data_42 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 42 _Entry.Title ; Two-Dimensional NMR Studies of Kazal Proteinase Inhibitors. 1. Sequence-Specific Assignments and Secondary Structure of Turkey Ovomucoid Third Domain ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-04-13 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _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 Andrew Robertson . D. . 42 2 William Westler . M. . 42 3 John Markley . L. . 42 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 42 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 361 42 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 5 . . 2010-06-10 . revision BMRB 'Complete natural source information' 42 4 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 42 3 . . 1996-04-13 . revision BMRB 'Link to the Protein Data Bank added' 42 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 42 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 42 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 42 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Robertson, Andrew D., Westler, William M., Markley, John L., "Two-Dimensional NMR Studies of Kazal Proteinase Inhibitors. 1. Sequence-Specific Assignments and Secondary Structure of Turkey Ovomucoid Third Domain," Biochemistry 27, 2519-2529 (1988). ; _Citation.Title ; Two-Dimensional NMR Studies of Kazal Proteinase Inhibitors. 1. Sequence-Specific Assignments and Secondary Structure of Turkey Ovomucoid Third Domain ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 27 _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 2519 _Citation.Page_last 2529 _Citation.Year 1988 _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 Andrew Robertson . D. . 42 1 2 William Westler . M. . 42 1 3 John Markley . L. . 42 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_ovomucoid_third_domain _Assembly.Sf_category assembly _Assembly.Sf_framecode system_ovomucoid_third_domain _Assembly.Entry_ID 42 _Assembly.ID 1 _Assembly.Name '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 . _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . 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 'ovomucoid third domain' 1 $ovomucoid_third_domain . . . . . . . . . 42 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'ovomucoid third domain' system 42 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_ovomucoid_third_domain _Entity.Sf_category entity _Entity.Sf_framecode ovomucoid_third_domain _Entity.Entry_ID 42 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name '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 ; LAAVSVDCSEYPKPACTLEY RPLCGSDNKTYGNKCNFCNA VVESNGTLTLSHFGKC ; _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 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 1374 . "ovomucoid third domain" . . . . . 67.86 38 100.00 100.00 3.19e-18 . . . . 42 1 2 no BMRB 1375 . "ovomucoid third domain" . . . . . 67.86 38 100.00 100.00 3.19e-18 . . . . 42 1 3 no BMRB 4068 . "turkey ovomucoid third domain" . . . . . 100.00 56 100.00 100.00 7.49e-32 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 1 9 no PDB 1DS2 . "Crystal Structure Of Sgpb:omtky3-Coo-Leu18i" . . . . . 91.07 51 98.04 98.04 1.15e-27 . . . . 42 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 . . . . 42 1 11 no PDB 1IY5 . "Solution Structure Of Wild Type Omsvp3" . . . . . 96.43 54 98.15 100.00 2.38e-30 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 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 . . . . 42 1 44 no PIR A31445 . "ovomucoid, third domain - ruffed grouse (fragment) [Bonasa umbellus]" . . . . . 100.00 56 98.21 100.00 1.04e-31 . . . . 42 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 . . . . 