data_4068 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4068 _Entry.Title ; Assignment of 1H, 13C, and 15N Signals of Turkey Ovomucoid Third Domain at pH 2.0 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1997-10-29 _Entry.Accession_date 1997-10-30 _Entry.Last_release_date 1998-05-01 _Entry.Original_release_date 1998-05-01 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Soheui Choe . . . 4068 2 Zeljko Dzakula . . . 4068 3 E. Kuloglu . Sonay . 4068 4 John Markley . L. . 4068 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4068 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 191 4068 '15N chemical shifts' 56 4068 '1H chemical shifts' 328 4068 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 . . 1998-05-01 1998-03-05 original author . 4068 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4068 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Choe, S., Dzakula, Z., Kuloglu, E. S., and Markley, J. L., "Assignment of 1H, 13C, and 15N Signals of Turkey Ovomucoid Third Domain at pH 2.0," J. Biomol. NMR, in press (1998). ; _Citation.Title 'Assignment of 1H, 13C, and IN Signals of Turkey Ovomucoid Third Domain at pH 2.0' _Citation.Status 'in press' _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year 1998 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Soheui Choe . . . 4068 1 2 Zeljko Dzakula . . . 4068 1 3 E. Kuloglu . Sonay . 4068 1 4 John Markley . L. . 4068 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'Donovan transition' 4068 1 'NMR assignments' 4068 1 'Proteinase inhibitor' 4068 1 'Turkey Ovomucoid' 4068 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_molecular_system _Assembly.Sf_category assembly _Assembly.Sf_framecode molecular_system _Assembly.Entry_ID 4068 _Assembly.ID 1 _Assembly.Name 'turkey ovomucoid third domain' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4068 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 OMTKY3 1 $OMTKY3 . . . native . . . . . 4068 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID OMTKY3 abbreviation 4068 1 'turkey ovomucoid third domain' system 4068 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID ; Ovomucoid third domains have potent inhibitory activity toward serine proteinases ; 4068 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_OMTKY3 _Entity.Sf_category entity _Entity.Sf_framecode OMTKY3 _Entity.Entry_ID 4068 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'turkey ovomucoid third domain' _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 ; LAAVSVDCSEYPKPACTLEY RPLCGSDNKTYGNKCNFCNA VVESNGTLTLSHFGKC ; _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 56 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 6000 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 1374 . "ovomucoid third domain" . . . . . 67.86 38 100.00 100.00 3.19e-18 . . . . 4068 1 2 no BMRB 1375 . "ovomucoid third domain" . . . . . 67.86 38 100.00 100.00 3.19e-18 . . . . 4068 1 3 no BMRB 42 . "ovomucoid third domain" . . . . . 100.00 56 100.00 100.00 7.49e-32 . . . . 4068 1 4 no PDB 1CHO . "Crystal And Molecular Structures Of The Complex Of Alpha- Chymotrypsin With Its Inhibitor Turkey Ovomucoid Third Domain At 1.8 " . . . . . 100.00 56 100.00 100.00 7.49e-32 . . . . 4068 1 5 no PDB 1CSO . "Crystal Structure Of The Omtky3 P1 Variant Omtky3-Ile18i In Complex With Sgpb" . . . . . 91.07 51 98.04 100.00 3.18e-28 . . . . 4068 1 6 no PDB 1CT0 . "Crystal Structure Of The Omtky3 P1 Variant Omtky3-Ser18i In Complex With Sgpb" . . . . . 91.07 51 98.04 98.04 1.37e-27 . . . . 4068 1 7 no PDB 1CT2 . "Crystal Structure Of The Omtky3 P1 Variant Omtky3-Thr18i In Complex With Sgpb" . . . . . 91.07 51 98.04 98.04 9.81e-28 . . . . 4068 1 8 no PDB 1CT4 . "Crystal Structure Of The Omtky3 P1 Variant Omtky3-Val18i In Complex With Sgpb" . . . . . 91.07 51 98.04 100.00 4.45e-28 . . . . 4068 1 9 no PDB 1DS2 . "Crystal Structure Of Sgpb:omtky3-Coo-Leu18i" . . . . . 91.07 51 98.04 98.04 1.15e-27 . . . . 4068 1 10 no PDB 1HJA . "Lys 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Alpha-Chymotrypsin" . . . . . 91.07 51 98.04 98.04 1.40e-27 . . . . 4068 1 11 no PDB 1IY5 . "Solution Structure Of Wild Type Omsvp3" . . . . . 96.43 54 98.15 100.00 2.38e-30 . . . . 4068 1 12 no PDB 1M8B . "Solution Structure Of The C State Of Turkey Ovomucoid At Ph 2.5" . . . . . 100.00 56 98.21 98.21 8.90e-31 . . . . 4068 1 13 no PDB 1M8C . "Solution Structure Of The T State Of Turkey Ovomucoid At Ph 2.5" . . . . . 100.00 56 98.21 98.21 8.90e-31 . . . . 4068 1 14 no PDB 1OMT . "Solution Structure Of Ovomucoid (Third Domain) From Domestic Turkey (298k, Ph 4.1) (Nmr, 50 Structures) (Standard Noesy Analysi" . . . . . 100.00 56 100.00 100.00 7.49e-32 . . . . 4068 1 15 no PDB 1OMU . "Solution Structure Of Ovomucoid (Third Domain) From Domestic Turkey (298k, Ph 4.1) (Nmr, 50 Structures) (Refined Model Using Ne" . . . . . 100.00 56 100.00 100.00 7.49e-32 . . . . 4068 1 16 no PDB 1PPF . "X-Ray Crystal Structure Of The Complex Of Human Leukocyte Elastase (Pmn Elastase) And The Third Domain Of The Turkey Ovomucoid " . . . . . 100.00 56 100.00 100.00 7.49e-32 . . . . 4068 1 17 no PDB 1R0R . "1.1 Angstrom Resolution Structure Of The Complex Between The Protein Inhibitor, Omtky3, And The Serine Protease, Subtilisin Car" . . . . . 91.07 51 100.00 100.00 1.77e-28 . . . . 4068 1 18 no PDB 1SGD . "Asp 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 6.5" . . . . . 91.07 51 98.04 98.04 2.24e-27 . . . . 4068 1 19 no PDB 1SGE . "Glu 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 6.5" . . . . . 91.07 51 98.04 98.04 1.65e-27 . . . . 4068 1 20 no PDB 1SGN . "Asn 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B" . . . . . 91.07 51 98.04 98.04 2.47e-27 . . . . 4068 1 21 no PDB 1SGP . "Ala 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B" . . . . . 91.07 51 98.04 98.04 9.40e-28 . . . . 4068 1 22 no PDB 1SGQ . "Gly 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B" . . . . . 91.07 51 98.04 98.04 2.55e-27 . . . . 4068 1 23 no PDB 1SGR . "Leu 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B" . . . . . 91.07 51 100.00 100.00 1.77e-28 . . . . 4068 1 24 no PDB 1SGY . "Tyr 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 6.5" . . . . . 91.07 51 98.04 98.04 1.14e-27 . . . . 4068 1 25 no PDB 1TUR . "Solution Structure Of Turkey Ovomucoid Third Domain As Determined From Nuclear Magnetic Resonance Data" . . . . . 100.00 56 100.00 100.00 7.49e-32 . . . . 4068 1 26 no PDB 1TUS . "Solution Structure Of Reactive-Site Hydrolyzed Turkey Ovomucoid Third Domain By Nuclear Magnetic Resonance And Distance Geometr" . . . . . 100.00 56 100.00 100.00 7.49e-32 . . . . 4068 1 27 no PDB 2GKR . "Crystal Structure Of The N-Terminally Truncated Omtky3- Del(1-5)" . . . . . 