2.20 0.01 . 1 . . . . . . . . . 4930 1 151 . 1 1 20 20 PRO HD2 H 1 3.92 0.01 . 2 . . . . . . . . . 4930 1 152 . 1 1 20 20 PRO HD3 H 1 3.79 0.01 . 2 . . . . . . . . . 4930 1 153 . 1 1 21 21 GLY H H 1 8.89 0.01 . 1 . . . . . . . . . 4930 1 154 . 1 1 21 21 GLY HA2 H 1 4.31 0.01 . 1 . . . . . . . . . 4930 1 155 . 1 1 21 21 GLY HA3 H 1 3.77 0.01 . 1 . . . . . . . . . 4930 1 156 . 1 1 21 21 GLY N N 15 113.3 0.05 . 1 . . . . . . . . . 4930 1 157 . 1 1 22 22 VAL H H 1 7.53 0.01 . 1 . . . . . . . . . 4930 1 158 . 1 1 22 22 VAL HA H 1 3.93 0.01 . 1 . . . . . . . . . 4930 1 159 . 1 1 22 22 VAL HB H 1 0.84 0.01 . 1 . . . . . . . . . 4930 1 160 . 1 1 22 22 VAL HG11 H 1 1.08 0.01 . 1 . . . . . . . . . 4930 1 161 . 1 1 22 22 VAL HG12 H 1 1.08 0.01 . 1 . . . . . . . . . 4930 1 162 . 1 1 22 22 VAL HG13 H 1 1.08 0.01 . 1 . . . . . . . . . 4930 1 163 . 1 1 22 22 VAL HG21 H 1 0.84 0.01 . 1 . . . . . . . . . 4930 1 164 . 1 1 22 22 VAL HG22 H 1 0.84 0.01 . 1 . . . . . . . . . 4930 1 165 . 1 1 22 22 VAL HG23 H 1 0.84 0.01 . 1 . . . . . . . . . 4930 1 166 . 1 1 22 22 VAL N N 15 121.9 0.05 . 1 . . . . . . . . . 4930 1 167 . 1 1 23 23 THR H H 1 8.12 0.01 . 1 . . . . . . . . . 4930 1 168 . 1 1 23 23 THR HA H 1 4.83 0.01 . 1 . . . . . . . . . 4930 1 169 . 1 1 23 23 THR HB H 1 4.64 0.01 . 1 . . . . . . . . . 4930 1 170 . 1 1 23 23 THR HG1 H 1 5.41 0.01 . 1 . . . . . . . . . 4930 1 171 . 1 1 23 23 THR HG21 H 1 1.33 0.01 . 1 . . . . . . . . . 4930 1 172 . 1 1 23 23 THR HG22 H 1 1.33 0.01 . 1 . . . . . . . . . 4930 1 173 . 1 1 23 23 THR HG23 H 1 1.33 0.01 . 1 . . . . . . . . . 4930 1 174 . 1 1 23 23 THR N N 15 117.45 0.05 . 1 . . . . . . . . . 4930 1 175 . 1 1 24 24 PRO HA H 1 3.22 0.01 . 1 . . . . . . . . . 4930 1 176 . 1 1 24 24 PRO HB2 H 1 1.74 0.01 . 1 . . . . . . . . . 4930 1 177 . 1 1 24 24 PRO HB3 H 1 1.60 0.01 . 1 . . . . . . . . . 4930 1 178 . 1 1 24 24 PRO HG2 H 1 1.74 0.01 . 2 . . . . . . . . . 4930 1 179 . 1 1 24 24 PRO HG3 H 1 0.70 0.01 . 2 . . . . . . . . . 4930 1 180 . 1 1 24 24 PRO HD2 H 1 3.29 0.01 . 1 . . . . . . . . . 4930 1 181 . 1 1 24 24 PRO HD3 H 1 3.67 0.01 . 1 . . . . . . . . . 4930 1 182 . 1 1 25 25 SER H H 1 8.09 0.01 . 1 . . . . . . . . . 4930 1 183 . 1 1 25 25 SER HA H 1 4.15 0.01 . 1 . . . . . . . . . 4930 1 184 . 1 1 25 25 SER HB2 H 1 3.78 0.01 . 1 . . . . . . . . . 4930 1 185 . 1 1 25 25 SER HB3 H 1 3.78 0.01 . 1 . . . . . . . . . 4930 1 186 . 1 1 25 25 SER N N 15 112.1 0.05 . 1 . . . . . . . . . 4930 1 187 . 1 1 26 26 GLN H H 1 7.63 0.01 . 