data_4396 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4396 _Entry.Title ; Anticoagulant protein from the nematode Ancylostoma caninum ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1999-09-09 _Entry.Accession_date 1999-09-09 _Entry.Last_release_date 2007-06-19 _Entry.Original_release_date 2007-06-19 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Brendan Duggan . M. . 4396 2 H. Dyson . Jane . 4396 3 Peter Wright . E. . 4396 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4396 coupling_constants 1 4396 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 22 4396 '15N chemical shifts' 85 4396 '1H chemical shifts' 511 4396 'coupling constants' 76 4396 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 . . 2007-06-19 1999-09-09 original author . 4396 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4396 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 99435967 _Citation.DOI . _Citation.PubMed_ID 10504384 _Citation.Full_citation . _Citation.Title ; Inherent flexibility in a potent inhibitor of blood coagulation, recombinant nematode anticoagulant protein c2 ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full . _Citation.Journal_volume 265 _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 539 _Citation.Page_last 548 _Citation.Year 1999 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Brendan Duggan . M. . 4396 1 2 H. Dyson . Jane . 4396 1 3 Peter Wright . E. . 4396 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID anticoagulant 4396 1 'protease inhibitor' 4396 1 stop_ save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 4396 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8700900 _Citation.Full_citation ; Stassens P, Bergum PW, Gansemans Y, Jespers L, Laroche Y, Huang S, Maki S, Messens J, Lauwereys M, Cappello M, Hotez PJ, Lasters I, Vlasuk GP. Anticoagulant repertoire of the hookworm Ancylostoma caninum. Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2149-54. ; _Citation.Title 'Anticoagulant repertoire of the hookworm Ancylostoma caninum.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Proc. Natl. Acad. Sci. U.S.A.' _Citation.Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Citation.Journal_volume 93 _Citation.Journal_issue 5 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0027-8424 _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 2149 _Citation.Page_last 2154 _Citation.Year 1996 _Citation.Details ; Hookworms are hematophagous nematodes that infect a wide range of mammalian hosts, including humans. There has been speculation for nearly a century as to the identity of the anticoagulant substances) used by these organisms to subvert host hemostasis. Using molecular cloning, we describe a family of potent small protein (75-84 amino acids) anticoagulants from the hookworm Ancylostoma caninum termed AcAP (A. caninum anticoagulant protein). Two recombinant AcAP members (AcAP5 and AcAP6) directly inhibited the catalytic activity of blood coagulation factor Xa (fXa), while a third form (AcAPc2) predominantly inhibited the catalytic activity of a complex composed of blood coagulation factor VIIa and tissue factor (fVIIa/TF). The inhibition of fVIIa/TF was by a unique mechanism that required the initial formation of a binary complex of the inhibitor with fXa at a site on the enzyme that is distinct from the catalytic center (exo-site). The sequence of AcAPc2 as well as the utilization of an exo-site on fXa distinguishes this inhibitor from the mammalian anticoagulant TFPI (tissue factor pathway inhibitor), which is functionally equivalent with respect to fXa-dependent inhibition of fIIa/TF. The relative sequence positions of the reactive site residues determined for AcAP5 with the homologous regions in AcAP6 and AcAPc2 as well as the pattern of 10 cysteine residues present in each of the inhibitors suggest that the AcAPs are distantly related to the family of small protein serine protease inhibitors found in the nonhematophagous nematode Ascaris lumbricoides var. suum. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 P Stassens P. . . 4396 2 2 'P W' Bergum P. W. . 4396 2 3 Y Gansemans Y. . . 4396 2 4 L Jespers L. . . 4396 2 5 Y Laroche Y. . . 4396 2 6 S Huang S. . . 4396 2 7 S Maki S. . . 4396 2 8 J Messens J. . . 4396 2 9 M Lauwereys M. . . 4396 2 10 M Cappello M. . . 4396 2 11 'P J' Hotez P. J. . 4396 2 12 I Lasters I. . . 4396 2 13 'G P' Vlasuk G. P. . 4396 2 stop_ save_ save_ref_22 _Citation.Sf_category citations _Citation.Sf_framecode ref_22 _Citation.Entry_ID 4396 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9367762 _Citation.Full_citation ; Guntert P, Mumenthaler C, Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol. 1997 Oct 17;273(1):283-98. ; _Citation.Title 'Torsion angle dynamics for NMR structure calculation with the new program DYANA.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 273 _Citation.Journal_issue 1 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 283 _Citation.Page_last 298 _Citation.Year 1997 _Citation.Details ; The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the "bundle" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 P Guntert P. . . 4396 3 2 C Mumenthaler C. . . 4396 3 3 K Wuthrich K. . . 4396 3 stop_ save_ save_ref_24 _Citation.Sf_category citations _Citation.Sf_framecode ref_24 _Citation.Entry_ID 4396 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 1579569 _Citation.Full_citation ; Morris AL, MacArthur MW, Hutchinson EG, Thornton JM. Stereochemical quality of protein structure coordinates. Proteins. 1992 Apr;12(4):345-64. ; _Citation.Title 'Stereochemical quality of protein structure coordinates.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Proteins _Citation.Journal_name_full Proteins _Citation.Journal_volume 12 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0887-3585 _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 345 _Citation.Page_last 364 _Citation.Year 1992 _Citation.Details ; Methods have been developed to assess the stereochemical quality of any protein structure both globally and locally using various criteria. Several parameters can be derived from the coordinates of a given structure. Global parameters include the distribution of phi, psi and chi 1 torsion angles, and hydrogen bond energies. There are clear correlations between these parameters and resolution; as the resolution improves, the distribution of the parameters becomes more clustered. These features show a broad distribution about ideal values derived from high-resolution structures. Some structures have tightly clustered distributions even at relatively low resolutions, while others show abnormal scatter though the data go to high resolution. Additional indicators of local irregularity include proline phi angles, peptide bond planarities, disulfide bond lengths, and their chi 3 torsion angles. These stereochemical parameters have been used to generate measures of stereochemical quality which provide a simple guide as to the reliability of a structure, in addition to the most important measures, resolution and R-factor. The parameters used in this evaluation are not novel, and are easily calculated from structure coordinates. A program suite is currently being developed which will quickly check a given structure, highlighting unusual stereochemistry and possible errors. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'A L' Morris A. L. . 4396 4 2 'M W' MacArthur M. W. . 4396 4 3 'E G' Hutchinson E. G. . 4396 4 4 'J M' Thornton J. M. . 4396 4 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_NAPc2 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_NAPc2 _Assembly.Entry_ID 4396 _Assembly.ID 1 _Assembly.Name 'Nematode Anticoagulant Protein c2' _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 4396 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 NAPc2 1 $NAPc2 . . . native . . . . . 4396 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 6 6 SG . 1 . 1 CYS 50 50 SG . . . . . . . . . . 4396 1 2 disulfide single . 1 . 1 CYS 15 15 SG . 1 . 1 CYS 46 46 SG . . . . . . . . . . 4396 1 3 disulfide single . 1 . 1 CYS 20 20 SG . 1 . 1 CYS 41 41 SG . . . . . . . . . . 4396 1 4 disulfide single . 1 . 1 CYS 24 24 SG . 1 . 1 CYS 70 70 SG . . . . . . . . . . 4396 1 5 disulfide single . 