91.07 51 100.00 100.00 1.77e-28 . . . . 4068 1 28 no PDB 2GKT . "Crystal Structure Of The P14'-Ala32 Variant Of The N- Terminally Truncated Omtky3-Del(1-5)" . . . . . 91.07 51 98.04 98.04 7.09e-28 . . . . 4068 1 29 no PDB 2GKV . "Crystal Structure Of The Sgpb:p14'-Ala32 Omtky3-Del(1-5) Complex" . . . . . 91.07 51 98.04 98.04 7.09e-28 . . . . 4068 1 30 no PDB 2NU0 . "Molecular Structures Of The Complexes Of Sgpb With Omtky3 Aromatic P1 Variants Trp18i, His18i, Phe18i, And Tyr18i" . . . . . 91.07 51 98.04 98.04 7.01e-28 . . . . 4068 1 31 no PDB 2NU1 . "Molecular Structures Of The Complexes Of Sgpb With Omtky3 Aromatic P1 Variants Trp18i, His18i, Phe18i And Tyr18i" . . . . . 91.07 51 98.04 98.04 1.60e-27 . . . . 4068 1 32 no PDB 2NU2 . "Accommodation Of Positively-Charged Residues In A Hydrophobic Specificity Pocket: Crystal Structures Of Sgpb In Complex With Om" . . . . . 91.07 51 98.04 98.04 1.08e-27 . . . . 4068 1 33 no PDB 2NU3 . "Accommodation Of Positively-Charged Residues In A Hydrophobic Specificity Pocket: Crystal Structures Of Sgpb In Complex With Om" . . . . . 91.07 51 98.04 98.04 1.40e-27 . . . . 4068 1 34 no PDB 2NU4 . "Accommodation Of Positively-Charged Residues In A Hydrophobic Specificity Pocket: Crystal Structures Of Sgpb In Complex With Om" . . . . . 91.07 51 98.04 98.04 1.40e-27 . . . . 4068 1 35 no PDB 2OVO . "The Crystal And Molecular Structure Of The Third Domain Of Silver Pheasant Ovomucoid (Omsvp3)" . . . . . 100.00 56 98.21 100.00 1.04e-31 . . . . 4068 1 36 no PDB 2SGD . "Asp 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 10.7" . . . . . 91.07 51 98.04 98.04 2.24e-27 . . . . 4068 1 37 no PDB 2SGE . "Glu 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 10.7" . . . . . 91.07 51 98.04 98.04 1.65e-27 . . . . 4068 1 38 no PDB 2SGF . "Phe 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B" . . . . . 91.07 51 98.04 98.04 5.96e-28 . . . . 4068 1 39 no PDB 2SGP . "Pro 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 6.5" . . . . . 91.07 51 98.04 98.04 2.12e-27 . . . . 4068 1 40 no PDB 2SGQ . "Gln 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 6.5" . . . . . 91.07 51 98.04 98.04 9.20e-28 . . . . 4068 1 41 no PDB 3SGB . "Structure Of The Complex Of Streptomyces Griseus Protease B And The Third Domain Of The Turkey Ovomucoid Inhibitor At 1.8 Angst" . . . . . 100.00 56 100.00 100.00 7.49e-32 . . . . 4068 1 42 no PDB 3SGQ . "Gln 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Streptomyces Griseus Proteinase B At Ph 10.7" . . . . . 91.07 51 98.04 98.04 9.20e-28 . . . . 4068 1 43 no PDB 4OVO . "Refined X-Ray Crystal Structures Of The Reactive Site Modified Ovomucoid Inhibitor Third Domains From Silver Pheasant (Omsvp3(A" . . . . . 98.21 56 98.18 100.00 5.12e-31 . . . . 4068 1 44 no PIR A31445 . "ovomucoid, third domain - ruffed grouse (fragment) [Bonasa umbellus]" . . . . . 100.00 56 98.21 100.00 1.04e-31 . . . . 4068 1 45 no PIR B61588 . "ovomucoid (PSTI-type proteinase inhibitor), third domain - white-tailed ptarmigan [Lagopus leucura]" . . . . . 100.00 56 98.21 100.00 1.04e-31 . . . . 4068 1 46 no PIR C31438 . "ovomucoid, third domain - cheer pheasant (fragment) [Catreus wallichii]" . . . . . 100.00 56 98.21 100.00 1.04e-31 . . . . 4068 1 47 no PIR E31437 . "ovomucoid, third domain - silver pheasant (fragment) [Lophura nycthemera]" . . . . . 100.00 56 98.21 100.00 1.04e-31 . . . . 4068 1 48 no PIR E31442 . "ovomucoid, third domain - koklass pheasant (fragment) [Pucrasia macrolopha]" . . . . . 100.00 56 98.21 100.00 1.04e-31 . . . . 4068 1 49 no SP P05609 . "RecName: Full=Ovomucoid" . . . . . 100.00 56 98.21 100.00 2.94e-31 . . . . 4068 1 50 no SP P52245 . "RecName: Full=Ovomucoid" . . . . . 100.00 56 100.00 100.00 7.49e-32 . . . . 4068 1 51 no SP P52263 . "RecName: Full=Ovomucoid" . . . . . 96.43 54 98.15 100.00 6.13e-30 . . . . 4068 1 52 no SP P67944 . "RecName: Full=Ovomucoid" . . . . . 100.00 56 98.21 100.00 1.04e-31 . . . . 4068 1 53 no SP P67945 . "RecName: Full=Ovomucoid" . . . . . 100.00 56 98.21 100.00 1.04e-31 . . . . 4068 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID OMTKY3 abbreviation 4068 1 'turkey ovomucoid third domain' common 4068 1 stop_ loop_ _Entity_systematic_name.Name _Entity_systematic_name.Naming_system _Entity_systematic_name.Entry_ID _Entity_systematic_name.Entity_ID 'avian ovomucoid domains' . 4068 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . LEU . 4068 1 2 . ALA . 4068 1 3 . ALA . 4068 1 4 . VAL . 4068 1 5 . SER . 4068 1 6 . VAL . 4068 1 7 . ASP . 4068 1 8 . CYS . 4068 1 9 . SER . 4068 1 10 . GLU . 4068 1 11 . TYR . 4068 1 12 . PRO . 4068 1 13 . LYS . 4068 1 14 . PRO . 4068 1 15 . ALA . 4068 1 16 . CYS . 4068 1 17 . THR . 4068 1 18 . LEU . 4068 1 19 . GLU . 4068 1 20 . TYR . 4068 1 21 . ARG . 4068 1 22 . PRO . 4068 1 23 . LEU . 4068 1 24 . CYS . 4068 1 25 . GLY . 4068 1 26 . SER . 4068 1 27 . ASP . 4068 1 28 . ASN . 4068 1 29 . LYS . 4068 1 30 . THR . 4068 1 31 . TYR . 4068 1 32 . GLY . 4068 1 33 . ASN . 4068 1 34 . LYS . 4068 1 35 . CYS . 4068 1 36 . ASN . 4068 1 37 . PHE . 4068 1 38 . CYS . 4068 1 39 . ASN . 4068 1 40 . ALA . 4068 1 41 . VAL . 4068 1 42 . VAL . 4068 1 43 . GLU . 4068 1 44 . SER . 4068 1 45 . ASN . 4068 1 46 . GLY . 4068 1 47 . THR . 4068 1 48 . LEU . 4068 1 49 . THR . 4068 1 50 . LEU . 4068 1 51 . SER . 4068 1 52 . HIS . 4068 1 53 . PHE . 4068 1 54 . GLY . 4068 1 55 . LYS . 4068 1 56 . CYS . 4068 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . LEU 1 1 4068 1 . ALA 2 2 4068 1 . ALA 3 3 4068 1 . VAL 4 4 4068 1 . SER 5 5 4068 1 . VAL 6 6 4068 1 . ASP 7 7 4068 1 . CYS 8 8 4068 1 . SER 9 9 4068 1 . GLU 10 10 4068 1 . TYR 11 11 4068 1 . PRO 12 12 4068 1 . LYS 13 13 4068 1 . PRO 14 14 4068 1 . ALA 15 15 4068 1 . CYS 16 16 4068 1 . THR 17 17 4068 1 . LEU 18 18 4068 1 . GLU 19 19 4068 1 . TYR 20 20 4068 1 . ARG 21 21 4068 1 . PRO 22 22 4068 1 . LEU 23 23 4068 1 . CYS 24 24 4068 1 . GLY 25 25 4068 1 . SER 26 26 4068 1 . ASP 27 27 4068 1 . ASN 28 28 4068 1 . LYS 29 29 4068 1 . THR 30 30 4068 1 . TYR 31 31 4068 1 . GLY 32 32 4068 1 . ASN 33 33 4068 1 . LYS 34 34 4068 1 . CYS 35 35 4068 1 . ASN 36 36 4068 1 . PHE 37 37 4068 1 . CYS 38 38 4068 1 . ASN 39 39 4068 1 . ALA 40 40 4068 1 . VAL 41 41 4068 1 . VAL 42 42 4068 1 . GLU 43 43 4068 1 . SER 44 44 4068 1 . ASN 45 45 4068 1 . GLY 46 46 4068 1 . THR 47 47 4068 1 . LEU 48 48 4068 1 . THR 49 49 4068 1 . LEU 50 50 4068 1 . SER 51 51 4068 1 . HIS 52 52 4068 1 . PHE 53 53 4068 1 . GLY 54 54 4068 1 . LYS 55 55 4068 1 . CYS 56 56 4068 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 4068 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $OMTKY3 . 9103 organism . 