data_76 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 76 _Entry.Title ; Assignment of resonances in the 1H NMR spectrum of human lysozyme ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-03-25 _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 Jonathan Boyd . . . 76 2 Christopher Dobson . M. . 76 3 Christina Redfield . . . 76 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 76 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 183 76 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 4 . . 2010-06-10 . revision BMRB 'Complete natural source information' 76 3 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 76 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 76 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 76 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 76 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Boyd, Jonathan, Dobson, Christopher M., Redfield, Christina, "Assignment of resonances in the 1H NMR spectrum of human lysozyme," Eur. J. Biochem. 153, 383-396 (1985). ; _Citation.Title 'Assignment of resonances in the 1H NMR spectrum of human lysozyme' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full . _Citation.Journal_volume 153 _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 383 _Citation.Page_last 396 _Citation.Year 1985 _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 Jonathan Boyd . . . 76 1 2 Christopher Dobson . M. . 76 1 3 Christina Redfield . . . 76 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_lysozyme _Assembly.Sf_category assembly _Assembly.Sf_framecode system_lysozyme _Assembly.Entry_ID 76 _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 . . . . . . . . . 76 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID lysozyme system 76 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_lysozyme _Entity.Sf_category entity _Entity.Sf_framecode lysozyme _Entity.Entry_ID 76 _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 VRQYVQGCGL ; _Entity.Polymer_seq_one_letter_code ; KVFERCELARTLKRLGMDGY RGISLANWMCLAKWESGYNT RATNYNAGDRSTDYGIFQIN SRYWCNDGKTPGAVNACHLS CSALLQDNIADAVACAKRVV RDPQGIRAWVAWRNRCQNRD VRQYVQGCGL ; _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 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 2542 . lysozyme . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 2 no BMRB 5123 . lysozyme . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 3 no BMRB 5124 . lysozyme_I56T . . . . . 100.00 130 98.46 99.23 2.24e-88 . . . . 76 1 4 no BMRB 5125 . lysozyme_67H . . . . . 100.00 130 98.46 99.23 3.78e-88 . . . . 76 1 5 no BMRB 5130 . human_lysozyme . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 6 no BMRB 5142 . human_lysozyme . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 7 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 98.46 99.23 2.21e-88 . . . . 76 1 8 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 98.46 99.23 2.05e-88 . . . . 76 1 9 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 98.46 100.00 1.56e-88 . . . . 76 1 10 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 98.46 100.00 1.56e-88 . . . . 76 1 11 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 98.46 100.00 1.56e-88 . . . . 76 1 12 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 98.46 100.00 1.56e-88 . . . . 76 1 13 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 98.46 100.00 1.56e-88 . . . . 76 1 14 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 98.46 100.00 1.56e-88 . . . . 76 1 15 no PDB 1B7L . "Verification Of Spmp Using Mutant Human Lysozymes" . . . . . 100.00 130 98.46 99.23 3.28e-88 . . . . 76 1 16 no PDB 1B7M . "Verification Of Spmp Using Mutant Human Lysozymes" . . . . . 100.00 130 98.46 99.23 2.47e-88 . . . . 76 1 17 no PDB 1B7N . "Verification Of Spmp Using Mutant Human Lysozymes" . . . . . 100.00 130 98.46 99.23 9.05e-88 . . . . 76 1 18 no PDB 1B7O . "Verification Of Spmp Using Mutant Human Lysozymes" . . . . . 100.00 130 98.46 99.23 4.91e-88 . . . . 76 1 19 no PDB 1B7P . "Verification Of Spmp Using Mutant Human Lysozymes" . . . . . 100.00 130 98.46 99.23 1.78e-87 . . . . 76 1 20 no PDB 1B7Q . "Verification Of Spmp Using Mutant Human Lysozymes" . . . . . 100.00 130 98.46 99.23 9.25e-88 . . . . 76 1 21 no PDB 1B7R . "Verification Of Spmp Using Mutant Human Lysozymes" . . . . . 100.00 130 98.46 99.23 6.88e-88 . . . . 76 1 22 no PDB 1B7S . "Verification Of Spmp Using Mutant Human Lysozymes" . . . . . 100.00 130 98.46 99.23 2.84e-88 . . . . 76 1 23 no PDB 1BB3 . "Human Lysozyme Mutant A96l" . . . . . 100.00 130 98.46 99.23 3.28e-88 . . . . 76 1 24 no PDB 1BB4 . "Human Lysozyme Double Mutant A96l, W109h" . . . . . 100.00 130 97.69 98.46 5.25e-87 . . . . 76 1 25 no PDB 1BB5 . "Human Lysozyme Mutant A96l Complexed With Chitotriose" . . . . . 100.00 130 98.46 99.23 3.28e-88 . . . . 76 1 26 no PDB 1C43 . "Mutant Human Lysozyme With Foreign N-Terminal Residues" . . . . . 99.23 130 99.22 100.00 2.52e-88 . . . . 76 1 27 no PDB 1C45 . "Mutant Human Lysozyme With Foreign N-Terminal Residues" . . . . . 99.23 130 99.22 100.00 2.81e-88 . . . . 76 1 28 no PDB 1C46 . "Mutant Human Lysozyme With Foreign N-Terminal Residues" . . . . . 100.00 131 99.23 100.00 5.77e-89 . . . . 76 1 29 no PDB 1C7P . "Crystal Structure Of Mutant Human Lysozyme With Four Extra Residues (Eaea) At The N-Terminal" . . . . . 100.00 134 99.23 100.00 2.75e-89 . . . . 76 1 30 no PDB 1CJ6 . "T11a Mutant Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.78e-88 . . . . 76 1 31 no PDB 1CJ7 . "T11v Mutant Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.63e-88 . . . . 76 1 32 no PDB 1CJ8 . "T40a Mutant Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.78e-88 . . . . 76 1 33 no PDB 1CJ9 . "T40v Mutant Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.63e-88 . . . . 