42 1 46 no PIR C31438 . "ovomucoid, third domain - cheer pheasant (fragment) [Catreus wallichii]" . . . . . 100.00 56 98.21 100.00 1.04e-31 . . . . 42 1 47 no PIR E31437 . "ovomucoid, third domain - silver pheasant (fragment) [Lophura nycthemera]" . . . . . 100.00 56 98.21 100.00 1.04e-31 . . . . 42 1 48 no PIR E31442 . "ovomucoid, third domain - koklass pheasant (fragment) [Pucrasia macrolopha]" . . . . . 100.00 56 98.21 100.00 1.04e-31 . . . . 42 1 49 no SP P05609 . "RecName: Full=Ovomucoid" . . . . . 100.00 56 98.21 100.00 2.94e-31 . . . . 42 1 50 no SP P52245 . "RecName: Full=Ovomucoid" . . . . . 100.00 56 100.00 100.00 7.49e-32 . . . . 42 1 51 no SP P52263 . "RecName: Full=Ovomucoid" . . . . . 96.43 54 98.15 100.00 6.13e-30 . . . . 42 1 52 no SP P67944 . "RecName: Full=Ovomucoid" . . . . . 100.00 56 98.21 100.00 1.04e-31 . . . . 42 1 53 no SP P67945 . "RecName: Full=Ovomucoid" . . . . . 100.00 56 98.21 100.00 1.04e-31 . . . . 42 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'ovomucoid third domain' common 42 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 . 42 1 2 . ALA . 42 1 3 . ALA . 42 1 4 . VAL . 42 1 5 . SER . 42 1 6 . VAL . 42 1 7 . ASP . 42 1 8 . CYS . 42 1 9 . SER . 42 1 10 . GLU . 42 1 11 . TYR . 42 1 12 . PRO . 42 1 13 . LYS . 42 1 14 . PRO . 42 1 15 . ALA . 42 1 16 . CYS . 42 1 17 . THR . 42 1 18 . LEU . 42 1 19 . GLU . 42 1 20 . TYR . 42 1 21 . ARG . 42 1 22 . PRO . 42 1 23 . LEU . 42 1 24 . CYS . 42 1 25 . GLY . 42 1 26 . SER . 42 1 27 . ASP . 42 1 28 . ASN . 42 1 29 . LYS . 42 1 30 . THR . 42 1 31 . TYR . 42 1 32 . GLY . 42 1 33 . ASN . 42 1 34 . LYS . 42 1 35 . CYS . 42 1 36 . ASN . 42 1 37 . PHE . 42 1 38 . CYS . 42 1 39 . ASN . 42 1 40 . ALA . 42 1 41 . VAL . 42 1 42 . VAL . 42 1 43 . GLU . 42 1 44 . SER . 42 1 45 . ASN . 42 1 46 . GLY . 42 1 47 . THR . 42 1 48 . LEU . 42 1 49 . THR . 42 1 50 . LEU . 42 1 51 . SER . 42 1 52 . HIS . 42 1 53 . PHE . 42 1 54 . GLY . 42 1 55 . LYS . 42 1 56 . CYS . 42 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 42 1 . ALA 2 2 42 1 . ALA 3 3 42 1 . VAL 4 4 42 1 . SER 5 5 42 1 . VAL 6 6 42 1 . ASP 7 7 42 1 . CYS 8 8 42 1 . SER 9 9 42 1 . GLU 10 10 42 1 . TYR 11 11 42 1 . PRO 12 12 42 1 . LYS 13 13 42 1 . PRO 14 14 42 1 . ALA 15 15 42 1 . CYS 16 16 42 1 . THR 17 17 42 1 . LEU 18 18 42 1 . GLU 19 19 42 1 . TYR 20 20 42 1 . ARG 21 21 42 1 . PRO 22 22 42 1 . LEU 23 23 42 1 . CYS 24 24 42 1 . GLY 25 25 42 1 . SER 26 26 42 1 . ASP 27 27 42 1 . ASN 28 28 42 1 . LYS 29 29 42 1 . THR 30 30 42 1 . TYR 31 31 42 1 . GLY 32 32 42 1 . ASN 33 33 42 1 . LYS 34 34 42 1 . CYS 35 35 42 1 . ASN 36 36 42 1 . PHE 37 37 42 1 . CYS 38 38 42 1 . ASN 39 39 42 1 . ALA 40 40 42 1 . VAL 41 41 42 1 . VAL 42 42 42 1 . GLU 43 43 42 1 . SER 44 44 42 1 . ASN 45 45 42 1 . GLY 46 46 42 1 . THR 47 47 42 1 . LEU 48 48 42 1 . THR 49 49 42 1 . LEU 50 50 42 1 . SER 51 51 42 1 . HIS 52 52 42 1 . PHE 53 53 42 1 . GLY 54 54 42 1 . LYS 55 55 42 1 . CYS 56 56 42 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 42 _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 $ovomucoid_third_domain . 9103 organism . 'Meleagris gallopavo' turkey . . Eukaryota Metazoa Meleagris gallopavo generic . . . egg . . . . . . . . . . . . . . . . 42 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 42 _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 $ovomucoid_third_domain . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 42 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 42 _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 . save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_condition_set_one _Sample_condition_list.Entry_ID 42 _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 4 . na 42 1 temperature 298 . K 42 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 42 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 42 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 unknown unknown . 