data_5030 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5030 _Entry.Title ; 1H, 13C and 15N Chemical Shift Assignment of the Honeybee Odorant-binding Protein ASP2 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-05-23 _Entry.Accession_date 2001-05-23 _Entry.Last_release_date 2001-05-23 _Entry.Original_release_date 2001-05-23 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.0.16 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Source_data_format . _Entry.Source_data_format_version . _Entry.Generated_software_name . _Entry.Generated_software_version . _Entry.Generated_software_ID . _Entry.Generated_software_label . _Entry.Generated_date . _Entry.DOI . _Entry.UUID . _Entry.Related_coordinate_file_name . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.ORCID _Entry_author.Entry_ID 1 Ewen Lescop . . . . 5030 2 Loic Briand . . . . 5030 3 Jean-Claude Pernollet . . . . 5030 4 Carine 'van Heijenoort' . . . . 5030 5 Eric Guittet . . . . 5030 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5030 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 361 5030 '15N chemical shifts' 119 5030 '1H chemical shifts' 466 5030 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 . . 2002-05-30 . original BMRB . 5030 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5030 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 21584505 _Citation.DOI . _Citation.PubMed_ID 11727984 _Citation.Full_citation . _Citation.Title ; Letter to the Editor: 1H, 13C and 15N Chemical Shift Assignment of the Honeybee Odorant-binding Protein ASP2 ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 21 _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 181 _Citation.Page_last 182 _Citation.Year 2001 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Ewen Lescop . . . . 5030 1 2 Loic Briand . . . . 5030 1 3 Jean-Claude Pernollet . . . . 5030 1 4 Carine 'van Heijenoort' . . . . 5030 1 5 Eric Guittet . . . . 5030 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'apis mellifera L.' 5030 1 insect 5030 1 'odorant binding protein' 5030 1 olfaction 5030 1 'resonances assignments' 5030 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5030 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11168415 _Citation.Full_citation ; Briand L, Nespoulous C, Huet JC, Takahashi M, Pernollet JC. Ligand binding and physico-chemical properties of ASP2, a recombinant odorant-binding protein from honeybee (Apis mellifera L.). Eur J Biochem. 2001 Feb;268(3):752-60. ; _Citation.Title ; Ligand binding and physico-chemical properties of ASP2, a recombinant odorant-binding protein from honeybee (Apis mellifera L.). ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full 'European journal of biochemistry / FEBS' _Citation.Journal_volume 268 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0014-2956 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 752 _Citation.Page_last 760 _Citation.Year 2001 _Citation.Details ; In insects, the transport of airborne, hydrophobic odorants and pheromones through the sensillum lymph is generally thought to be accomplished by odorant-binding proteins (OBPs). We report the structural and functional properties of a honeybee OBP called ASP2, heterologously expressed by the yeast Pichia pastoris. ASP2 disulfide bonds were assigned after classic trypsinolysis followed by ion-spray mass spectrometry combined with microsequencing. The pairing [Cys(I)-Cys(III), Cys(II)-Cys(V), Cys(IV)-Cys(VI)] was found to be identical to that of Bombyx mori OBP, suggesting that this pattern occurs commonly throughout the highly divergent insect OBPs. CD measurements revealed that ASP2 is mainly constituted of alpha helices, like other insect OBPs, but different from lipocalin-like vertebrate OBPs. Gel filtration analysis showed that ASP2 is homodimeric at neutral pH, but monomerizes upon acidification or addition of a chaotropic agent. A general volatile-odorant binding assay allowed us to examine the uptake of some odorants and pheromones by ASP2. Recombinant ASP2 bound all tested molecules, except beta-ionone, which could not interact with it at all. The affinity constants of ASP2 for these ligands, determined at neutral pH by isothermal titration calorimetry, are in the micromolar range, as observed for vertebrate OBP. These results suggest that odorants occupy three binding sites per dimer, probably one in the core of each monomer and another whose location and biological role are questionable. At acidic pH, no binding was observed, in correlation with monomerization and a local conformational change supported by CD experiments. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 L. Briand L. . . . 5030 2 2 C. Nespoulous C. . . . 5030 2 3 'J. C.' Huet J. C. . . 5030 2 4 M. Takahashi M. . . . 5030 2 5 'J. C.' Pernollet J. C. . . 5030 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5030 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10092496 _Citation.Full_citation ; Briand L, Perez V, Huet JC, Danty E, Masson C, Pernollet JC. Optimization of the production of a honeybee odorant-binding protein by Pichia pastoris. Protein Expr Purif. 1999 Apr;15(3):362-9. ; _Citation.Title ; Optimization of the production of a honeybee odorant-binding protein by Pichia pastoris. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Expr. Purif.' _Citation.Journal_name_full 'Protein expression and purification' _Citation.Journal_volume 15 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1046-5928 _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 362 _Citation.Page_last 369 _Citation.Year 1999 _Citation.Details ; A honeybee putative general odorant-binding protein ASP2 has been expressed in the methylotrophic yeast Pichia pastoris. It was secreted into the buffered minimal medium using either the alpha-factor preprosequence with and without the Glu-Ala-Glu-Ala spacer peptide of Saccharomyces cerevisiae or its native signal peptide. Whereas ASP2 secreted using the alpha-factor preprosequence with the spacer peptide showed N-terminal heterogeneity, the recombinant protein using the two other secretion peptides was correctly processed. Mass spectrometry showed that the protein secreted using the natural peptide sequence had a mass of 13,695.1 Da, in perfect agreement with the measured molecular mass of the native protein. These data showed a native-like processing and the three disulfide bridges formation confirmed by sulfhydryl titration analysis. After dialysis, the recombinant protein was purified by one-step anion-exchange chromatography in a highly pure form. The final expression yield after 7-day fermentation was approximately 150 mg/liter. To our knowledge, this is the first report of the use of a natural insect leader sequence for secretion with correct processing in P. pastoris. The overproduction of recombinant ASP2 should allow ligand binding and mutational analysis to understand the relationships between structure and biological function of the protein. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 L. Briand L. . . . 5030 3 2 V. Perez V. . . . 5030 3 3 'J. C.' Huet J. C. . . 5030 3 4 E. Danty E. . . . 5030 3 5 C. Masson C. . . . 5030 3 6 'J. C.' Pernollet J. C. . . 5030 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 5030 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10460253 _Citation.Full_citation ; Danty E, Briand L, Michard-Vanhee C, Perez V, Arnold G, Gaudemer O, Huet D, Huet JC, Ouali C, Masson C, Pernollet JC. Cloning and expression of a queen pheromone-binding protein in the honeybee: an olfactory-specific, developmentally regulated protein. J Neurosci. 1999 Sep 1;19(17):7468-75. ; _Citation.Title ; Cloning and expression of a queen pheromone-binding protein in the honeybee: an olfactory-specific, developmentally regulated protein. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Neurosci.' _Citation.Journal_name_full 'The Journal of neuroscience : the official journal of the Society for Neuroscience' _Citation.Journal_volume 19 _Citation.Journal_issue 17 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1529-2401 _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 7468 _Citation.Page_last 7475 _Citation.Year 1999 _Citation.Details ; Odorant-binding proteins (OBPs) are small abundant extracellular proteins thought to participate in perireceptor events of odor-pheromone detection by carrying, deactivating, and/or selecting odor stimuli. The honeybee queen pheromone is known to play a crucial role in colony organization, in addition to drone sex attraction. We identified, for the first time in a social insect, a binding protein called antennal-specific protein 1 (ASP1), which binds at least one of the major queen pheromone components. ASP1 was characterized by cDNA cloning, expression in Pichia pastoris, and pheromone binding. In situ hybridization showed that it is specifically expressed in the auxiliary cell layer of the antennal olfactory sensilla. The ASP1 sequence revealed it as a divergent member of the insect OBP family. The recombinant protein presented the exact characteristics of the native protein, as shown by mass spectrometry, and N-terminal sequencing and exclusion-diffusion chromatography showed that recombinant ASP1 is dimeric. ASP1 interacts with queen pheromone major components, opposite to another putative honeybee OBP, called ASP2. ASP1 biosynthetic accumulation, followed by nondenaturing electrophoresis during development, starts at day 1 before emergence, in concomitance with the functional maturation of olfactory neurons. The isobar ASP1b isoform appears simultaneously to ASP1a in workers, but only at approximately 2 weeks after emergence in drones. Comparison of in vivo and heterologous expressions suggests that the difference between ASP1 isoforms might be because of dimerization, which might play a physiological role in relation with mate attraction. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 E. Danty E. . . . 5030 4 2 L. Briand L. . . . 5030 4 3 C. Michard-Vanhee C. . . . 5030 4 4 V. Perez V. . . . 5030 4 5 G. Arnold G. . . . 5030 4 6 O. Gaudemer O. . . . 5030 4 7 D. Huet D. . . . 5030 4 8 'J. C.' Huet J. C. . . 5030 4 9 C. Ouali C. . . . 5030 4 10 C. Masson C. . . . 5030 4 11 'J. C.' Pernollet J. C. . . 5030 4 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_ASP2 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_ASP2 _Assembly.Entry_ID 5030 _Assembly.ID 1 _Assembly.Name 'Honeybee antennal specific Protein 2' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all disulfide bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomeric 5030 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 ASP2 1 $ASP2 . . . native . . . . . 5030 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_asym_ID_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_asym_ID_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 21 21 SG . 