'Meleagris gallapavo' turkey . . Eukaryota Metazoa Meleagris gallapavo . . . . . . . . . . . . . . . . . . . . . 4068 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 4068 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $OMTKY3 . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21(DE3)/pLysS . . . . . . . . . . . . plasmid . . PTNOM3 . . . ; native (OMTK3 was oveproduced as a fusion protein with Staphylococcal nuclease (SNase) in E. coli strain BL21(DE3)/pLysS transformed with PTNOM3 plasmid by using the T7 promoter/T7 polymerase expression system (Hinck et al., Protein Engineering 6, 221-227 (1993). IPTG was used to induce expression of the fusion protein.) ; . . 4068 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 4068 _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 'turkey ovomucoid third domain' . . . 1 $OMTKY3 . . . 2 3 mM . . . . 4068 1 2 H2O . . . . . . . 90 . . % . . . . 4068 1 3 D2O . . . . . . . 10 . . % . . . . 4068 1 stop_ save_ save_sample_two _Sample.Sf_category sample _Sample.Sf_framecode sample_two _Sample.Entry_ID 4068 _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 'turkey ovomucoid third domain' [U-15N] . . 1 $OMTKY3 . . . 2 3 mM . . . . 4068 2 2 H2O . . . . . . . 90 . . % . . . . 4068 2 3 D2O . . . . . . . 10 . . % . . . . 4068 2 stop_ save_ save_sample_three _Sample.Sf_category sample _Sample.Sf_framecode sample_three _Sample.Entry_ID 4068 _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 'turkey ovomucoid third domain' [U-15N;13C] . . 1 $OMTKY3 . . . 2 3 mM . . . . 4068 3 2 H2O . . . . . . . 90 . . % . . . . 4068 3 3 D2O . . . . . . . 10 . . % . . . . 4068 3 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions _Sample_condition_list.Entry_ID 4068 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 2.0 . n/a 4068 1 temperature 298 . K 4068 1 stop_ save_ ############################# # Purity of the molecules # ############################# save_molecule_purity_list _Entity_purity_list.Sf_category molecule_purity _Entity_purity_list.Sf_framecode molecule_purity_list _Entity_purity_list.Entry_ID 4068 _Entity_purity_list.ID 1 _Entity_purity_list.Details ; Sample purity was confirmed by SDS-PAGE and enzyme activity assays. The yields of pure OMTK3 were 10 mg per liter of culture in M9 medium, and 8.5 mg LB medium ; loop_ _Entity_purity.ID _Entity_purity.Sample_ID _Entity_purity.Sample_label _Entity_purity.Entity_ID _Entity_purity.Entity_label _Entity_purity.Val _Entity_purity.Val_units _Entity_purity.Measurement_method _Entity_purity.Details _Entity_purity.Entry_ID _Entity_purity.Entity_purity_list_ID 1 . . 1 $OMTKY3 10 mg/L SDS-PAGE 'M9 medium' 4068 1 2 . . 1 $OMTKY3 8.5 mg/L SDS-PAGE 'LB medium' 4068 1 stop_ save_ ############################ # Computer software used # ############################ save_software_one _Software.Sf_category software _Software.Sf_framecode software_one _Software.Entry_ID 4068 _Software.ID 1 _Software.Name FELIX _Software.Version 2.3 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Molecular Simulations, Inc' 'San Diego, CA' . 4068 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'NMR data processing' 4068 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_one _NMR_spectrometer.Entry_ID 4068 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX-500 _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_NMR_spectrometer_two _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer_two _NMR_spectrometer.Entry_ID 4068 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX-600 _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4068 _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_one Bruker DMX-500 . 500 . . . 4068 1 2 NMR_spectrometer_two Bruker DMX-600 . 600 . . . 4068 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 4068 _Experiment_list.ID 1 _Experiment_list.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference _Chem_shift_reference.Entry_ID 4068 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS methyl . . . . ppm 0.00 . indirect 0.251449530 . . . . . . . . . 4068 1 H 1 DSS methyl . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 4068 1 N 15 DSS methyl . . . . ppm 0.00 . indirect 0.101329118 . . . . . . . . . 4068 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_chemical_shift_assignment _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shift_assignment _Assigned_chem_shift_list.Entry_ID 4068 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 4068 1 . . 2 $sample_two . 4068 1 . . 3 $sample_three . 4068 1 stop_ loop_ _Chem_shift_software.Software_ID _Chem_shift_software.Software_label _Chem_shift_software.Method_ID _Chem_shift_software.Method_label _Chem_shift_software.Entry_ID _Chem_shift_software.Assigned_chem_shift_list_ID 1 $software_one . . 4068 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 2 2 ALA H H 1 8.66 . . 1 . . . . . . . . 4068 1 2 . 1 1 2 2 ALA HA H 1 4.38 . . 1 . . . . . . . . 4068 1 3 . 1 1 2 2 ALA HB1 H 1 1.39 . . 1 . . . . . . . . 4068 1 4 . 1 1 2 2 ALA HB2 H 1 1.39 . . 1 . . . . . . . . 4068 1 5 . 1 1 2 2 ALA HB3 H 1 1.39 . . 1 . . . . . . . . 4068 1 6 . 1 1 2 2 ALA C C 13 176.93 . . 1 . . . . . . . . 4068 1 7 . 1 1 2 2 ALA CA C 13 52.33 . . 1 . . . . . . . . 4068 1 8 . 1 1 2 2 ALA CB C 13 19.34 . . 1 . . . . . . . . 4068 1 9 . 1 1 3 3 ALA H H 1 8.42 . . 1 . . . . . . . . 4068 1 10 . 1 1 3 3 ALA HA H 1 4.34 . . 1 . . . . . . . . 4068 1 11 . 1 1 3 3 ALA HB1 H 1 1.39 . . 1 . . . . . . . . 4068 1 12 . 1 1 3 3 ALA HB2 H 1 1.39 . . 1 . . . . . . . . 4068 1 13 . 1 1 3 3 ALA HB3 H 1 1.39 . . 1 . . . . . . . . 4068 1 14 . 1 1 3 3 ALA C C 13 177.64 . . 1 . . . . . . . . 4068 1 15 . 1 1 3 3 ALA CA C 13 52.45 . . 1 . . . . . . . . 4068 1 16 . 1 1 3 3 ALA CB C 13 19.41 . . 1 . . . . . . . . 4068 1 17 . 1 1 3 3 ALA N N 15 124.54 . . 1 . . . . . . . . 4068 1 18 . 1 1 4 4 VAL H H 1 8.16 . . 1 . . . . . . . . 4068 1 19 . 1 1 4 4 VAL HA H 1 4.23 . . 1 . . . . . . . . 4068 1 20 . 1 1 4 4 VAL HB H 1 2.03 . . 1 . . . . . . . . 4068 1 21 . 1 1 4 4 VAL HG11 H 1 0.89 . . 2 . . . . . . . . 4068 1 22 . 1 1 4 4 VAL HG12 H 1 0.89 . . 2 . . . . . . . . 4068 1 23 . 1 1 4 4 VAL HG13 H 1 0.89 . . 2 . . . . . . . . 4068 1 24 . 1 1 4 4 VAL HG21 H 1 0.9 . . 2 . . . . . . . . 4068 1 25 . 1 1 4 4 VAL HG22 H 1 0.9 . . 2 . . . . . . . . 4068 1 26 . 1 1 4 4 VAL HG23 H 1 0.9 . . 2 . . . . . . . . 4068 1 27 . 1 1 4 4 VAL C C 13 176.31 . . 1 . . . . . . . . 4068 1 28 . 1 1 4 4 VAL CA C 13 61.76 . . 1 . . . . . . . . 4068 1 29 . 1 1 4 4 VAL CB C 13 33.15 . . 1 . . . . . . . . 4068 1 30 . 1 1 4 4 VAL CG1 C 13 21.05 . . 2 . . . . . . . . 4068 1 31 . 1 1 4 4 VAL N N 15 118.91 . . 1 . . . . . . . . 4068 1 32 . 1 1 5 5 SER H H 1 8.3 . . 1 . . . . . . . . 4068 1 33 . 1 1 5 5 SER HA H 1 4.56 . . 1 . . . . . . . . 