data_5754 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5754 _Entry.Title ; 1H, 13C and 15N backbone resonance assignment of the VASP EVH1 domain ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2003-03-24 _Entry.Accession_date 2003-03-24 _Entry.Last_release_date 2004-04-07 _Entry.Original_release_date 2004-04-07 _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 Martin Vogtherr . . . 5754 2 Susanne Grimme . . . 5754 3 Barbara Pescatore . . . 5754 4 Harald Schwalbe . . . 5754 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5754 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 110 5754 '1H chemical shifts' 460 5754 '13C chemical shifts' 332 5754 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 . . 2004-04-07 2003-03-24 original author . 5754 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5754 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 22794757 _Citation.DOI . _Citation.PubMed_ID 12913419 _Citation.Full_citation . _Citation.Title ; Letter to the Editor: 1H, 13C and 15N Backbone Resonance Assignment of the VASP EVH1 Domain ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 27 _Citation.Journal_issue 2 _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 189 _Citation.Page_last 190 _Citation.Year 2003 _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 Martin Vogtherr . . . 5754 1 2 Susanne Grimme . . . 5754 1 3 Barbara Pescatore . . . 5754 1 4 Harald Schwalbe . . . 5754 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5754 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Ch. Bartels, T.-H. Xia, M. Billeter, P. Guntert, K. Wuthrich (1995). J. Biomol. NMR 5, 1-10 ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5754 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10212987 _Citation.Full_citation ; G. Cornilescu, F. Delaglio, A. Bax (1999). J. Biomol. NMR 13, 289-302 ; _Citation.Title 'Protein backbone angle restraints from searching a database for chemical shift and sequence homology.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 13 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _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 289 _Citation.Page_last 302 _Citation.Year 1999 _Citation.Details ; Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error. ; 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 G Cornilescu G. . . 5754 3 2 F Delaglio F. . . 5754 3 3 A Bax A. . . 5754 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 5754 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10990454 _Citation.Full_citation ; Ball LJ, Kuhne R, Hoffmann B, Hafner A, Schmieder P, Volkmer-Engert R, Hof M, Wahl M, Schneider-Mergener J, Walter U, Oschkinat H, Jarchau T. EMBO J. 2000 Sep 15;19(18):4903-14. ; _Citation.Title 'Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'EMBO J.' _Citation.Journal_name_full 'The EMBO journal' _Citation.Journal_volume 19 _Citation.Journal_issue 18 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0261-4189 _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 4903 _Citation.Page_last 4914 _Citation.Year 2000 _Citation.Details ; The Ena-VASP family of proteins act as molecular adaptors linking the cytoskeletal system to signal transduction pathways. Their N-terminal EVH1 domains use groups of exposed aromatic residues to specifically recognize 'FPPPP' motifs found in the mammalian zyxin and vinculin proteins, and ActA protein of the intracellular bacterium Listeria monocytogenes. Here, evidence is provided that the affinities of these EVH1-peptide interactions are strongly dependent on the recognition of residues flanking the core FPPPP motifs. Determination of the VASP EVH1 domain solution structure, together with peptide library screening, measurement of individual K(d)s by fluorescence titration, and NMR chemical shift mapping, revealed a second affinity-determining epitope present in all four ActA EVH1-binding motifs. The epitope was shown to interact with a complementary hydrophobic site on the EVH1 surface and to increase strongly the affinity of ActA for EVH1 domains. We propose that this epitope, which is absent in the sequences of the native EVH1-interaction partners zyxin and vinculin, may provide the pathogen with an advantage when competing for the recruitment of the host VASP and Mena proteins in the infected cell. ; 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 'L. J.' Ball L. J. . 5754 4 2 R. Koehne R. . . 5754 4 3 B. Hoffmann B. . . 5754 4 4 A. Hoefner A. . . 5754 4 5 P. Schmieder P. . . 5754 4 6 R. Volkmer-Engert R. . . 5754 4 7 M. Hof M. . . 5754 4 8 M. Wahl M. . . 5754 4 9 J. Schneider-Mergener J. . . 5754 4 10 U. Walter U. . . 5754 4 11 H. Oschkinat H. . . 5754 4 12 T. Jarchau T. . . 5754 4 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_VASP_EVH1 _Assembly.Sf_category assembly _Assembly.Sf_framecode VASP_EVH1 _Assembly.Entry_ID 5754 _Assembly.ID 1 _Assembly.Name 'VASP EVH1 domain' _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 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 monomer 5754 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 'VASP EVH1 domain' 1 $EVH1 . . . native . . . . . 5754 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 . PDB 1EGX . . . . . 'N-terminal His-Tag' 5754 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'VASP EVH1 domain' system 5754 1 'VASP EVH1' abbreviation 5754 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'polypproline binding module' 5754 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_EVH1 _Entity.Sf_category entity _Entity.Sf_framecode EVH1 _Entity.Entry_ID 5754 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Human VASP Ena-Vasp homology domain 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 ; MSETVICSSRATVMLYDDGN KRWLPAGTGPQAFSRVQIYH NPTANSFRVVGRKMQPDQQV VINCAIVRGVKYNQATPNFH QWRDARQVWGLNFGSKEDAA QFAAGMASALEALEG ; _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 115 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID 1 _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 . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 18569 . EVH1 . . . . . 100.00 115 100.00 100.00 5.47e-80 . . . . 5754 1 2 no PDB 1EGX . "Solution Structure Of The Ena-Vasp Homology 1 (Evh1) Domain Of Human Vasodilator-Stimulated Phosphoprotein (Vasp)" . . . . . 100.00 115 100.00 100.00 5.47e-80 . . . . 5754 1 3 no DBJ BAG37336 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 380 100.00 100.00 4.03e-80 . . . . 5754 1 4 no DBJ BAJ21098 . "vasodilator-stimulated phosphoprotein [synthetic construct]" . . . . . 100.00 380 100.00 100.00 4.03e-80 . . . . 5754 1 5 no EMBL CAA67147 . "vasodilator-stimulated phosphoprotein [Homo sapiens]" . . . . . 98.26 378 100.00 100.00 1.29e-78 . . . . 5754 1 6 no EMBL CAA86523 . "vasodilator-stimulated phosphoprotein (VASP) [Homo sapiens]" . . . . . 100.00 380 100.00 100.00 4.03e-80 . . . . 5754 1 7 no GB AAH26019 . "Vasodilator-stimulated phosphoprotein [Homo sapiens]" . . . . . 99.13 380 100.00 100.00 2.88e-79 . . . . 5754 1 8 no GB AAH38224 . "Vasodilator-stimulated phosphoprotein [Homo sapiens]" . . . . . 100.00 380 100.00 100.00 4.03e-80 . . . . 5754 1 9 no GB AIC59345 . "VASP, partial [synthetic construct]" . . . . . 99.13 380 100.00 100.00 2.88e-79 . . . . 5754 1 10 no GB EAW57362 . "vasodilator-stimulated phosphoprotein, isoform CRA_a [Homo sapiens]" . . . . . 100.00 380 100.00 100.00 4.03e-80 . . . . 5754 1 11 no GB EAW57363 . "vasodilator-stimulated phosphoprotein, isoform CRA_b [Homo sapiens]" . . . . . 88.70 367 100.00 100.00 3.99e-70 . . . . 5754 1 12 no REF NP_003361 . "vasodilator-stimulated phosphoprotein [Homo sapiens]" . . . . . 100.00 380 100.00 100.00 4.03e-80 . . . . 5754 1 13 no REF XP_001106536 . "PREDICTED: vasodilator-stimulated phosphoprotein-like [Macaca mulatta]" . . . . . 98.26 420 99.12 100.00 1.46e-77 . . . . 5754 1 14 no REF XP_002829453 . "PREDICTED: vasodilator-stimulated phosphoprotein-like [Pongo abelii]" . . . . . 100.00 147 100.00 100.00 1.70e-80 . . . . 5754 1 15 no REF XP_003277690 . "PREDICTED: uncharacterized protein LOC100597154 [Nomascus leucogenys]" . . . . . 100.00 363 100.00 100.00 7.34e-80 . . . . 5754 1 16 no REF XP_003817563 . "PREDICTED: vasodilator-stimulated phosphoprotein isoform X1 [Pan paniscus]" . . . . . 100.00 380 100.00 100.00 4.54e-80 . . . . 5754 1 17 no SP P50552 . "RecName: Full=Vasodilator-stimulated phosphoprotein; Short=VASP [Homo sapiens]" . . . . . 100.00 380 100.00 100.00 4.03e-80 . . . . 5754 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Human VASP Ena-Vasp homology domain 1' common 5754 1 EVH1 abbreviation 5754 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 . MET . 5754 1 2 . SER . 5754 1 3 . GLU . 5754 1 4 . THR . 5754 1 5 . VAL . 5754 1 6 . ILE . 5754 1 7 . CYS . 5754 1 8 . SER . 5754 1 9 . SER . 5754 1 10 . ARG . 5754 1 11 . ALA . 5754 1 12 . THR . 5754 1 13 . VAL . 5754 1 14 . MET . 5754 1 15 . LEU . 5754 1 16 . TYR . 5754 1 17 . ASP . 5754 1 18 . ASP . 5754 1 19 . GLY . 5754 1 20 . ASN . 5754 1 21 . LYS . 5754 1 22 . ARG . 5754 1 23 . TRP . 5754 1 24 . LEU . 5754 1 25 . PRO . 5754 1 26 . ALA . 5754 1 27 . GLY . 5754 1 28 . THR . 5754 1 29 . GLY . 5754 1 30 . PRO . 5754 1 31 . GLN . 5754 1 32 . ALA . 5754 1 33 . PHE . 5754 1 34 . SER . 5754 1 35 . ARG . 5754 1 36 . VAL . 5754 1 37 . GLN . 5754 1 38 . ILE . 5754 1 39 . TYR . 5754 1 40 . HIS . 5754 1 41 . ASN . 5754 1 42 . PRO . 5754 1 43 . THR . 5754 1 44 . ALA . 5754 1 45 . ASN . 5754 1 46 . SER . 5754 1 47 . PHE . 5754 1 48 . ARG . 5754 1 49 . VAL . 5754 1 50 . VAL . 5754 1 51 . GLY . 5754 1 52 . ARG . 5754 1 53 . LYS . 5754 1 54 . MET . 