data_5130 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5130 _Entry.Title ; Assignment of 1H, 13C and 15N resonances of Human Lysozyme at 35 C ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-09-06 _Entry.Accession_date 2001-09-06 _Entry.Last_release_date 2001-09-06 _Entry.Original_release_date 2001-09-06 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.0.16 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Source_data_format . _Entry.Source_data_format_version . _Entry.Generated_software_name . _Entry.Generated_software_version . _Entry.Generated_software_ID . _Entry.Generated_software_label . _Entry.Generated_date . _Entry.DOI . _Entry.UUID . _Entry.Related_coordinate_file_name . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.ORCID _Entry_author.Entry_ID 1 Hiroyuki Kumeta . . . . 5130 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5130 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 248 5130 '15N chemical shifts' 127 5130 '1H chemical shifts' 732 5130 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2001-11-12 . original BMRB . 5130 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 5142 'human lysozyme at 4 C' 5130 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5130 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Assignment of 1H, 13C and 15N resonances of Human Lysozyme at 35 and 4 degree C ; _Citation.Status 'in preparation' _Citation.Type 'BMRB only' _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Hiroyuki Kumeta . . . . 5130 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'human lysozyme' 5130 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_human_lysozyme _Assembly.Sf_category assembly _Assembly.Sf_framecode system_human_lysozyme _Assembly.Entry_ID 5130 _Assembly.ID 1 _Assembly.Name 'human lysozyme at 35 degree C' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all disulfide bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number 3.2.1.17 _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5130 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'human lysozyme' 1 $human_lysozyme . . . native . . . . . 5130 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_asym_ID_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_asym_ID_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 6 6 SG . 1 . 1 CYS 128 128 SG . . . . . . . . . . . . 5130 1 2 disulfide single . 1 . 1 CYS 30 30 SG . 1 . 1 CYS 116 116 SG . . . . . . . . . . . . 5130 1 3 disulfide single . 1 . 1 CYS 65 65 SG . 1 . 1 CYS 81 81 SG . . . . . . . . . . . . 5130 1 4 disulfide single . 1 . 1 CYS 77 77 SG . 1 . 1 CYS 95 95 SG . . . . . . . . . . . . 5130 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'human lysozyme' abbreviation 5130 1 'human lysozyme at 35 degree C' system 5130 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_human_lysozyme _Entity.Sf_category entity _Entity.Sf_framecode human_lysozyme _Entity.Entry_ID 5130 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'human 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 . _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 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID . no BMRB 2542 . lysozyme . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no BMRB 5123 . lysozyme . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no BMRB 5124 . lysozyme . . . . . 100.00 130 99.23 99.23 5.75e-70 . . . . 5130 1 . no BMRB 5125 . lysozyme . . . . . 100.00 130 99.23 99.23 8.58e-70 . . . . 5130 1 . no BMRB 5142 . 'human lysozyme' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no BMRB 76 . lysozyme . . . . . 100.00 130 99.23 100.00 3.75e-70 . . . . 5130 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 5.24e-70 . . . . 5130 1 . 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 5.42e-70 . . . . 5130 1 . no PDB 1B5U . ; Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutant ; . . . . . 100.00 130 99.23 100.00 4.08e-70 . . . . 5130 1 . no PDB 1B5V . ; Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants ; . . . . . 100.00 130 99.23 100.00 4.08e-70 . . . . 5130 1 . no PDB 1B5W . ; Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants ; . . . . . 100.00 130 99.23 100.00 4.08e-70 . . . . 5130 1 . no PDB 1B5X . ; Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants ; . . . . . 100.00 130 99.23 100.00 4.08e-70 . . . . 5130 1 . no PDB 1B5Y . ; Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants ; . . . . . 100.00 130 99.23 100.00 4.08e-70 . . . . 5130 1 . no PDB 1B5Z . ; Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme: Calorimetry And X-Ray Analysis Of Six Ser->ala Mutants ; . . . . . 100.00 130 99.23 100.00 4.08e-70 . . . . 5130 1 . no PDB 1B7L . 'Verification Of Spmp Using Mutant Human Lysozymes' . . . . . 100.00 130 99.23 99.23 6.85e-70 . . . . 5130 1 . no PDB 1B7M . 'Verification Of Spmp Using Mutant Human Lysozymes' . . . . . 100.00 130 99.23 99.23 6.04e-70 . . . . 5130 1 . no PDB 1B7N . 'Verification Of Spmp Using Mutant Human Lysozymes' . . . . . 100.00 130 99.23 99.23 1.43e-69 . . . . 5130 1 . no PDB 1B7O . 'Verification Of Spmp Using Mutant Human Lysozymes' . . . . . 100.00 130 99.23 99.23 1.02e-69 . . . . 5130 1 . no PDB 1B7P . 'Verification Of Spmp Using Mutant Human Lysozymes' . . . . . 100.00 130 99.23 99.23 2.78e-69 . . . . 5130 1 . no PDB 1B7Q . 'Verification Of Spmp Using Mutant Human Lysozymes' . . . . . 100.00 130 99.23 99.23 1.53e-69 . . . . 5130 1 . no PDB 1B7R . 'Verification Of Spmp Using Mutant Human Lysozymes' . . . . . 100.00 130 99.23 99.23 1.37e-69 . . . . 5130 1 . no PDB 1B7S . 'Verification Of Spmp Using Mutant Human Lysozymes' . . . . . 100.00 130 99.23 99.23 6.73e-70 . . . . 5130 1 . no PDB 1BB3 . 'Human Lysozyme Mutant A96l' . . . . . 100.00 130 99.23 99.23 6.85e-70 . . . . 5130 1 . no PDB 1BB4 . 'Human Lysozyme Double Mutant A96l, W109h' . . . . . 100.00 130 98.46 98.46 5.03e-69 . . . . 5130 1 . no PDB 1BB5 . 'Human Lysozyme Mutant A96l Complexed With Chitotriose' . . . . . 100.00 130 99.23 99.23 6.85e-70 . . . . 5130 1 . no PDB 1C43 . 'Mutant Human Lysozyme With Foreign N-Terminal Residues' . . . . . 99.23 130 100.00 100.00 6.19e-70 . . . . 5130 1 . no PDB 1C45 . 'Mutant Human Lysozyme With Foreign N-Terminal Residues' . . . . . 99.23 130 100.00 100.00 6.41e-70 . . . . 5130 1 . no PDB 1C46 . 'Mutant Human Lysozyme With Foreign N-Terminal Residues' . . . . . 100.00 131 100.00 100.00 1.76e-70 . . . . 5130 1 . 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 1.11e-70 . . . . 5130 1 . no PDB 1CJ6 . 'T11a Mutant Human Lysozyme' . . . . . 100.00 130 99.23 99.23 6.57e-70 . . . . 5130 1 . no PDB 1CJ7 . 'T11v Mutant Human Lysozyme' . . . . . 100.00 130 99.23 99.23 6.09e-70 . . . . 5130 1 . no PDB 1CJ8 . 'T40a Mutant Human Lysozyme' . . . . . 