data_2542 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 2542 _Entry.Title ; 1H and 15N NMR Study of Human Lysozyme ; _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 Tadayasu Ohkubo . . . 2542 2 Yoshio Taniyama . . . 2542 3 Masakazu Kikuchi . . . 2542 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 2542 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 148 2542 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 . . 2010-06-17 . revision BMRB 'Complete natural source information' 2542 4 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 2542 3 . . 1996-04-13 . revision BMRB 'Link to the Protein Data Bank added' 2542 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 2542 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 2542 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 2542 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Ohkubo, Tadayasu, Taniyama, Yoshio, Kikuchi, Masakazu, "1H and 15N NMR Study of Human Lysozyme," J. Biochem. 110 (6), 1022-1029 (1991). ; _Citation.Title '1H and 15N NMR Study of Human Lysozyme' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biochem.' _Citation.Journal_name_full . _Citation.Journal_volume 110 _Citation.Journal_issue 6 _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 1022 _Citation.Page_last 1029 _Citation.Year 1991 _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 Tadayasu Ohkubo . . . 2542 1 2 Yoshio Taniyama . . . 2542 1 3 Masakazu Kikuchi . . . 2542 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_lysozyme _Assembly.Sf_category assembly _Assembly.Sf_framecode system_lysozyme _Assembly.Entry_ID 2542 _Assembly.ID 1 _Assembly.Name lysozyme _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 lysozyme 1 $lysozyme . . . . . . . . . 2542 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID lysozyme system 2542 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_lysozyme _Entity.Sf_category entity _Entity.Sf_framecode lysozyme _Entity.Entry_ID 2542 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name lysozyme _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 ; KVFERCELARTLKRLGMDGY RGISLANWMCLAKWESGYNT RATNYNAGDRSTDYGIFQIN SRYWCNDGKTPGAVNACHLS CSALLQDNIADAVACAKRVV RDPQGIRAWVAWRNRCQNRD VRQYVQGCGV ; _Entity.Polymer_seq_one_letter_code ; KVFERCELARTLKRLGMDGY RGISLANWMCLAKWESGYNT RATNYNAGDRSTDYGIFQIN SRYWCNDGKTPGAVNACHLS CSALLQDNIADAVACAKRVV RDPQGIRAWVAWRNRCQNRD VRQYVQGCGV ; _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 130 _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 3.2.1.17 _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 2015-11-25 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 PDB 133L . "Role Of Arg 115 In The Catalytic Action Of Human Lysozyme. X-Ray Structure Of His 115 And Glu 115 Mutants" . . . . . 100.00 130 99.23 99.23 1.15e-88 . . . . 2542 1 2 no PDB 134L . "Role Of Arg 115 In The Catalytic Action Of Human Lysozyme. X-Ray Structure Of His 115 And Glu 115 Mutants" . . . . . 100.00 130 99.23 99.23 1.20e-88 . . . . 2542 1 3 no PDB 1B5U . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->al" . . . . . 100.00 130 99.23 100.00 8.29e-89 . . . . 2542 1 4 no PDB 1B5V . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->al" . . . . . 100.00 130 99.23 100.00 8.29e-89 . . . . 2542 1 5 no PDB 1B5W . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->al" . . . . . 100.00 130 99.23 100.00 8.29e-89 . . . . 2542 1 6 no PDB 1B5X . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->al" . . . . . 100.00 130 99.23 100.00 8.29e-89 . . . . 2542 1 7 no PDB 1B5Y . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->al" . . . . . 100.00 130 99.23 100.00 8.29e-89 . . . . 2542 1 8 no PDB 1B5Z . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->al" . . . . . 100.00 130 99.23 100.00 8.29e-89 . . . . 2542 1 9 no PDB 1B7L . "Verification Of Spmp Using Mutant Human Lysozymes" . . . . . 100.00 130 99.23 99.23 1.63e-88 . . . . 2542 1 10 no PDB 1B7M . "Verification Of Spmp Using Mutant Human Lysozymes" . . . . . 100.00 130 99.23 99.23 1.39e-88 . . . . 2542 1 11 no PDB 1B7N . "Verification Of Spmp Using Mutant Human Lysozymes" . . . . . 100.00 130 99.23 99.23 4.27e-88 . . . . 2542 1 12 no PDB 1B7O . "Verification Of Spmp Using Mutant Human Lysozymes" . . . . . 100.00 130 99.23 99.23 2.76e-88 . . . . 2542 1 13 no PDB 1B7P . "Verification Of Spmp Using Mutant Human Lysozymes" . . . . . 100.00 130 99.23 99.23 1.02e-87 . . . . 2542 1 14 no PDB 1B7Q . "Verification Of Spmp Using Mutant Human Lysozymes" . . . . . 100.00 130 99.23 99.23 4.66e-88 . . . . 2542 1 15 no PDB 1B7R . "Verification Of Spmp Using Mutant Human Lysozymes" . . . . . 100.00 130 99.23 99.23 4.04e-88 . . . . 2542 1 16 no PDB 1B7S . "Verification Of Spmp Using Mutant Human Lysozymes" . . . . . 100.00 130 99.23 99.23 1.60e-88 . . . . 2542 1 17 no PDB 1BB3 . "Human Lysozyme Mutant A96l" . . . . . 100.00 130 99.23 99.23 1.63e-88 . . . . 2542 1 18 no PDB 1BB4 . "Human Lysozyme Double Mutant A96l, W109h" . . . . . 100.00 130 98.46 98.46 2.22e-87 . . . . 2542 1 19 no PDB 1BB5 . "Human Lysozyme Mutant A96l Complexed With Chitotriose" . . . . . 100.00 130 99.23 99.23 1.63e-88 . . . . 2542 1 20 no PDB 1C43 . "Mutant Human Lysozyme With Foreign N-Terminal Residues" . . . . . 99.23 130 100.00 100.00 1.43e-88 . . . . 2542 1 21 no PDB 1C45 . "Mutant Human Lysozyme With Foreign N-Terminal Residues" . . . . . 99.23 130 100.00 100.00 1.50e-88 . . . . 2542 1 22 no PDB 1C46 . "Mutant Human Lysozyme With Foreign N-Terminal Residues" . . . . . 100.00 131 100.00 100.00 2.84e-89 . . . . 2542 1 23 no PDB 1C7P . "Crystal Structure Of Mutant Human Lysozyme With Four Extra Residues (Eaea) At The N-Terminal" . . . . . 100.00 134 100.00 100.00 1.72e-89 . . . . 2542 1 24 no PDB 1CJ6 . "T11a Mutant Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.55e-88 . . . . 