1 . . . . . . . . . 4930 1 188 . 1 1 26 26 GLN HA H 1 4.02 0.01 . 1 . . . . . . . . . 4930 1 189 . 1 1 26 26 GLN HB2 H 1 1.95 0.01 . 1 . . . . . . . . . 4930 1 190 . 1 1 26 26 GLN HB3 H 1 2.37 0.01 . 1 . . . . . . . . . 4930 1 191 . 1 1 26 26 GLN HG2 H 1 2.50 0.01 . 1 . . . . . . . . . 4930 1 192 . 1 1 26 26 GLN HG3 H 1 2.50 0.01 . 1 . . . . . . . . . 4930 1 193 . 1 1 26 26 GLN HE21 H 1 6.82 0.01 . 2 . . . . . . . . . 4930 1 194 . 1 1 26 26 GLN HE22 H 1 7.51 0.01 . 2 . . . . . . . . . 4930 1 195 . 1 1 26 26 GLN N N 15 122.15 0.05 . 1 . . . . . . . . . 4930 1 196 . 1 1 26 26 GLN NE2 N 15 109.5 0.05 . 1 . . . . . . . . . 4930 1 197 . 1 1 27 27 CYS H H 1 8.38 0.01 . 1 . . . . . . . . . 4930 1 198 . 1 1 27 27 CYS HA H 1 3.91 0.01 . 1 . . . . . . . . . 4930 1 199 . 1 1 27 27 CYS HB2 H 1 3.20 0.01 . 1 . . . . . . . . . 4930 1 200 . 1 1 27 27 CYS HB3 H 1 2.93 0.01 . 1 . . . . . . . . . 4930 1 201 . 1 1 27 27 CYS N N 15 118.0 0.05 . 1 . . . . . . . . . 4930 1 202 . 1 1 28 28 ALA H H 1 8.27 0.01 . 1 . . . . . . . . . 4930 1 203 . 1 1 28 28 ALA HA H 1 4.27 0.01 . 1 . . . . . . . . . 4930 1 204 . 1 1 28 28 ALA HB1 H 1 1.47 0.01 . 1 . . . . . . . . . 4930 1 205 . 1 1 28 28 ALA HB2 H 1 1.47 0.01 . 1 . . . . . . . . . 4930 1 206 . 1 1 28 28 ALA HB3 H 1 1.47 0.01 . 1 . . . . . . . . . 4930 1 207 . 1 1 28 28 ALA N N 15 121.45 0.05 . 1 . . . . . . . . . 4930 1 208 . 1 1 29 29 ASN H H 1 8.21 0.01 . 1 . . . . . . . . . 4930 1 209 . 1 1 29 29 ASN HA H 1 4.53 0.01 . 1 . . . . . . . . . 4930 1 210 . 1 1 29 29 ASN HB2 H 1 2.88 0.01 . 2 . . . . . . . . . 4930 1 211 . 1 1 29 29 ASN HB3 H 1 2.94 0.01 . 2 . . . . . . . . . 4930 1 212 . 1 1 29 29 ASN HD21 H 1 6.89 0.01 . 2 . . . . . . . . . 4930 1 213 . 1 1 29 29 ASN HD22 H 1 7.58 0.01 . 2 . . . . . . . . . 4930 1 214 . 1 1 29 29 ASN N N 15 118.05 0.05 . 1 . . . . . . . . . 4930 1 215 . 1 1 29 29 ASN ND2 N 15 111.35 0.05 . 1 . . . . . . . . . 4930 1 216 . 1 1 30 30 LYS H H 1 7.31 0.01 . 1 . . . . . . . . . 4930 1 217 . 1 1 30 30 LYS HA H 1 4.44 0.01 . 1 . . . . . . . . . 4930 1 218 . 1 1 30 30 LYS HB2 H 1 1.94 0.01 . 1 . . . . . . . . . 4930 1 219 . 1 1 30 30 LYS HB3 H 1 1.94 0.01 . 1 . . . . . . . . . 4930 1 220 . 1 1 30 30 LYS HG2 H 1 1.74 0.01 . 1 . . . . . . . . . 4930 1 221 . 1 1 30 30 LYS HG3 H 1 1.74 0.01 . 1 . . . . . . . . . 4930 1 222 . 1 1 30 30 LYS HD2 H 1 1.68 0.01 . 1 . . . . . . . . . 4930 1 223 . 1 1 30 30 LYS HD3 H 1 1.68 0.01 . 1 . . . . . . . . . 4930 1 224 . 