100.00 130 99.23 99.23 6.57e-70 . . . . 5130 1 . no PDB 1CJ9 . 'T40v Mutant Human Lysozyme' . . . . . 100.00 130 99.23 99.23 6.09e-70 . . . . 5130 1 . no PDB 1CKC . 'T43a Mutant Human Lysozyme' . . . . . 100.00 130 99.23 99.23 6.57e-70 . . . . 5130 1 . no PDB 1CKD . 'T43v Mutant Human Lysozyme' . . . . . 100.00 130 99.23 99.23 6.09e-70 . . . . 5130 1 . no PDB 1CKF . 'T52a Mutant Human Lysozyme' . . . . . 100.00 130 99.23 99.23 6.57e-70 . . . . 5130 1 . no PDB 1CKG . 'T52v Mutant Human Lysozyme' . . . . . 100.00 130 99.23 99.23 6.09e-70 . . . . 5130 1 . no PDB 1CKH . 'T70v Mutant Human Lysozyme' . . . . . 100.00 130 99.23 99.23 6.09e-70 . . . . 5130 1 . no PDB 1D6P . "Human Lysozyme L63 Mutant Labelled With 2',3'-Epoxypropyl N, N'-Diacetylchitobiose" . . . . . 100.00 130 99.23 99.23 1.14e-69 . . . . 5130 1 . no PDB 1D6Q . "Human Lysozyme E102 Mutant Labelled With 2',3'-Epoxypropyl Glycoside Of N-Acetyllactosamine" . . . . . 100.00 130 99.23 100.00 4.29e-70 . . . . 5130 1 . 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 1.22e-69 . . . . 5130 1 . 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 6.63e-68 . . . . 5130 1 . 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 1.38e-68 . . . . 5130 1 . no PDB 1EQ4 . 'Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme' . . . . . 100.00 130 99.23 100.00 4.47e-70 . . . . 5130 1 . no PDB 1EQ5 . 'Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme' . . . . . 100.00 130 99.23 100.00 5.84e-70 . . . . 5130 1 . no PDB 1EQE . 'Crystal Structures Of Salt Bridge Mutants Of Human Lysozyme' . . . . . 100.00 130 99.23 100.00 5.84e-70 . . . . 5130 1 . no PDB 1GAY . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 1.22e-69 . . . . 5130 1 . no PDB 1GAZ . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 100.00 2.35e-70 . . . . 5130 1 . no PDB 1GB0 . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 100.00 3.75e-70 . . . . 5130 1 . no PDB 1GB2 . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 100.00 3.51e-70 . . . . 5130 1 . no PDB 1GB3 . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 5.47e-70 . . . . 5130 1 . no PDB 1GB5 . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 1.22e-69 . . . . 5130 1 . no PDB 1GB6 . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 100.00 2.35e-70 . . . . 5130 1 . no PDB 1GB7 . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 100.00 3.75e-70 . . . . 5130 1 . no PDB 1GB8 . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 100.00 3.51e-70 . . . . 5130 1 . no PDB 1GB9 . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 5.47e-70 . . . . 5130 1 . no PDB 1GBO . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 1.22e-69 . . . . 5130 1 . no PDB 1GBW . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 100.00 2.35e-70 . . . . 5130 1 . no PDB 1GBX . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 100.00 3.75e-70 . . . . 5130 1 . no PDB 1GBY . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 100.00 3.51e-70 . . . . 5130 1 . no PDB 1GBZ . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 5.47e-70 . . . . 5130 1 . no PDB 1GDW . 'Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions' . . . . . 100.00 130 99.23 99.23 1.22e-69 . . . . 5130 1 . no PDB 1GDX . 'Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions' . . . . . 100.00 130 99.23 99.23 8.58e-70 . . . . 5130 1 . no PDB 1GE0 . 'Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions' . . . . . 100.00 130 99.23 99.23 1.99e-69 . . . . 5130 1 . no PDB 1GE1 . 'Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions' . . . . . 100.00 130 99.23 99.23 8.23e-70 . . . . 5130 1 . no PDB 1GE2 . 'Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions' . . . . . 100.00 130 99.23 99.23 2.03e-69 . . . . 5130 1 . no PDB 1GE3 . 'Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions' . . . . . 100.00 130 99.23 99.23 8.79e-70 . . . . 5130 1 . no PDB 1GE4 . 'Crystal Structure Of Mutant Human Lysozyme Substituted At Left-Handed Helical Positions' . . . . . 100.00 130 99.23 99.23 1.05e-69 . . . . 5130 1 . no PDB 1GEV . 'Buried Polar Mutant Human Lysozyme' . . . . . 100.00 130 99.23 99.23 6.25e-70 . . . . 5130 1 . no PDB 1GEZ . 'Buried Polar Mutant Human Lysozyme' . . . . . 100.00 130 99.23 100.00 3.07e-70 . . . . 5130 1 . no PDB 1GF0 . 'Buried Polar Mutant Human Lysozyme' . . . . . 100.00 130 99.23 100.00 3.07e-70 . . . . 5130 1 . no PDB 1GF3 . 'Buried Polar Mutant Human Lysozyme' . . . . . 100.00 130 99.23 100.00 3.07e-70 . . . . 5130 1 . no PDB 1GF4 . 'Buried Polar Mutant Human Lysozyme' . . . . . 100.00 130 99.23 99.23 4.63e-70 . . . . 5130 1 . no PDB 1GF5 . 'Buried Polar Mutant Human Lysozyme' . . . . . 100.00 130 99.23 100.00 3.07e-70 . . . . 5130 1 . no PDB 1GF6 . 'Buried Polar Mutant Human Lysozyme' . . . . . 100.00 130 99.23 99.23 4.63e-70 . . . . 5130 1 . no PDB 1GF7 . 'Buried Polar Mutant Human Lysozyme' . . . . . 100.00 130 99.23 99.23 4.63e-70 . . . . 5130 1 . no PDB 1GF8 . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 6.73e-70 . . . . 5130 1 . no PDB 1GF9 . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 7.83e-70 . . . . 5130 1 . no PDB 1GFA . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 1.25e-69 . . . . 5130 1 . no PDB 1GFE . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 1.17e-69 . . . . 5130 1 . no PDB 1GFG . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 1.23e-69 . . . . 5130 1 . no PDB 1GFH . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 7.83e-70 . . . . 5130 1 . no PDB 1GFJ . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 1.25e-69 . . . . 5130 1 . no PDB 1GFK . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 1.17e-69 . . . . 5130 1 . no PDB 1GFR . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 1.23e-69 . . . . 5130 1 . no PDB 1GFT . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 7.83e-70 . . . . 5130 1 . no PDB 1GFU . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 1.25e-69 . . . . 5130 1 . no PDB 1GFV . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 1.17e-69 . . . . 5130 1 . 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 9.48e-70 . . . . 5130 1 . no PDB 1I1Z . 'Mutant Human Lysozyme (Q86d)' . . . . . 100.00 130 99.23 99.23 9.48e-70 . . . . 5130 1 . no PDB 1I20 . 'Mutant Human Lysozyme (A92d)' . . . . . 100.00 130 99.23 99.23 9.80e-70 . . . . 5130 1 . no PDB 1INU . 'Crystal Structure Of Mutant Human Lysozyme Substituted At The Surface Positions' . . . . . 100.00 130 99.23 99.23 1.23e-69 . . . . 5130 1 . no PDB 1IOC . 'Crystal Structure Of Mutant Human Lysozyme, Eaea-I56t' . . . . . 100.00 134 99.23 99.23 3.29e-70 . . . . 5130 1 . no PDB 1IP1 . 'G37a Human Lysozyme' . . . . . 100.00 130 99.23 99.23 5.99e-70 . . . . 5130 1 . no PDB 1IP2 . 'G48a Human Lysozyme' . . . . . 100.00 130 99.23 99.23 5.99e-70 . . . . 