2542 1 25 no PDB 1CJ7 . "T11v Mutant Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.40e-88 . . . . 2542 1 26 no PDB 1CJ8 . "T40a Mutant Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.55e-88 . . . . 2542 1 27 no PDB 1CJ9 . "T40v Mutant Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.40e-88 . . . . 2542 1 28 no PDB 1CKC . "T43a Mutant Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.55e-88 . . . . 2542 1 29 no PDB 1CKD . "T43v Mutant Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.40e-88 . . . . 2542 1 30 no PDB 1CKF . "T52a Mutant Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.55e-88 . . . . 2542 1 31 no PDB 1CKG . "T52v Mutant Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.40e-88 . . . . 2542 1 32 no PDB 1CKH . "T70v Mutant Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.40e-88 . . . . 2542 1 33 no PDB 1D6P . "Human Lysozyme L63 Mutant Labelled With 2',3'-Epoxypropyl N,N'- Diacetylchitobiose" . . . . . 100.00 130 99.23 99.23 3.18e-88 . . . . 2542 1 34 no PDB 1D6Q . "Human Lysozyme E102 Mutant Labelled With 2',3'-Epoxypropyl Glycoside Of N-Acetyllactosamine" . . . . . 100.00 130 99.23 100.00 8.86e-89 . . . . 2542 1 35 no PDB 1DI3 . "Role Of Amino Acid Residues At Turns In The Conformational Stability And Folding Of Human Lysozyme" . . . . . 100.00 130 99.23 99.23 3.47e-88 . . . . 2542 1 36 no PDB 1DI4 . "Role Of Amino Acid Residues At Turns In The Conformational Stability And Folding Of Human Lysozyme" . . . . . 100.00 128 98.46 98.46 6.07e-86 . . . . 2542 1 37 no PDB 1DI5 . "Role Of Amino Acid Residues At Turns In The Conformational Stability And Folding Of Human Lysozyme" . . . . . 100.00 129 99.23 99.23 8.06e-87 . . . . 2542 1 38 no PDB 1EQ4 . "Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme" . . . . . 100.00 130 99.23 100.00 9.35e-89 . . . . 2542 1 39 no PDB 1EQ5 . "Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme" . . . . . 100.00 130 99.23 100.00 1.33e-88 . . . . 2542 1 40 no PDB 1EQE . "Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme" . . . . . 100.00 130 99.23 100.00 1.33e-88 . . . . 2542 1 41 no PDB 1GAY . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 3.47e-88 . . . . 2542 1 42 no PDB 1GAZ . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 100.00 4.03e-89 . . . . 2542 1 43 no PDB 1GB0 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 100.00 7.44e-89 . . . . 2542 1 44 no PDB 1GB2 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 100.00 6.81e-89 . . . . 2542 1 45 no PDB 1GB3 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 1.22e-88 . . . . 2542 1 46 no PDB 1GB5 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 3.47e-88 . . . . 2542 1 47 no PDB 1GB6 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 100.00 4.03e-89 . . . . 2542 1 48 no PDB 1GB7 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 100.00 7.44e-89 . . . . 2542 1 49 no PDB 1GB8 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 100.00 6.81e-89 . . . . 2542 1 50 no PDB 1GB9 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 1.22e-88 . . . . 2542 1 51 no PDB 1GBO . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 3.47e-88 . . . . 2542 1 52 no PDB 1GBW . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 100.00 4.03e-89 . . . . 2542 1 53 no PDB 1GBX . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 100.00 7.44e-89 . . . . 2542 1 54 no PDB 1GBY . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 100.00 6.81e-89 . . . . 2542 1 55 no PDB 1GBZ . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 1.22e-88 . . . . 2542 1 56 no PDB 1GDW . "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" . . . . . 100.00 130 99.23 99.23 3.47e-88 . . . . 2542 1 57 no PDB 1GDX . "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" . . . . . 100.00 130 99.23 99.23 2.19e-88 . . . . 2542 1 58 no PDB 1GE0 . "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" . . . . . 100.00 130 99.23 99.23 6.61e-88 . . . . 2542 1 59 no PDB 1GE1 . "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" . . . . . 100.00 130 99.23 99.23 2.08e-88 . . . . 2542 1 60 no PDB 1GE2 . "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" . . . . . 100.00 130 99.23 99.23 6.75e-88 . . . . 2542 1 61 no PDB 1GE3 . "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" . . . . . 100.00 130 99.23 99.23 2.27e-88 . . . . 2542 1 62 no PDB 1GE4 . "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" . . . . . 100.00 130 99.23 99.23 2.85e-88 . . . . 2542 1 63 no PDB 1GEV . "Buried Polar Mutant Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.45e-88 . . . . 2542 1 64 no PDB 1GEZ . "Buried Polar Mutant Human Lysozyme" . . . . . 100.00 130 99.23 100.00 5.72e-89 . . . . 2542 1 65 no PDB 1GF0 . "Buried Polar Mutant Human Lysozyme" . . . . . 100.00 130 99.23 100.00 5.72e-89 . . . . 2542 1 66 no PDB 1GF3 . "Buried Polar Mutant Human Lysozyme" . . . . . 100.00 130 99.23 100.00 5.72e-89 . . . . 2542 1 67 no PDB 1GF4 . "Buried Polar Mutant Human Lysozyme" . . . . . 100.00 130 99.23 99.23 9.77e-89 . . . . 2542 1 68 no PDB 1GF5 . "Buried Polar Mutant Human Lysozyme" . . . . . 100.00 130 99.23 100.00 5.72e-89 . . . . 2542 1 69 no PDB 1GF6 . "Buried Polar Mutant Human Lysozyme" . . . . . 100.00 130 99.23 99.23 9.77e-89 . . . . 2542 1 70 no PDB 1GF7 . "Buried Polar Mutant Human Lysozyme" . . . . . 100.00 130 99.23 99.23 9.77e-89 . . . . 2542 1 71 no PDB 1GF8 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 1.60e-88 . . . . 2542 1 72 no PDB 1GF9 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 1.94e-88 . . . . 2542 1 73 no PDB 1GFA . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 3.58e-88 . . . . 2542 1 74 no PDB 1GFE . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 3.28e-88 . . . . 2542 1 75 no PDB 1GFG . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 3.51e-88 . . . . 2542 1 76 no PDB 1GFH . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 1.94e-88 . . . . 2542 1 77 no PDB 1GFJ . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 3.58e-88 . . . . 2542 1 78 no PDB 1GFK . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 3.28e-88 . . . . 2542 1 79 no PDB 1GFR . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 3.51e-88 . . . . 2542 1 80 no PDB 1GFT . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 1.94e-88 . . . . 2542 1 81 no PDB 1GFU . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 3.58e-88 . . . . 2542 1 82 no PDB 1GFV . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 3.28e-88 . . . . 2542 1 83 no PDB 1HNL . "Crystal Structure Of A Glutathionylated Human Lysozyme: A Folding Intermediate Mimic In The Formation Of A Disulfide Bond" . . . . . 100.00 130 99.23 99.23 2.50e-88 . . . . 2542 1 84 no PDB 1I1Z . "Mutant Human Lysozyme (Q86d)" . . . . . 100.00 130 99.23 99.23 2.50e-88 . . . . 2542 1 85 no PDB 1I20 . "Mutant Human Lysozyme (A92d)" . . . . . 100.00 130 99.23 99.23 2.61e-88 . . . . 2542 1 86 no PDB 1I22 . "Mutant Human Lysozyme (A83kQ86DA92D)" . . . . . 100.00 130 97.69 97.69 7.38e-87 . . . . 2542 1 87 no PDB 1INU . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 99.23 99.23 3.51e-88 . . . . 2542 1 88 no PDB 1IOC . "Crystal Structure Of Mutant Human Lysozyme, Eaea-I56t" . . . . . 100.00 134 99.23 99.23 7.12e-89 . . . . 2542 1 89 no PDB 1IP1 . "G37a Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.37e-88 . . . . 2542 1 90 no PDB 1IP2 . "G48a Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.37e-88 . . . . 2542 1 91 no PDB 1IP3 . "G68a Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.37e-88 . . . . 2542 1 92 no PDB 1IP4 . "G72a Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.37e-88 . . . . 2542 1 93 no PDB 1IP5 . "G105a Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.37e-88 . . . . 2542 1 94 no PDB 1IP6 . "G127a Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.37e-88 . . . . 2542 1 95 no PDB 1IP7 . "G129a Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.37e-88 . . . . 2542 1 96 no PDB 1IWT . "Crystal Structure Analysis Of Human Lysozyme At 113k." . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 97 no PDB 1IWU . "Crystal Structure Analysis Of Human Lysozyme At 127k." . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 98 no PDB 1IWV . "Crystal Structure Analysis Of Human Lysozyme At 147k." . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 99 no PDB 1IWW . "Crystal Structure Analysis Of Human Lysozyme At 152k." . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 100 no PDB 1IWX . "Crystal Structure Analysis Of Human Lysozyme At 161k." . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 101 no PDB 1IWY . "Crystal Structure Analysis Of Human Lysozyme At 170k." . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 102 no PDB 1IWZ . "Crystal Structure Analysis Of Human Lysozyme At 178k." . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 103 no PDB 1IX0 . "I59a-3ss Human Lysozyme" . . . . . 100.00 130 97.69 97.69 1.17e-86 . . . . 2542 1 104 no PDB 1IY3 . "Solution Structure Of The Human Lysozyme At 4 Degree C" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 105 no PDB 1IY4 . "Solution Structure Of The Human Lysozyme At 35 Degree C" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 106 no PDB 1JKA . "Human Lysozyme Mutant With Glu 35 Replaced By Asp" . . . . . 100.00 130 99.23 100.00 1.31e-88 . . . . 2542 1 107 no PDB 1JKB . "Human Lysozyme Mutant With Glu 35 Replaced By Ala" . . . . . 100.00 130 99.23 99.23 2.15e-88 . . . . 2542 1 108 no PDB 1JKC . "Human Lysozyme Mutant With Trp 109 Replaced By Phe" . . . . . 100.00 130 99.23 100.00 1.31e-88 . . . . 2542 1 109 no PDB 1JKD . "Human Lysozyme Mutant With Trp 109 Replaced By Ala" . . . . . 100.00 130 99.23 99.23 5.31e-88 . . . . 2542 1 110 no PDB 1JSF . "Full-Matrix Least-Squares Refinement Of Human Lysozyme" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 111 no PDB 1JWR . "Crystal Structure Of Human Lysozyme At 100 K" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 112 no PDB 1LAA . "X-Ray Structure Of Glu 53 Human Lysozyme" . . . . . 100.00 130 99.23 100.00 8.86e-89 . . . . 2542 1 113 no PDB 1LHH . "Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of P" . . . . . 100.00 130 99.23 99.23 1.84e-88 . . . . 2542 1 114 no PDB 1LHI . "Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of P" . . . . . 100.00 130 99.23 99.23 8.49e-88 . . . . 2542 1 115 no PDB 1LHJ . "Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of P" . . . . . 100.00 130 99.23 99.23 8.49e-88 . . . . 2542 1 116 no PDB 1LHK . "Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of P" . . . . . 100.00 130 99.23 99.23 2.45e-88 . . . . 2542 1 117 no PDB 1LHL . "Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of P" . . . . . 100.00 130 99.23 99.23 1.26e-88 . . . . 2542 1 118 no PDB 1LHM . "The Crystal Structure Of A Mutant Lysozyme C77(Slash)95a With Increased Secretion Efficiency In Yeast" . . . . . 100.00 130 98.46 98.46 1.73e-87 . . . . 2542 1 119 no PDB 1LOZ . "Amyloidogenic Variant (i56t) Variant Of Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.30e-88 . . . . 2542 1 120 no PDB 1LYY . "Amyloidogenic Variant (Asp67his) Of Human Lysozyme" . . . . . 100.00 130 99.23 99.23 2.19e-88 . . . . 2542 1 121 no PDB 1LZ1 . "Refinement Of Human Lysozyme At 1.5 Angstroms Resolution. Analysis Of Non-Bonded And Hydrogen-Bond Interactions" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 122 no PDB 1LZ4 . "Enthalpic Destabilization Of A Mutant Human Lysozyme Lacking A Disulfide Bridge Between Cysteine-77 And Cysteine-95" . . . . . 100.00 130 99.23 99.23 2.50e-88 . . . . 