1 . 1 CYS 52 52 SG . 1 . 1 CYS 64 64 SG . . . . . . . . . . 4396 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID NAPc2 abbreviation 4396 1 'Nematode Anticoagulant Protein c2' system 4396 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID anticoagulant 4396 1 'protease inhibitor' 4396 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_NAPc2 _Entity.Sf_category entity _Entity.Sf_framecode NAPc2 _Entity.Entry_ID 4396 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Nematode Anticoagulant Protein c2' _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 ; KATMQCGENEKYDSCGSKEC DKKCKYDGVEEEDDEEPNVP CLVRVCHQDCVCEEGFYRNK DDKCVSAEDCELDNMDFIYP GTRNP ; _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 85 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 9643 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1COU . "Anticoagulant Protein From The Nematode Ancylostoma Caninum" . . . . . 100.00 85 100.00 100.00 1.86e-52 . . . . 4396 1 2 no PDB 2H9E . "Crystal Structure Of FxaSELECTIDENAPC2 TERNARY COMPLEX" . . . . . 98.82 84 100.00 100.00 1.72e-51 . . . . 4396 1 3 no GB AAC47080 . "anti-coagulant protein C2 precursor, partial [Ancylostoma caninum]" . . . . . 98.82 91 100.00 100.00 1.70e-51 . . . . 4396 1 4 no PRF 2208501A . "anticoagulant protein:ISOTYPE=C2" . . . . . 98.82 91 100.00 100.00 1.70e-51 . . . . 4396 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID NAPc2 abbreviation 4396 1 'Nematode Anticoagulant Protein c2' common 4396 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 . LYS . 4396 1 2 . ALA . 4396 1 3 . THR . 4396 1 4 . MET . 4396 1 5 . GLN . 4396 1 6 . CYS . 4396 1 7 . GLY . 4396 1 8 . GLU . 4396 1 9 . ASN . 4396 1 10 . GLU . 4396 1 11 . LYS . 4396 1 12 . TYR . 4396 1 13 . ASP . 4396 1 14 . SER . 4396 1 15 . CYS . 4396 1 16 . GLY . 4396 1 17 . SER . 4396 1 18 . LYS . 4396 1 19 . GLU . 4396 1 20 . CYS . 4396 1 21 . ASP . 4396 1 22 . LYS . 4396 1 23 . LYS . 4396 1 24 . CYS . 4396 1 25 . LYS . 4396 1 26 . TYR . 4396 1 27 . ASP . 4396 1 28 . GLY . 4396 1 29 . VAL . 4396 1 30 . GLU . 4396 1 31 . GLU . 4396 1 32 . GLU . 4396 1 33 . ASP . 4396 1 34 . ASP . 4396 1 35 . GLU . 4396 1 36 . GLU . 4396 1 37 . PRO . 4396 1 38 . ASN . 4396 1 39 . VAL . 4396 1 40 . PRO . 4396 1 41 . CYS . 4396 1 42 . LEU . 4396 1 43 . VAL . 4396 1 44 . ARG . 4396 1 45 . VAL . 4396 1 46 . CYS . 4396 1 47 . HIS . 4396 1 48 . GLN . 4396 1 49 . ASP . 4396 1 50 . CYS . 4396 1 51 . VAL . 4396 1 52 . CYS . 4396 1 53 . GLU . 4396 1 54 . GLU . 4396 1 55 . GLY . 4396 1 56 . PHE . 4396 1 57 . TYR . 4396 1 58 . ARG . 4396 1 59 . ASN . 4396 1 60 . LYS . 4396 1 61 . ASP . 4396 1 62 . ASP . 4396 1 63 . LYS . 4396 1 64 . CYS . 4396 1 65 . VAL . 4396 1 66 . SER . 4396 1 67 . ALA . 4396 1 68 . GLU . 4396 1 69 . ASP . 4396 1 70 . CYS . 4396 1 71 . GLU . 4396 1 72 . LEU . 4396 1 73 . ASP . 4396 1 74 . ASN . 4396 1 75 . MET . 4396 1 76 . ASP . 4396 1 77 . PHE . 4396 1 78 . ILE . 4396 1 79 . TYR . 4396 1 80 . PRO . 4396 1 81 . GLY . 4396 1 82 . THR . 4396 1 83 . ARG . 4396 1 84 . ASN . 4396 1 85 . PRO . 4396 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 . LYS 1 1 4396 1 . ALA 2 2 4396 1 . THR 3 3 4396 1 . MET 4 4 4396 1 . GLN 5 5 4396 1 . CYS 6 6 4396 1 . GLY 7 7 4396 1 . GLU 8 8 4396 1 . ASN 9 9 4396 1 . GLU 10 10 4396 1 . LYS 11 11 4396 1 . TYR 12 12 4396 1 . ASP 13 13 4396 1 . SER 14 14 4396 1 . CYS 15 15 4396 1 . GLY 16 16 4396 1 . SER 17 17 4396 1 . LYS 18 18 4396 1 . GLU 19 19 4396 1 . CYS 20 20 4396 1 . ASP 21 21 4396 1 . LYS 22 22 4396 1 . LYS 23 23 4396 1 . CYS 24 24 4396 1 . LYS 25 25 4396 1 . TYR 26 26 4396 1 . ASP 27 27 4396 1 . GLY 28 28 4396 1 . VAL 29 29 4396 1 . GLU 30 30 4396 1 . GLU 31 31 4396 1 . GLU 32 32 4396 1 . ASP 33 33 4396 1 . ASP 34 34 4396 1 . GLU 35 35 4396 1 . GLU 36 36 4396 1 . PRO 37 37 4396 1 . ASN 38 38 4396 1 . VAL 39 39 4396 1 . PRO 40 40 4396 1 . CYS 41 41 4396 1 . LEU 42 42 4396 1 . VAL 43 43 4396 1 . ARG 44 44 4396 1 . VAL 45 45 4396 1 . CYS 46 46 4396 1 . HIS 47 47 4396 1 . GLN 48 48 4396 1 . ASP 49 49 4396 1 . CYS 50 50 4396 1 . VAL 51 51 4396 1 . CYS 52 52 4396 1 . GLU 53 53 4396 1 . GLU 54 54 4396 1 . GLY 55 55 4396 1 . PHE 56 56 4396 1 . TYR 57 57 4396 1 . ARG 58 58 4396 1 . ASN 59 59 4396 1 . LYS 60 60 4396 1 . ASP 61 61 4396 1 . ASP 62 62 4396 1 . LYS 63 63 4396 1 . CYS 64 64 4396 1 . VAL 65 65 4396 1 . SER 66 66 4396 1 . ALA 67 67 4396 1 . GLU 68 68 4396 1 . ASP 69 69 4396 1 . CYS 70 70 4396 1 . GLU 71 71 4396 1 . LEU 72 72 4396 1 . ASP 73 73 4396 1 . ASN 74 74 4396 1 . MET 75 75 4396 1 . ASP 76 76 4396 1 . PHE 77 77 4396 1 . ILE 78 78 4396 1 . TYR 79 79 4396 1 . PRO 80 80 4396 1 . GLY 81 81 4396 1 . THR 82 82 4396 1 . ARG 83 83 4396 1 . ASN 84 84 4396 1 . PRO 85 85 4396 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 4396 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $NAPc2 . 29170 organism . 'Ancylostoma caninum' 'dog hookworm' . . Eukaryota Metazoa Ancylostoma caninum . . . . . . . . . . . . . . . . . . . . . 4396 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 4396 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $NAPc2 . 'recombinant technology' 'Pichia pastoris' 'Pichia pastoris' . . Pichia pastoris GS115 . . . . . . . . . . . . . . . pYAM7SP8 . . . . . . 4396 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4396 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details 'The 15N label is around 50-60%' _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 'Nematode Anticoagulant Protein c2' '[U-55% 15N]' . . 1 $NAPc2 . . 2.0 . . mM . . . . 4396 1 2 'sodium chloride' . . . . . . . 50 . . mM . . . . 4396 1 3 DSS . . . . . . . 20 . . uM . . . . 4396 1 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 4396 _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' 0.05 0.01 M 4396 1 pH 4.5 0.05 n/a 4396 1 pressure 1 . atm 4396 1 temperature 298 1 K 4396 1 stop_ save_ ############################ # Computer software used # ############################ save_Felix _Software.Sf_category software _Software.Sf_framecode Felix _Software.Entry_ID 4396 _Software.ID 1 _Software.Name Felix _Software.Version '95 and 97' _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data processing and analysis' 4396 1 stop_ save_ save_Dyana _Software.Sf_category software _Software.Sf_framecode Dyana _Software.Entry_ID 4396 _Software.ID 2 _Software.Name Dyana _Software.Version 1.5 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'molecular dynamics' 4396 2 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 3 $ref_22 4396 2 stop_ save_ save_Amber _Software.Sf_category software _Software.Sf_framecode Amber _Software.Entry_ID 4396 _Software.ID 3 _Software.Name Amber _Software.Version 5.1 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'molecular dynamics' 4396 3 stop_ save_ save_Procheck-NMR _Software.Sf_category software _Software.Sf_framecode Procheck-NMR _Software.Entry_ID 4396 _Software.ID 4 _Software.Name Procheck-NMR _Software.Version 3.4.4 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure analysis' 4396 4 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 4 $ref_24 4396 4 stop_ save_ save_SANE _Software.Sf_category software _Software.Sf_framecode SANE _Software.Entry_ID 4396 _Software.ID 5 _Software.Name SANE _Software.Version 1 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'In-house software: automated NOESY assignment and restraint generation' 4396 5 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 4396 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 4396 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_3 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_3 _NMR_spectrometer.Entry_ID 4396 _NMR_spectrometer.ID 3 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_spectrometer_4 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_4 _NMR_spectrometer.Entry_ID 4396 _NMR_spectrometer.ID 4 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_5 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_5 _NMR_spectrometer.Entry_ID 4396 _NMR_spectrometer.ID 5 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4396 _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 spectrometer_1 Bruker AMX . 500 . . . 4396 1 2 spectrometer_2 Bruker AMX . 600 . . . 4396 1 3 spectrometer_3 Bruker DMX . 750 . . . 4396 1 4 spectrometer_4 Bruker DMX . 