0 'spectrometer information not available' . . 42 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 42 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_condition_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 42 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_par_set_one _Chem_shift_reference.Entry_ID 42 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H . TSP . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 42 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_data_set_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode 'chemical_shift_assignment_data_set_one' _Assigned_chem_shift_list.Entry_ID 42 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_condition_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_par_set_one _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 . 42 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 LEU HA H 1 4.05 . . 1 . . . . . . . . 42 1 2 . 1 1 1 1 LEU HG H 1 1.7 . . 1 . . . . . . . . 42 1 3 . 1 1 1 1 LEU HD11 H 1 1 . . 2 . . . . . . . . 42 1 4 . 1 1 1 1 LEU HD12 H 1 1 . . 2 . . . . . . . . 42 1 5 . 1 1 1 1 LEU HD13 H 1 1 . . 2 . . . . . . . . 42 1 6 . 1 1 1 1 LEU HD21 H 1 .96 . . 2 . . . . . . . . 42 1 7 . 1 1 1 1 LEU HD22 H 1 .96 . . 2 . . . . . . . . 42 1 8 . 1 1 1 1 LEU HD23 H 1 .96 . . 2 . . . . . . . . 42 1 9 . 1 1 2 2 ALA H H 1 8.65 . . 1 . . . . . . . . 42 1 10 . 1 1 2 2 ALA HA H 1 4.42 . . 1 . . . . . . . . 42 1 11 . 1 1 2 2 ALA HB1 H 1 1.42 . . 1 . . . . . . . . 42 1 12 . 1 1 2 2 ALA HB2 H 1 1.42 . . 1 . . . . . . . . 42 1 13 . 1 1 2 2 ALA HB3 H 1 1.42 . . 1 . . . . . . . . 42 1 14 . 1 1 3 3 ALA H H 1 8.42 . . 1 . . . . . . . . 42 1 15 . 1 1 3 3 ALA HA H 1 4.37 . . 1 . . . . . . . . 42 1 16 . 1 1 3 3 ALA HB1 H 1 1.41 . . 1 . . . . . . . . 42 1 17 . 1 1 3 3 ALA HB2 H 1 1.41 . . 1 . . . . . . . . 42 1 18 . 1 1 3 3 ALA HB3 H 1 1.41 . . 1 . . . . . . . . 42 1 19 . 1 1 4 4 VAL H H 1 8.15 . . 1 . . . . . . . . 42 1 20 . 1 1 4 4 VAL HA H 1 4.27 . . 1 . . . . . . . . 42 1 21 . 1 1 4 4 VAL HB H 1 2.05 . . 1 . . . . . . . . 42 1 22 . 1 1 4 4 VAL HG11 H 1 .93 . . 2 . . . . . . . . 42 1 23 . 1 1 4 4 VAL HG12 H 1 .93 . . 2 . . . . . . . . 42 1 24 . 1 1 4 4 VAL HG13 H 1 .93 . . 2 . . . . . . . . 42 1 25 . 1 1 4 4 VAL HG21 H 1 .88 . . 2 . . . . . . . . 42 1 26 . 1 1 4 4 VAL HG22 H 1 .88 . . 2 . . . . . . . . 42 1 27 . 1 1 4 4 VAL HG23 H 1 .88 . . 2 . . . . . . . . 42 1 28 . 1 1 5 5 SER H H 1 8.25 . . 1 . . . . . . . . 42 1 29 . 1 1 5 5 SER HA H 1 4.56 . . 1 . . . . . . . . 42 1 30 . 1 1 5 5 SER HB2 H 1 3.84 . . 1 . . . . . . . . 42 1 31 . 1 1 5 5 SER HB3 H 1 3.84 . . 1 . . . . . . . . 42 1 32 . 1 1 6 6 VAL H H 1 8.32 . . 1 . . . . . . . . 42 1 33 . 1 1 6 6 VAL HA H 1 4.29 . . 1 . . . . . . . . 42 1 34 . 1 1 6 6 VAL HB H 1 1.97 . . 1 . . . . . . . . 42 1 35 . 1 1 6 6 VAL HG11 H 1 .82 . . 2 . . . . . . . . 42 1 36 . 1 1 6 6 VAL HG12 H 1 .82 . . 2 . . . . . . . . 42 1 37 . 1 1 6 6 VAL HG13 H 1 .82 . . 2 . . . . . . . . 42 1 38 . 1 1 6 6 VAL HG21 H 1 .92 . . 2 . . . . . . . . 42 1 39 . 1 1 6 6 VAL HG22 H 1 .92 . . 2 . . . . . . . . 42 1 40 . 1 1 6 6 VAL HG23 H 1 .92 . . 2 . . . . . . . . 42 1 41 . 1 1 7 7 ASP H H 1 8.61 . . 1 . . . . . . . . 42 1 42 . 1 1 7 7 ASP HA H 1 4.76 . . 1 . . . . . . . . 42 1 43 . 1 1 7 7 ASP HB2 H 1 2.98 . . 2 . . . . . . . . 42 1 44 . 1 1 7 7 ASP HB3 H 1 2.72 . . 2 . . . . . . . . 42 1 45 . 1 1 8 8 CYS H H 1 8.9 . . 1 . . . . . . . . 42 1 46 . 1 1 8 8 CYS HA H 1 5.33 . . 1 . . . . . . . . 42 1 47 . 1 1 8 8 CYS HB2 H 1 2.55 . . 2 . . . . . . . . 42 1 48 . 