2542 1 123 no PDB 1LZ5 . "Structural And Functional Analyses Of The Arg-Gly-Asp Sequence Introduced Into Human Lysozyme" . . . . . 103.08 134 97.01 97.01 7.30e-87 . . . . 2542 1 124 no PDB 1LZR . "Structural Changes Of The Active Site Cleft And Different Saccharide Binding Modes In Human Lysozyme Co-Crystallized With Hexa-" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 125 no PDB 1LZS . "Structural Changes Of The Active Site Cleft And Different Saccharide Binding Modes In Human Lysozyme Co-Crystallized With Hexa-" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 126 no PDB 1OP9 . "Complex Of Human Lysozyme With Camelid Vhh Hl6 Antibody Fragment" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 127 no PDB 1OUA . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The I56t Mutant" . . . . . 100.00 130 99.23 99.23 1.30e-88 . . . . 2542 1 128 no PDB 1OUB . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-ray Structure Of The V100a Mutant" . . . . . 100.00 130 99.23 99.23 1.18e-88 . . . . 2542 1 129 no PDB 1OUC . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V110a Mutant" . . . . . 100.00 130 99.23 99.23 1.18e-88 . . . . 2542 1 130 no PDB 1OUD . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V121a Mutant" . . . . . 100.00 130 99.23 99.23 1.18e-88 . . . . 2542 1 131 no PDB 1OUE . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V125a Mutant" . . . . . 100.00 130 99.23 99.23 1.18e-88 . . . . 2542 1 132 no PDB 1OUF . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V130a Mutant" . . . . . 99.23 130 100.00 100.00 1.18e-88 . . . . 2542 1 133 no PDB 1OUG . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V2a Mutant" . . . . . 100.00 130 99.23 99.23 1.18e-88 . . . . 2542 1 134 no PDB 1OUH . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V74a Mutant" . . . . . 100.00 130 99.23 99.23 1.18e-88 . . . . 2542 1 135 no PDB 1OUI . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V93a Mutant" . . . . . 100.00 130 99.23 99.23 1.18e-88 . . . . 2542 1 136 no PDB 1OUJ . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V99a Mutant" . . . . . 100.00 130 99.23 99.23 1.18e-88 . . . . 2542 1 137 no PDB 1QSW . "Crystal Structure Analysis Of A Human Lysozyme Mutant W64c C65a" . . . . . 100.00 130 98.46 98.46 1.13e-86 . . . . 2542 1 138 no PDB 1RE2 . "Human Lysozyme Labelled With Two 2',3'-epoxypropyl Beta-glycoside Of N-acetyllactosamine" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 139 no PDB 1REM . "Human Lysozyme With Man-B1,4-Glcnac Covalently Attached To Asp53" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 140 no PDB 1REX . "Native Human Lysozyme" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 141 no PDB 1REY . "Human Lysozyme-N,N'-Diacetylchitobiose Complex" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 142 no PDB 1REZ . "Human Lysozyme-N-Acetyllactosamine Complex" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 143 no PDB 1TAY . "Dissection Of The Functional Role Of Structural Elements Of Tyrosine-63 In The Catalytic Action Of Human Lysozyme" . . . . . 100.00 130 99.23 99.23 3.83e-88 . . . . 2542 1 144 no PDB 1TBY . "Dissection Of The Functional Role Of Structural Elements Of Tyrosine-63 In The Catalytic Action Of Human Lysozyme" . . . . . 100.00 130 99.23 99.23 3.18e-88 . . . . 2542 1 145 no PDB 1TCY . "Dissection Of The Functional Role Of Structural Elements Of Tyrosine-63 In The Catalytic Action Of Human Lysozyme" . . . . . 100.00 130 99.23 100.00 7.36e-89 . . . . 2542 1 146 no PDB 1TDY . "Dissection Of The Functional Role Of Structural Elements Of Tyrosine-63 In The Catalytic Action Of Human Lysozyme" . . . . . 100.00 130 99.23 100.00 2.17e-88 . . . . 2542 1 147 no PDB 1UBZ . "Crystal Structure Of Glu102-Mutant Human Lysozyme Doubly Labeled With 2',3'-Epoxypropyl Beta-Glycoside Of N-Acetyllactosamine" . . . . . 100.00 130 99.23 100.00 8.86e-89 . . . . 2542 1 148 no PDB 1W08 . "Structure Of T70n Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.60e-88 . . . . 2542 1 149 no PDB 1WQM . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 99.23 100.00 7.36e-89 . . . . 2542 1 150 no PDB 1WQN . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 99.23 100.00 7.36e-89 . . . . 2542 1 151 no PDB 1WQO . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 99.23 100.00 7.36e-89 . . . . 2542 1 152 no PDB 1WQP . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 99.23 100.00 7.36e-89 . . . . 2542 1 153 no PDB 1WQQ . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 99.23 100.00 7.36e-89 . . . . 2542 1 154 no PDB 1WQR . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 99.23 100.00 7.36e-89 . . . . 2542 1 155 no PDB 1YAM . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of " . . . . . 100.00 130 99.23 100.00 4.65e-89 . . . . 2542 1 156 no PDB 1YAN . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of " . . . . . 100.00 130 99.23 100.00 4.65e-89 . . . . 2542 1 157 no PDB 1YAO . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of " . . . . . 100.00 130 99.23 100.00 4.65e-89 . . . . 2542 1 158 no PDB 1YAP . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of " . . . . . 100.00 130 99.23 100.00 4.65e-89 . . . . 2542 1 159 no PDB 1YAQ . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of " . . . . . 100.00 130 99.23 100.00 4.65e-89 . . . . 2542 1 160 no PDB 207L . "Mutant Human Lysozyme C77a" . . . . . 100.00 130 99.23 99.23 2.50e-88 . . . . 2542 1 161 no PDB 208L . "Mutant Human Lysozyme C77a" . . . . . 100.00 130 99.23 99.23 2.50e-88 . . . . 2542 1 162 no PDB 2BQA . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 98.46 98.46 1.73e-87 . . . . 2542 1 163 no PDB 2BQB . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 97.69 98.46 3.05e-87 . . . . 2542 1 164 no PDB 2BQC . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 97.69 98.46 3.05e-87 . . . . 