76 1 34 no PDB 1CKC . "T43a Mutant Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.78e-88 . . . . 76 1 35 no PDB 1CKD . "T43v Mutant Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.63e-88 . . . . 76 1 36 no PDB 1CKF . "T52a Mutant Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.78e-88 . . . . 76 1 37 no PDB 1CKG . "T52v Mutant Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.63e-88 . . . . 76 1 38 no PDB 1CKH . "T70v Mutant Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.63e-88 . . . . 76 1 39 no PDB 1D6P . "Human Lysozyme L63 Mutant Labelled With 2',3'-Epoxypropyl N,N'- Diacetylchitobiose" . . . . . 100.00 130 98.46 99.23 5.97e-88 . . . . 76 1 40 no PDB 1D6Q . "Human Lysozyme E102 Mutant Labelled With 2',3'-Epoxypropyl Glycoside Of N-Acetyllactosamine" . . . . . 100.00 130 98.46 100.00 1.46e-88 . . . . 76 1 41 no PDB 1DI3 . "Role Of Amino Acid Residues At Turns In The Conformational Stability And Folding Of Human Lysozyme" . . . . . 100.00 130 98.46 99.23 5.91e-88 . . . . 76 1 42 no PDB 1DI4 . "Role Of Amino Acid Residues At Turns In The Conformational Stability And Folding Of Human Lysozyme" . . . . . 100.00 128 97.69 98.46 1.15e-85 . . . . 76 1 43 no PDB 1DI5 . "Role Of Amino Acid Residues At Turns In The Conformational Stability And Folding Of Human Lysozyme" . . . . . 100.00 129 98.46 99.23 1.60e-86 . . . . 76 1 44 no PDB 1EQ4 . "Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme" . . . . . 100.00 130 98.46 100.00 1.61e-88 . . . . 76 1 45 no PDB 1EQ5 . "Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme" . . . . . 100.00 130 98.46 100.00 2.36e-88 . . . . 76 1 46 no PDB 1EQE . "Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme" . . . . . 100.00 130 98.46 100.00 2.36e-88 . . . . 76 1 47 no PDB 1GAY . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 5.97e-88 . . . . 76 1 48 no PDB 1GAZ . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 100.00 7.67e-89 . . . . 76 1 49 no PDB 1GB0 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 100.00 1.41e-88 . . . . 76 1 50 no PDB 1GB2 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 100.00 1.41e-88 . . . . 76 1 51 no PDB 1GB3 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 2.52e-88 . . . . 76 1 52 no PDB 1GB5 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 5.97e-88 . . . . 76 1 53 no PDB 1GB6 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 100.00 7.67e-89 . . . . 76 1 54 no PDB 1GB7 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 100.00 1.41e-88 . . . . 76 1 55 no PDB 1GB8 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 100.00 1.41e-88 . . . . 76 1 56 no PDB 1GB9 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 2.52e-88 . . . . 76 1 57 no PDB 1GBO . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 5.97e-88 . . . . 76 1 58 no PDB 1GBW . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 100.00 7.67e-89 . . . . 76 1 59 no PDB 1GBX . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 100.00 1.41e-88 . . . . 76 1 60 no PDB 1GBY . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 100.00 1.41e-88 . . . . 76 1 61 no PDB 1GBZ . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 2.52e-88 . . . . 76 1 62 no PDB 1GDW . "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" . . . . . 100.00 130 98.46 99.23 5.91e-88 . . . . 76 1 63 no PDB 1GDX . "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" . . . . . 100.00 130 98.46 99.23 3.78e-88 . . . . 76 1 64 no PDB 1GE0 . "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" . . . . . 100.00 130 98.46 99.23 1.14e-87 . . . . 76 1 65 no PDB 1GE1 . "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" . . . . . 100.00 130 98.46 99.23 3.78e-88 . . . . 76 1 66 no PDB 1GE2 . "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" . . . . . 100.00 130 98.46 99.23 1.20e-87 . . . . 76 1 67 no PDB 1GE3 . "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" . . . . . 100.00 130 98.46 99.23 3.90e-88 . . . . 76 1 68 no PDB 1GE4 . "Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions" . . . . . 100.00 130 98.46 99.23 4.70e-88 . . . . 76 1 69 no PDB 1GEV . "Buried Polar Mutant Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.69e-88 . . . . 76 1 70 no PDB 1GEZ . "Buried Polar Mutant Human Lysozyme" . . . . . 100.00 130 98.46 100.00 1.12e-88 . . . . 76 1 71 no PDB 1GF0 . "Buried Polar Mutant Human Lysozyme" . . . . . 100.00 130 98.46 100.00 1.12e-88 . . . . 76 1 72 no PDB 1GF3 . "Buried Polar Mutant Human Lysozyme" . . . . . 100.00 130 98.46 100.00 1.12e-88 . . . . 76 1 73 no PDB 1GF4 . "Buried Polar Mutant Human Lysozyme" . . . . . 100.00 130 98.46 99.23 1.65e-88 . . . . 76 1 74 no PDB 1GF5 . "Buried Polar Mutant Human Lysozyme" . . . . . 100.00 130 98.46 100.00 1.12e-88 . . . . 76 1 75 no PDB 1GF6 . "Buried Polar Mutant Human Lysozyme" . . . . . 100.00 130 98.46 99.23 1.65e-88 . . . . 76 1 76 no PDB 1GF7 . "Buried Polar Mutant Human Lysozyme" . . . . . 100.00 130 98.46 99.23 1.65e-88 . . . . 76 1 77 no PDB 1GF8 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 2.84e-88 . . . . 76 1 78 no PDB 1GF9 . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 3.39e-88 . . . . 76 1 79 no PDB 1GFA . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 6.17e-88 . . . . 76 1 80 no PDB 1GFE . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 5.59e-88 . . . . 76 1 81 no PDB 1GFG . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 6.17e-88 . . . . 76 1 82 no PDB 1GFH . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 3.39e-88 . . . . 76 1 83 no PDB 1GFJ . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 6.17e-88 . . . . 76 1 84 no PDB 1GFK . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 5.59e-88 . . . . 76 1 85 no PDB 1GFR . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 6.17e-88 . . . . 76 1 86 no PDB 1GFT . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 3.39e-88 . . . . 76 1 87 no PDB 1GFU . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 6.17e-88 . . . . 76 1 88 no PDB 1GFV . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 5.59e-88 . . . . 76 1 89 no PDB 1HNL . "Crystal Structure Of A Glutathionylated Human Lysozyme: A Folding Intermediate Mimic In The Formation Of A Disulfide Bond" . . . . . 100.00 130 98.46 99.23 4.80e-88 . . . . 76 1 90 no PDB 1I1Z . "Mutant Human Lysozyme (Q86d)" . . . . . 100.00 130 98.46 99.23 4.17e-88 . . . . 76 1 91 no PDB 1I20 . "Mutant Human Lysozyme (A92d)" . . . . . 100.00 130 98.46 99.23 4.40e-88 . . . . 76 1 92 no PDB 1I22 . "Mutant Human Lysozyme (A83kQ86DA92D)" . . . . . 100.00 130 96.92 97.69 1.37e-86 . . . . 76 1 93 no PDB 1INU . "Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions" . . . . . 100.00 130 98.46 99.23 6.17e-88 . . . . 76 1 94 no PDB 1IOC . "Crystal Structure Of Mutant Human Lysozyme, Eaea-I56t" . . . . . 100.00 134 98.46 99.23 1.41e-88 . . . . 76 1 95 no PDB 1IP1 . "G37a Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.66e-88 . . . . 76 1 96 no PDB 1IP2 . "G48a Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.66e-88 . . . . 76 1 97 no PDB 1IP3 . "G68a Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.66e-88 . . . . 76 1 98 no PDB 1IP4 . "G72a Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.66e-88 . . . . 76 1 99 no PDB 1IP5 . "G105a Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.66e-88 . . . . 76 1 100 no PDB 1IP6 . "G127a Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.66e-88 . . . . 76 1 101 no PDB 1IP7 . "G129a Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.66e-88 . . . . 76 1 102 no PDB 1IWT . "Crystal Structure Analysis Of Human Lysozyme At 113k." . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 103 no PDB 1IWU . "Crystal Structure Analysis Of Human Lysozyme At 127k." . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 104 no PDB 1IWV . "Crystal Structure Analysis Of Human Lysozyme At 147k." . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 105 no PDB 1IWW . "Crystal Structure Analysis Of Human Lysozyme At 152k." . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 106 no PDB 1IWX . "Crystal Structure Analysis Of Human Lysozyme At 161k." . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 107 no PDB 1IWY . "Crystal Structure Analysis Of Human Lysozyme At 170k." . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 108 no PDB 1IWZ . "Crystal Structure Analysis Of Human Lysozyme At 178k." . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 109 no PDB 1IX0 . "I59a-3ss Human Lysozyme" . . . . . 100.00 130 96.92 97.69 2.29e-86 . . . . 76 1 110 no PDB 1IY3 . "Solution Structure Of The Human Lysozyme At 4 Degree C" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 111 no PDB 1IY4 . "Solution Structure Of The Human Lysozyme At 35 Degree C" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 112 no PDB 1JKA . "Human Lysozyme Mutant With Glu 35 Replaced By Asp" . . . . . 100.00 130 98.46 100.00 2.21e-88 . . . . 76 1 113 no PDB 1JKB . "Human Lysozyme Mutant With Glu 35 Replaced By Ala" . . . . . 100.00 130 98.46 99.23 4.65e-88 . . . . 76 1 114 no PDB 1JKC . "Human Lysozyme Mutant With Trp 109 Replaced By Phe" . . . . . 100.00 130 98.46 100.00 2.91e-88 . . . . 76 1 115 no PDB 1JKD . "Human Lysozyme Mutant With Trp 109 Replaced By Ala" . . . . . 100.00 130 98.46 99.23 1.03e-87 . . . . 76 1 116 no PDB 1JSF . "Full-Matrix Least-Squares Refinement Of Human Lysozyme" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 117 no PDB 1JWR . "Crystal Structure Of Human Lysozyme At 100 K" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 118 no PDB 1LAA . "X-Ray Structure Of Glu 53 Human Lysozyme" . . . . . 100.00 130 98.46 100.00 1.46e-88 . . . . 76 1 119 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 98.46 99.23 3.21e-88 . . . . 76 1 120 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 98.46 99.23 1.48e-87 . . . . 76 1 121 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 98.46 99.23 1.48e-87 . . . . 76 1 122 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 98.46 99.23 4.26e-88 . . . . 76 1 123 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 98.46 99.23 2.24e-88 . . . . 76 1 124 no PDB 1LHM . "The Crystal Structure Of A Mutant Lysozyme C77(Slash)95a With Increased Secretion Efficiency In Yeast" . . . . . 100.00 130 97.69 98.46 3.32e-87 . . . . 76 1 125 no PDB 1LOZ . "Amyloidogenic Variant (i56t) Variant Of Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.24e-88 . . . . 76 1 126 no PDB 1LYY . "Amyloidogenic Variant (Asp67his) Of Human Lysozyme" . . . . . 100.00 130 98.46 99.23 3.78e-88 . . . . 76 1 127 no PDB 1LZ1 . "Refinement Of Human Lysozyme At 1.5 Angstroms Resolution. Analysis Of Non-Bonded And Hydrogen-Bond Interactions" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 128 no PDB 1LZ4 . "Enthalpic Destabilization Of A Mutant Human Lysozyme Lacking A Disulfide Bridge Between Cysteine-77 And Cysteine-95" . . . . . 100.00 130 98.46 99.23 4.80e-88 . . . . 76 1 129 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 99.23 100.00 5.06e-89 . . . . 76 1 130 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 99.23 100.00 5.06e-89 . . . . 76 1 131 no PDB 1OP9 . "Complex Of Human Lysozyme With Camelid Vhh Hl6 Antibody Fragment" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 132 no PDB 1OUA . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The I56t Mutant" . . . . . 100.00 130 98.46 99.23 2.24e-88 . . . . 76 1 133 no PDB 1OUB . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-ray Structure Of The V100a Mutant" . . . . . 100.00 130 98.46 99.23 1.98e-88 . . . . 76 1 134 no PDB 1OUC . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V110a Mutant" . . . . . 