1 1 8 8 CYS HB3 H 1 3.36 . . 2 . . . . . . . . 42 1 49 . 1 1 9 9 SER H H 1 8.69 . . 1 . . . . . . . . 42 1 50 . 1 1 9 9 SER HA H 1 4.27 . . 1 . . . . . . . . 42 1 51 . 1 1 9 9 SER HB2 H 1 3.98 . . 2 . . . . . . . . 42 1 52 . 1 1 9 9 SER HB3 H 1 4.08 . . 2 . . . . . . . . 42 1 53 . 1 1 10 10 GLU H H 1 8.73 . . 1 . . . . . . . . 42 1 54 . 1 1 10 10 GLU HA H 1 4.33 . . 1 . . . . . . . . 42 1 55 . 1 1 10 10 GLU HB2 H 1 1.78 . . 2 . . . . . . . . 42 1 56 . 1 1 10 10 GLU HB3 H 1 2.08 . . 2 . . . . . . . . 42 1 57 . 1 1 10 10 GLU HG2 H 1 2.31 . . 1 . . . . . . . . 42 1 58 . 1 1 10 10 GLU HG3 H 1 2.31 . . 1 . . . . . . . . 42 1 59 . 1 1 11 11 TYR H H 1 7.43 . . 1 . . . . . . . . 42 1 60 . 1 1 11 11 TYR HA H 1 4.07 . . 1 . . . . . . . . 42 1 61 . 1 1 11 11 TYR HB2 H 1 2.78 . . 2 . . . . . . . . 42 1 62 . 1 1 11 11 TYR HB3 H 1 2.9 . . 2 . . . . . . . . 42 1 63 . 1 1 11 11 TYR HD1 H 1 7.15 . . 1 . . . . . . . . 42 1 64 . 1 1 11 11 TYR HD2 H 1 7.15 . . 1 . . . . . . . . 42 1 65 . 1 1 12 12 PRO HA H 1 5.22 . . 1 . . . . . . . . 42 1 66 . 1 1 12 12 PRO HB2 H 1 2.08 . . 2 . . . . . . . . 42 1 67 . 1 1 12 12 PRO HB3 H 1 2.47 . . 2 . . . . . . . . 42 1 68 . 1 1 12 12 PRO HG2 H 1 1.87 . . 2 . . . . . . . . 42 1 69 . 1 1 12 12 PRO HG3 H 1 1.98 . . 2 . . . . . . . . 42 1 70 . 1 1 12 12 PRO HD2 H 1 3.56 . . 2 . . . . . . . . 42 1 71 . 1 1 12 12 PRO HD3 H 1 3.68 . . 2 . . . . . . . . 42 1 72 . 1 1 13 13 LYS H H 1 9.37 . . 1 . . . . . . . . 42 1 73 . 1 1 13 13 LYS HA H 1 4.89 . . 1 . . . . . . . . 42 1 74 . 1 1 13 13 LYS HB2 H 1 1.59 . . 2 . . . . . . . . 42 1 75 . 1 1 13 13 LYS HB3 H 1 1.9 . . 2 . . . . . . . . 42 1 76 . 1 1 13 13 LYS HG2 H 1 .91 . . 2 . . . . . . . . 42 1 77 . 1 1 13 13 LYS HG3 H 1 1.14 . . 2 . . . . . . . . 42 1 78 . 1 1 13 13 LYS HD2 H 1 1.6 . . 2 . . . . . . . . 42 1 79 . 1 1 13 13 LYS HD3 H 1 1.43 . . 2 . . . . . . . . 42 1 80 . 1 1 13 13 LYS HE2 H 1 2.4 . . 2 . . . . . . . . 42 1 81 . 1 1 13 13 LYS HE3 H 1 2.57 . . 2 . . . . . . . . 42 1 82 . 1 1 14 14 PRO HA H 1 4.36 . . 1 . . . . . . . . 42 1 83 . 1 1 14 14 PRO HB2 H 1 2.31 . . 1 . . . . . . . . 42 1 84 . 1 1 14 14 PRO HB3 H 1 2.31 . . 1 . . . . . . . . 42 1 85 . 1 1 14 14 PRO HG2 H 1 2.05 . . 1 . . . . . . . . 42 1 86 . 1 1 14 14 PRO HG3 H 1 2.05 . . 1 . . . . . . . . 42 1 87 . 1 1 14 14 PRO HD2 H 1 3.76 . . 2 . . . . . . . . 42 1 88 . 1 1 14 14 PRO HD3 H 1 3.82 . . 2 . . . . . . . . 42 1 89 . 1 1 15 15 ALA H H 1 7.48 . . 1 . . . . . . . . 42 1 90 . 1 1 15 15 ALA HA H 1 4.58 . . 1 . . . . . . . . 42 1 91 . 1 1 15 15 ALA HB1 H 1 1.33 . . 1 . . . . . . . . 42 1 92 . 1 1 15 15 ALA HB2 H 1 1.33 . . 1 . . . . . . . . 42 1 93 . 1 1 15 15 ALA HB3 H 1 1.33 . . 1 . . . . . . . . 42 1 94 . 1 1 16 16 CYS H H 1 8.58 . . 1 . . . . . . . . 42 1 95 . 1 1 16 16 CYS HA H 1 5.32 . . 1 . . . . . . . . 42 1 96 . 1 1 16 16 CYS HB2 H 1 2.79 . . 2 . . . . . . . . 42 1 97 . 1 1 16 16 CYS HB3 H 1 3.37 . . 2 . . . . . . . . 42 1 98 . 1 1 17 17 THR H H 1 8.27 . . 1 . . . . . . . . 42 1 99 . 1 1 17 17 THR HA H 1 4.53 . . 1 . . . . . . . . 42 1 100 . 1 1 17 17 THR HB H 1 4.63 . . 1 . . . . . . . . 42 1 101 . 1 1 17 17 THR HG21 H 1 1.36 . . 1 . . . . . . . . 42 1 102 . 1 1 17 17 THR HG22 H 1 1.36 . . 1 . . . . . . . . 42 1 103 . 1 1 17 17 THR HG23 H 1 1.36 . . 1 . . . . . . . . 42 1 104 . 1 1 18 18 LEU H H 1 8.42 . . 1 . . . . . . . . 42 1 105 . 1 1 18 18 LEU HA H 1 4.42 . . 1 . . . . . . . . 42 1 106 . 1 1 18 18 LEU HB2 H 1 1.66 . . 1 . . . . . . . . 42 1 107 . 1 1 18 18 LEU HB3 H 1 1.66 . . 1 . . . . . . . . 42 1 108 . 1 1 18 18 LEU HG H 1 1.73 . . 1 . . . . . . . . 42 1 109 . 1 1 18 18 LEU HD11 H 1 .9 . . 2 . . . . . . . . 42 1 110 . 1 1 18 18 LEU HD12 H 1 .9 . . 2 . . . . . . . . 42 1 111 . 1 1 18 18 LEU HD13 H 1 .9 . . 