5754 1 55 . GLN . 5754 1 56 . PRO . 5754 1 57 . ASP . 5754 1 58 . GLN . 5754 1 59 . GLN . 5754 1 60 . VAL . 5754 1 61 . VAL . 5754 1 62 . ILE . 5754 1 63 . ASN . 5754 1 64 . CYS . 5754 1 65 . ALA . 5754 1 66 . ILE . 5754 1 67 . VAL . 5754 1 68 . ARG . 5754 1 69 . GLY . 5754 1 70 . VAL . 5754 1 71 . LYS . 5754 1 72 . TYR . 5754 1 73 . ASN . 5754 1 74 . GLN . 5754 1 75 . ALA . 5754 1 76 . THR . 5754 1 77 . PRO . 5754 1 78 . ASN . 5754 1 79 . PHE . 5754 1 80 . HIS . 5754 1 81 . GLN . 5754 1 82 . TRP . 5754 1 83 . ARG . 5754 1 84 . ASP . 5754 1 85 . ALA . 5754 1 86 . ARG . 5754 1 87 . GLN . 5754 1 88 . VAL . 5754 1 89 . TRP . 5754 1 90 . GLY . 5754 1 91 . LEU . 5754 1 92 . ASN . 5754 1 93 . PHE . 5754 1 94 . GLY . 5754 1 95 . SER . 5754 1 96 . LYS . 5754 1 97 . GLU . 5754 1 98 . ASP . 5754 1 99 . ALA . 5754 1 100 . ALA . 5754 1 101 . GLN . 5754 1 102 . PHE . 5754 1 103 . ALA . 5754 1 104 . ALA . 5754 1 105 . GLY . 5754 1 106 . MET . 5754 1 107 . ALA . 5754 1 108 . SER . 5754 1 109 . ALA . 5754 1 110 . LEU . 5754 1 111 . GLU . 5754 1 112 . ALA . 5754 1 113 . LEU . 5754 1 114 . GLU . 5754 1 115 . GLY . 5754 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 . MET 1 1 5754 1 . SER 2 2 5754 1 . GLU 3 3 5754 1 . THR 4 4 5754 1 . VAL 5 5 5754 1 . ILE 6 6 5754 1 . CYS 7 7 5754 1 . SER 8 8 5754 1 . SER 9 9 5754 1 . ARG 10 10 5754 1 . ALA 11 11 5754 1 . THR 12 12 5754 1 . VAL 13 13 5754 1 . MET 14 14 5754 1 . LEU 15 15 5754 1 . TYR 16 16 5754 1 . ASP 17 17 5754 1 . ASP 18 18 5754 1 . GLY 19 19 5754 1 . ASN 20 20 5754 1 . LYS 21 21 5754 1 . ARG 22 22 5754 1 . TRP 23 23 5754 1 . LEU 24 24 5754 1 . PRO 25 25 5754 1 . ALA 26 26 5754 1 . GLY 27 27 5754 1 . THR 28 28 5754 1 . GLY 29 29 5754 1 . PRO 30 30 5754 1 . GLN 31 31 5754 1 . ALA 32 32 5754 1 . PHE 33 33 5754 1 . SER 34 34 5754 1 . ARG 35 35 5754 1 . VAL 36 36 5754 1 . GLN 37 37 5754 1 . ILE 38 38 5754 1 . TYR 39 39 5754 1 . HIS 40 40 5754 1 . ASN 41 41 5754 1 . PRO 42 42 5754 1 . THR 43 43 5754 1 . ALA 44 44 5754 1 . ASN 45 45 5754 1 . SER 46 46 5754 1 . PHE 47 47 5754 1 . ARG 48 48 5754 1 . VAL 49 49 5754 1 . VAL 50 50 5754 1 . GLY 51 51 5754 1 . ARG 52 52 5754 1 . LYS 53 53 5754 1 . MET 54 54 5754 1 . GLN 55 55 5754 1 . PRO 56 56 5754 1 . ASP 57 57 5754 1 . GLN 58 58 5754 1 . GLN 59 59 5754 1 . VAL 60 60 5754 1 . VAL 61 61 5754 1 . ILE 62 62 5754 1 . ASN 63 63 5754 1 . CYS 64 64 5754 1 . ALA 65 65 5754 1 . ILE 66 66 5754 1 . VAL 67 67 5754 1 . ARG 68 68 5754 1 . GLY 69 69 5754 1 . VAL 70 70 5754 1 . LYS 71 71 5754 1 . TYR 72 72 5754 1 . ASN 73 73 5754 1 . GLN 74 74 5754 1 . ALA 75 75 5754 1 . THR 76 76 5754 1 . PRO 77 77 5754 1 . ASN 78 78 5754 1 . PHE 79 79 5754 1 . HIS 80 80 5754 1 . GLN 81 81 5754 1 . TRP 82 82 5754 1 . ARG 83 83 5754 1 . ASP 84 84 5754 1 . ALA 85 85 5754 1 . ARG 86 86 5754 1 . GLN 87 87 5754 1 . VAL 88 88 5754 1 . TRP 89 89 5754 1 . GLY 90 90 5754 1 . LEU 91 91 5754 1 . ASN 92 92 5754 1 . PHE 93 93 5754 1 . GLY 94 94 5754 1 . SER 95 95 5754 1 . LYS 96 96 5754 1 . GLU 97 97 5754 1 . ASP 98 98 5754 1 . ALA 99 99 5754 1 . ALA 100 100 5754 1 . GLN 101 101 5754 1 . PHE 102 102 5754 1 . ALA 103 103 5754 1 . ALA 104 104 5754 1 . GLY 105 105 5754 1 . MET 106 106 5754 1 . ALA 107 107 5754 1 . SER 108 108 5754 1 . ALA 109 109 5754 1 . LEU 110 110 5754 1 . GLU 111 111 5754 1 . ALA 112 112 5754 1 . LEU 113 113 5754 1 . GLU 114 114 5754 1 . GLY 115 115 5754 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 5754 _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 $EVH1 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5754 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 5754 _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 $EVH1 . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5754 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5754 _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 'Human VASP Ena-Vasp homology domain 1' '[U-13C; U-15N]' . . 1 $EVH1 . . 1.0 . . mM . . . . 5754 1 2 DTT . . . . . . . 10 . . mM . . . . 5754 1 3 KCl . . . . . . . 50 . . mM . . . . 5754 1 4 KPi . . . . . . . 20 . . mM . . . . 5754 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 5754 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'Human VASP Ena-Vasp homology domain 1' [U-15N] . . 1 $EVH1 . . 1.0 . . mM . . . . 5754 2 2 DTT . . . . . . . 10 . . mM . . . . 5754 2 3 KCl . . . . . . . 50 . . mM . . . . 5754 2 4 KPi . . . . . . . 20 . . mM . . . . 5754 2 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 5754 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 6.5 0.2 n/a 5754 1 temperature 298 0.1 K 5754 1 stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Software.Sf_category software _Software.Sf_framecode xwinnmr _Software.Entry_ID 5754 _Software.ID 1 _Software.Name xwinnmr _Software.Version 2.9 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID acqusition 5754 1 processing 5754 1 stop_ save_ save_xeasy _Software.Sf_category software _Software.Sf_framecode xeasy _Software.Entry_ID 5754 _Software.ID 2 _Software.Name xeasy _Software.Version 1.3.14 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'peak assignment' 5754 2 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 2 $ref_1 5754 2 stop_ save_ save_talos _Software.Sf_category software _Software.Sf_framecode talos _Software.Entry_ID 5754 _Software.ID 3 _Software.Name talos _Software.Version 1999.019.15.47 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID assignment 5754 3 'structure validation' 5754 3 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 3 $ref_2 5754 3 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 5754 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5754 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer Bruker DRX . 800 . . . 5754 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 5754 _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 HNCO . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5754 1 2 HN(CA)CO . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5754 1 3 CBCA(CO)NH . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5754 1 4 HNCACB . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5754 1 5 HCC(CO)NH-TOCSY . . . . . . . . . . . . . . . . 1 $Ex-cond_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5754 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 5754 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 . direct 1.0 . . . . . . . . . 5754 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5754 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5754 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 5754 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-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 . 5754 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 MET N N 15 121.003 0.032 . 1 . . . . . . . . 5754 1 2 . 1 1 1 1 MET H H 1 8.278 0.014 . 1 . . . . . . . . 5754 1 3 . 1 1 1 1 MET CA C 13 53.340 0.000 . 1 . . . . . . . . 5754 1 4 . 1 1 1 1 MET HA H 1 4.309 0.000 . 1 . . . . . . . . 5754 1 5 . 1 1 1 1 MET CB C 13 30.209 0.000 . 1 . . . . . . . . 5754 1 6 . 1 1 1 1 MET HB2 H 1 2.365 0.000 . 1 . . . . . . . . 5754 1 7 . 1 1 1 1 MET HG2 H 1 1.909 0.000 . 1 . . . . . . . . 5754 1 8 . 1 1 1 1 MET C C 13 173.625 0.000 . 1 . . . . . . . . 5754 1 9 . 1 1 2 2 SER N N 15 116.117 0.067 . 1 . . . . . . . . 5754 1 10 . 1 1 2 2 SER H H 1 8.275 0.001 . 1 . . . . . . . . 5754 1 11 . 1 1 2 2 SER CA C 13 55.919 0.000 . 1 . . . . . . . . 5754 1 12 . 1 1 2 2 SER HA H 1 3.768 0.000 . 1 . . . . . . . . 5754 1 13 . 1 1 2 2 SER CB C 13 61.288 0.000 . 1 . . . . . . . . 5754 1 14 . 1 1 2 2 SER C C 13 171.292 0.000 . 1 . . . . . . . . 5754 1 15 . 1 1 3 3 GLU N N 15 119.075 0.077 . 1 . . . . . . . . 5754 1 16 . 1 1 3 3 GLU H H 1 7.860 0.000 . 1 . . . . . . . . 5754 1 17 . 1 1 3 3 GLU CA C 13 53.013 0.000 . 1 . . . . . . . . 5754 1 18 . 1 1 3 3 GLU HA H 1 4.777 0.000 . 1 . . . . . . . . 5754 1 19 . 1 1 3 3 GLU CB C 13 30.462 0.000 . 1 . . . . . . . . 5754 1 20 . 1 1 3 3 GLU HB2 H 1 1.857 0.000 . 1 . . . . . . . . 5754 1 21 . 1 1 3 3 GLU HG2 H 1 2.102 0.000 . 1 . . . . . . . . 5754 1 22 . 1 1 3 3 GLU C C 13 173.642 0.000 . 1 . . . . . . . . 5754 1 23 . 1 1 4 4 THR N N 15 116.283 0.074 . 1 . . . . . . . . 5754 1 24 . 1 1 4 4 THR H H 1 8.874 0.000 . 1 . . . . . . . . 5754 1 25 . 1 1 4 4 THR CA C 13 57.927 0.000 . 1 . . . . . . . . 5754 1 26 . 1 1 4 4 THR HA H 1 4.553 0.000 . 1 . . . . . . . . 5754 1 27 . 1 1 4 4 THR CB C 13 68.742 0.000 . 1 . . . . . . . . 5754 1 28 . 1 1 4 4 THR C C 13 170.996 0.000 . 1 . . . . . . . . 5754 1 29 . 1 1 5 5 VAL N N 15 125.428 0.366 . 1 . . . . . . . . 5754 1 30 . 1 1 5 5 VAL H H 1 8.576 0.002 . 1 . . . . . . . . 5754 1 31 . 1 1 5 5 VAL CA C 13 59.838 0.000 . 1 . . . . . . . . 5754 1 32 . 1 1 5 5 VAL HA H 1 4.013 0.000 . 1 . . . . . . . . 5754 1 33 . 1 1 5 5 VAL CB C 13 29.577 0.000 . 1 . . . . . . . . 5754 1 34 . 1 1 5 5 VAL HB H 1 1.778 0.000 . 1 . . . . . . . . 5754 1 35 . 1 1 5 5 VAL HG11 H 1 0.595 0.000 . 1 . . . . . . . . 5754 1 36 . 1 1 5 5 VAL HG12 H 1 0.595 0.000 . 1 . . . . . . . . 5754 1 37 . 1 1 5 5 VAL HG13 H 1 0.595 0.000 . 1 . . . . . . . . 5754 1 38 . 1 1 5 5 VAL HG21 H 1 0.454 0.000 . 1 . . . . . . . . 5754 1 39 . 1 1 5 5 VAL HG22 H 1 0.454 0.000 . 1 . . . . . . . . 5754 1 40 . 1 1 5 5 VAL HG23 H 1 0.454 0.000 . 1 . . . . . . . . 5754 1 41 . 1 1 5 5 VAL C C 13 174.562 0.000 . 1 . . . . . . . . 5754 1 42 . 1 1 6 6 ILE N N 15 123.571 0.007 . 1 . . . . . . . . 5754 1 43 . 1 1 6 6 ILE H H 1 8.864 0.013 . 1 . . . . . . . . 5754 1 44 . 1 1 6 6 ILE CA C 13 58.309 0.000 . 1 . . . . . . . . 5754 1 45 . 1 1 6 6 ILE HA H 1 4.258 0.000 . 1 . . . . . . . . 5754 1 46 . 