1 . 1 CYS 53 53 SG . . . . . . . . . . . . 5030 1 2 disulfide single . 1 . 1 CYS 49 49 SG . 1 . 1 CYS 107 107 SG . . . . . . . . . . . . 5030 1 3 disulfide single . 1 . 1 CYS 96 96 SG . 1 . 1 CYS 116 116 SG . . . . . . . . . . . . 5030 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID ASP2 abbreviation 5030 1 'Honeybee antennal specific Protein 2' system 5030 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'General Odorant-Binding Protein' 5030 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_ASP2 _Entity.Sf_category entity _Entity.Sf_framecode ASP2 _Entity.Entry_ID 5030 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name ASP2 _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 ; IDQDTVVAKYMEYLMPDIMP CADELHISEDIATNIQAAKN GADMSQLGCLKACVMKRIEM LKGTELYVEPVYKMIEVVHA GNADDIQLVKGIANECIENA KGETDECNIGNKYTDCYIEK LFS ; _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 123 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 13695 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID . no PDB 1TUJ . 'Solution Structure Of The Honey Bee General Odorant Binding Protein Asp2 In Complex With Trimethylsilyl-D4 Propionate' . . . . . 100.00 123 100.00 100.00 2.35e-65 . . . . 5030 1 . no GenBank AAD51945 . 'putative odorant-binding protein ASP2 [Apis mellifera]' . . . . . 100.00 142 100.00 100.00 7.06e-66 . . . . 5030 1 . no GenBank AAL60418 . 'odorant binding protein ASP2 [Apis mellifera]' . . . . . 100.00 142 100.00 100.00 7.06e-66 . . . . 5030 1 . no GenBank ABD97844 . 'odorant binding protein ASP2 [Apis cerana cerana]' . . . . . 100.00 142 98.37 99.19 1.61e-64 . . . . 5030 1 . no REF NP_001011591 . 'odorant binding protein ASP2 [Apis mellifera]' . . . . . 100.00 142 100.00 100.00 7.06e-66 . . . . 5030 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID ASP2 abbreviation 5030 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 . ILE . 5030 1 2 . ASP . 5030 1 3 . GLN . 5030 1 4 . ASP . 5030 1 5 . THR . 5030 1 6 . VAL . 5030 1 7 . VAL . 5030 1 8 . ALA . 5030 1 9 . LYS . 5030 1 10 . TYR . 5030 1 11 . MET . 5030 1 12 . GLU . 5030 1 13 . TYR . 5030 1 14 . LEU . 5030 1 15 . MET . 5030 1 16 . PRO . 5030 1 17 . ASP . 5030 1 18 . ILE . 5030 1 19 . MET . 5030 1 20 . PRO . 5030 1 21 . CYS . 5030 1 22 . ALA . 5030 1 23 . ASP . 5030 1 24 . GLU . 5030 1 25 . LEU . 5030 1 26 . HIS . 5030 1 27 . ILE . 5030 1 28 . SER . 5030 1 29 . GLU . 5030 1 30 . ASP . 5030 1 31 . ILE . 5030 1 32 . ALA . 5030 1 33 . THR . 5030 1 34 . ASN . 5030 1 35 . ILE . 5030 1 36 . GLN . 5030 1 37 . ALA . 5030 1 38 . ALA . 5030 1 39 . LYS . 5030 1 40 . ASN . 5030 1 41 . GLY . 5030 1 42 . ALA . 5030 1 43 . ASP . 5030 1 44 . MET . 5030 1 45 . SER . 5030 1 46 . GLN . 5030 1 47 . LEU . 5030 1 48 . GLY . 5030 1 49 . CYS . 5030 1 50 . LEU . 5030 1 51 . LYS . 5030 1 52 . ALA . 5030 1 53 . CYS . 5030 1 54 . VAL . 5030 1 55 . MET . 5030 1 56 . LYS . 5030 1 57 . ARG . 5030 1 58 . ILE . 5030 1 59 . GLU . 5030 1 60 . MET . 5030 1 61 . LEU . 5030 1 62 . LYS . 5030 1 63 . GLY . 5030 1 64 . THR . 5030 1 65 . GLU . 5030 1 66 . LEU . 5030 1 67 . TYR . 5030 1 68 . VAL . 5030 1 69 . GLU . 5030 1 70 . PRO . 5030 1 71 . VAL . 5030 1 72 . TYR . 5030 1 73 . LYS . 5030 1 74 . MET . 5030 1 75 . ILE . 5030 1 76 . GLU . 5030 1 77 . VAL . 5030 1 78 . VAL . 5030 1 79 . HIS . 5030 1 80 . ALA . 5030 1 81 . GLY . 5030 1 82 . ASN . 5030 1 83 . ALA . 5030 1 84 . ASP . 5030 1 85 . ASP . 5030 1 86 . ILE . 5030 1 87 . GLN . 5030 1 88 . LEU . 5030 1 89 . VAL . 5030 1 90 . LYS . 5030 1 91 . GLY . 5030 1 92 . ILE . 5030 1 93 . ALA . 5030 1 94 . ASN . 5030 1 95 . GLU . 5030 1 96 . CYS . 5030 1 97 . ILE . 5030 1 98 . GLU . 5030 1 99 . ASN . 5030 1 100 . ALA . 5030 1 101 . LYS . 5030 1 102 . GLY . 5030 1 103 . GLU . 5030 1 104 . THR . 5030 1 105 . ASP . 5030 1 106 . GLU . 5030 1 107 . CYS . 5030 1 108 . ASN . 5030 1 109 . ILE . 5030 1 110 . GLY . 5030 1 111 . ASN . 5030 1 112 . LYS . 5030 1 113 . TYR . 5030 1 114 . THR . 5030 1 115 . ASP . 5030 1 116 . CYS . 5030 1 117 . TYR . 5030 1 118 . ILE . 5030 1 119 . GLU . 5030 1 120 . LYS . 5030 1 121 . LEU . 5030 1 122 . PHE . 5030 1 123 . SER . 5030 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 . ILE 1 1 5030 1 . ASP 2 2 5030 1 . GLN 3 3 5030 1 . ASP 4 4 5030 1 . THR 5 5 5030 1 . VAL 6 6 5030 1 . VAL 7 7 5030 1 . ALA 8 8 5030 1 . LYS 9 9 5030 1 . TYR 10 10 5030 1 . MET 11 11 5030 1 . GLU 12 12 5030 1 . TYR 13 13 5030 1 . LEU 14 14 5030 1 . MET 15 15 5030 1 . PRO 16 16 5030 1 . ASP 17 17 5030 1 . ILE 18 18 5030 1 . MET 19 19 5030 1 . PRO 20 20 5030 1 . CYS 21 21 5030 1 . ALA 22 22 5030 1 . ASP 23 23 5030 1 . GLU 24 24 5030 1 . LEU 25 25 5030 1 . HIS 26 26 5030 1 . ILE 27 27 5030 1 . SER 28 28 5030 1 . GLU 29 29 5030 1 . ASP 30 30 5030 1 . ILE 31 31 5030 1 . ALA 32 32 5030 1 . THR 33 33 5030 1 . ASN 34 34 5030 1 . ILE 35 35 5030 1 . GLN 36 36 5030 1 . ALA 37 37 5030 1 . ALA 38 38 5030 1 . LYS 39 39 5030 1 . ASN 40 40 5030 1 . GLY 41 41 5030 1 . ALA 42 42 5030 1 . ASP 43 43 5030 1 . MET 44 44 5030 1 . SER 45 45 5030 1 . GLN 46 46 5030 1 . LEU 47 47 5030 1 . GLY 48 48 5030 1 . CYS 49 49 5030 1 . LEU 50 50 5030 1 . LYS 51 51 5030 1 . ALA 52 52 5030 1 . CYS 53 53 5030 1 . VAL 54 54 5030 1 . MET 55 55 5030 1 . LYS 56 56 5030 1 . ARG 57 57 5030 1 . ILE 58 58 5030 1 . GLU 59 59 5030 1 . MET 60 60 5030 1 . LEU 61 61 5030 1 . LYS 62 62 5030 1 . GLY 63 63 5030 1 . THR 64 64 5030 1 . GLU 65 65 5030 1 . LEU 66 66 5030 1 . TYR 67 67 5030 1 . VAL 68 68 5030 1 . GLU 69 69 5030 1 . PRO 70 70 5030 1 . VAL 71 71 5030 1 . TYR 72 72 5030 1 . LYS 73 73 5030 1 . MET 74 74 5030 1 . ILE 75 75 5030 1 . GLU 76 76 5030 1 . VAL 77 77 5030 1 . VAL 78 78 5030 1 . HIS 79 79 5030 1 . ALA 80 80 5030 1 . GLY 81 81 5030 1 . ASN 82 82 5030 1 . ALA 83 83 5030 1 . ASP 84 84 5030 1 . ASP 85 85 5030 1 . ILE 86 86 5030 1 . GLN 87 87 5030 1 . LEU 88 88 5030 1 . VAL 89 89 5030 1 . LYS 90 90 5030 1 . GLY 91 91 5030 1 . ILE 92 92 5030 1 . ALA 93 93 5030 1 . ASN 94 94 5030 1 . GLU 95 95 5030 1 . CYS 96 96 5030 1 . ILE 97 97 5030 1 . GLU 98 98 5030 1 . ASN 99 99 5030 1 . ALA 100 100 5030 1 . LYS 101 101 5030 1 . GLY 102 102 5030 1 . GLU 103 103 5030 1 . THR 104 104 5030 1 . ASP 105 105 5030 1 . GLU 106 106 5030 1 . CYS 107 107 5030 1 . ASN 108 108 5030 1 . ILE 109 109 5030 1 . GLY 110 110 5030 1 . ASN 111 111 5030 1 . LYS 112 112 5030 1 . TYR 113 113 5030 1 . THR 114 114 5030 1 . ASP 115 115 5030 1 . CYS 116 116 5030 1 . TYR 117 117 5030 1 . ILE 118 118 5030 1 . GLU 119 119 5030 1 . LYS 120 120 5030 1 . LEU 121 121 5030 1 . PHE 122 122 5030 1 . SER 123 123 5030 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 5030 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $ASP2 . 7460 organism . 'Apis mellifera' Honeybee . . Eukaryota Metazoa Apis mellifera . . antennae . . . . . . 'sensillum lymph' . . . 5030 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 5030 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $ASP2 . 'recombinant technology' 'Pichia pastoris' 'P. pastoris' . . Pichia pastoris GS115 Muts . pHIL-D2 . . pNatASP2 . . 'The host-vector system used was extremely efficient (around 100mg/L), see ref_2.' 5030 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_15N13C_H2O _Sample.Sf_category sample _Sample.Sf_framecode 15N13C_H2O _Sample.Entry_ID 5030 _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 ASP2 '[U-98% 13C; U-98% 15N]' . . 1 $ASP2 . . . 0.7 1.5 mM . . . . 5030 1 2 TSP . . . . . . . 0.1 . . mM . . . . 5030 1 3 'phosphate buffer' . . . . . . . 100 . . mM . . . . 5030 1 4 NaN3 . . . . . . . 0.1 . . mM . . . . 5030 1 5 H2O . . . . . . . 90 . . % . . . . 5030 1 6 D2O . . . . . . . 10 . . % . . . . 5030 1 stop_ save_ save_15N13C_D2O _Sample.Sf_category sample _Sample.Sf_framecode 15N13C_D2O _Sample.Entry_ID 5030 _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 ASP2 '[U-98% 13C; U-98% 15N]' . . 1 $ASP2 . . 1.3 . . mM . . . . 5030 2 2 TSP . . . . . . . 0.1 . . mM . . . . 5030 2 3 'phosphate buffer' . . . . . . . 100 . . mM . . . . 5030 2 4 NaN3 . . . . . . . 0.1 . . mM . . . . 5030 2 5 D2O . . . . . . . 100 . . % . . . . 5030 2 stop_ save_ save_15N_H2O _Sample.Sf_category sample _Sample.Sf_framecode 15N_H2O _Sample.Entry_ID 5030 _Sample.ID 3 _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 ASP2 '[U-98% 15N]' . . 1 $ASP2 . . 1 . . mM . . . . 5030 3 2 TSP . . . . . . . 0.1 . . mM . . . . 5030 3 3 'phosphate buffer' . . . . . . . 100 . . mM . . . . 5030 3 4 NaN3 . . . . . . . 0.1 . . mM . . . . 5030 3 5 H2O . . . . . . . 90 . . % . . . . 5030 3 6 D2O . . . . . . . 10 . . % . . . . 5030 3 stop_ save_ ####################### # Sample conditions # ####################### save_Cond_D2O _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Cond_D2O _Sample_condition_list.Entry_ID 5030 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.11 . M 5030 1 pH 7.7 0.1 n/a 5030 1 temperature 308 1 K 5030 1 stop_ save_ save_Cond_H2O _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Cond_H2O _Sample_condition_list.Entry_ID 5030 _Sample_condition_list.ID 2 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.11 . M 5030 2 pH 5.7 0.1 n/a 5030 2 temperature 308 1 K 5030 2 stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 5030 _Software.ID 1 _Software.Type . _Software.Name XWINNMR _Software.Version 2.6 _Software.DOI . _Software.Details 'Developed by Bruker' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID acquisition 5030 1 processing 5030 1 stop_ save_ save_AURELIA _Software.Sf_category software _Software.Sf_framecode AURELIA _Software.Entry_ID 5030 _Software.ID 2 _Software.Type . _Software.Name AURELIA _Software.Version 2.8.4 _Software.DOI . _Software.Details 'Developed by Bruker' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID Analysis 5030 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5030 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details ; Spectrometer equipped with a 5 mm TXI triple resonance, triple-axis gradient probe. ; _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 5030 _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 ; Spectrometer equipped with a 5 mm TXI triple resonance, triple-axis gradient probe. ; . . 5030 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 5030 _Experiment_list.ID 1 _Experiment_list.Details ; The 1H-15N NOESY and 1H-15N TOCSY experiments were collected on the 15N protein in H2O (sample 15N_H20). The HNCA,HN(CO)CA, HNCO, HN(CA)CO, HNCACB and CBCA(CO)NH experiments were collected on the 13C-15N protein in 100%H20 (sample 15N13C_H2O). The HCCH-TOCSY and 13C and NOESY-HSQC experiments were collected on the 13C-15N protein in 100% D2O (sample 13C15N_D2O). ; 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 '1H-15N NOESY' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5030 1 2 '1H-15N TOCSY' . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5030 1 3 HNCA . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5030 1 4 HN(CO)CA . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5030 1 5 HNCO . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5030 1 6 HN(CA)CO . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5030 1 7 HNCACB . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5030 1 8 CBCA(CO)NH . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5030 1 9 HCCH-TOCSY . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5030 1 10 NOESY-HSQC . . . . . . . . . . . . . . . . . . . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 5030 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 5030 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 TSP 'methyl protons' . . . . ppm 0.00 internal indirect 0.101329118 internal . . . . 5030 1 H 1 TSP 'methyl protons' . . . . ppm 0.00 internal direct 1.0 internal . . . . 5030 1 N 15 TSP 'methyl protons' . . . . ppm 0.00 internal indirect 0.251449530 internal . . . . 5030 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_ASP2_shift_set _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode ASP2_shift_set _Assigned_chem_shift_list.Entry_ID 5030 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Cond_D2O _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 '1H-15N NOESY' . . . 5030 1 2 '1H-15N TOCSY' . . . 5030 1 3 HNCA . . . 5030 1 4 HN(CO)CA . . . 5030 1 5 HNCO . . . 5030 1 6 HN(CA)CO . . . 5030 1 7 HNCACB . . . 5030 1 8 CBCA(CO)NH . . . 5030 1 9 HCCH-TOCSY . . . 5030 1 10 NOESY-HSQC . . . 5030 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Ambiguity_set_ID _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 ILE HA H 1 3.77 0.02 . 1 . . . . . . . . . 5030 1 2 . 1 1 1 1 ILE HB H 1 2.01 0.02 . 1 . . . . . . . . . 5030 1 3 . 1 1 1 1 ILE C C 13 171.70 0.05 . 1 . . . . . . . . . 5030 1 4 . 1 1 1 1 ILE CA C 13 59.70 0.20 . 1 . . . . . . . . . 5030 1 5 . 1 1 1 1 ILE CB C 13 38.90 0.40 . 1 . . . . . . . . . 5030 1 6 . 1 1 2 2 ASP H H 1 8.79 0.01 . 1 . . . . . . . . . 5030 1 7 . 1 1 2 2 ASP HA H 1 4.89 0.02 . 1 . . . . . . . . . 5030 1 8 . 1 1 2 2 ASP HB2 H 1 2.69 0.02 . 2 . . . . . . . . . 5030 1 9 . 1 1 2 2 ASP HB3 H 1 2.92 0.02 . 2 . . . . . . . . . 5030 1 10 . 1 1 2 2 ASP C C 13 175.50 0.05 . 1 . . . . . . . . . 5030 1 11 . 1 1 2 2 ASP CA C 13 53.20 0.20 . 1 . . . . . . . . . 5030 1 12 . 1 1 2 2 ASP CB C 13 41.10 0.40 . 1 . . . . . . . . . 5030 1 13 . 1 1 2 2 ASP N N 15 126.70 0.10 . 1 . . . . . . . . . 5030 1 14 . 1 1 3 3 GLN H H 1 8.80 0.01 . 1 . . . . . . . . . 5030 1 15 . 1 1 3 3 GLN HA H 1 3.81 0.02 . 1 . . . . . . . . . 5030 1 16 . 1 1 3 3 GLN HB2 H 1 1.88 0.02 . 1 . . . . . . . . . 5030 1 17 . 1 1 3 3 GLN HB3 H 1 1.88 0.02 . 1 . . . . . . . . . 5030 1 18 . 1 1 3 3 GLN C C 13 176.70 0.05 . 1 . . . . . . . . . 5030 1 19 . 1 1 3 3 GLN CA C 13 59.50 0.20 . 1 . . . . . . . . . 5030 1 20 . 1 1 3 3 GLN CB C 13 28.40 0.40 . 1 . . . . . . . . . 5030 1 21 . 1 1 3 3 GLN N N 15 125.00 0.10 . 1 . . . . . . . . . 5030 1 22 . 1 1 4 4 ASP H H 1 8.51 0.01 . 1 . . . . . . . . . 5030 1 23 . 1 1 4 4 ASP HA H 1 4.40 0.02 . 1 . . . . . . . . . 5030 1 24 . 1 1 4 4 ASP HB2 H 1 2.70 0.02 . 2 . . . . . . . . . 5030 1 25 . 1 1 4 4 ASP HB3 H 1 2.77 0.02 . 2 . . . . . . . . . 5030 1 26 . 1 1 4 4 ASP C C 13 178.76 0.05 . 1 . . . . . . . . . 5030 1 27 . 1 1 4 4 ASP CA C 13 57.10 0.20 . 1 . . . . . . . . . 5030 1 28 . 1 1 4 4 ASP CB C 13 40.40 0.40 . 1 . . . . . . . . . 5030 1 29 . 1 1 4 4 ASP N N 15 117.10 0.10 . 1 . . . . . . . . . 5030 1 30 . 1 1 5 5 THR H H 1 7.69 0.01 . 1 . . . . . . . . . 5030 1 31 . 1 1 5 5 THR HA H 1 4.31 0.02 . 2 . . . . . . . . . 5030 1 32 . 1 1 5 5 THR HB H 1 4.29 0.02 . 2 . . . . . . . . . 5030 1 33 . 1 1 5 5 THR C C 13 176.50 0.05 . 1 . . . . . . . . . 5030 1 34 . 1 1 5 5 THR CA C 13 64.50 0.20 . 1 . . . . . . . . . 5030 1 35 . 1 1 5 5 THR CB C 13 69.60 0.40 . 1 . . . . . . . . . 5030 1 36 . 1 1 5 5 THR N N 15 113.30 0.10 . 1 . . . . . . . . . 5030 1 37 . 1 1 6 6 VAL H H 1 7.94 0.01 . 1 . . . . . . . . . 5030 1 38 . 1 1 6 6 VAL HA H 1 3.81 0.02 . 1 . . . . . . . . . 5030 1 39 . 1 1 6 6 VAL HB H 1 2.33 0.02 . 1 . . . . . . . . . 5030 1 40 . 1 1 6 6 VAL C C 13 177.40 0.05 . 1 . . . . . . . . . 5030 1 41 . 1 1 6 6 VAL CA C 13 66.20 0.20 . 1 . . . . . . . . . 5030 1 42 . 1 1 6 6 VAL CB C 13 31.80 0.40 . 1 . . . . . . . . . 5030 1 43 . 1 1 6 6 VAL N N 15 120.40 0.10 . 1 . . . . . . . . . 5030 1 44 . 1 1 7 7 VAL H H 1 8.49 0.01 . 1 . . . . . . . . . 5030 1 45 . 1 1 7 7 VAL HA H 1 3.79 0.02 . 1 . . . . . . . . . 5030 1 46 . 1 1 7 7 VAL HB H 1 2.21 0.02 . 1 . . . . . . . . . 5030 1 47 . 1 1 7 7 VAL C C 13 177.60 0.05 . 1 . . . . . . . . . 5030 1 48 . 1 1 7 7 VAL CA C 13 68.00 0.20 . 1 . . . . . . . . . 5030 1 49 . 1 1 7 7 VAL CB C 13 32.00 0.40 . 1 . . . . . . . . . 5030 1 50 . 1 1 7 7 VAL N N 15 120.60 0.10 . 1 . . . . . . . . . 5030 1 51 . 1 1 8 8 ALA H H 1 7.70 0.01 . 1 . . . . . . . . . 5030 1 52 . 1 1 8 8 ALA HA H 1 4.16 0.02 . 1 . . . . . . . . . 5030 1 53 . 1 1 8 8 ALA HB1 H 1 1.56 0.02 . 1 . . . . . . . . . 5030 1 54 . 1 1 8 8 ALA HB2 H 1 1.56 0.02 . 1 . . . . . . . . . 5030 1 55 . 1 1 8 8 ALA HB3 H 1 1.56 0.02 . 1 . . . . . . . . . 5030 1 56 . 1 1 8 8 ALA C C 13 180.70 0.05 . 1 . . . . . . . . . 5030 1 57 . 1 1 8 8 ALA CA C 13 55.20 0.20 . 1 . . . . . . . . . 5030 1 58 . 1 1 8 8 ALA CB C 13 17.80 0.40 . 1 . . . . . . . . . 5030 1 59 . 1 1 8 8 ALA N N 15 120.10 0.10 . 1 . . . . . . . . . 5030 1 60 . 1 1 9 9 LYS H H 1 7.79 0.01 . 1 . . . . . . . . . 5030 1 61 . 1 1 9 9 LYS HA H 1 4.22 0.02 . 1 . . . . . . . . . 5030 1 62 . 1 1 9 9 LYS HB2 H 1 1.78 0.02 . 2 . . . . . . . . . 5030 1 63 . 1 1 9 9 LYS HB3 H 1 2.02 0.02 . 2 . . . . . . . . . 5030 1 64 . 1 1 9 9 LYS C C 13 180.30 0.05 . 1 . . . . . . . . . 5030 1 65 . 1 1 9 9 LYS CA C 13 59.20 0.20 . 1 . . . . . . . . . 5030 1 66 . 1 1 9 9 LYS CB C 13 33.00 0.40 . 1 . . . . . . . . . 5030 1 67 . 1 1 9 9 LYS N N 15 118.30 0.10 . 1 . . . . . . . . . 5030 1 68 . 1 1 10 10 TYR H H 1 8.47 0.01 . 1 . . . . . . . . . 5030 1 69 . 1 1 10 10 TYR HA H 1 4.20 0.02 . 1 . . . . . . . . . 5030 1 70 . 1 1 10 10 TYR HB2 H 1 2.98 0.02 . 2 . . . . . . . . . 5030 1 71 . 1 1 10 10 TYR HB3 H 1 3.29 0.02 . 2 . . . . . . . . . 5030 1 72 . 1 1 10 10 TYR C C 13 178.50 0.05 . 1 . . . . . . . . . 5030 1 73 . 1 1 10 10 TYR CA C 13 63.20 0.20 . 1 . . . . . . . . . 5030 1 74 . 1 1 10 10 TYR CB C 13 38.80 0.40 . 1 . . . . . . . . . 5030 1 75 . 1 1 10 10 TYR N N 15 120.20 0.10 . 1 . . . . . . . . . 5030 1 76 . 1 1 11 11 MET H H 1 8.57 0.01 . 1 . . . . . . . . . 5030 1 77 . 1 1 11 11 MET HA H 1 4.21 0.02 . 1 . . . . . . . . . 5030 1 78 . 1 1 11 11 MET HB2 H 1 2.28 0.02 . 2 . . . . . . . . . 5030 1 79 . 1 1 11 11 MET HB3 H 1 2.00 0.02 . 2 . . . . . . . . . 5030 1 80 . 1 1 11 11 MET C C 13 178.30 0.05 . 1 . . . . . . . . . 5030 1 81 . 1 1 11 11 MET CA C 13 58.00 0.20 . 1 . . . . . . . . . 5030 1 82 . 1 1 11 11 MET CB C 13 31.50 0.40 . 1 . . . . . . . . . 5030 1 83 . 1 1 11 11 MET N N 15 116.70 0.10 . 1 . . . . . . . . . 5030 1 84 . 1 1 12 12 GLU H H 1 8.16 0.01 . 1 . . . . . . . . . 5030 1 85 . 1 1 12 12 GLU HA H 1 4.02 0.02 . 1 . . . . . . . . . 5030 1 86 . 1 1 12 12 GLU HB2 H 1 2.16 0.02 . 2 . . . . . . . . . 5030 1 87 . 1 1 12 12 GLU HB3 H 1 2.20 0.02 . 2 . . . . . . . . . 5030 1 88 . 1 1 12 12 GLU C C 13 178.80 0.05 . 1 . . . . . . . . . 5030 1 89 . 1 1 12 12 GLU CA C 13 59.40 0.20 . 1 . . . . . . . . . 5030 1 90 . 1 1 12 12 GLU CB C 13 29.60 0.40 . 1 . . . . . . . . . 5030 1 91 . 1 1 12 12 GLU N N 15 118.40 0.10 . 1 . . . . . . . . . 5030 1 92 . 1 1 13 13 TYR H H 1 7.79 0.01 . 1 . . . . . . . . . 5030 1 93 . 1 1 13 13 TYR HA H 1 4.03 0.02 . 1 . . . . . . . . . 5030 1 94 . 1 1 13 13 TYR HB2 H 1 3.31 0.02 . 2 . . . . . . . . . 5030 1 95 . 1 1 13 13 TYR HB3 H 1 3.02 0.02 . 2 . . . . . . . . . 5030 1 96 . 1 1 13 13 TYR C C 13 177.50 0.05 . 1 . . . . . . . . . 5030 1 97 . 1 1 13 13 TYR CA C 13 61.20 0.20 . 1 . . . . . . . . . 5030 1 98 . 1 1 13 13 TYR CB C 13 38.90 0.40 . 1 . . . . . . . . . 5030 1 99 . 1 1 13 13 TYR N N 15 119.10 0.10 . 1 . . . . . . . . . 5030 1 100 . 1 1 14 14 LEU H H 1 8.30 0.01 . 1 . . . . . . . . . 5030 1 101 . 1 1 14 14 LEU HA H 1 4.58 0.02 . 1 . . . . . . . . . 5030 1 102 . 1 1 14 14 LEU HB2 H 1 1.62 0.02 . 2 . . . . . . . . . 5030 1 103 . 1 1 14 14 LEU HB3 H 1 2.06 0.02 . 2 . . . . . . . . . 5030 1 104 . 1 1 14 14 LEU C C 13 178.62 0.05 . 1 . . . . . . . . . 5030 1 105 . 1 1 14 14 LEU CA C 13 55.00 0.20 . 1 . . . . . . . . . 5030 1 106 . 1 1 14 14 LEU CB C 13 43.70 0.40 . 1 . . . . . . . . . 5030 1 107 . 1 1 14 14 LEU N N 15 114.50 0.10 . 1 . . . . . . . . . 5030 1 108 . 1 1 15 15 MET H H 1 8.30 0.01 . 1 . . . . . . . . . 5030 1 109 . 1 1 15 15 MET HA H 1 4.56 0.02 . 1 . . . . . . . . . 5030 1 110 . 1 1 15 15 MET HB2 H 1 2.59 0.02 . 2 . . . . . . . . . 5030 1 111 . 1 1 15 15 MET HB3 H 1 2.21 0.02 . 2 . . . . . . . . . 5030 1 112 . 1 1 15 15 MET C C 13 173.77 0.05 . 1 . . . . . . . . . 5030 1 113 . 1 1 15 15 MET CA C 13 59.50 0.20 . 1 . . . . . . . . . 5030 1 114 . 1 1 15 15 MET CB C 13 28.20 0.40 . 1 . . . . . . . . . 5030 1 115 . 1 1 15 15 MET N N 15 124.20 0.10 . 1 . . . . . . . . . 5030 1 116 . 1 1 16 16 PRO HA H 1 4.39 0.02 . 1 . . . . . . . . . 5030 1 117 . 1 1 16 16 PRO HB2 H 1 2.31 0.02 . 2 . . . . . . . . . 5030 1 118 . 1 1 16 16 PRO HB3 H 1 1.76 0.02 . 2 . . . . . . . . . 5030 1 119 . 1 1 16 16 PRO C C 13 176.13 0.05 . 1 . . . . . . . . . 5030 1 120 . 1 1 16 16 PRO CA C 13 65.50 0.20 . 1 . . . . . . . . . 5030 1 121 . 1 1 16 16 PRO CB C 13 31.00 0.40 . 1 . . . . . . . . . 5030 1 122 . 1 1 17 17 ASP H H 1 8.02 0.01 . 1 . . . . . . . . . 5030 1 123 . 1 1 17 17 ASP HA H 1 4.84 0.02 . 1 . . . . . . . . . 5030 1 124 . 1 1 17 17 ASP HB2 H 1 2.52 0.02 . 2 . . . . . . . . . 5030 1 125 . 1 1 17 17 ASP HB3 H 1 2.62 0.02 . 2 . . . . . . . . . 5030 1 126 . 1 1 17 17 ASP C C 13 175.95 0.05 . 1 . . . . . . . . . 5030 1 127 . 1 1 17 17 ASP CA C 13 55.80 0.20 . 1 . . . . . . . . . 5030 1 128 . 1 1 17 17 ASP CB C 13 44.60 0.40 . 1 . . . . . . . . . 5030 1 129 . 1 1 17 17 ASP N N 15 113.70 0.10 . 1 . . . . . . . . . 5030 1 130 . 1 1 18 18 ILE H H 1 8.42 0.01 . 1 . . . . . . . . . 5030 1 131 . 1 1 18 18 ILE HA H 1 3.44 0.02 . 1 . . . . . . . . . 5030 1 132 . 1 1 18 18 ILE HB H 1 1.89 0.02 . 1 . . . . . . . . . 5030 1 133 . 1 1 18 18 ILE C C 13 177.66 0.05 . 1 . . . . . . . . . 5030 1 134 . 1 1 18 18 ILE CA C 13 65.60 0.20 . 1 . . . . . . . . . 5030 1 135 . 1 1 18 18 ILE CB C 13 37.90 0.40 . 1 . . . . . . . . . 5030 1 136 . 1 1 18 18 ILE N N 15 120.40 0.10 . 1 . . . . . . . . . 5030 1 137 . 1 1 19 19 MET H H 1 7.83 0.01 . 1 . . . . . . . . . 5030 1 138 . 1 1 19 19 MET HA H 1 4.43 0.02 . 1 . . . . . . . . . 5030 1 139 . 1 1 19 19 MET HB2 H 1 2.12 0.02 . 1 . . . . . . . . . 5030 1 140 . 1 1 19 19 MET HB3 H 1 2.12 0.02 . 1 . . . . . . . . . 5030 1 141 . 1 1 19 19 MET C C 13 175.95 0.05 . 1 . . . . . . . . . 5030 1 142 . 1 1 19 19 MET CA C 13 59.60 0.20 . 