2542 1 165 no PDB 2BQD . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 97.69 98.46 3.05e-87 . . . . 2542 1 166 no PDB 2BQE . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 97.69 98.46 3.05e-87 . . . . 2542 1 167 no PDB 2BQF . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 97.69 98.46 3.05e-87 . . . . 2542 1 168 no PDB 2BQG . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 97.69 97.69 7.54e-87 . . . . 2542 1 169 no PDB 2BQH . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 97.69 97.69 7.54e-87 . . . . 2542 1 170 no PDB 2BQI . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 97.69 97.69 7.54e-87 . . . . 2542 1 171 no PDB 2BQJ . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 97.69 97.69 7.54e-87 . . . . 2542 1 172 no PDB 2BQK . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 99.23 130 98.45 98.45 7.54e-87 . . . . 2542 1 173 no PDB 2BQL . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 97.69 97.69 7.54e-87 . . . . 2542 1 174 no PDB 2BQM . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 97.69 97.69 7.54e-87 . . . . 2542 1 175 no PDB 2BQN . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 97.69 97.69 7.54e-87 . . . . 2542 1 176 no PDB 2BQO . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 97.69 97.69 7.54e-87 . . . . 2542 1 177 no PDB 2HEA . "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" . . . . . 100.00 130 99.23 99.23 1.78e-88 . . . . 2542 1 178 no PDB 2HEB . "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" . . . . . 100.00 130 99.23 99.23 1.78e-88 . . . . 2542 1 179 no PDB 2HEC . "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" . . . . . 100.00 130 99.23 99.23 1.78e-88 . . . . 2542 1 180 no PDB 2HED . "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" . . . . . 100.00 130 99.23 99.23 1.78e-88 . . . . 2542 1 181 no PDB 2HEE . "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" . . . . . 100.00 130 99.23 99.23 4.46e-88 . . . . 2542 1 182 no PDB 2HEF . "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" . . . . . 100.00 130 99.23 99.23 1.78e-88 . . . . 2542 1 183 no PDB 2LHM . "Crystal Structures Of The Apo-And Holomutant Human Lysozymes With An Introduced Ca2+ Binding Site" . . . . . 100.00 130 98.46 98.46 2.06e-87 . . . . 2542 1 184 no PDB 2MEA . "Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions" . . . . . 100.00 130 99.23 99.23 1.15e-88 . . . . 2542 1 185 no PDB 2MEB . "Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions" . . . . . 100.00 130 99.23 100.00 6.04e-89 . . . . 2542 1 186 no PDB 2MEC . "Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions" . . . . . 100.00 130 99.23 100.00 7.04e-89 . . . . 2542 1 187 no PDB 2MED . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.15e-88 . . . . 2542 1 188 no PDB 2MEE . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 99.23 100.00 6.04e-89 . . . . 2542 1 189 no PDB 2MEF . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 99.23 100.00 7.04e-89 . . . . 2542 1 190 no PDB 2MEG . "Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions" . . . . . 100.00 130 99.23 99.23 2.19e-88 . . . . 2542 1 191 no PDB 2MEH . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 99.23 99.23 1.30e-88 . . . . 2542 1 192 no PDB 2MEI . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 99.23 99.23 2.37e-88 . . . . 2542 1 193 no PDB 2NWD . "Structure Of Chemically Synthesized Human Lysozyme At 1 Angstrom Resolution" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 194 no PDB 2ZIJ . "Crystal Structure Of Human Lysozyme Expressed In E. Coli." . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 195 no PDB 2ZIK . "Crystal Structure Of Human Lysozyme From Pichia Pastoris" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 196 no PDB 2ZIL . "Crystal Structure Of Human Lysozyme From Urine" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 197 no PDB 2ZWB . "Neutron Crystal Structure Of Wild Type Human Lysozyme In D2o" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 198 no PDB 3EBA . "Cabhul6 Fglw Mutant (Humanized) In Complex With Human Lysozyme" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 199 no PDB 3FE0 . "X-Ray Crystal Structure Of Wild Type Human Lysozyme In D2o" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 200 no PDB 3LHM . "Crystal Structures Of The Apo-And Holomutant Human Lysozymes With An Introduced Ca2+ Binding Site" . . . . . 100.00 130 98.46 98.46 2.06e-87 . . . . 2542 1 201 no PDB 3LN2 . "Crystal Structure Of A Charge Engineered Human Lysozyme Variant" . . . . . 100.00 130 98.46 98.46 1.10e-87 . . . . 2542 1 202 no PDB 4I0C . "The Structure Of The Camelid Antibody Cabhul5 In Complex With Human Lysozyme" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 203 no PDB 4ML7 . "Crystal Structure Of Brucella Abortus Plic In Complex With Human Lysozyme" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 204 no DBJ BAA00314 . "lysozyme [synthetic construct]" . . . . . 100.00 131 99.23 99.23 2.76e-88 . . . . 2542 1 205 no DBJ BAG34722 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 148 100.00 100.00 5.99e-90 . . . . 2542 1 206 no DBJ BAG73364 . "lysozyme [synthetic construct]" . . . . . 100.00 148 99.23 99.23 5.26e-89 . . . . 2542 1 207 no EMBL CAA32175 . "lysozyme [Homo sapiens]" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 208 no EMBL CAA53144 . "lysozyme [synthetic construct]" . . . . . 100.00 131 100.00 100.00 2.78e-89 . . . . 2542 1 209 no GB AAA36188 . "lysozyme precursor (EC 3.2.1.17) [Homo sapiens]" . . . . . 100.00 148 99.23 100.00 1.64e-89 . . . . 2542 1 210 no GB AAA59535 . "lysozyme precursor (EC 3.2.1.17) [Homo sapiens]" . . . . . 100.00 148 100.00 100.00 5.99e-90 . . . . 2542 1 211 no GB AAA59536 . "lysozyme precursor (EC 3.2.1.17) [Homo sapiens]" . . . . . 100.00 148 100.00 100.00 5.99e-90 . . . . 