1 1 6 6 ILE CB C 13 35.641 0.000 . 1 . . . . . . . . 5754 1 47 . 1 1 6 6 ILE HB H 1 1.873 0.000 . 1 . . . . . . . . 5754 1 48 . 1 1 6 6 ILE HG13 H 1 0.787 0.000 . 1 . . . . . . . . 5754 1 49 . 1 1 6 6 ILE HG12 H 1 1.120 0.000 . 1 . . . . . . . . 5754 1 50 . 1 1 6 6 ILE C C 13 173.56 0.000 . 1 . . . . . . . . 5754 1 51 . 1 1 7 7 CYS N N 15 114.316 0.227 . 1 . . . . . . . . 5754 1 52 . 1 1 7 7 CYS H H 1 7.174 0.000 . 1 . . . . . . . . 5754 1 53 . 1 1 7 7 CYS CA C 13 54.41 0.000 . 1 . . . . . . . . 5754 1 54 . 1 1 7 7 CYS HA H 1 4.573 0.000 . 1 . . . . . . . . 5754 1 55 . 1 1 7 7 CYS CB C 13 26.861 0.000 . 1 . . . . . . . . 5754 1 56 . 1 1 7 7 CYS HB2 H 1 2.790 0.000 . 1 . . . . . . . . 5754 1 57 . 1 1 7 7 CYS HB3 H 1 2.617 0.000 . 1 . . . . . . . . 5754 1 58 . 1 1 7 7 CYS C C 13 169.304 0.000 . 1 . . . . . . . . 5754 1 59 . 1 1 8 8 SER N N 15 117.450 0.097 . 1 . . . . . . . . 5754 1 60 . 1 1 8 8 SER H H 1 8.502 0.005 . 1 . . . . . . . . 5754 1 61 . 1 1 8 8 SER CA C 13 54.869 0.000 . 1 . . . . . . . . 5754 1 62 . 1 1 8 8 SER HA H 1 3.644 0.000 . 1 . . . . . . . . 5754 1 63 . 1 1 8 8 SER CB C 13 62.172 0.000 . 1 . . . . . . . . 5754 1 64 . 1 1 8 8 SER HB2 H 1 3.504 0.000 . 1 . . . . . . . . 5754 1 65 . 1 1 8 8 SER C C 13 170.848 0.000 . 1 . . . . . . . . 5754 1 66 . 1 1 9 9 SER N N 15 119.857 0.027 . 1 . . . . . . . . 5754 1 67 . 1 1 9 9 SER H H 1 9.168 0.000 . 1 . . . . . . . . 5754 1 68 . 1 1 9 9 SER CA C 13 55.175 0.000 . 1 . . . . . . . . 5754 1 69 . 1 1 9 9 SER HA H 1 3.881 0.000 . 1 . . . . . . . . 5754 1 70 . 1 1 9 9 SER CB C 13 64.573 0.000 . 1 . . . . . . . . 5754 1 71 . 1 1 9 9 SER HB2 H 1 3.750 0.000 . 1 . . . . . . . . 5754 1 72 . 1 1 9 9 SER C C 13 169.747 0.000 . 1 . . . . . . . . 5754 1 73 . 1 1 10 10 ARG N N 15 124.242 0.107 . 1 . . . . . . . . 5754 1 74 . 1 1 10 10 ARG H H 1 8.781 0.002 . 1 . . . . . . . . 5754 1 75 . 1 1 10 10 ARG CA C 13 52.27 0.000 . 1 . . . . . . . . 5754 1 76 . 1 1 10 10 ARG HA H 1 5.358 0.000 . 1 . . . . . . . . 5754 1 77 . 1 1 10 10 ARG CB C 13 29.451 0.000 . 1 . . . . . . . . 5754 1 78 . 1 1 10 10 ARG HB2 H 1 1.637 0.000 . 1 . . . . . . . . 5754 1 79 . 1 1 10 10 ARG HB3 H 1 1.532 0.000 . 1 . . . . . . . . 5754 1 80 . 1 1 10 10 ARG HG2 H 1 1.182 0.000 . 1 . . . . . . . . 5754 1 81 . 1 1 10 10 ARG C C 13 173.494 0.000 . 1 . . . . . . . . 5754 1 82 . 1 1 11 11 ALA N N 15 125.559 0.300 . 1 . . . . . . . . 5754 1 83 . 1 1 11 11 ALA H H 1 9.119 0.000 . 1 . . . . . . . . 5754 1 84 . 1 1 11 11 ALA CA C 13 49.159 0.000 . 1 . . . . . . . . 5754 1 85 . 1 1 11 11 ALA HA H 1 4.737 0.000 . 1 . . . . . . . . 5754 1 86 . 1 1 11 11 ALA HB1 H 1 0.425 0.000 . 1 . . . . . . . . 5754 1 87 . 1 1 11 11 ALA HB2 H 1 0.425 0.000 . 1 . . . . . . . . 5754 1 88 . 1 1 11 11 ALA HB3 H 1 0.425 0.000 . 1 . . . . . . . . 5754 1 89 . 1 1 11 11 ALA CB C 13 20.481 0.000 . 1 . . . . . . . . 5754 1 90 . 1 1 11 11 ALA C C 13 173.905 0.000 . 1 . . . . . . . . 5754 1 91 . 1 1 12 12 THR N N 15 118.974 0.161 . 1 . . . . . . . . 5754 1 92 . 1 1 12 12 THR H H 1 8.885 0.002 . 1 . . . . . . . . 5754 1 93 . 1 1 12 12 THR CA C 13 59.898 0.000 . 1 . . . . . . . . 5754 1 94 . 1 1 12 12 THR CB C 13 66.089 0.000 . 1 . . . . . . . . 5754 1 95 . 1 1 12 12 THR C C 13 171.637 0.000 . 1 . . . . . . . . 5754 1 96 . 1 1 13 13 VAL N N 15 127.690 0.232 . 1 . . . . . . . . 5754 1 97 . 1 1 13 13 VAL H H 1 8.227 0.005 . 1 . . . . . . . . 5754 1 98 . 1 1 13 13 VAL CA C 13 59.961 0.000 . 1 . . . . . . . . 5754 1 99 . 1 1 13 13 VAL HA H 1 4.145 0.000 . 1 . . . . . . . . 5754 1 100 . 1 1 13 13 VAL CB C 13 28.756 0.000 . 1 . . . . . . . . 5754 1 101 . 1 1 13 13 VAL HB H 1 1.830 0.000 . 1 . . . . . . . . 5754 1 102 . 1 1 13 13 VAL HG11 H 1 0.884 0.000 . 1 . . . . . . . . 5754 1 103 . 1 1 13 13 VAL HG12 H 1 0.884 0.000 . 1 . . . . . . . . 5754 1 104 . 1 1 13 13 VAL HG13 H 1 0.884 0.000 . 1 . . . . . . . . 5754 1 105 . 1 1 13 13 VAL HG21 H 1 0.595 0.000 . 1 . . . . . . . . 5754 1 106 . 1 1 13 13 VAL HG22 H 1 0.595 0.000 . 1 . . . . . . . . 5754 1 107 . 1 1 13 13 VAL HG23 H 1 0.595 0.000 . 1 . . . . . . . . 5754 1 108 . 1 1 13 13 VAL C C 13 172.886 0.000 . 1 . . . . . . . . 5754 1 109 . 1 1 14 14 MET N N 15 129.645 0.580 . 1 . . . . . . . . 5754 1 110 . 1 1 14 14 MET H H 1 9.877 0.010 . 1 . . . . . . . . 5754 1 111 . 1 1 14 14 MET CA C 13 50.802 0.000 . 1 . . . . . . . . 5754 1 112 . 1 1 14 14 MET HA H 1 5.409 0.000 . 1 . . . . . . . . 5754 1 113 . 1 1 14 14 MET CB C 13 33.873 0.000 . 1 . . . . . . . . 5754 1 114 . 1 1 14 14 MET HB2 H 1 2.251 0.000 . 1 . . . . . . . . 5754 1 115 . 1 1 14 14 MET HG2 H 1 1.725 0.000 . 1 . . . . . . . . 5754 1 116 . 1 1 14 14 MET C C 13 171.144 0.000 . 1 . . . . . . . . 5754 1 117 . 1 1 15 15 LEU N N 15 121.002 0.067 . 1 . . . . . . . . 5754 1 118 . 1 1 15 15 LEU H H 1 9.578 0.003 . 1 . . . . . . . . 5754 1 119 . 1 1 15 15 LEU CA C 13 50.97 0.000 . 1 . . . . . . . . 5754 1 120 . 1 1 15 15 LEU HA H 1 5.038 0.000 . 1 . . . . . . . . 5754 1 121 . 1 1 15 15 LEU CB C 13 43.98 0.000 . 1 . . . . . . . . 5754 1 122 . 1 1 15 15 LEU HB2 H 1 1.296 0.000 . 1 . . . . . . . . 5754 1 123 . 1 1 15 15 LEU C C 13 173.675 0.000 . 1 . . . . . . . . 5754 1 124 . 1 1 16 16 TYR N N 15 124.959 0.182 . 1 . . . . . . . . 5754 1 125 . 1 1 16 16 TYR H H 1 8.082 0.002 . 1 . . . . . . . . 5754 1 126 . 1 1 16 16 TYR CA C 13 55.476 0.000 . 1 . . . . . . . . 5754 1 127 . 1 1 16 16 TYR HA H 1 3.728 0.000 . 1 . . . . . . . . 5754 1 128 . 1 1 16 16 TYR CB C 13 35.705 0.000 . 1 . . . . . . . . 5754 1 129 . 1 1 16 16 TYR HB2 H 1 2.025 0.000 . 1 . . . . . . . . 5754 1 130 . 1 1 16 16 TYR HB3 H 1 0.904 0.000 . 1 . . . . . . . . 5754 1 131 . 1 1 16 16 TYR C C 13 171.818 0.000 . 1 . . . . . . . . 5754 1 132 . 1 1 17 17 ASP N N 15 128.127 0.354 . 1 . . . . . . . . 5754 1 133 . 1 1 17 17 ASP H H 1 8.047 0.001 . 1 . . . . . . . . 5754 1 134 . 1 1 17 17 ASP CA C 13 49.475 0.000 . 1 . . . . . . . . 5754 1 135 . 1 1 17 17 ASP HA H 1 3.583 0.000 . 1 . . . . . . . . 5754 1 136 . 1 1 17 17 ASP CB C 13 38.61 0.000 . 1 . . . . . . . . 5754 1 137 . 1 1 17 17 ASP HB2 H 1 2.617 0.000 . 1 . . . . . . . . 5754 1 138 . 1 1 17 17 ASP HB3 H 1 2.233 0.000 . 1 . . . . . . . . 5754 1 139 . 1 1 17 17 ASP C C 13 172.837 0.000 . 1 . . . . . . . . 5754 1 140 . 1 1 18 18 ASP N N 15 123.544 0.087 . 1 . . . . . . . . 5754 1 141 . 1 1 18 18 ASP H H 1 8.277 0.002 . 1 . . . . . . . . 5754 1 142 . 1 1 18 18 ASP CA C 13 53.799 0.000 . 1 . . . . . . . . 5754 1 143 . 1 1 18 18 ASP HA H 1 3.942 0.000 . 1 . . . . . . . . 5754 1 144 . 1 1 18 18 ASP CB C 13 38.989 0.000 . 1 . . . . . . . . 5754 1 145 . 1 1 18 18 ASP HB2 H 1 2.484 0.000 . 1 . . . . . . . . 5754 1 146 . 1 1 18 18 ASP C C 13 175.351 0.000 . 1 . . . . . . . . 5754 1 147 . 1 1 19 19 GLY N N 15 106.527 0.336 . 1 . . . . . . . . 5754 1 148 . 1 1 19 19 GLY H H 1 8.275 0.004 . 1 . . . . . . . . 5754 1 149 . 1 1 19 19 GLY CA C 13 44.09 0.000 . 1 . . . . . . . . 5754 1 150 . 1 1 19 19 GLY HA2 H 1 3.707 0.000 . 1 . . . . . . . . 5754 1 151 . 1 1 19 19 GLY C C 13 170.907 0.000 . 1 . . . . . . . . 5754 1 152 . 1 1 20 20 ASN N N 15 115.493 0.186 . 1 . . . . . . . . 5754 1 153 . 1 1 20 20 ASN H H 1 7.237 0.003 . 1 . . . . . . . . 5754 1 154 . 1 1 20 20 ASN CA C 13 50.206 0.000 . 1 . . . . . . . . 5754 1 155 . 1 1 20 20 ASN CB C 13 36.827 0.000 . 1 . . . . . . . . 5754 1 156 . 1 1 20 20 ASN HB2 H 1 2.504 0.000 . 1 . . . . . . . . 5754 1 157 . 1 1 20 20 ASN HB3 H 1 2.127 0.000 . 1 . . . . . . . . 5754 1 158 . 1 1 20 20 ASN C C 13 170.914 0.000 . 1 . . . . . . . . 5754 1 159 . 1 1 21 21 LYS N N 15 118.177 0.046 . 1 . . . . . . . . 5754 1 160 . 1 1 21 21 LYS H H 1 7.611 0.001 . 1 . . . . . . . . 5754 1 161 . 1 1 21 21 LYS CA C 13 53.897 0.000 . 1 . . . . . . . . 5754 1 162 . 1 1 21 21 LYS HA H 1 3.493 0.000 . 1 . . . . . . . . 5754 1 163 . 1 1 21 21 LYS CB C 13 26.125 0.000 . 1 . . . . . . . . 5754 1 164 . 1 1 21 21 LYS HB2 H 1 1.971 0.000 . 1 . . . . . . . . 5754 1 165 . 1 1 21 21 LYS HB3 H 1 1.620 0.000 . 1 . . . . . . . . 5754 1 166 . 1 1 21 21 LYS HG2 H 1 1.291 0.109 . 1 . . . . . . . . 5754 1 167 . 1 1 21 21 LYS C C 13 172.261 0.000 . 1 . . . . . . . . 5754 1 168 . 1 1 22 22 ARG N N 15 113.687 0.168 . 1 . . . . . . . . 5754 1 169 . 1 1 22 22 ARG H H 1 6.921 0.001 . 1 . . . . . . . . 5754 1 170 . 1 1 22 22 ARG CA C 13 51.276 0.000 . 1 . . . . . . . . 5754 1 171 . 1 1 22 22 ARG HA H 1 4.604 0.000 . 1 . . . . . . . . 5754 1 172 . 1 1 22 22 ARG CB C 13 30.841 0.000 . 1 . . . . . . . . 5754 1 173 . 1 1 22 22 ARG HB2 H 1 1.585 0.000 . 1 . . . . . . . . 5754 1 174 . 1 1 22 22 ARG HG2 H 1 1.191 0.000 . 1 . . . . . . . . 5754 1 175 . 1 1 22 22 ARG C C 13 170.848 0.000 . 1 . . . . . . . . 5754 1 176 . 1 1 23 23 TRP N N 15 121.494 0.202 . 1 . . . . . . . . 5754 1 177 . 1 1 23 23 TRP H H 1 8.659 0.001 . 1 . . . . . . . . 5754 1 178 . 1 1 23 23 TRP CA C 13 54.181 0.000 . 1 . . . . . . . . 5754 1 179 . 1 1 23 23 TRP HA H 1 4.808 0.000 . 1 . . . . . . . . 5754 1 180 . 1 1 23 23 TRP CB C 13 28.377 0.000 . 1 . . . . . . . . 5754 1 181 . 1 1 23 23 TRP HB2 H 1 2.908 0.000 . 1 . . . . . . . . 5754 1 182 . 1 1 23 23 TRP C C 13 173.445 0.000 . 1 . . . . . . . . 5754 1 183 . 1 1 24 24 LEU N N 15 122.971 0.120 . 1 . . . . . . . . 5754 1 184 . 1 1 24 24 LEU H H 1 9.029 0.002 . 1 . . . . . . . . 5754 1 185 . 1 1 24 24 LEU CA C 13 49.441 0.000 . 1 . . . . . . . . 5754 1 186 . 1 1 24 24 LEU CB C 13 41.642 0.000 . 1 . . . . . . . . 5754 1 187 . 1 1 24 24 LEU C C 13 171.525 0.000 . 1 . . . . . . . . 5754 1 188 . 1 1 25 25 PRO CA C 13 60.467 0.000 . 1 . . . . . . . . 5754 1 189 . 1 1 25 25 PRO HA H 1 4.900 0.000 . 1 . . . . . . . . 5754 1 190 . 1 1 25 25 PRO CB C 13 29.072 0.000 . 1 . . . . . . . . 