5130 1 . no PDB 1IP3 . 'G68a Human Lysozyme' . . . . . 100.00 130 99.23 99.23 5.99e-70 . . . . 5130 1 . no PDB 1IP4 . 'G72a Human Lysozyme' . . . . . 100.00 130 99.23 99.23 5.99e-70 . . . . 5130 1 . no PDB 1IP5 . 'G105a Human Lysozyme' . . . . . 100.00 130 99.23 99.23 5.99e-70 . . . . 5130 1 . no PDB 1IP6 . 'G127a Human Lysozyme' . . . . . 100.00 130 99.23 99.23 5.99e-70 . . . . 5130 1 . no PDB 1IP7 . 'G129a Human Lysozyme' . . . . . 100.00 130 99.23 99.23 5.99e-70 . . . . 5130 1 . no PDB 1IWT . 'Crystal Structure Analysis Of Human Lysozyme At 113k.' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1IWU . 'Crystal Structure Analysis Of Human Lysozyme At 127k.' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1IWV . 'Crystal Structure Analysis Of Human Lysozyme At 147k.' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1IWW . 'Crystal Structure Analysis Of Human Lysozyme At 152k.' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1IWX . 'Crystal Structure Analysis Of Human Lysozyme At 161k.' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1IWY . 'Crystal Structure Analysis Of Human Lysozyme At 170k.' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1IWZ . 'Crystal Structure Analysis Of Human Lysozyme At 178k.' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1IY3 . 'Solution Structure Of The Human Lysozyme At 4 Degree C' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1IY4 . 'Solution Structure Of The Human Lysozyme At 35 Degree C' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1JKA . 'Human Lysozyme Mutant With Glu 35 Replaced By Asp' . . . . . 100.00 130 99.23 100.00 5.79e-70 . . . . 5130 1 . no PDB 1JKB . 'Human Lysozyme Mutant With Glu 35 Replaced By Ala' . . . . . 100.00 130 99.23 99.23 8.44e-70 . . . . 5130 1 . no PDB 1JKC . 'Human Lysozyme Mutant With Trp 109 Replaced By Phe' . . . . . 100.00 130 99.23 100.00 5.79e-70 . . . . 5130 1 . no PDB 1JKD . 'Human Lysozyme Mutant With Trp 109 Replaced By Ala' . . . . . 100.00 130 99.23 99.23 1.69e-69 . . . . 5130 1 . no PDB 1JSF . 'Full-Matrix Least-Squares Refinement Of Human Lysozyme' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1JWR . 'Crystal Structure Of Human Lysozyme At 100 K' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1LAA . 'X-Ray Structure Of Glu 53 Human Lysozyme' . . . . . 100.00 130 99.23 100.00 4.29e-70 . . . . 5130 1 . no PDB 1LHH . ; Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of Proline Mutants ; . . . . . 100.00 130 99.23 99.23 7.51e-70 . . . . 5130 1 . no PDB 1LHI . ; Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of Proline Mutants ; . . . . . 100.00 130 99.23 99.23 2.41e-69 . . . . 5130 1 . no PDB 1LHJ . ; Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of Proline Mutants ; . . . . . 100.00 130 99.23 99.23 2.41e-69 . . . . 5130 1 . no PDB 1LHK . ; Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of Proline Mutants ; . . . . . 100.00 130 99.23 99.23 9.32e-70 . . . . 5130 1 . no PDB 1LHL . ; Role Of Proline Residues In Human Lysozyme Stability: A Scanning Calorimetric Study Combined With X-Ray Structure Analysis Of Proline Mutants ; . . . . . 100.00 130 99.23 99.23 5.60e-70 . . . . 5130 1 . 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 4.15e-69 . . . . 5130 1 . no PDB 1LOZ . 'Amyloidogenic Variant (I56t) Variant Of Human Lysozyme' . . . . . 100.00 130 99.23 99.23 5.75e-70 . . . . 5130 1 . no PDB 1LYY . 'Amyloidogenic Variant (Asp67his) Of Human Lysozyme' . . . . . 100.00 130 99.23 99.23 8.58e-70 . . . . 5130 1 . 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 1.85e-70 . . . . 5130 1 . 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 9.48e-70 . . . . 5130 1 . no PDB 1LZR . ; Structural Changes Of The Active Site Cleft And Different saccharide Binding Modes In Human Lysozyme Co-Crystallized With Hexa-N-Acetyl-Chitohexaose At Ph 4.0 ; . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1LZS . ; Structural Changes Of The Active Site Cleft And Different saccharide Binding Modes In Human Lysozyme Co-Crystallized With Hexa-N-Acetyl-Chitohexaose At Ph 4.0 ; . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1OP9 . 'Complex Of Human Lysozyme With Camelid Vhh Hl6 Antibody Fragment' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . 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 5.75e-70 . . . . 5130 1 . 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 5.33e-70 . . . . 5130 1 . 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 5.33e-70 . . . . 5130 1 . 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 5.33e-70 . . . . 5130 1 . 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 5.33e-70 . . . . 5130 1 . 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 5.33e-70 . . . . 5130 1 . 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 5.33e-70 . . . . 5130 1 . 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 5.33e-70 . . . . 5130 1 . 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 5.33e-70 . . . . 5130 1 . 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 5.33e-70 . . . . 5130 1 . no PDB 1QSW . 'Crystal Structure Analysis Of A Human Lysozyme Mutant W64c C65a' . . . . . 100.00 130 98.46 98.46 1.74e-68 . . . . 5130 1 . no PDB 1RE2 . "Human Lysozyme Labelled With Two 2',3'-Epoxypropyl Beta- Glycoside Of N-Acetyllactosamine" . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1REM . 'Human Lysozyme With Man-B1,4-Glcnac Covalently Attached To Asp53' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1REX . 'Native Human Lysozyme' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1REY . "Human Lysozyme-N,N'-Diacetylchitobiose Complex" . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no PDB 1REZ . 'Human Lysozyme-N-Acetyllactosamine Complex' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . 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 1.31e-69 . . . . 5130 1 . 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 1.14e-69 . . . . 5130 1 . 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 3.72e-70 . . . . 5130 1 . 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 8.51e-70 . . . . 5130 1 . 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 4.29e-70 . . . . 5130 1 . no PDB 1W08 . 'Structure Of T70n Human Lysozyme' . . . . . 100.00 130 99.23 99.23 6.73e-70 . . . . 5130 1 . no PDB 1WQM . 'Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme' . . . . . 100.00 130 99.23 100.00 3.72e-70 . . . . 5130 1 . no PDB 1WQN . 'Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme' . . . . . 100.00 130 99.23 100.00 3.72e-70 . . . . 5130 1 . no PDB 1WQO . 'Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme' . . . . . 100.00 130 99.23 100.00 3.72e-70 . . . . 5130 1 . no PDB 1WQP . 'Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme' . . . . . 