100.00 130 98.46 99.23 1.98e-88 . . . . 76 1 135 no PDB 1OUD . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V121a Mutant" . . . . . 100.00 130 98.46 99.23 1.98e-88 . . . . 76 1 136 no PDB 1OUE . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V125a Mutant" . . . . . 100.00 130 98.46 99.23 1.98e-88 . . . . 76 1 137 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 7.58e-89 . . . . 76 1 138 no PDB 1OUG . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V2a Mutant" . . . . . 100.00 130 98.46 99.23 1.98e-88 . . . . 76 1 139 no PDB 1OUH . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V74a Mutant" . . . . . 100.00 130 98.46 99.23 1.98e-88 . . . . 76 1 140 no PDB 1OUI . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V93a Mutant" . . . . . 100.00 130 98.46 99.23 1.98e-88 . . . . 76 1 141 no PDB 1OUJ . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: X-Ray Structure Of The V99a Mutant" . . . . . 100.00 130 98.46 99.23 1.98e-88 . . . . 76 1 142 no PDB 1QSW . "Crystal Structure Analysis Of A Human Lysozyme Mutant W64c C65a" . . . . . 100.00 130 97.69 98.46 2.15e-86 . . . . 76 1 143 no PDB 1RE2 . "Human Lysozyme Labelled With Two 2',3'-epoxypropyl Beta-glycoside Of N-acetyllactosamine" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 144 no PDB 1REM . "Human Lysozyme With Man-B1,4-Glcnac Covalently Attached To Asp53" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 145 no PDB 1REX . "Native Human Lysozyme" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 146 no PDB 1REY . "Human Lysozyme-N,N'-Diacetylchitobiose Complex" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 147 no PDB 1REZ . "Human Lysozyme-N-Acetyllactosamine Complex" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 148 no PDB 1TAY . "Dissection Of The Functional Role Of Structural Elements Of Tyrosine-63 In The Catalytic Action Of Human Lysozyme" . . . . . 100.00 130 98.46 99.23 7.04e-88 . . . . 76 1 149 no PDB 1TBY . "Dissection Of The Functional Role Of Structural Elements Of Tyrosine-63 In The Catalytic Action Of Human Lysozyme" . . . . . 100.00 130 98.46 99.23 5.97e-88 . . . . 76 1 150 no PDB 1TCY . "Dissection Of The Functional Role Of Structural Elements Of Tyrosine-63 In The Catalytic Action Of Human Lysozyme" . . . . . 100.00 130 98.46 100.00 1.27e-88 . . . . 76 1 151 no PDB 1TDY . "Dissection Of The Functional Role Of Structural Elements Of Tyrosine-63 In The Catalytic Action Of Human Lysozyme" . . . . . 100.00 130 98.46 100.00 3.99e-88 . . . . 76 1 152 no PDB 1UBZ . "Crystal Structure Of Glu102-Mutant Human Lysozyme Doubly Labeled With 2',3'-Epoxypropyl Beta-Glycoside Of N-Acetyllactosamine" . . . . . 100.00 130 98.46 100.00 1.46e-88 . . . . 76 1 153 no PDB 1W08 . "Structure Of T70n Human Lysozyme" . . . . . 100.00 130 98.46 99.23 3.17e-88 . . . . 76 1 154 no PDB 1WQM . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 98.46 100.00 1.27e-88 . . . . 76 1 155 no PDB 1WQN . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 98.46 100.00 1.27e-88 . . . . 76 1 156 no PDB 1WQO . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 98.46 100.00 1.27e-88 . . . . 76 1 157 no PDB 1WQP . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 98.46 100.00 1.27e-88 . . . . 76 1 158 no PDB 1WQQ . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 98.46 100.00 1.27e-88 . . . . 76 1 159 no PDB 1WQR . "Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 98.46 100.00 1.27e-88 . . . . 76 1 160 no PDB 1YAM . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of " . . . . . 100.00 130 98.46 100.00 7.92e-89 . . . . 76 1 161 no PDB 1YAN . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of " . . . . . 100.00 130 98.46 100.00 7.92e-89 . . . . 76 1 162 no PDB 1YAO . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of " . . . . . 100.00 130 98.46 100.00 7.92e-89 . . . . 76 1 163 no PDB 1YAP . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of " . . . . . 100.00 130 98.46 100.00 7.92e-89 . . . . 76 1 164 no PDB 1YAQ . "Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of " . . . . . 100.00 130 98.46 100.00 7.92e-89 . . . . 76 1 165 no PDB 207L . "Mutant Human Lysozyme C77a" . . . . . 100.00 130 98.46 99.23 4.80e-88 . . . . 76 1 166 no PDB 208L . "Mutant Human Lysozyme C77a" . . . . . 100.00 130 98.46 99.23 4.80e-88 . . . . 76 1 167 no PDB 2BQA . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 97.69 98.46 3.32e-87 . . . . 76 1 168 no PDB 2BQB . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 96.92 98.46 4.71e-87 . . . . 76 1 169 no PDB 2BQC . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 96.92 98.46 4.71e-87 . . . . 76 1 170 no PDB 2BQD . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 96.92 98.46 4.71e-87 . . . . 76 1 171 no PDB 2BQE . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 96.92 98.46 4.71e-87 . . . . 76 1 172 no PDB 2BQF . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 96.92 98.46 4.71e-87 . . . . 76 1 173 no PDB 2BQG . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 96.92 97.69 1.31e-86 . . . . 76 1 174 no PDB 2BQH . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 96.92 97.69 1.31e-86 . . . . 76 1 175 no PDB 2BQI . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 96.92 97.69 1.31e-86 . . . . 76 1 176 no PDB 2BQJ . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 96.92 97.69 1.31e-86 . . . . 76 1 177 no PDB 2BQK . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 99.23 130 98.45 98.45 4.97e-87 . . . . 76 1 178 no PDB 2BQL . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 96.92 97.69 1.31e-86 . . . . 76 1 179 no PDB 2BQM . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 96.92 97.69 1.31e-86 . . . . 76 1 180 no PDB 2BQN . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 96.92 97.69 1.31e-86 . . . . 