5754 1 191 . 1 1 25 25 PRO HB2 H 1 2.101 0.000 . 1 . . . . . . . . 5754 1 192 . 1 1 25 25 PRO HB3 H 1 1.864 0.000 . 1 . . . . . . . . 5754 1 193 . 1 1 25 25 PRO C C 13 174.578 0.000 . 1 . . . . . . . . 5754 1 194 . 1 1 26 26 ALA N N 15 125.732 0.243 . 1 . . . . . . . . 5754 1 195 . 1 1 26 26 ALA H H 1 8.359 0.006 . 1 . . . . . . . . 5754 1 196 . 1 1 26 26 ALA CA C 13 49.948 0.000 . 1 . . . . . . . . 5754 1 197 . 1 1 26 26 ALA HA H 1 2.905 1.495 . 1 . . . . . . . . 5754 1 198 . 1 1 26 26 ALA CB C 13 17.828 0.000 . 1 . . . . . . . . 5754 1 199 . 1 1 27 27 GLY N N 15 110.626 0.245 . 1 . . . . . . . . 5754 1 200 . 1 1 27 27 GLY H H 1 8.856 0.004 . 1 . . . . . . . . 5754 1 201 . 1 1 27 27 GLY CA C 13 41.644 0.000 . 1 . . . . . . . . 5754 1 202 . 1 1 27 27 GLY HA2 H 1 4.309 0.000 . 1 . . . . . . . . 5754 1 203 . 1 1 27 27 GLY HA3 H 1 3.860 0.000 . 1 . . . . . . . . 5754 1 204 . 1 1 27 27 GLY C C 13 172.754 0.000 . 1 . . . . . . . . 5754 1 205 . 1 1 28 28 THR N N 15 111.410 0.233 . 1 . . . . . . . . 5754 1 206 . 1 1 28 28 THR H H 1 8.625 0.003 . 1 . . . . . . . . 5754 1 207 . 1 1 28 28 THR CA C 13 58.003 0.000 . 1 . . . . . . . . 5754 1 208 . 1 1 28 28 THR HA H 1 4.594 0.000 . 1 . . . . . . . . 5754 1 209 . 1 1 28 28 THR CB C 13 68.868 0.000 . 1 . . . . . . . . 5754 1 210 . 1 1 28 28 THR C C 13 172.771 0.000 . 1 . . . . . . . . 5754 1 211 . 1 1 29 29 GLY N N 15 109.181 0.279 . 1 . . . . . . . . 5754 1 212 . 1 1 29 29 GLY H H 1 8.471 0.003 . 1 . . . . . . . . 5754 1 213 . 1 1 29 29 GLY CA C 13 42.021 0.000 . 1 . . . . . . . . 5754 1 214 . 1 1 30 30 PRO CA C 13 52.255 0.000 . 1 . . . . . . . . 5754 1 215 . 1 1 30 30 PRO HA H 1 4.482 0.000 . 1 . . . . . . . . 5754 1 216 . 1 1 30 30 PRO CB C 13 27.682 0.000 . 1 . . . . . . . . 5754 1 217 . 1 1 30 30 PRO HB2 H 1 2.109 0.000 . 1 . . . . . . . . 5754 1 218 . 1 1 30 30 PRO HB3 H 1 1.855 0.000 . 1 . . . . . . . . 5754 1 219 . 1 1 30 30 PRO HG2 H 1 2.434 0.000 . 1 . . . . . . . . 5754 1 220 . 1 1 30 30 PRO C C 13 172.837 0.000 . 1 . . . . . . . . 5754 1 221 . 1 1 31 31 GLN N N 15 120.161 0.189 . 1 . . . . . . . . 5754 1 222 . 1 1 31 31 GLN H H 1 8.231 0.002 . 1 . . . . . . . . 5754 1 223 . 1 1 31 31 GLN CA C 13 53.455 0.000 . 1 . . . . . . . . 5754 1 224 . 1 1 31 31 GLN HA H 1 4.115 0.000 . 1 . . . . . . . . 5754 1 225 . 1 1 31 31 GLN CB C 13 26.229 0.000 . 1 . . . . . . . . 5754 1 226 . 1 1 31 31 GLN HB2 H 1 1.917 0.000 . 1 . . . . . . . . 5754 1 227 . 1 1 31 31 GLN HB3 H 1 1.830 0.000 . 1 . . . . . . . . 5754 1 228 . 1 1 31 31 GLN HG2 H 1 2.137 0.000 . 1 . . . . . . . . 5754 1 229 . 1 1 31 31 GLN C C 13 173.132 0.000 . 1 . . . . . . . . 5754 1 230 . 1 1 32 32 ALA N N 15 126.957 0.500 . 1 . . . . . . . . 5754 1 231 . 1 1 32 32 ALA H H 1 8.822 0.006 . 1 . . . . . . . . 5754 1 232 . 1 1 32 32 ALA CA C 13 49.033 0.000 . 1 . . . . . . . . 5754 1 233 . 1 1 32 32 ALA HA H 1 4.482 0.000 . 1 . . . . . . . . 5754 1 234 . 1 1 32 32 ALA HB1 H 1 1.241 0.000 . 1 . . . . . . . . 5754 1 235 . 1 1 32 32 ALA HB2 H 1 1.241 0.000 . 1 . . . . . . . . 5754 1 236 . 1 1 32 32 ALA HB3 H 1 1.241 0.000 . 1 . . . . . . . . 5754 1 237 . 1 1 32 32 ALA CB C 13 20.039 0.000 . 1 . . . . . . . . 5754 1 238 . 1 1 32 32 ALA C C 13 174.299 0.000 . 1 . . . . . . . . 5754 1 239 . 1 1 33 33 PHE N N 15 118.001 0.035 . 1 . . . . . . . . 5754 1 240 . 1 1 33 33 PHE H H 1 8.521 0.006 . 1 . . . . . . . . 5754 1 241 . 1 1 33 33 PHE CA C 13 56.933 0.000 . 1 . . . . . . . . 5754 1 242 . 1 1 33 33 PHE HA H 1 5.450 0.000 . 1 . . . . . . . . 5754 1 243 . 1 1 33 33 PHE CB C 13 38.421 0.000 . 1 . . . . . . . . 5754 1 244 . 1 1 33 33 PHE HB2 H 1 3.119 0.000 . 1 . . . . . . . . 5754 1 245 . 1 1 33 33 PHE HB3 H 1 2.759 0.000 . 1 . . . . . . . . 5754 1 246 . 1 1 33 33 PHE C C 13 172.738 0.000 . 1 . . . . . . . . 5754 1 247 . 1 1 34 34 SER N N 15 115.141 0.079 . 1 . . . . . . . . 5754 1 248 . 1 1 34 34 SER H H 1 8.756 0.002 . 1 . . . . . . . . 5754 1 249 . 1 1 34 34 SER CA C 13 56.613 0.000 . 1 . . . . . . . . 5754 1 250 . 1 1 34 34 SER CB C 13 63.688 0.000 . 1 . . . . . . . . 5754 1 251 . 1 1 34 34 SER C C 13 170.832 0.000 . 1 . . . . . . . . 5754 1 252 . 1 1 35 35 ARG N N 15 121.930 0.030 . 1 . . . . . . . . 5754 1 253 . 1 1 35 35 ARG H H 1 8.494 0.005 . 1 . . . . . . . . 5754 1 254 . 1 1 35 35 ARG CA C 13 52.697 0.000 . 1 . . . . . . . . 5754 1 255 . 1 1 35 35 ARG HA H 1 4.757 0.000 . 1 . . . . . . . . 5754 1 256 . 1 1 35 35 ARG CB C 13 27.429 0.000 . 1 . . . . . . . . 5754 1 257 . 1 1 35 35 ARG HB2 H 1 1.725 0.000 . 1 . . . . . . . . 5754 1 258 . 1 1 35 35 ARG HB3 H 1 1.883 0.000 . 1 . . . . . . . . 5754 1 259 . 1 1 35 35 ARG HG2 H 1 1.480 0.000 . 1 . . . . . . . . 5754 1 260 . 1 1 35 35 ARG C C 13 173.576 0.000 . 1 . . . . . . . . 5754 1 261 . 1 1 36 36 VAL N N 15 129.231 0.495 . 1 . . . . . . . . 5754 1 262 . 1 1 36 36 VAL H H 1 9.362 0.008 . 1 . . . . . . . . 5754 1 263 . 1 1 36 36 VAL CA C 13 58.538 0.000 . 1 . . . . . . . . 5754 1 264 . 1 1 36 36 VAL HA H 1 4.757 0.000 . 1 . . . . . . . . 5754 1 265 . 1 1 36 36 VAL CB C 13 30.019 0.000 . 1 . . . . . . . . 5754 1 266 . 1 1 36 36 VAL HB H 1 1.618 0.000 . 1 . . . . . . . . 5754 1 267 . 1 1 36 36 VAL HG11 H 1 0.497 0.000 . 1 . . . . . . . . 5754 1 268 . 1 1 36 36 VAL HG12 H 1 0.497 0.000 . 1 . . . . . . . . 5754 1 269 . 1 1 36 36 VAL HG13 H 1 0.497 0.000 . 1 . . . . . . . . 5754 1 270 . 1 1 36 36 VAL C C 13 172.015 0.000 . 1 . . . . . . . . 5754 1 271 . 1 1 37 37 GLN N N 15 123.710 0.385 . 1 . . . . . . . . 5754 1 272 . 1 1 37 37 GLN H H 1 9.095 0.004 . 1 . . . . . . . . 5754 1 273 . 1 1 37 37 GLN CA C 13 51.199 0.000 . 1 . . . . . . . . 5754 1 274 . 1 1 37 37 GLN HA H 1 5.450 0.000 . 1 . . . . . . . . 5754 1 275 . 1 1 37 37 GLN CB C 13 31.725 0.000 . 1 . . . . . . . . 5754 1 276 . 1 1 37 37 GLN HB2 H 1 1.964 0.000 . 1 . . . . . . . . 5754 1 277 . 1 1 37 37 GLN C C 13 172.327 0.000 . 1 . . . . . . . . 5754 1 278 . 1 1 38 38 ILE N N 15 117.834 0.218 . 1 . . . . . . . . 5754 1 279 . 1 1 38 38 ILE H H 1 7.513 0.003 . 1 . . . . . . . . 5754 1 280 . 1 1 38 38 ILE CA C 13 58.129 0.000 . 1 . . . . . . . . 5754 1 281 . 1 1 38 38 ILE HA H 1 5.002 0.000 . 1 . . . . . . . . 5754 1 282 . 1 1 38 38 ILE CB C 13 36.905 0.000 . 1 . . . . . . . . 5754 1 283 . 1 1 38 38 ILE HB H 1 1.393 0.000 . 1 . . . . . . . . 5754 1 284 . 1 1 38 38 ILE HG21 H 1 0.621 0.000 . 1 . . . . . . . . 5754 1 285 . 1 1 38 38 ILE HG22 H 1 0.621 0.000 . 1 . . . . . . . . 5754 1 286 . 1 1 38 38 ILE HG23 H 1 0.621 0.000 . 1 . . . . . . . . 5754 1 287 . 1 1 38 38 ILE C C 13 172.771 0.000 . 1 . . . . . . . . 5754 1 288 . 1 1 39 39 TYR N N 15 126.470 0.326 . 1 . . . . . . . . 5754 1 289 . 1 1 39 39 TYR H H 1 9.401 0.011 . 1 . . . . . . . . 5754 1 290 . 1 1 39 39 TYR CA C 13 53.875 0.000 . 1 . . . . . . . . 5754 1 291 . 1 1 39 39 TYR HA H 1 5.175 0.000 . 1 . . . . . . . . 5754 1 292 . 1 1 39 39 TYR CB C 13 39.431 0.000 . 1 . . . . . . . . 5754 1 293 . 1 1 39 39 TYR HB2 H 1 2.708 0.000 . 1 . . . . . . . . 5754 1 294 . 1 1 39 39 TYR C C 13 173.346 0.000 . 1 . . . . . . . . 5754 1 295 . 1 1 40 40 HIS N N 15 121.613 0.001 . 1 . . . . . . . . 5754 1 296 . 1 1 40 40 HIS H H 1 9.476 0.008 . 1 . . . . . . . . 5754 1 297 . 1 1 40 40 HIS CA C 13 49.9 0.000 . 1 . . . . . . . . 5754 1 298 . 1 1 40 40 HIS HA H 1 4.523 0.000 . 1 . . . . . . . . 5754 1 299 . 1 1 40 40 HIS CB C 13 32.42 0.000 . 1 . . . . . . . . 5754 1 300 . 1 1 40 40 HIS HB2 H 1 2.496 0.000 . 1 . . . . . . . . 5754 1 301 . 1 1 40 40 HIS C C 13 171.045 0.000 . 1 . . . . . . . . 5754 1 302 . 1 1 41 41 ASN N N 15 125.606 0.337 . 1 . . . . . . . . 5754 1 303 . 1 1 41 41 ASN H H 1 8.434 0.008 . 1 . . . . . . . . 5754 1 304 . 1 1 41 41 ASN CA C 13 46.57 0.000 . 1 . . . . . . . . 5754 1 305 . 1 1 41 41 ASN CB C 13 36.21 0.000 . 1 . . . . . . . . 5754 1 306 . 1 1 41 41 ASN HB2 H 1 1.969 0.000 . 1 . . . . . . . . 5754 1 307 . 1 1 41 41 ASN C C 13 171.87 0.000 . 1 . . . . . . . . 5754 1 308 . 1 1 42 42 PRO CA C 13 61.288 0.000 . 1 . . . . . . . . 5754 1 309 . 1 1 42 42 PRO HA H 1 3.677 0.000 . 1 . . . . . . . . 5754 1 310 . 1 1 42 42 PRO CB C 13 29.388 0.000 . 1 . . . . . . . . 5754 1 311 . 1 1 42 42 PRO HB3 H 1 1.803 0.000 . 1 . . . . . . . . 5754 1 312 . 1 1 42 42 PRO C C 13 175.548 0.000 . 1 . . . . . . . . 5754 1 313 . 1 1 43 43 THR N N 15 113.893 0.074 . 1 . . . . . . . . 5754 1 314 . 1 1 43 43 THR H H 1 7.657 0.001 . 1 . . . . . . . . 5754 1 315 . 1 1 43 43 THR CA C 13 62.743 0.000 . 1 . . . . . . . . 5754 1 316 . 1 1 43 43 THR HA H 1 4.064 0.000 . 1 . . . . . . . . 5754 1 317 . 1 1 43 43 THR CB C 13 65.583 0.000 . 1 . . . . . . . . 5754 1 318 . 1 1 43 43 THR HG21 H 1 1.118 0.000 . 1 . . . . . . . . 5754 1 319 . 1 1 43 43 THR HG22 H 1 1.118 0.000 . 1 . . . . . . . . 5754 1 320 . 1 1 43 43 THR HG23 H 1 1.118 0.000 . 1 . . . . . . . . 5754 1 321 . 1 1 43 43 THR C C 13 172.738 0.000 . 1 . . . . . . . . 5754 1 322 . 1 1 44 44 ALA N N 15 121.481 0.110 . 1 . . . . . . . . 5754 1 323 . 1 1 44 44 ALA H H 1 6.874 0.006 . 1 . . . . . . . . 5754 1 324 . 1 1 44 44 ALA CA C 13 48.906 0.000 . 1 . . . . . . . . 5754 1 325 . 1 1 44 44 ALA HA H 1 4.223 0.000 . 1 . . . . . . . . 5754 1 326 . 1 1 44 44 ALA HB1 H 1 1.128 0.000 . 1 . . . . . . . . 5754 1 327 . 1 1 44 44 ALA HB2 H 1 1.128 0.000 . 1 . . . . . . . . 5754 1 328 . 1 1 44 44 ALA HB3 H 1 1.128 0.000 . 1 . . . . . . . . 5754 1 329 . 1 1 44 44 ALA CB C 13 16.754 0.000 . 1 . . . . . . . . 5754 1 330 . 1 1 44 44 ALA C C 13 174.644 0.000 . 1 . . . . . . . . 5754 1 331 . 1 1 45 45 ASN N N 15 116.712 0.136 . 1 . . . . . . . . 5754 1 332 . 1 1 45 45 ASN H H 1 7.841 0.002 . 1 . . . . . . . . 5754 1 333 . 1 1 45 45 ASN CA C 13 51.123 0.000 . 1 . . . . . . . . 5754 1 334 . 