2 . . . . . . . . 42 1 112 . 1 1 18 18 LEU HD21 H 1 .96 . . 2 . . . . . . . . 42 1 113 . 1 1 18 18 LEU HD22 H 1 .96 . . 2 . . . . . . . . 42 1 114 . 1 1 18 18 LEU HD23 H 1 .96 . . 2 . . . . . . . . 42 1 115 . 1 1 19 19 GLU H H 1 8.06 . . 1 . . . . . . . . 42 1 116 . 1 1 19 19 GLU HA H 1 4.14 . . 1 . . . . . . . . 42 1 117 . 1 1 19 19 GLU HB2 H 1 2 . . 1 . . . . . . . . 42 1 118 . 1 1 19 19 GLU HB3 H 1 2 . . 1 . . . . . . . . 42 1 119 . 1 1 19 19 GLU HG2 H 1 2.28 . . 2 . . . . . . . . 42 1 120 . 1 1 19 19 GLU HG3 H 1 2.37 . . 2 . . . . . . . . 42 1 121 . 1 1 20 20 TYR H H 1 8.93 . . 1 . . . . . . . . 42 1 122 . 1 1 20 20 TYR HA H 1 5.06 . . 1 . . . . . . . . 42 1 123 . 1 1 20 20 TYR HB2 H 1 2.92 . . 2 . . . . . . . . 42 1 124 . 1 1 20 20 TYR HB3 H 1 3.11 . . 2 . . . . . . . . 42 1 125 . 1 1 20 20 TYR HD1 H 1 7.28 . . 1 . . . . . . . . 42 1 126 . 1 1 20 20 TYR HD2 H 1 7.28 . . 1 . . . . . . . . 42 1 127 . 1 1 20 20 TYR HE1 H 1 6.82 . . 1 . . . . . . . . 42 1 128 . 1 1 20 20 TYR HE2 H 1 6.82 . . 1 . . . . . . . . 42 1 129 . 1 1 21 21 ARG H H 1 8.89 . . 1 . . . . . . . . 42 1 130 . 1 1 21 21 ARG HA H 1 4.46 . . 1 . . . . . . . . 42 1 131 . 1 1 21 21 ARG HB2 H 1 1.74 . . 1 . . . . . . . . 42 1 132 . 1 1 21 21 ARG HB3 H 1 1.74 . . 1 . . . . . . . . 42 1 133 . 1 1 21 21 ARG HG2 H 1 1.59 . . 1 . . . . . . . . 42 1 134 . 1 1 21 21 ARG HG3 H 1 1.59 . . 1 . . . . . . . . 42 1 135 . 1 1 21 21 ARG HD2 H 1 3.2 . . 2 . . . . . . . . 42 1 136 . 1 1 21 21 ARG HD3 H 1 3.29 . . 2 . . . . . . . . 42 1 137 . 1 1 21 21 ARG HE H 1 7.25 . . 1 . . . . . . . . 42 1 138 . 1 1 22 22 PRO HA H 1 4.52 . . 1 . . . . . . . . 42 1 139 . 1 1 22 22 PRO HB2 H 1 1.67 . . 1 . . . . . . . . 42 1 140 . 1 1 22 22 PRO HB3 H 1 1.67 . . 1 . . . . . . . . 42 1 141 . 1 1 22 22 PRO HG2 H 1 1.73 . . 1 . . . . . . . . 42 1 142 . 1 1 22 22 PRO HG3 H 1 1.73 . . 1 . . . . . . . . 42 1 143 . 1 1 22 22 PRO HD2 H 1 3.36 . . 1 . . . . . . . . 42 1 144 . 1 1 22 22 PRO HD3 H 1 3.36 . . 1 . . . . . . . . 42 1 145 . 1 1 23 23 LEU H H 1 8.48 . . 1 . . . . . . . . 42 1 146 . 1 1 23 23 LEU HA H 1 4.28 . . 1 . . . . . . . . 42 1 147 . 1 1 23 23 LEU HB2 H 1 .98 . . 1 . . . . . . . . 42 1 148 . 1 1 23 23 LEU HB3 H 1 .98 . . 1 . . . . . . . . 42 1 149 . 1 1 23 23 LEU HG H 1 1.39 . . 1 . . . . . . . . 42 1 150 . 1 1 23 23 LEU HD11 H 1 .41 . . 2 . . . . . . . . 42 1 151 . 1 1 23 23 LEU HD12 H 1 .41 . . 2 . . . . . . . . 42 1 152 . 1 1 23 23 LEU HD13 H 1 .41 . . 2 . . . . . . . . 42 1 153 . 1 1 23 23 LEU HD21 H 1 .48 . . 2 . . . . . . . . 42 1 154 . 1 1 23 23 LEU HD22 H 1 .48 . . 2 . . . . . . . . 42 1 155 . 1 1 23 23 LEU HD23 H 1 .48 . . 2 . . . . . . . . 42 1 156 . 1 1 24 24 CYS H H 1 8.17 . . 1 . . . . . . . . 42 1 157 . 1 1 24 24 CYS HA H 1 5.23 . . 1 . . . . . . . . 42 1 158 . 1 1 24 24 CYS HB2 H 1 1.35 . . 2 . . . . . . . . 42 1 159 . 1 1 24 24 CYS HB3 H 1 2.4 . . 2 . . . . . . . . 42 1 160 . 1 1 25 25 GLY H H 1 9.4 . . 1 . . . . . . . . 42 1 161 . 1 1 25 25 GLY HA2 H 1 4.5 . . 2 . . . . . . . . 42 1 162 . 1 1 25 25 GLY HA3 H 1 4.68 . . 2 . . . . . . . . 42 1 163 . 1 1 26 26 SER H H 1 9.37 . . 1 . . . . . . . . 42 1 164 . 1 1 26 26 SER HA H 1 4.15 . . 1 . . . . . . . . 42 1 165 . 1 1 26 26 SER HB2 H 1 3.82 . . 2 . . . . . . . . 42 1 166 . 1 1 26 26 SER HB3 H 1 4.1 . . 2 . . . . . . . . 42 1 167 . 1 1 27 27 ASP H H 1 8.43 . . 1 . . . . . . . . 42 1 168 . 1 1 27 27 ASP HA H 1 4.43 . . 1 . . . . . . . . 42 1 169 . 1 1 27 27 ASP HB2 H 1 2.59 . . 2 . . . . . . . . 42 1 170 . 1 1 27 27 ASP HB3 H 1 3.01 . . 2 . . . . . . . . 42 1 171 . 1 1 28 28 ASN H H 1 8.65 . . 1 . . . . . . . . 42 1 172 . 1 1 28 28 ASN HA H 1 4.4 . . 1 . . . . . . . . 42 1 173 . 1 1 28 28 ASN HB2 H 1 2.82 . . 2 . . . . . . . . 42 1 174 . 1 1 28 28 ASN HB3 H 1 3.17 . . 