1 . . . . . . . . . 5030 1 143 . 1 1 19 19 MET CB C 13 29.20 0.40 . 1 . . . . . . . . . 5030 1 144 . 1 1 19 19 MET N N 15 115.30 0.10 . 1 . . . . . . . . . 5030 1 145 . 1 1 20 20 PRO HA H 1 4.48 0.02 . 1 . . . . . . . . . 5030 1 146 . 1 1 20 20 PRO HB2 H 1 2.36 0.02 . 2 . . . . . . . . . 5030 1 147 . 1 1 20 20 PRO HB3 H 1 1.75 0.02 . 2 . . . . . . . . . 5030 1 148 . 1 1 20 20 PRO C C 13 180.30 0.05 . 1 . . . . . . . . . 5030 1 149 . 1 1 20 20 PRO CA C 13 65.70 0.20 . 1 . . . . . . . . . 5030 1 150 . 1 1 20 20 PRO CB C 13 30.80 0.40 . 1 . . . . . . . . . 5030 1 151 . 1 1 21 21 CYS H H 1 6.77 0.01 . 1 . . . . . . . . . 5030 1 152 . 1 1 21 21 CYS HA H 1 4.41 0.02 . 1 . . . . . . . . . 5030 1 153 . 1 1 21 21 CYS HB2 H 1 2.74 0.02 . 2 . . . . . . . . . 5030 1 154 . 1 1 21 21 CYS HB3 H 1 3.24 0.02 . 2 . . . . . . . . . 5030 1 155 . 1 1 21 21 CYS C C 13 175.30 0.05 . 1 . . . . . . . . . 5030 1 156 . 1 1 21 21 CYS CA C 13 59.70 0.20 . 1 . . . . . . . . . 5030 1 157 . 1 1 21 21 CYS CB C 13 41.00 0.40 . 1 . . . . . . . . . 5030 1 158 . 1 1 21 21 CYS N N 15 116.60 0.10 . 1 . . . . . . . . . 5030 1 159 . 1 1 22 22 ALA H H 1 8.86 0.01 . 1 . . . . . . . . . 5030 1 160 . 1 1 22 22 ALA HA H 1 3.84 0.02 . 1 . . . . . . . . . 5030 1 161 . 1 1 22 22 ALA HB1 H 1 1.42 0.02 . 1 . . . . . . . . . 5030 1 162 . 1 1 22 22 ALA HB2 H 1 1.42 0.02 . 1 . . . . . . . . . 5030 1 163 . 1 1 22 22 ALA HB3 H 1 1.42 0.02 . 1 . . . . . . . . . 5030 1 164 . 1 1 22 22 ALA C C 13 179.30 0.05 . 1 . . . . . . . . . 5030 1 165 . 1 1 22 22 ALA CA C 13 55.60 0.20 . 1 . . . . . . . . . 5030 1 166 . 1 1 22 22 ALA CB C 13 16.60 0.40 . 1 . . . . . . . . . 5030 1 167 . 1 1 22 22 ALA N N 15 123.70 0.10 . 1 . . . . . . . . . 5030 1 168 . 1 1 23 23 ASP H H 1 7.95 0.01 . 1 . . . . . . . . . 5030 1 169 . 1 1 23 23 ASP HA H 1 4.40 0.02 . 1 . . . . . . . . . 5030 1 170 . 1 1 23 23 ASP HB2 H 1 2.74 0.02 . 2 . . . . . . . . . 5030 1 171 . 1 1 23 23 ASP HB3 H 1 2.93 0.02 . 2 . . . . . . . . . 5030 1 172 . 1 1 23 23 ASP C C 13 179.40 0.05 . 1 . . . . . . . . . 5030 1 173 . 1 1 23 23 ASP CA C 13 57.10 0.20 . 1 . . . . . . . . . 5030 1 174 . 1 1 23 23 ASP CB C 13 41.10 0.40 . 1 . . . . . . . . . 5030 1 175 . 1 1 23 23 ASP N N 15 117.00 0.10 . 1 . . . . . . . . . 5030 1 176 . 1 1 24 24 GLU H H 1 8.01 0.01 . 1 . . . . . . . . . 5030 1 177 . 1 1 24 24 GLU HA H 1 3.92 0.02 . 1 . . . . . . . . . 5030 1 178 . 1 1 24 24 GLU HB2 H 1 2.25 0.02 . 2 . . . . . . . . . 5030 1 179 . 1 1 24 24 GLU HB3 H 1 2.10 0.02 . 2 . . . . . . . . . 5030 1 180 . 1 1 24 24 GLU C C 13 177.96 0.05 . 1 . . . . . . . . . 5030 1 181 . 1 1 24 24 GLU CA C 13 58.90 0.20 . 1 . . . . . . . . . 5030 1 182 . 1 1 24 24 GLU CB C 13 29.40 0.40 . 1 . . . . . . . . . 5030 1 183 . 1 1 24 24 GLU N N 15 120.20 0.10 . 1 . . . . . . . . . 5030 1 184 . 1 1 25 25 LEU H H 1 7.64 0.01 . 1 . . . . . . . . . 5030 1 185 . 1 1 25 25 LEU HA H 1 4.22 0.02 . 1 . . . . . . . . . 5030 1 186 . 1 1 25 25 LEU HB2 H 1 1.63 0.02 . 1 . . . . . . . . . 5030 1 187 . 1 1 25 25 LEU HB3 H 1 1.63 0.02 . 1 . . . . . . . . . 5030 1 188 . 1 1 25 25 LEU C C 13 175.80 0.05 . 1 . . . . . . . . . 5030 1 189 . 1 1 25 25 LEU CA C 13 54.40 0.20 . 1 . . . . . . . . . 5030 1 190 . 1 1 25 25 LEU CB C 13 42.00 0.40 . 1 . . . . . . . . . 5030 1 191 . 1 1 25 25 LEU N N 15 116.30 0.10 . 1 . . . . . . . . . 5030 1 192 . 1 1 26 26 HIS H H 1 7.75 0.01 . 1 . . . . . . . . . 5030 1 193 . 1 1 26 26 HIS HA H 1 4.35 0.02 . 1 . . . . . . . . . 5030 1 194 . 1 1 26 26 HIS HB2 H 1 3.35 0.02 . 2 . . . . . . . . . 5030 1 195 . 1 1 26 26 HIS HB3 H 1 3.51 0.02 . 2 . . . . . . . . . 5030 1 196 . 1 1 26 26 HIS C C 13 174.00 0.05 . 1 . . . . . . . . . 5030 1 197 . 1 1 26 26 HIS CA C 13 55.90 0.20 . 1 . . . . . . . . . 5030 1 198 . 1 1 26 26 HIS CB C 13 26.00 0.40 . 1 . . . . . . . . . 5030 1 199 . 1 1 26 26 HIS N N 15 115.60 0.10 . 1 . . . . . . . . . 5030 1 200 . 1 1 27 27 ILE H H 1 8.47 0.01 . 1 . . . . . . . . . 5030 1 201 . 1 1 27 27 ILE HA H 1 4.30 0.02 . 1 . . . . . . . . . 5030 1 202 . 1 1 27 27 ILE HB H 1 1.53 0.02 . 1 . . . . . . . . . 5030 1 203 . 1 1 27 27 ILE C C 13 175.40 0.05 . 1 . . . . . . . . . 5030 1 204 . 1 1 27 27 ILE CA C 13 59.80 0.20 . 1 . . . . . . . . . 5030 1 205 . 1 1 27 27 ILE CB C 13 39.60 0.40 . 1 . . . . . . . . . 5030 1 206 . 1 1 27 27 ILE N N 15 118.90 0.10 . 1 . . . . . . . . . 5030 1 207 . 1 1 28 28 SER H H 1 8.36 0.01 . 1 . . . . . . . . . 5030 1 208 . 1 1 28 28 SER HA H 1 4.26 0.02 . 1 . . . . . . . . . 5030 1 209 . 1 1 28 28 SER HB2 H 1 3.92 0.02 . 2 . . . . . . . . . 5030 1 210 . 1 1 28 28 SER HB3 H 1 4.12 0.02 . 2 . . . . . . . . . 5030 1 211 . 1 1 28 28 SER C C 13 175.60 0.05 . 1 . . . . . . . . . 5030 1 212 . 1 1 28 28 SER CA C 13 58.80 0.20 . 1 . . . . . . . . . 5030 1 213 . 1 1 28 28 SER CB C 13 63.70 0.40 . 1 . . . . . . . . . 5030 1 214 . 1 1 28 28 SER N N 15 120.70 0.10 . 1 . . . . . . . . . 5030 1 215 . 1 1 29 29 GLU H H 1 8.79 0.01 . 1 . . . . . . . . . 5030 1 216 . 1 1 29 29 GLU HA H 1 3.91 0.02 . 1 . . . . . . . . . 5030 1 217 . 1 1 29 29 GLU HB2 H 1 2.05 0.02 . 1 . . . . . . . . . 5030 1 218 . 1 1 29 29 GLU C C 13 177.15 0.05 . 1 . . . . . . . . . 5030 1 219 . 1 1 29 29 GLU CA C 13 59.50 0.20 . 1 . . . . . . . . . 5030 1 220 . 1 1 29 29 GLU CB C 13 28.90 0.40 . 1 . . . . . . . . . 5030 1 221 . 1 1 29 29 GLU N N 15 123.70 0.10 . 1 . . . . . . . . . 5030 1 222 . 1 1 30 30 ASP H H 1 8.31 0.01 . 1 . . . . . . . . . 5030 1 223 . 1 1 30 30 ASP HA H 1 4.40 0.02 . 1 . . . . . . . . . 5030 1 224 . 1 1 30 30 ASP HB2 H 1 2.61 0.02 . 2 . . . . . . . . . 5030 1 225 . 1 1 30 30 ASP HB3 H 1 2.70 0.02 . 2 . . . . . . . . . 5030 1 226 . 1 1 30 30 ASP C C 13 177.22 0.05 . 1 . . . . . . . . . 5030 1 227 . 1 1 30 30 ASP CA C 13 55.70 0.20 . 1 . . . . . . . . . 5030 1 228 . 1 1 30 30 ASP CB C 13 39.50 0.40 . 1 . . . . . . . . . 5030 1 229 . 1 1 30 30 ASP N N 15 118.20 0.10 . 1 . . . . . . . . . 5030 1 230 . 1 1 31 31 ILE H H 1 7.41 0.01 . 1 . . . . . . . . . 5030 1 231 . 1 1 31 31 ILE HA H 1 3.92 0.02 . 1 . . . . . . . . . 5030 1 232 . 1 1 31 31 ILE HB H 1 1.92 0.02 . 1 . . . . . . . . . 5030 1 233 . 1 1 31 31 ILE C C 13 177.14 0.05 . 1 . . . . . . . . . 5030 1 234 . 1 1 31 31 ILE CA C 13 62.60 0.20 . 1 . . . . . . . . . 5030 1 235 . 1 1 31 31 ILE CB C 13 39.40 0.40 . 1 . . . . . . . . . 5030 1 236 . 1 1 31 31 ILE N N 15 119.90 0.10 . 1 . . . . . . . . . 5030 1 237 . 1 1 32 32 ALA H H 1 8.02 0.01 . 1 . . . . . . . . . 5030 1 238 . 1 1 32 32 ALA HA H 1 3.85 0.02 . 1 . . . . . . . . . 5030 1 239 . 1 1 32 32 ALA HB1 H 1 1.29 0.02 . 1 . . . . . . . . . 5030 1 240 . 1 1 32 32 ALA HB2 H 1 1.29 0.02 . 1 . . . . . . . . . 5030 1 241 . 1 1 32 32 ALA HB3 H 1 1.29 0.02 . 1 . . . . . . . . . 5030 1 242 . 1 1 32 32 ALA C C 13 176.60 0.05 . 1 . . . . . . . . . 5030 1 243 . 1 1 32 32 ALA CA C 13 54.10 0.20 . 1 . . . . . . . . . 5030 1 244 . 1 1 32 32 ALA CB C 13 19.70 0.40 . 1 . . . . . . . . . 5030 1 245 . 1 1 32 32 ALA N N 15 120.40 0.10 . 1 . . . . . . . . . 5030 1 246 . 1 1 33 33 THR H H 1 7.64 0.01 . 1 . . . . . . . . . 5030 1 247 . 1 1 33 33 THR HA H 1 4.16 0.02 . 1 . . . . . . . . . 5030 1 248 . 1 1 33 33 THR HB H 1 4.24 0.02 . 1 . . . . . . . . . 5030 1 249 . 1 1 33 33 THR C C 13 174.16 0.05 . 1 . . . . . . . . . 5030 1 250 . 1 1 33 33 THR CA C 13 62.90 0.20 . 1 . . . . . . . . . 5030 1 251 . 1 1 33 33 THR CB C 13 70.70 0.40 . 1 . . . . . . . . . 5030 1 252 . 1 1 33 33 THR N N 15 118.50 0.10 . 1 . . . . . . . . . 5030 1 253 . 1 1 34 34 ASN H H 1 7.42 0.01 . 1 . . . . . . . . . 5030 1 254 . 1 1 34 34 ASN HA H 1 4.79 0.02 . 1 . . . . . . . . . 5030 1 255 . 1 1 34 34 ASN HB2 H 1 2.89 0.02 . 2 . . . . . . . . . 5030 1 256 . 1 1 34 34 ASN HB3 H 1 2.81 0.02 . 2 . . . . . . . . . 5030 1 257 . 1 1 34 34 ASN C C 13 175.96 0.05 . 1 . . . . . . . . . 5030 1 258 . 1 1 34 34 ASN CA C 13 53.00 0.20 . 1 . . . . . . . . . 5030 1 259 . 1 1 34 34 ASN CB C 13 38.90 0.40 . 1 . . . . . . . . . 5030 1 260 . 1 1 34 34 ASN N N 15 120.00 0.10 . 1 . . . . . . . . . 5030 1 261 . 1 1 35 35 ILE H H 1 8.34 0.01 . 1 . . . . . . . . . 5030 1 262 . 1 1 35 35 ILE HA H 1 3.96 0.02 . 1 . . . . . . . . . 5030 1 263 . 1 1 35 35 ILE HB H 1 1.92 0.02 . 1 . . . . . . . . . 5030 1 264 . 1 1 35 35 ILE C C 13 176.57 0.05 . 1 . . . . . . . . . 5030 1 265 . 1 1 35 35 ILE CA C 13 63.10 0.20 . 1 . . . . . . . . . 5030 1 266 . 1 1 35 35 ILE N N 15 122.00 0.10 . 1 . . . . . . . . . 5030 1 267 . 1 1 36 36 GLN H H 1 8.05 0.01 . 1 . . . . . . . . . 5030 1 268 . 1 1 36 36 GLN HA H 1 3.94 0.02 . 1 . . . . . . . . . 5030 1 269 . 1 1 36 36 GLN HB2 H 1 2.08 0.02 . 2 . . . . . . . . . 5030 1 270 . 1 1 36 36 GLN HB3 H 1 2.23 0.02 . 2 . . . . . . . . . 5030 1 271 . 1 1 36 36 GLN C C 13 176.57 0.05 . 1 . . . . . . . . . 5030 1 272 . 1 1 36 36 GLN CA C 13 56.70 0.20 . 1 . . . . . . . . . 5030 1 273 . 1 1 36 36 GLN CB C 13 29.00 0.40 . 1 . . . . . . . . . 5030 1 274 . 1 1 36 36 GLN N N 15 119.80 0.10 . 1 . . . . . . . . . 5030 1 275 . 1 1 37 37 ALA H H 1 7.81 0.01 . 1 . . . . . . . . . 5030 1 276 . 1 1 37 37 ALA HA H 1 4.20 0.02 . 1 . . . . . . . . . 5030 1 277 . 1 1 37 37 ALA HB1 H 1 1.43 0.02 . 1 . . . . . . . . . 5030 1 278 . 1 1 37 37 ALA HB2 H 1 1.43 0.02 . 1 . . . . . . . . . 5030 1 279 . 1 1 37 37 ALA HB3 H 1 1.43 0.02 . 1 . . . . . . . . . 5030 1 280 . 1 1 37 37 ALA C C 13 178.43 0.05 . 1 . . . . . . . . . 5030 1 281 . 1 1 37 37 ALA CA C 13 53.50 0.20 . 1 . . . . . . . . . 5030 1 282 . 1 1 37 37 ALA CB C 13 18.50 0.40 . 1 . . . . . . . . . 5030 1 283 . 1 1 37 37 ALA N N 15 122.30 0.10 . 1 . . . . . . . . . 5030 1 284 . 1 1 38 38 ALA H H 1 8.06 0.01 . 1 . . . . . . . . . 5030 1 285 . 1 1 38 38 ALA HA H 1 4.12 0.02 . 1 . . . . . . . . . 5030 1 286 . 1 1 38 38 ALA HB1 H 1 1.42 0.02 . 1 . . . . . . . . . 5030 1 287 . 1 1 38 38 ALA HB2 H 1 1.42 0.02 . 1 . . . . . . . . . 5030 1 288 . 1 1 38 38 ALA HB3 H 1 1.42 0.02 . 1 . . . . . . . . . 5030 1 289 . 1 1 38 38 ALA C C 13 178.70 0.05 . 1 . . . . . . . . . 5030 1 290 . 1 1 38 38 ALA CA C 13 54.40 0.20 . 1 . . . . . . . . . 5030 1 291 . 1 1 38 38 ALA CB C 13 18.50 0.40 . 1 . . . . . . . . . 5030 1 292 . 1 1 38 38 ALA N N 15 121.10 0.10 . 1 . . . . . . . . . 5030 1 293 . 1 1 39 39 LYS H H 1 7.99 0.01 . 1 . . . . . . . . . 5030 1 294 . 1 1 39 39 LYS HA H 1 4.23 0.02 . 1 . . . . . . . . . 5030 1 295 . 1 1 39 39 LYS HB2 H 1 1.80 0.02 . 1 . . . . . . . . . 5030 1 296 . 1 1 39 39 LYS HB3 H 1 1.80 0.02 . 1 . . . . . . . . . 5030 1 297 . 1 1 39 39 LYS C C 13 176.70 0.05 . 1 . . . . . . . . . 5030 1 298 . 1 1 39 39 LYS CA C 13 57.20 0.20 . 1 . . . . . . . . . 5030 1 299 . 1 1 39 39 LYS CB C 13 32.70 0.40 . 1 . . . . . . . . . 5030 1 300 . 1 1 39 39 LYS N N 15 118.30 0.10 . 1 . . . . . . . . . 5030 1 301 . 1 1 40 40 ASN H H 1 7.95 0.01 . 1 . . . . . . . . . 5030 1 302 . 1 1 40 40 ASN HA H 1 4.75 0.02 . 1 . . . . . . . . . 5030 1 303 . 1 1 40 40 ASN HB2 H 1 2.91 0.02 . 2 . . . . . . . . . 5030 1 304 . 1 1 40 40 ASN HB3 H 1 2.77 0.02 . 