500 . . . 4396 1 5 spectrometer_5 Bruker DMX . 600 . . . 4396 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 4396 _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 . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4396 1 2 DQ-COSY . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4396 1 3 '15N HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4396 1 4 '15N NOESY-HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4396 1 5 '15N TOCSY-HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4396 1 6 '15N HSQC-NOESY-HSQ' . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4396 1 7 HNHA . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4396 1 8 '13C HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4396 1 9 '15N {1H} NOE' . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4396 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 4396 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 4396 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.000000000 . . . . . . . . . 4396 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4396 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_chem_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chem_shift_set_1 _Assigned_chem_shift_list.Entry_ID 4396 _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 $sample_1 . 4396 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 LYS HA H 1 3.99 . . . . . . . . . . . 4396 1 2 . 1 1 1 1 LYS HB2 H 1 1.89 . . . . . . . . . . . 4396 1 3 . 1 1 1 1 LYS HB3 H 1 1.89 . . . . . . . . . . . 4396 1 4 . 1 1 1 1 LYS HG2 H 1 1.44 . . . . . . . . . . . 4396 1 5 . 1 1 1 1 LYS HG3 H 1 1.44 . . . . . . . . . . . 4396 1 6 . 1 1 2 2 ALA N N 15 127.737 . . . . . . . . . . . 4396 1 7 . 1 1 2 2 ALA CB C 13 19.3 . . . . . . . . . . . 4396 1 8 . 1 1 2 2 ALA H H 1 8.710 . . . . . . . . . . . 4396 1 9 . 1 1 2 2 ALA HA H 1 4.392 . . . . . . . . . . . 4396 1 10 . 1 1 2 2 ALA HB1 H 1 1.362 . . . . . . . . . . . 4396 1 11 . 1 1 2 2 ALA HB2 H 1 1.362 . . . . . . . . . . . 4396 1 12 . 1 1 2 2 ALA HB3 H 1 1.362 . . . . . . . . . . . 4396 1 13 . 1 1 3 3 THR N N 15 115.176 . . . . . . . . . . . 4396 1 14 . 1 1 3 3 THR CG2 C 13 21.5 . . . . . . . . . . . 4396 1 15 . 1 1 3 3 THR H H 1 8.125 . . . . . . . . . . . 4396 1 16 . 1 1 3 3 THR HA H 1 4.160 . . . . . . . . . . . 4396 1 17 . 1 1 3 3 THR HB H 1 3.994 . . . . . . . . . . . 4396 1 18 . 1 1 3 3 THR HG21 H 1 1.114 . . . . . . . . . . . 4396 1 19 . 1 1 3 3 THR HG22 H 1 1.114 . . . . . . . . . . . 4396 1 20 . 1 1 3 3 THR HG23 H 1 1.114 . . . . . . . . . . . 4396 1 21 . 1 1 4 4 MET N N 15 122.803 . . . . . . . . . . . 4396 1 22 . 1 1 4 4 MET CE C 13 17.1 . . . . . . . . . . . 4396 1 23 . 1 1 4 4 MET H H 1 7.737 . . . . . . . . . . . 4396 1 24 . 1 1 4 4 MET HA H 1 4.303 . . . . . . . . . . . 4396 1 25 . 1 1 4 4 MET HB2 H 1 1.910 . . . . . . . . . . . 4396 1 26 . 1 1 4 4 MET HB3 H 1 1.830 . . . . . . . . . . . 4396 1 27 . 1 1 4 4 MET HG2 H 1 2.37 . . . . . . . . . . . 4396 1 28 . 1 1 4 4 MET HG3 H 1 2.32 . . . . . . . . . . . 4396 1 29 . 1 1 4 4 MET HE1 H 1 2.08 . . . . . . . . . . . 4396 1 30 . 1 1 4 4 MET HE2 H 1 2.08 . . . . . . . . . . . 4396 1 31 . 1 1 4 4 MET HE3 H 1 2.08 . . . . . . . . . . . 4396 1 32 . 1 1 5 5 GLN N N 15 123.326 . . . . . . . . . . . 4396 1 33 . 1 1 5 5 GLN NE2 N 15 113.7 . . . . . . . . . . . 4396 1 34 . 1 1 5 5 GLN H H 1 8.355 . . . . . . . . . . . 4396 1 35 . 1 1 5 5 GLN HA H 1 4.371 . . . . . . . . . . . 4396 1 36 . 1 1 5 5 GLN HB2 H 1 2.060 . . . . . . . . . . . 4396 1 37 . 1 1 5 5 GLN HB3 H 1 1.940 . . . . . . . . . . . 4396 1 38 . 1 1 5 5 GLN HG2 H 1 2.332 . . . . . . . . . . . 4396 1 39 . 1 1 5 5 GLN HG3 H 1 2.332 . . . . . . . . . . . 4396 1 40 . 1 1 5 5 GLN HE21 H 1 7.488 . . . . . . . . . . . 4396 1 41 . 1 1 5 5 GLN HE22 H 1 6.780 . . . . . . . . . . . 4396 1 42 . 1 1 6 6 CYS N N 15 122.745 . . . . . . . . . . . 4396 1 43 . 1 1 6 6 CYS H H 1 8.515 . . . . . . . . . . . 4396 1 44 . 1 1 6 6 CYS HA H 1 5.054 . . . . . . . . . . . 4396 1 45 . 1 1 6 6 CYS HB2 H 1 3.369 . . . . . . . . . . . 4396 1 46 . 1 1 6 6 CYS HB3 H 1 2.643 . . . . . . . . . . . 4396 1 47 . 1 1 7 7 GLY N N 15 109.73 . . . . . . . . . . . 4396 1 48 . 1 1 7 7 GLY H H 1 8.437 . . . . . . . . . . . 4396 1 49 . 1 1 7 7 GLY HA2 H 1 4.355 . . . . . . . . . . . 4396 1 50 . 1 1 7 7 GLY HA3 H 1 3.576 . . . . . . . . . . . 4396 1 51 . 1 1 8 8 GLU N N 15 121.059 . . . . . . . . . . . 4396 1 52 . 1 1 8 8 GLU H H 1 8.299 . . . . . . . . . . . 4396 1 53 . 1 1 8 8 GLU HA H 1 3.926 . . . . . . . . . . . 4396 1 54 . 1 1 8 8 GLU HB2 H 1 1.926 . . . . . . . . . . . 4396 1 55 . 1 1 8 8 GLU HB3 H 1 1.926 . . . . . . . . . . . 4396 1 56 . 1 1 8 8 GLU HG2 H 1 2.333 . . . . . . . . . . . 4396 1 57 . 1 1 8 8 GLU HG3 H 1 2.333 . . . . . . . . . . . 4396 1 58 . 1 1 9 9 ASN N N 15 118.507 . . . . . . . . . . . 4396 1 59 . 1 1 9 9 ASN ND2 N 15 116.192 . . . . . . . . . . . 4396 1 60 . 1 1 9 9 ASN H H 1 8.942 . . . . . . . . . . . 4396 1 61 . 1 1 9 9 ASN HA H 1 3.732 . . . . . . . . . . . 4396 1 62 . 1 1 9 9 ASN HB2 H 1 2.647 . . . . . . . . . . . 4396 1 63 . 1 1 9 9 ASN HB3 H 1 1.245 . . . . . . . . . . . 4396 1 64 . 1 1 9 9 ASN HD21 H 1 7.346 . . . . . . . . . . . 4396 1 65 . 1 1 9 9 ASN HD22 H 1 6.841 . . . . . . . . . . . 4396 1 66 . 1 1 10 10 GLU N N 15 114.396 . . . . . . . . . . . 4396 1 67 . 1 1 10 10 GLU H H 1 7.194 . . . . . . . . . . . 4396 1 68 . 1 1 10 10 GLU HA H 1 5.152 . . . . . . . . . . . 4396 1 69 . 1 1 10 10 GLU HB2 H 1 1.943 . . . . . . . . . . . 4396 1 70 . 1 1 10 10 GLU HB3 H 1 1.613 . . . . . . . . . . . 4396 1 71 . 1 1 10 10 GLU HG2 H 1 2.133 . . . . . . . . . . . 4396 1 72 . 1 1 10 10 GLU HG3 H 1 2.067 . . . . . . . . . . . 4396 1 73 . 1 1 11 11 LYS N N 15 119.220 . . . . . . . . . . . 4396 1 74 . 1 1 11 11 LYS CG C 13 23.8 . . . . . . . . . . . 4396 1 75 . 1 1 11 11 LYS H H 1 9.524 . . . . . . . . . . . 4396 1 76 . 1 1 11 11 LYS HA H 1 4.688 . . . . . . . . . . . 4396 1 77 . 1 1 11 11 LYS HB2 H 1 1.711 . . . . . . . . . . . 4396 1 78 . 1 1 11 11 LYS HG2 H 1 1.180 . . . . . . . . . . . 4396 1 79 . 1 1 11 11 LYS HD2 H 1 1.637 . . . . . . . . . . . 4396 1 80 . 1 1 11 11 LYS HD3 H 1 1.637 . . . . . . . . . . . 4396 1 81 . 1 1 12 12 TYR N N 15 124.482 . . . . . . . . . . . 4396 1 82 . 1 1 12 12 TYR H H 1 8.592 . . . . . . . . . . . 4396 1 83 . 1 1 12 12 TYR HA H 1 4.620 . . . . . . . . . . . 4396 1 84 . 1 1 12 12 TYR HB2 H 1 3.074 . . . . . . . . . . . 4396 1 85 . 1 1 12 12 TYR HB3 H 1 2.782 . . . . . . . . . . . 4396 1 86 . 1 1 12 12 TYR HD1 H 1 6.920 . . . . . . . . . . . 4396 1 87 . 1 1 12 12 TYR HD2 H 1 6.920 . . . . . . . . . . . 4396 1 88 . 1 1 12 12 TYR HE1 H 1 6.686 . . . . . . . . . . . 4396 1 89 . 1 1 12 12 TYR HE2 H 1 6.686 . . . . . . . . . . . 4396 1 90 . 1 1 13 13 ASP N N 15 130.5 . . . . . . . . . . . 4396 1 91 . 1 1 13 13 ASP H H 1 8.453 . . . . . . . . . . . 4396 1 92 . 1 1 13 13 ASP HA H 1 4.588 . . . . . . . . . . . 4396 1 93 . 1 1 13 13 ASP HB2 H 1 2.508 . . . . . . . . . . . 4396 1 94 . 1 1 13 13 ASP HB3 H 1 2.234 . . . . . . . . . . . 4396 1 95 . 1 1 14 14 SER N N 15 120.197 . . . . . . . . . . . 4396 1 96 . 1 1 14 14 SER H H 1 8.359 . . . . . . . . . . . 4396 1 97 . 1 1 14 14 SER HA H 1 4.588 . . . . . . . . . . . 4396 1 98 . 1 1 14 14 SER HB2 H 1 4.045 . . . . . . . . . . . 4396 1 99 . 1 1 14 14 SER HB3 H 1 3.909 . . . . . . . . . . . 4396 1 100 . 1 1 15 15 CYS N N 15 124.85 . . . . . . . . . . . 4396 1 101 . 1 1 15 15 CYS H H 1 8.653 . . . . . . . . . . . 4396 1 102 . 1 1 15 15 CYS HA H 1 4.587 . . . . . . . . . . . 4396 1 103 . 1 1 15 15 CYS HB2 H 1 3.421 . . . . . . . . . . . 4396 1 104 . 1 1 15 15 CYS HB3 H 1 2.567 . . . . . . . . . . . 4396 1 105 . 1 1 16 16 GLY N N 15 111.383 . . . . . . . . . . . 4396 1 106 . 1 1 16 16 GLY H H 1 8.239 . . . . . . . . . . . 4396 1 107 . 1 1 16 16 GLY HA2 H 1 4.391 . . . . . . . . . . . 4396 1 108 . 1 1 16 16 GLY HA3 H 1 3.405 . . . . . . . . . . . 4396 1 109 . 1 1 17 17 SER N N 15 111.165 . . . . . . . . . . . 4396 1 110 . 1 1 17 17 SER H H 1 8.125 . . . . . . . . . . . 4396 1 111 . 1 1 17 17 SER HA H 1 4.885 . . . . . . . . . . . 4396 1 112 . 1 1 17 17 SER HB2 H 1 3.850 . . . . . . . . . . . 4396 1 113 . 1 1 17 17 SER HB3 H 1 3.554 . . . . . . . . . . . 4396 1 114 . 1 1 18 18 LYS N N 15 131.16 . . . . . . . . . . . 4396 1 115 . 