2 . . . . . . . . 42 1 175 . 1 1 28 28 ASN HD21 H 1 6.85 . . 2 . . . . . . . . 42 1 176 . 1 1 28 28 ASN HD22 H 1 7.53 . . 2 . . . . . . . . 42 1 177 . 1 1 29 29 LYS H H 1 7.8 . . 1 . . . . . . . . 42 1 178 . 1 1 29 29 LYS HA H 1 4.4 . . 1 . . . . . . . . 42 1 179 . 1 1 29 29 LYS HB2 H 1 1.44 . . 2 . . . . . . . . 42 1 180 . 1 1 29 29 LYS HB3 H 1 1.66 . . 2 . . . . . . . . 42 1 181 . 1 1 29 29 LYS HG2 H 1 .81 . . 2 . . . . . . . . 42 1 182 . 1 1 29 29 LYS HG3 H 1 1.14 . . 2 . . . . . . . . 42 1 183 . 1 1 29 29 LYS HD2 H 1 1.43 . . 2 . . . . . . . . 42 1 184 . 1 1 29 29 LYS HD3 H 1 1.54 . . 2 . . . . . . . . 42 1 185 . 1 1 29 29 LYS HE2 H 1 2.82 . . 1 . . . . . . . . 42 1 186 . 1 1 29 29 LYS HE3 H 1 2.82 . . 1 . . . . . . . . 42 1 187 . 1 1 29 29 LYS HZ1 H 1 7.45 . . 1 . . . . . . . . 42 1 188 . 1 1 29 29 LYS HZ2 H 1 7.45 . . 1 . . . . . . . . 42 1 189 . 1 1 29 29 LYS HZ3 H 1 7.45 . . 1 . . . . . . . . 42 1 190 . 1 1 30 30 THR H H 1 8.29 . . 1 . . . . . . . . 42 1 191 . 1 1 30 30 THR HA H 1 4.78 . . 1 . . . . . . . . 42 1 192 . 1 1 30 30 THR HB H 1 4.02 . . 1 . . . . . . . . 42 1 193 . 1 1 30 30 THR HG21 H 1 1.18 . . 1 . . . . . . . . 42 1 194 . 1 1 30 30 THR HG22 H 1 1.18 . . 1 . . . . . . . . 42 1 195 . 1 1 30 30 THR HG23 H 1 1.18 . . 1 . . . . . . . . 42 1 196 . 1 1 31 31 TYR H H 1 9.7 . . 1 . . . . . . . . 42 1 197 . 1 1 31 31 TYR HA H 1 4.5 . . 1 . . . . . . . . 42 1 198 . 1 1 31 31 TYR HB2 H 1 2.79 . . 2 . . . . . . . . 42 1 199 . 1 1 31 31 TYR HB3 H 1 2.9 . . 2 . . . . . . . . 42 1 200 . 1 1 32 32 GLY H H 1 9.21 . . 1 . . . . . . . . 42 1 201 . 1 1 32 32 GLY HA2 H 1 3.68 . . 2 . . . . . . . . 42 1 202 . 1 1 32 32 GLY HA3 H 1 4.12 . . 2 . . . . . . . . 42 1 203 . 1 1 33 33 ASN H H 1 7.43 . . 1 . . . . . . . . 42 1 204 . 1 1 33 33 ASN HA H 1 4.81 . . 1 . . . . . . . . 42 1 205 . 1 1 33 33 ASN HB2 H 1 3.19 . . 2 . . . . . . . . 42 1 206 . 1 1 33 33 ASN HB3 H 1 3.67 . . 2 . . . . . . . . 42 1 207 . 1 1 33 33 ASN HD21 H 1 6.32 . . 2 . . . . . . . . 42 1 208 . 1 1 33 33 ASN HD22 H 1 8.11 . . 2 . . . . . . . . 42 1 209 . 1 1 34 34 LYS H H 1 8.92 . . 1 . . . . . . . . 42 1 210 . 1 1 34 34 LYS HA H 1 3.86 . . 1 . . . . . . . . 42 1 211 . 1 1 34 34 LYS HB2 H 1 1.86 . . 2 . . . . . . . . 42 1 212 . 1 1 34 34 LYS HB3 H 1 1.98 . . 2 . . . . . . . . 42 1 213 . 1 1 34 34 LYS HG2 H 1 1.34 . . 2 . . . . . . . . 42 1 214 . 1 1 34 34 LYS HG3 H 1 1.46 . . 2 . . . . . . . . 42 1 215 . 1 1 34 34 LYS HD2 H 1 1.78 . . 1 . . . . . . . . 42 1 216 . 1 1 34 34 LYS HD3 H 1 1.78 . . 1 . . . . . . . . 42 1 217 . 1 1 34 34 LYS HE2 H 1 3.04 . . 2 . . . . . . . . 42 1 218 . 1 1 34 34 LYS HE3 H 1 3.1 . . 2 . . . . . . . . 42 1 219 . 1 1 35 35 CYS H H 1 8.3 . . 1 . . . . . . . . 42 1 220 . 1 1 35 35 CYS HA H 1 4.53 . . 1 . . . . . . . . 42 1 221 . 1 1 35 35 CYS HB2 H 1 3.25 . . 2 . . . . . . . . 42 1 222 . 1 1 35 35 CYS HB3 H 1 3.47 . . 2 . . . . . . . . 42 1 223 . 1 1 36 36 ASN H H 1 8.39 . . 1 . . . . . . . . 42 1 224 . 1 1 36 36 ASN HA H 1 4.58 . . 1 . . . . . . . . 42 1 225 . 1 1 36 36 ASN HB2 H 1 2.84 . . 2 . . . . . . . . 42 1 226 . 1 1 36 36 ASN HB3 H 1 3.22 . . 2 . . . . . . . . 42 1 227 . 1 1 36 36 ASN HD21 H 1 7.11 . . 2 . . . . . . . . 42 1 228 . 1 1 36 36 ASN HD22 H 1 7.61 . . 2 . . . . . . . . 42 1 229 . 1 1 37 37 PHE H H 1 8.39 . . 1 . . . . . . . . 42 1 230 . 1 1 37 37 PHE HA H 1 3.51 . . 1 . . . . . . . . 42 1 231 . 1 1 37 37 PHE HB2 H 1 2.78 . . 2 . . . . . . . . 42 1 232 . 1 1 37 37 PHE HB3 H 1 2.848 . . 2 . . . . . . . . 42 1 233 . 1 1 37 37 PHE HD1 H 1 6.55 . . 1 . . . . . . . . 42 1 234 . 1 1 37 37 PHE HD2 H 1 6.55 . . 1 . . . . . . . . 42 1 235 . 1 1 37 37 PHE HE1 H 1 6.82 . . 1 . . . . . . . . 42 1 236 . 1 1 37 37 PHE HE2 H 1 6.82 . . 1 . . . . . . . . 