2 . . . . . . . . . 5030 1 305 . 1 1 40 40 ASN C C 13 175.70 0.05 . 1 . . . . . . . . . 5030 1 306 . 1 1 40 40 ASN CA C 13 53.30 0.20 . 1 . . . . . . . . . 5030 1 307 . 1 1 40 40 ASN CB C 13 38.8 0.40 . 1 . . . . . . . . . 5030 1 308 . 1 1 40 40 ASN N N 15 117.00 0.10 . 1 . . . . . . . . . 5030 1 309 . 1 1 41 41 GLY H H 1 8.10 0.01 . 1 . . . . . . . . . 5030 1 310 . 1 1 41 41 GLY HA2 H 1 3.90 0.02 . 1 . . . . . . . . . 5030 1 311 . 1 1 41 41 GLY HA3 H 1 4.04 0.02 . 1 . . . . . . . . . 5030 1 312 . 1 1 41 41 GLY C C 13 174.30 0.05 . 1 . . . . . . . . . 5030 1 313 . 1 1 41 41 GLY CA C 13 45.40 0.20 . 1 . . . . . . . . . 5030 1 314 . 1 1 41 41 GLY N N 15 108.30 0.10 . 1 . . . . . . . . . 5030 1 315 . 1 1 42 42 ALA H H 1 7.89 0.01 . 1 . . . . . . . . . 5030 1 316 . 1 1 42 42 ALA HA H 1 4.30 0.02 . 1 . . . . . . . . . 5030 1 317 . 1 1 42 42 ALA HB1 H 1 1.33 0.02 . 1 . . . . . . . . . 5030 1 318 . 1 1 42 42 ALA HB2 H 1 1.33 0.02 . 1 . . . . . . . . . 5030 1 319 . 1 1 42 42 ALA HB3 H 1 1.33 0.02 . 1 . . . . . . . . . 5030 1 320 . 1 1 42 42 ALA C C 13 177.21 0.05 . 1 . . . . . . . . . 5030 1 321 . 1 1 42 42 ALA CA C 13 52.50 0.20 . 1 . . . . . . . . . 5030 1 322 . 1 1 42 42 ALA CB C 13 19.40 0.40 . 1 . . . . . . . . . 5030 1 323 . 1 1 42 42 ALA N N 15 123.00 0.10 . 1 . . . . . . . . . 5030 1 324 . 1 1 43 43 ASP H H 1 8.32 0.01 . 1 . . . . . . . . . 5030 1 325 . 1 1 43 43 ASP HA H 1 4.59 0.02 . 1 . . . . . . . . . 5030 1 326 . 1 1 43 43 ASP HB2 H 1 2.71 0.02 . 2 . . . . . . . . . 5030 1 327 . 1 1 43 43 ASP HB3 H 1 2.80 0.02 . 2 . . . . . . . . . 5030 1 328 . 1 1 43 43 ASP C C 13 176.80 0.05 . 1 . . . . . . . . . 5030 1 329 . 1 1 43 43 ASP CA C 13 54.10 0.20 . 1 . . . . . . . . . 5030 1 330 . 1 1 43 43 ASP CB C 13 41.20 0.40 . 1 . . . . . . . . . 5030 1 331 . 1 1 43 43 ASP N N 15 118.90 0.10 . 1 . . . . . . . . . 5030 1 332 . 1 1 44 44 MET H H 1 8.50 0.01 . 1 . . . . . . . . . 5030 1 333 . 1 1 44 44 MET HA H 1 4.51 0.02 . 1 . . . . . . . . . 5030 1 334 . 1 1 44 44 MET HB2 H 1 2.13 0.02 . 2 . . . . . . . . . 5030 1 335 . 1 1 44 44 MET HB3 H 1 2.05 0.02 . 2 . . . . . . . . . 5030 1 336 . 1 1 44 44 MET C C 13 178.76 0.05 . 1 . . . . . . . . . 5030 1 337 . 1 1 44 44 MET CA C 13 56.10 0.20 . 1 . . . . . . . . . 5030 1 338 . 1 1 44 44 MET CB C 13 32.20 0.40 . 1 . . . . . . . . . 5030 1 339 . 1 1 44 44 MET N N 15 123.10 0.10 . 1 . . . . . . . . . 5030 1 340 . 1 1 45 45 SER H H 1 8.58 0.01 . 1 . . . . . . . . . 5030 1 341 . 1 1 45 45 SER HA H 1 4.03 0.02 . 1 . . . . . . . . . 5030 1 342 . 1 1 45 45 SER HB2 H 1 4.26 0.02 . 1 . . . . . . . . . 5030 1 343 . 1 1 45 45 SER HB3 H 1 4.26 0.02 . 1 . . . . . . . . . 5030 1 344 . 1 1 45 45 SER C C 13 176.33 0.05 . 1 . . . . . . . . . 5030 1 345 . 1 1 45 45 SER CA C 13 62.60 0.20 . 1 . . . . . . . . . 5030 1 346 . 1 1 45 45 SER CB C 13 61.40 0.20 . 1 . . . . . . . . . 5030 1 347 . 1 1 45 45 SER N N 15 118.80 0.10 . 1 . . . . . . . . . 5030 1 348 . 1 1 46 46 GLN H H 1 8.41 0.01 . 1 . . . . . . . . . 5030 1 349 . 1 1 46 46 GLN HA H 1 4.32 0.02 . 1 . . . . . . . . . 5030 1 350 . 1 1 46 46 GLN HB2 H 1 2.13 0.02 . 2 . . . . . . . . . 5030 1 351 . 1 1 46 46 GLN HB3 H 1 2.22 0.02 . 2 . . . . . . . . . 5030 1 352 . 1 1 46 46 GLN C C 13 177.89 0.05 . 1 . . . . . . . . . 5030 1 353 . 1 1 46 46 GLN CA C 13 57.60 0.20 . 1 . . . . . . . . . 5030 1 354 . 1 1 46 46 GLN CB C 13 28.80 0.40 . 1 . . . . . . . . . 5030 1 355 . 1 1 46 46 GLN N N 15 121.00 0.10 . 1 . . . . . . . . . 5030 1 356 . 1 1 47 47 LEU H H 1 7.93 0.01 . 1 . . . . . . . . . 5030 1 357 . 1 1 47 47 LEU HA H 1 4.35 0.02 . 1 . . . . . . . . . 5030 1 358 . 1 1 47 47 LEU HB2 H 1 1.76 0.02 . 2 . . . . . . . . . 5030 1 359 . 1 1 47 47 LEU HB3 H 1 1.87 0.02 . 2 . . . . . . . . . 5030 1 360 . 1 1 47 47 LEU C C 13 178.70 0.05 . 1 . . . . . . . . . 5030 1 361 . 1 1 47 47 LEU CA C 13 56.10 0.20 . 1 . . . . . . . . . 5030 1 362 . 1 1 47 47 LEU CB C 13 42.30 0.40 . 1 . . . . . . . . . 5030 1 363 . 1 1 47 47 LEU N N 15 119.00 0.10 . 1 . . . . . . . . . 5030 1 364 . 1 1 48 48 GLY H H 1 8.29 0.01 . 1 . . . . . . . . . 5030 1 365 . 1 1 48 48 GLY HA2 H 1 3.70 0.02 . 1 . . . . . . . . . 5030 1 366 . 1 1 48 48 GLY HA3 H 1 4.18 0.02 . 1 . . . . . . . . . 5030 1 367 . 1 1 48 48 GLY C C 13 176.42 0.05 . 1 . . . . . . . . . 5030 1 368 . 1 1 48 48 GLY CA C 13 48.20 0.20 . 1 . . . . . . . . . 5030 1 369 . 1 1 48 48 GLY N N 15 110.30 0.10 . 1 . . . . . . . . . 5030 1 370 . 1 1 49 49 CYS H H 1 8.23 0.01 . 1 . . . . . . . . . 5030 1 371 . 1 1 49 49 CYS HA H 1 4.29 0.02 . 1 . . . . . . . . . 5030 1 372 . 1 1 49 49 CYS HB2 H 1 2.59 0.02 . 2 . . . . . . . . . 5030 1 373 . 1 1 49 49 CYS HB3 H 1 2.72 0.02 . 2 . . . . . . . . . 5030 1 374 . 1 1 49 49 CYS C C 13 177.90 0.05 . 1 . . . . . . . . . 5030 1 375 . 1 1 49 49 CYS CA C 13 58.50 0.20 . 1 . . . . . . . . . 5030 1 376 . 1 1 49 49 CYS CB C 13 37.50 0.40 . 1 . . . . . . . . . 5030 1 377 . 1 1 49 49 CYS N N 15 120.00 0.10 . 1 . . . . . . . . . 5030 1 378 . 1 1 50 50 LEU H H 1 8.03 0.01 . 1 . . . . . . . . . 5030 1 379 . 1 1 50 50 LEU HA H 1 4.00 0.02 . 1 . . . . . . . . . 5030 1 380 . 1 1 50 50 LEU HB2 H 1 1.54 0.02 . 2 . . . . . . . . . 5030 1 381 . 1 1 50 50 LEU HB3 H 1 2.30 0.02 . 2 . . . . . . . . . 5030 1 382 . 1 1 50 50 LEU C C 13 177.70 0.05 . 1 . . . . . . . . . 5030 1 383 . 1 1 50 50 LEU CA C 13 58.80 0.20 . 1 . . . . . . . . . 5030 1 384 . 1 1 50 50 LEU CB C 13 40.50 0.40 . 1 . . . . . . . . . 5030 1 385 . 1 1 50 50 LEU N N 15 125.60 0.10 . 1 . . . . . . . . . 5030 1 386 . 1 1 51 51 LYS H H 1 8.25 0.01 . 1 . . . . . . . . . 5030 1 387 . 1 1 51 51 LYS HA H 1 3.84 0.02 . 1 . . . . . . . . . 5030 1 388 . 1 1 51 51 LYS HB2 H 1 1.82 0.02 . 1 . . . . . . . . . 5030 1 389 . 1 1 51 51 LYS HB3 H 1 1.82 0.02 . 1 . . . . . . . . . 5030 1 390 . 1 1 51 51 LYS C C 13 178.62 0.05 . 1 . . . . . . . . . 5030 1 391 . 1 1 51 51 LYS CA C 13 60.30 0.20 . 1 . . . . . . . . . 5030 1 392 . 1 1 51 51 LYS CB C 13 29.50 0.40 . 1 . . . . . . . . . 5030 1 393 . 1 1 51 51 LYS N N 15 118.90 0.10 . 1 . . . . . . . . . 5030 1 394 . 1 1 52 52 ALA H H 1 8.38 0.01 . 1 . . . . . . . . . 5030 1 395 . 1 1 52 52 ALA HA H 1 4.10 0.02 . 1 . . . . . . . . . 5030 1 396 . 1 1 52 52 ALA HB1 H 1 1.42 0.02 . 1 . . . . . . . . . 5030 1 397 . 1 1 52 52 ALA HB2 H 1 1.42 0.02 . 1 . . . . . . . . . 5030 1 398 . 1 1 52 52 ALA HB3 H 1 1.42 0.02 . 1 . . . . . . . . . 5030 1 399 . 1 1 52 52 ALA C C 13 178.50 0.05 . 1 . . . . . . . . . 5030 1 400 . 1 1 52 52 ALA CA C 13 54.70 0.20 . 1 . . . . . . . . . 5030 1 401 . 1 1 52 52 ALA CB C 13 18.50 0.40 . 1 . . . . . . . . . 5030 1 402 . 1 1 52 52 ALA N N 15 119.90 0.10 . 1 . . . . . . . . . 5030 1 403 . 1 1 53 53 CYS H H 1 8.07 0.01 . 1 . . . . . . . . . 5030 1 404 . 1 1 53 53 CYS HA H 1 4.17 0.02 . 1 . . . . . . . . . 5030 1 405 . 1 1 53 53 CYS HB2 H 1 3.52 0.02 . 2 . . . . . . . . . 5030 1 406 . 1 1 53 53 CYS HB3 H 1 3.26 0.02 . 2 . . . . . . . . . 5030 1 407 . 1 1 53 53 CYS C C 13 177.10 0.05 . 1 . . . . . . . . . 5030 1 408 . 1 1 53 53 CYS CA C 13 60.60 0.20 . 1 . . . . . . . . . 5030 1 409 . 1 1 53 53 CYS CB C 13 38.20 0.40 . 1 . . . . . . . . . 5030 1 410 . 1 1 53 53 CYS N N 15 118.60 0.10 . 1 . . . . . . . . . 5030 1 411 . 1 1 54 54 VAL H H 1 8.14 0.01 . 1 . . . . . . . . . 5030 1 412 . 1 1 54 54 VAL HA H 1 3.38 0.02 . 1 . . . . . . . . . 5030 1 413 . 1 1 54 54 VAL HB H 1 2.31 0.02 . 1 . . . . . . . . . 5030 1 414 . 1 1 54 54 VAL C C 13 177.30 0.05 . 1 . . . . . . . . . 5030 1 415 . 1 1 54 54 VAL CA C 13 67.00 0.20 . 1 . . . . . . . . . 5030 1 416 . 1 1 54 54 VAL CB C 13 31.90 0.40 . 1 . . . . . . . . . 5030 1 417 . 1 1 54 54 VAL N N 15 123.30 0.10 . 1 . . . . . . . . . 5030 1 418 . 1 1 55 55 MET H H 1 8.26 0.01 . 1 . . . . . . . . . 5030 1 419 . 1 1 55 55 MET HA H 1 3.79 0.02 . 1 . . . . . . . . . 5030 1 420 . 1 1 55 55 MET HB2 H 1 2.21 0.02 . 2 . . . . . . . . . 5030 1 421 . 1 1 55 55 MET HB3 H 1 1.93 0.02 . 2 . . . . . . . . . 5030 1 422 . 1 1 55 55 MET C C 13 179.00 0.05 . 1 . . . . . . . . . 5030 1 423 . 1 1 55 55 MET CA C 13 59.70 0.20 . 1 . . . . . . . . . 5030 1 424 . 1 1 55 55 MET CB C 13 34.00 0.40 . 1 . . . . . . . . . 5030 1 425 . 1 1 55 55 MET N N 15 117.40 0.10 . 1 . . . . . . . . . 5030 1 426 . 1 1 56 56 LYS H H 1 8.55 0.01 . 1 . . . . . . . . . 5030 1 427 . 1 1 56 56 LYS HA H 1 4.53 0.02 . 1 . . . . . . . . . 5030 1 428 . 1 1 56 56 LYS HB2 H 1 2.05 0.02 . 1 . . . . . . . . . 5030 1 429 . 1 1 56 56 LYS HB3 H 1 2.05 0.02 . 1 . . . . . . . . . 5030 1 430 . 1 1 56 56 LYS C C 13 181.00 0.05 . 1 . . . . . . . . . 5030 1 431 . 1 1 56 56 LYS CA C 13 59.70 0.20 . 1 . . . . . . . . . 5030 1 432 . 1 1 56 56 LYS CB C 13 32.20 0.40 . 1 . . . . . . . . . 5030 1 433 . 1 1 56 56 LYS N N 15 120.30 0.10 . 1 . . . . . . . . . 5030 1 434 . 1 1 57 57 ARG H H 1 8.21 0.01 . 1 . . . . . . . . . 5030 1 435 . 1 1 57 57 ARG HA H 1 4.08 0.02 . 1 . . . . . . . . . 5030 1 436 . 1 1 57 57 ARG HB2 H 1 2.04 0.02 . 2 . . . . . . . . . 5030 1 437 . 1 1 57 57 ARG HB3 H 1 1.99 0.02 . 2 . . . . . . . . . 5030 1 438 . 1 1 57 57 ARG C C 13 179.10 0.05 . 1 . . . . . . . . . 5030 1 439 . 1 1 57 57 ARG CA C 13 60.60 0.20 . 1 . . . . . . . . . 5030 1 440 . 1 1 57 57 ARG CB C 13 30.60 0.40 . 1 . . . . . . . . . 5030 1 441 . 1 1 57 57 ARG N N 15 122.00 0.10 . 1 . . . . . . . . . 5030 1 442 . 1 1 58 58 ILE H H 1 7.80 0.01 . 1 . . . . . . . . . 5030 1 443 . 1 1 58 58 ILE HA H 1 4.56 0.02 . 1 . . . . . . . . . 5030 1 444 . 1 1 58 58 ILE HB H 1 2.34 0.02 . 1 . . . . . . . . . 5030 1 445 . 1 1 58 58 ILE C C 13 174.90 0.05 . 1 . . . . . . . . . 5030 1 446 . 1 1 58 58 ILE CA C 13 61.40 0.20 . 1 . . . . . . . . . 5030 1 447 . 1 1 58 58 ILE CB C 13 37.60 0.40 . 1 . . . . . . . . . 5030 1 448 . 1 1 58 58 ILE N N 15 109.80 0.10 . 1 . . . . . . . . . 5030 1 449 . 1 1 59 59 GLU H H 1 7.50 0.01 . 1 . . . . . . . . . 5030 1 450 . 1 1 59 59 GLU HA H 1 3.78 0.02 . 1 . . . . . . . . . 5030 1 451 . 1 1 59 59 GLU HB2 H 1 2.13 0.02 . 2 . . . . . . . . . 5030 1 452 . 1 1 59 59 GLU HB3 H 1 2.09 0.02 . 2 . . . . . . . . . 5030 1 453 . 1 1 59 59 GLU C C 13 174.50 0.05 . 1 . . . . . . . . . 5030 1 454 . 1 1 59 59 GLU CA C 13 58.20 0.20 . 1 . . . . . . . . . 5030 1 455 . 1 1 59 59 GLU CB C 13 26.20 0.40 . 1 . . . . . . . . . 5030 1 456 . 1 1 59 59 GLU N N 15 111.60 0.10 . 1 . . . . . . . . . 5030 1 457 . 1 1 60 60 MET H H 1 8.21 0.01 . 1 . . . . . . . . . 5030 1 458 . 1 1 60 60 MET HA H 1 4.84 0.02 . 1 . . . . . . . . . 5030 1 459 . 1 1 60 60 MET HB2 H 1 1.68 0.02 . 2 . . . . . . . . . 5030 1 460 . 1 1 60 60 MET HB3 H 1 2.23 0.02 . 2 . . . . . . . . . 5030 1 461 . 1 1 60 60 MET C C 13 173.20 0.05 . 1 . . . . . . . . . 5030 1 462 . 1 1 60 60 MET CA C 13 56.80 0.20 . 1 . . . . . . . . . 5030 1 463 . 1 1 60 60 MET CB C 13 34.20 0.40 . 1 . . . . . . . . . 5030 1 464 . 1 1 60 60 MET N N 15 116.10 0.10 . 1 . . . . . . . . . 5030 1 465 . 1 1 61 61 LEU H H 1 6.67 0.01 . 1 . . . . . . . . . 5030 1 466 . 1 1 61 61 LEU HA H 1 5.23 0.02 . 