4068 1 34 . 1 1 5 5 SER HB2 H 1 3.87 . . 2 . . . . . . . . 4068 1 35 . 1 1 5 5 SER C C 13 173.4 . . 1 . . . . . . . . 4068 1 36 . 1 1 5 5 SER CA C 13 64.73 . . 1 . . . . . . . . 4068 1 37 . 1 1 5 5 SER CB C 13 57.82 . . 1 . . . . . . . . 4068 1 38 . 1 1 5 5 SER N N 15 118.01 . . 1 . . . . . . . . 4068 1 39 . 1 1 6 6 VAL H H 1 8.37 . . 1 . . . . . . . . 4068 1 40 . 1 1 6 6 VAL HA H 1 4.34 . . 1 . . . . . . . . 4068 1 41 . 1 1 6 6 VAL HB H 1 1.97 . . 1 . . . . . . . . 4068 1 42 . 1 1 6 6 VAL HG11 H 1 0.92 . . 2 . . . . . . . . 4068 1 43 . 1 1 6 6 VAL HG12 H 1 0.92 . . 2 . . . . . . . . 4068 1 44 . 1 1 6 6 VAL HG13 H 1 0.92 . . 2 . . . . . . . . 4068 1 45 . 1 1 6 6 VAL HG21 H 1 0.81 . . 2 . . . . . . . . 4068 1 46 . 1 1 6 6 VAL HG22 H 1 0.81 . . 2 . . . . . . . . 4068 1 47 . 1 1 6 6 VAL HG23 H 1 0.81 . . 2 . . . . . . . . 4068 1 48 . 1 1 6 6 VAL C C 13 174.2 . . 1 . . . . . . . . 4068 1 49 . 1 1 6 6 VAL CA C 13 61.26 . . 1 . . . . . . . . 4068 1 50 . 1 1 6 6 VAL CB C 13 34.23 . . 1 . . . . . . . . 4068 1 51 . 1 1 6 6 VAL CG1 C 13 20.5 . . 2 . . . . . . . . 4068 1 52 . 1 1 6 6 VAL CG2 C 13 21.59 . . 2 . . . . . . . . 4068 1 53 . 1 1 6 6 VAL N N 15 120.24 . . 1 . . . . . . . . 4068 1 54 . 1 1 7 7 ASP H H 1 8.71 . . 1 . . . . . . . . 4068 1 55 . 1 1 7 7 ASP HA H 1 4.83 . . 1 . . . . . . . . 4068 1 56 . 1 1 7 7 ASP HB2 H 1 2.88 . . 2 . . . . . . . . 4068 1 57 . 1 1 7 7 ASP HB3 H 1 3.19 . . 2 . . . . . . . . 4068 1 58 . 1 1 7 7 ASP C C 13 176.18 . . 1 . . . . . . . . 4068 1 59 . 1 1 7 7 ASP CA C 13 52.35 . . 1 . . . . . . . . 4068 1 60 . 1 1 7 7 ASP CB C 13 38.27 . . 1 . . . . . . . . 4068 1 61 . 1 1 7 7 ASP N N 15 123.31 . . 1 . . . . . . . . 4068 1 62 . 1 1 8 8 CYS H H 1 9.02 . . 1 . . . . . . . . 4068 1 63 . 1 1 8 8 CYS HA H 1 5.25 . . 1 . . . . . . . . 4068 1 64 . 1 1 8 8 CYS HB2 H 1 3.29 . . 1 . . . . . . . . 4068 1 65 . 1 1 8 8 CYS HB3 H 1 2.58 . . 1 . . . . . . . . 4068 1 66 . 1 1 8 8 CYS C C 13 175.24 . . 1 . . . . . . . . 4068 1 67 . 1 1 8 8 CYS CA C 13 51.85 . . 1 . . . . . . . . 4068 1 68 . 1 1 8 8 CYS CB C 13 33.94 . . 1 . . . . . . . . 4068 1 69 . 1 1 8 8 CYS N N 15 125.5 . . 1 . . . . . . . . 4068 1 70 . 1 1 9 9 SER H H 1 8.32 . . 1 . . . . . . . . 4068 1 71 . 1 1 9 9 SER HA H 1 4.35 . . 1 . . . . . . . . 4068 1 72 . 1 1 9 9 SER HB2 H 1 4.03 . . 2 . . . . . . . . 4068 1 73 . 1 1 9 9 SER C C 13 175.28 . . 1 . . . . . . . . 4068 1 74 . 1 1 9 9 SER CA C 13 61.67 . . 1 . . . . . . . . 4068 1 75 . 1 1 9 9 SER CB C 13 34.4 . . 1 . . . . . . . . 4068 1 76 . 1 1 9 9 SER N N 15 118.04 . . 1 . . . . . . . . 4068 1 77 . 1 1 10 10 GLU H H 1 8.69 . . 1 . . . . . . . . 4068 1 78 . 1 1 10 10 GLU HA H 1 4.29 . . 1 . . . . . . . . 4068 1 79 . 1 1 10 10 GLU HB2 H 1 1.87 . . 1 . . . . . . . . 4068 1 80 . 1 1 10 10 GLU HB3 H 1 2.07 . . 1 . . . . . . . . 4068 1 81 . 1 1 10 10 GLU HG2 H 1 2.4 . . 2 . . . . . . . . 4068 1 82 . 1 1 10 10 GLU C C 13 173.79 . . 1 . . . . . . . . 4068 1 83 . 1 1 10 10 GLU CA C 13 56.19 . . 1 . . . . . . . . 4068 1 84 . 1 1 10 10 GLU CB C 13 28.95 . . 1 . . . . . . . . 4068 1 85 . 1 1 10 10 GLU CG C 13 33.31 . . 1 . . . . . . . . 4068 1 86 . 1 1 10 10 GLU N N 15 118.4 . . 1 . . . . . . . . 4068 1 87 . 1 1 11 11 TYR H H 1 7.52 . . 1 . . . . . . . . 4068 1 88 . 1 1 11 11 TYR HA H 1 4.16 . . 1 . . . . . . . . 4068 1 89 . 1 1 11 11 TYR HB2 H 1 2.85 . . 2 . . . . . . . . 4068 1 90 . 1 1 11 11 TYR HB3 H 1 2.8 . . 2 . . . . . . . . 4068 1 91 . 1 1 11 11 TYR HD1 H 1 7.15 . . 2 . . . . . . . . 4068 1 92 . 1 1 11 11 TYR HD2 H 1 7.1 . . 2 . . . . . . . . 4068 1 93 . 1 1 11 11 TYR CA C 13 57.83 . . 1 . . . . . . . . 4068 1 94 . 1 1 11 11 TYR CB C 13 38.48 . . 1 . . . . . . . . 4068 1 95 . 1 1 11 11 TYR N N 15 118.61 . . 1 . . . . . . . . 4068 1 96 . 1 1 12 12 PRO HA H 1 5.19 . . 1 . . . . . . . . 4068 1 97 . 1 1 12 12 PRO HB2 H 1 2.44 . . 2 . . . . . . . . 4068 1 98 . 1 1 12 12 PRO HB3 H 1 2.07 . . 2 . . . . . . . . 4068 1 99 . 1 1 12 12 PRO HD2 H 1 3.53 . . 2 . . . . . . . . 4068 1 100 . 1 1 12 12 PRO HD3 H 1 3.674 . . 2 . . . . . . . . 4068 1 101 . 1 1 12 12 PRO C C 13 175.75 . . 1 . . . . . . . . 4068 1 102 . 1 1 12 12 PRO CA C 13 62.22 . . 1 . . . . . . . . 4068 1 103 . 1 1 12 12 PRO CB C 13 36.3 . . 1 . . . . . . . . 4068 1 104 . 1 1 13 13 LYS H H 1 9.36 . . 1 . . . . . . . . 4068 1 105 . 1 1 13 13 LYS HA H 1 4.86 . . 1 . . . . . . . . 4068 1 106 . 1 1 13 13 LYS HB2 H 1 1.9 . . 2 . . . . . . . . 4068 1 107 . 1 1 13 13 LYS HB3 H 1 1.59 . . 2 . . . . . . . . 4068 1 108 . 1 1 13 13 LYS HG2 H 1 1.19 . . 2 . . . . . . . . 4068 1 109 . 1 1 13 13 LYS HG3 H 1 0.98 . . 2 . . . . . . . . 4068 1 110 . 1 1 13 13 LYS HD2 H 1 1.6 . . 2 . . . . . . . . 4068 1 111 . 1 1 13 13 LYS HD3 H 1 1.44 . . 2 . . . . . . . . 4068 1 112 . 1 1 13 13 LYS HE2 H 1 2.59 . . 2 . . . . . . . . 4068 1 113 . 1 1 13 13 LYS HE3 H 1 2.44 . . 2 . . . . . . . . 4068 1 114 . 1 1 13 13 LYS CA C 13 53.71 . . 1 . . . . . . . . 4068 1 115 . 1 1 13 13 LYS CB C 13 35.21 . . 1 . . . . . . . . 4068 1 116 . 1 1 13 13 LYS CG C 13 25.41 . . 1 . . . . . . . . 4068 1 117 . 1 1 13 13 LYS CD C 13 29.22 . . 1 . . . . . . . . 4068 1 118 . 1 1 13 13 LYS CE C 13 42.3 . . 1 . . . . . . . . 4068 1 119 . 1 1 13 13 LYS N N 15 121.45 . . 1 . . . . . . . . 4068 1 120 . 1 1 14 14 PRO HA H 1 4.35 . . 1 . . . . . . . . 4068 1 121 . 1 1 14 14 PRO HB2 H 1 2.04 . . 2 . . . . . . . . 4068 1 122 . 1 1 14 14 PRO HB3 H 1 2.26 . . 2 . . . . . . . . 4068 1 123 . 1 1 14 14 PRO HG2 H 1 2.1 . . 2 . . . . . . . . 4068 1 124 . 1 1 14 14 PRO HG3 H 1 2.04 . . 2 . . . . . . . . 4068 1 125 . 1 1 14 14 PRO HD2 H 1 3.76 . . 2 . . . . . . . . 4068 1 126 . 1 1 14 14 PRO HD3 H 1 3.8 . . 2 . . . . . . . . 4068 1 127 . 1 1 14 14 PRO C C 13 175.69 . . 1 . . . . . . . . 4068 1 128 . 1 1 14 14 PRO CA C 13 64.09 . . 1 . . . . . . . . 4068 1 129 . 1 1 14 14 PRO CB C 13 32.3 . . 1 . . . . . . . . 4068 1 130 . 1 1 14 14 PRO CG C 13 27.04 . . 1 . . . . . . . . 4068 1 131 . 1 1 14 14 PRO CD C 13 51.02 . . 1 . . . . . . . . 4068 1 132 . 1 1 15 15 ALA H H 1 7.51 . . 1 . . . . . . . . 4068 1 133 . 1 1 15 15 ALA HA H 1 4.57 . . 1 . . . . . . . . 4068 1 134 . 1 1 15 15 ALA HB1 H 1 1.33 . . 1 . . . . . . . . 4068 1 135 . 1 1 15 15 ALA HB2 H 1 1.33 . . 1 . . . . . . . . 4068 1 136 . 1 1 15 15 ALA HB3 H 1 1.33 . . 1 . . . . . . . . 4068 1 137 . 1 1 15 15 ALA C C 13 175.96 . . 1 . . . . . . . . 4068 1 138 . 1 1 15 15 ALA CA C 13 51.31 . . 1 . . . . . . . . 4068 1 139 . 1 1 15 15 ALA CB C 13 21.09 . . 1 . . . . . . . . 4068 1 140 . 1 1 15 15 ALA N N 15 118.88 . . 1 . . . . . . . . 4068 1 141 . 1 1 16 16 CYS H H 1 8.59 . . 1 . . . . . . . . 4068 1 142 . 1 1 16 16 CYS HA H 1 5.25 . . 1 . . . . . . . . 4068 1 143 . 1 1 16 16 CYS HB2 H 1 2.76 . . 2 . . . . . . . . 4068 1 144 . 1 1 16 16 CYS HB3 H 1 3.35 . . 