1 1 18 18 LYS H H 1 9.249 . . . . . . . . . . . 4396 1 116 . 1 1 18 18 LYS HA H 1 4.160 . . . . . . . . . . . 4396 1 117 . 1 1 18 18 LYS HB2 H 1 1.892 . . . . . . . . . . . 4396 1 118 . 1 1 18 18 LYS HB3 H 1 1.749 . . . . . . . . . . . 4396 1 119 . 1 1 18 18 LYS HG2 H 1 1.438 . . . . . . . . . . . 4396 1 120 . 1 1 18 18 LYS HG3 H 1 1.438 . . . . . . . . . . . 4396 1 121 . 1 1 18 18 LYS HD2 H 1 1.595 . . . . . . . . . . . 4396 1 122 . 1 1 18 18 LYS HD3 H 1 1.595 . . . . . . . . . . . 4396 1 123 . 1 1 19 19 GLU N N 15 120.262 . . . . . . . . . . . 4396 1 124 . 1 1 19 19 GLU H H 1 8.553 . . . . . . . . . . . 4396 1 125 . 1 1 19 19 GLU HA H 1 4.172 . . . . . . . . . . . 4396 1 126 . 1 1 19 19 GLU HB2 H 1 2.100 . . . . . . . . . . . 4396 1 127 . 1 1 19 19 GLU HB3 H 1 1.984 . . . . . . . . . . . 4396 1 128 . 1 1 19 19 GLU HG2 H 1 2.387 . . . . . . . . . . . 4396 1 129 . 1 1 19 19 GLU HG3 H 1 2.387 . . . . . . . . . . . 4396 1 130 . 1 1 20 20 CYS N N 15 115.120 . . . . . . . . . . . 4396 1 131 . 1 1 20 20 CYS H H 1 7.638 . . . . . . . . . . . 4396 1 132 . 1 1 20 20 CYS HA H 1 4.782 . . . . . . . . . . . 4396 1 133 . 1 1 20 20 CYS HB2 H 1 3.479 . . . . . . . . . . . 4396 1 134 . 1 1 20 20 CYS HB3 H 1 3.111 . . . . . . . . . . . 4396 1 135 . 1 1 21 21 ASP N N 15 123.113 . . . . . . . . . . . 4396 1 136 . 1 1 21 21 ASP H H 1 7.481 . . . . . . . . . . . 4396 1 137 . 1 1 21 21 ASP HA H 1 4.546 . . . . . . . . . . . 4396 1 138 . 1 1 21 21 ASP HB2 H 1 2.801 . . . . . . . . . . . 4396 1 139 . 1 1 21 21 ASP HB3 H 1 2.726 . . . . . . . . . . . 4396 1 140 . 1 1 22 22 LYS N N 15 123.744 . . . . . . . . . . . 4396 1 141 . 1 1 22 22 LYS H H 1 8.942 . . . . . . . . . . . 4396 1 142 . 1 1 22 22 LYS HA H 1 4.353 . . . . . . . . . . . 4396 1 143 . 1 1 22 22 LYS HB2 H 1 1.949 . . . . . . . . . . . 4396 1 144 . 1 1 22 22 LYS HB3 H 1 1.949 . . . . . . . . . . . 4396 1 145 . 1 1 22 22 LYS HG2 H 1 1.560 . . . . . . . . . . . 4396 1 146 . 1 1 22 22 LYS HG3 H 1 1.560 . . . . . . . . . . . 4396 1 147 . 1 1 22 22 LYS HD2 H 1 1.695 . . . . . . . . . . . 4396 1 148 . 1 1 22 22 LYS HD3 H 1 1.695 . . . . . . . . . . . 4396 1 149 . 1 1 23 23 LYS N N 15 122.056 . . . . . . . . . . . 4396 1 150 . 1 1 23 23 LYS H H 1 8.591 . . . . . . . . . . . 4396 1 151 . 1 1 23 23 LYS HA H 1 4.978 . . . . . . . . . . . 4396 1 152 . 1 1 23 23 LYS HB2 H 1 2.097 . . . . . . . . . . . 4396 1 153 . 1 1 23 23 LYS HB3 H 1 2.097 . . . . . . . . . . . 4396 1 154 . 1 1 23 23 LYS HG2 H 1 1.556 . . . . . . . . . . . 4396 1 155 . 1 1 23 23 LYS HG3 H 1 1.556 . . . . . . . . . . . 4396 1 156 . 1 1 23 23 LYS HD2 H 1 1.696 . . . . . . . . . . . 4396 1 157 . 1 1 23 23 LYS HD3 H 1 1.696 . . . . . . . . . . . 4396 1 158 . 1 1 24 24 CYS N N 15 120.125 . . . . . . . . . . . 4396 1 159 . 1 1 24 24 CYS H H 1 8.396 . . . . . . . . . . . 4396 1 160 . 1 1 24 24 CYS HA H 1 4.082 . . . . . . . . . . . 4396 1 161 . 1 1 24 24 CYS HB2 H 1 2.722 . . . . . . . . . . . 4396 1 162 . 1 1 24 24 CYS HB3 H 1 2.642 . . . . . . . . . . . 4396 1 163 . 1 1 25 25 LYS HA H 1 4.199 . . . . . . . . . . . 4396 1 164 . 1 1 25 25 LYS HB2 H 1 2.10 . . . . . . . . . . . 4396 1 165 . 1 1 25 25 LYS HB3 H 1 1.98 . . . . . . . . . . . 4396 1 166 . 1 1 25 25 LYS HG2 H 1 1.24 . . . . . . . . . . . 4396 1 167 . 1 1 25 25 LYS HG3 H 1 1.24 . . . . . . . . . . . 4396 1 168 . 1 1 25 25 LYS HD2 H 1 1.609 . . . . . . . . . . . 4396 1 169 . 1 1 25 25 LYS HD3 H 1 1.609 . . . . . . . . . . . 4396 1 170 . 1 1 26 26 TYR N N 15 122.090 . . . . . . . . . . . 4396 1 171 . 1 1 26 26 TYR H H 1 8.225 . . . . . . . . . . . 4396 1 172 . 1 1 26 26 TYR HA H 1 4.625 . . . . . . . . . . . 4396 1 173 . 1 1 26 26 TYR HB2 H 1 3.168 . . . . . . . . . . . 4396 1 174 . 1 1 26 26 TYR HB3 H 1 2.776 . . . . . . . . . . . 4396 1 175 . 1 1 26 26 TYR HD1 H 1 7.054 . . . . . . . . . . . 4396 1 176 . 1 1 26 26 TYR HD2 H 1 7.054 . . . . . . . . . . . 4396 1 177 . 1 1 26 26 TYR HE1 H 1 6.841 . . . . . . . . . . . 4396 1 178 . 1 1 26 26 TYR HE2 H 1 6.841 . . . . . . . . . . . 4396 1 179 . 1 1 27 27 ASP N N 15 121.092 . . . . . . . . . . . 4396 1 180 . 1 1 27 27 ASP H H 1 8.240 . . . . . . . . . . . 4396 1 181 . 1 1 27 27 ASP HA H 1 4.593 . . . . . . . . . . . 4396 1 182 . 1 1 27 27 ASP HB2 H 1 2.721 . . . . . . . . . . . 4396 1 183 . 1 1 27 27 ASP HB3 H 1 2.721 . . . . . . . . . . . 4396 1 184 . 1 1 28 28 GLY N N 15 109.440 . . . . . . . . . . . 4396 1 185 . 1 1 28 28 GLY H H 1 8.100 . . . . . . . . . . . 4396 1 186 . 1 1 28 28 GLY HA2 H 1 4.007 . . . . . . . . . . . 4396 1 187 . 1 1 28 28 GLY HA3 H 1 3.848 . . . . . . . . . . . 4396 1 188 . 1 1 29 29 VAL N N 15 119.706 . . . . . . . . . . . 4396 1 189 . 1 1 29 29 VAL H H 1 7.852 . . . . . . . . . . . 4396 1 190 . 1 1 29 29 VAL HA H 1 4.102 . . . . . . . . . . . 4396 1 191 . 1 1 29 29 VAL HB H 1 2.099 . . . . . . . . . . . 4396 1 192 . 1 1 29 29 VAL HG11 H 1 0.897 . . . . . . . . . . . 4396 1 193 . 1 1 29 29 VAL HG12 H 1 0.897 . . . . . . . . . . . 4396 1 194 . 1 1 29 29 VAL HG13 H 1 0.897 . . . . . . . . . . . 4396 1 195 . 1 1 29 29 VAL HG21 H 1 0.897 . . . . . . . . . . . 4396 1 196 . 1 1 29 29 VAL HG22 H 1 0.897 . . . . . . . . . . . 4396 1 197 . 1 1 29 29 VAL HG23 H 1 0.897 . . . . . . . . . . . 4396 1 198 . 1 1 30 30 GLU N N 15 124.047 . . . . . . . . . . . 4396 1 199 . 1 1 30 30 GLU H H 1 8.471 . . . . . . . . . . . 4396 1 200 . 1 1 30 30 GLU HA H 1 4.316 . . . . . . . . . . . 4396 1 201 . 1 1 30 30 GLU HB2 H 1 2.099 . . . . . . . . . . . 4396 1 202 . 1 1 30 30 GLU HB3 H 1 1.982 . . . . . . . . . . . 4396 1 203 . 1 1 30 30 GLU HG2 H 1 2.34 . . . . . . . . . . . 4396 1 204 . 1 1 30 30 GLU HG3 H 1 2.34 . . . . . . . . . . . 4396 1 205 . 1 1 31 31 GLU N N 15 122.045 . . . . . . . . . . . 4396 1 206 . 1 1 31 31 GLU H H 1 8.319 . . . . . . . . . . . 4396 1 207 . 1 1 31 31 GLU HA H 1 4.315 . . . . . . . . . . . 4396 1 208 . 1 1 31 31 GLU HB2 H 1 2.101 . . . . . . . . . . . 4396 1 209 . 1 1 31 31 GLU HB3 H 1 1.983 . . . . . . . . . . . 4396 1 210 . 1 1 31 31 GLU HG2 H 1 2.372 . . . . . . . . . . . 4396 1 211 . 1 1 31 31 GLU HG3 H 1 2.372 . . . . . . . . . . . 4396 1 212 . 1 1 32 32 GLU N N 15 121.888 . . . . . . . . . . . 4396 1 213 . 1 1 32 32 GLU H H 1 8.356 . . . . . . . . . . . 4396 1 214 . 1 1 32 32 GLU HA H 1 4.316 . . . . . . . . . . . 4396 1 215 . 1 1 32 32 GLU HB2 H 1 2.101 . . . . . . . . . . . 4396 1 216 . 1 1 32 32 GLU HB3 H 1 1.983 . . . . . . . . . . . 4396 1 217 . 1 1 32 32 GLU HG2 H 1 2.390 . . . . . . . . . . . 4396 1 218 . 1 1 32 32 GLU HG3 H 1 2.390 . . . . . . . . . . . 4396 1 219 . 1 1 33 33 ASP N N 15 121.05 . . . . . . . . . . . 4396 1 220 . 1 1 33 33 ASP H H 1 8.41 . . . . . . . . . . . 4396 1 221 . 1 1 33 33 ASP HA H 1 4.648 . . . . . . . . . . . 4396 1 222 . 1 1 33 33 ASP HB2 H 1 2.837 . . . . . . . . . . . 4396 1 223 . 1 1 33 33 ASP HB3 H 1 2.757 . . . . . . . . . . . 4396 1 224 . 1 1 34 34 ASP N N 15 120.528 . . . . . . . . . . . 4396 1 225 . 1 1 34 34 ASP H H 1 8.280 . . . . . . . . . . . 4396 1 226 . 1 1 34 34 ASP HA H 1 4.652 . . . . . . . . . . . 4396 1 227 . 1 1 34 34 ASP HB2 H 1 2.840 . . . . . . . . . . . 4396 1 228 . 1 1 34 34 ASP HB3 H 1 2.762 . . . . . . . . . . . 4396 1 229 . 1 1 35 35 GLU N N 15 120.506 . . . . . . . . . . . 4396 1 230 . 1 1 35 35 GLU H H 1 8.187 . . . . . . . . . . . 4396 1 231 . 1 1 35 35 GLU HA H 1 4.337 . . . . . . . . . . . 4396 1 232 . 1 1 35 35 GLU HB2 H 1 2.139 . . . . . . . . . . . 4396 1 233 . 1 1 35 35 GLU HB3 H 1 1.985 . . . . . . . . . . . 4396 1 234 . 1 1 35 35 GLU HG2 H 1 2.410 . . . . . . . . . . . 4396 1 235 . 1 1 35 35 GLU HG3 H 1 2.410 . . . . . . . . . . . 4396 1 236 . 1 1 36 36 GLU N N 15 122.444 . . . . . . . . . . . 4396 1 237 . 1 1 36 36 GLU H H 1 8.163 . . . . . . . . . . . 4396 1 238 . 1 1 36 36 GLU HA H 1 4.647 . . . . . . . . . . . 4396 1 239 . 1 1 36 36 GLU HB2 H 1 2.126 . . . . . . . . . . . 4396 1 240 . 1 1 36 36 GLU HB3 H 1 1.947 . . . . . . . . . . . 4396 1 241 . 1 1 36 36 GLU HG2 H 1 2.432 . . . . . . . . . . . 4396 1 242 . 1 1 36 36 GLU HG3 H 1 2.432 . . . . . . . . . . . 4396 1 243 . 1 1 37 37 PRO CD C 13 50.8 . . . . . . . . . . . 4396 1 244 . 1 1 37 37 PRO HA H 1 4.404 . . . . . . . . . . . 4396 1 245 . 1 1 37 37 PRO HB2 H 1 2.290 . . . . . . . . . . . 4396 1 246 . 1 1 37 37 PRO HB3 H 1 2.017 . . . . . . . . . . . 4396 1 247 . 