100.00 130 99.23 100.00 3.72e-70 . . . . 5130 1 . no PDB 1WQQ . 'Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme' . . . . . 100.00 130 99.23 100.00 3.72e-70 . . . . 5130 1 . no PDB 1WQR . 'Contribution Of Hydrogen Bonds To The Conformational Stability Of Human Lysozyme' . . . . . 100.00 130 99.23 100.00 3.72e-70 . . . . 5130 1 . no PDB 1YAM . ; Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of The Five Isoleucine To Valine Mutants ; . . . . . 100.00 130 99.23 100.00 2.62e-70 . . . . 5130 1 . no PDB 1YAN . ; Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of The Five Isoleucine To Valine Mutants ; . . . . . 100.00 130 99.23 100.00 2.62e-70 . . . . 5130 1 . no PDB 1YAO . ; Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of The Five Isoleucine To Valine Mutants ; . . . . . 100.00 130 99.23 100.00 2.62e-70 . . . . 5130 1 . no PDB 1YAP . ; Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of The Five Isoleucine To Valine Mutants ; . . . . . 100.00 130 99.23 100.00 2.62e-70 . . . . 5130 1 . no PDB 1YAQ . ; Contribution Of Hydrophobic Residues To The Stability Of Human Lysozyme: Calorimetric Studies And X-Ray Structural Analysis Of The Five Isoleucine To Valine Mutants ; . . . . . 100.00 130 99.23 100.00 2.62e-70 . . . . 5130 1 . no PDB 207L . 'Mutant Human Lysozyme C77a' . . . . . 100.00 130 99.23 99.23 9.48e-70 . . . . 5130 1 . no PDB 208L . 'Mutant Human Lysozyme C77a' . . . . . 100.00 130 99.23 99.23 9.48e-70 . . . . 5130 1 . no PDB 2BQA . 'Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme' . . . . . 100.00 130 98.46 98.46 4.15e-69 . . . . 5130 1 . no PDB 2BQK . 'Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme' . . . . . 99.23 130 98.45 98.45 1.28e-68 . . . . 5130 1 . no PDB 2HEA . 'Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability' . . . . . 100.00 130 99.23 99.23 7.32e-70 . . . . 5130 1 . no PDB 2HEB . 'Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability' . . . . . 100.00 130 99.23 99.23 7.32e-70 . . . . 5130 1 . no PDB 2HEC . 'Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability' . . . . . 100.00 130 99.23 99.23 7.32e-70 . . . . 5130 1 . no PDB 2HED . 'Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability' . . . . . 100.00 130 99.23 99.23 7.32e-70 . . . . 5130 1 . no PDB 2HEE . 'Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability' . . . . . 100.00 130 99.23 99.23 1.48e-69 . . . . 5130 1 . no PDB 2HEF . 'Contribution Of Water Molecules In The Interior Of A Protein To The Conformational Stability' . . . . . 100.00 130 99.23 99.23 7.32e-70 . . . . 5130 1 . 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 4.74e-69 . . . . 5130 1 . no PDB 2MEA . 'Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions' . . . . . 100.00 130 99.23 99.23 5.24e-70 . . . . 5130 1 . no PDB 2MEB . 'Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions' . . . . . 100.00 130 99.23 100.00 3.20e-70 . . . . 5130 1 . no PDB 2MEC . 'Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions' . . . . . 100.00 130 99.23 100.00 3.60e-70 . . . . 5130 1 . no PDB 2MED . 'Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme' . . . . . 100.00 130 99.23 99.23 5.24e-70 . . . . 5130 1 . no PDB 2MEE . 'Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme' . . . . . 100.00 130 99.23 100.00 3.20e-70 . . . . 5130 1 . no PDB 2MEF . 'Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme' . . . . . 100.00 130 99.23 100.00 3.60e-70 . . . . 5130 1 . no PDB 2MEG . 'Changes In Conformational Stability Of A Series Of Mutant Human Lysozymes At Constant Positions' . . . . . 100.00 130 99.23 99.23 8.58e-70 . . . . 5130 1 . no PDB 2MEH . 'Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme' . . . . . 100.00 130 99.23 99.23 5.75e-70 . . . . 5130 1 . no PDB 2MEI . 'Contribution Of Hydrophobic Effect To The Conformational Stability Of Human Lysozyme' . . . . . 100.00 130 99.23 99.23 9.09e-70 . . . . 5130 1 . no PDB 2NWD . 'Structure Of Chemically Synthesized Human Lysozyme At 1 Angstrom Resolution' . . . . . 99.23 130 100.00 100.00 6.19e-70 . . . . 5130 1 . 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 4.74e-69 . . . . 5130 1 . no DBJ BAA00314 . 'lysozyme [synthetic construct]' . . . . . 100.00 131 99.23 99.23 9.97e-70 . . . . 5130 1 . no DBJ BAG34722 . 'unnamed protein product [Homo sapiens]' . . . . . 100.00 148 100.00 100.00 3.48e-71 . . . . 5130 1 . no EMBL CAA32175 . 'lysozyme [Homo sapiens]' . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no EMBL CAA53144 . 'lysozyme [synthetic construct]' . . . . . 100.00 131 100.00 100.00 1.73e-70 . . . . 5130 1 . no GenBank AAA36188 . 'lysozyme precursor (EC 3.2.1.17)' . . . . . 100.00 148 99.23 100.00 7.50e-71 . . . . 5130 1 . no GenBank AAA59535 . 'lysozyme precursor (EC 3.2.1.17)' . . . . . 100.00 148 100.00 100.00 3.48e-71 . . . . 5130 1 . no GenBank AAA59536 . 'lysozyme precursor (EC 3.2.1.17)' . . . . . 100.00 148 100.00 100.00 3.48e-71 . . . . 5130 1 . no GenBank AAA72819 . lysozyme . . . . . 100.00 130 100.00 100.00 1.85e-70 . . . . 5130 1 . no GenBank AAB26052 . 'lysozyme=amyloid fibril protein [human, Peptide Mutant, 130 aa]' . . . . . 100.00 130 99.23 99.23 5.75e-70 . . . . 5130 1 . no REF NP_000230 . 'lysozyme precursor [Homo sapiens]' . . . . . 100.00 148 100.00 100.00 3.48e-71 . . . . 5130 1 . no REF NP_001009073 . 'lysozyme [Pan troglodytes]' . . . . . 100.00 148 100.00 100.00 3.48e-71 . . . . 5130 1 . no SWISS-PROT P61626 . 'Lysozyme C precursor (1,4-beta-N-acetylmuramidase C)' . . . . . 100.00 148 100.00 100.00 3.48e-71 . . . . 5130 1 . no SWISS-PROT P61627 . 'Lysozyme C precursor (1,4-beta-N-acetylmuramidase C)' . . . . . 100.00 148 100.00 100.00 3.48e-71 . . . . 5130 1 . no SWISS-PROT P61628 . 'Lysozyme C precursor (1,4-beta-N-acetylmuramidase C)' . . . . . 100.00 148 100.00 100.00 3.48e-71 . . . . 5130 1 . no SWISS-PROT P79179 . 'Lysozyme C precursor (1,4-beta-N-acetylmuramidase C)' . . . . . 100.00 148 100.00 100.00 4.05e-71 . . . . 5130 1 . no SWISS-PROT P79239 . 'Lysozyme C precursor (1,4-beta-N-acetylmuramidase C)' . . . . . 100.00 148 99.23 99.23 9.88e-71 . . . . 5130 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'human lysozyme' common 5130 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 . 5130 1 2 . VAL . 5130 1 3 . PHE . 5130 1 4 . GLU . 5130 1 5 . ARG . 5130 1 6 . CYS . 5130 1 7 . GLU . 5130 1 8 . LEU . 5130 1 9 . ALA . 5130 1 10 . ARG . 5130 1 11 . THR . 5130 1 12 . LEU . 5130 1 13 . LYS . 5130 1 14 . ARG . 5130 1 15 . LEU . 5130 1 16 . GLY . 5130 1 17 . MET . 5130 1 18 . ASP . 5130 1 19 . GLY . 5130 1 20 . TYR . 5130 1 21 . ARG . 5130 1 22 . GLY . 5130 1 23 . ILE . 5130 1 24 . SER . 5130 1 25 . LEU . 5130 1 26 . ALA . 5130 1 27 . ASN . 5130 1 28 . TRP . 5130 1 29 . MET . 