2 . . . . . . . . 4068 1 145 . 1 1 16 16 CYS C C 13 175.46 . . 1 . . . . . . . . 4068 1 146 . 1 1 16 16 CYS CA C 13 52.1 . . 1 . . . . . . . . 4068 1 147 . 1 1 16 16 CYS CB C 13 40.12 . . 1 . . . . . . . . 4068 1 148 . 1 1 16 16 CYS N N 15 118.53 . . 1 . . . . . . . . 4068 1 149 . 1 1 17 17 THR H H 1 8.39 . . 1 . . . . . . . . 4068 1 150 . 1 1 17 17 THR HA H 1 4.39 . . 1 . . . . . . . . 4068 1 151 . 1 1 17 17 THR HB H 1 4.55 . . 1 . . . . . . . . 4068 1 152 . 1 1 17 17 THR HG21 H 1 1.37 . . 1 . . . . . . . . 4068 1 153 . 1 1 17 17 THR HG22 H 1 1.37 . . 1 . . . . . . . . 4068 1 154 . 1 1 17 17 THR HG23 H 1 1.37 . . 1 . . . . . . . . 4068 1 155 . 1 1 17 17 THR C C 13 176.94 . . 1 . . . . . . . . 4068 1 156 . 1 1 17 17 THR CA C 13 61.59 . . 1 . . . . . . . . 4068 1 157 . 1 1 17 17 THR CB C 13 70.06 . . 1 . . . . . . . . 4068 1 158 . 1 1 17 17 THR CG2 C 13 21.59 . . 1 . . . . . . . . 4068 1 159 . 1 1 17 17 THR N N 15 113.72 . . 1 . . . . . . . . 4068 1 160 . 1 1 18 18 LEU H H 1 8.4 . . 1 . . . . . . . . 4068 1 161 . 1 1 18 18 LEU HA H 1 4.42 . . 1 . . . . . . . . 4068 1 162 . 1 1 18 18 LEU HB2 H 1 1.79 . . 2 . . . . . . . . 4068 1 163 . 1 1 18 18 LEU HB3 H 1 1.84 . . 2 . . . . . . . . 4068 1 164 . 1 1 18 18 LEU HG H 1 1.66 . . 1 . . . . . . . . 4068 1 165 . 1 1 18 18 LEU HD11 H 1 0.94 . . 2 . . . . . . . . 4068 1 166 . 1 1 18 18 LEU HD12 H 1 0.94 . . 2 . . . . . . . . 4068 1 167 . 1 1 18 18 LEU HD13 H 1 0.94 . . 2 . . . . . . . . 4068 1 168 . 1 1 18 18 LEU HD21 H 1 0.9 . . 2 . . . . . . . . 4068 1 169 . 1 1 18 18 LEU HD22 H 1 0.9 . . 2 . . . . . . . . 4068 1 170 . 1 1 18 18 LEU HD23 H 1 0.9 . . 2 . . . . . . . . 4068 1 171 . 1 1 18 18 LEU C C 13 177.38 . . 1 . . . . . . . . 4068 1 172 . 1 1 18 18 LEU CA C 13 54.65 . . 1 . . . . . . . . 4068 1 173 . 1 1 18 18 LEU CB C 13 41.23 . . 1 . . . . . . . . 4068 1 174 . 1 1 18 18 LEU CG C 13 27.04 . . 1 . . . . . . . . 4068 1 175 . 1 1 18 18 LEU CD1 C 13 27.04 . . 2 . . . . . . . . 4068 1 176 . 1 1 18 18 LEU CD2 C 13 23.5 . . 2 . . . . . . . . 4068 1 177 . 1 1 18 18 LEU N N 15 120.45 . . 1 . . . . . . . . 4068 1 178 . 1 1 19 19 GLU H H 1 7.67 . . 1 . . . . . . . . 4068 1 179 . 1 1 19 19 GLU HA H 1 4.14 . . 1 . . . . . . . . 4068 1 180 . 1 1 19 19 GLU HB2 H 1 2.05 . . 2 . . . . . . . . 4068 1 181 . 1 1 19 19 GLU HB3 H 1 1.98 . . 2 . . . . . . . . 4068 1 182 . 1 1 19 19 GLU HG2 H 1 2.5 . . 2 . . . . . . . . 4068 1 183 . 1 1 19 19 GLU C C 13 175.41 . . 1 . . . . . . . . 4068 1 184 . 1 1 19 19 GLU CA C 13 57.00 . . 1 . . . . . . . . 4068 1 185 . 1 1 19 19 GLU CB C 13 28.65 . . 1 . . . . . . . . 4068 1 186 . 1 1 19 19 GLU CG C 13 31.94 . . 1 . . . . . . . . 4068 1 187 . 1 1 19 19 GLU N N 15 120.78 . . 1 . . . . . . . . 4068 1 188 . 1 1 20 20 TYR H H 1 8.95 . . 1 . . . . . . . . 4068 1 189 . 1 1 20 20 TYR HA H 1 5.03 . . 1 . . . . . . . . 4068 1 190 . 1 1 20 20 TYR HB2 H 1 3.12 . . 1 . . . . . . . . 4068 1 191 . 1 1 20 20 TYR HB3 H 1 2.95 . . 1 . . . . . . . . 4068 1 192 . 1 1 20 20 TYR HD1 H 1 7.28 . . 2 . . . . . . . . 4068 1 193 . 1 1 20 20 TYR HE1 H 1 7.18 . . 2 . . . . . . . . 4068 1 194 . 1 1 20 20 TYR C C 13 174.92 . . 1 . . . . . . . . 4068 1 195 . 1 1 20 20 TYR CA C 13 57.57 . . 1 . . . . . . . . 4068 1 196 . 1 1 20 20 TYR CB C 13 38.78 . . 1 . . . . . . . . 4068 1 197 . 1 1 20 20 TYR N N 15 128.17 . . 1 . . . . . . . . 4068 1 198 . 1 1 21 21 ARG H H 1 8.91 . . 1 . . . . . . . . 4068 1 199 . 1 1 21 21 ARG HA H 1 4.46 . . 1 . . . . . . . . 4068 1 200 . 1 1 21 21 ARG HB2 H 1 1.79 . . 2 . . . . . . . . 4068 1 201 . 1 1 21 21 ARG HG2 H 1 1.59 . . 2 . . . . . . . . 4068 1 202 . 1 1 21 21 ARG HD2 H 1 3.28 . . 2 . . . . . . . . 4068 1 203 . 1 1 21 21 ARG HD3 H 1 3.27 . . 2 . . . . . . . . 4068 1 204 . 1 1 21 21 ARG HE H 1 7.18 . . 1 . . . . . . . . 4068 1 205 . 1 1 21 21 ARG CA C 13 58.11 . . 1 . . . . . . . . 4068 1 206 . 1 1 21 21 ARG CB C 13 31.13 . . 1 . . . . . . . . 4068 1 207 . 1 1 21 21 ARG CG C 13 27.31 . . 1 . . . . . . . . 4068 1 208 . 1 1 21 21 ARG CD C 13 43.66 . . 1 . . . . . . . . 4068 1 209 . 1 1 21 21 ARG N N 15 118.6 . . 1 . . . . . . . . 4068 1 210 . 1 1 22 22 PRO HA H 1 4.5 . . 1 . . . . . . . . 4068 1 211 . 1 1 22 22 PRO HB2 H 1 1.84 . . 2 . . . . . . . . 4068 1 212 . 1 1 22 22 PRO HB3 H 1 1.68 . . 2 . . . . . . . . 4068 1 213 . 1 1 22 22 PRO HG3 H 1 1.78 . . 2 . . . . . . . . 4068 1 214 . 1 1 22 22 PRO HD2 H 1 3.56 . . 2 . . . . . . . . 4068 1 215 . 1 1 22 22 PRO HD3 H 1 3.38 . . 2 . . . . . . . . 4068 1 216 . 1 1 22 22 PRO C C 13 176.7 . . 1 . . . . . . . . 4068 1 217 . 1 1 22 22 PRO CA C 13 63.12 . . 1 . . . . . . . . 4068 1 218 . 1 1 22 22 PRO CB C 13 27.59 . . 1 . . . . . . . . 4068 1 219 . 1 1 22 22 PRO CD C 13 49.65 . . 1 . . . . . . . . 4068 1 220 . 1 1 23 23 LEU H H 1 8.5 . . 1 . . . . . . . . 4068 1 221 . 1 1 23 23 LEU HA H 1 4.31 . . 1 . . . . . . . . 4068 1 222 . 1 1 23 23 LEU HB2 H 1 1.4 . . 2 . . . . . . . . 4068 1 223 . 1 1 23 23 LEU HG H 1 0.98 . . 1 . . . . . . . . 4068 1 224 . 1 1 23 23 LEU HD11 H 1 0.49 . . 2 . . . . . . . . 4068 1 225 . 1 1 23 23 LEU HD12 H 1 0.49 . . 2 . . . . . . . . 4068 1 226 . 1 1 23 23 LEU HD13 H 1 0.49 . . 2 . . . . . . . . 4068 1 227 . 1 1 23 23 LEU HD21 H 1 0.42 . . 2 . . . . . . . . 4068 1 228 . 1 1 23 23 LEU HD22 H 1 0.42 . . 2 . . . . . . . . 4068 1 229 . 1 1 23 23 LEU HD23 H 1 0.42 . . 2 . . . . . . . . 4068 1 230 . 1 1 23 23 LEU C C 13 173.9 . . 1 . . . . . . . . 4068 1 231 . 1 1 23 23 LEU CA C 13 55.13 . . 1 . . . . . . . . 4068 1 232 . 1 1 23 23 LEU CB C 13 27.31 . . 1 . . . . . . . . 4068 1 233 . 1 1 23 23 LEU CG C 13 45.3 . . 1 . . . . . . . . 4068 1 234 . 1 1 23 23 LEU CD1 C 13 25.68 . . 2 . . . . . . . . 4068 1 235 . 1 1 23 23 LEU CD2 C 13 26.22 . . 2 . . . . . . . . 4068 1 236 . 1 1 23 23 LEU N N 15 119.1 . . 1 . . . . . . . . 4068 1 237 . 1 1 24 24 CYS H H 1 8.21 . . 1 . . . . . . . . 4068 1 238 . 1 1 24 24 CYS HA H 1 5.23 . . 1 . . . . . . . . 4068 1 239 . 1 1 24 24 CYS HB2 H 1 1.37 . . 1 . . . . . . . . 4068 1 240 . 1 1 24 24 CYS HB3 H 1 2.41 . . 1 . . . . . . . . 4068 1 241 . 1 1 24 24 CYS C C 13 175.6 . . 1 . . . . . . . . 4068 1 242 . 1 1 24 24 CYS CA C 13 54.39 . . 1 . . . . . . . . 4068 1 243 . 1 1 24 24 CYS CB C 13 38.75 . . 1 . . . . . . . . 4068 1 244 . 1 1 24 24 CYS N N 15 120.2 . . 1 . . . . . . . . 4068 1 245 . 1 1 25 25 GLY H H 1 9.3 . . 1 . . . . . . . . 4068 1 246 . 1 1 25 25 GLY HA2 H 1 4.3 . . 2 . . . . . . . . 4068 1 247 . 1 1 25 25 GLY HA3 H 1 4.85 . . 2 . . . . . . . . 4068 1 248 . 1 1 25 25 GLY C C 13 174.4 . . 1 . . . . . . . . 4068 1 249 . 1 1 25 25 GLY CA C 13 45.27 . . 1 . . . . . . . . 4068 1 250 . 1 1 25 25 GLY N N 15 115.13 . . 1 . . . . . . . . 4068 1 251 . 1 1 26 26 SER H H 1 9.41 . . 1 . . . . . . . . 4068 1 252 . 1 1 26 26 SER HA H 1 4.2 . . 