1 . . . . . . . . . 5030 1 467 . 1 1 61 61 LEU HB2 H 1 0.96 0.02 . 2 . . . . . . . . . 5030 1 468 . 1 1 61 61 LEU HB3 H 1 1.42 0.02 . 2 . . . . . . . . . 5030 1 469 . 1 1 61 61 LEU C C 13 175.00 0.05 . 1 . . . . . . . . . 5030 1 470 . 1 1 61 61 LEU CA C 13 52.70 0.20 . 1 . . . . . . . . . 5030 1 471 . 1 1 61 61 LEU CB C 13 46.00 0.40 . 1 . . . . . . . . . 5030 1 472 . 1 1 61 61 LEU N N 15 120.20 0.10 . 1 . . . . . . . . . 5030 1 473 . 1 1 62 62 LYS H H 1 8.73 0.01 . 1 . . . . . . . . . 5030 1 474 . 1 1 62 62 LYS HA H 1 4.50 0.02 . 1 . . . . . . . . . 5030 1 475 . 1 1 62 62 LYS HB2 H 1 1.81 0.02 . 1 . . . . . . . . . 5030 1 476 . 1 1 62 62 LYS HB3 H 1 1.81 0.02 . 1 . . . . . . . . . 5030 1 477 . 1 1 62 62 LYS C C 13 176.50 0.05 . 1 . . . . . . . . . 5030 1 478 . 1 1 62 62 LYS CA C 13 55.70 0.20 . 1 . . . . . . . . . 5030 1 479 . 1 1 62 62 LYS CB C 13 33.60 0.40 . 1 . . . . . . . . . 5030 1 480 . 1 1 62 62 LYS N N 15 126.50 0.10 . 1 . . . . . . . . . 5030 1 481 . 1 1 63 63 GLY H H 1 9.04 0.01 . 1 . . . . . . . . . 5030 1 482 . 1 1 63 63 GLY HA2 H 1 4.19 0.02 . 1 . . . . . . . . . 5030 1 483 . 1 1 63 63 GLY HA3 H 1 3.67 0.02 . 1 . . . . . . . . . 5030 1 484 . 1 1 63 63 GLY C C 13 173.90 0.05 . 1 . . . . . . . . . 5030 1 485 . 1 1 63 63 GLY CA C 13 47.00 0.20 . 1 . . . . . . . . . 5030 1 486 . 1 1 63 63 GLY N N 15 117.70 0.10 . 1 . . . . . . . . . 5030 1 487 . 1 1 64 64 THR H H 1 8.60 0.01 . 1 . . . . . . . . . 5030 1 488 . 1 1 64 64 THR HA H 1 4.24 0.02 . 1 . . . . . . . . . 5030 1 489 . 1 1 64 64 THR HB H 1 4.58 0.02 . 1 . . . . . . . . . 5030 1 490 . 1 1 64 64 THR C C 13 173.00 0.05 . 1 . . . . . . . . . 5030 1 491 . 1 1 64 64 THR CA C 13 60.80 0.20 . 1 . . . . . . . . . 5030 1 492 . 1 1 64 64 THR CB C 13 68.50 0.40 . 1 . . . . . . . . . 5030 1 493 . 1 1 64 64 THR N N 15 116.60 0.10 . 1 . . . . . . . . . 5030 1 494 . 1 1 65 65 GLU H H 1 7.98 0.01 . 1 . . . . . . . . . 5030 1 495 . 1 1 65 65 GLU HA H 1 4.42 0.02 . 1 . . . . . . . . . 5030 1 496 . 1 1 65 65 GLU HB2 H 1 1.88 0.02 . 2 . . . . . . . . . 5030 1 497 . 1 1 65 65 GLU HB3 H 1 2.12 0.02 . 2 . . . . . . . . . 5030 1 498 . 1 1 65 65 GLU C C 13 174.10 0.05 . 1 . . . . . . . . . 5030 1 499 . 1 1 65 65 GLU CA C 13 55.40 0.20 . 1 . . . . . . . . . 5030 1 500 . 1 1 65 65 GLU CB C 13 32.20 0.40 . 1 . . . . . . . . . 5030 1 501 . 1 1 65 65 GLU N N 15 122.00 0.10 . 1 . . . . . . . . . 5030 1 502 . 1 1 66 66 LEU H H 1 7.82 0.01 . 1 . . . . . . . . . 5030 1 503 . 1 1 66 66 LEU HA H 1 5.25 0.02 . 1 . . . . . . . . . 5030 1 504 . 1 1 66 66 LEU HB2 H 1 0.94 0.02 . 2 . . . . . . . . . 5030 1 505 . 1 1 66 66 LEU HB3 H 1 1.58 0.02 . 2 . . . . . . . . . 5030 1 506 . 1 1 66 66 LEU C C 13 176.40 0.05 . 1 . . . . . . . . . 5030 1 507 . 1 1 66 66 LEU CA C 13 52.90 0.20 . 1 . . . . . . . . . 5030 1 508 . 1 1 66 66 LEU CB C 13 45.20 0.40 . 1 . . . . . . . . . 5030 1 509 . 1 1 66 66 LEU N N 15 121.60 0.10 . 1 . . . . . . . . . 5030 1 510 . 1 1 67 67 TYR H H 1 9.14 0.01 . 1 . . . . . . . . . 5030 1 511 . 1 1 67 67 TYR HA H 1 4.55 0.02 . 1 . . . . . . . . . 5030 1 512 . 1 1 67 67 TYR HB2 H 1 3.16 0.02 . 2 . . . . . . . . . 5030 1 513 . 1 1 67 67 TYR HB3 H 1 2.81 0.02 . 2 . . . . . . . . . 5030 1 514 . 1 1 67 67 TYR C C 13 175.00 0.05 . 1 . . . . . . . . . 5030 1 515 . 1 1 67 67 TYR CA C 13 56.80 0.20 . 1 . . . . . . . . . 5030 1 516 . 1 1 67 67 TYR CB C 13 40.20 0.40 . 1 . . . . . . . . . 5030 1 517 . 1 1 67 67 TYR N N 15 122.00 0.10 . 1 . . . . . . . . . 5030 1 518 . 1 1 68 68 VAL H H 1 8.07 0.01 . 1 . . . . . . . . . 5030 1 519 . 1 1 68 68 VAL HA H 1 3.91 0.02 . 1 . . . . . . . . . 5030 1 520 . 1 1 68 68 VAL HB H 1 1.75 0.02 . 1 . . . . . . . . . 5030 1 521 . 1 1 68 68 VAL C C 13 177.00 0.05 . 1 . . . . . . . . . 5030 1 522 . 1 1 68 68 VAL CA C 13 62.80 0.20 . 1 . . . . . . . . . 5030 1 523 . 1 1 68 68 VAL CB C 13 33.30 0.40 . 1 . . . . . . . . . 5030 1 524 . 1 1 68 68 VAL N N 15 117.90 0.10 . 1 . . . . . . . . . 5030 1 525 . 1 1 69 69 GLU H H 1 8.91 0.01 . 1 . . . . . . . . . 5030 1 526 . 1 1 69 69 GLU HA H 1 3.83 0.02 . 1 . . . . . . . . . 5030 1 527 . 1 1 69 69 GLU HB2 H 1 2.01 0.02 . 2 . . . . . . . . . 5030 1 528 . 1 1 69 69 GLU HB3 H 1 2.19 0.02 . 2 . . . . . . . . . 5030 1 529 . 1 1 69 69 GLU C C 13 176.10 0.05 . 1 . . . . . . . . . 5030 1 530 . 1 1 69 69 GLU CA C 13 63.00 0.20 . 1 . . . . . . . . . 5030 1 531 . 1 1 69 69 GLU CB C 13 26.40 0.40 . 1 . . . . . . . . . 5030 1 532 . 1 1 69 69 GLU N N 15 123.90 0.10 . 1 . . . . . . . . . 5030 1 533 . 1 1 70 70 PRO HA H 1 4.37 0.02 . 1 . . . . . . . . . 5030 1 534 . 1 1 70 70 PRO HB2 H 1 1.52 0.02 . 2 . . . . . . . . . 5030 1 535 . 1 1 70 70 PRO HB3 H 1 2.60 0.02 . 2 . . . . . . . . . 5030 1 536 . 1 1 70 70 PRO C C 13 179.53 0.05 . 1 . . . . . . . . . 5030 1 537 . 1 1 70 70 PRO CA C 13 65.20 0.20 . 1 . . . . . . . . . 5030 1 538 . 1 1 70 70 PRO CB C 13 32.40 0.40 . 1 . . . . . . . . . 5030 1 539 . 1 1 71 71 VAL H H 1 7.46 0.01 . 1 . . . . . . . . . 5030 1 540 . 1 1 71 71 VAL HA H 1 3.82 0.02 . 1 . . . . . . . . . 5030 1 541 . 1 1 71 71 VAL HB H 1 2.37 0.02 . 1 . . . . . . . . . 5030 1 542 . 1 1 71 71 VAL C C 13 178.06 0.05 . 1 . . . . . . . . . 5030 1 543 . 1 1 71 71 VAL CA C 13 65.20 0.20 . 1 . . . . . . . . . 5030 1 544 . 1 1 71 71 VAL CB C 13 31.60 0.40 . 1 . . . . . . . . . 5030 1 545 . 1 1 71 71 VAL N N 15 117.60 0.10 . 1 . . . . . . . . . 5030 1 546 . 1 1 72 72 TYR H H 1 8.28 0.01 . 1 . . . . . . . . . 5030 1 547 . 1 1 72 72 TYR HA H 1 4.43 0.02 . 1 . . . . . . . . . 5030 1 548 . 1 1 72 72 TYR HB2 H 1 3.67 0.02 . 2 . . . . . . . . . 5030 1 549 . 1 1 72 72 TYR HB3 H 1 3.18 0.02 . 2 . . . . . . . . . 5030 1 550 . 1 1 72 72 TYR C C 13 177.83 0.05 . 1 . . . . . . . . . 5030 1 551 . 1 1 72 72 TYR CA C 13 58.50 0.20 . 1 . . . . . . . . . 5030 1 552 . 1 1 72 72 TYR CB C 13 35.60 0.40 . 1 . . . . . . . . . 5030 1 553 . 1 1 72 72 TYR N N 15 120.60 0.10 . 1 . . . . . . . . . 5030 1 554 . 1 1 73 73 LYS H H 1 7.80 0.01 . 1 . . . . . . . . . 5030 1 555 . 1 1 73 73 LYS HA H 1 4.05 0.02 . 1 . . . . . . . . . 5030 1 556 . 1 1 73 73 LYS HB2 H 1 1.98 0.02 . 1 . . . . . . . . . 5030 1 557 . 1 1 73 73 LYS HB3 H 1 1.98 0.02 . 1 . . . . . . . . . 5030 1 558 . 1 1 73 73 LYS C C 13 177.98 0.05 . 1 . . . . . . . . . 5030 1 559 . 1 1 73 73 LYS CA C 13 59.80 0.20 . 1 . . . . . . . . . 5030 1 560 . 1 1 73 73 LYS CB C 13 32.00 0.40 . 1 . . . . . . . . . 5030 1 561 . 1 1 73 73 LYS N N 15 117.20 0.10 . 1 . . . . . . . . . 5030 1 562 . 1 1 74 74 MET H H 1 7.14 0.01 . 1 . . . . . . . . . 5030 1 563 . 1 1 74 74 MET HA H 1 3.51 0.02 . 1 . . . . . . . . . 5030 1 564 . 1 1 74 74 MET HB2 H 1 1.92 0.02 . 2 . . . . . . . . . 5030 1 565 . 1 1 74 74 MET HB3 H 1 1.26 0.02 . 2 . . . . . . . . . 5030 1 566 . 1 1 74 74 MET C C 13 177.80 0.05 . 1 . . . . . . . . . 5030 1 567 . 1 1 74 74 MET CA C 13 58.50 0.20 . 1 . . . . . . . . . 5030 1 568 . 1 1 74 74 MET CB C 13 30.00 0.40 . 1 . . . . . . . . . 5030 1 569 . 1 1 74 74 MET N N 15 118.40 0.10 . 1 . . . . . . . . . 5030 1 570 . 1 1 75 75 ILE H H 1 8.83 0.01 . 1 . . . . . . . . . 5030 1 571 . 1 1 75 75 ILE HA H 1 3.63 0.02 . 1 . . . . . . . . . 5030 1 572 . 1 1 75 75 ILE HB H 1 2.09 0.02 . 1 . . . . . . . . . 5030 1 573 . 1 1 75 75 ILE C C 13 177.25 0.05 . 1 . . . . . . . . . 5030 1 574 . 1 1 75 75 ILE CA C 13 65.90 0.20 . 1 . . . . . . . . . 5030 1 575 . 1 1 75 75 ILE CB C 13 38.60 0.40 . 1 . . . . . . . . . 5030 1 576 . 1 1 75 75 ILE N N 15 121.50 0.10 . 1 . . . . . . . . . 5030 1 577 . 1 1 76 76 GLU H H 1 7.98 0.01 . 1 . . . . . . . . . 5030 1 578 . 1 1 76 76 GLU HA H 1 3.77 0.02 . 1 . . . . . . . . . 5030 1 579 . 1 1 76 76 GLU HB2 H 1 2.21 0.02 . 2 . . . . . . . . . 5030 1 580 . 1 1 76 76 GLU HB3 H 1 2.08 0.02 . 2 . . . . . . . . . 5030 1 581 . 1 1 76 76 GLU C C 13 177.60 0.05 . 1 . . . . . . . . . 5030 1 582 . 1 1 76 76 GLU CA C 13 58.90 0.20 . 1 . . . . . . . . . 5030 1 583 . 1 1 76 76 GLU CB C 13 29.20 0.40 . 1 . . . . . . . . . 5030 1 584 . 1 1 76 76 GLU N N 15 116.40 0.10 . 1 . . . . . . . . . 5030 1 585 . 1 1 77 77 VAL H H 1 7.24 0.01 . 1 . . . . . . . . . 5030 1 586 . 1 1 77 77 VAL HA H 1 3.94 0.02 . 1 . . . . . . . . . 5030 1 587 . 1 1 77 77 VAL HB H 1 2.14 0.02 . 1 . . . . . . . . . 5030 1 588 . 1 1 77 77 VAL C C 13 178.60 0.05 . 1 . . . . . . . . . 5030 1 589 . 1 1 77 77 VAL CA C 13 65.50 0.20 . 1 . . . . . . . . . 5030 1 590 . 1 1 77 77 VAL CB C 13 32.40 0.20 . 1 . . . . . . . . . 5030 1 591 . 1 1 77 77 VAL N N 15 117.10 0.10 . 1 . . . . . . . . . 5030 1 592 . 1 1 78 78 VAL H H 1 8.66 0.01 . 1 . . . . . . . . . 5030 1 593 . 1 1 78 78 VAL HA H 1 3.33 0.02 . 1 . . . . . . . . . 5030 1 594 . 1 1 78 78 VAL HB H 1 1.32 0.02 . 1 . . . . . . . . . 5030 1 595 . 1 1 78 78 VAL C C 13 176.80 0.05 . 1 . . . . . . . . . 5030 1 596 . 1 1 78 78 VAL CA C 13 66.50 0.20 . 1 . . . . . . . . . 5030 1 597 . 1 1 78 78 VAL CB C 13 31.70 0.40 . 1 . . . . . . . . . 5030 1 598 . 1 1 78 78 VAL N N 15 120.30 0.10 . 1 . . . . . . . . . 5030 1 599 . 1 1 79 79 HIS H H 1 8.29 0.01 . 1 . . . . . . . . . 5030 1 600 . 1 1 79 79 HIS HA H 1 4.59 0.02 . 1 . . . . . . . . . 5030 1 601 . 1 1 79 79 HIS HB2 H 1 3.03 0.02 . 2 . . . . . . . . . 5030 1 602 . 1 1 79 79 HIS HB3 H 1 3.40 0.02 . 2 . . . . . . . . . 5030 1 603 . 1 1 79 79 HIS C C 13 172.80 0.05 . 1 . . . . . . . . . 5030 1 604 . 1 1 79 79 HIS CA C 13 54.90 0.20 . 1 . . . . . . . . . 5030 1 605 . 1 1 79 79 HIS CB C 13 27.10 0.40 . 1 . . . . . . . . . 5030 1 606 . 1 1 79 79 HIS N N 15 114.80 0.10 . 1 . . . . . . . . . 5030 1 607 . 1 1 80 80 ALA H H 1 6.54 0.01 . 1 . . . . . . . . . 5030 1 608 . 1 1 80 80 ALA HA H 1 3.98 0.02 . 1 . . . . . . . . . 5030 1 609 . 1 1 80 80 ALA HB1 H 1 1.53 0.02 . 1 . . . . . . . . . 5030 1 610 . 1 1 80 80 ALA HB2 H 1 1.53 0.02 . 1 . . . . . . . . . 5030 1 611 . 1 1 80 80 ALA HB3 H 1 1.53 0.02 . 1 . . . . . . . . . 5030 1 612 . 1 1 80 80 ALA C C 13 178.60 0.05 . 1 . . . . . . . . . 5030 1 613 . 1 1 80 80 ALA CA C 13 54.10 0.20 . 1 . . . . . . . . . 5030 1 614 . 1 1 80 80 ALA CB C 13 19.00 0.40 . 1 . . . . . . . . . 5030 1 615 . 1 1 80 80 ALA N N 15 119.90 0.10 . 1 . . . . . . . . . 5030 1 616 . 1 1 81 81 GLY H H 1 8.91 0.01 . 1 . . . . . . . . . 5030 1 617 . 1 1 81 81 GLY HA2 H 1 3.70 0.02 . 1 . . . . . . . . . 5030 1 618 . 1 1 81 81 GLY HA3 H 1 4.34 0.02 . 1 . . . . . . . . . 5030 1 619 . 1 1 81 81 GLY C C 13 174.00 0.05 . 1 . . . . . . . . . 5030 1 620 . 1 1 81 81 GLY CA C 13 44.80 0.20 . 1 . . . . . . . . . 5030 1 621 . 1 1 81 81 GLY N N 15 109.00 0.10 . 1 . . . . . . . . . 5030 1 622 . 1 1 82 82 ASN H H 1 7.61 0.01 . 1 . . . . . . . . . 5030 1 623 . 1 1 82 82 ASN HA H 1 5.00 0.02 . 1 . . . . . . . . . 5030 1 624 . 1 1 82 82 ASN HB2 H 1 2.73 0.02 . 2 . . . . . . . . . 5030 1 625 . 1 1 82 82 ASN HB3 H 1 3.14 0.02 . 2 . . . . . . . . . 5030 1 626 . 1 1 82 82 ASN C C 13 174.00 0.05 . 1 . . . . . . . . . 5030 1 627 . 1 1 82 82 ASN CA C 13 52.20 0.20 . 1 . . . . . . . . . 5030 1 628 . 1 1 82 82 ASN CB C 13 39.40 0.40 . 