1 1 30 30 LYS N N 15 117.05 0.05 . 1 . . . . . . . . . 4930 1 225 . 1 1 31 31 GLY H H 1 8.08 0.01 . 1 . . . . . . . . . 4930 1 226 . 1 1 31 31 GLY HA2 H 1 3.78 0.01 . 1 . . . . . . . . . 4930 1 227 . 1 1 31 31 GLY HA3 H 1 4.18 0.01 . 1 . . . . . . . . . 4930 1 228 . 1 1 31 31 GLY N N 15 106.55 0.05 . 1 . . . . . . . . . 4930 1 229 . 1 1 32 32 CYS H H 1 7.40 0.01 . 1 . . . . . . . . . 4930 1 230 . 1 1 32 32 CYS HA H 1 4.41 0.01 . 1 . . . . . . . . . 4930 1 231 . 1 1 32 32 CYS HB2 H 1 3.16 0.01 . 1 . . . . . . . . . 4930 1 232 . 1 1 32 32 CYS HB3 H 1 2.59 0.01 . 1 . . . . . . . . . 4930 1 233 . 1 1 32 32 CYS N N 15 117.45 0.05 . 1 . . . . . . . . . 4930 1 234 . 1 1 33 33 CYS H H 1 8.50 0.01 . 1 . . . . . . . . . 4930 1 235 . 1 1 33 33 CYS HA H 1 4.30 0.01 . 1 . . . . . . . . . 4930 1 236 . 1 1 33 33 CYS HB2 H 1 2.21 0.01 . 1 . . . . . . . . . 4930 1 237 . 1 1 33 33 CYS HB3 H 1 0.88 0.01 . 1 . . . . . . . . . 4930 1 238 . 1 1 33 33 CYS N N 15 120.05 0.05 . 1 . . . . . . . . . 4930 1 239 . 1 1 34 34 PHE H H 1 8.56 0.01 . 1 . . . . . . . . . 4930 1 240 . 1 1 34 34 PHE HA H 1 5.85 0.01 . 1 . . . . . . . . . 4930 1 241 . 1 1 34 34 PHE HB2 H 1 3.06 0.01 . 1 . . . . . . . . . 4930 1 242 . 1 1 34 34 PHE HB3 H 1 2.64 0.01 . 1 . . . . . . . . . 4930 1 243 . 1 1 34 34 PHE HD1 H 1 7.02 0.01 . 1 . . . . . . . . . 4930 1 244 . 1 1 34 34 PHE HD2 H 1 7.02 0.01 . 1 . . . . . . . . . 4930 1 245 . 1 1 34 34 PHE HE1 H 1 7.23 0.01 . 1 . . . . . . . . . 4930 1 246 . 1 1 34 34 PHE HE2 H 1 7.23 0.01 . 1 . . . . . . . . . 4930 1 247 . 1 1 34 34 PHE HZ H 1 7.39 0.01 . 1 . . . . . . . . . 4930 1 248 . 1 1 34 34 PHE N N 15 122.75 0.05 . 1 . . . . . . . . . 4930 1 249 . 1 1 35 35 ASP H H 1 9.16 0.01 . 1 . . . . . . . . . 4930 1 250 . 1 1 35 35 ASP HA H 1 4.52 0.01 . 1 . . . . . . . . . 4930 1 251 . 1 1 35 35 ASP HB2 H 1 2.78 0.01 . 1 . . . . . . . . . 4930 1 252 . 1 1 35 35 ASP HB3 H 1 3.00 0.01 . 1 . . . . . . . . . 4930 1 253 . 1 1 35 35 ASP N N 15 127.5 0.05 . 1 . . . . . . . . . 4930 1 254 . 1 1 36 36 ASP H H 1 7.93 0.01 . 1 . . . . . . . . . 4930 1 255 . 1 1 36 36 ASP HA H 1 3.03 0.01 . 1 . . . . . . . . . 4930 1 256 . 1 1 36 36 ASP HB2 H 1 1.30 0.01 . 1 . . . . . . . . . 4930 1 257 . 1 1 36 36 ASP HB3 H 1 1.18 0.01 . 1 . . . . . . . . . 4930 1 258 . 1 1 36 36 ASP N N 15 124.85 0.05 . 1 . . . . . . . . . 4930 1 259 . 1 1 37 37 THR H H 1 7.97 0.01 . 1 . . . . . . . . . 4930 1 260 . 1 1 37 37 THR HA H 1 4.00 0.01 . 1 . . . . . . . . . 4930 1 261 . 1 1 37 37 THR HB H 1 4.28 0.01 . 