5130 1 30 . CYS . 5130 1 31 . LEU . 5130 1 32 . ALA . 5130 1 33 . LYS . 5130 1 34 . TRP . 5130 1 35 . GLU . 5130 1 36 . SER . 5130 1 37 . GLY . 5130 1 38 . TYR . 5130 1 39 . ASN . 5130 1 40 . THR . 5130 1 41 . ARG . 5130 1 42 . ALA . 5130 1 43 . THR . 5130 1 44 . ASN . 5130 1 45 . TYR . 5130 1 46 . ASN . 5130 1 47 . ALA . 5130 1 48 . GLY . 5130 1 49 . ASP . 5130 1 50 . ARG . 5130 1 51 . SER . 5130 1 52 . THR . 5130 1 53 . ASP . 5130 1 54 . TYR . 5130 1 55 . GLY . 5130 1 56 . ILE . 5130 1 57 . PHE . 5130 1 58 . GLN . 5130 1 59 . ILE . 5130 1 60 . ASN . 5130 1 61 . SER . 5130 1 62 . ARG . 5130 1 63 . TYR . 5130 1 64 . TRP . 5130 1 65 . CYS . 5130 1 66 . ASN . 5130 1 67 . ASP . 5130 1 68 . GLY . 5130 1 69 . LYS . 5130 1 70 . THR . 5130 1 71 . PRO . 5130 1 72 . GLY . 5130 1 73 . ALA . 5130 1 74 . VAL . 5130 1 75 . ASN . 5130 1 76 . ALA . 5130 1 77 . CYS . 5130 1 78 . HIS . 5130 1 79 . LEU . 5130 1 80 . SER . 5130 1 81 . CYS . 5130 1 82 . SER . 5130 1 83 . ALA . 5130 1 84 . LEU . 5130 1 85 . LEU . 5130 1 86 . GLN . 5130 1 87 . ASP . 5130 1 88 . ASN . 5130 1 89 . ILE . 5130 1 90 . ALA . 5130 1 91 . ASP . 5130 1 92 . ALA . 5130 1 93 . VAL . 5130 1 94 . ALA . 5130 1 95 . CYS . 5130 1 96 . ALA . 5130 1 97 . LYS . 5130 1 98 . ARG . 5130 1 99 . VAL . 5130 1 100 . VAL . 5130 1 101 . ARG . 5130 1 102 . ASP . 5130 1 103 . PRO . 5130 1 104 . GLN . 5130 1 105 . GLY . 5130 1 106 . ILE . 5130 1 107 . ARG . 5130 1 108 . ALA . 5130 1 109 . TRP . 5130 1 110 . VAL . 5130 1 111 . ALA . 5130 1 112 . TRP . 5130 1 113 . ARG . 5130 1 114 . ASN . 5130 1 115 . ARG . 5130 1 116 . CYS . 5130 1 117 . GLN . 5130 1 118 . ASN . 5130 1 119 . ARG . 5130 1 120 . ASP . 5130 1 121 . VAL . 5130 1 122 . ARG . 5130 1 123 . GLN . 5130 1 124 . TYR . 5130 1 125 . VAL . 5130 1 126 . GLN . 5130 1 127 . GLY . 5130 1 128 . CYS . 5130 1 129 . GLY . 5130 1 130 . VAL . 5130 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 5130 1 . VAL 2 2 5130 1 . PHE 3 3 5130 1 . GLU 4 4 5130 1 . ARG 5 5 5130 1 . CYS 6 6 5130 1 . GLU 7 7 5130 1 . LEU 8 8 5130 1 . ALA 9 9 5130 1 . ARG 10 10 5130 1 . THR 11 11 5130 1 . LEU 12 12 5130 1 . LYS 13 13 5130 1 . ARG 14 14 5130 1 . LEU 15 15 5130 1 . GLY 16 16 5130 1 . MET 17 17 5130 1 . ASP 18 18 5130 1 . GLY 19 19 5130 1 . TYR 20 20 5130 1 . ARG 21 21 5130 1 . GLY 22 22 5130 1 . ILE 23 23 5130 1 . SER 24 24 5130 1 . LEU 25 25 5130 1 . ALA 26 26 5130 1 . ASN 27 27 5130 1 . TRP 28 28 5130 1 . MET 29 29 5130 1 . CYS 30 30 5130 1 . LEU 31 31 5130 1 . ALA 32 32 5130 1 . LYS 33 33 5130 1 . TRP 34 34 5130 1 . GLU 35 35 5130 1 . SER 36 36 5130 1 . GLY 37 37 5130 1 . TYR 38 38 5130 1 . ASN 39 39 5130 1 . THR 40 40 5130 1 . ARG 41 41 5130 1 . ALA 42 42 5130 1 . THR 43 43 5130 1 . ASN 44 44 5130 1 . TYR 45 45 5130 1 . ASN 46 46 5130 1 . ALA 47 47 5130 1 . GLY 48 48 5130 1 . ASP 49 49 5130 1 . ARG 50 50 5130 1 . SER 51 51 5130 1 . THR 52 52 5130 1 . ASP 53 53 5130 1 . TYR 54 54 5130 1 . GLY 55 55 5130 1 . ILE 56 56 5130 1 . PHE 57 57 5130 1 . GLN 58 58 5130 1 . ILE 59 59 5130 1 . ASN 60 60 5130 1 . SER 61 61 5130 1 . ARG 62 62 5130 1 . TYR 63 63 5130 1 . TRP 64 64 5130 1 . CYS 65 65 5130 1 . ASN 66 66 5130 1 . ASP 67 67 5130 1 . GLY 68 68 5130 1 . LYS 69 69 5130 1 . THR 70 70 5130 1 . PRO 71 71 5130 1 . GLY 72 72 5130 1 . ALA 73 73 5130 1 . VAL 74 74 5130 1 . ASN 75 75 5130 1 . ALA 76 76 5130 1 . CYS 77 77 5130 1 . HIS 78 78 5130 1 . LEU 79 79 5130 1 . SER 80 80 5130 1 . CYS 81 81 5130 1 . SER 82 82 5130 1 . ALA 83 83 5130 1 . LEU 84 84 5130 1 . LEU 85 85 5130 1 . GLN 86 86 5130 1 . ASP 87 87 5130 1 . ASN 88 88 5130 1 . ILE 89 89 5130 1 . ALA 90 90 5130 1 . ASP 91 91 5130 1 . ALA 92 92 5130 1 . VAL 93 93 5130 1 . ALA 94 94 5130 1 . CYS 95 95 5130 1 . ALA 96 96 5130 1 . LYS 97 97 5130 1 . ARG 98 98 5130 1 . VAL 99 99 5130 1 . VAL 100 100 5130 1 . ARG 101 101 5130 1 . ASP 102 102 5130 1 . PRO 103 103 5130 1 . GLN 104 104 5130 1 . GLY 105 105 5130 1 . ILE 106 106 5130 1 . ARG 107 107 5130 1 . ALA 108 108 5130 1 . TRP 109 109 5130 1 . VAL 110 110 5130 1 . ALA 111 111 5130 1 . TRP 112 112 5130 1 . ARG 113 113 5130 1 . ASN 114 114 5130 1 . ARG 115 115 5130 1 . CYS 116 116 5130 1 . GLN 117 117 5130 1 . ASN 118 118 5130 1 . ARG 119 119 5130 1 . ASP 120 120 5130 1 . VAL 121 121 5130 1 . ARG 122 122 5130 1 . GLN 123 123 5130 1 . TYR 124 124 5130 1 . VAL 125 125 5130 1 . GLN 126 126 5130 1 . GLY 127 127 5130 1 . CYS 128 128 5130 1 . GLY 129 129 5130 1 . VAL 130 130 5130 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 5130 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $human_lysozyme . 9606 . . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 5130 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 5130 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $human_lysozyme . 'recombinant technology' . . . . . . . . . . . . . . . . 5130 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5130 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'human lysozyme' . . . 1 $human_lysozyme . . 2 . . mM . . . . 5130 1 stop_ save_ ####################### # Sample conditions # ####################### save_condition_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode condition_1 _Sample_condition_list.Entry_ID 5130 _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* 3.8 0.1 n/a 5130 1 temperature 308 1 K 5130 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 5130 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model Unity _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5130 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer Varian Unity . 500 . . . 5130 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 5130 _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 '15N-edited NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5130 1 2 '15N-edited TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5130 1 3 CBCA(CO)NNH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5130 1 4 HNCACB . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5130 1 5 '13C-edited NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5130 1 6 '1H-13C-1H HCCH-TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5130 1 7 '1H-15N HSQC' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5130 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5130 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . 5130 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_HL35_shift_set _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode HL35_shift_set _Assigned_chem_shift_list.Entry_ID 5130 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $condition_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '15N-edited NOESY' 1 $sample_1 . 5130 1 2 '15N-edited TOCSY' 1 $sample_1 . 5130 1 3 CBCA(CO)NNH 1 $sample_1 . 5130 1 4 HNCACB 1 $sample_1 . 5130 1 5 '13C-edited NOESY' 1 $sample_1 . 