2542 1 212 no GB AAA72819 . "lysozyme, partial [synthetic construct]" . . . . . 100.00 130 100.00 100.00 2.94e-89 . . . . 2542 1 213 no GB AAB26052 . "lysozyme=amyloid fibril protein [human, Peptide Mutant, 130 aa]" . . . . . 100.00 130 99.23 99.23 1.30e-88 . . . . 2542 1 214 no REF NP_000230 . "lysozyme C precursor [Homo sapiens]" . . . . . 100.00 148 100.00 100.00 5.99e-90 . . . . 2542 1 215 no REF NP_001009073 . "lysozyme C precursor [Pan troglodytes]" . . . . . 100.00 148 100.00 100.00 5.99e-90 . . . . 2542 1 216 no REF NP_001266591 . "lysozyme precursor [Gorilla gorilla]" . . . . . 100.00 148 100.00 100.00 7.29e-90 . . . . 2542 1 217 no REF XP_002823550 . "PREDICTED: lysozyme C [Pongo abelii]" . . . . . 100.00 148 99.23 99.23 2.35e-89 . . . . 2542 1 218 no REF XP_003259554 . "PREDICTED: lysozyme C isoform X2 [Nomascus leucogenys]" . . . . . 100.00 148 96.92 99.23 5.15e-88 . . . . 2542 1 219 no SP P61626 . "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor" . . . . . 100.00 148 100.00 100.00 5.99e-90 . . . . 2542 1 220 no SP P61627 . "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor" . . . . . 100.00 148 100.00 100.00 5.99e-90 . . . . 2542 1 221 no SP P61628 . "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor" . . . . . 100.00 148 100.00 100.00 5.99e-90 . . . . 2542 1 222 no SP P79179 . "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor" . . . . . 100.00 148 100.00 100.00 7.29e-90 . . . . 2542 1 223 no SP P79180 . "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor" . . . . . 100.00 148 96.92 99.23 3.75e-88 . . . . 2542 1 224 no TPE CDM98740 . "TPA: lysozyme F1 [Homo sapiens]" . . . . . 100.00 148 100.00 100.00 5.99e-90 . . . . 2542 1 225 no TPE CDM98750 . "TPA: lysozyme F1 [Pongo abelii]" . . . . . 100.00 148 99.23 99.23 2.35e-89 . . . . 2542 1 226 no TPE CDM98754 . "TPA: lysozyme F1 [Nomascus leucogenys]" . . . . . 100.00 148 96.92 99.23 5.15e-88 . . . . 2542 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID lysozyme common 2542 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . LYS . 2542 1 2 . VAL . 2542 1 3 . PHE . 2542 1 4 . GLU . 2542 1 5 . ARG . 2542 1 6 . CYS . 2542 1 7 . GLU . 2542 1 8 . LEU . 2542 1 9 . ALA . 2542 1 10 . ARG . 2542 1 11 . THR . 2542 1 12 . LEU . 2542 1 13 . LYS . 2542 1 14 . ARG . 2542 1 15 . LEU . 2542 1 16 . GLY . 2542 1 17 . MET . 2542 1 18 . ASP . 2542 1 19 . GLY . 2542 1 20 . TYR . 2542 1 21 . ARG . 2542 1 22 . GLY . 2542 1 23 . ILE . 2542 1 24 . SER . 2542 1 25 . LEU . 2542 1 26 . ALA . 2542 1 27 . ASN . 2542 1 28 . TRP . 2542 1 29 . MET . 2542 1 30 . CYS . 2542 1 31 . LEU . 2542 1 32 . ALA . 2542 1 33 . LYS . 2542 1 34 . TRP . 2542 1 35 . GLU . 2542 1 36 . SER . 2542 1 37 . GLY . 2542 1 38 . TYR . 2542 1 39 . ASN . 2542 1 40 . THR . 2542 1 41 . ARG . 2542 1 42 . ALA . 2542 1 43 . THR . 2542 1 44 . ASN . 2542 1 45 . TYR . 2542 1 46 . ASN . 2542 1 47 . ALA . 2542 1 48 . GLY . 2542 1 49 . ASP . 2542 1 50 . ARG . 2542 1 51 . SER . 2542 1 52 . THR . 2542 1 53 . ASP . 2542 1 54 . TYR . 2542 1 55 . GLY . 2542 1 56 . ILE . 2542 1 57 . PHE . 2542 1 58 . GLN . 2542 1 59 . ILE . 2542 1 60 . ASN . 2542 1 61 . SER . 2542 1 62 . ARG . 2542 1 63 . TYR . 2542 1 64 . TRP . 2542 1 65 . CYS . 2542 1 66 . ASN . 2542 1 67 . ASP . 2542 1 68 . GLY . 2542 1 69 . LYS . 2542 1 70 . THR . 2542 1 71 . PRO . 2542 1 72 . GLY . 2542 1 73 . ALA . 2542 1 74 . VAL . 2542 1 75 . ASN . 2542 1 76 . ALA . 2542 1 77 . CYS . 2542 1 78 . HIS . 2542 1 79 . LEU . 2542 1 80 . SER . 2542 1 81 . CYS . 2542 1 82 . SER . 2542 1 83 . ALA . 2542 1 84 . LEU . 2542 1 85 . LEU . 2542 1 86 . GLN . 2542 1 87 . ASP . 2542 1 88 . ASN . 2542 1 89 . ILE . 2542 1 90 . ALA . 2542 1 91 . ASP . 2542 1 92 . ALA . 2542 1 93 . VAL . 2542 1 94 . ALA . 2542 1 95 . CYS . 2542 1 96 . ALA . 2542 1 97 . LYS . 2542 1 98 . ARG . 2542 1 99 . VAL . 2542 1 100 . VAL . 2542 1 101 . ARG . 2542 1 102 . ASP . 2542 1 103 . PRO . 2542 1 104 . GLN . 2542 1 105 . GLY . 2542 1 106 . ILE . 2542 1 107 . ARG . 2542 1 108 . ALA . 2542 1 109 . TRP . 2542 1 110 . VAL . 2542 1 111 . ALA . 2542 1 112 . TRP . 2542 1 113 . ARG . 2542 1 114 . ASN . 2542 1 115 . ARG . 2542 1 116 . CYS . 2542 1 117 . GLN . 2542 1 118 . ASN . 2542 1 119 . ARG . 2542 1 120 . ASP . 2542 1 121 . VAL . 2542 1 122 . ARG . 2542 1 123 . GLN . 2542 1 124 . TYR . 2542 1 125 . VAL . 2542 1 126 . GLN . 2542 1 127 . GLY . 2542 1 128 . CYS . 2542 1 129 . GLY . 2542 1 130 . VAL . 2542 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . LYS 1 1 2542 1 . VAL 2 2 2542 1 . PHE 3 3 2542 1 . GLU 4 4 2542 1 . ARG 5 5 2542 1 . CYS 6 6 2542 1 . GLU 7 7 2542 1 . LEU 8 8 2542 1 . ALA 9 9 2542 1 . ARG 10 10 2542 1 . THR 11 11 2542 1 . LEU 12 12 2542 1 . LYS 13 13 2542 1 . ARG 14 14 2542 1 . LEU 15 15 2542 1 . GLY 16 16 2542 1 . MET 17 17 2542 1 . ASP 18 18 2542 1 . GLY 19 19 2542 1 . TYR 20 20 2542 1 . ARG 21 21 2542 1 . GLY 22 22 2542 1 . ILE 23 23 2542 1 . SER 24 24 2542 1 . LEU 25 25 2542 1 . ALA 26 26 2542 1 . ASN 27 27 2542 1 . TRP 28 28 2542 1 . MET 29 29 2542 1 . CYS 30 30 2542 1 . LEU 31 31 2542 1 . ALA 32 32 2542 1 . LYS 33 33 2542 1 . TRP 34 34 2542 1 . GLU 35 35 2542 1 . SER 36 36 2542 1 . GLY 37 37 2542 1 . TYR 38 38 2542 1 . ASN 39 39 2542 1 . THR 40 40 2542 1 . ARG 41 41 2542 1 . ALA 42 42 2542 1 . THR 43 43 2542 1 . ASN 44 44 2542 1 . TYR 45 45 2542 1 . ASN 46 46 2542 1 . ALA 47 47 2542 1 . GLY 48 48 2542 1 . ASP 49 49 2542 1 . ARG 50 50 2542 1 . SER 51 51 2542 1 . THR 52 52 2542 1 . ASP 53 53 2542 1 . TYR 54 54 2542 1 . GLY 55 55 2542 1 . ILE 56 56 2542 1 . PHE 57 57 2542 1 . GLN 58 58 2542 1 . ILE 59 59 2542 1 . ASN 60 60 2542 1 . SER 61 61 2542 1 . ARG 62 62 2542 1 . TYR 63 63 2542 1 . TRP 64 64 2542 1 . CYS 65 65 2542 1 . ASN 66 66 2542 1 . ASP 67 67 2542 1 . GLY 68 68 2542 1 . LYS 69 69 2542 1 . THR 70 70 2542 1 . PRO 