42 1 237 . 1 1 37 37 PHE HZ H 1 6.55 . . 1 . . . . . . . . 42 1 238 . 1 1 38 38 CYS H H 1 9.19 . . 1 . . . . . . . . 42 1 239 . 1 1 38 38 CYS HA H 1 3.97 . . 1 . . . . . . . . 42 1 240 . 1 1 38 38 CYS HB2 H 1 1.38 . . 2 . . . . . . . . 42 1 241 . 1 1 38 38 CYS HB3 H 1 1.77 . . 2 . . . . . . . . 42 1 242 . 1 1 39 39 ASN H H 1 8.17 . . 1 . . . . . . . . 42 1 243 . 1 1 39 39 ASN HA H 1 4.69 . . 1 . . . . . . . . 42 1 244 . 1 1 39 39 ASN HB2 H 1 2.78 . . 2 . . . . . . . . 42 1 245 . 1 1 39 39 ASN HB3 H 1 2.98 . . 2 . . . . . . . . 42 1 246 . 1 1 39 39 ASN HD21 H 1 6.81 . . 2 . . . . . . . . 42 1 247 . 1 1 39 39 ASN HD22 H 1 7.52 . . 2 . . . . . . . . 42 1 248 . 1 1 40 40 ALA H H 1 7.22 . . 1 . . . . . . . . 42 1 249 . 1 1 40 40 ALA HA H 1 4.17 . . 1 . . . . . . . . 42 1 250 . 1 1 40 40 ALA HB1 H 1 1.3 . . 1 . . . . . . . . 42 1 251 . 1 1 40 40 ALA HB2 H 1 1.3 . . 1 . . . . . . . . 42 1 252 . 1 1 40 40 ALA HB3 H 1 1.3 . . 1 . . . . . . . . 42 1 253 . 1 1 41 41 VAL H H 1 8.6 . . 1 . . . . . . . . 42 1 254 . 1 1 41 41 VAL HA H 1 3.18 . . 1 . . . . . . . . 42 1 255 . 1 1 41 41 VAL HB H 1 2.06 . . 1 . . . . . . . . 42 1 256 . 1 1 41 41 VAL HG11 H 1 .02 . . 2 . . . . . . . . 42 1 257 . 1 1 41 41 VAL HG12 H 1 .02 . . 2 . . . . . . . . 42 1 258 . 1 1 41 41 VAL HG13 H 1 .02 . . 2 . . . . . . . . 42 1 259 . 1 1 41 41 VAL HG21 H 1 .72 . . 2 . . . . . . . . 42 1 260 . 1 1 41 41 VAL HG22 H 1 .72 . . 2 . . . . . . . . 42 1 261 . 1 1 41 41 VAL HG23 H 1 .72 . . 2 . . . . . . . . 42 1 262 . 1 1 42 42 VAL H H 1 8.06 . . 1 . . . . . . . . 42 1 263 . 1 1 42 42 VAL HA H 1 3.93 . . 1 . . . . . . . . 42 1 264 . 1 1 42 42 VAL HB H 1 2.31 . . 1 . . . . . . . . 42 1 265 . 1 1 42 42 VAL HG11 H 1 1 . . 2 . . . . . . . . 42 1 266 . 1 1 42 42 VAL HG12 H 1 1 . . 2 . . . . . . . . 42 1 267 . 1 1 42 42 VAL HG13 H 1 1 . . 2 . . . . . . . . 42 1 268 . 1 1 42 42 VAL HG21 H 1 1.05 . . 2 . . . . . . . . 42 1 269 . 1 1 42 42 VAL HG22 H 1 1.05 . . 2 . . . . . . . . 42 1 270 . 1 1 42 42 VAL HG23 H 1 1.05 . . 2 . . . . . . . . 42 1 271 . 1 1 43 43 GLU H H 1 7.63 . . 1 . . . . . . . . 42 1 272 . 1 1 43 43 GLU HA H 1 4.32 . . 1 . . . . . . . . 42 1 273 . 1 1 43 43 GLU HB2 H 1 2.1 . . 2 . . . . . . . . 42 1 274 . 1 1 43 43 GLU HB3 H 1 2.25 . . 2 . . . . . . . . 42 1 275 . 1 1 43 43 GLU HG2 H 1 2.58 . . 1 . . . . . . . . 42 1 276 . 1 1 43 43 GLU HG3 H 1 2.58 . . 1 . . . . . . . . 42 1 277 . 1 1 44 44 SER H H 1 7.8 . . 1 . . . . . . . . 42 1 278 . 1 1 44 44 SER HA H 1 4.52 . . 1 . . . . . . . . 42 1 279 . 1 1 44 44 SER HB2 H 1 3.98 . . 2 . . . . . . . . 42 1 280 . 1 1 44 44 SER HB3 H 1 4.22 . . 2 . . . . . . . . 42 1 281 . 1 1 45 45 ASN H H 1 8.5 . . 1 . . . . . . . . 42 1 282 . 1 1 45 45 ASN HA H 1 4.48 . . 1 . . . . . . . . 42 1 283 . 1 1 45 45 ASN HB2 H 1 2.85 . . 2 . . . . . . . . 42 1 284 . 1 1 45 45 ASN HB3 H 1 3.15 . . 2 . . . . . . . . 42 1 285 . 1 1 45 45 ASN HD21 H 1 6.85 . . 2 . . . . . . . . 42 1 286 . 1 1 45 45 ASN HD22 H 1 7.58 . . 2 . . . . . . . . 42 1 287 . 1 1 46 46 GLY H H 1 8.12 . . 1 . . . . . . . . 42 1 288 . 1 1 46 46 GLY HA2 H 1 3.58 . . 2 . . . . . . . . 42 1 289 . 1 1 46 46 GLY HA3 H 1 4.1 . . 2 . . . . . . . . 42 1 290 . 1 1 47 47 THR H H 1 7.58 . . 1 . . . . . . . . 42 1 291 . 1 1 47 47 THR HA H 1 4.22 . . 1 . . . . . . . . 42 1 292 . 1 1 47 47 THR HB H 1 4.26 . . 1 . . . . . . . . 42 1 293 . 1 1 47 47 THR HG21 H 1 1.26 . . 1 . . . . . . . . 42 1 294 . 1 1 47 47 THR HG22 H 1 1.26 . . 1 . . . . . . . . 42 1 295 . 1 1 47 47 THR HG23 H 1 1.26 . . 1 . . . . . . . . 42 1 296 . 1 1 48 48 LEU H H 1 7.65 . . 1 . . . . . . . . 42 1 297 . 1 1 48 48 LEU HA H 1 4.28 . . 1 . . . . . . . . 42 1 298 . 1 1 48 48 LEU HB2 H 1 1.51 . . 1 . . . . . . . . 42 1 299 . 1 1 48 48 LEU HB3 H 1 1.51 . . 