1 . . . . . . . . 4068 1 253 . 1 1 26 26 SER HB2 H 1 3.87 . . 1 . . . . . . . . 4068 1 254 . 1 1 26 26 SER HB3 H 1 4.12 . . 1 . . . . . . . . 4068 1 255 . 1 1 26 26 SER C C 13 173.88 . . 1 . . . . . . . . 4068 1 256 . 1 1 26 26 SER CA C 13 45.43 . . 1 . . . . . . . . 4068 1 257 . 1 1 26 26 SER N N 15 118.00 . . 1 . . . . . . . . 4068 1 258 . 1 1 27 27 ASP H H 1 7.84 . . 1 . . . . . . . . 4068 1 259 . 1 1 27 27 ASP HA H 1 4.65 . . 1 . . . . . . . . 4068 1 260 . 1 1 27 27 ASP HB2 H 1 3.32 . . 2 . . . . . . . . 4068 1 261 . 1 1 27 27 ASP HB3 H 1 2.87 . . 2 . . . . . . . . 4068 1 262 . 1 1 27 27 ASP C C 13 174.94 . . 1 . . . . . . . . 4068 1 263 . 1 1 27 27 ASP CA C 13 52.31 . . 1 . . . . . . . . 4068 1 264 . 1 1 27 27 ASP CB C 13 37.89 . . 1 . . . . . . . . 4068 1 265 . 1 1 27 27 ASP N N 15 118.00 . . 1 . . . . . . . . 4068 1 266 . 1 1 28 28 ASN H H 1 8.69 . . 1 . . . . . . . . 4068 1 267 . 1 1 28 28 ASN HA H 1 4.42 . . 1 . . . . . . . . 4068 1 268 . 1 1 28 28 ASN HB2 H 1 2.79 . . 1 . . . . . . . . 4068 1 269 . 1 1 28 28 ASN HB3 H 1 3.15 . . 1 . . . . . . . . 4068 1 270 . 1 1 28 28 ASN HD21 H 1 7.56 . . 2 . . . . . . . . 4068 1 271 . 1 1 28 28 ASN HD22 H 1 6.83 . . 2 . . . . . . . . 4068 1 272 . 1 1 28 28 ASN C C 13 173.64 . . 1 . . . . . . . . 4068 1 273 . 1 1 28 28 ASN CA C 13 54.9 . . 1 . . . . . . . . 4068 1 274 . 1 1 28 28 ASN CB C 13 37.51 . . 1 . . . . . . . . 4068 1 275 . 1 1 28 28 ASN N N 15 116.03 . . 1 . . . . . . . . 4068 1 276 . 1 1 28 28 ASN ND2 N 15 109.313 . . 1 . . . . . . . . 4068 1 277 . 1 1 29 29 LYS H H 1 7.21 . . 1 . . . . . . . . 4068 1 278 . 1 1 29 29 LYS HA H 1 4.46 . . 1 . . . . . . . . 4068 1 279 . 1 1 29 29 LYS HB2 H 1 1.39 . . 2 . . . . . . . . 4068 1 280 . 1 1 29 29 LYS HB3 H 1 1.546 . . 2 . . . . . . . . 4068 1 281 . 1 1 29 29 LYS HG2 H 1 1.16 . . 2 . . . . . . . . 4068 1 282 . 1 1 29 29 LYS HG3 H 1 0.89 . . 2 . . . . . . . . 4068 1 283 . 1 1 29 29 LYS HD2 H 1 1.51 . . 2 . . . . . . . . 4068 1 284 . 1 1 29 29 LYS HE2 H 1 2.87 . . 2 . . . . . . . . 4068 1 285 . 1 1 29 29 LYS C C 13 175.94 . . 1 . . . . . . . . 4068 1 286 . 1 1 29 29 LYS CA C 13 56.05 . . 1 . . . . . . . . 4068 1 287 . 1 1 29 29 LYS CB C 13 34.12 . . 1 . . . . . . . . 4068 1 288 . 1 1 29 29 LYS CG C 13 25.13 . . 1 . . . . . . . . 4068 1 289 . 1 1 29 29 LYS CD C 13 28.95 . . 1 . . . . . . . . 4068 1 290 . 1 1 29 29 LYS CE C 13 42.57 . . 1 . . . . . . . . 4068 1 291 . 1 1 29 29 LYS N N 15 116.95 . . 1 . . . . . . . . 4068 1 292 . 1 1 30 30 THR H H 1 8.42 . . 1 . . . . . . . . 4068 1 293 . 1 1 30 30 THR HA H 1 4.81 . . 1 . . . . . . . . 4068 1 294 . 1 1 30 30 THR HB H 1 4.02 . . 1 . . . . . . . . 4068 1 295 . 1 1 30 30 THR HG21 H 1 1.19 . . 1 . . . . . . . . 4068 1 296 . 1 1 30 30 THR HG22 H 1 1.19 . . 1 . . . . . . . . 4068 1 297 . 1 1 30 30 THR HG23 H 1 1.19 . . 1 . . . . . . . . 4068 1 298 . 1 1 30 30 THR C C 13 174.67 . . 1 . . . . . . . . 4068 1 299 . 1 1 30 30 THR CA C 13 62.83 . . 1 . . . . . . . . 4068 1 300 . 1 1 30 30 THR N N 15 122.17 . . 1 . . . . . . . . 4068 1 301 . 1 1 31 31 TYR H H 1 9.67 . . 1 . . . . . . . . 4068 1 302 . 1 1 31 31 TYR HA H 1 4.57 . . 1 . . . . . . . . 4068 1 303 . 1 1 31 31 TYR HB2 H 1 2.77 . . 2 . . . . . . . . 4068 1 304 . 1 1 31 31 TYR HB3 H 1 2.96 . . 2 . . . . . . . . 4068 1 305 . 1 1 31 31 TYR HD1 H 1 7.1 . . 2 . . . . . . . . 4068 1 306 . 1 1 31 31 TYR C C 13 176.82 . . 1 . . . . . . . . 4068 1 307 . 1 1 31 31 TYR CA C 13 58.19 . . 1 . . . . . . . . 4068 1 308 . 1 1 31 31 TYR CB C 13 41.45 . . 1 . . . . . . . . 4068 1 309 . 1 1 31 31 TYR N N 15 128.69 . . 1 . . . . . . . . 4068 1 310 . 1 1 32 32 GLY H H 1 9.23 . . 1 . . . . . . . . 4068 1 311 . 1 1 32 32 GLY HA2 H 1 4.12 . . 2 . . . . . . . . 4068 1 312 . 1 1 32 32 GLY HA3 H 1 3.71 . . 2 . . . . . . . . 4068 1 313 . 1 1 32 32 GLY C C 13 171.83 . . 1 . . . . . . . . 4068 1 314 . 1 1 32 32 GLY CA C 13 47.93 . . 1 . . . . . . . . 4068 1 315 . 1 1 32 32 GLY N N 15 109.63 . . 1 . . . . . . . . 4068 1 316 . 1 1 33 33 ASN H H 1 7.42 . . 1 . . . . . . . . 4068 1 317 . 1 1 33 33 ASN HA H 1 4.82 . . 1 . . . . . . . . 4068 1 318 . 1 1 33 33 ASN HB2 H 1 3.24 . . 1 . . . . . . . . 4068 1 319 . 1 1 33 33 ASN HB3 H 1 3.66 . . 1 . . . . . . . . 4068 1 320 . 1 1 33 33 ASN HD21 H 1 8.09 . . 2 . . . . . . . . 4068 1 321 . 1 1 33 33 ASN HD22 H 1 6.34 . . 2 . . . . . . . . 4068 1 322 . 1 1 33 33 ASN C C 13 175.98 . . 1 . . . . . . . . 4068 1 323 . 1 1 33 33 ASN CA C 13 52.01 . . 1 . . . . . . . . 4068 1 324 . 1 1 33 33 ASN CB C 13 39.21 . . 1 . . . . . . . . 4068 1 325 . 1 1 33 33 ASN N N 15 106.82 . . 1 . . . . . . . . 4068 1 326 . 1 1 33 33 ASN ND2 N 15 115.479 . . 1 . . . . . . . . 4068 1 327 . 1 1 34 34 LYS H H 1 8.92 . . 1 . . . . . . . . 4068 1 328 . 1 1 34 34 LYS HA H 1 3.88 . . 1 . . . . . . . . 4068 1 329 . 1 1 34 34 LYS HB2 H 1 1.91 . . 1 . . . . . . . . 4068 1 330 . 1 1 34 34 LYS HB3 H 1 2.00 . . 1 . . . . . . . . 4068 1 331 . 1 1 34 34 LYS HG2 H 1 1.5 . . 2 . . . . . . . . 4068 1 332 . 1 1 34 34 LYS HG3 H 1 1.36 . . 2 . . . . . . . . 4068 1 333 . 1 1 34 34 LYS HD2 H 1 1.81 . . 2 . . . . . . . . 4068 1 334 . 1 1 34 34 LYS HE2 H 1 3.04 . . 2 . . . . . . . . 4068 1 335 . 1 1 34 34 LYS HE3 H 1 3.1 . . 2 . . . . . . . . 4068 1 336 . 1 1 34 34 LYS C C 13 176.03 . . 1 . . . . . . . . 4068 1 337 . 1 1 34 34 LYS CA C 13 60.3 . . 1 . . . . . . . . 4068 1 338 . 1 1 34 34 LYS CB C 13 32.76 . . 1 . . . . . . . . 4068 1 339 . 1 1 34 34 LYS CG C 13 25.41 . . 1 . . . . . . . . 4068 1 340 . 1 1 34 34 LYS CD C 13 29.77 . . 1 . . . . . . . . 4068 1 341 . 1 1 34 34 LYS CE C 13 42.3 . . 1 . . . . . . . . 4068 1 342 . 1 1 34 34 LYS N N 15 119.2 . . 1 . . . . . . . . 4068 1 343 . 1 1 35 35 CYS H H 1 8.34 . . 1 . . . . . . . . 4068 1 344 . 1 1 35 35 CYS HA H 1 4.46 . . 1 . . . . . . . . 4068 1 345 . 1 1 35 35 CYS HB2 H 1 3.48 . . 2 . . . . . . . . 4068 1 346 . 1 1 35 35 CYS HB3 H 1 3.31 . . 2 . . . . . . . . 4068 1 347 . 1 1 35 35 CYS C C 13 175.86 . . 1 . . . . . . . . 4068 1 348 . 1 1 35 35 CYS CA C 13 58.86 . . 1 . . . . . . . . 4068 1 349 . 1 1 35 35 CYS CB C 13 36.66 . . 1 . . . . . . . . 4068 1 350 . 1 1 35 35 CYS N N 15 121.7 . . 1 . . . . . . . . 4068 1 351 . 1 1 36 36 ASN H H 1 8.44 . . 1 . . . . . . . . 4068 1 352 . 1 1 36 36 ASN HA H 1 4.59 . . 1 . . . . . . . . 4068 1 353 . 1 1 36 36 ASN HB2 H 1 3.22 . . 1 . . . . . . . . 4068 1 354 . 1 1 36 36 ASN HB3 H 1 2.83 . . 1 . . . . . . . . 4068 1 355 . 1 1 36 36 ASN HD21 H 1 7.62 . . 2 . . . . . . . . 4068 1 356 . 1 1 36 36 ASN HD22 H 1 7.13 . . 2 . . . . . . . . 4068 1 357 . 1 1 36 36 ASN C C 13 178.7 . . 1 . . . . . . . . 4068 1 358 . 1 1 36 36 ASN CA C 13 56.68 . . 1 . . . . . . . . 4068 1 359 . 1 1 36 36 ASN CB C 13 40.63 . . 1 . . . . . . . . 4068 1 360 . 1 1 36 36 ASN N N 15 118.77 . . 