1 1 45 45 ASN HA H 1 4.135 0.000 . 1 . . . . . . . . 5754 1 335 . 1 1 45 45 ASN CB C 13 34.631 0.000 . 1 . . . . . . . . 5754 1 336 . 1 1 45 45 ASN HB2 H 1 3.304 0.000 . 1 . . . . . . . . 5754 1 337 . 1 1 45 45 ASN HB3 H 1 2.417 0.000 . 1 . . . . . . . . 5754 1 338 . 1 1 45 45 ASN C C 13 169.912 0.000 . 1 . . . . . . . . 5754 1 339 . 1 1 46 46 SER N N 15 109.097 0.297 . 1 . . . . . . . . 5754 1 340 . 1 1 46 46 SER H H 1 7.492 0.003 . 1 . . . . . . . . 5754 1 341 . 1 1 46 46 SER CA C 13 53.493 0.000 . 1 . . . . . . . . 5754 1 342 . 1 1 46 46 SER HA H 1 4.074 0.000 . 1 . . . . . . . . 5754 1 343 . 1 1 46 46 SER CB C 13 64.194 0.000 . 1 . . . . . . . . 5754 1 344 . 1 1 46 46 SER HB2 H 1 3.495 0.000 . 1 . . . . . . . . 5754 1 345 . 1 1 46 46 SER C C 13 171.21 0.000 . 1 . . . . . . . . 5754 1 346 . 1 1 47 47 PHE N N 15 119.533 0.079 . 1 . . . . . . . . 5754 1 347 . 1 1 47 47 PHE H H 1 9.320 0.000 . 1 . . . . . . . . 5754 1 348 . 1 1 47 47 PHE CA C 13 53.951 0.000 . 1 . . . . . . . . 5754 1 349 . 1 1 47 47 PHE HA H 1 5.797 0.000 . 1 . . . . . . . . 5754 1 350 . 1 1 47 47 PHE CB C 13 42.337 0.000 . 1 . . . . . . . . 5754 1 351 . 1 1 47 47 PHE HB2 H 1 2.663 0.000 . 1 . . . . . . . . 5754 1 352 . 1 1 47 47 PHE C C 13 173.067 0.000 . 1 . . . . . . . . 5754 1 353 . 1 1 48 48 ARG N N 15 118.531 0.079 . 1 . . . . . . . . 5754 1 354 . 1 1 48 48 ARG H H 1 8.842 0.004 . 1 . . . . . . . . 5754 1 355 . 1 1 48 48 ARG CA C 13 52.27 0.000 . 1 . . . . . . . . 5754 1 356 . 1 1 48 48 ARG HA H 1 5.185 0.000 . 1 . . . . . . . . 5754 1 357 . 1 1 48 48 ARG CB C 13 31.409 0.000 . 1 . . . . . . . . 5754 1 358 . 1 1 48 48 ARG HB2 H 1 1.743 0.000 . 1 . . . . . . . . 5754 1 359 . 1 1 48 48 ARG HG2 H 1 1.524 0.000 . 1 . . . . . . . . 5754 1 360 . 1 1 48 48 ARG C C 13 171.029 0.000 . 1 . . . . . . . . 5754 1 361 . 1 1 49 49 VAL N N 15 122.356 0.040 . 1 . . . . . . . . 5754 1 362 . 1 1 49 49 VAL H H 1 9.143 0.001 . 1 . . . . . . . . 5754 1 363 . 1 1 49 49 VAL CA C 13 58.066 0.000 . 1 . . . . . . . . 5754 1 364 . 1 1 49 49 VAL HA H 1 5.002 0.000 . 1 . . . . . . . . 5754 1 365 . 1 1 49 49 VAL CB C 13 31.156 0.000 . 1 . . . . . . . . 5754 1 366 . 1 1 49 49 VAL HB H 1 1.944 0.000 . 1 . . . . . . . . 5754 1 367 . 1 1 49 49 VAL HG11 H 1 0.812 0.000 . 1 . . . . . . . . 5754 1 368 . 1 1 49 49 VAL HG12 H 1 0.812 0.000 . 1 . . . . . . . . 5754 1 369 . 1 1 49 49 VAL HG13 H 1 0.812 0.000 . 1 . . . . . . . . 5754 1 370 . 1 1 49 49 VAL C C 13 172.196 0.000 . 1 . . . . . . . . 5754 1 371 . 1 1 50 50 VAL N N 15 124.720 0.326 . 1 . . . . . . . . 5754 1 372 . 1 1 50 50 VAL H H 1 8.808 0.001 . 1 . . . . . . . . 5754 1 373 . 1 1 50 50 VAL CA C 13 57.94 0.000 . 1 . . . . . . . . 5754 1 374 . 1 1 50 50 VAL HA H 1 5.002 0.000 . 1 . . . . . . . . 5754 1 375 . 1 1 50 50 VAL CB C 13 32.925 0.000 . 1 . . . . . . . . 5754 1 376 . 1 1 50 50 VAL HB H 1 1.954 0.000 . 1 . . . . . . . . 5754 1 377 . 1 1 50 50 VAL HG11 H 1 0.925 0.000 . 1 . . . . . . . . 5754 1 378 . 1 1 50 50 VAL HG12 H 1 0.925 0.000 . 1 . . . . . . . . 5754 1 379 . 1 1 50 50 VAL HG13 H 1 0.925 0.000 . 1 . . . . . . . . 5754 1 380 . 1 1 50 50 VAL HG21 H 1 0.762 0.000 . 1 . . . . . . . . 5754 1 381 . 1 1 50 50 VAL HG22 H 1 0.762 0.000 . 1 . . . . . . . . 5754 1 382 . 1 1 50 50 VAL HG23 H 1 0.762 0.000 . 1 . . . . . . . . 5754 1 383 . 1 1 50 50 VAL C C 13 172.944 0.000 . 1 . . . . . . . . 5754 1 384 . 1 1 51 51 GLY N N 15 115.618 0.157 . 1 . . . . . . . . 5754 1 385 . 1 1 51 51 GLY H H 1 8.971 0.003 . 1 . . . . . . . . 5754 1 386 . 1 1 51 51 GLY CA C 13 42.332 0.000 . 1 . . . . . . . . 5754 1 387 . 1 1 51 51 GLY HA2 H 1 5.685 0.000 . 1 . . . . . . . . 5754 1 388 . 1 1 51 51 GLY HA3 H 1 3.057 0.000 . 1 . . . . . . . . 5754 1 389 . 1 1 51 51 GLY C C 13 173.355 0.000 . 1 . . . . . . . . 5754 1 390 . 1 1 52 52 ARG N N 15 123.065 0.071 . 1 . . . . . . . . 5754 1 391 . 1 1 52 52 ARG H H 1 8.051 0.001 . 1 . . . . . . . . 5754 1 392 . 1 1 52 52 ARG CA C 13 51.352 0.000 . 1 . . . . . . . . 5754 1 393 . 1 1 52 52 ARG HA H 1 5.277 0.000 . 1 . . . . . . . . 5754 1 394 . 1 1 52 52 ARG CB C 13 31.283 0.000 . 1 . . . . . . . . 5754 1 395 . 1 1 52 52 ARG HB2 H 1 1.550 0.000 . 1 . . . . . . . . 5754 1 396 . 1 1 52 52 ARG C C 13 173.346 0.000 . 1 . . . . . . . . 5754 1 397 . 1 1 53 53 LYS N N 15 124.940 0.198 . 1 . . . . . . . . 5754 1 398 . 1 1 53 53 LYS H H 1 9.116 0.002 . 1 . . . . . . . . 5754 1 399 . 1 1 53 53 LYS CA C 13 55.54 0.000 . 1 . . . . . . . . 5754 1 400 . 1 1 53 53 LYS HA H 1 4.472 0.000 . 1 . . . . . . . . 5754 1 401 . 1 1 53 53 LYS CB C 13 32.483 0.000 . 1 . . . . . . . . 5754 1 402 . 1 1 53 53 LYS HB2 H 1 1.637 0.000 . 1 . . . . . . . . 5754 1 403 . 1 1 53 53 LYS HG2 H 1 1.383 0.000 . 1 . . . . . . . . 5754 1 404 . 1 1 53 53 LYS C C 13 175.318 0.000 . 1 . . . . . . . . 5754 1 405 . 1 1 54 54 MET N N 15 121.877 0.107 . 1 . . . . . . . . 5754 1 406 . 1 1 54 54 MET H H 1 8.867 0.006 . 1 . . . . . . . . 5754 1 407 . 1 1 54 54 MET CA C 13 52.76 0.000 . 1 . . . . . . . . 5754 1 408 . 1 1 54 54 MET HA H 1 4.521 0.000 . 1 . . . . . . . . 5754 1 409 . 1 1 54 54 MET CB C 13 27.493 0.000 . 1 . . . . . . . . 5754 1 410 . 1 1 54 54 MET C C 13 172.246 0.000 . 1 . . . . . . . . 5754 1 411 . 1 1 55 55 GLN N N 15 120.457 0.033 . 1 . . . . . . . . 5754 1 412 . 1 1 55 55 GLN H H 1 8.557 0.038 . 1 . . . . . . . . 5754 1 413 . 1 1 55 55 GLN CA C 13 52.823 0.000 . 1 . . . . . . . . 5754 1 414 . 1 1 55 55 GLN CB C 13 27.556 0.000 . 1 . . . . . . . . 5754 1 415 . 1 1 56 56 PRO CA C 13 64.194 0.000 . 1 . . . . . . . . 5754 1 416 . 1 1 56 56 PRO HA H 1 4.166 0.000 . 1 . . . . . . . . 5754 1 417 . 1 1 56 56 PRO CB C 13 29.324 0.000 . 1 . . . . . . . . 5754 1 418 . 1 1 56 56 PRO HB2 H 1 2.311 0.000 . 1 . . . . . . . . 5754 1 419 . 1 1 56 56 PRO HB3 H 1 1.890 0.000 . 1 . . . . . . . . 5754 1 420 . 1 1 56 56 PRO C C 13 174.192 0.000 . 1 . . . . . . . . 5754 1 421 . 1 1 57 57 ASP N N 15 112.857 0.146 . 1 . . . . . . . . 5754 1 422 . 1 1 57 57 ASP H H 1 8.211 0.007 . 1 . . . . . . . . 5754 1 423 . 1 1 57 57 ASP CA C 13 51.658 0.000 . 1 . . . . . . . . 5754 1 424 . 1 1 57 57 ASP HA H 1 4.298 0.000 . 1 . . . . . . . . 5754 1 425 . 1 1 57 57 ASP CB C 13 37.157 0.000 . 1 . . . . . . . . 5754 1 426 . 1 1 57 57 ASP HB2 H 1 2.899 0.000 . 1 . . . . . . . . 5754 1 427 . 1 1 57 57 ASP HB3 H 1 2.575 0.000 . 1 . . . . . . . . 5754 1 428 . 1 1 57 57 ASP C C 13 173.79 0.000 . 1 . . . . . . . . 5754 1 429 . 1 1 58 58 GLN N N 15 115.909 0.029 . 1 . . . . . . . . 5754 1 430 . 1 1 58 58 GLN H H 1 8.316 0.004 . 1 . . . . . . . . 5754 1 431 . 1 1 58 58 GLN CA C 13 53.455 0.000 . 1 . . . . . . . . 5754 1 432 . 1 1 58 58 GLN HA H 1 4.468 0.000 . 1 . . . . . . . . 5754 1 433 . 1 1 58 58 GLN CB C 13 25.408 0.000 . 1 . . . . . . . . 5754 1 434 . 1 1 58 58 GLN HB2 H 1 2.084 0.000 . 1 . . . . . . . . 5754 1 435 . 1 1 58 58 GLN HG2 H 1 2.330 0.000 . 1 . . . . . . . . 5754 1 436 . 1 1 58 58 GLN C C 13 173.797 0.000 . 1 . . . . . . . . 5754 1 437 . 1 1 59 59 GLN N N 15 115.852 0.099 . 1 . . . . . . . . 5754 1 438 . 1 1 59 59 GLN H H 1 7.421 0.000 . 1 . . . . . . . . 5754 1 439 . 1 1 59 59 GLN CA C 13 54.869 0.000 . 1 . . . . . . . . 5754 1 440 . 1 1 59 59 GLN HA H 1 3.789 0.000 . 1 . . . . . . . . 5754 1 441 . 1 1 59 59 GLN CB C 13 28.693 0.000 . 1 . . . . . . . . 5754 1 442 . 1 1 59 59 GLN HB2 H 1 1.673 0.000 . 1 . . . . . . . . 5754 1 443 . 1 1 59 59 GLN HG2 H 1 2.067 0.000 . 1 . . . . . . . . 5754 1 444 . 1 1 59 59 GLN C C 13 173.757 0.000 . 1 . . . . . . . . 5754 1 445 . 1 1 60 60 VAL N N 15 126.866 0.270 . 1 . . . . . . . . 5754 1 446 . 1 1 60 60 VAL H H 1 8.731 0.002 . 1 . . . . . . . . 5754 1 447 . 1 1 60 60 VAL CA C 13 60.373 0.000 . 1 . . . . . . . . 5754 1 448 . 1 1 60 60 VAL HA H 1 4.380 0.000 . 1 . . . . . . . . 5754 1 449 . 1 1 60 60 VAL CB C 13 28.819 0.000 . 1 . . . . . . . . 5754 1 450 . 1 1 60 60 VAL HB H 1 2.025 0.000 . 1 . . . . . . . . 5754 1 451 . 1 1 60 60 VAL HG11 H 1 1.037 0.000 . 1 . . . . . . . . 5754 1 452 . 1 1 60 60 VAL HG12 H 1 1.037 0.000 . 1 . . . . . . . . 5754 1 453 . 1 1 60 60 VAL HG13 H 1 1.037 0.000 . 1 . . . . . . . . 5754 1 454 . 1 1 60 60 VAL HG21 H 1 0.925 0.000 . 1 . . . . . . . . 5754 1 455 . 1 1 60 60 VAL HG22 H 1 0.925 0.000 . 1 . . . . . . . . 5754 1 456 . 1 1 60 60 VAL HG23 H 1 0.925 0.000 . 1 . . . . . . . . 5754 1 457 . 1 1 60 60 VAL C C 13 175.104 0.000 . 1 . . . . . . . . 5754 1 458 . 1 1 61 61 VAL N N 15 119.962 0.071 . 1 . . . . . . . . 5754 1 459 . 1 1 61 61 VAL H H 1 8.356 0.002 . 1 . . . . . . . . 5754 1 460 . 1 1 61 61 VAL CA C 13 58.508 0.000 . 1 . . . . . . . . 5754 1 461 . 1 1 61 61 VAL HA H 1 4.461 0.000 . 1 . . . . . . . . 5754 1 462 . 1 1 61 61 VAL CB C 13 30.525 0.000 . 1 . . . . . . . . 5754 1 463 . 1 1 61 61 VAL HB H 1 2.046 0.000 . 1 . . . . . . . . 5754 1 464 . 1 1 61 61 VAL HG11 H 1 0.863 0.000 . 1 . . . . . . . . 5754 1 465 . 1 1 61 61 VAL HG12 H 1 0.863 0.000 . 1 . . . . . . . . 5754 1 466 . 1 1 61 61 VAL HG13 H 1 0.863 0.000 . 1 . . . . . . . . 5754 1 467 . 1 1 61 61 VAL HG21 H 1 0.700 0.000 . 1 . . . . . . . . 5754 1 468 . 1 1 61 61 VAL HG22 H 1 0.700 0.000 . 1 . . . . . . . . 5754 1 469 . 1 1 61 61 VAL HG23 H 1 0.700 0.000 . 1 . . . . . . . . 5754 1 470 . 1 1 61 61 VAL C C 13 171.867 0.000 . 1 . . . . . . . . 5754 1 471 . 1 1 62 62 ILE N N 15 116.389 0.163 . 1 . . . . . . . . 5754 1 472 . 1 1 62 62 ILE H H 1 7.183 0.005 . 1 . . . . . . . . 5754 1 473 . 1 1 62 62 ILE CA C 13 58.003 0.000 . 1 . . . . . . . . 5754 1 474 . 1 1 62 62 ILE HA H 1 4.054 0.000 . 1 . . . . . . . . 5754 1 475 . 1 1 62 62 ILE CB C 13 36.652 0.000 . 1 . . . . . . . . 5754 1 476 . 1 1 62 62 ILE HB H 1 1.366 0.000 . 1 . . . . . . . . 5754 1 477 . 