1 . . . . . . . . . 4930 1 262 . 1 1 37 37 THR HG21 H 1 1.24 0.01 . 1 . . . . . . . . . 4930 1 263 . 1 1 37 37 THR HG22 H 1 1.24 0.01 . 1 . . . . . . . . . 4930 1 264 . 1 1 37 37 THR HG23 H 1 1.24 0.01 . 1 . . . . . . . . . 4930 1 265 . 1 1 37 37 THR N N 15 109.2 0.05 . 1 . . . . . . . . . 4930 1 266 . 1 1 38 38 VAL H H 1 7.70 0.01 . 1 . . . . . . . . . 4930 1 267 . 1 1 38 38 VAL HA H 1 4.28 0.01 . 1 . . . . . . . . . 4930 1 268 . 1 1 38 38 VAL HB H 1 1.79 0.01 . 1 . . . . . . . . . 4930 1 269 . 1 1 38 38 VAL HG11 H 1 0.86 0.01 . 1 . . . . . . . . . 4930 1 270 . 1 1 38 38 VAL HG12 H 1 0.86 0.01 . 1 . . . . . . . . . 4930 1 271 . 1 1 38 38 VAL HG13 H 1 0.86 0.01 . 1 . . . . . . . . . 4930 1 272 . 1 1 38 38 VAL HG21 H 1 0.79 0.01 . 1 . . . . . . . . . 4930 1 273 . 1 1 38 38 VAL HG22 H 1 0.79 0.01 . 1 . . . . . . . . . 4930 1 274 . 1 1 38 38 VAL HG23 H 1 0.79 0.01 . 1 . . . . . . . . . 4930 1 275 . 1 1 38 38 VAL N N 15 121.1 0.05 . 1 . . . . . . . . . 4930 1 276 . 1 1 39 39 ARG H H 1 8.73 0.01 . 1 . . . . . . . . . 4930 1 277 . 1 1 39 39 ARG HA H 1 4.55 0.01 . 1 . . . . . . . . . 4930 1 278 . 1 1 39 39 ARG HB2 H 1 1.86 0.01 . 2 . . . . . . . . . 4930 1 279 . 1 1 39 39 ARG HB3 H 1 1.83 0.01 . 2 . . . . . . . . . 4930 1 280 . 1 1 39 39 ARG HG2 H 1 1.72 0.01 . 1 . . . . . . . . . 4930 1 281 . 1 1 39 39 ARG HG3 H 1 1.72 0.01 . 1 . . . . . . . . . 4930 1 282 . 1 1 39 39 ARG HD2 H 1 3.28 0.01 . 1 . . . . . . . . . 4930 1 283 . 1 1 39 39 ARG HD3 H 1 3.28 0.01 . 1 . . . . . . . . . 4930 1 284 . 1 1 39 39 ARG HE H 1 7.27 0.01 . 1 . . . . . . . . . 4930 1 285 . 1 1 39 39 ARG N N 15 126.85 0.05 . 1 . . . . . . . . . 4930 1 286 . 1 1 40 40 GLY H H 1 8.96 0.01 . 1 . . . . . . . . . 4930 1 287 . 1 1 40 40 GLY HA2 H 1 4.05 0.01 . 2 . . . . . . . . . 4930 1 288 . 1 1 40 40 GLY HA3 H 1 3.66 0.01 . 2 . . . . . . . . . 4930 1 289 . 1 1 40 40 GLY N N 15 109.55 0.05 . 1 . . . . . . . . . 4930 1 290 . 1 1 41 41 VAL H H 1 7.09 0.01 . 1 . . . . . . . . . 4930 1 291 . 1 1 41 41 VAL HA H 1 4.69 0.01 . 1 . . . . . . . . . 4930 1 292 . 1 1 41 41 VAL HB H 1 2.06 0.01 . 1 . . . . . . . . . 4930 1 293 . 1 1 41 41 VAL HG11 H 1 0.61 0.01 . 1 . . . . . . . . . 4930 1 294 . 1 1 41 41 VAL HG12 H 1 0.61 0.01 . 1 . . . . . . . . . 4930 1 295 . 1 1 41 41 VAL HG13 H 1 0.61 0.01 . 1 . . . . . . . . . 4930 1 296 . 1 1 41 41 VAL HG21 H 1 0.76 0.01 . 1 . . . . . . . . . 4930 1 297 . 1 1 41 41 VAL HG22 H 1 0.76 0.01 . 1 . . . . . . . . . 4930 1 298 . 