1 . . . . . . . . 4068 1 361 . 1 1 36 36 ASN ND2 N 15 111.41 . . 1 . . . . . . . . 4068 1 362 . 1 1 37 37 PHE H H 1 8.41 . . 1 . . . . . . . . 4068 1 363 . 1 1 37 37 PHE HA H 1 3.47 . . 1 . . . . . . . . 4068 1 364 . 1 1 37 37 PHE HB2 H 1 2.85 . . 1 . . . . . . . . 4068 1 365 . 1 1 37 37 PHE HB3 H 1 2.79 . . 1 . . . . . . . . 4068 1 366 . 1 1 37 37 PHE HD1 H 1 6.57 . . 2 . . . . . . . . 4068 1 367 . 1 1 37 37 PHE HE1 H 1 6.82 . . 2 . . . . . . . . 4068 1 368 . 1 1 37 37 PHE C C 13 175.64 . . 1 . . . . . . . . 4068 1 369 . 1 1 37 37 PHE CA C 13 61.2 . . 1 . . . . . . . . 4068 1 370 . 1 1 37 37 PHE CB C 13 40.66 . . 1 . . . . . . . . 4068 1 371 . 1 1 37 37 PHE N N 15 119.63 . . 1 . . . . . . . . 4068 1 372 . 1 1 38 38 CYS H H 1 9.21 . . 1 . . . . . . . . 4068 1 373 . 1 1 38 38 CYS HA H 1 3.99 . . 1 . . . . . . . . 4068 1 374 . 1 1 38 38 CYS HB2 H 1 1.81 . . 1 . . . . . . . . 4068 1 375 . 1 1 38 38 CYS HB3 H 1 1.53 . . 1 . . . . . . . . 4068 1 376 . 1 1 38 38 CYS CA C 13 55.96 . . 1 . . . . . . . . 4068 1 377 . 1 1 38 38 CYS CB C 13 32.76 . . 1 . . . . . . . . 4068 1 378 . 1 1 38 38 CYS N N 15 117.17 . . 1 . . . . . . . . 4068 1 379 . 1 1 39 39 ASN H H 1 8.17 . . 1 . . . . . . . . 4068 1 380 . 1 1 39 39 ASN HA H 1 4.68 . . 1 . . . . . . . . 4068 1 381 . 1 1 39 39 ASN HB2 H 1 2.99 . . 2 . . . . . . . . 4068 1 382 . 1 1 39 39 ASN HB3 H 1 2.78 . . 2 . . . . . . . . 4068 1 383 . 1 1 39 39 ASN HD21 H 1 7.59 . . 2 . . . . . . . . 4068 1 384 . 1 1 39 39 ASN HD22 H 1 6.93 . . 2 . . . . . . . . 4068 1 385 . 1 1 39 39 ASN C C 13 177.58 . . 1 . . . . . . . . 4068 1 386 . 1 1 39 39 ASN CA C 13 55.75 . . 1 . . . . . . . . 4068 1 387 . 1 1 39 39 ASN CB C 13 36.99 . . 1 . . . . . . . . 4068 1 388 . 1 1 39 39 ASN N N 15 120.52 . . 1 . . . . . . . . 4068 1 389 . 1 1 39 39 ASN ND2 N 15 112.64 . . 1 . . . . . . . . 4068 1 390 . 1 1 40 40 ALA H H 1 7.22 . . 1 . . . . . . . . 4068 1 391 . 1 1 40 40 ALA HA H 1 4.15 . . 1 . . . . . . . . 4068 1 392 . 1 1 40 40 ALA HB1 H 1 1.26 . . 1 . . . . . . . . 4068 1 393 . 1 1 40 40 ALA HB2 H 1 1.26 . . 1 . . . . . . . . 4068 1 394 . 1 1 40 40 ALA HB3 H 1 1.26 . . 1 . . . . . . . . 4068 1 395 . 1 1 40 40 ALA C C 13 181.03 . . 1 . . . . . . . . 4068 1 396 . 1 1 40 40 ALA CA C 13 54.81 . . 1 . . . . . . . . 4068 1 397 . 1 1 40 40 ALA CB C 13 18.52 . . 1 . . . . . . . . 4068 1 398 . 1 1 40 40 ALA N N 15 123.23 . . 1 . . . . . . . . 4068 1 399 . 1 1 41 41 VAL H H 1 8.59 . . 1 . . . . . . . . 4068 1 400 . 1 1 41 41 VAL HA H 1 3.18 . . 1 . . . . . . . . 4068 1 401 . 1 1 41 41 VAL HB H 1 2.04 . . 1 . . . . . . . . 4068 1 402 . 1 1 41 41 VAL HG11 H 1 0.74 . . 2 . . . . . . . . 4068 1 403 . 1 1 41 41 VAL HG12 H 1 0.74 . . 2 . . . . . . . . 4068 1 404 . 1 1 41 41 VAL HG13 H 1 0.74 . . 2 . . . . . . . . 4068 1 405 . 1 1 41 41 VAL HG21 H 1 -0.02 . . 2 . . . . . . . . 4068 1 406 . 1 1 41 41 VAL HG22 H 1 -0.02 . . 2 . . . . . . . . 4068 1 407 . 1 1 41 41 VAL HG23 H 1 -0.02 . . 2 . . . . . . . . 4068 1 408 . 1 1 41 41 VAL C C 13 181.47 . . 1 . . . . . . . . 4068 1 409 . 1 1 41 41 VAL CA C 13 67.36 . . 1 . . . . . . . . 4068 1 410 . 1 1 41 41 VAL CB C 13 31.94 . . 1 . . . . . . . . 4068 1 411 . 1 1 41 41 VAL CG1 C 13 21.32 . . 2 . . . . . . . . 4068 1 412 . 1 1 41 41 VAL CG2 C 13 22.68 . . 2 . . . . . . . . 4068 1 413 . 1 1 41 41 VAL N N 15 123.3 . . 1 . . . . . . . . 4068 1 414 . 1 1 42 42 VAL H H 1 8.08 . . 1 . . . . . . . . 4068 1 415 . 1 1 42 42 VAL HA H 1 3.94 . . 1 . . . . . . . . 4068 1 416 . 1 1 42 42 VAL HB H 1 2.31 . . 1 . . . . . . . . 4068 1 417 . 1 1 42 42 VAL HG11 H 1 1.02 . . 2 . . . . . . . . 4068 1 418 . 1 1 42 42 VAL HG12 H 1 1.02 . . 2 . . . . . . . . 4068 1 419 . 1 1 42 42 VAL HG13 H 1 1.02 . . 2 . . . . . . . . 4068 1 420 . 1 1 42 42 VAL HG21 H 1 1.06 . . 2 . . . . . . . . 4068 1 421 . 1 1 42 42 VAL HG22 H 1 1.06 . . 2 . . . . . . . . 4068 1 422 . 1 1 42 42 VAL HG23 H 1 1.06 . . 2 . . . . . . . . 4068 1 423 . 1 1 42 42 VAL C C 13 178.91 . . 1 . . . . . . . . 4068 1 424 . 1 1 42 42 VAL CA C 13 65.84 . . 1 . . . . . . . . 4068 1 425 . 1 1 42 42 VAL CB C 13 31.13 . . 1 . . . . . . . . 4068 1 426 . 1 1 42 42 VAL CG1 C 13 20.5 . . 2 . . . . . . . . 4068 1 427 . 1 1 42 42 VAL N N 15 118.73 . . 1 . . . . . . . . 4068 1 428 . 1 1 43 43 GLU H H 1 7.6 . . 1 . . . . . . . . 4068 1 429 . 1 1 43 43 GLU HA H 1 4.36 . . 1 . . . . . . . . 4068 1 430 . 1 1 43 43 GLU HB2 H 1 2.29 . . 2 . . . . . . . . 4068 1 431 . 1 1 43 43 GLU HB3 H 1 2.09 . . 2 . . . . . . . . 4068 1 432 . 1 1 43 43 GLU HG2 H 1 2.63 . . 2 . . . . . . . . 4068 1 433 . 1 1 43 43 GLU C C 13 176.54 . . 1 . . . . . . . . 4068 1 434 . 1 1 43 43 GLU CA C 13 57.15 . . 1 . . . . . . . . 4068 1 435 . 1 1 43 43 GLU CB C 13 28.03 . . 1 . . . . . . . . 4068 1 436 . 1 1 43 43 GLU CG C 13 33.03 . . 1 . . . . . . . . 4068 1 437 . 1 1 43 43 GLU N N 15 119.63 . . 1 . . . . . . . . 4068 1 438 . 1 1 44 44 SER H H 1 7.79 . . 1 . . . . . . . . 4068 1 439 . 1 1 44 44 SER HA H 1 4.55 . . 1 . . . . . . . . 4068 1 440 . 1 1 44 44 SER HB2 H 1 4.14 . . 2 . . . . . . . . 4068 1 441 . 1 1 44 44 SER HB3 H 1 3.96 . . 2 . . . . . . . . 4068 1 442 . 1 1 44 44 SER C C 13 175.47 . . 1 . . . . . . . . 4068 1 443 . 1 1 44 44 SER CA C 13 59.17 . . 1 . . . . . . . . 4068 1 444 . 1 1 44 44 SER CB C 13 64.44 . . 1 . . . . . . . . 4068 1 445 . 1 1 44 44 SER N N 15 113.86 . . 1 . . . . . . . . 4068 1 446 . 1 1 45 45 ASN H H 1 8.54 . . 1 . . . . . . . . 4068 1 447 . 1 1 45 45 ASN HA H 1 4.49 . . 1 . . . . . . . . 4068 1 448 . 1 1 45 45 ASN HB2 H 1 2.88 . . 1 . . . . . . . . 4068 1 449 . 1 1 45 45 ASN HB3 H 1 3.16 . . 1 . . . . . . . . 4068 1 450 . 1 1 45 45 ASN HD21 H 1 7.67 . . 2 . . . . . . . . 4068 1 451 . 1 1 45 45 ASN HD22 H 1 6.93 . . 2 . . . . . . . . 4068 1 452 . 1 1 45 45 ASN CA C 13 54.01 . . 1 . . . . . . . . 4068 1 453 . 1 1 45 45 ASN CB C 13 37.56 . . 1 . . . . . . . . 4068 1 454 . 1 1 45 45 ASN N N 15 120.96 . . 1 . . . . . . . . 4068 1 455 . 1 1 45 45 ASN ND2 N 15 112.64 . . 1 . . . . . . . . 4068 1 456 . 1 1 46 46 GLY H H 1 8.13 . . 1 . . . . . . . . 4068 1 457 . 1 1 46 46 GLY HA2 H 1 3.59 . . 2 . . . . . . . . 4068 1 458 . 1 1 46 46 GLY HA3 H 1 4.1 . . 2 . . . . . . . . 4068 1 459 . 1 1 46 46 GLY C C 13 175.09 . . 1 . . . . . . . . 4068 1 460 . 1 1 46 46 GLY CA C 13 45.86 . . 1 . . . . . . . . 4068 1 461 . 1 1 46 46 GLY N N 15 103.6 . . 1 . . . . . . . . 4068 1 462 . 1 1 47 47 THR H H 1 7.58 . . 1 . . . . . . . . 4068 1 463 . 1 1 47 47 THR HA H 1 4.25 . . 1 . . . . . . . . 4068 1 464 . 1 1 47 47 THR HB H 1 4.38 . . 1 . . . . . . . . 4068 1 465 . 1 1 47 47 THR HG21 H 1 1.26 . . 1 . . . . . . . . 4068 1 466 . 1 1 47 47 THR HG22 H 1 1.26 . . 1 . . . . . . . . 4068 1 467 . 1 1 47 47 THR HG23 H 1 1.26 . . 1 . . . . . . . . 4068 1 468 . 