71 71 2542 1 . GLY 72 72 2542 1 . ALA 73 73 2542 1 . VAL 74 74 2542 1 . ASN 75 75 2542 1 . ALA 76 76 2542 1 . CYS 77 77 2542 1 . HIS 78 78 2542 1 . LEU 79 79 2542 1 . SER 80 80 2542 1 . CYS 81 81 2542 1 . SER 82 82 2542 1 . ALA 83 83 2542 1 . LEU 84 84 2542 1 . LEU 85 85 2542 1 . GLN 86 86 2542 1 . ASP 87 87 2542 1 . ASN 88 88 2542 1 . ILE 89 89 2542 1 . ALA 90 90 2542 1 . ASP 91 91 2542 1 . ALA 92 92 2542 1 . VAL 93 93 2542 1 . ALA 94 94 2542 1 . CYS 95 95 2542 1 . ALA 96 96 2542 1 . LYS 97 97 2542 1 . ARG 98 98 2542 1 . VAL 99 99 2542 1 . VAL 100 100 2542 1 . ARG 101 101 2542 1 . ASP 102 102 2542 1 . PRO 103 103 2542 1 . GLN 104 104 2542 1 . GLY 105 105 2542 1 . ILE 106 106 2542 1 . ARG 107 107 2542 1 . ALA 108 108 2542 1 . TRP 109 109 2542 1 . VAL 110 110 2542 1 . ALA 111 111 2542 1 . TRP 112 112 2542 1 . ARG 113 113 2542 1 . ASN 114 114 2542 1 . ARG 115 115 2542 1 . CYS 116 116 2542 1 . GLN 117 117 2542 1 . ASN 118 118 2542 1 . ARG 119 119 2542 1 . ASP 120 120 2542 1 . VAL 121 121 2542 1 . ARG 122 122 2542 1 . GLN 123 123 2542 1 . TYR 124 124 2542 1 . VAL 125 125 2542 1 . GLN 126 126 2542 1 . GLY 127 127 2542 1 . CYS 128 128 2542 1 . GLY 129 129 2542 1 . VAL 130 130 2542 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 2542 _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 $lysozyme . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 2542 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 2542 _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 $lysozyme . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 2542 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 2542 _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 2542 _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 2542 1 temperature 313 . K 2542 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 2542 _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 2542 _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' . . 2542 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 2542 _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 . . . . . . . . . . . . . . . . 2542 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 2542 _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 N . 'liquid NH3' . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 2542 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 2542 _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 . 2542 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 VAL N N 15 129.1 . . 1 . . . . . . . . 2542 1 2 . 1 1 3 3 PHE N N 15 129.7 . . 1 . . . . . . . . 2542 1 3 . 1 1 4 4 GLU N N 15 122.4 . . 1 . . . . . . . . 2542 1 4 . 1 1 5 5 ARG N N 15 127.9 . . 1 . . . . . . . . 2542 1 5 . 1 1 6 6 CYS N N 15 116.6 . . 1 . . . . . . . . 2542 1 6 . 1 1 7 7 GLU N N 15 125.8 . . 1 . . . . . . . . 2542 1 7 . 1 1 8 8 LEU N N 15 124.1 . . 1 . . . . . . . . 2542 1 8 . 1 1 9 9 ALA N N 15 126 . . 1 . . . . . . . . 2542 1 9 . 1 1 10 10 ARG N N 15 117.4 . . 1 . . . . . . . . 2542 1 10 . 1 1 11 11 THR N N 15 120.8 . . 1 . . . . . . . . 2542 1 11 . 1 1 12 12 LEU N N 15 121.4 . . 1 . . . . . . . . 2542 1 12 . 1 1 13 13 LYS N N 15 121.6 . . 1 . . . . . . . . 2542 1 13 . 1 1 14 14 ARG N N 15 123.8 . . 1 . . . . . . . . 2542 1 14 . 1 1 15 15 LEU N N 15 119.3 . . 1 . . . . . . . . 2542 1 15 . 1 1 16 16 GLY N N 15 108.6 . . 1 . . . . . . . . 2542 1 16 . 1 1 17 17 MET N N 15 116.4 . . 1 . . . . . . . . 2542 1 17 . 1 1 18 18 ASP N N 15 120.6 . . 1 . . . . . . . . 2542 1 18 . 1 1 19 19 GLY N N 15 121.4 . . 1 . . . . . . . . 2542 1 19 . 1 1 20 20 TYR N N 15 128.4 . . 1 . . . . . . . . 2542 1 20 . 1 1 21 21 ARG N N 15 128.1 . . 1 . . . . . . . . 2542 1 21 . 1 1 22 22 GLY N N 15 105.5 . . 1 . . . . . . . . 2542 1 22 . 1 1 23 23 ILE N N 15 126.6 . . 1 . . . . . . . . 2542 1 23 . 1 1 24 24 SER N N 15 125.2 . . 1 . . . . . . . . 2542 1 24 . 1 1 25 25 LEU N N 15 124.1 . . 1 . . . . . . . . 2542 1 25 . 1 1 26 26 ALA N N 15 120.8 . . 1 . . . . . . . . 2542 1 26 . 1 1 27 27 ASN ND2 N 15 116.7 . . 1 . . . . . . . . 2542 1 27 . 1 1 27 27 ASN N N 15 119.1 . . 1 . . . . . . . . 2542 1 28 . 1 1 28 28 TRP NE1 N 15 130.8 . . 1 . . . . . . . . 2542 1 29 . 1 1 28 28 TRP N N 15 122.3 . . 1 . . . . . . . . 2542 1 30 . 1 1 29 29 MET N N 15 118.7 . . 1 . . . . . . . . 2542 1 31 . 1 1 30 30 CYS N N 15 122 . . 1 . . . . . . . . 2542 1 32 . 1 1 31 31 LEU N N 15 120.9 . . 1 . . . . . . . . 2542 1 33 . 1 1 32 32 ALA N N 15 121.4 . . 1 . . . . . . . . 2542 1 34 . 1 1 33 33 LYS N N 15 122.1 . . 1 . . . . . . . . 2542 1 35 . 1 1 34 34 TRP NE1 N 15 129.2 . . 1 . . . . . . . . 2542 1 36 . 1 1 34 34 TRP N N 15 120.1 . . 1 . . . . . . . . 2542 1 37 . 1 1 35 35 GLU N N 15 118.5 . . 1 . . . . . . . . 2542 1 38 . 1 1 36 36 SER N N 15 110.2 . . 1 . . . . . . . . 2542 1 39 . 1 1 37 37 GLY N N 15 118.3 . . 1 . . . . . . . . 2542 1 40 . 1 1 38 38 TYR N N 15 110.8 . . 1 . . . . . . . . 2542 1 41 . 1 1 39 39 ASN ND2 N 15 113.5 . . 1 . . . . . . . . 2542 1 42 . 1 1 39 39 ASN N N 15 119.6 . . 1 . . . . . . . . 2542 1 43 . 1 1 40 40 THR N N 15 117.6 . . 1 . . . . . . . . 2542 1 44 . 1 1 41 41 ARG N N 15 114.1 . . 1 . . . . . . . . 2542 1 45 . 1 1 42 42 ALA N N 15 124.9 . . 1 . . . . . . . . 2542 1 46 . 1 1 43 43 THR N N 15 116.2 . . 1 . . . . . . . . 2542 1 47 . 1 1 44 44 ASN ND2 N 15 116.8 . . 1 . . . . . . . . 2542 1 48 . 1 1 44 44 ASN N N 15 121.5 . . 1 . . . . . . . . 2542 1 49 . 1 1 45 45 TYR N N 15 129.6 . . 1 . . . . . . . . 2542 1 50 . 1 1 46 46 ASN ND2 N 15 116.1 . . 1 . . . . . . . . 2542 1 51 . 1 1 46 46 ASN N N 15 130.3 . . 1 . . . . . . . . 2542 1 52 . 1 1 47 47 ALA N N 15 127.8 . . 1 . . . . . . . . 2542 1 53 . 1 1 48 48 GLY N N 15 106.4 . . 1 . . . . . . . . 2542 1 54 . 1 1 49 49 ASP N N 15 119.1 . . 1 . . . . . . . . 2542 1 55 . 1 1 50 50 ARG N N 15 116.6 . . 1 . . . . . . . . 2542 1 56 . 