1 1 37 37 PRO HG2 H 1 1.899 . . . . . . . . . . . 4396 1 248 . 1 1 37 37 PRO HG3 H 1 1.899 . . . . . . . . . . . 4396 1 249 . 1 1 37 37 PRO HD2 H 1 3.763 . . . . . . . . . . . 4396 1 250 . 1 1 37 37 PRO HD3 H 1 3.685 . . . . . . . . . . . 4396 1 251 . 1 1 38 38 ASN N N 15 119.682 . . . . . . . . . . . 4396 1 252 . 1 1 38 38 ASN ND2 N 15 113.7 . . . . . . . . . . . 4396 1 253 . 1 1 38 38 ASN H H 1 8.537 . . . . . . . . . . . 4396 1 254 . 1 1 38 38 ASN HA H 1 4.684 . . . . . . . . . . . 4396 1 255 . 1 1 38 38 ASN HB2 H 1 2.836 . . . . . . . . . . . 4396 1 256 . 1 1 38 38 ASN HB3 H 1 2.765 . . . . . . . . . . . 4396 1 257 . 1 1 38 38 ASN HD21 H 1 7.602 . . . . . . . . . . . 4396 1 258 . 1 1 38 38 ASN HD22 H 1 6.923 . . . . . . . . . . . 4396 1 259 . 1 1 39 39 VAL N N 15 122.476 . . . . . . . . . . . 4396 1 260 . 1 1 39 39 VAL H H 1 8.006 . . . . . . . . . . . 4396 1 261 . 1 1 39 39 VAL HA H 1 4.392 . . . . . . . . . . . 4396 1 262 . 1 1 39 39 VAL HB H 1 2.119 . . . . . . . . . . . 4396 1 263 . 1 1 39 39 VAL HG11 H 1 0.953 . . . . . . . . . . . 4396 1 264 . 1 1 39 39 VAL HG12 H 1 0.953 . . . . . . . . . . . 4396 1 265 . 1 1 39 39 VAL HG13 H 1 0.953 . . . . . . . . . . . 4396 1 266 . 1 1 39 39 VAL HG21 H 1 0.953 . . . . . . . . . . . 4396 1 267 . 1 1 39 39 VAL HG22 H 1 0.953 . . . . . . . . . . . 4396 1 268 . 1 1 39 39 VAL HG23 H 1 0.953 . . . . . . . . . . . 4396 1 269 . 1 1 40 40 PRO HA H 1 4.368 . . . . . . . . . . . 4396 1 270 . 1 1 40 40 PRO HB2 H 1 2.289 . . . . . . . . . . . 4396 1 271 . 1 1 40 40 PRO HB3 H 1 2.092 . . . . . . . . . . . 4396 1 272 . 1 1 40 40 PRO HG2 H 1 1.978 . . . . . . . . . . . 4396 1 273 . 1 1 40 40 PRO HG3 H 1 1.820 . . . . . . . . . . . 4396 1 274 . 1 1 40 40 PRO HD2 H 1 3.813 . . . . . . . . . . . 4396 1 275 . 1 1 40 40 PRO HD3 H 1 3.685 . . . . . . . . . . . 4396 1 276 . 1 1 41 41 CYS N N 15 121.122 . . . . . . . . . . . 4396 1 277 . 1 1 41 41 CYS H H 1 8.435 . . . . . . . . . . . 4396 1 278 . 1 1 41 41 CYS HA H 1 4.511 . . . . . . . . . . . 4396 1 279 . 1 1 41 41 CYS HB2 H 1 3.189 . . . . . . . . . . . 4396 1 280 . 1 1 41 41 CYS HB3 H 1 3.111 . . . . . . . . . . . 4396 1 281 . 1 1 42 42 LEU N N 15 128.458 . . . . . . . . . . . 4396 1 282 . 1 1 42 42 LEU CB C 13 42.6 . . . . . . . . . . . 4396 1 283 . 1 1 42 42 LEU H H 1 8.437 . . . . . . . . . . . 4396 1 284 . 1 1 42 42 LEU HA H 1 4.430 . . . . . . . . . . . 4396 1 285 . 1 1 42 42 LEU HB2 H 1 1.634 . . . . . . . . . . . 4396 1 286 . 1 1 42 42 LEU HB3 H 1 1.559 . . . . . . . . . . . 4396 1 287 . 1 1 42 42 LEU HD11 H 1 0.891 . . . . . . . . . . . 4396 1 288 . 1 1 42 42 LEU HD12 H 1 0.891 . . . . . . . . . . . 4396 1 289 . 1 1 42 42 LEU HD13 H 1 0.891 . . . . . . . . . . . 4396 1 290 . 1 1 42 42 LEU HD21 H 1 0.853 . . . . . . . . . . . 4396 1 291 . 1 1 42 42 LEU HD22 H 1 0.853 . . . . . . . . . . . 4396 1 292 . 1 1 42 42 LEU HD23 H 1 0.853 . . . . . . . . . . . 4396 1 293 . 1 1 43 43 VAL N N 15 122.730 . . . . . . . . . . . 4396 1 294 . 1 1 43 43 VAL H H 1 8.105 . . . . . . . . . . . 4396 1 295 . 1 1 43 43 VAL HA H 1 4.082 . . . . . . . . . . . 4396 1 296 . 1 1 43 43 VAL HB H 1 2.024 . . . . . . . . . . . 4396 1 297 . 1 1 43 43 VAL HG11 H 1 0.877 . . . . . . . . . . . 4396 1 298 . 1 1 43 43 VAL HG12 H 1 0.877 . . . . . . . . . . . 4396 1 299 . 1 1 43 43 VAL HG13 H 1 0.877 . . . . . . . . . . . 4396 1 300 . 1 1 43 43 VAL HG21 H 1 0.877 . . . . . . . . . . . 4396 1 301 . 1 1 43 43 VAL HG22 H 1 0.877 . . . . . . . . . . . 4396 1 302 . 1 1 43 43 VAL HG23 H 1 0.877 . . . . . . . . . . . 4396 1 303 . 1 1 44 44 ARG N N 15 125.838 . . . . . . . . . . . 4396 1 304 . 1 1 44 44 ARG H H 1 8.436 . . . . . . . . . . . 4396 1 305 . 1 1 44 44 ARG HA H 1 4.239 . . . . . . . . . . . 4396 1 306 . 1 1 44 44 ARG HB2 H 1 1.909 . . . . . . . . . . . 4396 1 307 . 1 1 44 44 ARG HB3 H 1 1.787 . . . . . . . . . . . 4396 1 308 . 1 1 44 44 ARG HG2 H 1 1.618 . . . . . . . . . . . 4396 1 309 . 1 1 44 44 ARG HG3 H 1 1.618 . . . . . . . . . . . 4396 1 310 . 1 1 44 44 ARG HD2 H 1 3.17 . . . . . . . . . . . 4396 1 311 . 1 1 44 44 ARG HD3 H 1 3.17 . . . . . . . . . . . 4396 1 312 . 1 1 45 45 VAL N N 15 119.467 . . . . . . . . . . . 4396 1 313 . 1 1 45 45 VAL H H 1 7.597 . . . . . . . . . . . 4396 1 314 . 1 1 45 45 VAL HA H 1 4.105 . . . . . . . . . . . 4396 1 315 . 1 1 45 45 VAL HB H 1 1.924 . . . . . . . . . . . 4396 1 316 . 1 1 45 45 VAL HG11 H 1 0.857 . . . . . . . . . . . 4396 1 317 . 1 1 45 45 VAL HG12 H 1 0.857 . . . . . . . . . . . 4396 1 318 . 1 1 45 45 VAL HG13 H 1 0.857 . . . . . . . . . . . 4396 1 319 . 1 1 45 45 VAL HG21 H 1 0.857 . . . . . . . . . . . 4396 1 320 . 1 1 45 45 VAL HG22 H 1 0.857 . . . . . . . . . . . 4396 1 321 . 1 1 45 45 VAL HG23 H 1 0.857 . . . . . . . . . . . 4396 1 322 . 1 1 46 46 CYS N N 15 124.023 . . . . . . . . . . . 4396 1 323 . 1 1 46 46 CYS H H 1 8.632 . . . . . . . . . . . 4396 1 324 . 1 1 46 46 CYS HA H 1 4.549 . . . . . . . . . . . 4396 1 325 . 1 1 46 46 CYS HB2 H 1 3.111 . . . . . . . . . . . 4396 1 326 . 1 1 46 46 CYS HB3 H 1 2.840 . . . . . . . . . . . 4396 1 327 . 1 1 47 47 HIS HA H 1 4.85 . . . . . . . . . . . 4396 1 328 . 1 1 47 47 HIS HB2 H 1 3.26 . . . . . . . . . . . 4396 1 329 . 1 1 47 47 HIS HB3 H 1 3.26 . . . . . . . . . . . 4396 1 330 . 1 1 47 47 HIS HD2 H 1 7.35 . . . . . . . . . . . 4396 1 331 . 1 1 47 47 HIS HE1 H 1 8.70 . . . . . . . . . . . 4396 1 332 . 1 1 48 48 GLN N N 15 120.652 . . . . . . . . . . . 4396 1 333 . 1 1 48 48 GLN NE2 N 15 113.0 . . . . . . . . . . . 4396 1 334 . 1 1 48 48 GLN H H 1 8.406 . . . . . . . . . . . 4396 1 335 . 1 1 48 48 GLN HA H 1 4.85 . . . . . . . . . . . 4396 1 336 . 1 1 48 48 GLN HB2 H 1 2.29 . . . . . . . . . . . 4396 1 337 . 1 1 48 48 GLN HB3 H 1 2.10 . . . . . . . . . . . 4396 1 338 . 1 1 48 48 GLN HG2 H 1 2.47 . . . . . . . . . . . 4396 1 339 . 1 1 48 48 GLN HG3 H 1 2.47 . . . . . . . . . . . 4396 1 340 . 1 1 48 48 GLN HE21 H 1 7.539 . . . . . . . . . . . 4396 1 341 . 1 1 48 48 GLN HE22 H 1 6.879 . . . . . . . . . . . 4396 1 342 . 1 1 49 49 ASP N N 15 123.482 . . . . . . . . . . . 4396 1 343 . 1 1 49 49 ASP H H 1 8.550 . . . . . . . . . . . 4396 1 344 . 1 1 49 49 ASP HA H 1 4.862 . . . . . . . . . . . 4396 1 345 . 1 1 49 49 ASP HB2 H 1 2.487 . . . . . . . . . . . 4396 1 346 . 1 1 49 49 ASP HB3 H 1 2.257 . . . . . . . . . . . 4396 1 347 . 1 1 50 50 CYS N N 15 119.515 . . . . . . . . . . . 4396 1 348 . 1 1 50 50 CYS H H 1 8.644 . . . . . . . . . . . 4396 1 349 . 1 1 50 50 CYS HA H 1 5.209 . . . . . . . . . . . 4396 1 350 . 1 1 50 50 CYS HB2 H 1 2.957 . . . . . . . . . . . 4396 1 351 . 1 1 50 50 CYS HB3 H 1 2.841 . . . . . . . . . . . 4396 1 352 . 1 1 51 51 VAL N N 15 116.200 . . . . . . . . . . . 4396 1 353 . 1 1 51 51 VAL CG1 C 13 21.4 . . . . . . . . . . . 4396 1 354 . 1 1 51 51 VAL H H 1 8.709 . . . . . . . . . . . 4396 1 355 . 1 1 51 51 VAL HA H 1 4.666 . . . . . . . . . . . 4396 1 356 . 1 1 51 51 VAL HB H 1 2.839 . . . . . . . . . . . 4396 1 357 . 1 1 51 51 VAL HG11 H 1 0.757 . . . . . . . . . . . 4396 1 358 . 1 1 51 51 VAL HG12 H 1 0.757 . . . . . . . . . . . 4396 1 359 . 1 1 51 51 VAL HG13 H 1 0.757 . . . . . . . . . . . 4396 1 360 . 1 1 51 51 VAL HG21 H 1 0.643 . . . . . . . . . . . 4396 1 361 . 1 1 51 51 VAL HG22 H 1 0.643 . . . . . . . . . . . 4396 1 362 . 1 1 51 51 VAL HG23 H 1 0.643 . . . . . . . . . . . 4396 1 363 . 1 1 52 52 CYS N N 15 118.373 . . . . . . . . . . . 4396 1 364 . 1 1 52 52 CYS H H 1 9.449 . . . . . . . . . . . 4396 1 365 . 1 1 52 52 CYS HA H 1 4.912 . . . . . . . . . . . 4396 1 366 . 1 1 52 52 CYS HB2 H 1 3.151 . . . . . . . . . . . 4396 1 367 . 1 1 52 52 CYS HB3 H 1 2.647 . . . . . . . . . . . 4396 1 368 . 1 1 53 53 GLU N N 15 121.210 . . . . . . . . . . . 4396 1 369 . 1 1 53 53 GLU H H 1 8.328 . . . . . . . . . . . 4396 1 370 . 1 1 53 53 GLU HA H 1 3.965 . . . . . . . . . . . 4396 1 371 . 1 1 53 53 GLU HB2 H 1 1.655 . . . . . . . . . . . 4396 1 372 . 1 1 53 53 GLU HB3 H 1 1.655 . . . . . . . . . . . 4396 1 373 . 1 1 53 53 GLU HG2 H 1 2.099 . . . . . . . . . . . 4396 1 374 . 1 1 53 53 GLU HG3 H 1 2.099 . . . . . . . . . . . 4396 1 375 . 1 1 54 54 GLU N N 15 122.655 . . . . . . . . . . . 4396 1 376 . 1 1 54 54 GLU H H 1 8.666 . . . . . . . . . . . 4396 1 377 . 1 1 54 54 GLU HA H 1 4.047 . . . . . . . . . . . 4396 1 378 . 1 1 54 54 GLU HB2 H 1 2.061 . . . . . . . . . . . 4396 1 379 . 