1 . . . . . . . . 42 1 300 . 1 1 48 48 LEU HG H 1 1.12 . . 1 . . . . . . . . 42 1 301 . 1 1 48 48 LEU HD11 H 1 .3 . . 2 . . . . . . . . 42 1 302 . 1 1 48 48 LEU HD12 H 1 .3 . . 2 . . . . . . . . 42 1 303 . 1 1 48 48 LEU HD13 H 1 .3 . . 2 . . . . . . . . 42 1 304 . 1 1 48 48 LEU HD21 H 1 1.17 . . 2 . . . . . . . . 42 1 305 . 1 1 48 48 LEU HD22 H 1 1.17 . . 2 . . . . . . . . 42 1 306 . 1 1 48 48 LEU HD23 H 1 1.17 . . 2 . . . . . . . . 42 1 307 . 1 1 49 49 THR H H 1 8.56 . . 1 . . . . . . . . 42 1 308 . 1 1 49 49 THR HA H 1 4.68 . . 1 . . . . . . . . 42 1 309 . 1 1 49 49 THR HB H 1 4.36 . . 1 . . . . . . . . 42 1 310 . 1 1 49 49 THR HG21 H 1 1.13 . . 1 . . . . . . . . 42 1 311 . 1 1 49 49 THR HG22 H 1 1.13 . . 1 . . . . . . . . 42 1 312 . 1 1 49 49 THR HG23 H 1 1.13 . . 1 . . . . . . . . 42 1 313 . 1 1 50 50 LEU H H 1 8.77 . . 1 . . . . . . . . 42 1 314 . 1 1 50 50 LEU HA H 1 4.1 . . 1 . . . . . . . . 42 1 315 . 1 1 50 50 LEU HB2 H 1 1 . . 2 . . . . . . . . 42 1 316 . 1 1 50 50 LEU HB3 H 1 1.78 . . 2 . . . . . . . . 42 1 317 . 1 1 50 50 LEU HG H 1 .65 . . 1 . . . . . . . . 42 1 318 . 1 1 50 50 LEU HD11 H 1 .12 . . 2 . . . . . . . . 42 1 319 . 1 1 50 50 LEU HD12 H 1 .12 . . 2 . . . . . . . . 42 1 320 . 1 1 50 50 LEU HD13 H 1 .12 . . 2 . . . . . . . . 42 1 321 . 1 1 50 50 LEU HD21 H 1 .04 . . 2 . . . . . . . . 42 1 322 . 1 1 50 50 LEU HD22 H 1 .04 . . 2 . . . . . . . . 42 1 323 . 1 1 50 50 LEU HD23 H 1 .04 . . 2 . . . . . . . . 42 1 324 . 1 1 51 51 SER H H 1 8.85 . . 1 . . . . . . . . 42 1 325 . 1 1 51 51 SER HA H 1 4.53 . . 1 . . . . . . . . 42 1 326 . 1 1 51 51 SER HB2 H 1 3.38 . . 2 . . . . . . . . 42 1 327 . 1 1 51 51 SER HB3 H 1 3.53 . . 2 . . . . . . . . 42 1 328 . 1 1 52 52 HIS H H 1 7.27 . . 1 . . . . . . . . 42 1 329 . 1 1 52 52 HIS HA H 1 4.52 . . 1 . . . . . . . . 42 1 330 . 1 1 52 52 HIS HB2 H 1 3.32 . . 2 . . . . . . . . 42 1 331 . 1 1 52 52 HIS HB3 H 1 3.79 . . 2 . . . . . . . . 42 1 332 . 1 1 52 52 HIS HD2 H 1 7.26 . . 1 . . . . . . . . 42 1 333 . 1 1 52 52 HIS HE1 H 1 8.8 . . 1 . . . . . . . . 42 1 334 . 1 1 53 53 PHE H H 1 9.17 . . 1 . . . . . . . . 42 1 335 . 1 1 53 53 PHE HA H 1 4.32 . . 1 . . . . . . . . 42 1 336 . 1 1 53 53 PHE HB2 H 1 3.04 . . 2 . . . . . . . . 42 1 337 . 1 1 53 53 PHE HB3 H 1 3.24 . . 2 . . . . . . . . 42 1 338 . 1 1 53 53 PHE HD1 H 1 7.28 . . 1 . . . . . . . . 42 1 339 . 1 1 53 53 PHE HD2 H 1 7.28 . . 1 . . . . . . . . 42 1 340 . 1 1 53 53 PHE HE1 H 1 7.17 . . 1 . . . . . . . . 42 1 341 . 1 1 53 53 PHE HE2 H 1 7.17 . . 1 . . . . . . . . 42 1 342 . 1 1 54 54 GLY H H 1 8.26 . . 1 . . . . . . . . 42 1 343 . 1 1 54 54 GLY HA2 H 1 3.57 . . 2 . . . . . . . . 42 1 344 . 1 1 54 54 GLY HA3 H 1 4.61 . . 2 . . . . . . . . 42 1 345 . 1 1 55 55 LYS H H 1 7.99 . . 1 . . . . . . . . 42 1 346 . 1 1 55 55 LYS HA H 1 4.05 . . 1 . . . . . . . . 42 1 347 . 1 1 55 55 LYS HB2 H 1 1.74 . . 2 . . . . . . . . 42 1 348 . 1 1 55 55 LYS HB3 H 1 1.88 . . 2 . . . . . . . . 42 1 349 . 1 1 55 55 LYS HG2 H 1 1.49 . . 2 . . . . . . . . 42 1 350 . 1 1 55 55 LYS HG3 H 1 1.55 . . 2 . . . . . . . . 42 1 351 . 1 1 55 55 LYS HD2 H 1 1.75 . . 1 . . . . . . . . 42 1 352 . 1 1 55 55 LYS HD3 H 1 1.75 . . 1 . . . . . . . . 42 1 353 . 1 1 55 55 LYS HE2 H 1 3.09 . . 1 . . . . . . . . 42 1 354 . 1 1 55 55 LYS HE3 H 1 3.09 . . 1 . . . . . . . . 42 1 355 . 1 1 55 55 LYS HZ1 H 1 7.54 . . 1 . . . . . . . . 42 1 356 . 1 1 55 55 LYS HZ2 H 1 7.54 . . 1 . . . . . . . . 42 1 357 . 1 1 55 55 LYS HZ3 H 1 7.54 . . 1 . . . . . . . . 42 1 358 . 1 1 56 56 CYS H H 1 8.31 . . 1 . . . . . . . . 42 1 359 . 1 1 56 56 CYS HA H 1 4.39 . . 1 . . . . . . . . 42 1 360 . 1 1 56 56 CYS HB2 H 1 2.52 . . 2 . . . . . . . . 42 1 361 . 1 1 56 56 CYS HB3 H 1 3.15 . . 2 . . . . . . . . 42 1 stop_ save_