1 . . . . . . . . . 5030 1 629 . 1 1 82 82 ASN N N 15 118.70 0.10 . 1 . . . . . . . . . 5030 1 630 . 1 1 83 83 ALA H H 1 8.74 0.01 . 1 . . . . . . . . . 5030 1 631 . 1 1 83 83 ALA HA H 1 4.00 0.02 . 1 . . . . . . . . . 5030 1 632 . 1 1 83 83 ALA HB1 H 1 1.46 0.02 . 1 . . . . . . . . . 5030 1 633 . 1 1 83 83 ALA HB2 H 1 1.46 0.02 . 1 . . . . . . . . . 5030 1 634 . 1 1 83 83 ALA HB3 H 1 1.46 0.02 . 1 . . . . . . . . . 5030 1 635 . 1 1 83 83 ALA C C 13 180.00 0.05 . 1 . . . . . . . . . 5030 1 636 . 1 1 83 83 ALA CA C 13 55.40 0.20 . 1 . . . . . . . . . 5030 1 637 . 1 1 83 83 ALA CB C 13 18.90 0.40 . 1 . . . . . . . . . 5030 1 638 . 1 1 83 83 ALA N N 15 127.00 0.10 . 1 . . . . . . . . . 5030 1 639 . 1 1 84 84 ASP H H 1 8.26 0.01 . 1 . . . . . . . . . 5030 1 640 . 1 1 84 84 ASP HA H 1 4.41 0.02 . 1 . . . . . . . . . 5030 1 641 . 1 1 84 84 ASP HB2 H 1 2.71 0.02 . 2 . . . . . . . . . 5030 1 642 . 1 1 84 84 ASP HB3 H 1 2.78 0.02 . 2 . . . . . . . . . 5030 1 643 . 1 1 84 84 ASP C C 13 178.80 0.05 . 1 . . . . . . . . . 5030 1 644 . 1 1 84 84 ASP CA C 13 57.10 0.20 . 1 . . . . . . . . . 5030 1 645 . 1 1 84 84 ASP CB C 13 40.00 0.40 . 1 . . . . . . . . . 5030 1 646 . 1 1 84 84 ASP N N 15 118.20 0.10 . 1 . . . . . . . . . 5030 1 647 . 1 1 85 85 ASP H H 1 7.95 0.01 . 1 . . . . . . . . . 5030 1 648 . 1 1 85 85 ASP HA H 1 4.33 0.02 . 1 . . . . . . . . . 5030 1 649 . 1 1 85 85 ASP HB2 H 1 2.34 0.02 . 2 . . . . . . . . . 5030 1 650 . 1 1 85 85 ASP HB3 H 1 2.87 0.02 . 2 . . . . . . . . . 5030 1 651 . 1 1 85 85 ASP C C 13 177.50 0.05 . 1 . . . . . . . . . 5030 1 652 . 1 1 85 85 ASP CA C 13 56.70 0.20 . 1 . . . . . . . . . 5030 1 653 . 1 1 85 85 ASP CB C 13 39.40 0.40 . 1 . . . . . . . . . 5030 1 654 . 1 1 85 85 ASP N N 15 122.20 0.10 . 1 . . . . . . . . . 5030 1 655 . 1 1 86 86 ILE H H 1 8.00 0.01 . 1 . . . . . . . . . 5030 1 656 . 1 1 86 86 ILE HA H 1 3.17 0.02 . 1 . . . . . . . . . 5030 1 657 . 1 1 86 86 ILE HB H 1 1.81 0.02 . 1 . . . . . . . . . 5030 1 658 . 1 1 86 86 ILE C C 13 177.00 0.05 . 1 . . . . . . . . . 5030 1 659 . 1 1 86 86 ILE CA C 13 66.30 0.20 . 1 . . . . . . . . . 5030 1 660 . 1 1 86 86 ILE CB C 13 37.80 0.40 . 1 . . . . . . . . . 5030 1 661 . 1 1 86 86 ILE N N 15 119.10 0.10 . 1 . . . . . . . . . 5030 1 662 . 1 1 87 87 GLN H H 1 7.57 0.01 . 1 . . . . . . . . . 5030 1 663 . 1 1 87 87 GLN HA H 1 3.87 0.02 . 1 . . . . . . . . . 5030 1 664 . 1 1 87 87 GLN HB2 H 1 2.15 0.02 . 1 . . . . . . . . . 5030 1 665 . 1 1 87 87 GLN HB3 H 1 2.15 0.02 . 1 . . . . . . . . . 5030 1 666 . 1 1 87 87 GLN C C 13 178.90 0.05 . 1 . . . . . . . . . 5030 1 667 . 1 1 87 87 GLN CA C 13 58.90 0.20 . 1 . . . . . . . . . 5030 1 668 . 1 1 87 87 GLN CB C 13 28.70 0.40 . 1 . . . . . . . . . 5030 1 669 . 1 1 87 87 GLN N N 15 116.60 0.10 . 1 . . . . . . . . . 5030 1 670 . 1 1 88 88 LEU H H 1 7.87 0.01 . 1 . . . . . . . . . 5030 1 671 . 1 1 88 88 LEU HA H 1 4.04 0.02 . 1 . . . . . . . . . 5030 1 672 . 1 1 88 88 LEU HB2 H 1 1.78 0.02 . 2 . . . . . . . . . 5030 1 673 . 1 1 88 88 LEU HB3 H 1 1.89 0.02 . 2 . . . . . . . . . 5030 1 674 . 1 1 88 88 LEU C C 13 179.80 0.05 . 1 . . . . . . . . . 5030 1 675 . 1 1 88 88 LEU CA C 13 58.10 0.20 . 1 . . . . . . . . . 5030 1 676 . 1 1 88 88 LEU CB C 13 42.40 0.40 . 1 . . . . . . . . . 5030 1 677 . 1 1 88 88 LEU N N 15 121.80 0.10 . 1 . . . . . . . . . 5030 1 678 . 1 1 89 89 VAL H H 1 8.68 0.01 . 1 . . . . . . . . . 5030 1 679 . 1 1 89 89 VAL HA H 1 3.44 0.02 . 1 . . . . . . . . . 5030 1 680 . 1 1 89 89 VAL HB H 1 1.73 0.02 . 1 . . . . . . . . . 5030 1 681 . 1 1 89 89 VAL C C 13 178.30 0.05 . 1 . . . . . . . . . 5030 1 682 . 1 1 89 89 VAL CA C 13 66.20 0.20 . 1 . . . . . . . . . 5030 1 683 . 1 1 89 89 VAL CB C 13 30.80 0.40 . 1 . . . . . . . . . 5030 1 684 . 1 1 89 89 VAL N N 15 120.20 0.10 . 1 . . . . . . . . . 5030 1 685 . 1 1 90 90 LYS H H 1 8.49 0.01 . 1 . . . . . . . . . 5030 1 686 . 1 1 90 90 LYS HA H 1 3.87 0.02 . 1 . . . . . . . . . 5030 1 687 . 1 1 90 90 LYS HB2 H 1 1.76 0.02 . 2 . . . . . . . . . 5030 1 688 . 1 1 90 90 LYS HB3 H 1 1.51 0.02 . 2 . . . . . . . . . 5030 1 689 . 1 1 90 90 LYS C C 13 179.00 0.05 . 1 . . . . . . . . . 5030 1 690 . 1 1 90 90 LYS CA C 13 61.60 0.20 . 1 . . . . . . . . . 5030 1 691 . 1 1 90 90 LYS CB C 13 32.40 0.40 . 1 . . . . . . . . . 5030 1 692 . 1 1 90 90 LYS N N 15 120.60 0.10 . 1 . . . . . . . . . 5030 1 693 . 1 1 91 91 GLY H H 1 7.54 0.01 . 1 . . . . . . . . . 5030 1 694 . 1 1 91 91 GLY HA2 H 1 3.98 0.02 . 1 . . . . . . . . . 5030 1 695 . 1 1 91 91 GLY HA3 H 1 3.95 0.02 . 1 . . . . . . . . . 5030 1 696 . 1 1 91 91 GLY C C 13 176.80 0.05 . 1 . . . . . . . . . 5030 1 697 . 1 1 91 91 GLY CA C 13 47.40 0.20 . 1 . . . . . . . . . 5030 1 698 . 1 1 91 91 GLY N N 15 105.30 0.10 . 1 . . . . . . . . . 5030 1 699 . 1 1 92 92 ILE H H 1 7.60 0.01 . 1 . . . . . . . . . 5030 1 700 . 1 1 92 92 ILE HA H 1 3.57 0.02 . 1 . . . . . . . . . 5030 1 701 . 1 1 92 92 ILE HB H 1 1.83 0.02 . 1 . . . . . . . . . 5030 1 702 . 1 1 92 92 ILE C C 13 177.30 0.05 . 1 . . . . . . . . . 5030 1 703 . 1 1 92 92 ILE CA C 13 65.40 0.20 . 1 . . . . . . . . . 5030 1 704 . 1 1 92 92 ILE CB C 13 38.00 0.40 . 1 . . . . . . . . . 5030 1 705 . 1 1 92 92 ILE N N 15 124.70 0.10 . 1 . . . . . . . . . 5030 1 706 . 1 1 93 93 ALA H H 1 8.76 0.01 . 1 . . . . . . . . . 5030 1 707 . 1 1 93 93 ALA HA H 1 4.23 0.02 . 1 . . . . . . . . . 5030 1 708 . 1 1 93 93 ALA HB1 H 1 1.75 0.02 . 1 . . . . . . . . . 5030 1 709 . 1 1 93 93 ALA HB2 H 1 1.75 0.02 . 1 . . . . . . . . . 5030 1 710 . 1 1 93 93 ALA HB3 H 1 1.75 0.02 . 1 . . . . . . . . . 5030 1 711 . 1 1 93 93 ALA C C 13 181.00 0.05 . 1 . . . . . . . . . 5030 1 712 . 1 1 93 93 ALA CA C 13 54.50 0.20 . 1 . . . . . . . . . 5030 1 713 . 1 1 93 93 ALA CB C 13 18.90 0.40 . 1 . . . . . . . . . 5030 1 714 . 1 1 93 93 ALA N N 15 121.00 0.10 . 1 . . . . . . . . . 5030 1 715 . 1 1 94 94 ASN H H 1 7.99 0.01 . 1 . . . . . . . . . 5030 1 716 . 1 1 94 94 ASN HA H 1 4.62 0.02 . 1 . . . . . . . . . 5030 1 717 . 1 1 94 94 ASN HB2 H 1 2.97 0.02 . 2 . . . . . . . . . 5030 1 718 . 1 1 94 94 ASN HB3 H 1 3.18 0.02 . 2 . . . . . . . . . 5030 1 719 . 1 1 94 94 ASN C C 13 178.20 0.05 . 1 . . . . . . . . . 5030 1 720 . 1 1 94 94 ASN CA C 13 56.20 0.20 . 1 . . . . . . . . . 5030 1 721 . 1 1 94 94 ASN CB C 13 39.50 0.40 . 1 . . . . . . . . . 5030 1 722 . 1 1 94 94 ASN N N 15 114.40 0.10 . 1 . . . . . . . . . 5030 1 723 . 1 1 95 95 GLU H H 1 8.60 0.01 . 1 . . . . . . . . . 5030 1 724 . 1 1 95 95 GLU HA H 1 4.10 0.02 . 1 . . . . . . . . . 5030 1 725 . 1 1 95 95 GLU HB2 H 1 2.01 0.02 . 2 . . . . . . . . . 5030 1 726 . 1 1 95 95 GLU HB3 H 1 2.22 0.02 . 2 . . . . . . . . . 5030 1 727 . 1 1 95 95 GLU C C 13 180.10 0.05 . 1 . . . . . . . . . 5030 1 728 . 1 1 95 95 GLU CA C 13 59.90 0.20 . 1 . . . . . . . . . 5030 1 729 . 1 1 95 95 GLU CB C 13 29.50 0.40 . 1 . . . . . . . . . 5030 1 730 . 1 1 95 95 GLU N N 15 122.40 0.10 . 1 . . . . . . . . . 5030 1 731 . 1 1 96 96 CYS H H 1 8.55 0.01 . 1 . . . . . . . . . 5030 1 732 . 1 1 96 96 CYS HA H 1 4.66 0.02 . 1 . . . . . . . . . 5030 1 733 . 1 1 96 96 CYS HB2 H 1 2.45 0.02 . 2 . . . . . . . . . 5030 1 734 . 1 1 96 96 CYS HB3 H 1 2.67 0.02 . 2 . . . . . . . . . 5030 1 735 . 1 1 96 96 CYS C C 13 177.20 0.05 . 1 . . . . . . . . . 5030 1 736 . 1 1 96 96 CYS CA C 13 56.20 0.20 . 1 . . . . . . . . . 5030 1 737 . 1 1 96 96 CYS CB C 13 37.50 0.40 . 1 . . . . . . . . . 5030 1 738 . 1 1 96 96 CYS N N 15 115.10 0.10 . 1 . . . . . . . . . 5030 1 739 . 1 1 97 97 ILE H H 1 7.92 0.01 . 1 . . . . . . . . . 5030 1 740 . 1 1 97 97 ILE HA H 1 3.89 0.02 . 1 . . . . . . . . . 5030 1 741 . 1 1 97 97 ILE HB H 1 2.44 0.02 . 1 . . . . . . . . . 5030 1 742 . 1 1 97 97 ILE C C 13 178.30 0.05 . 1 . . . . . . . . . 5030 1 743 . 1 1 97 97 ILE CA C 13 65.50 0.20 . 1 . . . . . . . . . 5030 1 744 . 1 1 97 97 ILE CB C 13 39.30 0.40 . 1 . . . . . . . . . 5030 1 745 . 1 1 97 97 ILE N N 15 123.20 0.10 . 1 . . . . . . . . . 5030 1 746 . 1 1 98 98 GLU H H 1 7.47 0.01 . 1 . . . . . . . . . 5030 1 747 . 1 1 98 98 GLU HA H 1 4.05 0.02 . 1 . . . . . . . . . 5030 1 748 . 1 1 98 98 GLU HB2 H 1 2.22 0.02 . 1 . . . . . . . . . 5030 1 749 . 1 1 98 98 GLU HB3 H 1 2.22 0.02 . 1 . . . . . . . . . 5030 1 750 . 1 1 98 98 GLU C C 13 178.70 0.05 . 1 . . . . . . . . . 5030 1 751 . 1 1 98 98 GLU CA C 13 58.60 0.20 . 1 . . . . . . . . . 5030 1 752 . 1 1 98 98 GLU CB C 13 29.30 0.40 . 1 . . . . . . . . . 5030 1 753 . 1 1 98 98 GLU N N 15 117.60 0.10 . 1 . . . . . . . . . 5030 1 754 . 1 1 99 99 ASN H H 1 7.68 0.01 . 1 . . . . . . . . . 5030 1 755 . 1 1 99 99 ASN HA H 1 4.54 0.02 . 1 . . . . . . . . . 5030 1 756 . 1 1 99 99 ASN HB2 H 1 2.82 0.02 . 2 . . . . . . . . . 5030 1 757 . 1 1 99 99 ASN HB3 H 1 2.86 0.02 . 2 . . . . . . . . . 5030 1 758 . 1 1 99 99 ASN C C 13 175.50 0.05 . 1 . . . . . . . . . 5030 1 759 . 1 1 99 99 ASN CA C 13 55.20 0.20 . 1 . . . . . . . . . 5030 1 760 . 1 1 99 99 ASN CB C 13 39.00 0.40 . 1 . . . . . . . . . 5030 1 761 . 1 1 99 99 ASN N N 15 116.00 0.10 . 1 . . . . . . . . . 5030 1 762 . 1 1 100 100 ALA H H 1 7.53 0.01 . 1 . . . . . . . . . 5030 1 763 . 1 1 100 100 ALA HA H 1 4.39 0.02 . 1 . . . . . . . . . 5030 1 764 . 1 1 100 100 ALA HB1 H 1 1.54 0.02 . 1 . . . . . . . . . 5030 1 765 . 1 1 100 100 ALA HB2 H 1 1.54 0.02 . 1 . . . . . . . . . 5030 1 766 . 1 1 100 100 ALA HB3 H 1 1.54 0.02 . 1 . . . . . . . . . 5030 1 767 . 1 1 100 100 ALA C C 13 176.40 0.05 . 1 . . . . . . . . . 5030 1 768 . 1 1 100 100 ALA CA C 13 51.90 0.20 . 1 . . . . . . . . . 5030 1 769 . 1 1 100 100 ALA CB C 13 19.90 0.40 . 1 . . . . . . . . . 5030 1 770 . 1 1 100 100 ALA N N 15 119.20 0.10 . 1 . . . . . . . . . 5030 1 771 . 1 1 101 101 LYS H H 1 7.32 0.01 . 1 . . . . . . . . . 5030 1 772 . 1 1 101 101 LYS HA H 1 4.16 0.02 . 1 . . . . . . . . . 5030 1 773 . 1 1 101 101 LYS HB2 H 1 1.96 0.02 . 2 . . . . . . . . . 5030 1 774 . 1 1 101 101 LYS HB3 H 1 1.91 0.02 . 2 . . . . . . . . . 5030 1 775 . 1 1 101 101 LYS C C 13 177.30 0.05 . 1 . . . . . . . . . 5030 1 776 . 1 1 101 101 LYS CA C 13 58.20 0.20 . 1 . . . . . . . . . 5030 1 777 . 1 1 101 101 LYS CB C 13 32.40 0.40 . 1 . . . . . . . . . 5030 1 778 . 1 1 101 101 LYS N N 15 118.60 0.10 . 1 . . . . . . . . . 5030 1 779 . 1 1 102 102 GLY H H 1 8.70 0.01 . 1 . . . . . . . . . 5030 1 780 . 1 1 102 102 GLY HA2 H 1 4.18 0.02 . 1 . . . . . . . . . 5030 1 781 . 1 1 102 102 GLY HA3 H 1 3.78 0.02 . 1 . . . . . . . . . 5030 1 782 . 1 1 102 102 GLY C C 13 174.40 0.05 . 1 . . . . . . . . . 5030 1 783 . 1 1 102 102 GLY CA C 13 45.00 0.20 . 1 . . . . . . . . . 5030 1 784 . 1 1 102 102 GLY N N 15 111.20 0.10 . 1 . . . . . . . . . 5030 1 785 . 1 1 103 103 GLU H H 1 7.50 0.01 . 1 . . . . . . . . . 5030 1 786 . 1 1 103 103 GLU HA H 1 4.43 0.02 . 1 . . . . . . . . . 5030 1 787 . 1 1 103 103 GLU HB2 H 1 2.00 0.02 . 2 . . . . . . . . . 5030 1 788 . 1 1 103 103 GLU HB3 H 1 2.10 0.02 . 2 . . . . . . . . . 5030 1 789 . 1 1 103 103 GLU C C 13 176.20 0.05 . 1 . . . . . . . . . 