76 1 181 no PDB 2BQO . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 96.92 97.69 1.31e-86 . . . . 76 1 182 no PDB 2HEA . "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" . . . . . 100.00 130 98.46 99.23 3.17e-88 . . . . 76 1 183 no PDB 2HEB . "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" . . . . . 100.00 130 98.46 99.23 3.17e-88 . . . . 76 1 184 no PDB 2HEC . "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" . . . . . 100.00 130 98.46 99.23 3.17e-88 . . . . 76 1 185 no PDB 2HED . "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" . . . . . 100.00 130 98.46 99.23 3.17e-88 . . . . 76 1 186 no PDB 2HEE . "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" . . . . . 100.00 130 98.46 99.23 7.76e-88 . . . . 76 1 187 no PDB 2HEF . "Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability" . . . . . 100.00 130 98.46 99.23 3.17e-88 . . . . 76 1 188 no PDB 2LHM . "Crystal Structures Of The Apo-And Holomutant Human Lysozymes With An Introduced Ca2+ Binding Site" . . . . . 100.00 130 97.69 98.46 3.43e-87 . . . . 76 1 189 no PDB 2MEA . "Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions" . . . . . 100.00 130 98.46 99.23 1.98e-88 . . . . 76 1 190 no PDB 2MEB . "Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions" . . . . . 100.00 130 98.46 100.00 1.25e-88 . . . . 76 1 191 no PDB 2MEC . "Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions" . . . . . 100.00 130 98.46 100.00 1.37e-88 . . . . 76 1 192 no PDB 2MED . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 98.46 99.23 1.98e-88 . . . . 76 1 193 no PDB 2MEE . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 98.46 100.00 1.25e-88 . . . . 76 1 194 no PDB 2MEF . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 98.46 100.00 1.37e-88 . . . . 76 1 195 no PDB 2MEG . "Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions" . . . . . 100.00 130 98.46 99.23 3.90e-88 . . . . 76 1 196 no PDB 2MEH . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 98.46 99.23 2.24e-88 . . . . 76 1 197 no PDB 2MEI . "Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme" . . . . . 100.00 130 98.46 99.23 4.12e-88 . . . . 76 1 198 no PDB 2NWD . "Structure Of Chemically Synthesized Human Lysozyme At 1 Angstrom Resolution" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 199 no PDB 2ZIJ . "Crystal Structure Of Human Lysozyme Expressed In E. Coli." . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 200 no PDB 2ZIK . "Crystal Structure Of Human Lysozyme From Pichia Pastoris" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 201 no PDB 2ZIL . "Crystal Structure Of Human Lysozyme From Urine" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 202 no PDB 2ZWB . "Neutron Crystal Structure Of Wild Type Human Lysozyme In D2o" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 203 no PDB 3EBA . "Cabhul6 Fglw Mutant (Humanized) In Complex With Human Lysozyme" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 204 no PDB 3FE0 . "X-Ray Crystal Structure Of Wild Type Human Lysozyme In D2o" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 205 no PDB 3LHM . "Crystal Structures Of The Apo-And Holomutant Human Lysozymes With An Introduced Ca2+ Binding Site" . . . . . 100.00 130 97.69 98.46 3.43e-87 . . . . 76 1 206 no PDB 3LN2 . "Crystal Structure Of A Charge Engineered Human Lysozyme Variant" . . . . . 100.00 130 97.69 98.46 1.84e-87 . . . . 76 1 207 no PDB 4I0C . "The Structure Of The Camelid Antibody Cabhul5 In Complex With Human Lysozyme" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 208 no PDB 4ML7 . "Crystal Structure Of Brucella Abortus Plic In Complex With Human Lysozyme" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 209 no DBJ BAA00314 . "lysozyme [synthetic construct]" . . . . . 100.00 131 98.46 99.23 4.40e-88 . . . . 76 1 210 no DBJ BAG34722 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 148 99.23 100.00 1.18e-89 . . . . 76 1 211 no DBJ BAG73364 . "lysozyme [synthetic construct]" . . . . . 100.00 148 98.46 99.23 1.01e-88 . . . . 76 1 212 no EMBL CAA32175 . "lysozyme [Homo sapiens]" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 213 no EMBL CAA53144 . "lysozyme [synthetic construct]" . . . . . 100.00 131 99.23 100.00 4.16e-89 . . . . 76 1 214 no GB AAA36188 . "lysozyme precursor (EC 3.2.1.17) [Homo sapiens]" . . . . . 100.00 148 98.46 100.00 3.32e-89 . . . . 76 1 215 no GB AAA59535 . "lysozyme precursor (EC 3.2.1.17) [Homo sapiens]" . . . . . 100.00 148 99.23 100.00 1.18e-89 . . . . 76 1 216 no GB AAA59536 . "lysozyme precursor (EC 3.2.1.17) [Homo sapiens]" . . . . . 100.00 148 99.23 100.00 1.18e-89 . . . . 76 1 217 no GB AAA72819 . "lysozyme, partial [synthetic construct]" . . . . . 100.00 130 99.23 100.00 5.06e-89 . . . . 76 1 218 no GB AAB26052 . "lysozyme=amyloid fibril protein [human, Peptide Mutant, 130 aa]" . . . . . 100.00 130 98.46 99.23 2.24e-88 . . . . 76 1 219 no REF NP_000230 . "lysozyme C precursor [Homo sapiens]" . . . . . 100.00 148 99.23 100.00 1.18e-89 . . . . 76 1 220 no REF NP_001009073 . "lysozyme C precursor [Pan troglodytes]" . . . . . 100.00 148 99.23 100.00 1.18e-89 . . . . 76 1 221 no REF NP_001266591 . "lysozyme precursor [Gorilla gorilla]" . . . . . 100.00 148 99.23 100.00 1.20e-89 . . . . 76 1 222 no REF XP_002823550 . "PREDICTED: lysozyme C [Pongo abelii]" . . . . . 100.00 148 98.46 99.23 4.97e-89 . . . . 76 1 223 no REF XP_003808770 . "PREDICTED: lysozyme C [Pan paniscus]" . . . . . 100.00 148 99.23 100.00 1.18e-89 . . . . 76 1 224 no SP P61626 . "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Homo sapiens]" . . . . . 100.00 148 99.23 100.00 1.18e-89 . . . . 76 1 225 no SP P61627 . "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Pan paniscus]" . . . . . 100.00 148 99.23 100.00 1.18e-89 . . . . 