1 1 41 41 VAL HG23 H 1 0.76 0.01 . 1 . . . . . . . . . 4930 1 299 . 1 1 41 41 VAL N N 15 112.9 0.05 . 1 . . . . . . . . . 4930 1 300 . 1 1 42 42 PRO HA H 1 4.12 0.01 . 1 . . . . . . . . . 4930 1 301 . 1 1 42 42 PRO HB2 H 1 2.24 0.01 . 1 . . . . . . . . . 4930 1 302 . 1 1 42 42 PRO HB3 H 1 1.75 0.01 . 1 . . . . . . . . . 4930 1 303 . 1 1 42 42 PRO HG2 H 1 2.24 0.01 . 2 . . . . . . . . . 4930 1 304 . 1 1 42 42 PRO HG3 H 1 1.78 0.01 . 2 . . . . . . . . . 4930 1 305 . 1 1 42 42 PRO HD2 H 1 3.69 0.01 . 1 . . . . . . . . . 4930 1 306 . 1 1 42 42 PRO HD3 H 1 3.50 0.01 . 1 . . . . . . . . . 4930 1 307 . 1 1 43 43 TRP H H 1 8.00 0.01 . 1 . . . . . . . . . 4930 1 308 . 1 1 43 43 TRP HA H 1 4.88 0.01 . 1 . . . . . . . . . 4930 1 309 . 1 1 43 43 TRP HB2 H 1 2.29 0.01 . 1 . . . . . . . . . 4930 1 310 . 1 1 43 43 TRP HB3 H 1 2.78 0.01 . 1 . . . . . . . . . 4930 1 311 . 1 1 43 43 TRP HD1 H 1 7.11 0.01 . 1 . . . . . . . . . 4930 1 312 . 1 1 43 43 TRP HE1 H 1 9.75 0.01 . 1 . . . . . . . . . 4930 1 313 . 1 1 43 43 TRP HE3 H 1 7.80 0.01 . 1 . . . . . . . . . 4930 1 314 . 1 1 43 43 TRP HZ2 H 1 7.45 0.01 . 1 . . . . . . . . . 4930 1 315 . 1 1 43 43 TRP HZ3 H 1 7.32 0.01 . 1 . . . . . . . . . 4930 1 316 . 1 1 43 43 TRP HH2 H 1 7.32 0.01 . 1 . . . . . . . . . 4930 1 317 . 1 1 43 43 TRP N N 15 123.15 0.05 . 1 . . . . . . . . . 4930 1 318 . 1 1 43 43 TRP NE1 N 15 126.6 0.05 . 1 . . . . . . . . . 4930 1 319 . 1 1 44 44 CYS H H 1 8.67 0.01 . 1 . . . . . . . . . 4930 1 320 . 1 1 44 44 CYS HA H 1 5.96 0.01 . 1 . . . . . . . . . 4930 1 321 . 1 1 44 44 CYS HB2 H 1 2.98 0.01 . 1 . . . . . . . . . 4930 1 322 . 1 1 44 44 CYS HB3 H 1 2.64 0.01 . 1 . . . . . . . . . 4930 1 323 . 1 1 44 44 CYS N N 15 116.5 0.05 . 1 . . . . . . . . . 4930 1 324 . 1 1 45 45 PHE H H 1 9.37 0.01 . 1 . . . . . . . . . 4930 1 325 . 1 1 45 45 PHE HA H 1 5.71 0.01 . 1 . . . . . . . . . 4930 1 326 . 1 1 45 45 PHE HB2 H 1 2.58 0.01 . 1 . . . . . . . . . 4930 1 327 . 1 1 45 45 PHE HB3 H 1 3.18 0.01 . 1 . . . . . . . . . 4930 1 328 . 1 1 45 45 PHE HD1 H 1 7.29 0.01 . 3 . . . . . . . . . 4930 1 329 . 1 1 45 45 PHE HD2 H 1 6.96 0.01 . 3 . . . . . . . . . 4930 1 330 . 1 1 45 45 PHE HE1 H 1 7.28 0.01 . 3 . . . . . . . . . 4930 1 331 . 1 1 45 45 PHE HE2 H 1 7.14 0.01 . 3 . . . . . . . . . 4930 1 332 . 1 1 45 45 PHE HZ H 1 7.43 0.01 . 1 . . . . . . . . . 4930 1 333 . 1 1 45 45 PHE N N 15 125.55 0.05 . 1 . . . . . . . . . 4930 1 334 . 1 1 46 46 TYR H H 1 7.95 0.01 . 1 . . . . . . . . . 4930 1 335 . 