1 1 47 47 THR C C 13 174.53 . . 1 . . . . . . . . 4068 1 469 . 1 1 47 47 THR CA C 13 70.08 . . 1 . . . . . . . . 4068 1 470 . 1 1 47 47 THR CB C 13 63.08 . . 1 . . . . . . . . 4068 1 471 . 1 1 47 47 THR CG2 C 13 22.00 . . 1 . . . . . . . . 4068 1 472 . 1 1 47 47 THR N N 15 110.3 . . 1 . . . . . . . . 4068 1 473 . 1 1 48 48 LEU H H 1 7.65 . . 1 . . . . . . . . 4068 1 474 . 1 1 48 48 LEU HA H 1 4.29 . . 1 . . . . . . . . 4068 1 475 . 1 1 48 48 LEU HB2 H 1 1.55 . . 2 . . . . . . . . 4068 1 476 . 1 1 48 48 LEU HB3 H 1 1.12 . . 2 . . . . . . . . 4068 1 477 . 1 1 48 48 LEU HG H 1 0.3 . . 1 . . . . . . . . 4068 1 478 . 1 1 48 48 LEU HD11 H 1 1.25 . . 2 . . . . . . . . 4068 1 479 . 1 1 48 48 LEU HD12 H 1 1.25 . . 2 . . . . . . . . 4068 1 480 . 1 1 48 48 LEU HD13 H 1 1.25 . . 2 . . . . . . . . 4068 1 481 . 1 1 48 48 LEU HD21 H 1 1.12 . . 2 . . . . . . . . 4068 1 482 . 1 1 48 48 LEU HD22 H 1 1.12 . . 2 . . . . . . . . 4068 1 483 . 1 1 48 48 LEU HD23 H 1 1.12 . . 2 . . . . . . . . 4068 1 484 . 1 1 48 48 LEU C C 13 174.49 . . 1 . . . . . . . . 4068 1 485 . 1 1 48 48 LEU CA C 13 55.38 . . 1 . . . . . . . . 4068 1 486 . 1 1 48 48 LEU CB C 13 43.39 . . 1 . . . . . . . . 4068 1 487 . 1 1 48 48 LEU CG C 13 21.59 . . 1 . . . . . . . . 4068 1 488 . 1 1 48 48 LEU CD2 C 13 23.4 . . 2 . . . . . . . . 4068 1 489 . 1 1 48 48 LEU N N 15 124.82 . . 1 . . . . . . . . 4068 1 490 . 1 1 49 49 THR H H 1 8.58 . . 1 . . . . . . . . 4068 1 491 . 1 1 49 49 THR HA H 1 4.64 . . 1 . . . . . . . . 4068 1 492 . 1 1 49 49 THR HB H 1 4.42 . . 1 . . . . . . . . 4068 1 493 . 1 1 49 49 THR HG21 H 1 1.14 . . 1 . . . . . . . . 4068 1 494 . 1 1 49 49 THR HG22 H 1 1.14 . . 1 . . . . . . . . 4068 1 495 . 1 1 49 49 THR HG23 H 1 1.14 . . 1 . . . . . . . . 4068 1 496 . 1 1 49 49 THR C C 13 173.5 . . 1 . . . . . . . . 4068 1 497 . 1 1 49 49 THR CA C 13 59.43 . . 1 . . . . . . . . 4068 1 498 . 1 1 49 49 THR CB C 13 54.83 . . 1 . . . . . . . . 4068 1 499 . 1 1 49 49 THR N N 15 116.04 . . 1 . . . . . . . . 4068 1 500 . 1 1 50 50 LEU H H 1 8.83 . . 1 . . . . . . . . 4068 1 501 . 1 1 50 50 LEU HA H 1 4.11 . . 1 . . . . . . . . 4068 1 502 . 1 1 50 50 LEU HB2 H 1 1.01 . . 2 . . . . . . . . 4068 1 503 . 1 1 50 50 LEU HB3 H 1 1.828 . . 2 . . . . . . . . 4068 1 504 . 1 1 50 50 LEU HG H 1 0.68 . . 1 . . . . . . . . 4068 1 505 . 1 1 50 50 LEU HD11 H 1 0.05 . . 2 . . . . . . . . 4068 1 506 . 1 1 50 50 LEU HD12 H 1 0.05 . . 2 . . . . . . . . 4068 1 507 . 1 1 50 50 LEU HD13 H 1 0.05 . . 2 . . . . . . . . 4068 1 508 . 1 1 50 50 LEU HD21 H 1 -0.11 . . 2 . . . . . . . . 4068 1 509 . 1 1 50 50 LEU HD22 H 1 -0.11 . . 2 . . . . . . . . 4068 1 510 . 1 1 50 50 LEU HD23 H 1 -0.11 . . 2 . . . . . . . . 4068 1 511 . 1 1 50 50 LEU C C 13 176.43 . . 1 . . . . . . . . 4068 1 512 . 1 1 50 50 LEU CA C 13 54.82 . . 1 . . . . . . . . 4068 1 513 . 1 1 50 50 LEU CB C 13 42.81 . . 1 . . . . . . . . 4068 1 514 . 1 1 50 50 LEU CG C 13 26.77 . . 1 . . . . . . . . 4068 1 515 . 1 1 50 50 LEU CD1 C 13 25.95 . . 2 . . . . . . . . 4068 1 516 . 1 1 50 50 LEU CD2 C 13 24.32 . . 2 . . . . . . . . 4068 1 517 . 1 1 50 50 LEU N N 15 122.55 . . 1 . . . . . . . . 4068 1 518 . 1 1 51 51 SER H H 1 8.83 . . 1 . . . . . . . . 4068 1 519 . 1 1 51 51 SER HA H 1 4.52 . . 1 . . . . . . . . 4068 1 520 . 1 1 51 51 SER HB2 H 1 3.39 . . 1 . . . . . . . . 4068 1 521 . 1 1 51 51 SER HB3 H 1 3.57 . . 1 . . . . . . . . 4068 1 522 . 1 1 51 51 SER C C 13 174.95 . . 1 . . . . . . . . 4068 1 523 . 1 1 51 51 SER CA C 13 60.29 . . 1 . . . . . . . . 4068 1 524 . 1 1 51 51 SER CB C 13 63.45 . . 1 . . . . . . . . 4068 1 525 . 1 1 51 51 SER N N 15 123.12 . . 1 . . . . . . . . 4068 1 526 . 1 1 52 52 HIS H H 1 7.28 . . 1 . . . . . . . . 4068 1 527 . 1 1 52 52 HIS HA H 1 4.51 . . 1 . . . . . . . . 4068 1 528 . 1 1 52 52 HIS HB2 H 1 3.78 . . 2 . . . . . . . . 4068 1 529 . 1 1 52 52 HIS HB3 H 1 3.35 . . 2 . . . . . . . . 4068 1 530 . 1 1 52 52 HIS HD2 H 1 8.76 . . 1 . . . . . . . . 4068 1 531 . 1 1 52 52 HIS HE1 H 1 7.26 . . 1 . . . . . . . . 4068 1 532 . 1 1 52 52 HIS C C 13 173.23 . . 1 . . . . . . . . 4068 1 533 . 1 1 52 52 HIS CA C 13 54.69 . . 1 . . . . . . . . 4068 1 534 . 1 1 52 52 HIS CB C 13 29.23 . . 1 . . . . . . . . 4068 1 535 . 1 1 52 52 HIS N N 15 107.82 . . 1 . . . . . . . . 4068 1 536 . 1 1 53 53 PHE H H 1 9.2 . . 1 . . . . . . . . 4068 1 537 . 1 1 53 53 PHE HA H 1 4.33 . . 1 . . . . . . . . 4068 1 538 . 1 1 53 53 PHE HB2 H 1 3.04 . . 1 . . . . . . . . 4068 1 539 . 1 1 53 53 PHE HB3 H 1 3.24 . . 1 . . . . . . . . 4068 1 540 . 1 1 53 53 PHE HD1 H 1 6.9 . . 2 . . . . . . . . 4068 1 541 . 1 1 53 53 PHE HE1 H 1 6.67 . . 2 . . . . . . . . 4068 1 542 . 1 1 53 53 PHE HZ H 1 6.62 . . 1 . . . . . . . . 4068 1 543 . 1 1 53 53 PHE C C 13 178.01 . . 1 . . . . . . . . 4068 1 544 . 1 1 53 53 PHE CA C 13 60.5 . . 1 . . . . . . . . 4068 1 545 . 1 1 53 53 PHE CB C 13 39.65 . . 1 . . . . . . . . 4068 1 546 . 1 1 53 53 PHE N N 15 120.46 . . 1 . . . . . . . . 4068 1 547 . 1 1 54 54 GLY H H 1 8.27 . . 1 . . . . . . . . 4068 1 548 . 1 1 54 54 GLY HA2 H 1 4.57 . . 2 . . . . . . . . 4068 1 549 . 1 1 54 54 GLY HA3 H 1 3.58 . . 2 . . . . . . . . 4068 1 550 . 1 1 54 54 GLY C C 13 177.99 . . 1 . . . . . . . . 4068 1 551 . 1 1 54 54 GLY CA C 13 44.39 . . 1 . . . . . . . . 4068 1 552 . 1 1 54 54 GLY N N 15 114.32 . . 1 . . . . . . . . 4068 1 553 . 1 1 55 55 LYS H H 1 8.09 . . 1 . . . . . . . . 4068 1 554 . 1 1 55 55 LYS HA H 1 4.06 . . 1 . . . . . . . . 4068 1 555 . 1 1 55 55 LYS HB2 H 1 1.88 . . 2 . . . . . . . . 4068 1 556 . 1 1 55 55 LYS HB3 H 1 1.77 . . 2 . . . . . . . . 4068 1 557 . 1 1 55 55 LYS HG2 H 1 1.76 . . 2 . . . . . . . . 4068 1 558 . 1 1 55 55 LYS HD2 H 1 1.53 . . 2 . . . . . . . . 4068 1 559 . 1 1 55 55 LYS HE2 H 1 3.01 . . 2 . . . . . . . . 4068 1 560 . 1 1 55 55 LYS HZ1 H 1 7.64 . . 1 . . . . . . . . 4068 1 561 . 1 1 55 55 LYS HZ2 H 1 7.64 . . 1 . . . . . . . . 4068 1 562 . 1 1 55 55 LYS HZ3 H 1 7.64 . . 1 . . . . . . . . 4068 1 563 . 1 1 55 55 LYS CA C 13 56.19 . . 1 . . . . . . . . 4068 1 564 . 1 1 55 55 LYS CB C 13 33.31 . . 1 . . . . . . . . 4068 1 565 . 1 1 55 55 LYS CG C 13 29.77 . . 1 . . . . . . . . 4068 1 566 . 1 1 55 55 LYS CD C 13 24.86 . . 1 . . . . . . . . 4068 1 567 . 1 1 55 55 LYS CE C 13 42.3 . . 1 . . . . . . . . 4068 1 568 . 1 1 55 55 LYS N N 15 113.43 . . 1 . . . . . . . . 4068 1 569 . 1 1 56 56 CYS H H 1 8.5 . . 1 . . . . . . . . 4068 1 570 . 1 1 56 56 CYS HA H 1 4.53 . . 1 . . . . . . . . 4068 1 571 . 1 1 56 56 CYS HB2 H 1 2.59 . . 2 . . . . . . . . 4068 1 572 . 1 1 56 56 CYS HB3 H 1 3.3 . . 2 . . . . . . . . 4068 1 573 . 1 1 56 56 CYS CA C 13 54.83 . . 1 . . . . . . . . 4068 1 574 . 1 1 56 56 CYS CB C 13 37.67 . . 1 . . . . . . . . 4068 1 575 . 1 1 56 56 CYS N N 15 121.63 . . 1 . . . . . . . . 4068 1 stop_ save_