1 1 51 51 SER N N 15 115.9 . . 1 . . . . . . . . 2542 1 57 . 1 1 52 52 THR N N 15 118.5 . . 1 . . . . . . . . 2542 1 58 . 1 1 53 53 ASP N N 15 126.7 . . 1 . . . . . . . . 2542 1 59 . 1 1 54 54 TYR N N 15 120.7 . . 1 . . . . . . . . 2542 1 60 . 1 1 55 55 GLY N N 15 114.6 . . 1 . . . . . . . . 2542 1 61 . 1 1 56 56 ILE N N 15 123.9 . . 1 . . . . . . . . 2542 1 62 . 1 1 57 57 PHE N N 15 117.6 . . 1 . . . . . . . . 2542 1 63 . 1 1 58 58 GLN NE2 N 15 117.8 . . 1 . . . . . . . . 2542 1 64 . 1 1 58 58 GLN N N 15 116.2 . . 1 . . . . . . . . 2542 1 65 . 1 1 59 59 ILE N N 15 124.3 . . 1 . . . . . . . . 2542 1 66 . 1 1 60 60 ASN ND2 N 15 117.8 . . 1 . . . . . . . . 2542 1 67 . 1 1 60 60 ASN N N 15 129.9 . . 1 . . . . . . . . 2542 1 68 . 1 1 61 61 SER N N 15 121.6 . . 1 . . . . . . . . 2542 1 69 . 1 1 62 62 ARG N N 15 126 . . 1 . . . . . . . . 2542 1 70 . 1 1 63 63 TYR N N 15 116.5 . . 1 . . . . . . . . 2542 1 71 . 1 1 64 64 TRP NE1 N 15 130.3 . . 1 . . . . . . . . 2542 1 72 . 1 1 64 64 TRP N N 15 116.9 . . 1 . . . . . . . . 2542 1 73 . 1 1 65 65 CYS N N 15 113.4 . . 1 . . . . . . . . 2542 1 74 . 1 1 66 66 ASN ND2 N 15 115.3 . . 1 . . . . . . . . 2542 1 75 . 1 1 66 66 ASN N N 15 121.6 . . 1 . . . . . . . . 2542 1 76 . 1 1 67 67 ASP N N 15 133.4 . . 1 . . . . . . . . 2542 1 77 . 1 1 68 68 GLY N N 15 110.9 . . 1 . . . . . . . . 2542 1 78 . 1 1 69 69 LYS N N 15 120 . . 1 . . . . . . . . 2542 1 79 . 1 1 70 70 THR N N 15 122.9 . . 1 . . . . . . . . 2542 1 80 . 1 1 72 72 GLY N N 15 112.5 . . 1 . . . . . . . . 2542 1 81 . 1 1 73 73 ALA N N 15 113.1 . . 1 . . . . . . . . 2542 1 82 . 1 1 74 74 VAL N N 15 122.7 . . 1 . . . . . . . . 2542 1 83 . 1 1 75 75 ASN ND2 N 15 107.5 . . 1 . . . . . . . . 2542 1 84 . 1 1 75 75 ASN N N 15 120.9 . . 1 . . . . . . . . 2542 1 85 . 1 1 76 76 ALA N N 15 122.8 . . 1 . . . . . . . . 2542 1 86 . 1 1 77 77 CYS N N 15 113 . . 1 . . . . . . . . 2542 1 87 . 1 1 78 78 HIS N N 15 119.8 . . 1 . . . . . . . . 2542 1 88 . 1 1 79 79 LEU N N 15 120.4 . . 1 . . . . . . . . 2542 1 89 . 1 1 80 80 SER N N 15 119.6 . . 1 . . . . . . . . 2542 1 90 . 1 1 81 81 CYS N N 15 128 . . 1 . . . . . . . . 2542 1 91 . 1 1 82 82 SER N N 15 116.7 . . 1 . . . . . . . . 2542 1 92 . 1 1 83 83 ALA N N 15 128 . . 1 . . . . . . . . 2542 1 93 . 1 1 84 84 LEU N N 15 118.7 . . 1 . . . . . . . . 2542 1 94 . 1 1 85 85 LEU N N 15 119.8 . . 1 . . . . . . . . 2542 1 95 . 1 1 86 86 GLN NE2 N 15 115.1 . . 1 . . . . . . . . 2542 1 96 . 1 1 86 86 GLN N N 15 118.6 . . 1 . . . . . . . . 2542 1 97 . 1 1 87 87 ASP N N 15 122.3 . . 1 . . . . . . . . 2542 1 98 . 1 1 88 88 ASN ND2 N 15 114.3 . . 1 . . . . . . . . 2542 1 99 . 1 1 88 88 ASN N N 15 116.7 . . 1 . . . . . . . . 2542 1 100 . 1 1 89 89 ILE N N 15 120.4 . . 1 . . . . . . . . 2542 1 101 . 1 1 90 90 ALA N N 15 128.2 . . 1 . . . . . . . . 2542 1 102 . 1 1 91 91 ASP N N 15 120.4 . . 1 . . . . . . . . 2542 1 103 . 1 1 92 92 ALA N N 15 125.3 . . 1 . . . . . . . . 2542 1 104 . 1 1 93 93 VAL N N 15 120.4 . . 1 . . . . . . . . 2542 1 105 . 1 1 94 94 ALA N N 15 123.7 . . 1 . . . . . . . . 2542 1 106 . 1 1 95 95 CYS N N 15 117.8 . . 1 . . . . . . . . 2542 1 107 . 1 1 96 96 ALA N N 15 126.5 . . 1 . . . . . . . . 2542 1 108 . 1 1 97 97 LYS N N 15 116.5 . . 1 . . . . . . . . 2542 1 109 . 1 1 98 98 ARG N N 15 120.6 . . 1 . . . . . . . . 2542 1 110 . 1 1 99 99 VAL N N 15 125.4 . . 1 . . . . . . . . 2542 1 111 . 1 1 100 100 VAL N N 15 110.8 . . 1 . . . . . . . . 2542 1 112 . 1 1 101 101 ARG N N 15 119.5 . . 1 . . . . . . . . 2542 1 113 . 1 1 102 102 ASP N N 15 123.5 . . 1 . . . . . . . . 2542 1 114 . 1 1 104 104 GLN NE2 N 15 113.4 . . 1 . . . . . . . . 2542 1 115 . 1 1 104 104 GLN N N 15 116.2 . . 1 . . . . . . . . 2542 1 116 . 1 1 105 105 GLY N N 15 111 . . 1 . . . . . . . . 2542 1 117 . 1 1 106 106 ILE N N 15 128.4 . . 1 . . . . . . . . 2542 1 118 . 1 1 107 107 ARG N N 15 119.1 . . 1 . . . . . . . . 2542 1 119 . 1 1 108 108 ALA N N 15 122.4 . . 1 . . . . . . . . 2542 1 120 . 1 1 109 109 TRP NE1 N 15 132.4 . . 1 . . . . . . . . 2542 1 121 . 1 1 109 109 TRP N N 15 118.8 . . 1 . . . . . . . . 2542 1 122 . 1 1 110 110 VAL N N 15 126.3 . . 1 . . . . . . . . 2542 1 123 . 1 1 111 111 ALA N N 15 122.3 . . 1 . . . . . . . . 2542 1 124 . 1 1 112 112 TRP NE1 N 15 130.6 . . 1 . . . . . . . . 2542 1 125 . 1 1 112 112 TRP N N 15 117.1 . . 1 . . . . . . . . 2542 1 126 . 1 1 113 113 ARG N N 15 121 . . 1 . . . . . . . . 2542 1 127 . 1 1 114 114 ASN ND2 N 15 113.3 . . 1 . . . . . . . . 2542 1 128 . 1 1 114 114 ASN N N 15 114 . . 1 . . . . . . . . 2542 1 129 . 1 1 115 115 ARG N N 15 116.2 . . 1 . . . . . . . . 2542 1 130 . 1 1 116 116 CYS N N 15 116.7 . . 1 . . . . . . . . 2542 1 131 . 1 1 117 117 GLN NE2 N 15 111.5 . . 1 . . . . . . . . 2542 1 132 . 1 1 117 117 GLN N N 15 123 . . 1 . . . . . . . . 2542 1 133 . 1 1 118 118 ASN ND2 N 15 114.9 . . 1 . . . . . . . . 2542 1 134 . 1 1 118 118 ASN N N 15 121.6 . . 1 . . . . . . . . 2542 1 135 . 1 1 119 119 ARG N N 15 118.9 . . 1 . . . . . . . . 2542 1 136 . 1 1 120 120 ASP N N 15 121.5 . . 1 . . . . . . . . 2542 1 137 . 1 1 121 121 VAL N N 15 120.8 . . 1 . . . . . . . . 2542 1 138 . 1 1 122 122 ARG N N 15 125.8 . . 1 . . . . . . . . 2542 1 139 . 1 1 123 123 GLN NE2 N 15 113.5 . . 1 . . . . . . . . 2542 1 140 . 1 1 123 123 GLN N N 15 118.2 . . 1 . . . . . . . . 2542 1 141 . 1 1 124 124 TYR N N 15 118.8 . . 1 . . . . . . . . 2542 1 142 . 1 1 125 125 VAL N N 15 107.1 . . 1 . . . . . . . . 2542 1 143 . 1 1 126 126 GLN NE2 N 15 113.3 . . 1 . . . . . . . . 2542 1 144 . 1 1 126 126 GLN N N 15 126.7 . . 1 . . . . . . . . 2542 1 145 . 1 1 127 127 GLY N N 15 115.7 . . 1 . . . . . . . . 2542 1 146 . 1 1 128 128 CYS N N 15 116.5 . . 1 . . . . . . . . 2542 1 147 . 1 1 129 129 GLY N N 15 113.8 . . 1 . . . . . . . . 2542 1 148 . 1 1 130 130 VAL N N 15 119.1 . . 1 . . . . . . . . 2542 1 stop_ save_