1 1 46 46 TYR HA H 1 4.78 0.01 . 1 . . . . . . . . . 4930 1 336 . 1 1 46 46 TYR HB2 H 1 3.34 0.01 . 1 . . . . . . . . . 4930 1 337 . 1 1 46 46 TYR HB3 H 1 2.89 0.01 . 1 . . . . . . . . . 4930 1 338 . 1 1 46 46 TYR HD1 H 1 7.16 0.01 . 1 . . . . . . . . . 4930 1 339 . 1 1 46 46 TYR HD2 H 1 7.16 0.01 . 1 . . . . . . . . . 4930 1 340 . 1 1 46 46 TYR HE1 H 1 6.94 0.01 . 1 . . . . . . . . . 4930 1 341 . 1 1 46 46 TYR HE2 H 1 6.94 0.01 . 1 . . . . . . . . . 4930 1 342 . 1 1 46 46 TYR N N 15 120.0 0.05 . 1 . . . . . . . . . 4930 1 343 . 1 1 47 47 PRO HA H 1 4.81 0.01 . 1 . . . . . . . . . 4930 1 344 . 1 1 47 47 PRO HB2 H 1 2.13 0.01 . 1 . . . . . . . . . 4930 1 345 . 1 1 47 47 PRO HB3 H 1 1.97 0.01 . 1 . . . . . . . . . 4930 1 346 . 1 1 47 47 PRO HG2 H 1 1.92 0.01 . 1 . . . . . . . . . 4930 1 347 . 1 1 47 47 PRO HG3 H 1 1.92 0.01 . 1 . . . . . . . . . 4930 1 348 . 1 1 47 47 PRO HD2 H 1 3.87 0.01 . 2 . . . . . . . . . 4930 1 349 . 1 1 47 47 PRO HD3 H 1 4.05 0.01 . 2 . . . . . . . . . 4930 1 350 . 1 1 48 48 ASN H H 1 8.67 0.01 . 1 . . . . . . . . . 4930 1 351 . 1 1 48 48 ASN HA H 1 4.93 0.01 . 1 . . . . . . . . . 4930 1 352 . 1 1 48 48 ASN HB2 H 1 2.80 0.01 . 1 . . . . . . . . . 4930 1 353 . 1 1 48 48 ASN HB3 H 1 2.80 0.01 . 1 . . . . . . . . . 4930 1 354 . 1 1 48 48 ASN HD21 H 1 6.93 0.01 . 2 . . . . . . . . . 4930 1 355 . 1 1 48 48 ASN HD22 H 1 7.49 0.01 . 2 . . . . . . . . . 4930 1 356 . 1 1 48 48 ASN N N 15 116.75 0.05 . 1 . . . . . . . . . 4930 1 357 . 1 1 48 48 ASN ND2 N 15 111.65 0.05 . 1 . . . . . . . . . 4930 1 358 . 1 1 49 49 THR H H 1 8.04 0.01 . 1 . . . . . . . . . 4930 1 359 . 1 1 49 49 THR HA H 1 4.54 0.01 . 1 . . . . . . . . . 4930 1 360 . 1 1 49 49 THR HB H 1 4.21 0.01 . 1 . . . . . . . . . 4930 1 361 . 1 1 49 49 THR HG21 H 1 1.20 0.01 . 1 . . . . . . . . . 4930 1 362 . 1 1 49 49 THR HG22 H 1 1.20 0.01 . 1 . . . . . . . . . 4930 1 363 . 1 1 49 49 THR HG23 H 1 1.20 0.01 . 1 . . . . . . . . . 4930 1 364 . 1 1 49 49 THR N N 15 113.05 0.05 . 1 . . . . . . . . . 4930 1 365 . 1 1 50 50 ILE H H 1 8.08 0.01 . 1 . . . . . . . . . 4930 1 366 . 1 1 50 50 ILE HA H 1 4.28 0.01 . 1 . . . . . . . . . 4930 1 367 . 1 1 50 50 ILE HB H 1 1.83 0.01 . 1 . . . . . . . . . 4930 1 368 . 1 1 50 50 ILE HG12 H 1 1.39 0.01 . 1 . . . . . . . . . 4930 1 369 . 1 1 50 50 ILE HG13 H 1 1.08 0.01 . 1 . . . . . . . . . 4930 1 370 . 1 1 50 50 ILE HG21 H 1 0.85 0.01 . 1 . . . . . . . . . 4930 1 371 . 1 1 50 50 ILE HG22 H 1 0.85 0.01 . 1 . . . . . . . . . 4930 1 372 . 