1 1 54 54 GLU HB3 H 1 1.986 . . . . . . . . . . . 4396 1 380 . 1 1 54 54 GLU HG2 H 1 2.396 . . . . . . . . . . . 4396 1 381 . 1 1 54 54 GLU HG3 H 1 2.396 . . . . . . . . . . . 4396 1 382 . 1 1 55 55 GLY N N 15 113.471 . . . . . . . . . . . 4396 1 383 . 1 1 55 55 GLY H H 1 8.512 . . . . . . . . . . . 4396 1 384 . 1 1 55 55 GLY HA2 H 1 4.060 . . . . . . . . . . . 4396 1 385 . 1 1 55 55 GLY HA3 H 1 3.452 . . . . . . . . . . . 4396 1 386 . 1 1 56 56 PHE N N 15 118.209 . . . . . . . . . . . 4396 1 387 . 1 1 56 56 PHE H H 1 7.735 . . . . . . . . . . . 4396 1 388 . 1 1 56 56 PHE HA H 1 4.859 . . . . . . . . . . . 4396 1 389 . 1 1 56 56 PHE HB2 H 1 3.036 . . . . . . . . . . . 4396 1 390 . 1 1 56 56 PHE HB3 H 1 2.645 . . . . . . . . . . . 4396 1 391 . 1 1 56 56 PHE HD1 H 1 6.727 . . . . . . . . . . . 4396 1 392 . 1 1 56 56 PHE HD2 H 1 6.727 . . . . . . . . . . . 4396 1 393 . 1 1 56 56 PHE HE1 H 1 7.192 . . . . . . . . . . . 4396 1 394 . 1 1 56 56 PHE HE2 H 1 7.192 . . . . . . . . . . . 4396 1 395 . 1 1 56 56 PHE HZ H 1 7.348 . . . . . . . . . . . 4396 1 396 . 1 1 57 57 TYR N N 15 120.327 . . . . . . . . . . . 4396 1 397 . 1 1 57 57 TYR H H 1 9.754 . . . . . . . . . . . 4396 1 398 . 1 1 57 57 TYR HA H 1 4.563 . . . . . . . . . . . 4396 1 399 . 1 1 57 57 TYR HB2 H 1 2.644 . . . . . . . . . . . 4396 1 400 . 1 1 57 57 TYR HB3 H 1 2.528 . . . . . . . . . . . 4396 1 401 . 1 1 57 57 TYR HD1 H 1 6.883 . . . . . . . . . . . 4396 1 402 . 1 1 57 57 TYR HD2 H 1 6.883 . . . . . . . . . . . 4396 1 403 . 1 1 57 57 TYR HE1 H 1 6.670 . . . . . . . . . . . 4396 1 404 . 1 1 57 57 TYR HE2 H 1 6.670 . . . . . . . . . . . 4396 1 405 . 1 1 58 58 ARG N N 15 120.097 . . . . . . . . . . . 4396 1 406 . 1 1 58 58 ARG H H 1 9.249 . . . . . . . . . . . 4396 1 407 . 1 1 58 58 ARG HA H 1 4.900 . . . . . . . . . . . 4396 1 408 . 1 1 58 58 ARG HB2 H 1 2.100 . . . . . . . . . . . 4396 1 409 . 1 1 58 58 ARG HB3 H 1 1.948 . . . . . . . . . . . 4396 1 410 . 1 1 58 58 ARG HG2 H 1 1.869 . . . . . . . . . . . 4396 1 411 . 1 1 58 58 ARG HG3 H 1 1.719 . . . . . . . . . . . 4396 1 412 . 1 1 59 59 ASN N N 15 127.920 . . . . . . . . . . . 4396 1 413 . 1 1 59 59 ASN ND2 N 15 113.6 . . . . . . . . . . . 4396 1 414 . 1 1 59 59 ASN H H 1 9.292 . . . . . . . . . . . 4396 1 415 . 1 1 59 59 ASN HA H 1 4.787 . . . . . . . . . . . 4396 1 416 . 1 1 59 59 ASN HB2 H 1 4.336 . . . . . . . . . . . 4396 1 417 . 1 1 59 59 ASN HB3 H 1 3.034 . . . . . . . . . . . 4396 1 418 . 1 1 59 59 ASN HD21 H 1 7.740 . . . . . . . . . . . 4396 1 419 . 1 1 59 59 ASN HD22 H 1 7.232 . . . . . . . . . . . 4396 1 420 . 1 1 60 60 LYS N N 15 119.505 . . . . . . . . . . . 4396 1 421 . 1 1 60 60 LYS H H 1 8.864 . . . . . . . . . . . 4396 1 422 . 1 1 60 60 LYS HA H 1 4.174 . . . . . . . . . . . 4396 1 423 . 1 1 60 60 LYS HB2 H 1 1.869 . . . . . . . . . . . 4396 1 424 . 1 1 60 60 LYS HB3 H 1 1.778 . . . . . . . . . . . 4396 1 425 . 1 1 60 60 LYS HG2 H 1 1.365 . . . . . . . . . . . 4396 1 426 . 1 1 60 60 LYS HG3 H 1 1.365 . . . . . . . . . . . 4396 1 427 . 1 1 60 60 LYS HD2 H 1 1.579 . . . . . . . . . . . 4396 1 428 . 1 1 60 60 LYS HD3 H 1 1.579 . . . . . . . . . . . 4396 1 429 . 1 1 61 61 ASP N N 15 119.503 . . . . . . . . . . . 4396 1 430 . 1 1 61 61 ASP H H 1 7.464 . . . . . . . . . . . 4396 1 431 . 1 1 61 61 ASP HA H 1 4.897 . . . . . . . . . . . 4396 1 432 . 1 1 61 61 ASP HB2 H 1 2.995 . . . . . . . . . . . 4396 1 433 . 1 1 61 61 ASP HB3 H 1 2.528 . . . . . . . . . . . 4396 1 434 . 1 1 62 62 ASP N N 15 117.211 . . . . . . . . . . . 4396 1 435 . 1 1 62 62 ASP CB C 13 39.1 . . . . . . . . . . . 4396 1 436 . 1 1 62 62 ASP H H 1 8.512 . . . . . . . . . . . 4396 1 437 . 1 1 62 62 ASP HA H 1 4.354 . . . . . . . . . . . 4396 1 438 . 1 1 62 62 ASP HB2 H 1 3.304 . . . . . . . . . . . 4396 1 439 . 1 1 62 62 ASP HB3 H 1 2.667 . . . . . . . . . . . 4396 1 440 . 1 1 63 63 LYS N N 15 120.606 . . . . . . . . . . . 4396 1 441 . 1 1 63 63 LYS H H 1 8.126 . . . . . . . . . . . 4396 1 442 . 1 1 63 63 LYS HA H 1 4.584 . . . . . . . . . . . 4396 1 443 . 1 1 63 63 LYS HB2 H 1 1.829 . . . . . . . . . . . 4396 1 444 . 1 1 63 63 LYS HB3 H 1 1.829 . . . . . . . . . . . 4396 1 445 . 1 1 63 63 LYS HG2 H 1 1.459 . . . . . . . . . . . 4396 1 446 . 1 1 63 63 LYS HG3 H 1 1.355 . . . . . . . . . . . 4396 1 447 . 1 1 63 63 LYS HD2 H 1 1.646 . . . . . . . . . . . 4396 1 448 . 1 1 63 63 LYS HD3 H 1 1.646 . . . . . . . . . . . 4396 1 449 . 1 1 64 64 CYS N N 15 122.460 . . . . . . . . . . . 4396 1 450 . 1 1 64 64 CYS H H 1 9.216 . . . . . . . . . . . 4396 1 451 . 1 1 64 64 CYS HA H 1 4.939 . . . . . . . . . . . 4396 1 452 . 1 1 64 64 CYS HB2 H 1 2.993 . . . . . . . . . . . 4396 1 453 . 1 1 64 64 CYS HB3 H 1 2.484 . . . . . . . . . . . 4396 1 454 . 1 1 65 65 VAL N N 15 120.922 . . . . . . . . . . . 4396 1 455 . 1 1 65 65 VAL CG2 C 13 18.6 . . . . . . . . . . . 4396 1 456 . 1 1 65 65 VAL H H 1 10.069 . . . . . . . . . . . 4396 1 457 . 1 1 65 65 VAL HA H 1 5.150 . . . . . . . . . . . 4396 1 458 . 1 1 65 65 VAL HB H 1 2.607 . . . . . . . . . . . 4396 1 459 . 1 1 65 65 VAL HG11 H 1 1.05 . . . . . . . . . . . 4396 1 460 . 1 1 65 65 VAL HG12 H 1 1.05 . . . . . . . . . . . 4396 1 461 . 1 1 65 65 VAL HG13 H 1 1.05 . . . . . . . . . . . 4396 1 462 . 1 1 65 65 VAL HG21 H 1 0.935 . . . . . . . . . . . 4396 1 463 . 1 1 65 65 VAL HG22 H 1 0.935 . . . . . . . . . . . 4396 1 464 . 1 1 65 65 VAL HG23 H 1 0.935 . . . . . . . . . . . 4396 1 465 . 1 1 66 66 SER N N 15 118.728 . . . . . . . . . . . 4396 1 466 . 1 1 66 66 SER H H 1 9.250 . . . . . . . . . . . 4396 1 467 . 1 1 66 66 SER HA H 1 4.242 . . . . . . . . . . . 4396 1 468 . 1 1 66 66 SER HB2 H 1 3.962 . . . . . . . . . . . 4396 1 469 . 1 1 66 66 SER HB3 H 1 3.962 . . . . . . . . . . . 4396 1 470 . 1 1 67 67 ALA N N 15 122.354 . . . . . . . . . . . 4396 1 471 . 1 1 67 67 ALA CA C 13 56.0 . . . . . . . . . . . 4396 1 472 . 1 1 67 67 ALA CB C 13 18.1 . . . . . . . . . . . 4396 1 473 . 1 1 67 67 ALA H H 1 8.941 . . . . . . . . . . . 4396 1 474 . 1 1 67 67 ALA HA H 1 3.644 . . . . . . . . . . . 4396 1 475 . 1 1 67 67 ALA HB1 H 1 1.323 . . . . . . . . . . . 4396 1 476 . 1 1 67 67 ALA HB2 H 1 1.323 . . . . . . . . . . . 4396 1 477 . 1 1 67 67 ALA HB3 H 1 1.323 . . . . . . . . . . . 4396 1 478 . 1 1 68 68 GLU N N 15 116.779 . . . . . . . . . . . 4396 1 479 . 1 1 68 68 GLU H H 1 8.512 . . . . . . . . . . . 4396 1 480 . 1 1 68 68 GLU HA H 1 4.048 . . . . . . . . . . . 4396 1 481 . 1 1 68 68 GLU HB2 H 1 2.061 . . . . . . . . . . . 4396 1 482 . 1 1 68 68 GLU HB3 H 1 1.983 . . . . . . . . . . . 4396 1 483 . 1 1 68 68 GLU HG2 H 1 2.464 . . . . . . . . . . . 4396 1 484 . 1 1 68 68 GLU HG3 H 1 2.373 . . . . . . . . . . . 4396 1 485 . 1 1 69 69 ASP N N 15 121.852 . . . . . . . . . . . 4396 1 486 . 1 1 69 69 ASP H H 1 7.852 . . . . . . . . . . . 4396 1 487 . 1 1 69 69 ASP HA H 1 4.665 . . . . . . . . . . . 4396 1 488 . 1 1 69 69 ASP HB2 H 1 3.032 . . . . . . . . . . . 4396 1 489 . 1 1 69 69 ASP HB3 H 1 2.760 . . . . . . . . . . . 4396 1 490 . 1 1 70 70 CYS N N 15 122.467 . . . . . . . . . . . 4396 1 491 . 1 1 70 70 CYS H H 1 8.278 . . . . . . . . . . . 4396 1 492 . 1 1 70 70 CYS HA H 1 4.368 . . . . . . . . . . . 4396 1 493 . 1 1 70 70 CYS HB2 H 1 3.205 . . . . . . . . . . . 4396 1 494 . 1 1 70 70 CYS HB3 H 1 2.896 . . . . . . . . . . . 4396 1 495 . 1 1 71 71 GLU N N 15 117.291 . . . . . . . . . . . 4396 1 496 . 1 1 71 71 GLU H H 1 7.675 . . . . . . . . . . . 4396 1 497 . 1 1 71 71 GLU HA H 1 4.236 . . . . . . . . . . . 4396 1 498 . 1 1 71 71 GLU HB2 H 1 2.215 . . . . . . . . . . . 4396 1 499 . 1 1 71 71 GLU HB3 H 1 2.103 . . . . . . . . . . . 4396 1 500 . 1 1 71 71 GLU HG2 H 1 2.486 . . . . . . . . . . . 4396 1 501 . 1 1 71 71 GLU HG3 H 1 2.486 . . . . . . . . . . . 4396 1 502 . 1 1 72 72 LEU N N 15 119.786 . . . . . . . . . . . 4396 1 503 . 1 1 72 72 LEU CB C 13 41.6 . . . . . . . . . . . 4396 1 504 . 1 1 72 72 LEU H H 1 7.617 . . . . . . . . . . . 4396 1 505 . 1 1 72 72 LEU HA H 1 4.224 . . . . . . . . . . . 4396 1 506 . 1 1 72 72 LEU HB2 H 1 1.901 . . . . . . . . . . . 4396 1 507 . 1 1 72 72 LEU HB3 H 1 1.649 . . . . . . . . . . . 4396 1 508 . 1 1 72 72 LEU HG H 1 1.769 . . . . . . . . . . . 4396 1 509 . 1 1 72 72 LEU HD11 H 1 0.965 . . . . . . . . . . . 4396 1 510 . 1 1 72 72 LEU HD12 H 1 0.965 . . . . . . . . . . . 4396 1 511 . 