1 1 62 62 ILE HG21 H 1 0.533 0.000 . 1 . . . . . . . . 5754 1 478 . 1 1 62 62 ILE HG22 H 1 0.533 0.000 . 1 . . . . . . . . 5754 1 479 . 1 1 62 62 ILE HG23 H 1 0.533 0.000 . 1 . . . . . . . . 5754 1 480 . 1 1 62 62 ILE C C 13 170.24 0.000 . 1 . . . . . . . . 5754 1 481 . 1 1 63 63 ASN N N 15 125.023 0.210 . 1 . . . . . . . . 5754 1 482 . 1 1 63 63 ASN H H 1 8.121 0.003 . 1 . . . . . . . . 5754 1 483 . 1 1 63 63 ASN CA C 13 50.053 0.000 . 1 . . . . . . . . 5754 1 484 . 1 1 63 63 ASN HA H 1 5.348 0.000 . 1 . . . . . . . . 5754 1 485 . 1 1 63 63 ASN CB C 13 35.136 0.000 . 1 . . . . . . . . 5754 1 486 . 1 1 63 63 ASN HB2 H 1 2.780 0.000 . 1 . . . . . . . . 5754 1 487 . 1 1 63 63 ASN HB3 H 1 2.566 0.000 . 1 . . . . . . . . 5754 1 488 . 1 1 63 63 ASN C C 13 171.867 0.000 . 1 . . . . . . . . 5754 1 489 . 1 1 64 64 CYS N N 15 119.774 0.019 . 1 . . . . . . . . 5754 1 490 . 1 1 64 64 CYS H H 1 8.835 0.003 . 1 . . . . . . . . 5754 1 491 . 1 1 64 64 CYS CA C 13 53.187 0.000 . 1 . . . . . . . . 5754 1 492 . 1 1 64 64 CYS HA H 1 5.012 0.000 . 1 . . . . . . . . 5754 1 493 . 1 1 64 64 CYS CB C 13 28.44 0.000 . 1 . . . . . . . . 5754 1 494 . 1 1 64 64 CYS HB2 H 1 2.812 0.000 . 1 . . . . . . . . 5754 1 495 . 1 1 64 64 CYS C C 13 170.536 0.000 . 1 . . . . . . . . 5754 1 496 . 1 1 65 65 ALA N N 15 126.960 0.400 . 1 . . . . . . . . 5754 1 497 . 1 1 65 65 ALA H H 1 8.844 0.003 . 1 . . . . . . . . 5754 1 498 . 1 1 65 65 ALA CA C 13 49.981 0.000 . 1 . . . . . . . . 5754 1 499 . 1 1 65 65 ALA HA H 1 4.533 0.000 . 1 . . . . . . . . 5754 1 500 . 1 1 65 65 ALA HB1 H 1 1.427 0.000 . 1 . . . . . . . . 5754 1 501 . 1 1 65 65 ALA HB2 H 1 1.427 0.000 . 1 . . . . . . . . 5754 1 502 . 1 1 65 65 ALA HB3 H 1 1.427 0.000 . 1 . . . . . . . . 5754 1 503 . 1 1 65 65 ALA CB C 13 16.88 0.000 . 1 . . . . . . . . 5754 1 504 . 1 1 65 65 ALA C C 13 175.17 0.000 . 1 . . . . . . . . 5754 1 505 . 1 1 66 66 ILE N N 15 123.013 0.126 . 1 . . . . . . . . 5754 1 506 . 1 1 66 66 ILE H H 1 8.146 0.003 . 1 . . . . . . . . 5754 1 507 . 1 1 66 66 ILE CA C 13 58.256 0.000 . 1 . . . . . . . . 5754 1 508 . 1 1 66 66 ILE HA H 1 4.033 0.000 . 1 . . . . . . . . 5754 1 509 . 1 1 66 66 ILE CB C 13 35.073 0.000 . 1 . . . . . . . . 5754 1 510 . 1 1 66 66 ILE HB H 1 1.506 0.000 . 1 . . . . . . . . 5754 1 511 . 1 1 66 66 ILE HG21 H 1 0.454 0.000 . 1 . . . . . . . . 5754 1 512 . 1 1 66 66 ILE HG22 H 1 0.454 0.000 . 1 . . . . . . . . 5754 1 513 . 1 1 66 66 ILE HG23 H 1 0.454 0.000 . 1 . . . . . . . . 5754 1 514 . 1 1 66 66 ILE C C 13 171.522 0.000 . 1 . . . . . . . . 5754 1 515 . 1 1 67 67 VAL N N 15 117.971 0.089 . 1 . . . . . . . . 5754 1 516 . 1 1 67 67 VAL H H 1 6.796 0.010 . 1 . . . . . . . . 5754 1 517 . 1 1 67 67 VAL CA C 13 56.245 0.000 . 1 . . . . . . . . 5754 1 518 . 1 1 67 67 VAL HA H 1 4.645 0.000 . 1 . . . . . . . . 5754 1 519 . 1 1 67 67 VAL CB C 13 32.672 0.000 . 1 . . . . . . . . 5754 1 520 . 1 1 67 67 VAL HB H 1 2.242 0.000 . 1 . . . . . . . . 5754 1 521 . 1 1 67 67 VAL HG11 H 1 1.015 0.000 . 1 . . . . . . . . 5754 1 522 . 1 1 67 67 VAL HG12 H 1 1.015 0.000 . 1 . . . . . . . . 5754 1 523 . 1 1 67 67 VAL HG13 H 1 1.015 0.000 . 1 . . . . . . . . 5754 1 524 . 1 1 67 67 VAL HG21 H 1 0.884 0.000 . 1 . . . . . . . . 5754 1 525 . 1 1 67 67 VAL HG22 H 1 0.884 0.000 . 1 . . . . . . . . 5754 1 526 . 1 1 67 67 VAL HG23 H 1 0.884 0.000 . 1 . . . . . . . . 5754 1 527 . 1 1 67 67 VAL C C 13 171.916 0.000 . 1 . . . . . . . . 5754 1 528 . 1 1 68 68 ARG N N 15 119.554 0.010 . 1 . . . . . . . . 5754 1 529 . 1 1 68 68 ARG H H 1 8.429 0.003 . 1 . . . . . . . . 5754 1 530 . 1 1 68 68 ARG CA C 13 55.71 0.000 . 1 . . . . . . . . 5754 1 531 . 1 1 68 68 ARG HA H 1 3.840 0.000 . 1 . . . . . . . . 5754 1 532 . 1 1 68 68 ARG CB C 13 27.619 0.000 . 1 . . . . . . . . 5754 1 533 . 1 1 68 68 ARG HB2 H 1 1.708 0.000 . 1 . . . . . . . . 5754 1 534 . 1 1 68 68 ARG HG2 H 1 1.559 0.000 . 1 . . . . . . . . 5754 1 535 . 1 1 68 68 ARG C C 13 175.061 0.000 . 1 . . . . . . . . 5754 1 536 . 1 1 69 69 GLY N N 15 113.357 0.217 . 1 . . . . . . . . 5754 1 537 . 1 1 69 69 GLY H H 1 8.973 0.003 . 1 . . . . . . . . 5754 1 538 . 1 1 69 69 GLY CA C 13 42.527 0.000 . 1 . . . . . . . . 5754 1 539 . 1 1 69 69 GLY HA2 H 1 4.278 0.000 . 1 . . . . . . . . 5754 1 540 . 1 1 69 69 GLY HA3 H 1 3.574 0.000 . 1 . . . . . . . . 5754 1 541 . 1 1 69 69 GLY C C 13 172.392 0.000 . 1 . . . . . . . . 5754 1 542 . 1 1 70 70 VAL N N 15 121.252 0.139 . 1 . . . . . . . . 5754 1 543 . 1 1 70 70 VAL H H 1 7.463 0.004 . 1 . . . . . . . . 5754 1 544 . 1 1 70 70 VAL CA C 13 61.288 0.000 . 1 . . . . . . . . 5754 1 545 . 1 1 70 70 VAL HA H 1 4.064 0.000 . 1 . . . . . . . . 5754 1 546 . 1 1 70 70 VAL CB C 13 29.64 0.000 . 1 . . . . . . . . 5754 1 547 . 1 1 70 70 VAL HB H 1 2.087 0.000 . 1 . . . . . . . . 5754 1 548 . 1 1 70 70 VAL HG11 H 1 1.251 0.000 . 1 . . . . . . . . 5754 1 549 . 1 1 70 70 VAL HG12 H 1 1.251 0.000 . 1 . . . . . . . . 5754 1 550 . 1 1 70 70 VAL HG13 H 1 1.251 0.000 . 1 . . . . . . . . 5754 1 551 . 1 1 70 70 VAL HG21 H 1 0.833 0.000 . 1 . . . . . . . . 5754 1 552 . 1 1 70 70 VAL HG22 H 1 0.833 0.000 . 1 . . . . . . . . 5754 1 553 . 1 1 70 70 VAL HG23 H 1 0.833 0.000 . 1 . . . . . . . . 5754 1 554 . 1 1 70 70 VAL C C 13 172.297 0.000 . 1 . . . . . . . . 5754 1 555 . 1 1 71 71 LYS N N 15 126.220 0.409 . 1 . . . . . . . . 5754 1 556 . 1 1 71 71 LYS H H 1 8.439 0.004 . 1 . . . . . . . . 5754 1 557 . 1 1 71 71 LYS CA C 13 51.813 0.000 . 1 . . . . . . . . 5754 1 558 . 1 1 71 71 LYS HA H 1 4.533 0.000 . 1 . . . . . . . . 5754 1 559 . 1 1 71 71 LYS CB C 13 30.082 0.000 . 1 . . . . . . . . 5754 1 560 . 1 1 71 71 LYS HB2 H 1 1.760 0.000 . 1 . . . . . . . . 5754 1 561 . 1 1 71 71 LYS HG2 H 1 1.410 0.000 . 1 . . . . . . . . 5754 1 562 . 1 1 71 71 LYS C C 13 172.076 0.000 . 1 . . . . . . . . 5754 1 563 . 1 1 72 72 TYR N N 15 127.700 0.434 . 1 . . . . . . . . 5754 1 564 . 1 1 72 72 TYR H H 1 8.690 0.001 . 1 . . . . . . . . 5754 1 565 . 1 1 72 72 TYR CA C 13 55.098 0.000 . 1 . . . . . . . . 5754 1 566 . 1 1 72 72 TYR HA H 1 4.971 0.000 . 1 . . . . . . . . 5754 1 567 . 1 1 72 72 TYR CB C 13 37.979 0.000 . 1 . . . . . . . . 5754 1 568 . 1 1 72 72 TYR HB2 H 1 2.829 0.000 . 1 . . . . . . . . 5754 1 569 . 1 1 72 72 TYR HB3 H 1 2.465 0.109 . 1 . . . . . . . . 5754 1 570 . 1 1 72 72 TYR C C 13 171.999 0.000 . 1 . . . . . . . . 5754 1 571 . 1 1 73 73 ASN N N 15 126.666 0.416 . 1 . . . . . . . . 5754 1 572 . 1 1 73 73 ASN H H 1 9.082 0.001 . 1 . . . . . . . . 5754 1 573 . 1 1 73 73 ASN CA C 13 49.791 0.000 . 1 . . . . . . . . 5754 1 574 . 1 1 73 73 ASN CB C 13 38.8 0.000 . 1 . . . . . . . . 5754 1 575 . 1 1 73 73 ASN HB2 H 1 2.688 0.000 . 1 . . . . . . . . 5754 1 576 . 1 1 73 73 ASN C C 13 172.048 0.000 . 1 . . . . . . . . 5754 1 577 . 1 1 74 74 GLN N N 15 125.366 0.316 . 1 . . . . . . . . 5754 1 578 . 1 1 74 74 GLN H H 1 8.722 0.005 . 1 . . . . . . . . 5754 1 579 . 1 1 74 74 GLN CA C 13 51.964 0.000 . 1 . . . . . . . . 5754 1 580 . 1 1 74 74 GLN HA H 1 4.125 0.000 . 1 . . . . . . . . 5754 1 581 . 1 1 74 74 GLN CB C 13 23.702 0.000 . 1 . . . . . . . . 5754 1 582 . 1 1 74 74 GLN HB2 H 1 1.436 0.000 . 1 . . . . . . . . 5754 1 583 . 1 1 74 74 GLN HG2 H 1 1.646 0.000 . 1 . . . . . . . . 5754 1 584 . 1 1 74 74 GLN C C 13 172.327 0.000 . 1 . . . . . . . . 5754 1 585 . 1 1 75 75 ALA N N 15 129.438 0.525 . 1 . . . . . . . . 5754 1 586 . 1 1 75 75 ALA H H 1 7.682 0.003 . 1 . . . . . . . . 5754 1 587 . 1 1 75 75 ALA CA C 13 52.958 0.000 . 1 . . . . . . . . 5754 1 588 . 1 1 75 75 ALA HA H 1 3.972 0.000 . 1 . . . . . . . . 5754 1 589 . 1 1 75 75 ALA HB1 H 1 1.480 0.000 . 1 . . . . . . . . 5754 1 590 . 1 1 75 75 ALA HB2 H 1 1.480 0.000 . 1 . . . . . . . . 5754 1 591 . 1 1 75 75 ALA HB3 H 1 1.480 0.000 . 1 . . . . . . . . 5754 1 592 . 1 1 75 75 ALA CB C 13 16.375 0.000 . 1 . . . . . . . . 5754 1 593 . 1 1 75 75 ALA C C 13 176.337 0.000 . 1 . . . . . . . . 5754 1 594 . 1 1 76 76 THR N N 15 109.493 0.348 . 1 . . . . . . . . 5754 1 595 . 1 1 76 76 THR H H 1 8.732 0.003 . 1 . . . . . . . . 5754 1 596 . 1 1 76 76 THR CA C 13 56.398 0.000 . 1 . . . . . . . . 5754 1 597 . 1 1 76 76 THR CB C 13 67.036 0.000 . 1 . . . . . . . . 5754 1 598 . 1 1 76 76 THR C C 13 170.752 0.000 . 1 . . . . . . . . 5754 1 599 . 1 1 77 77 PRO CA C 13 62.381 0.000 . 1 . . . . . . . . 5754 1 600 . 1 1 77 77 PRO HA H 1 4.459 0.000 . 1 . . . . . . . . 5754 1 601 . 1 1 77 77 PRO CB C 13 29.451 0.000 . 1 . . . . . . . . 5754 1 602 . 1 1 77 77 PRO HB2 H 1 1.917 0.000 . 1 . . . . . . . . 5754 1 603 . 1 1 77 77 PRO HB3 H 1 1.785 0.000 . 1 . . . . . . . . 5754 1 604 . 1 1 77 77 PRO C C 13 174.417 0.000 . 1 . . . . . . . . 5754 1 605 . 1 1 78 78 ASN N N 15 109.109 0.301 . 1 . . . . . . . . 5754 1 606 . 1 1 78 78 ASN H H 1 7.772 0.007 . 1 . . . . . . . . 5754 1 607 . 1 1 78 78 ASN CA C 13 50.681 0.000 . 1 . . . . . . . . 5754 1 608 . 1 1 78 78 ASN CB C 13 37.93 0.000 . 1 . . . . . . . . 5754 1 609 . 1 1 78 78 ASN HB2 H 1 2.759 0.000 . 1 . . . . . . . . 5754 1 610 . 1 1 78 78 ASN HB3 H 1 2.645 0.000 . 1 . . . . . . . . 5754 1 611 . 1 1 78 78 ASN C C 13 170.224 0.000 . 1 . . . . . . . . 5754 1 612 . 1 1 79 79 PHE N N 15 122.806 0.098 . 1 . . . . . . . . 5754 1 613 . 1 1 79 79 PHE H H 1 7.841 0.000 . 1 . . . . . . . . 5754 1 614 . 1 1 79 79 PHE CA C 13 54.104 0.000 . 1 . . . . . . . . 5754 1 615 . 1 1 79 79 PHE HA H 1 5.695 0.000 . 1 . . . . . . . . 5754 1 616 . 1 1 79 79 PHE CB C 13 38.294 0.000 . 1 . . . . . . . . 5754 1 617 . 1 1 79 79 PHE HB2 H 1 3.106 0.000 . 1 . . . . . . . . 5754 1 618 . 1 1 79 79 PHE HB3 H 1 2.525 0.000 . 1 . . . . . . . . 5754 1 619 . 1 1 79 79 PHE C C 13 171.276 0.000 . 1 . . . . . . . . 5754 1 620 . 