1 1 50 50 ILE HG23 H 1 0.85 0.01 . 1 . . . . . . . . . 4930 1 373 . 1 1 50 50 ILE HD11 H 1 0.81 0.01 . 1 . . . . . . . . . 4930 1 374 . 1 1 50 50 ILE HD12 H 1 0.81 0.01 . 1 . . . . . . . . . 4930 1 375 . 1 1 50 50 ILE HD13 H 1 0.81 0.01 . 1 . . . . . . . . . 4930 1 376 . 1 1 50 50 ILE N N 15 122.4 0.05 . 1 . . . . . . . . . 4930 1 377 . 1 1 51 51 ASP H H 1 8.38 0.01 . 1 . . . . . . . . . 4930 1 378 . 1 1 51 51 ASP HA H 1 4.69 0.01 . 1 . . . . . . . . . 4930 1 379 . 1 1 51 51 ASP HB2 H 1 2.56 0.01 . 1 . . . . . . . . . 4930 1 380 . 1 1 51 51 ASP HB3 H 1 2.68 0.01 . 1 . . . . . . . . . 4930 1 381 . 1 1 51 51 ASP N N 15 124.6 0.05 . 1 . . . . . . . . . 4930 1 382 . 1 1 52 52 VAL H H 1 8.07 0.01 . 1 . . . . . . . . . 4930 1 383 . 1 1 52 52 VAL HA H 1 4.37 0.01 . 1 . . . . . . . . . 4930 1 384 . 1 1 52 52 VAL HB H 1 2.02 0.01 . 1 . . . . . . . . . 4930 1 385 . 1 1 52 52 VAL HG11 H 1 0.93 0.01 . 2 . . . . . . . . . 4930 1 386 . 1 1 52 52 VAL HG12 H 1 0.93 0.01 . 2 . . . . . . . . . 4930 1 387 . 1 1 52 52 VAL HG13 H 1 0.93 0.01 . 2 . . . . . . . . . 4930 1 388 . 1 1 52 52 VAL HG21 H 1 0.88 0.01 . 2 . . . . . . . . . 4930 1 389 . 1 1 52 52 VAL HG22 H 1 0.88 0.01 . 2 . . . . . . . . . 4930 1 390 . 1 1 52 52 VAL HG23 H 1 0.88 0.01 . 2 . . . . . . . . . 4930 1 391 . 1 1 52 52 VAL N N 15 121.95 0.05 . 1 . . . . . . . . . 4930 1 392 . 1 1 53 53 PRO HA H 1 4.65 0.01 . 1 . . . . . . . . . 4930 1 393 . 1 1 53 53 PRO HB2 H 1 2.32 0.01 . 2 . . . . . . . . . 4930 1 394 . 1 1 53 53 PRO HB3 H 1 1.88 0.01 . 2 . . . . . . . . . 4930 1 395 . 1 1 53 53 PRO HG2 H 1 2.03 0.01 . 2 . . . . . . . . . 4930 1 396 . 1 1 53 53 PRO HG3 H 1 1.96 0.01 . 2 . . . . . . . . . 4930 1 397 . 1 1 53 53 PRO HD2 H 1 3.85 0.01 . 2 . . . . . . . . . 4930 1 398 . 1 1 53 53 PRO HD3 H 1 3.65 0.01 . 2 . . . . . . . . . 4930 1 399 . 1 1 54 54 PRO HG2 H 1 2.03 0.01 . 1 . . . . . . . . . 4930 1 400 . 1 1 54 54 PRO HG3 H 1 2.03 0.01 . 1 . . . . . . . . . 4930 1 401 . 1 1 54 54 PRO HD2 H 1 3.65 0.01 . 2 . . . . . . . . . 4930 1 402 . 1 1 54 54 PRO HD3 H 1 3.80 0.01 . 2 . . . . . . . . . 4930 1 403 . 1 1 55 55 GLU H H 1 8.47 0.01 . 1 . . . . . . . . . 4930 1 404 . 1 1 55 55 GLU HA H 1 4.27 0.01 . 1 . . . . . . . . . 4930 1 405 . 1 1 55 55 GLU HB2 H 1 2.04 0.01 . 2 . . . . . . . . . 4930 1 406 . 1 1 55 55 GLU HB3 H 1 1.93 0.01 . 2 . . . . . . . . . 4930 1 407 . 1 1 55 55 GLU HG2 H 1 2.30 0.01 . 1 . . . . . . . . . 4930 1 408 . 1 1 55 55 GLU HG3 H 1 2.30 0.01 . 1 . . . . . . . . . 4930 1 409 . 