1 1 72 72 LEU HD13 H 1 0.965 . . . . . . . . . . . 4396 1 512 . 1 1 72 72 LEU HD21 H 1 0.888 . . . . . . . . . . . 4396 1 513 . 1 1 72 72 LEU HD22 H 1 0.888 . . . . . . . . . . . 4396 1 514 . 1 1 72 72 LEU HD23 H 1 0.888 . . . . . . . . . . . 4396 1 515 . 1 1 73 73 ASP N N 15 119.226 . . . . . . . . . . . 4396 1 516 . 1 1 73 73 ASP H H 1 7.870 . . . . . . . . . . . 4396 1 517 . 1 1 73 73 ASP HA H 1 4.567 . . . . . . . . . . . 4396 1 518 . 1 1 73 73 ASP HB3 H 1 2.898 . . . . . . . . . . . 4396 1 519 . 1 1 73 73 ASP HB2 H 1 2.778 . . . . . . . . . . . 4396 1 520 . 1 1 74 74 ASN N N 15 118.213 . . . . . . . . . . . 4396 1 521 . 1 1 74 74 ASN ND2 N 15 112.9 . . . . . . . . . . . 4396 1 522 . 1 1 74 74 ASN H H 1 7.834 . . . . . . . . . . . 4396 1 523 . 1 1 74 74 ASN HA H 1 4.665 . . . . . . . . . . . 4396 1 524 . 1 1 74 74 ASN HB2 H 1 2.892 . . . . . . . . . . . 4396 1 525 . 1 1 74 74 ASN HB3 H 1 2.666 . . . . . . . . . . . 4396 1 526 . 1 1 74 74 ASN HD21 H 1 7.504 . . . . . . . . . . . 4396 1 527 . 1 1 74 74 ASN HD22 H 1 6.725 . . . . . . . . . . . 4396 1 528 . 1 1 75 75 MET N N 15 120.800 . . . . . . . . . . . 4396 1 529 . 1 1 75 75 MET CE C 13 17.1 . . . . . . . . . . . 4396 1 530 . 1 1 75 75 MET H H 1 8.084 . . . . . . . . . . . 4396 1 531 . 1 1 75 75 MET HA H 1 4.406 . . . . . . . . . . . 4396 1 532 . 1 1 75 75 MET HB2 H 1 2.062 . . . . . . . . . . . 4396 1 533 . 1 1 75 75 MET HB3 H 1 1.974 . . . . . . . . . . . 4396 1 534 . 1 1 75 75 MET HG2 H 1 2.507 . . . . . . . . . . . 4396 1 535 . 1 1 75 75 MET HG3 H 1 2.507 . . . . . . . . . . . 4396 1 536 . 1 1 75 75 MET HE1 H 1 2.08 . . . . . . . . . . . 4396 1 537 . 1 1 75 75 MET HE2 H 1 2.08 . . . . . . . . . . . 4396 1 538 . 1 1 75 75 MET HE3 H 1 2.08 . . . . . . . . . . . 4396 1 539 . 1 1 76 76 ASP N N 15 120.094 . . . . . . . . . . . 4396 1 540 . 1 1 76 76 ASP H H 1 8.205 . . . . . . . . . . . 4396 1 541 . 1 1 76 76 ASP HA H 1 4.588 . . . . . . . . . . . 4396 1 542 . 1 1 76 76 ASP HB2 H 1 2.721 . . . . . . . . . . . 4396 1 543 . 1 1 76 76 ASP HB3 H 1 2.631 . . . . . . . . . . . 4396 1 544 . 1 1 77 77 PHE N N 15 120.586 . . . . . . . . . . . 4396 1 545 . 1 1 77 77 PHE H H 1 7.891 . . . . . . . . . . . 4396 1 546 . 1 1 77 77 PHE HA H 1 4.519 . . . . . . . . . . . 4396 1 547 . 1 1 77 77 PHE HB2 H 1 2.996 . . . . . . . . . . . 4396 1 548 . 1 1 77 77 PHE HB3 H 1 2.996 . . . . . . . . . . . 4396 1 549 . 1 1 77 77 PHE HD1 H 1 7.102 . . . . . . . . . . . 4396 1 550 . 1 1 77 77 PHE HD2 H 1 7.102 . . . . . . . . . . . 4396 1 551 . 1 1 77 77 PHE HE1 H 1 7.212 . . . . . . . . . . . 4396 1 552 . 1 1 77 77 PHE HE2 H 1 7.212 . . . . . . . . . . . 4396 1 553 . 1 1 77 77 PHE HZ H 1 7.32 . . . . . . . . . . . 4396 1 554 . 1 1 78 78 ILE N N 15 123.193 . . . . . . . . . . . 4396 1 555 . 1 1 78 78 ILE CB C 13 38.7 . . . . . . . . . . . 4396 1 556 . 1 1 78 78 ILE CG1 C 13 27.1 . . . . . . . . . . . 4396 1 557 . 1 1 78 78 ILE CG2 C 13 17.4 . . . . . . . . . . . 4396 1 558 . 1 1 78 78 ILE CD1 C 13 12.7 . . . . . . . . . . . 4396 1 559 . 1 1 78 78 ILE H H 1 7.735 . . . . . . . . . . . 4396 1 560 . 1 1 78 78 ILE HA H 1 4.041 . . . . . . . . . . . 4396 1 561 . 1 1 78 78 ILE HB H 1 1.673 . . . . . . . . . . . 4396 1 562 . 1 1 78 78 ILE HG12 H 1 1.340 . . . . . . . . . . . 4396 1 563 . 1 1 78 78 ILE HG13 H 1 1.063 . . . . . . . . . . . 4396 1 564 . 1 1 78 78 ILE HG21 H 1 0.72 . . . . . . . . . . . 4396 1 565 . 1 1 78 78 ILE HG22 H 1 0.72 . . . . . . . . . . . 4396 1 566 . 1 1 78 78 ILE HG23 H 1 0.72 . . . . . . . . . . . 4396 1 567 . 1 1 78 78 ILE HD11 H 1 0.78 . . . . . . . . . . . 4396 1 568 . 1 1 78 78 ILE HD12 H 1 0.78 . . . . . . . . . . . 4396 1 569 . 1 1 78 78 ILE HD13 H 1 0.78 . . . . . . . . . . . 4396 1 570 . 1 1 79 79 TYR N N 15 126.280 . . . . . . . . . . . 4396 1 571 . 1 1 79 79 TYR CA C 13 55.9 . . . . . . . . . . . 4396 1 572 . 1 1 79 79 TYR H H 1 8.221 . . . . . . . . . . . 4396 1 573 . 1 1 79 79 TYR HA H 1 4.743 . . . . . . . . . . . 4396 1 574 . 1 1 79 79 TYR HB3 H 1 3.046 . . . . . . . . . . . 4396 1 575 . 1 1 79 79 TYR HB2 H 1 2.894 . . . . . . . . . . . 4396 1 576 . 1 1 79 79 TYR HD1 H 1 7.190 . . . . . . . . . . . 4396 1 577 . 1 1 79 79 TYR HD2 H 1 7.190 . . . . . . . . . . . 4396 1 578 . 1 1 79 79 TYR HE1 H 1 6.842 . . . . . . . . . . . 4396 1 579 . 1 1 79 79 TYR HE2 H 1 6.842 . . . . . . . . . . . 4396 1 580 . 1 1 80 80 PRO CD C 13 50.8 . . . . . . . . . . . 4396 1 581 . 1 1 80 80 PRO HA H 1 4.40 . . . . . . . . . . . 4396 1 582 . 1 1 80 80 PRO HB2 H 1 2.253 . . . . . . . . . . . 4396 1 583 . 1 1 80 80 PRO HB3 H 1 1.981 . . . . . . . . . . . 4396 1 584 . 1 1 80 80 PRO HD2 H 1 3.82 . . . . . . . . . . . 4396 1 585 . 1 1 80 80 PRO HD3 H 1 3.54 . . . . . . . . . . . 4396 1 586 . 1 1 81 81 GLY N N 15 109.439 . . . . . . . . . . . 4396 1 587 . 1 1 81 81 GLY H H 1 8.046 . . . . . . . . . . . 4396 1 588 . 1 1 81 81 GLY HA2 H 1 4.01 . . . . . . . . . . . 4396 1 589 . 1 1 81 81 GLY HA3 H 1 3.97 . . . . . . . . . . . 4396 1 590 . 1 1 82 82 THR N N 15 114.580 . . . . . . . . . . . 4396 1 591 . 1 1 82 82 THR CG2 C 13 21.6 . . . . . . . . . . . 4396 1 592 . 1 1 82 82 THR H H 1 7.990 . . . . . . . . . . . 4396 1 593 . 1 1 82 82 THR HA H 1 4.339 . . . . . . . . . . . 4396 1 594 . 1 1 82 82 THR HB H 1 4.199 . . . . . . . . . . . 4396 1 595 . 1 1 82 82 THR HG21 H 1 1.226 . . . . . . . . . . . 4396 1 596 . 1 1 82 82 THR HG22 H 1 1.226 . . . . . . . . . . . 4396 1 597 . 1 1 82 82 THR HG23 H 1 1.226 . . . . . . . . . . . 4396 1 598 . 1 1 83 83 ARG N N 15 124.269 . . . . . . . . . . . 4396 1 599 . 1 1 83 83 ARG H H 1 8.357 . . . . . . . . . . . 4396 1 600 . 1 1 83 83 ARG HA H 1 4.353 . . . . . . . . . . . 4396 1 601 . 1 1 83 83 ARG HB2 H 1 1.831 . . . . . . . . . . . 4396 1 602 . 1 1 83 83 ARG HB3 H 1 1.750 . . . . . . . . . . . 4396 1 603 . 1 1 83 83 ARG HG2 H 1 1.595 . . . . . . . . . . . 4396 1 604 . 1 1 83 83 ARG HG3 H 1 1.595 . . . . . . . . . . . 4396 1 605 . 1 1 83 83 ARG HD2 H 1 3.14 . . . . . . . . . . . 4396 1 606 . 1 1 83 83 ARG HD3 H 1 3.14 . . . . . . . . . . . 4396 1 607 . 1 1 84 84 ASN N N 15 122.371 . . . . . . . . . . . 4396 1 608 . 1 1 84 84 ASN CA C 13 51.5 . . . . . . . . . . . 4396 1 609 . 1 1 84 84 ASN ND2 N 15 114.2 . . . . . . . . . . . 4396 1 610 . 1 1 84 84 ASN H H 1 8.454 . . . . . . . . . . . 4396 1 611 . 1 1 84 84 ASN HA H 1 4.960 . . . . . . . . . . . 4396 1 612 . 1 1 84 84 ASN HB2 H 1 2.827 . . . . . . . . . . . 4396 1 613 . 1 1 84 84 ASN HB3 H 1 2.644 . . . . . . . . . . . 4396 1 614 . 1 1 84 84 ASN HD21 H 1 7.602 . . . . . . . . . . . 4396 1 615 . 1 1 84 84 ASN HD22 H 1 6.899 . . . . . . . . . . . 4396 1 616 . 1 1 85 85 PRO CD C 13 50.5 . . . . . . . . . . . 4396 1 617 . 1 1 85 85 PRO HD2 H 1 3.73 . . . . . . . . . . . 4396 1 618 . 1 1 85 85 PRO HD3 H 1 3.68 . . . . . . . . . . . 4396 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_set_1 _Coupling_constant_list.Sf_category coupling_constants _Coupling_constant_list.Sf_framecode coupling_constants_set_1 _Coupling_constant_list.Entry_ID 4396 _Coupling_constant_list.ID 1 _Coupling_constant_list.Sample_condition_list_ID 1 _Coupling_constant_list.Sample_condition_list_label $sample_cond_1 _Coupling_constant_list.Spectrometer_frequency_1H 750 _Coupling_constant_list.Details . _Coupling_constant_list.Text_data_format . _Coupling_constant_list.Text_data . loop_ _Coupling_constant_experiment.Experiment_ID _Coupling_constant_experiment.Experiment_name _Coupling_constant_experiment.Sample_ID _Coupling_constant_experiment.Sample_label _Coupling_constant_experiment.Sample_state _Coupling_constant_experiment.Entry_ID _Coupling_constant_experiment.Coupling_constant_list_ID . . 1 $sample_1 . 4396 1 stop_ loop_ _Coupling_constant.ID _Coupling_constant.Code _Coupling_constant.Assembly_atom_ID_1 _Coupling_constant.Entity_assembly_ID_1 _Coupling_constant.Entity_ID_1 _Coupling_constant.Comp_index_ID_1 _Coupling_constant.Seq_ID_1 _Coupling_constant.Comp_ID_1 _Coupling_constant.Atom_ID_1 _Coupling_constant.Atom_type_1 _Coupling_constant.Atom_isotope_number_1 _Coupling_constant.Ambiguity_code_1 _Coupling_constant.Assembly_atom_ID_2 _Coupling_constant.Entity_assembly_ID_2 _Coupling_constant.Entity_ID_2 _Coupling_constant.Comp_index_ID_2 _Coupling_constant.Seq_ID_2 _Coupling_constant.Comp_ID_2 _Coupling_constant.Atom_ID_2 _Coupling_constant.Atom_type_2 _Coupling_constant.Atom_isotope_number_2 _Coupling_constant.Ambiguity_code_2 _Coupling_constant.Val _Coupling_constant.Val_min _Coupling_constant.Val_max _Coupling_constant.Val_err _Coupling_constant.Resonance_ID_1 _Coupling_constant.Resonance_ID_2 _Coupling_constant.Auth_entity_assembly_ID_1 _Coupling_constant.Auth_seq_ID_1 _Coupling_constant.Auth_comp_ID_1 _Coupling_constant.Auth_atom_ID_1 _Coupling_constant.Auth_entity_assembly_ID_2 _Coupling_constant.Auth_seq_ID_2 _Coupling_constant.Auth_comp_ID_2 _Coupling_constant.Auth_atom_ID_2 _Coupling_constant.Details _Coupling_constant.Entry_ID _Coupling_constant.Coupling_constant_list_ID 1 3JHNHA . 