1 1 80 80 HIS N N 15 125.802 0.473 . 1 . . . . . . . . 5754 1 621 . 1 1 80 80 HIS H H 1 8.006 0.008 . 1 . . . . . . . . 5754 1 622 . 1 1 80 80 HIS CA C 13 49.059 0.000 . 1 . . . . . . . . 5754 1 623 . 1 1 80 80 HIS HA H 1 5.450 0.000 . 1 . . . . . . . . 5754 1 624 . 1 1 80 80 HIS CB C 13 32.609 0.000 . 1 . . . . . . . . 5754 1 625 . 1 1 80 80 HIS HB2 H 1 2.996 0.000 . 1 . . . . . . . . 5754 1 626 . 1 1 80 80 HIS HB3 H 1 2.750 0.000 . 1 . . . . . . . . 5754 1 627 . 1 1 80 80 HIS C C 13 170.917 0.000 . 1 . . . . . . . . 5754 1 628 . 1 1 81 81 GLN N N 15 115.074 0.074 . 1 . . . . . . . . 5754 1 629 . 1 1 81 81 GLN H H 1 8.758 0.002 . 1 . . . . . . . . 5754 1 630 . 1 1 81 81 GLN CA C 13 51.623 0.000 . 1 . . . . . . . . 5754 1 631 . 1 1 81 81 GLN HA H 1 5.623 0.000 . 1 . . . . . . . . 5754 1 632 . 1 1 81 81 GLN CB C 13 31.599 0.000 . 1 . . . . . . . . 5754 1 633 . 1 1 81 81 GLN HB2 H 1 2.093 0.000 . 1 . . . . . . . . 5754 1 634 . 1 1 81 81 GLN HG2 H 1 1.900 0.000 . 1 . . . . . . . . 5754 1 635 . 1 1 81 81 GLN C C 13 171.489 0.000 . 1 . . . . . . . . 5754 1 636 . 1 1 82 82 TRP N N 15 119.178 0.093 . 1 . . . . . . . . 5754 1 637 . 1 1 82 82 TRP H H 1 9.026 0.004 . 1 . . . . . . . . 5754 1 638 . 1 1 82 82 TRP CA C 13 55.287 0.000 . 1 . . . . . . . . 5754 1 639 . 1 1 82 82 TRP HA H 1 5.256 0.000 . 1 . . . . . . . . 5754 1 640 . 1 1 82 82 TRP CB C 13 30.525 0.000 . 1 . . . . . . . . 5754 1 641 . 1 1 82 82 TRP HB2 H 1 3.565 0.000 . 1 . . . . . . . . 5754 1 642 . 1 1 82 82 TRP HB3 H 1 3.127 0.000 . 1 . . . . . . . . 5754 1 643 . 1 1 82 82 TRP C C 13 169.632 0.000 . 1 . . . . . . . . 5754 1 644 . 1 1 83 83 ARG N N 15 119.565 0.202 . 1 . . . . . . . . 5754 1 645 . 1 1 83 83 ARG H H 1 8.409 0.000 . 1 . . . . . . . . 5754 1 646 . 1 1 83 83 ARG CA C 13 52.318 0.000 . 1 . . . . . . . . 5754 1 647 . 1 1 83 83 ARG HA H 1 5.124 0.000 . 1 . . . . . . . . 5754 1 648 . 1 1 83 83 ARG CB C 13 30.588 0.000 . 1 . . . . . . . . 5754 1 649 . 1 1 83 83 ARG HB2 H 1 1.830 0.000 . 1 . . . . . . . . 5754 1 650 . 1 1 83 83 ARG HG2 H 1 1.594 0.000 . 1 . . . . . . . . 5754 1 651 . 1 1 83 83 ARG C C 13 173.707 0.000 . 1 . . . . . . . . 5754 1 652 . 1 1 84 84 ASP N N 15 126.177 0.391 . 1 . . . . . . . . 5754 1 653 . 1 1 84 84 ASP H H 1 8.898 0.004 . 1 . . . . . . . . 5754 1 654 . 1 1 84 84 ASP CA C 13 50.129 0.000 . 1 . . . . . . . . 5754 1 655 . 1 1 84 84 ASP HA H 1 4.512 0.000 . 1 . . . . . . . . 5754 1 656 . 1 1 84 84 ASP CB C 13 40.379 0.000 . 1 . . . . . . . . 5754 1 657 . 1 1 84 84 ASP HB2 H 1 2.978 0.000 . 1 . . . . . . . . 5754 1 658 . 1 1 84 84 ASP C C 13 172.952 0.000 . 1 . . . . . . . . 5754 1 659 . 1 1 85 85 ALA N N 15 120.951 0.046 . 1 . . . . . . . . 5754 1 660 . 1 1 85 85 ALA H H 1 8.483 0.002 . 1 . . . . . . . . 5754 1 661 . 1 1 85 85 ALA CA C 13 52.27 0.000 . 1 . . . . . . . . 5754 1 662 . 1 1 85 85 ALA HA H 1 4.012 0.000 . 1 . . . . . . . . 5754 1 663 . 1 1 85 85 ALA HB1 H 1 1.475 0.000 . 1 . . . . . . . . 5754 1 664 . 1 1 85 85 ALA HB2 H 1 1.475 0.000 . 1 . . . . . . . . 5754 1 665 . 1 1 85 85 ALA HB3 H 1 1.475 0.000 . 1 . . . . . . . . 5754 1 666 . 1 1 85 85 ALA CB C 13 15.68 0.000 . 1 . . . . . . . . 5754 1 667 . 1 1 85 85 ALA C C 13 175.548 0.000 . 1 . . . . . . . . 5754 1 668 . 1 1 86 86 ARG N N 15 116.586 0.116 . 1 . . . . . . . . 5754 1 669 . 1 1 86 86 ARG H H 1 8.569 0.003 . 1 . . . . . . . . 5754 1 670 . 1 1 86 86 ARG CA C 13 54.104 0.000 . 1 . . . . . . . . 5754 1 671 . 1 1 86 86 ARG HA H 1 4.398 0.000 . 1 . . . . . . . . 5754 1 672 . 1 1 86 86 ARG CB C 13 29.703 0.000 . 1 . . . . . . . . 5754 1 673 . 1 1 86 86 ARG HB2 H 1 1.857 0.000 . 1 . . . . . . . . 5754 1 674 . 1 1 86 86 ARG HG2 H 1 1.585 0.000 . 1 . . . . . . . . 5754 1 675 . 1 1 86 86 ARG C C 13 173.395 0.000 . 1 . . . . . . . . 5754 1 676 . 1 1 87 87 GLN N N 15 119.361 0.045 . 1 . . . . . . . . 5754 1 677 . 1 1 87 87 GLN H H 1 8.540 0.002 . 1 . . . . . . . . 5754 1 678 . 1 1 87 87 GLN CA C 13 52.652 0.000 . 1 . . . . . . . . 5754 1 679 . 1 1 87 87 GLN HA H 1 4.410 0.000 . 1 . . . . . . . . 5754 1 680 . 1 1 87 87 GLN CB C 13 29.072 0.000 . 1 . . . . . . . . 5754 1 681 . 1 1 87 87 GLN HB2 H 1 1.366 0.000 . 1 . . . . . . . . 5754 1 682 . 1 1 87 87 GLN HG2 H 1 1.637 0.000 . 1 . . . . . . . . 5754 1 683 . 1 1 87 87 GLN C C 13 170.553 0.000 . 1 . . . . . . . . 5754 1 684 . 1 1 88 88 VAL N N 15 121.106 0.004 . 1 . . . . . . . . 5754 1 685 . 1 1 88 88 VAL H H 1 8.142 0.000 . 1 . . . . . . . . 5754 1 686 . 1 1 88 88 VAL CA C 13 59.203 0.000 . 1 . . . . . . . . 5754 1 687 . 1 1 88 88 VAL HA H 1 4.360 0.000 . 1 . . . . . . . . 5754 1 688 . 1 1 88 88 VAL CB C 13 29.64 0.000 . 1 . . . . . . . . 5754 1 689 . 1 1 88 88 VAL HB H 1 1.690 0.000 . 1 . . . . . . . . 5754 1 690 . 1 1 88 88 VAL HG11 H 1 0.709 0.000 . 1 . . . . . . . . 5754 1 691 . 1 1 88 88 VAL HG12 H 1 0.709 0.000 . 1 . . . . . . . . 5754 1 692 . 1 1 88 88 VAL HG13 H 1 0.709 0.000 . 1 . . . . . . . . 5754 1 693 . 1 1 88 88 VAL C C 13 171.851 0.000 . 1 . . . . . . . . 5754 1 694 . 1 1 89 89 TRP N N 15 126.988 0.366 . 1 . . . . . . . . 5754 1 695 . 1 1 89 89 TRP H H 1 8.370 0.005 . 1 . . . . . . . . 5754 1 696 . 1 1 89 89 TRP CA C 13 52.958 0.000 . 1 . . . . . . . . 5754 1 697 . 1 1 89 89 TRP HA H 1 4.933 0.000 . 1 . . . . . . . . 5754 1 698 . 1 1 89 89 TRP CB C 13 28.945 0.000 . 1 . . . . . . . . 5754 1 699 . 1 1 89 89 TRP HB2 H 1 2.209 0.000 . 1 . . . . . . . . 5754 1 700 . 1 1 89 89 TRP HB3 H 1 1.199 0.000 . 1 . . . . . . . . 5754 1 701 . 1 1 89 89 TRP C C 13 173.118 0.000 . 1 . . . . . . . . 5754 1 702 . 1 1 90 90 GLY N N 15 106.082 0.410 . 1 . . . . . . . . 5754 1 703 . 1 1 90 90 GLY H H 1 8.859 0.003 . 1 . . . . . . . . 5754 1 704 . 1 1 90 90 GLY CA C 13 41.644 0.000 . 1 . . . . . . . . 5754 1 705 . 1 1 90 90 GLY HA2 H 1 4.686 0.000 . 1 . . . . . . . . 5754 1 706 . 1 1 90 90 GLY HA3 H 1 2.777 0.000 . 1 . . . . . . . . 5754 1 707 . 1 1 90 90 GLY C C 13 170.197 0.000 . 1 . . . . . . . . 5754 1 708 . 1 1 91 91 LEU N N 15 121.346 0.029 . 1 . . . . . . . . 5754 1 709 . 1 1 91 91 LEU H H 1 8.416 0.000 . 1 . . . . . . . . 5754 1 710 . 1 1 91 91 LEU CA C 13 49.9 0.000 . 1 . . . . . . . . 5754 1 711 . 1 1 91 91 LEU HA H 1 3.732 0.000 . 1 . . . . . . . . 5754 1 712 . 1 1 91 91 LEU CB C 13 42.021 0.000 . 1 . . . . . . . . 5754 1 713 . 1 1 91 91 LEU HB2 H 1 1.049 0.000 . 1 . . . . . . . . 5754 1 714 . 1 1 91 91 LEU HD11 H 1 -0.362 0.000 . 1 . . . . . . . . 5754 1 715 . 1 1 91 91 LEU HD12 H 1 -0.362 0.000 . 1 . . . . . . . . 5754 1 716 . 1 1 91 91 LEU HD13 H 1 -0.362 0.000 . 1 . . . . . . . . 5754 1 717 . 1 1 91 91 LEU C C 13 170.175 0.000 . 1 . . . . . . . . 5754 1 718 . 1 1 92 92 ASN N N 15 119.373 0.150 . 1 . . . . . . . . 5754 1 719 . 1 1 92 92 ASN H H 1 8.005 0.003 . 1 . . . . . . . . 5754 1 720 . 1 1 92 92 ASN CA C 13 48.465 0.000 . 1 . . . . . . . . 5754 1 721 . 1 1 92 92 ASN HA H 1 5.336 0.000 . 1 . . . . . . . . 5754 1 722 . 1 1 92 92 ASN CB C 13 37.157 0.000 . 1 . . . . . . . . 5754 1 723 . 1 1 92 92 ASN HB2 H 1 2.780 0.000 . 1 . . . . . . . . 5754 1 724 . 1 1 92 92 ASN HB3 H 1 2.137 0.000 . 1 . . . . . . . . 5754 1 725 . 1 1 92 92 ASN C C 13 173.28 0.000 . 1 . . . . . . . . 5754 1 726 . 1 1 93 93 PHE N N 15 123.968 0.283 . 1 . . . . . . . . 5754 1 727 . 1 1 93 93 PHE H H 1 8.957 0.003 . 1 . . . . . . . . 5754 1 728 . 1 1 93 93 PHE CA C 13 57.056 0.000 . 1 . . . . . . . . 5754 1 729 . 1 1 93 93 PHE HA H 1 4.451 0.000 . 1 . . . . . . . . 5754 1 730 . 1 1 93 93 PHE CB C 13 39.179 0.000 . 1 . . . . . . . . 5754 1 731 . 1 1 93 93 PHE HB2 H 1 3.208 0.000 . 1 . . . . . . . . 5754 1 732 . 1 1 93 93 PHE HB3 H 1 2.759 0.000 . 1 . . . . . . . . 5754 1 733 . 1 1 93 93 PHE C C 13 174.492 0.000 . 1 . . . . . . . . 5754 1 734 . 1 1 94 94 GLY N N 15 106.859 0.291 . 1 . . . . . . . . 5754 1 735 . 1 1 94 94 GLY H H 1 9.110 0.000 . 1 . . . . . . . . 5754 1 736 . 1 1 94 94 GLY CA C 13 43.727 0.000 . 1 . . . . . . . . 5754 1 737 . 1 1 94 94 GLY HA2 H 1 4.003 0.000 . 1 . . . . . . . . 5754 1 738 . 1 1 94 94 GLY HA3 H 1 3.493 0.000 . 1 . . . . . . . . 5754 1 739 . 1 1 94 94 GLY C C 13 172.123 0.000 . 1 . . . . . . . . 5754 1 740 . 1 1 95 95 SER N N 15 109.973 0.241 . 1 . . . . . . . . 5754 1 741 . 1 1 95 95 SER H H 1 7.559 0.000 . 1 . . . . . . . . 5754 1 742 . 1 1 95 95 SER CA C 13 54.563 0.000 . 1 . . . . . . . . 5754 1 743 . 1 1 95 95 SER HA H 1 4.195 0.000 . 1 . . . . . . . . 5754 1 744 . 1 1 95 95 SER CB C 13 63.878 0.000 . 1 . . . . . . . . 5754 1 745 . 1 1 95 95 SER HB2 H 1 4.054 0.000 . 1 . . . . . . . . 5754 1 746 . 1 1 95 95 SER C C 13 172.146 0.000 . 1 . . . . . . . . 5754 1 747 . 1 1 96 96 LYS N N 15 122.524 0.098 . 1 . . . . . . . . 5754 1 748 . 1 1 96 96 LYS H H 1 9.063 0.000 . 1 . . . . . . . . 5754 1 749 . 1 1 96 96 LYS CA C 13 56.424 0.000 . 1 . . . . . . . . 5754 1 750 . 1 1 96 96 LYS HA H 1 4.083 0.000 . 1 . . . . . . . . 5754 1 751 . 1 1 96 96 LYS CB C 13 29.64 0.000 . 1 . . . . . . . . 5754 1 752 . 1 1 96 96 LYS HB2 H 1 1.786 0.000 . 1 . . . . . . . . 5754 1 753 . 1 1 96 96 LYS C C 13 176.592 0.000 . 1 . . . . . . . . 5754 1 754 . 1 1 97 97 GLU N N 15 121.695 0.098 . 1 . . . . . . . . 5754 1 755 . 1 1 97 97 GLU H H 1 8.794 0.003 . 1 . . . . . . . . 5754 1 756 . 1 1 97 97 GLU CA C 13 57.927 0.000 . 1 . . . . . . . . 5754 1 757 . 1 1 97 97 GLU HA H 1 4.023 0.000 . 1 . . . . . . . . 5754 1 758 . 1 1 97 97 GLU CB C 13 25.85 0.000 . 1 . . . . . . . . 5754 1 759 . 1 1 97 97 GLU HB2 H 1 1.900 0.000 . 1 . . . . . . . . 5754 1 760 . 1 1 97 97 GLU HG2 H 1 2.067 0.000 . 1 . . . . . . . . 5754 1 761 . 1 1 97 97 GLU C C 13 176.583 0.000 . 1 . . . . . . . . 5754 1 762 . 1 1 98 98 ASP N N 15 120.377 0.191 . 1 . . . . . . . . 5754 1 763 . 1 1 98 98 ASP H H 1 7.814 0.003 . 