1 1 55 55 GLU N N 15 120.7 0.05 . 1 . . . . . . . . . 4930 1 410 . 1 1 56 56 GLU H H 1 8.41 0.01 . 1 . . . . . . . . . 4930 1 411 . 1 1 56 56 GLU HA H 1 4.24 0.01 . 1 . . . . . . . . . 4930 1 412 . 1 1 56 56 GLU HB2 H 1 2.05 0.01 . 2 . . . . . . . . . 4930 1 413 . 1 1 56 56 GLU HB3 H 1 1.91 0.01 . 2 . . . . . . . . . 4930 1 414 . 1 1 56 56 GLU HG2 H 1 2.28 0.01 . 1 . . . . . . . . . 4930 1 415 . 1 1 56 56 GLU HG3 H 1 2.28 0.01 . 1 . . . . . . . . . 4930 1 416 . 1 1 56 56 GLU N N 15 121.75 0.05 . 1 . . . . . . . . . 4930 1 417 . 1 1 57 57 GLU H H 1 8.42 0.01 . 1 . . . . . . . . . 4930 1 418 . 1 1 57 57 GLU HA H 1 4.31 0.01 . 1 . . . . . . . . . 4930 1 419 . 1 1 57 57 GLU HB2 H 1 2.05 0.01 . 2 . . . . . . . . . 4930 1 420 . 1 1 57 57 GLU HB3 H 1 1.91 0.01 . 2 . . . . . . . . . 4930 1 421 . 1 1 57 57 GLU HG2 H 1 2.28 0.01 . 1 . . . . . . . . . 4930 1 422 . 1 1 57 57 GLU HG3 H 1 2.28 0.01 . 1 . . . . . . . . . 4930 1 423 . 1 1 57 57 GLU N N 15 121.85 0.05 . 1 . . . . . . . . . 4930 1 424 . 1 1 58 58 CYS H H 1 8.55 0.01 . 1 . . . . . . . . . 4930 1 425 . 1 1 58 58 CYS HA H 1 4.64 0.01 . 1 . . . . . . . . . 4930 1 426 . 1 1 58 58 CYS HB2 H 1 3.13 0.01 . 2 . . . . . . . . . 4930 1 427 . 1 1 58 58 CYS HB3 H 1 2.95 0.01 . 2 . . . . . . . . . 4930 1 428 . 1 1 58 58 CYS N N 15 119.65 0.05 . 1 . . . . . . . . . 4930 1 429 . 1 1 59 59 GLU H H 1 8.36 0.01 . 1 . . . . . . . . . 4930 1 430 . 1 1 59 59 GLU HA H 1 4.29 0.01 . 1 . . . . . . . . . 4930 1 431 . 1 1 59 59 GLU HB2 H 1 1.95 0.01 . 2 . . . . . . . . . 4930 1 432 . 1 1 59 59 GLU HB3 H 1 1.84 0.01 . 2 . . . . . . . . . 4930 1 433 . 1 1 59 59 GLU HG2 H 1 2.25 0.01 . 1 . . . . . . . . . 4930 1 434 . 1 1 59 59 GLU HG3 H 1 2.25 0.01 . 1 . . . . . . . . . 4930 1 435 . 1 1 59 59 GLU N N 15 123.25 0.05 . 1 . . . . . . . . . 4930 1 436 . 1 1 60 60 PHE H H 1 7.72 0.01 . 1 . . . . . . . . . 4930 1 437 . 1 1 60 60 PHE HA H 1 4.42 0.01 . 1 . . . . . . . . . 4930 1 438 . 1 1 60 60 PHE HB2 H 1 3.16 0.01 . 2 . . . . . . . . . 4930 1 439 . 1 1 60 60 PHE HB3 H 1 2.93 0.01 . 2 . . . . . . . . . 4930 1 440 . 1 1 60 60 PHE HD1 H 1 7.22 0.01 . 1 . . . . . . . . . 4930 1 441 . 1 1 60 60 PHE HD2 H 1 7.22 0.01 . 1 . . . . . . . . . 4930 1 442 . 1 1 60 60 PHE HE1 H 1 7.32 0.01 . 1 . . . . . . . . . 4930 1 443 . 1 1 60 60 PHE HE2 H 1 7.32 0.01 . 1 . . . . . . . . . 4930 1 444 . 1 1 60 60 PHE HZ H 1 7.28 0.01 . 1 . . . . . . . . . 4930 1 445 . 1 1 60 60 PHE N N 15 126.05 0.05 . 1 . . . . . . . . . 4930 1 stop_ save_