5030 1 790 . 1 1 103 103 GLU CA C 13 55.40 0.20 . 1 . . . . . . . . . 5030 1 791 . 1 1 103 103 GLU CB C 13 30.80 0.40 . 1 . . . . . . . . . 5030 1 792 . 1 1 103 103 GLU N N 15 119.90 0.10 . 1 . . . . . . . . . 5030 1 793 . 1 1 104 104 THR H H 1 8.23 0.01 . 1 . . . . . . . . . 5030 1 794 . 1 1 104 104 THR HA H 1 4.45 0.02 . 1 . . . . . . . . . 5030 1 795 . 1 1 104 104 THR HB H 1 4.38 0.02 . 1 . . . . . . . . . 5030 1 796 . 1 1 104 104 THR C C 13 174.00 0.05 . 1 . . . . . . . . . 5030 1 797 . 1 1 104 104 THR CA C 13 61.60 0.20 . 1 . . . . . . . . . 5030 1 798 . 1 1 104 104 THR CB C 13 70.00 0.40 . 1 . . . . . . . . . 5030 1 799 . 1 1 104 104 THR N N 15 112.00 0.10 . 1 . . . . . . . . . 5030 1 800 . 1 1 105 105 ASP H H 1 8.42 0.01 . 1 . . . . . . . . . 5030 1 801 . 1 1 105 105 ASP HA H 1 4.84 0.02 . 1 . . . . . . . . . 5030 1 802 . 1 1 105 105 ASP HB2 H 1 2.61 0.02 . 2 . . . . . . . . . 5030 1 803 . 1 1 105 105 ASP HB3 H 1 2.93 0.02 . 2 . . . . . . . . . 5030 1 804 . 1 1 105 105 ASP C C 13 177.20 0.05 . 1 . . . . . . . . . 5030 1 805 . 1 1 105 105 ASP CA C 13 53.00 0.20 . 1 . . . . . . . . . 5030 1 806 . 1 1 105 105 ASP CB C 13 43.00 0.40 . 1 . . . . . . . . . 5030 1 807 . 1 1 105 105 ASP N N 15 123.60 0.10 . 1 . . . . . . . . . 5030 1 808 . 1 1 106 106 GLU H H 1 9.18 0.01 . 1 . . . . . . . . . 5030 1 809 . 1 1 106 106 GLU HA H 1 3.87 0.02 . 1 . . . . . . . . . 5030 1 810 . 1 1 106 106 GLU HB2 H 1 2.01 0.02 . 2 . . . . . . . . . 5030 1 811 . 1 1 106 106 GLU HB3 H 1 2.20 0.02 . 2 . . . . . . . . . 5030 1 812 . 1 1 106 106 GLU C C 13 177.11 0.05 . 1 . . . . . . . . . 5030 1 813 . 1 1 106 106 GLU CA C 13 59.00 0.20 . 1 . . . . . . . . . 5030 1 814 . 1 1 106 106 GLU CB C 13 29.70 0.40 . 1 . . . . . . . . . 5030 1 815 . 1 1 106 106 GLU N N 15 126.10 0.10 . 1 . . . . . . . . . 5030 1 816 . 1 1 107 107 CYS H H 1 8.36 0.01 . 1 . . . . . . . . . 5030 1 817 . 1 1 107 107 CYS HA H 1 4.22 0.02 . 1 . . . . . . . . . 5030 1 818 . 1 1 107 107 CYS HB2 H 1 2.81 0.02 . 2 . . . . . . . . . 5030 1 819 . 1 1 107 107 CYS HB3 H 1 3.78 0.02 . 2 . . . . . . . . . 5030 1 820 . 1 1 107 107 CYS C C 13 175.86 0.05 . 1 . . . . . . . . . 5030 1 821 . 1 1 107 107 CYS CA C 13 60.10 0.20 . 1 . . . . . . . . . 5030 1 822 . 1 1 107 107 CYS CB C 13 30.00 0.40 . 1 . . . . . . . . . 5030 1 823 . 1 1 107 107 CYS N N 15 117.90 0.10 . 1 . . . . . . . . . 5030 1 824 . 1 1 108 108 ASN H H 1 7.82 0.01 . 1 . . . . . . . . . 5030 1 825 . 1 1 108 108 ASN HA H 1 4.67 0.02 . 1 . . . . . . . . . 5030 1 826 . 1 1 108 108 ASN HB2 H 1 2.81 0.02 . 2 . . . . . . . . . 5030 1 827 . 1 1 108 108 ASN HB3 H 1 3.07 0.02 . 2 . . . . . . . . . 5030 1 828 . 1 1 108 108 ASN C C 13 178.42 0.05 . 1 . . . . . . . . . 5030 1 829 . 1 1 108 108 ASN CA C 13 55.20 0.20 . 1 . . . . . . . . . 5030 1 830 . 1 1 108 108 ASN CB C 13 37.70 0.40 . 1 . . . . . . . . . 5030 1 831 . 1 1 108 108 ASN N N 15 118.70 0.10 . 1 . . . . . . . . . 5030 1 832 . 1 1 109 109 ILE H H 1 8.20 0.01 . 1 . . . . . . . . . 5030 1 833 . 1 1 109 109 ILE HA H 1 3.44 0.02 . 1 . . . . . . . . . 5030 1 834 . 1 1 109 109 ILE HB H 1 1.99 0.02 . 1 . . . . . . . . . 5030 1 835 . 1 1 109 109 ILE C C 13 177.40 0.05 . 1 . . . . . . . . . 5030 1 836 . 1 1 109 109 ILE CA C 13 67.10 0.20 . 1 . . . . . . . . . 5030 1 837 . 1 1 109 109 ILE CB C 13 37.50 0.40 . 1 . . . . . . . . . 5030 1 838 . 1 1 109 109 ILE N N 15 122.00 0.10 . 1 . . . . . . . . . 5030 1 839 . 1 1 110 110 GLY H H 1 8.11 0.01 . 1 . . . . . . . . . 5030 1 840 . 1 1 110 110 GLY HA2 H 1 3.88 0.02 . 1 . . . . . . . . . 5030 1 841 . 1 1 110 110 GLY HA3 H 1 3.83 0.02 . 1 . . . . . . . . . 5030 1 842 . 1 1 110 110 GLY C C 13 175.92 0.05 . 1 . . . . . . . . . 5030 1 843 . 1 1 110 110 GLY CA C 13 47.50 0.20 . 1 . . . . . . . . . 5030 1 844 . 1 1 110 110 GLY N N 15 104.80 0.10 . 1 . . . . . . . . . 5030 1 845 . 1 1 111 111 ASN H H 1 7.52 0.01 . 1 . . . . . . . . . 5030 1 846 . 1 1 111 111 ASN HA H 1 4.47 0.02 . 1 . . . . . . . . . 5030 1 847 . 1 1 111 111 ASN HB2 H 1 2.85 0.02 . 1 . . . . . . . . . 5030 1 848 . 1 1 111 111 ASN HB3 H 1 2.85 0.02 . 1 . . . . . . . . . 5030 1 849 . 1 1 111 111 ASN C C 13 176.16 0.05 . 1 . . . . . . . . . 5030 1 850 . 1 1 111 111 ASN CA C 13 55.90 0.20 . 1 . . . . . . . . . 5030 1 851 . 1 1 111 111 ASN CB C 13 38.50 0.40 . 1 . . . . . . . . . 5030 1 852 . 1 1 111 111 ASN N N 15 119.50 0.10 . 1 . . . . . . . . . 5030 1 853 . 1 1 112 112 LYS H H 1 8.79 0.01 . 1 . . . . . . . . . 5030 1 854 . 1 1 112 112 LYS HA H 1 4.07 0.02 . 1 . . . . . . . . . 5030 1 855 . 1 1 112 112 LYS HB2 H 1 1.92 0.02 . 2 . . . . . . . . . 5030 1 856 . 1 1 112 112 LYS HB3 H 1 1.76 0.02 . 2 . . . . . . . . . 5030 1 857 . 1 1 112 112 LYS C C 13 180.18 0.05 . 1 . . . . . . . . . 5030 1 858 . 1 1 112 112 LYS CA C 13 59.40 0.20 . 1 . . . . . . . . . 5030 1 859 . 1 1 112 112 LYS CB C 13 33.00 0.40 . 1 . . . . . . . . . 5030 1 860 . 1 1 112 112 LYS N N 15 119.20 0.10 . 1 . . . . . . . . . 5030 1 861 . 1 1 113 113 TYR H H 1 8.85 0.01 . 1 . . . . . . . . . 5030 1 862 . 1 1 113 113 TYR HA H 1 3.95 0.02 . 1 . . . . . . . . . 5030 1 863 . 1 1 113 113 TYR HB2 H 1 2.79 0.02 . 2 . . . . . . . . . 5030 1 864 . 1 1 113 113 TYR HB3 H 1 2.86 0.02 . 2 . . . . . . . . . 5030 1 865 . 1 1 113 113 TYR C C 13 176.70 0.05 . 1 . . . . . . . . . 5030 1 866 . 1 1 113 113 TYR CA C 13 63.20 0.20 . 1 . . . . . . . . . 5030 1 867 . 1 1 113 113 TYR CB C 13 39.50 0.40 . 1 . . . . . . . . . 5030 1 868 . 1 1 113 113 TYR N N 15 118.00 0.10 . 1 . . . . . . . . . 5030 1 869 . 1 1 114 114 THR H H 1 7.44 0.01 . 1 . . . . . . . . . 5030 1 870 . 1 1 114 114 THR HA H 1 3.67 0.02 . 1 . . . . . . . . . 5030 1 871 . 1 1 114 114 THR HB H 1 4.35 0.02 . 1 . . . . . . . . . 5030 1 872 . 1 1 114 114 THR C C 13 175.62 0.05 . 1 . . . . . . . . . 5030 1 873 . 1 1 114 114 THR CA C 13 66.90 0.20 . 1 . . . . . . . . . 5030 1 874 . 1 1 114 114 THR CB C 13 68.80 0.40 . 1 . . . . . . . . . 5030 1 875 . 1 1 114 114 THR N N 15 111.50 0.10 . 1 . . . . . . . . . 5030 1 876 . 1 1 115 115 ASP H H 1 8.54 0.01 . 1 . . . . . . . . . 5030 1 877 . 1 1 115 115 ASP HA H 1 4.32 0.02 . 1 . . . . . . . . . 5030 1 878 . 1 1 115 115 ASP HB2 H 1 2.56 0.02 . 2 . . . . . . . . . 5030 1 879 . 1 1 115 115 ASP HB3 H 1 2.71 0.02 . 2 . . . . . . . . . 5030 1 880 . 1 1 115 115 ASP C C 13 178.16 0.05 . 1 . . . . . . . . . 5030 1 881 . 1 1 115 115 ASP CA C 13 57.30 0.20 . 1 . . . . . . . . . 5030 1 882 . 1 1 115 115 ASP CB C 13 39.50 0.40 . 1 . . . . . . . . . 5030 1 883 . 1 1 115 115 ASP N N 15 120.90 0.10 . 1 . . . . . . . . . 5030 1 884 . 1 1 116 116 CYS H H 1 7.00 0.01 . 1 . . . . . . . . . 5030 1 885 . 1 1 116 116 CYS HA H 1 4.14 0.02 . 1 . . . . . . . . . 5030 1 886 . 1 1 116 116 CYS HB2 H 1 3.05 0.02 . 2 . . . . . . . . . 5030 1 887 . 1 1 116 116 CYS HB3 H 1 3.27 0.02 . 2 . . . . . . . . . 5030 1 888 . 1 1 116 116 CYS C C 13 173.95 0.05 . 1 . . . . . . . . . 5030 1 889 . 1 1 116 116 CYS CA C 13 59.30 0.20 . 1 . . . . . . . . . 5030 1 890 . 1 1 116 116 CYS CB C 13 36.50 0.40 . 1 . . . . . . . . . 5030 1 891 . 1 1 116 116 CYS N N 15 118.40 0.10 . 1 . . . . . . . . . 5030 1 892 . 1 1 117 117 TYR H H 1 7.95 0.01 . 1 . . . . . . . . . 5030 1 893 . 1 1 117 117 TYR HA H 1 3.52 0.02 . 1 . . . . . . . . . 5030 1 894 . 1 1 117 117 TYR HB2 H 1 2.34 0.02 . 2 . . . . . . . . . 5030 1 895 . 1 1 117 117 TYR HB3 H 1 3.05 0.02 . 2 . . . . . . . . . 5030 1 896 . 1 1 117 117 TYR C C 13 177.35 0.05 . 1 . . . . . . . . . 5030 1 897 . 1 1 117 117 TYR CA C 13 61.00 0.20 . 1 . . . . . . . . . 5030 1 898 . 1 1 117 117 TYR CB C 13 40.30 0.40 . 1 . . . . . . . . . 5030 1 899 . 1 1 117 117 TYR N N 15 123.50 0.10 . 1 . . . . . . . . . 5030 1 900 . 1 1 118 118 ILE H H 1 8.44 0.01 . 1 . . . . . . . . . 5030 1 901 . 1 1 118 118 ILE HA H 1 3.78 0.02 . 1 . . . . . . . . . 5030 1 902 . 1 1 118 118 ILE HB H 1 2.01 0.02 . 1 . . . . . . . . . 5030 1 903 . 1 1 118 118 ILE C C 13 178.06 0.05 . 1 . . . . . . . . . 5030 1 904 . 1 1 118 118 ILE CA C 13 63.90 0.20 . 1 . . . . . . . . . 5030 1 905 . 1 1 118 118 ILE CB C 13 38.50 0.40 . 1 . . . . . . . . . 5030 1 906 . 1 1 118 118 ILE N N 15 115.00 0.10 . 1 . . . . . . . . . 5030 1 907 . 1 1 119 119 GLU H H 1 7.86 0.01 . 1 . . . . . . . . . 5030 1 908 . 1 1 119 119 GLU HA H 1 4.00 0.02 . 1 . . . . . . . . . 5030 1 909 . 1 1 119 119 GLU HB2 H 1 2.08 0.02 . 2 . . . . . . . . . 5030 1 910 . 1 1 119 119 GLU HB3 H 1 2.14 0.02 . 2 . . . . . . . . . 5030 1 911 . 1 1 119 119 GLU C C 13 179.45 0.05 . 1 . . . . . . . . . 5030 1 912 . 1 1 119 119 GLU CA C 13 59.20 0.20 . 1 . . . . . . . . . 5030 1 913 . 1 1 119 119 GLU CB C 13 29.40 0.40 . 1 . . . . . . . . . 5030 1 914 . 1 1 119 119 GLU N N 15 119.50 0.10 . 1 . . . . . . . . . 5030 1 915 . 1 1 120 120 LYS H H 1 7.80 0.01 . 1 . . . . . . . . . 5030 1 916 . 1 1 120 120 LYS HA H 1 4.01 0.02 . 1 . . . . . . . . . 5030 1 917 . 1 1 120 120 LYS HB2 H 1 1.76 0.02 . 2 . . . . . . . . . 5030 1 918 . 1 1 120 120 LYS HB3 H 1 1.58 0.02 . 2 . . . . . . . . . 5030 1 919 . 1 1 120 120 LYS C C 13 178.77 0.05 . 1 . . . . . . . . . 5030 1 920 . 1 1 120 120 LYS CA C 13 58.60 0.20 . 1 . . . . . . . . . 5030 1 921 . 1 1 120 120 LYS CB C 13 33.30 0.40 . 1 . . . . . . . . . 5030 1 922 . 1 1 120 120 LYS N N 15 116.10 0.10 . 1 . . . . . . . . . 5030 1 923 . 1 1 121 121 LEU H H 1 8.14 0.01 . 1 . . . . . . . . . 5030 1 924 . 1 1 121 121 LEU HA H 1 3.78 0.02 . 1 . . . . . . . . . 5030 1 925 . 1 1 121 121 LEU HB2 H 1 1.14 0.02 . 2 . . . . . . . . . 5030 1 926 . 1 1 121 121 LEU HB3 H 1 1.34 0.02 . 2 . . . . . . . . . 5030 1 927 . 1 1 121 121 LEU C C 13 177.53 0.05 . 1 . . . . . . . . . 5030 1 928 . 1 1 121 121 LEU CA C 13 57.30 0.20 . 1 . . . . . . . . . 5030 1 929 . 1 1 121 121 LEU CB C 13 42.60 0.40 . 1 . . . . . . . . . 5030 1 930 . 1 1 121 121 LEU N N 15 120.50 0.10 . 1 . . . . . . . . . 5030 1 931 . 1 1 122 122 PHE H H 1 7.43 0.01 . 1 . . . . . . . . . 5030 1 932 . 1 1 122 122 PHE HA H 1 4.90 0.02 . 1 . . . . . . . . . 5030 1 933 . 1 1 122 122 PHE HB2 H 1 2.95 0.02 . 2 . . . . . . . . . 5030 1 934 . 1 1 122 122 PHE HB3 H 1 3.50 0.02 . 2 . . . . . . . . . 5030 1 935 . 1 1 122 122 PHE C C 13 175.40 0.05 . 1 . . . . . . . . . 5030 1 936 . 1 1 122 122 PHE CA C 13 56.20 0.20 . 1 . . . . . . . . . 5030 1 937 . 1 1 122 122 PHE CB C 13 38.60 0.40 . 1 . . . . . . . . . 5030 1 938 . 1 1 122 122 PHE N N 15 113.50 0.10 . 1 . . . . . . . . . 5030 1 939 . 1 1 123 123 SER H H 1 7.35 0.01 . 1 . . . . . . . . . 5030 1 940 . 1 1 123 123 SER HA H 1 4.36 0.02 . 1 . . . . . . . . . 5030 1 941 . 1 1 123 123 SER HB2 H 1 3.97 0.02 . 1 . . . . . . . . . 5030 1 942 . 1 1 123 123 SER HB3 H 1 3.97 0.02 . 1 . . . . . . . . . 5030 1 943 . 1 1 123 123 SER C C 13 178.76 0.05 . 1 . . . . . . . . . 5030 1 944 . 1 1 123 123 SER CA C 13 60.50 0.20 . 1 . . . . . . . . . 5030 1 945 . 1 1 123 123 SER CB C 13 64.80 0.40 . 1 . . . . . . . . . 5030 1 946 . 1 1 123 123 SER N N 15 120.90 0.10 . 1 . . . . . . . . . 5030 1 stop_ save_