5130 1 6 '1H-13C-1H HCCH-TOCSY' 1 $sample_1 . 5130 1 7 '1H-15N HSQC' 1 $sample_1 . 5130 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Ambiguity_set_ID _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 LYS CA C 13 55.899 . . . . . . . . . . . . 5130 1 2 . 1 1 1 1 LYS HA H 1 3.935 . . . . . . . . . . . . 5130 1 3 . 1 1 1 1 LYS CB C 13 34.015 . . . . . . . . . . . . 5130 1 4 . 1 1 1 1 LYS HB2 H 1 1.683 . . . . . . . . . . . . 5130 1 5 . 1 1 1 1 LYS HG3 H 1 1.153 . . . . . . . . . . . . 5130 1 6 . 1 1 1 1 LYS HD2 H 1 0.897 . . . . . . . . . . . . 5130 1 7 . 1 1 1 1 LYS HD3 H 1 0.637 . . . . . . . . . . . . 5130 1 8 . 1 1 1 1 LYS HE2 H 1 3.935 . . . . . . . . . . . . 5130 1 9 . 1 1 2 2 VAL N N 15 127.203 . . . . . . . . . . . . 5130 1 10 . 1 1 2 2 VAL H H 1 8.859 . . . . . . . . . . . . 5130 1 11 . 1 1 2 2 VAL CA C 13 61.911 . . . . . . . . . . . . 5130 1 12 . 1 1 2 2 VAL HA H 1 4.86 . . . . . . . . . . . . 5130 1 13 . 1 1 2 2 VAL CB C 13 31.883 . . . . . . . . . . . . 5130 1 14 . 1 1 2 2 VAL HB H 1 1.985 . . . . . . . . . . . . 5130 1 15 . 1 1 2 2 VAL HG11 H 1 1.017 . . . . . . . . . . . . 5130 1 16 . 1 1 2 2 VAL HG12 H 1 1.017 . . . . . . . . . . . . 5130 1 17 . 1 1 2 2 VAL HG13 H 1 1.017 . . . . . . . . . . . . 5130 1 18 . 1 1 2 2 VAL HG21 H 1 0.912 . . . . . . . . . . . . 5130 1 19 . 1 1 2 2 VAL HG22 H 1 0.912 . . . . . . . . . . . . 5130 1 20 . 1 1 2 2 VAL HG23 H 1 0.912 . . . . . . . . . . . . 5130 1 21 . 1 1 3 3 PHE N N 15 127.487 . . . . . . . . . . . . 5130 1 22 . 1 1 3 3 PHE H H 1 8.865 . . . . . . . . . . . . 5130 1 23 . 1 1 3 3 PHE CA C 13 59.517 . . . . . . . . . . . . 5130 1 24 . 1 1 3 3 PHE HA H 1 4.11 . . . . . . . . . . . . 5130 1 25 . 1 1 3 3 PHE CB C 13 41.633 . . . . . . . . . . . . 5130 1 26 . 1 1 3 3 PHE HB2 H 1 2.987 . . . . . . . . . . . . 5130 1 27 . 1 1 3 3 PHE HB3 H 1 2.75 . . . . . . . . . . . . 5130 1 28 . 1 1 4 4 GLU N N 15 120.766 . . . . . . . . . . . . 5130 1 29 . 1 1 4 4 GLU H H 1 8.38 . . . . . . . . . . . . 5130 1 30 . 1 1 4 4 GLU CA C 13 56.406 . . . . . . . . . . . . 5130 1 31 . 1 1 4 4 GLU HA H 1 4.364 . . . . . . . . . . . . 5130 1 32 . 1 1 4 4 GLU CB C 13 30.13 . . . . . . . . . . . . 5130 1 33 . 1 1 4 4 GLU HB2 H 1 2.369 . . . . . . . . . . . . 5130 1 34 . 1 1 4 4 GLU HB3 H 1 2.231 . . . . . . . . . . . . 5130 1 35 . 1 1 4 4 GLU HG2 H 1 2.611 . . . . . . . . . . . . 5130 1 36 . 1 1 4 4 GLU HG3 H 1 2.48 . . . . . . . . . . . . 5130 1 37 . 1 1 5 5 ARG N N 15 125.877 . . . . . . . . . . . . 5130 1 38 . 1 1 5 5 ARG H H 1 8.565 . . . . . . . . . . . . 5130 1 39 . 1 1 5 5 ARG CA C 13 61.224 . . . . . . . . . . . . 5130 1 40 . 1 1 5 5 ARG HA H 1 3.213 . . . . . . . . . . . . 5130 1 41 . 1 1 5 5 ARG CB C 13 32.183 . . . . . . . . . . . . 5130 1 42 . 1 1 5 5 ARG HB2 H 1 1.898 . . . . . . . . . . . . 5130 1 43 . 1 1 5 5 ARG HG2 H 1 1.571 . . . . . . . . . . . . 5130 1 44 . 1 1 5 5 ARG HG3 H 1 1.312 . . . . . . . . . . . . 5130 1 45 . 1 1 5 5 ARG HD2 H 1 3.581 . . . . . . . . . . . . 5130 1 46 . 1 1 5 5 ARG HD3 H 1 3.348 . . . . . . . . . . . . 5130 1 47 . 1 1 6 6 CYS N N 15 114.737 . . . . . . . . . . . . 5130 1 48 . 1 1 6 6 CYS H H 1 8.901 . . . . . . . . . . . . 5130 1 49 . 1 1 6 6 CYS CA C 13 54.731 . . . . . . . . . . . . 5130 1 50 . 1 1 6 6 CYS HA H 1 4.75 . . . . . . . . . . . . 5130 1 51 . 1 1 6 6 CYS CB C 13 33.085 . . . . . . . . . . . . 5130 1 52 . 1 1 6 6 CYS HB2 H 1 3.17 . . . . . . . . . . . . 5130 1 53 . 1 1 6 6 CYS HB3 H 1 2.986 . . . . . . . . . . . . 5130 1 54 . 1 1 7 7 GLU N N 15 125.732 . . . . . . . . . . . . 5130 1 55 . 1 1 7 7 GLU H H 1 7.834 . . . . . . . . . . . . 5130 1 56 . 1 1 7 7 GLU CA C 13 59.242 . . . . . . . . . . . . 5130 1 57 . 1 1 7 7 GLU HA H 1 4.137 . . . . . . . . . . . . 5130 1 58 . 1 1 7 7 GLU CB C 13 30.005 . . . . . . . . . . . . 5130 1 59 . 1 1 7 7 GLU HB2 H 1 2.588 . . . . . . . . . . . . 5130 1 60 . 1 1 7 7 GLU HG2 H 1 2.341 . . . . . . . . . . . . 5130 1 61 . 1 1 8 8 LEU N N 15 122.074 . . . . . . . . . . . . 5130 1 62 . 1 1 8 8 LEU H H 1 8.501 . . . . . . . . . . . . 5130 1 63 . 1 1 8 8 LEU CA C 13 57.89 . . . . . . . . . . . . 5130 1 64 . 1 1 8 8 LEU HA H 1 3.675 . . . . . . . . . . . . 5130 1 65 . 1 1 8 8 LEU CB C 13 39.852 . . . . . . . . . . . . 5130 1 66 . 1 1 8 8 LEU HB2 H 1 1.589 . . . . . . . . . . . . 5130 1 67 . 1 1 8 8 LEU HB3 H 1 1.204 . . . . . . . . . . . . 5130 1 68 . 1 1 8 8 LEU HG H 1 0.796 . . . . . . . . . . . . 5130 1 69 . 1 1 8 8 LEU HD11 H 1 0.369 . . . . . . . . . . . . 5130 1 70 . 1 1 8 8 LEU HD12 H 1 0.369 . . . . . . . . . . . . 5130 1 71 . 1 1 8 8 LEU HD13 H 1 0.369 . . . . . . . . . . . . 5130 1 72 . 1 1 8 8 LEU HD21 H 1 -0.275 . . . . . . . . . . . . 5130 1 73 . 1 1 8 8 LEU HD22 H 1 -0.275 . . . . . . . . . . . . 5130 1 74 . 1 1 8 8 LEU HD23 H 1 -0.275 . . . . . . . . . . . . 5130 1 75 . 1 1 9 9 ALA N N 15 123.004 . . . . . . . . . . . . 5130 1 76 . 1 1 9 9 ALA H H 1 8.367 . . . . . . . . . . . . 5130 1 77 . 1 1 9 9 ALA CA C 13 56.648 . . . . . . . . . . . . 5130 1 78 . 1 1 9 9 ALA HA H 1 4.014 . . . . . . . . . . . . 5130 1 79 . 1 1 9 9 ALA CB C 13 18.157 . . . . . . . . . . . . 5130 1 80 . 1 1 9 9 ALA HB1 H 1 1.506 . . . . . . . . . . . . 5130 1 81 . 1 1 9 9 ALA HB2 H 1 1.506 . . . . . . . . . . . . 5130 1 82 . 1 1 9 9 ALA HB3 H 1 1.506 . . . . . . . . . . . . 5130 1 83 . 1 1 10 10 ARG N N 15 115.113 . . . . . . . . . . . . 5130 1 84 . 1 1 10 10 ARG H H 1 8.302 . . . . . . . . . . . . 5130 1 85 . 1 1 10 10 ARG CA C 13 60.347 . . . . . . . . . . . . 5130 1 86 . 1 1 10 10 ARG HA H 1 3.873 . . . . . . . . . . . . 5130 1 87 . 1 1 10 10 ARG CB C 13 31.175 . . . . . . . . . . . . 5130 1 88 . 1 1 10 10 ARG HB2 H 1 1.94 . . . . . . . . . . . . 5130 1 89 . 1 1 10 10 ARG HB3 H 1 1.881 . . . . . . . . . . . . 5130 1 90 . 1 1 10 10 ARG HG3 H 1 1.605 . . . . . . . . . . . . 5130 1 91 . 1 1 10 10 ARG HD2 H 1 3.337 . . . . . . . . . . . . 5130 1 92 . 1 1 10 10 ARG HD3 H 1 3.086 . . . . . . . . . . . . 5130 1 93 . 1 1 11 11 THR N N 15 118.762 . . . . . . . . . . . . 5130 1 94 . 1 1 11 11 THR H H 1 7.83 . . . . . . . . . . . . 5130 1 95 . 1 1 11 11 THR CA C 13 67.392 . . . . . . . . . . . . 5130 1 96 . 1 1 11 11 THR HA H 1 3.953 . . . . . . . . . . . . 5130 1 97 . 1 1 11 11 THR CB C 13 68.566 . . . . . . . . . . . . 5130 1 98 . 1 1 11 11 THR HB H 1 4.235 . . . . . . . . . . . . 5130 1 99 . 1 1 11 11 THR HG21 H 1 1.187 . . . . . . . . . . . . 5130 1 100 . 1 1 11 11 THR HG22 H 1 1.187 . . . . . . . . . . . . 5130 1 101 . 1 1 11 11 THR HG23 H 1 1.187 . . . . . . . . . . . . 5130 1 102 . 1 1 12 12 LEU N N 15 119.162 . . . . . . . . . . . . 5130 1 103 . 1 1 12 12 LEU H H 1 8.804 . . . . . . . . . . . . 5130 1 104 . 1 1 12 12 LEU CA C 13 58.163 . . . . . . . . . . . . 5130 1 105 . 1 1 12 12 LEU HA H 1 3.639 . . . . . . . . . . . . 5130 1 106 . 