1 . . . . . . . . 5754 1 764 . 1 1 98 98 ASP CA C 13 54.945 0.000 . 1 . . . . . . . . 5754 1 765 . 1 1 98 98 ASP HA H 1 4.349 0.000 . 1 . . . . . . . . 5754 1 766 . 1 1 98 98 ASP CB C 13 39.495 0.000 . 1 . . . . . . . . 5754 1 767 . 1 1 98 98 ASP HB2 H 1 2.917 0.000 . 1 . . . . . . . . 5754 1 768 . 1 1 98 98 ASP C C 13 175.762 0.000 . 1 . . . . . . . . 5754 1 769 . 1 1 99 99 ALA N N 15 122.249 0.226 . 1 . . . . . . . . 5754 1 770 . 1 1 99 99 ALA H H 1 7.122 0.000 . 1 . . . . . . . . 5754 1 771 . 1 1 99 99 ALA CA C 13 51.199 0.000 . 1 . . . . . . . . 5754 1 772 . 1 1 99 99 ALA HA H 1 4.125 0.000 . 1 . . . . . . . . 5754 1 773 . 1 1 99 99 ALA HB1 H 1 0.945 0.000 . 1 . . . . . . . . 5754 1 774 . 1 1 99 99 ALA HB2 H 1 0.945 0.000 . 1 . . . . . . . . 5754 1 775 . 1 1 99 99 ALA HB3 H 1 0.945 0.000 . 1 . . . . . . . . 5754 1 776 . 1 1 99 99 ALA CB C 13 17.259 0.000 . 1 . . . . . . . . 5754 1 777 . 1 1 99 99 ALA C C 13 176.041 0.000 . 1 . . . . . . . . 5754 1 778 . 1 1 100 100 ALA N N 15 119.182 0.074 . 1 . . . . . . . . 5754 1 779 . 1 1 100 100 ALA H H 1 7.938 0.007 . 1 . . . . . . . . 5754 1 780 . 1 1 100 100 ALA CA C 13 52.255 0.000 . 1 . . . . . . . . 5754 1 781 . 1 1 100 100 ALA HA H 1 4.039 0.000 . 1 . . . . . . . . 5754 1 782 . 1 1 100 100 ALA HB1 H 1 1.404 0.000 . 1 . . . . . . . . 5754 1 783 . 1 1 100 100 ALA HB2 H 1 1.404 0.000 . 1 . . . . . . . . 5754 1 784 . 1 1 100 100 ALA HB3 H 1 1.404 0.000 . 1 . . . . . . . . 5754 1 785 . 1 1 100 100 ALA CB C 13 15.554 0.000 . 1 . . . . . . . . 5754 1 786 . 1 1 100 100 ALA C C 13 179.245 0.000 . 1 . . . . . . . . 5754 1 787 . 1 1 101 101 GLN N N 15 117.146 0.074 . 1 . . . . . . . . 5754 1 788 . 1 1 101 101 GLN H H 1 7.940 0.001 . 1 . . . . . . . . 5754 1 789 . 1 1 101 101 GLN CA C 13 55.71 0.000 . 1 . . . . . . . . 5754 1 790 . 1 1 101 101 GLN HA H 1 3.972 0.000 . 1 . . . . . . . . 5754 1 791 . 1 1 101 101 GLN CB C 13 25.85 0.000 . 1 . . . . . . . . 5754 1 792 . 1 1 101 101 GLN HB2 H 1 2.111 0.000 . 1 . . . . . . . . 5754 1 793 . 1 1 101 101 GLN HG2 H 1 2.453 0.000 . 1 . . . . . . . . 5754 1 794 . 1 1 101 101 GLN C C 13 176.254 0.000 . 1 . . . . . . . . 5754 1 795 . 1 1 102 102 PHE N N 15 122.346 0.196 . 1 . . . . . . . . 5754 1 796 . 1 1 102 102 PHE H H 1 7.717 0.003 . 1 . . . . . . . . 5754 1 797 . 1 1 102 102 PHE CA C 13 59.303 0.000 . 1 . . . . . . . . 5754 1 798 . 1 1 102 102 PHE HA H 1 4.105 0.000 . 1 . . . . . . . . 5754 1 799 . 1 1 102 102 PHE CB C 13 37.663 0.000 . 1 . . . . . . . . 5754 1 800 . 1 1 102 102 PHE HB2 H 1 3.048 0.000 . 1 . . . . . . . . 5754 1 801 . 1 1 102 102 PHE HB3 H 1 2.899 0.000 . 1 . . . . . . . . 5754 1 802 . 1 1 102 102 PHE C C 13 174.792 0.000 . 1 . . . . . . . . 5754 1 803 . 1 1 103 103 ALA N N 15 119.806 0.155 . 1 . . . . . . . . 5754 1 804 . 1 1 103 103 ALA H H 1 8.589 0.003 . 1 . . . . . . . . 5754 1 805 . 1 1 103 103 ALA CA C 13 52.575 0.000 . 1 . . . . . . . . 5754 1 806 . 1 1 103 103 ALA HA H 1 3.748 0.000 . 1 . . . . . . . . 5754 1 807 . 1 1 103 103 ALA HB1 H 1 1.506 0.000 . 1 . . . . . . . . 5754 1 808 . 1 1 103 103 ALA HB2 H 1 1.506 0.000 . 1 . . . . . . . . 5754 1 809 . 1 1 103 103 ALA HB3 H 1 1.506 0.000 . 1 . . . . . . . . 5754 1 810 . 1 1 103 103 ALA CB C 13 15.617 0.000 . 1 . . . . . . . . 5754 1 811 . 1 1 103 103 ALA C C 13 178.095 0.000 . 1 . . . . . . . . 5754 1 812 . 1 1 104 104 ALA N N 15 119.638 0.009 . 1 . . . . . . . . 5754 1 813 . 1 1 104 104 ALA H H 1 7.666 0.001 . 1 . . . . . . . . 5754 1 814 . 1 1 104 104 ALA CA C 13 52.117 0.000 . 1 . . . . . . . . 5754 1 815 . 1 1 104 104 ALA HA H 1 4.004 0.000 . 1 . . . . . . . . 5754 1 816 . 1 1 104 104 ALA HB1 H 1 1.322 0.000 . 1 . . . . . . . . 5754 1 817 . 1 1 104 104 ALA HB2 H 1 1.322 0.000 . 1 . . . . . . . . 5754 1 818 . 1 1 104 104 ALA HB3 H 1 1.322 0.000 . 1 . . . . . . . . 5754 1 819 . 1 1 104 104 ALA CB C 13 15.111 0.000 . 1 . . . . . . . . 5754 1 820 . 1 1 104 104 ALA C C 13 178.266 0.000 . 1 . . . . . . . . 5754 1 821 . 1 1 105 105 GLY N N 15 108.488 0.226 . 1 . . . . . . . . 5754 1 822 . 1 1 105 105 GLY H H 1 7.563 0.001 . 1 . . . . . . . . 5754 1 823 . 1 1 105 105 GLY CA C 13 44.396 0.000 . 1 . . . . . . . . 5754 1 824 . 1 1 105 105 GLY HA2 H 1 3.494 0.000 . 1 . . . . . . . . 5754 1 825 . 1 1 105 105 GLY HA3 H 1 3.363 0.000 . 1 . . . . . . . . 5754 1 826 . 1 1 105 105 GLY C C 13 175.155 0.000 . 1 . . . . . . . . 5754 1 827 . 1 1 106 106 MET N N 15 121.535 0.097 . 1 . . . . . . . . 5754 1 828 . 1 1 106 106 MET H H 1 8.064 0.001 . 1 . . . . . . . . 5754 1 829 . 1 1 106 106 MET CA C 13 53.897 0.000 . 1 . . . . . . . . 5754 1 830 . 1 1 106 106 MET HA H 1 3.544 0.000 . 1 . . . . . . . . 5754 1 831 . 1 1 106 106 MET CB C 13 27.24 0.000 . 1 . . . . . . . . 5754 1 832 . 1 1 106 106 MET HB2 H 1 1.243 0.000 . 1 . . . . . . . . 5754 1 833 . 1 1 106 106 MET HG2 H 1 0.928 0.000 . 1 . . . . . . . . 5754 1 834 . 1 1 106 106 MET C C 13 175.17 0.000 . 1 . . . . . . . . 5754 1 835 . 1 1 107 107 ALA N N 15 119.688 0.106 . 1 . . . . . . . . 5754 1 836 . 1 1 107 107 ALA H H 1 7.885 0.002 . 1 . . . . . . . . 5754 1 837 . 1 1 107 107 ALA CA C 13 52.551 0.000 . 1 . . . . . . . . 5754 1 838 . 1 1 107 107 ALA HA H 1 3.758 0.000 . 1 . . . . . . . . 5754 1 839 . 1 1 107 107 ALA HB1 H 1 1.261 0.000 . 1 . . . . . . . . 5754 1 840 . 1 1 107 107 ALA HB2 H 1 1.261 0.000 . 1 . . . . . . . . 5754 1 841 . 1 1 107 107 ALA HB3 H 1 1.261 0.000 . 1 . . . . . . . . 5754 1 842 . 1 1 107 107 ALA CB C 13 14.796 0.000 . 1 . . . . . . . . 5754 1 843 . 1 1 107 107 ALA C C 13 178.276 0.000 . 1 . . . . . . . . 5754 1 844 . 1 1 108 108 SER N N 15 113.882 0.105 . 1 . . . . . . . . 5754 1 845 . 1 1 108 108 SER H H 1 7.570 0.000 . 1 . . . . . . . . 5754 1 846 . 1 1 108 108 SER CA C 13 58.508 0.000 . 1 . . . . . . . . 5754 1 847 . 1 1 108 108 SER HA H 1 3.723 0.000 . 1 . . . . . . . . 5754 1 848 . 1 1 108 108 SER CB C 13 59.961 0.000 . 1 . . . . . . . . 5754 1 849 . 1 1 108 108 SER C C 13 175.424 0.000 . 1 . . . . . . . . 5754 1 850 . 1 1 109 109 ALA N N 15 125.865 0.467 . 1 . . . . . . . . 5754 1 851 . 1 1 109 109 ALA H H 1 7.525 0.002 . 1 . . . . . . . . 5754 1 852 . 1 1 109 109 ALA CA C 13 51.582 0.000 . 1 . . . . . . . . 5754 1 853 . 1 1 109 109 ALA HA H 1 2.593 0.000 . 1 . . . . . . . . 5754 1 854 . 1 1 109 109 ALA HB1 H 1 0.323 0.000 . 1 . . . . . . . . 5754 1 855 . 1 1 109 109 ALA HB2 H 1 0.323 0.000 . 1 . . . . . . . . 5754 1 856 . 1 1 109 109 ALA HB3 H 1 0.323 0.000 . 1 . . . . . . . . 5754 1 857 . 1 1 109 109 ALA CB C 13 14.922 0.000 . 1 . . . . . . . . 5754 1 858 . 1 1 109 109 ALA C C 13 175.433 0.000 . 1 . . . . . . . . 5754 1 859 . 1 1 110 110 LEU N N 15 115.022 0.116 . 1 . . . . . . . . 5754 1 860 . 1 1 110 110 LEU H H 1 7.961 0.003 . 1 . . . . . . . . 5754 1 861 . 1 1 110 110 LEU CA C 13 55.098 0.000 . 1 . . . . . . . . 5754 1 862 . 1 1 110 110 LEU HA H 1 3.575 0.000 . 1 . . . . . . . . 5754 1 863 . 1 1 110 110 LEU CB C 13 38.042 0.000 . 1 . . . . . . . . 5754 1 864 . 1 1 110 110 LEU HB2 H 1 1.576 0.000 . 1 . . . . . . . . 5754 1 865 . 1 1 110 110 LEU HB3 H 1 1.252 0.000 . 1 . . . . . . . . 5754 1 866 . 1 1 110 110 LEU C C 13 177.848 0.000 . 1 . . . . . . . . 5754 1 867 . 1 1 111 111 GLU N N 15 118.327 0.074 . 1 . . . . . . . . 5754 1 868 . 1 1 111 111 GLU H H 1 7.811 0.000 . 1 . . . . . . . . 5754 1 869 . 1 1 111 111 GLU CA C 13 56.398 0.000 . 1 . . . . . . . . 5754 1 870 . 1 1 111 111 GLU HA H 1 3.881 0.000 . 1 . . . . . . . . 5754 1 871 . 1 1 111 111 GLU CB C 13 27.05 0.000 . 1 . . . . . . . . 5754 1 872 . 1 1 111 111 GLU HB2 H 1 1.927 0.000 . 1 . . . . . . . . 5754 1 873 . 1 1 111 111 GLU HG2 H 1 2.172 0.000 . 1 . . . . . . . . 5754 1 874 . 1 1 111 111 GLU C C 13 176.912 0.000 . 1 . . . . . . . . 5754 1 875 . 1 1 112 112 ALA N N 15 121.885 0.214 . 1 . . . . . . . . 5754 1 876 . 1 1 112 112 ALA H H 1 7.466 0.007 . 1 . . . . . . . . 5754 1 877 . 1 1 112 112 ALA CA C 13 52.002 0.000 . 1 . . . . . . . . 5754 1 878 . 1 1 112 112 ALA HA H 1 4.074 0.000 . 1 . . . . . . . . 5754 1 879 . 1 1 112 112 ALA HB1 H 1 1.515 0.000 . 1 . . . . . . . . 5754 1 880 . 1 1 112 112 ALA HB2 H 1 1.515 0.000 . 1 . . . . . . . . 5754 1 881 . 1 1 112 112 ALA HB3 H 1 1.515 0.000 . 1 . . . . . . . . 5754 1 882 . 1 1 112 112 ALA CB C 13 16.059 0.000 . 1 . . . . . . . . 5754 1 883 . 1 1 112 112 ALA C C 13 178.111 0.000 . 1 . . . . . . . . 5754 1 884 . 1 1 113 113 LEU N N 15 117.049 0.074 . 1 . . . . . . . . 5754 1 885 . 1 1 113 113 LEU H H 1 7.732 0.006 . 1 . . . . . . . . 5754 1 886 . 1 1 113 113 LEU CA C 13 53.722 0.000 . 1 . . . . . . . . 5754 1 887 . 1 1 113 113 LEU HA H 1 4.156 0.000 . 1 . . . . . . . . 5754 1 888 . 1 1 113 113 LEU CB C 13 40.632 0.000 . 1 . . . . . . . . 5754 1 889 . 1 1 113 113 LEU HB2 H 1 1.751 0.000 . 1 . . . . . . . . 5754 1 890 . 1 1 113 113 LEU HB3 H 1 1.322 0.000 . 1 . . . . . . . . 5754 1 891 . 1 1 113 113 LEU C C 13 175.646 0.000 . 1 . . . . . . . . 5754 1 892 . 1 1 114 114 GLU N N 15 118.131 0.026 . 1 . . . . . . . . 5754 1 893 . 1 1 114 114 GLU H H 1 7.544 0.003 . 1 . . . . . . . . 5754 1 894 . 1 1 114 114 GLU CA C 13 54.402 0.000 . 1 . . . . . . . . 5754 1 895 . 1 1 114 114 GLU HA H 1 4.115 0.000 . 1 . . . . . . . . 5754 1 896 . 1 1 114 114 GLU CB C 13 27.493 0.000 . 1 . . . . . . . . 5754 1 897 . 1 1 114 114 GLU HB2 H 1 2.058 0.000 . 1 . . . . . . . . 5754 1 898 . 1 1 114 114 GLU HG2 H 1 2.321 0.000 . 1 . . . . . . . . 5754 1 899 . 1 1 114 114 GLU C C 13 174.034 0.000 . 1 . . . . . . . . 5754 1 900 . 1 1 115 115 GLY N N 15 113.010 0.123 . 1 . . . . . . . . 5754 1 901 . 1 1 115 115 GLY H H 1 7.545 0.000 . 1 . . . . . . . . 5754 1 902 . 1 1 115 115 GLY CA C 13 43.727 0.000 . 1 . . . . . . . . 5754 1 stop_ save_