76 1 226 no SP P61628 . "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Pan troglodytes]" . . . . . 100.00 148 99.23 100.00 1.18e-89 . . . . 76 1 227 no SP P79179 . "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Gorilla gorilla gorilla]" . . . . . 100.00 148 99.23 100.00 1.20e-89 . . . . 76 1 228 no SP P79239 . "RecName: Full=Lysozyme C; AltName: Full=1,4-beta-N-acetylmuramidase C; Flags: Precursor [Pongo pygmaeus]" . . . . . 100.00 148 98.46 99.23 4.97e-89 . . . . 76 1 229 no TPE CDM98740 . "TPA: lysozyme F1 [Homo sapiens]" . . . . . 100.00 148 99.23 100.00 1.18e-89 . . . . 76 1 230 no TPE CDM98750 . "TPA: lysozyme F1 [Pongo abelii]" . . . . . 100.00 148 98.46 99.23 4.97e-89 . . . . 76 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID lysozyme common 76 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 . 76 1 2 . VAL . 76 1 3 . PHE . 76 1 4 . GLU . 76 1 5 . ARG . 76 1 6 . CYS . 76 1 7 . GLU . 76 1 8 . LEU . 76 1 9 . ALA . 76 1 10 . ARG . 76 1 11 . THR . 76 1 12 . LEU . 76 1 13 . LYS . 76 1 14 . ARG . 76 1 15 . LEU . 76 1 16 . GLY . 76 1 17 . MET . 76 1 18 . ASP . 76 1 19 . GLY . 76 1 20 . TYR . 76 1 21 . ARG . 76 1 22 . GLY . 76 1 23 . ILE . 76 1 24 . SER . 76 1 25 . LEU . 76 1 26 . ALA . 76 1 27 . ASN . 76 1 28 . TRP . 76 1 29 . MET . 76 1 30 . CYS . 76 1 31 . LEU . 76 1 32 . ALA . 76 1 33 . LYS . 76 1 34 . TRP . 76 1 35 . GLU . 76 1 36 . SER . 76 1 37 . GLY . 76 1 38 . TYR . 76 1 39 . ASN . 76 1 40 . THR . 76 1 41 . ARG . 76 1 42 . ALA . 76 1 43 . THR . 76 1 44 . ASN . 76 1 45 . TYR . 76 1 46 . ASN . 76 1 47 . ALA . 76 1 48 . GLY . 76 1 49 . ASP . 76 1 50 . ARG . 76 1 51 . SER . 76 1 52 . THR . 76 1 53 . ASP . 76 1 54 . TYR . 76 1 55 . GLY . 76 1 56 . ILE . 76 1 57 . PHE . 76 1 58 . GLN . 76 1 59 . ILE . 76 1 60 . ASN . 76 1 61 . SER . 76 1 62 . ARG . 76 1 63 . TYR . 76 1 64 . TRP . 76 1 65 . CYS . 76 1 66 . ASN . 76 1 67 . ASP . 76 1 68 . GLY . 76 1 69 . LYS . 76 1 70 . THR . 76 1 71 . PRO . 76 1 72 . GLY . 76 1 73 . ALA . 76 1 74 . VAL . 76 1 75 . ASN . 76 1 76 . ALA . 76 1 77 . CYS . 76 1 78 . HIS . 76 1 79 . LEU . 76 1 80 . SER . 76 1 81 . CYS . 76 1 82 . SER . 76 1 83 . ALA . 76 1 84 . LEU . 76 1 85 . LEU . 76 1 86 . GLN . 76 1 87 . ASP . 76 1 88 . ASN . 76 1 89 . ILE . 76 1 90 . ALA . 76 1 91 . ASP . 76 1 92 . ALA . 76 1 93 . VAL . 76 1 94 . ALA . 76 1 95 . CYS . 76 1 96 . ALA . 76 1 97 . LYS . 76 1 98 . ARG . 76 1 99 . VAL . 76 1 100 . VAL . 76 1 101 . ARG . 76 1 102 . ASP . 76 1 103 . PRO . 76 1 104 . GLN . 76 1 105 . GLY . 76 1 106 . ILE . 76 1 107 . ARG . 76 1 108 . ALA . 76 1 109 . TRP . 76 1 110 . VAL . 76 1 111 . ALA . 76 1 112 . TRP . 76 1 113 . ARG . 76 1 114 . ASN . 76 1 115 . ARG . 76 1 116 . CYS . 76 1 117 . GLN . 76 1 118 . ASN . 76 1 119 . ARG . 76 1 120 . ASP . 76 1 121 . VAL . 76 1 122 . ARG . 76 1 123 . GLN . 76 1 124 . TYR . 76 1 125 . VAL . 76 1 126 . GLN . 76 1 127 . GLY . 76 1 128 . CYS . 76 1 129 . GLY . 76 1 130 . LEU . 76 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 76 1 . VAL 2 2 76 1 . PHE 3 3 76 1 . GLU 4 4 76 1 . ARG 5 5 76 1 . CYS 6 6 76 1 . GLU 7 7 76 1 . LEU 8 8 76 1 . ALA 9 9 76 1 . ARG 10 10 76 1 . THR 11 11 76 1 . LEU 12 12 76 1 . LYS 13 13 76 1 . ARG 14 14 76 1 . LEU 15 15 76 1 . GLY 16 16 76 1 . MET 17 17 76 1 . ASP 18 18 76 1 . GLY 19 19 76 1 . TYR 20 20 76 1 . ARG 21 21 76 1 . GLY 22 22 76 1 . ILE 23 23 76 1 . SER 24 24 76 1 . LEU 25 25 76 1 . ALA 26 26 76 1 . ASN 27 27 76 1 . TRP 28 28 76 1 . MET 29 29 76 1 . CYS 30 30 76 1 . LEU 31 31 76 1 . ALA 32 32 76 1 . LYS 33 33 76 1 . TRP 34 34 76 1 . GLU 35 35 76 1 . SER 36 36 76 1 . GLY 37 37 76 1 . TYR 38 38 76 1 . ASN 39 39 76 1 . THR 40 40 76 1 . ARG 41 41 76 1 . ALA 42 42 76 1 . THR 43 43 76 1 . ASN 44 44 76 1 . TYR 45 45 76 1 . ASN 46 46 76 1 . ALA 47 47 76 1 . GLY 48 48 76 1 . ASP 49 49 76 1 . ARG 50 50 76 1 . SER 51 51 76 1 . THR 52 52 76 1 . ASP 53 53 76 1 . TYR 54 54 76 1 . GLY 55 55 76 1 . ILE 56 56 76 1 . PHE 57 57 76 1 . GLN 58 58 76 1 . ILE 59 59 76 1 . ASN 60 60 76 1 . SER 61 61 76 1 . ARG 62 62 76 1 . TYR 63 63 76 1 . TRP 64 64 76 1 . CYS 65 65 76 1 . ASN 66 66 76 1 . ASP 67 67 76 1 . GLY 68 68 76 1 . LYS 69 69 76 1 . THR 70 70 76 1 . PRO 71 71 76 1 . GLY 72 72 76 1 . ALA 73 73 76 1 . VAL 74 74 76 1 . ASN 75 75 76 1 . ALA 76 76 76 1 . CYS 77 77 76 1 . HIS 78 78 76 1 . LEU 79 79 76 1 . SER 80 80 76 1 . CYS 81 81 76 1 . SER 82 82 76 1 . ALA 83 83 76 1 . LEU 84 84 76 1 . LEU 85 85 76 1 . GLN 86 86 76 1 . ASP 87 87 76 1 . ASN 88 88 76 1 . ILE 89 89 76 1 . ALA 90 90 76 1 . ASP 91 91 76 1 . ALA 92 92 76 1 . VAL 93 93 76 1 . ALA 94 94 76 1 . CYS 95 95 76 1 . ALA 96 96 76 1 . LYS 97 97 76 1 . ARG 98 98 76 1 . VAL 99 99 76 1 . VAL 100 100 76 1 . ARG 101 101 76 1 . ASP 102 102 76 1 . PRO 103 103 76 1 . GLN 104 104 76 1 . GLY 105 105 76 1 . ILE 106 106 76 1 . ARG 107 107 76 1 . ALA 108 108 76 1 . TRP 109 109 76 1 . VAL 110 110 76 1 . ALA 111 111 76 1 . TRP 112 112 76 1 . ARG 113 113 76 1 . ASN 114 114 76 1 . ARG 115 115 76 1 . CYS 116 116 76 1 . GLN 117 117 76 1 . ASN 118 118 76 1 . ARG 119 119 76 1 . ASP 120 120 76 1 . VAL 121 121 76 1 . ARG 122 122 76 1 . GLN 123 123 76 1 . TYR 124 124 76 1 . VAL 125 125 76 1 . GLN 126 126 76 1 . GLY 127 127 76 1 . CYS 128 128 76 1 . GLY 129 129 76 1 . LEU 130 130 76 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 76 _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 generic . . . . . . . . . . . milk . . . . . . . . 76 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 76 _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' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 76 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 76 _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 76 _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 5.3 . na 76 1 temperature 330 . K 76 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 76 _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 76 _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' . . 