1 1 12 12 LEU CB C 13 41.45 . . . . . . . . . . . . 5130 1 107 . 1 1 12 12 LEU HB2 H 1 1.904 . . . . . . . . . . . . 5130 1 108 . 1 1 12 12 LEU HG H 1 1.654 . . . . . . . . . . . . 5130 1 109 . 1 1 12 12 LEU HD11 H 1 0.742 . . . . . . . . . . . . 5130 1 110 . 1 1 12 12 LEU HD12 H 1 0.742 . . . . . . . . . . . . 5130 1 111 . 1 1 12 12 LEU HD13 H 1 0.742 . . . . . . . . . . . . 5130 1 112 . 1 1 12 12 LEU HD21 H 1 0.504 . . . . . . . . . . . . 5130 1 113 . 1 1 12 12 LEU HD22 H 1 0.504 . . . . . . . . . . . . 5130 1 114 . 1 1 12 12 LEU HD23 H 1 0.504 . . . . . . . . . . . . 5130 1 115 . 1 1 13 13 LYS N N 15 119.475 . . . . . . . . . . . . 5130 1 116 . 1 1 13 13 LYS H H 1 8.172 . . . . . . . . . . . . 5130 1 117 . 1 1 13 13 LYS CA C 13 59.09 . . . . . . . . . . . . 5130 1 118 . 1 1 13 13 LYS HA H 1 4.049 . . . . . . . . . . . . 5130 1 119 . 1 1 13 13 LYS CB C 13 33.028 . . . . . . . . . . . . 5130 1 120 . 1 1 13 13 LYS HB2 H 1 2.184 . . . . . . . . . . . . 5130 1 121 . 1 1 13 13 LYS HG3 H 1 1.921 . . . . . . . . . . . . 5130 1 122 . 1 1 13 13 LYS HD2 H 1 1.718 . . . . . . . . . . . . 5130 1 123 . 1 1 13 13 LYS HD3 H 1 1.554 . . . . . . . . . . . . 5130 1 124 . 1 1 13 13 LYS HE2 H 1 3.166 . . . . . . . . . . . . 5130 1 125 . 1 1 14 14 ARG N N 15 121.748 . . . . . . . . . . . . 5130 1 126 . 1 1 14 14 ARG H H 1 7.967 . . . . . . . . . . . . 5130 1 127 . 1 1 14 14 ARG CA C 13 59.394 . . . . . . . . . . . . 5130 1 128 . 1 1 14 14 ARG HA H 1 4.178 . . . . . . . . . . . . 5130 1 129 . 1 1 14 14 ARG CB C 13 30.152 . . . . . . . . . . . . 5130 1 130 . 1 1 14 14 ARG HB2 H 1 2.055 . . . . . . . . . . . . 5130 1 131 . 1 1 14 14 ARG HG3 H 1 1.808 . . . . . . . . . . . . 5130 1 132 . 1 1 14 14 ARG HD2 H 1 3.283 . . . . . . . . . . . . 5130 1 133 . 1 1 15 15 LEU N N 15 117.087 . . . . . . . . . . . . 5130 1 134 . 1 1 15 15 LEU H H 1 7.508 . . . . . . . . . . . . 5130 1 135 . 1 1 15 15 LEU CA C 13 54.784 . . . . . . . . . . . . 5130 1 136 . 1 1 15 15 LEU HA H 1 4.405 . . . . . . . . . . . . 5130 1 137 . 1 1 15 15 LEU CB C 13 42.084 . . . . . . . . . . . . 5130 1 138 . 1 1 15 15 LEU HB2 H 1 1.917 . . . . . . . . . . . . 5130 1 139 . 1 1 15 15 LEU HB3 H 1 1.797 . . . . . . . . . . . . 5130 1 140 . 1 1 15 15 LEU HG H 1 1.497 . . . . . . . . . . . . 5130 1 141 . 1 1 15 15 LEU HD11 H 1 0.843 . . . . . . . . . . . . 5130 1 142 . 1 1 15 15 LEU HD12 H 1 0.843 . . . . . . . . . . . . 5130 1 143 . 1 1 15 15 LEU HD13 H 1 0.843 . . . . . . . . . . . . 5130 1 144 . 1 1 15 15 LEU HD21 H 1 0.726 . . . . . . . . . . . . 5130 1 145 . 1 1 15 15 LEU HD22 H 1 0.726 . . . . . . . . . . . . 5130 1 146 . 1 1 15 15 LEU HD23 H 1 0.726 . . . . . . . . . . . . 5130 1 147 . 1 1 16 16 GLY N N 15 106.523 . . . . . . . . . . . . 5130 1 148 . 1 1 16 16 GLY H H 1 7.555 . . . . . . . . . . . . 5130 1 149 . 1 1 16 16 GLY CA C 13 47.589 . . . . . . . . . . . . 5130 1 150 . 1 1 16 16 GLY HA2 H 1 4.088 . . . . . . . . . . . . 5130 1 151 . 1 1 16 16 GLY HA3 H 1 3.894 . . . . . . . . . . . . 5130 1 152 . 1 1 17 17 MET N N 15 114.251 . . . . . . . . . . . . 5130 1 153 . 1 1 17 17 MET H H 1 7.427 . . . . . . . . . . . . 5130 1 154 . 1 1 17 17 MET CA C 13 57.005 . . . . . . . . . . . . 5130 1 155 . 1 1 17 17 MET HA H 1 4.019 . . . . . . . . . . . . 5130 1 156 . 1 1 17 17 MET CB C 13 34.4 . . . . . . . . . . . . 5130 1 157 . 1 1 17 17 MET HB2 H 1 1.346 . . . . . . . . . . . . 5130 1 158 . 1 1 17 17 MET HB3 H 1 1.285 . . . . . . . . . . . . 5130 1 159 . 1 1 17 17 MET HG2 H 1 1.499 . . . . . . . . . . . . 5130 1 160 . 1 1 18 18 ASP N N 15 118.685 . . . . . . . . . . . . 5130 1 161 . 1 1 18 18 ASP H H 1 8.98 . . . . . . . . . . . . 5130 1 162 . 1 1 18 18 ASP CA C 13 56.005 . . . . . . . . . . . . 5130 1 163 . 1 1 18 18 ASP HA H 1 4.46 . . . . . . . . . . . . 5130 1 164 . 1 1 18 18 ASP CB C 13 41.609 . . . . . . . . . . . . 5130 1 165 . 1 1 18 18 ASP HB2 H 1 3.283 . . . . . . . . . . . . 5130 1 166 . 1 1 18 18 ASP HB3 H 1 2.354 . . . . . . . . . . . . 5130 1 167 . 1 1 19 19 GLY N N 15 119.43 . . . . . . . . . . . . 5130 1 168 . 1 1 19 19 GLY H H 1 9.036 . . . . . . . . . . . . 5130 1 169 . 1 1 19 19 GLY CA C 13 45.923 . . . . . . . . . . . . 5130 1 170 . 1 1 19 19 GLY HA2 H 1 4.229 . . . . . . . . . . . . 5130 1 171 . 1 1 19 19 GLY HA3 H 1 3.306 . . . . . . . . . . . . 5130 1 172 . 1 1 20 20 TYR N N 15 126.315 . . . . . . . . . . . . 5130 1 173 . 1 1 20 20 TYR H H 1 7.899 . . . . . . . . . . . . 5130 1 174 . 1 1 20 20 TYR CA C 13 60.925 . . . . . . . . . . . . 5130 1 175 . 1 1 20 20 TYR HA H 1 4.153 . . . . . . . . . . . . 5130 1 176 . 1 1 20 20 TYR CB C 13 38.852 . . . . . . . . . . . . 5130 1 177 . 1 1 20 20 TYR HB2 H 1 3.351 . . . . . . . . . . . . 5130 1 178 . 1 1 20 20 TYR HB3 H 1 3.115 . . . . . . . . . . . . 5130 1 179 . 1 1 21 21 ARG N N 15 126.013 . . . . . . . . . . . . 5130 1 180 . 1 1 21 21 ARG H H 1 8.908 . . . . . . . . . . . . 5130 1 181 . 1 1 21 21 ARG CA C 13 56.709 . . . . . . . . . . . . 5130 1 182 . 1 1 21 21 ARG HA H 1 3.566 . . . . . . . . . . . . 5130 1 183 . 1 1 21 21 ARG CB C 13 27.378 . . . . . . . . . . . . 5130 1 184 . 1 1 21 21 ARG HB2 H 1 2.048 . . . . . . . . . . . . 5130 1 185 . 1 1 21 21 ARG HG2 H 1 1.108 . . . . . . . . . . . . 5130 1 186 . 1 1 21 21 ARG HG3 H 1 1.624 . . . . . . . . . . . . 5130 1 187 . 1 1 21 21 ARG HD2 H 1 3.092 . . . . . . . . . . . . 5130 1 188 . 1 1 21 21 ARG HD3 H 1 2.965 . . . . . . . . . . . . 5130 1 189 . 1 1 22 22 GLY N N 15 103.392 . . . . . . . . . . . . 5130 1 190 . 1 1 22 22 GLY H H 1 7.838 . . . . . . . . . . . . 5130 1 191 . 1 1 22 22 GLY CA C 13 45.651 . . . . . . . . . . . . 5130 1 192 . 1 1 22 22 GLY HA2 H 1 4.037 . . . . . . . . . . . . 5130 1 193 . 1 1 22 22 GLY HA3 H 1 3.584 . . . . . . . . . . . . 5130 1 194 . 1 1 23 23 ILE N N 15 124.579 . . . . . . . . . . . . 5130 1 195 . 1 1 23 23 ILE H H 1 7.759 . . . . . . . . . . . . 5130 1 196 . 1 1 23 23 ILE CA C 13 61.132 . . . . . . . . . . . . 5130 1 197 . 1 1 23 23 ILE HA H 1 3.859 . . . . . . . . . . . . 5130 1 198 . 1 1 23 23 ILE CB C 13 38.168 . . . . . . . . . . . . 5130 1 199 . 1 1 23 23 ILE HB H 1 2.021 . . . . . . . . . . . . 5130 1 200 . 1 1 23 23 ILE HG12 H 1 1.298 . . . . . . . . . . . . 5130 1 201 . 1 1 23 23 ILE HG13 H 1 1.298 . . . . . . . . . . . . 5130 1 202 . 1 1 23 23 ILE HG21 H 1 0.595 . . . . . . . . . . . . 5130 1 203 . 1 1 23 23 ILE HG22 H 1 0.595 . . . . . . . . . . . . 5130 1 204 . 1 1 23 23 ILE HG23 H 1 0.595 . . . . . . . . . . . . 5130 1 205 . 1 1 23 23 ILE HD11 H 1 -0.277 . . . . . . . . . . . . 5130 1 206 . 1 1 23 23 ILE HD12 H 1 -0.277 . . . . . . . . . . . . 5130 1 207 . 1 1 23 23 ILE HD13 H 1 -0.277 . . . . . . . . . . . . 5130 1 208 . 1 1 24 24 SER N N 15 123.121 . . . . . . . . . . . . 5130 1 209 . 1 1 24 24 SER H H 1 8.775 . . . . . . . . . . . . 