1 1 2 2 ALA H . . . . 1 1 2 2 ALA HA . . . 5.24 . . 0.1 . . . . . . . . . . . 4396 1 2 3JHNHA . 1 1 3 3 THR H . . . . 1 1 3 3 THR HA . . . 7.13 . . 0.1 . . . . . . . . . . . 4396 1 3 3JHNHA . 1 1 4 4 MET H . . . . 1 1 4 4 MET HA . . . 6.23 . . 0.1 . . . . . . . . . . . 4396 1 4 3JHNHA . 1 1 5 5 GLN H . . . . 1 1 5 5 GLN HA . . . 7.44 . . 0.1 . . . . . . . . . . . 4396 1 5 3JHNHA . 1 1 6 6 CYS H . . . . 1 1 6 6 CYS HA . . . 7.53 . . 0.1 . . . . . . . . . . . 4396 1 6 3JHNHA . 1 1 7 7 GLY H . . . . 1 1 7 7 GLY HA . . . 6.62 . . 0.1 . . . . . . . . . . . 4396 1 7 3JHNHA . 1 1 8 8 GLU H . . . . 1 1 8 8 GLU HA . . . 2.69 . . 0.1 . . . . . . . . . . . 4396 1 8 3JHNHA . 1 1 9 9 ASN H . . . . 1 1 9 9 ASN HA . . . 6.37 . . 0.1 . . . . . . . . . . . 4396 1 9 3JHNHA . 1 1 10 10 GLU H . . . . 1 1 10 10 GLU HA . . . 8.14 . . 0.1 . . . . . . . . . . . 4396 1 10 3JHNHA . 1 1 11 11 LYS H . . . . 1 1 11 11 LYS HA . . . 8.11 . . 0.1 . . . . . . . . . . . 4396 1 11 3JHNHA . 1 1 12 12 TYR H . . . . 1 1 12 12 TYR HA . . . 3.99 . . 0.1 . . . . . . . . . . . 4396 1 12 3JHNHA . 1 1 13 13 ASP H . . . . 1 1 13 13 ASP HA . . . 8.67 . . 0.1 . . . . . . . . . . . 4396 1 13 3JHNHA . 1 1 14 14 SER H . . . . 1 1 14 14 SER HA . . . 3.90 . . 0.1 . . . . . . . . . . . 4396 1 14 3JHNHA . 1 1 15 15 CYS H . . . . 1 1 15 15 CYS HA . . . 6.40 . . 0.1 . . . . . . . . . . . 4396 1 15 3JHNHA . 1 1 16 16 GLY H . . . . 1 1 16 16 GLY HA . . . 6.69 . . 0.1 . . . . . . . . . . . 4396 1 16 3JHNHA . 1 1 16 16 GLY H . . . . 1 1 16 16 GLY HA . . . 1.82 . . 0.1 . . . . . . . . . . . 4396 1 17 3JHNHA . 1 1 17 17 SER H . . . . 1 1 17 17 SER HA . . . 6.38 . . 0.1 . . . . . . . . . . . 4396 1 18 3JHNHA . 1 1 19 19 GLU H . . . . 1 1 19 19 GLU HA . . . 5.50 . . 0.1 . . . . . . . . . . . 4396 1 19 3JHNHA . 1 1 20 20 CYS H . . . . 1 1 20 20 CYS HA . . . 3.18 . . 0.1 . . . . . . . . . . . 4396 1 20 3JHNHA . 1 1 21 21 ASP H . . . . 1 1 21 21 ASP HA . . . 4.13 . . 0.1 . . . . . . . . . . . 4396 1 21 3JHNHA . 1 1 22 22 LYS H . . . . 1 1 22 22 LYS HA . . . 5.26 . . 0.1 . . . . . . . . . . . 4396 1 22 3JHNHA . 1 1 23 23 LYS H . . . . 1 1 23 23 LYS HA . . . 7.53 . . 0.1 . . . . . . . . . . . 4396 1 23 3JHNHA . 1 1 26 26 TYR H . . . . 1 1 26 26 TYR HA . . . 7.30 . . 0.1 . . . . . . . . . . . 4396 1 24 3JHNHA . 1 1 27 27 ASP H . . . . 1 1 27 27 ASP HA . . . 5.65 . . 0.1 . . . . . . . . . . . 4396 1 25 3JHNHA . 1 1 28 28 GLY H . . . . 1 1 28 28 GLY HA . . . 6.16 . . 0.1 . . . . . . . . . . . 4396 1 26 3JHNHA . 1 1 28 28 GLY H . . . . 1 1 28 28 GLY HA . . . 4.58 . . 0.1 . . . . . . . . . . . 4396 1 27 3JHNHA . 1 1 29 29 VAL H . . . . 1 1 29 29 VAL HA . . . 7.24 . . 0.1 . . . . . . . . . . . 4396 1 28 3JHNHA . 1 1 30 30 GLU H . . . . 1 1 30 30 GLU HA . . . 6.05 . . 0.1 . . . . . . . . . . . 4396 1 29 3JHNHA . 1 1 31 31 GLU H . . . . 1 1 31 31 GLU HA . . . 6.19 . . 0.1 . . . . . . . . . . . 4396 1 30 3JHNHA . 1 1 32 32 GLU H . . . . 1 1 32 32 GLU HA . . . 6.49 . . 0.1 . . . . . . . . . . . 4396 1 31 3JHNHA . 1 1 33 33 ASP H . . . . 1 1 33 33 ASP HA . . . 6.24 . . 0.1 . . . . . . . . . . . 4396 1 32 3JHNHA . 1 1 34 34 ASP H . . . . 1 1 34 34 ASP HA . . . 7.08 . . 0.1 . . . . . . . . . . . 4396 1 33 3JHNHA . 1 1 35 35 GLU H . . . . 1 1 35 35 GLU HA . . . 5.95 . . 0.1 . . . . . . . . . . . 4396 1 34 3JHNHA . 1 1 36 36 GLU H . . . . 1 1 36 36 GLU HA . . . 6.56 . . 0.1 . . . . . . . . . . . 4396 1 35 3JHNHA . 1 1 38 38 ASN H . . . . 1 1 38 38 ASN HA . . . 7.07 . . 0.1 . . . . . . . . . . . 4396 1 36 3JHNHA . 1 1 39 39 VAL H . . . . 1 1 39 39 VAL HA . . . 7.09 . . 0.1 . . . . . . . . . . . 4396 1 37 3JHNHA . 1 1 41 41 CYS H . . . . 1 1 41 41 CYS HA . . . 4.06 . . 0.1 . . . . . . . . . . . 4396 1 38 3JHNHA . 1 1 42 42 LEU H . . . . 1 1 42 42 LEU HA . . . 6.79 . . 0.1 . . . . . . . . . . . 4396 1 39 3JHNHA . 1 1 43 43 VAL H . . . . 1 1 43 43 VAL HA . . . 6.35 . . 0.1 . . . . . . . . . . . 4396 1 40 3JHNHA . 1 1 44 44 ARG H . . . . 1 1 44 44 ARG HA . . . 6.62 . . 0.1 . . . . . . . . . . . 4396 1 41 3JHNHA . 1 1 45 45 VAL H . . . . 1 1 45 45 VAL HA . . . 6.25 . . 0.1 . . . . . . . . . . . 4396 1 42 3JHNHA . 1 1 46 46 CYS H . . . . 1 1 46 46 CYS HA . . . 4.20 . . 0.1 . . . . . . . . . . . 4396 1 43 3JHNHA . 1 1 48 48 GLN H . . . . 1 1 48 48 GLN HA . . . 4.74 . . 0.1 . . . . . . . . . . . 4396 1 44 3JHNHA . 1 1 49 49 ASP H . . . . 1 1 49 49 ASP HA . . . 6.43 . . 0.1 . . . . . . . . . . . 4396 1 45 3JHNHA . 1 1 50 50 CYS H . . . . 1 1 50 50 CYS HA . . . 8.22 . . 0.1 . . . . . . . . . . . 4396 1 46 3JHNHA . 1 1 51 51 VAL H . . . . 1 1 51 51 VAL HA . . . 8.18 . . 0.1 . . . . . . . . . . . 4396 1 47 3JHNHA . 1 1 53 53 GLU H . . . . 1 1 53 53 GLU HA . . . 2.65 . . 0.1 . . . . . . . . . . . 4396 1 48 3JHNHA . 1 1 54 54 GLU H . . . . 1 1 54 54 GLU HA . . . 2.31 . . 0.1 . . . . . . . . . . . 4396 1 49 3JHNHA . 1 1 55 55 GLY H . . . . 1 1 55 55 GLY HA . . . 7.21 . . 0.1 . . . . . . . . . . . 4396 1 50 3JHNHA . 1 1 55 55 GLY H . . . . 1 1 55 55 GLY HA . . . 4.14 . . 0.1 . . . . . . . . . . . 4396 1 51 3JHNHA . 1 1 56 56 PHE H . . . . 1 1 56 56 PHE HA . . . 8.55 . . 0.1 . . . . . . . . . . . 4396 1 52 3JHNHA . 1 1 57 57 TYR H . . . . 1 1 57 57 TYR HA . . . 8.56 . . 0.1 . . . . . . . . . . . 4396 1 53 3JHNHA . 1 1 58 58 ARG H . . . . 1 1 58 58 ARG HA . . . 4.64 . . 0.1 . . . . . . . . . . . 4396 1 54 3JHNHA . 1 1 59 59 ASN H . . . . 1 1 59 59 ASN HA . . . 6.73 . . 0.1 . . . . . . . . . . . 4396 1 55 3JHNHA . 1 1 61 61 ASP H . . . . 1 1 61 61 ASP HA . . . 8.58 . . 0.1 . . . . . . . . . . . 4396 1 56 3JHNHA . 1 1 62 62 ASP H . . . . 1 1 62 62 ASP HA . . . 5.21 . . 0.1 . . . . . . . . . . . 4396 1 57 3JHNHA . 1 1 63 63 LYS H . . . . 1 1 63 63 LYS HA . . . 5.66 . . 0.1 . . . . . . . . . . . 4396 1 58 3JHNHA . 1 1 64 64 CYS H . . . . 1 1 64 64 CYS HA . . . 6.27 . . 0.1 . . . . . . . . . . . 4396 1 59 3JHNHA . 1 1 65 65 VAL H . . . . 1 1 65 65 VAL HA . . . 8.48 . . 0.1 . . . . . . . . . . . 4396 1 60 3JHNHA . 1 1 66 66 SER H . . . . 1 1 66 66 SER HA . . . 3.68 . . 0.1 . . . . . . . . . . . 4396 1 61 3JHNHA . 1 1 67 67 ALA H . . . . 1 1 67 67 ALA HA . . . 1.88 . . 0.1 . . . . . . . . . . . 4396 1 62 3JHNHA . 1 1 68 68 GLU H . . . . 1 1 68 68 GLU HA . . . 4.00 . . 0.1 . . . . . . . . . . . 4396 1 63 3JHNHA . 1 1 69 69 ASP H . . . . 1 1 69 69 ASP HA . . . 6.10 . . 0.1 . . . . . . . . . . . 4396 1 64 3JHNHA . 1 1 70 70 CYS H . . . . 1 1 70 70 CYS HA . . . 4.05 . . 0.1 . . . . . . . . . . . 4396 1 65 3JHNHA . 1 1 71 71 GLU H . . . . 1 1 71 71 GLU HA . . . 4.60 . . 0.1 . . . . . . . . . . . 4396 1 66 3JHNHA . 1 1 72 72 LEU H . . . . 1 1 72 72 LEU HA . . . 4.63 . . 0.1 . . . . . . . . . . . 4396 1 67 3JHNHA . 1 1 73 73 ASP H . . . . 1 1 73 73 ASP HA . . . 5.70 . . 0.1 . . . . . . . . . . . 4396 1 68 3JHNHA . 1 1 74 74 ASN H . . . . 1 1 74 74 ASN HA . . . 7.18 . . 0.1 . . . . . . . . . . . 4396 1 69 3JHNHA . 1 1 75 75 MET H . . . . 1 1 75 75 MET HA . . . 6.14 . . 0.1 . . . . . . . . . . . 4396 1 70 3JHNHA . 1 1 76 76 ASP H . . . . 1 1 76 76 ASP HA . . . 6.15 . . 0.1 . . . . . . . . . . . 4396 1 71 3JHNHA . 1 1 77 77 PHE H . . . . 1 1 77 77 PHE HA . . . 6.81 . . 0.1 . . . . . . . . . . . 4396 1 72 3JHNHA . 1 1 78 78 ILE H . . . . 1 1 78 78 ILE HA . . . 7.60 . . 0.1 . . . . . . . . . . . 4396 1 73 3JHNHA . 1 1 79 79 TYR H . . . . 1 1 79 79 TYR HA . . . 6.41 . . 0.1 . . . . . . . . . . . 4396 1 74 3JHNHA . 1 1 82 82 THR H . . . . 1 1 82 82 THR HA . . . 7.11 . . 0.1 . . . . . . . . . . . 4396 1 75 3JHNHA . 1 1 83 83 ARG H . . . . 1 1 83 83 ARG HA . . . 6.82 . . 0.1 . . . . . . . . . . . 4396 1 76 3JHNHA . 1 1 84 84 ASN H . . . . 1 1 84 84 ASN HA . . . 14.09 . . 0.1 . . . . . . . . . . . 4396 1 stop_ save_