76 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 76 _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 . . . . . . . . . . . . . . . . 76 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 76 _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 . DSS . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 76 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 76 _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 . 76 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 3 3 PHE HD1 H 1 7.035 . . 1 . . . . . . . . 76 1 2 . 1 1 3 3 PHE HD2 H 1 7.035 . . 1 . . . . . . . . 76 1 3 . 1 1 3 3 PHE HE1 H 1 7.244 . . 1 . . . . . . . . 76 1 4 . 1 1 3 3 PHE HE2 H 1 7.244 . . 1 . . . . . . . . 76 1 5 . 1 1 3 3 PHE HZ H 1 7.461 . . 1 . . . . . . . . 76 1 6 . 1 1 8 8 LEU HB2 H 1 1.23 . . 1 . . . . . . . . 76 1 7 . 1 1 8 8 LEU HB3 H 1 1.23 . . 1 . . . . . . . . 76 1 8 . 1 1 8 8 LEU HD11 H 1 .249 . . 2 . . . . . . . . 76 1 9 . 1 1 8 8 LEU HD12 H 1 .249 . . 2 . . . . . . . . 76 1 10 . 1 1 8 8 LEU HD13 H 1 .249 . . 2 . . . . . . . . 76 1 11 . 1 1 8 8 LEU HD21 H 1 .369 . . 2 . . . . . . . . 76 1 12 . 1 1 8 8 LEU HD22 H 1 .369 . . 2 . . . . . . . . 76 1 13 . 1 1 8 8 LEU HD23 H 1 .369 . . 2 . . . . . . . . 76 1 14 . 1 1 11 11 THR HA H 1 3.89 . . 1 . . . . . . . . 76 1 15 . 1 1 11 11 THR HB H 1 4.27 . . 1 . . . . . . . . 76 1 16 . 1 1 11 11 THR HG21 H 1 1.179 . . 1 . . . . . . . . 76 1 17 . 1 1 11 11 THR HG22 H 1 1.179 . . 1 . . . . . . . . 76 1 18 . 1 1 11 11 THR HG23 H 1 1.179 . . 1 . . . . . . . . 76 1 19 . 1 1 12 12 LEU HB2 H 1 1.69 . . 1 . . . . . . . . 76 1 20 . 1 1 12 12 LEU HB3 H 1 1.69 . . 1 . . . . . . . . 76 1 21 . 1 1 12 12 LEU HD11 H 1 .512 . . 2 . . . . . . . . 76 1 22 . 1 1 12 12 LEU HD12 H 1 .512 . . 2 . . . . . . . . 76 1 23 . 1 1 12 12 LEU HD13 H 1 .512 . . 2 . . . . . . . . 76 1 24 . 1 1 12 12 LEU HD21 H 1 .619 . . 2 . . . . . . . . 76 1 25 . 1 1 12 12 LEU HD22 H 1 .619 . . 2 . . . . . . . . 76 1 26 . 1 1 12 12 LEU HD23 H 1 .619 . . 2 . . . . . . . . 76 1 27 . 1 1 17 17 MET HE1 H 1 .04 . . 1 . . . . . . . . 76 1 28 . 1 1 17 17 MET HE2 H 1 .04 . . 1 . . . . . . . . 76 1 29 . 1 1 17 17 MET HE3 H 1 .04 . . 1 . . . . . . . . 76 1 30 . 1 1 20 20 TYR HD1 H 1 7.174 . . 1 . . . . . . . . 76 1 31 . 1 1 20 20 TYR HD2 H 1 7.174 . . 1 . . . . . . . . 76 1 32 . 1 1 20 20 TYR HE1 H 1 6.994 . . 1 . . . . . . . . 76 1 33 . 1 1 20 20 TYR HE2 H 1 6.994 . . 1 . . . . . . . . 76 1 34 . 1 1 23 23 ILE HA H 1 3.88 . . 1 . . . . . . . . 76 1 35 . 1 1 23 23 ILE HB H 1 2.05 . . 1 . . . . . . . . 76 1 36 . 1 1 23 23 ILE HG21 H 1 -.236 . . 1 . . . . . . . . 76 1 37 . 1 1 23 23 ILE HG22 H 1 -.236 . . 1 . . . . . . . . 76 1 38 . 1 1 23 23 ILE HG23 H 1 -.236 . . 1 . . . . . . . . 76 1 39 . 1 1 23 23 ILE HD11 H 1 .58 . . 1 . . . . . . . . 76 1 40 . 1 1 23 23 ILE HD12 H 1 .58 . . 1 . . . . . . . . 76 1 41 . 1 1 23 23 ILE HD13 H 1 .58 . . 1 . . . . . . . . 76 1 42 . 1 1 28 28 TRP HD1 H 1 6.883 . . 1 . . . . . . . . 76 1 43 . 1 1 28 28 TRP HE1 H 1 9.16 . . 1 . . . . . . . . 76 1 44 . 1 1 28 28 TRP HE3 H 1 6.911 . . 1 . . . . . . . . 76 1 45 . 1 1 28 28 TRP HZ2 H 1 7.208 . . 1 . . . . . . . . 76 1 46 . 1 1 28 28 TRP HZ3 H 1 6.056 . . 1 . . . . . . . . 76 1 47 . 1 1 28 28 TRP HH2 H 1 6.825 . . 1 . . . . . . . . 76 1 48 . 1 1 29 29 MET HE1 H 1 2.09 . . 1 . . . . . . . . 76 1 49 . 1 1 29 29 MET HE2 H 1 2.09 . . 1 . . . . . . . . 76 1 50 . 1 1 29 29 MET HE3 H 1 2.09 . . 1 . . . . . . . . 76 1 51 . 1 1 31 31 LEU HB2 H 1 1.13 . . 1 . . . . . . . . 76 1 52 . 1 1 31 31 LEU HB3 H 1 1.13 . . 1 . . . . . . . . 76 1 53 . 1 1 31 31 LEU HD11 H 1 .041 . . 2 . . . . . . . . 76 1 54 . 1 1 31 31 LEU HD12 H 1 .041 . . 2 . . . . . . . . 76 1 55 . 1 1 31 31 LEU HD13 H 1 .041 . . 2 . . . . . . . . 76 1 56 . 1 1 31 31 LEU HD21 H 1 .434 . . 2 . . . . . . . . 76 1 57 . 1 1 31 31 LEU HD22 H 1 .434 . . 2 . . . . . . . . 76 1 58 . 1 1 31 31 LEU HD23 H 1 .434 . . 2 . . . . . . . . 76 1 59 . 1 1 32 32 ALA HA H 1 4.11 . . 1 . . . . . . . . 76 1 60 . 1 1 32 32 ALA HB1 H 1 1.39 . . 1 . . . . . . . . 76 1 61 . 1 1 32 32 ALA HB2 H 1 1.39 . . 1 . . . . . . . . 76 1 62 . 1 1 32 32 ALA HB3 H 1 1.39 . . 1 . . . . . . . . 76 1 63 . 1 1 34 34 TRP HD1 H 1 7.784 . . 1 . . . . . . . . 76 1 64 . 1 1 34 34 TRP HE1 H 1 9.72 . . 1 . . . . . . . . 76 1 65 . 1 1 34 34 TRP HE3 H 1 7.719 . . 1 . . . . . . . . 76 1 66 . 1 1 34 34 TRP HZ2 H 1 7.583 . . 1 . . . . . . . . 76 1 67 . 1 1 34 34 TRP HZ3 H 1 7.168 . . 1 . . . . . . . . 76 1 68 . 1 1 34 34 TRP HH2 H 1 7.256 . . 1 . . . . . . . . 76 1 69 . 1 1 38 38 TYR HD1 H 1 6.769 . . 1 . . . . . . . . 76 1 70 . 1 1 38 38 TYR HD2 H 1 6.769 . . 1 . . . . . . . . 76 1 71 . 1 1 38 38 TYR HE1 H 1 6.726 . . 1 . . . . . . . . 76 1 72 . 1 1 38 38 TYR HE2 H 1 6.726 . . 1 . . . . . . . . 76 1 73 . 1 1 40 40 THR HB H 1 4.47 . . 1 . . . . . . . . 76 1 74 . 1 1 40 40 THR HG21 H 1 1.55 . . 1 . . . . . . . . 76 1 75 . 1 1 40 40 THR HG22 H 1 1.55 . . 1 . . . . . . . . 76 1 76 . 1 1 40 40 THR HG23 H 1 1.55 . . 1 . . . . . . . . 76 1 77 . 1 1 43 43 THR HA H 1 5.28 . . 1 . . . . . . . . 76 1 78 . 1 1 43 43 THR HB H 1 3.8 . . 1 . . . . . . . . 76 1 79 . 1 1 43 43 THR HG21 H 1 1.124 . . 1 . . . . . . . . 76 1 80 . 1 1 43 43 THR HG22 H 1 1.124 . . 1 . . . . . . . . 76 1 81 . 1 1 43 43 THR HG23 H 1 1.124 . . 1 . . . . . . . . 76 1 82 . 1 1 45 45 TYR HD1 H 1 7.162 . . 1 . . . . . . . . 76 1 83 . 1 1 45 45 TYR HD2 H 1 7.162 . . 1 . . . . . . . . 76 1 84 . 1 1 45 45 TYR HE1 H 1 6.587 . . 1 . . . . . . . . 76 1 85 . 1 1 45 45 TYR HE2 H 1 6.587 . . 1 . . . . . . . . 76 1 86 . 1 1 47 47 ALA HA H 1 3.7 . . 1 . . . . . . . . 76 1 87 . 1 1 47 47 ALA HB1 H 1 1.456 . . 1 . . . . . . . . 76 1 88 . 1 1 47 47 ALA HB2 H 1 1.456 . . 1 . . . . . . . . 76 1 89 . 1 1 47 47 ALA HB3 H 1 1.456 . . 1 . . . . . . . . 76 1 90 . 1 1 52 52 THR HA H 1 5.09 . . 1 . . . . . . . . 76 1 91 . 1 1 52 52 THR HB H 1 3.87 . . 1 . . . . . . . . 76 1 92 . 1 1 52 52 THR HG21 H 1 .411 . . 1 . . . . . . . . 76 1 93 . 1 1 52 52 THR HG22 H 1 .411 . . 1 . . . . . . . . 76 1 94 . 1 1 52 52 THR HG23 H 1 .411 . . 1 . . . . . . . . 76 1 95 . 1 1 54 54 TYR HD1 H 1 7.162 . . 1 . . . . . . . . 76 1 96 . 1 1 54 54 TYR HD2 H 1 7.162 . . 1 . . . . . . . . 76 1 97 . 1 1 54 54 TYR HE1 H 1 6.87 . . 1 . . . . . . . . 76 1 98 . 1 1 54 54 TYR HE2 H 1 6.87 . . 1 . . . . . . . . 76 1 99 . 1 1 56 56 ILE HB H 1 1.26 . . 1 . . . . . . . . 76 1 100 . 1 1 56 56 ILE HG12 H 1 .58 . . 2 . . . . . . . . 76 1 101 . 1 1 56 56 ILE HG13 H 1 1.2 . . 2 . . . . . . . . 76 1 102 . 1 1 56 56 ILE HG21 H 1 .06 . . 1 . . . . . . . . 76 1 103 . 1 1 56 56 ILE HG22 H 1 .06 . . 1 . . . . . . . . 76 1 104 . 1 1 56 56 ILE HG23 H 1 .06 . . 1 . . . . . . . . 76 1 105 . 1 1 56 56 ILE HD11 H 1 .418 . . 1 . . . . . . . . 76 1 106 . 1 1 56 56 ILE HD12 H 1 .418 . . 1 . . . . . . . . 76 1 107 . 1 1 56 56 ILE HD13 H 1 .418 . . 1 . . . . . . . . 76 1 108 . 1 1 57 57 PHE HD1 H 1 6.877 . . 1 . . . . . . . . 76 1 109 . 1 1 57 57 PHE HD2 H 1 6.877 . . 1 . . . . . . . . 76 1 110 . 1 1 57 57 PHE HE1 H 1 6.902 . . 1 . . . . . . . . 76 1 111 . 1 1 57 57 PHE HE2 H 1 6.902 . . 1 . . . . . . . . 76 1 112 . 1 1 57 57 PHE HZ H 1 6.653 . . 1 . . . . . . . . 76 1 113 . 1 1 59 59 ILE HA H 1 4.37 . . 1 . . . . . . . . 76 1 114 . 1 1 59 59 ILE HB H 1 1.97 . . 1 . . . . . . . . 76 1 115 . 1 1 59 59 ILE HG21 H 1 1.098 . . 1 . . . . . . . . 76 1 116 . 1 1 59 59 ILE HG22 H 1 1.098 . . 1 . . . . . . . . 76 1 117 . 1 1 59 59 ILE HG23 H 1 1.098 . . 1 . . . . . . . . 76 1 118 . 1 1 63 63 TYR HD1 H 1 6.527 . . 1 . . . . . . . . 76 1 119 . 1 1 63 63 TYR HD2 H 1 6.527 . . 1 . . . . . . . . 76 1 120 . 1 1 63 63 TYR HE1 H 1 6.69 . . 1 . . . . . . . . 76 1 121 . 1 1 63 63 TYR HE2 H 1 6.69 . . 1 . . . . . . . . 76 1 122 . 1 1 64 64 TRP HD1 H 1 7.677 . . 1 . . . . . . . . 76 1 123 . 1 1 64 64 TRP HE1 H 1 10.27 . . 1 . . . . . . . . 76 1 124 . 1 1 64 64 TRP HE3 H 1 7.617 . . 1 . . . . . . . . 76 1 125 . 1 1 64 64 TRP HZ2 H 1 7.303 . . 1 . . . . . . . . 76 1 126 . 1 1 64 64 TRP HZ3 H 1 6.716 . . 1 . . . . . . . . 76 1 127 . 1 1 64 64 TRP HH2 H 1 7.221 . . 1 . . . . . . . . 76 1 128 . 1 1 70 70 THR HA H 1 4.83 . . 1 . . . . . . . . 76 1 129 . 1 1 70 70 THR HB H 1 4.19 . . 1 . . . . . . . . 76 1 130 . 1 1 70 70 THR HG21 H 1 1.074 . . 1 . . . . . . . . 76 1 131 . 1 1 70 70 THR HG22 H 1 1.074 . . 1 . . . . . . . . 76 1 132 . 1 1 70 70 THR HG23 H 1 1.074 . . 1 . . . . . . . . 76 1 133 . 1 1 74 74 VAL HA H 1 3.88 . . 1 . . . . . . . . 76 1 134 . 1 1 74 74 VAL HB H 1 2 . . 1 . . . . . . . . 76 1 135 . 1 1 76 76 ALA HA H 1 4.08 . . 1 . . . . . . . . 76 1 136 . 1 1 76 76 ALA HB1 H 1 1.468 . . 1 . . . . . . . . 76 1 137 . 1 1 76 76 ALA HB2 H 1 1.468 . . 1 . . . . . . . . 76 1 138 . 1 1 76 76 ALA HB3 H 1 1.468 . . 1 . . . . . . . . 76 1 139 . 1 1 78 78 HIS HD2 H 1 7.273 . . 1 . . . . . . . . 76 1 140 . 1 1 78 78 HIS HE1 H 1 8.56 . . 1 . . . . . . . . 76 1 141 . 1 1 89 89 ILE HB H 1 2.14 . . 1 . . . . . . . . 76 1 142 . 1 1 89 89 ILE HG12 H 1 1.29 . . 2 . . . . . . . . 76 1 143 . 1 1 89 89 ILE HG13 H 1 .99 . . 2 . . . . . . . . 76 1 144 . 1 1 89 89 ILE HG21 H 1 .994 . . 1 . . . . . . . . 76 1 145 . 1 1 89 89 ILE HG22 H 1 .994 . . 1 . . . . . . . . 76 1 146 . 1 1 89 89 ILE HG23 H 1 .994 . . 1 . . . . . . . . 76 1 147 . 1 1 89 89 ILE HD11 H 1 .294 . . 1 . . . . . . . . 76 1 148 . 1 1 89 89 ILE HD12 H 1 .294 . . 1 . . . . . . . . 76 1 149 . 1 1 89 89 ILE HD13 H 1 .294 . . 1 . . . . . . . . 76 1 150 . 1 1 93 93 VAL HA H 1 3.28 . . 1 . . . . . . . . 76 1 151 . 1 1 93 93 VAL HB H 1 2.21 . . 1 . . . . . . . . 76 1 152 . 1 1 96 96 ALA HA H 1 3.83 . . 1 . . . . . . . . 76 1 153 . 1 1 96 96 ALA HB1 H 1 .886 . . 1 . . . . . . . . 76 1 154 . 1 1 96 96 ALA HB2 H 1 .886 . . 1 . . . . . . . . 76 1 155 . 1 1 96 96 ALA HB3 H 1 .886 . . 1 . . . . . . . . 76 1 156 . 1 1 99 99 VAL HA H 1 2.491 . . 1 . . . . . . . . 76 1 157 . 1 1 99 99 VAL HB H 1 1.91 . . 1 . . . . . . . . 76 1 158 . 1 1 100 100 VAL HA H 1 3.655 . . 1 . . . . . . . . 76 1 159 . 1 1 100 100 VAL HB H 1 2.22 . . 1 . . . . . . . . 76 1 160 . 1 1 106 106 ILE HB H 1 .95 . . 1 . . . . . . . . 76 1 161 . 1 1 106 106 ILE HG12 H 1 .21 . . 2 . . . . . . . . 76 1 162 . 1 1 106 106 ILE HG13 H 1 .86 . . 2 . . . . . . . . 76 1 163 . 1 1 106 106 ILE HG21 H 1 -.542 . . 1 . . . . . . . . 76 1 164 . 1 1 106 106 ILE HG22 H 1 -.542 . . 1 . . . . . . . . 76 1 165 . 1 1 106 106 ILE HG23 H 1 -.542 . . 1 . . . . . . . . 76 1 166 . 1 1 106 106 ILE HD11 H 1 -.415 . . 1 . . . . . . . . 76 1 167 . 1 1 106 106 ILE HD12 H 1 -.415 . . 1 . . . . . . . . 76 1 168 . 1 1 106 106 ILE HD13 H 1 -.415 . . 1 . . . . . . . . 76 1 169 . 1 1 109 109 TRP HD1 H 1 7.348 . . 1 . . . . . . . . 76 1 170 . 1 1 109 109 TRP HE1 H 1 9.9 . . 1 . . . . . . . . 76 1 171 . 1 1 109 109 TRP HE3 H 1 7.84 . . 1 . . . . . . . . 76 1 172 . 1 1 109 109 TRP HZ2 H 1 6.994 . . 1 . . . . . . . . 76 1 173 . 1 1 109 109 TRP HZ3 H 1 6.61 . . 1 . . . . . . . . 76 1 174 . 1 1 109 109 TRP HH2 H 1 6.86 . . 1 . . . . . . . . 76 1 175 . 1 1 112 112 TRP HD1 H 1 6.933 . . 1 . . . . . . . . 76 1 176 . 1 1 112 112 TRP HE1 H 1 9.82 . . 1 . . . . . . . . 76 1 177 . 1 1 112 112 TRP HZ2 H 1 7.294 . . 1 . . . . . . . . 76 1 178 . 1 1 112 112 TRP HZ3 H 1 6.875 . . 1 . . . . . . . . 76 1 179 . 1 1 112 112 TRP HH2 H 1 7.141 . . 1 . . . . . . . . 76 1 180 . 1 1 124 124 TYR HD1 H 1 7.488 . . 1 . . . . . . . . 76 1 181 . 1 1 124 124 TYR HD2 H 1 7.488 . . 1 . . . . . . . . 76 1 182 . 1 1 124 124 TYR HE1 H 1 6.889 . . 1 . . . . . . . . 76 1 183 . 1 1 124 124 TYR HE2 H 1 6.889 . . 1 . . . . . . . . 76 1 stop_ save_