5130 1 210 . 1 1 24 24 SER CA C 13 57.864 . . . . . . . . . . . . 5130 1 211 . 1 1 24 24 SER HA H 1 4.46 . . . . . . . . . . . . 5130 1 212 . 1 1 24 24 SER CB C 13 65.594 . . . . . . . . . . . . 5130 1 213 . 1 1 24 24 SER HB2 H 1 4.41 . . . . . . . . . . . . 5130 1 214 . 1 1 24 24 SER HB3 H 1 4.172 . . . . . . . . . . . . 5130 1 215 . 1 1 25 25 LEU N N 15 121.883 . . . . . . . . . . . . 5130 1 216 . 1 1 25 25 LEU H H 1 8.838 . . . . . . . . . . . . 5130 1 217 . 1 1 25 25 LEU CA C 13 58.773 . . . . . . . . . . . . 5130 1 218 . 1 1 25 25 LEU HA H 1 4.211 . . . . . . . . . . . . 5130 1 219 . 1 1 25 25 LEU CB C 13 42.782 . . . . . . . . . . . . 5130 1 220 . 1 1 25 25 LEU HB2 H 1 1.974 . . . . . . . . . . . . 5130 1 221 . 1 1 25 25 LEU HG H 1 1.399 . . . . . . . . . . . . 5130 1 222 . 1 1 25 25 LEU HD11 H 1 0.976 . . . . . . . . . . . . 5130 1 223 . 1 1 25 25 LEU HD12 H 1 0.976 . . . . . . . . . . . . 5130 1 224 . 1 1 25 25 LEU HD13 H 1 0.976 . . . . . . . . . . . . 5130 1 225 . 1 1 25 25 LEU HD21 H 1 0.976 . . . . . . . . . . . . 5130 1 226 . 1 1 25 25 LEU HD22 H 1 0.976 . . . . . . . . . . . . 5130 1 227 . 1 1 25 25 LEU HD23 H 1 0.976 . . . . . . . . . . . . 5130 1 228 . 1 1 26 26 ALA N N 15 118.808 . . . . . . . . . . . . 5130 1 229 . 1 1 26 26 ALA H H 1 8.836 . . . . . . . . . . . . 5130 1 230 . 1 1 26 26 ALA CA C 13 56.319 . . . . . . . . . . . . 5130 1 231 . 1 1 26 26 ALA HA H 1 3.925 . . . . . . . . . . . . 5130 1 232 . 1 1 26 26 ALA CB C 13 18.564 . . . . . . . . . . . . 5130 1 233 . 1 1 26 26 ALA HB1 H 1 1.558 . . . . . . . . . . . . 5130 1 234 . 1 1 26 26 ALA HB2 H 1 1.558 . . . . . . . . . . . . 5130 1 235 . 1 1 26 26 ALA HB3 H 1 1.558 . . . . . . . . . . . . 5130 1 236 . 1 1 27 27 ASN N N 15 117.054 . . . . . . . . . . . . 5130 1 237 . 1 1 27 27 ASN H H 1 7.752 . . . . . . . . . . . . 5130 1 238 . 1 1 27 27 ASN CA C 13 58.488 . . . . . . . . . . . . 5130 1 239 . 1 1 27 27 ASN HA H 1 4.581 . . . . . . . . . . . . 5130 1 240 . 1 1 27 27 ASN CB C 13 40.845 . . . . . . . . . . . . 5130 1 241 . 1 1 27 27 ASN HB2 H 1 3.038 . . . . . . . . . . . . 5130 1 242 . 1 1 27 27 ASN HB3 H 1 2.105 . . . . . . . . . . . . 5130 1 243 . 1 1 27 27 ASN HD21 H 1 7.575 . . . . . . . . . . . . 5130 1 244 . 1 1 27 27 ASN HD22 H 1 6.884 . . . . . . . . . . . . 5130 1 245 . 1 1 28 28 TRP N N 15 120.179 . . . . . . . . . . . . 5130 1 246 . 1 1 28 28 TRP H H 1 7.819 . . . . . . . . . . . . 5130 1 247 . 1 1 28 28 TRP CA C 13 60.734 . . . . . . . . . . . . 5130 1 248 . 1 1 28 28 TRP HA H 1 4.378 . . . . . . . . . . . . 5130 1 249 . 1 1 28 28 TRP CB C 13 30.816 . . . . . . . . . . . . 5130 1 250 . 1 1 28 28 TRP HB2 H 1 3.323 . . . . . . . . . . . . 5130 1 251 . 1 1 28 28 TRP HB3 H 1 3.054 . . . . . . . . . . . . 5130 1 252 . 1 1 29 29 MET N N 15 116.706 . . . . . . . . . . . . 5130 1 253 . 1 1 29 29 MET H H 1 8.384 . . . . . . . . . . . . 5130 1 254 . 1 1 29 29 MET CA C 13 55.879 . . . . . . . . . . . . 5130 1 255 . 1 1 29 29 MET HA H 1 4.435 . . . . . . . . . . . . 5130 1 256 . 1 1 29 29 MET CB C 13 31.059 . . . . . . . . . . . . 5130 1 257 . 1 1 29 29 MET HB2 H 1 2.281 . . . . . . . . . . . . 5130 1 258 . 1 1 29 29 MET HB3 H 1 2.072 . . . . . . . . . . . . 5130 1 259 . 1 1 29 29 MET HG2 H 1 2.397 . . . . . . . . . . . . 5130 1 260 . 1 1 29 29 MET HG3 H 1 2.283 . . . . . . . . . . . . 5130 1 261 . 1 1 30 30 CYS N N 15 119.92 . . . . . . . . . . . . 5130 1 262 . 1 1 30 30 CYS H H 1 8.024 . . . . . . . . . . . . 5130 1 263 . 1 1 30 30 CYS CA C 13 60.704 . . . . . . . . . . . . 5130 1 264 . 1 1 30 30 CYS HA H 1 2.96 . . . . . . . . . . . . 5130 1 265 . 1 1 30 30 CYS CB C 13 44.861 . . . . . . . . . . . . 5130 1 266 . 1 1 30 30 CYS HB2 H 1 3.147 . . . . . . . . . . . . 5130 1 267 . 1 1 31 31 LEU N N 15 118.658 . . . . . . . . . . . . 5130 1 268 . 1 1 31 31 LEU H H 1 8.102 . . . . . . . . . . . . 5130 1 269 . 1 1 31 31 LEU CA C 13 59.34 . . . . . . . . . . . . 5130 1 270 . 1 1 31 31 LEU HA H 1 3.988 . . . . . . . . . . . . 5130 1 271 . 1 1 31 31 LEU CB C 13 42.591 . . . . . . . . . . . . 5130 1 272 . 1 1 31 31 LEU HB2 H 1 2.366 . . . . . . . . . . . . 5130 1 273 . 1 1 31 31 LEU HB3 H 1 1.523 . . . . . . . . . . . . 5130 1 274 . 1 1 31 31 LEU HG H 1 1.091 . . . . . . . . . . . . 5130 1 275 . 1 1 31 31 LEU HD11 H 1 0.473 . . . . . . . . . . . . 5130 1 276 . 1 1 31 31 LEU HD12 H 1 0.473 . . . . . . . . . . . . 5130 1 277 . 1 1 31 31 LEU HD13 H 1 0.473 . . . . . . . . . . . . 5130 1 278 . 1 1 31 31 LEU HD21 H 1 -0.09 . . . . . . . . . . . . 5130 1 279 . 1 1 31 31 LEU HD22 H 1 -0.09 . . . . . . . . . . . . 5130 1 280 . 1 1 31 31 LEU HD23 H 1 -0.09 . . . . . . . . . . . . 5130 1 281 . 1 1 32 32 ALA N N 15 119.313 . . . . . . . . . . . . 5130 1 282 . 1 1 32 32 ALA H H 1 8.385 . . . . . . . . . . . . 5130 1 283 . 1 1 32 32 ALA CA C 13 55.408 . . . . . . . . . . . . 5130 1 284 . 1 1 32 32 ALA HA H 1 4.084 . . . . . . . . . . . . 5130 1 285 . 1 1 32 32 ALA CB C 13 18.83 . . . . . . . . . . . . 5130 1 286 . 1 1 32 32 ALA HB1 H 1 1.386 . . . . . . . . . . . . 5130 1 287 . 1 1 32 32 ALA HB2 H 1 1.386 . . . . . . . . . . . . 5130 1 288 . 1 1 32 32 ALA HB3 H 1 1.386 . . . . . . . . . . . . 5130 1 289 . 1 1 33 33 LYS N N 15 119.869 . . . . . . . . . . . . 5130 1 290 . 1 1 33 33 LYS H H 1 8.673 . . . . . . . . . . . . 5130 1 291 . 1 1 33 33 LYS CA C 13 60.639 . . . . . . . . . . . . 5130 1 292 . 1 1 33 33 LYS HA H 1 4.228 . . . . . . . . . . . . 5130 1 293 . 1 1 33 33 LYS CB C 13 30.973 . . . . . . . . . . . . 5130 1 294 . 1 1 33 33 LYS HB2 H 1 2.07 . . . . . . . . . . . . 5130 1 295 . 1 1 33 33 LYS HG3 H 1 1.47 . . . . . . . . . . . . 5130 1 296 . 1 1 33 33 LYS HD2 H 1 0.652 . . . . . . . . . . . . 5130 1 297 . 1 1 33 33 LYS HD3 H 1 0.52 . . . . . . . . . . . . 5130 1 298 . 1 1 33 33 LYS HE2 H 1 2.661 . . . . . . . . . . . . 5130 1 299 . 1 1 34 34 TRP N N 15 118.114 . . . . . . . . . . . . 5130 1 300 . 1 1 34 34 TRP H H 1 7.714 . . . . . . . . . . . . 5130 1 301 . 1 1 34 34 TRP CA C 13 59.594 . . . . . . . . . . . . 5130 1 302 . 1 1 34 34 TRP HA H 1 4.347 . . . . . . . . . . . . 5130 1 303 . 1 1 34 34 TRP CB C 13 29.866 . . . . . . . . . . . . 5130 1 304 . 1 1 34 34 TRP HB2 H 1 3.332 . . . . . . . . . . . . 5130 1 305 . 1 1 34 34 TRP HB3 H 1 2.792 . . . . . . . . . . . . 5130 1 306 . 1 1 35 35 GLU N N 15 116.361 . . . . . . . . . . . . 5130 1 307 . 1 1 35 35 GLU H H 1 8.721 . . . . . . . . . . . . 5130 1 308 . 1 1 35 35 GLU CA C 13 58.032 . . . . . . . . . . . . 5130 1 309 . 1 1 35 35 GLU HA H 1 4.5 . . . . . . . . . . . . 5130 1 310 . 1 1 35 35 GLU CB C 13 27.975 . . . . . . . . . . . . 5130 1 311 . 1 1 35 35 GLU HB2 H 1 2.036 . . . . . . . . . . . . 5130 1 312 . 1 1 35 35 GLU HB3 H 1 2.069 . . . . . . . . . . . . 5130 1 313 . 1 1 35 35 GLU HG2 H 1 1.694 . . . . . . . . . . . . 5130 1 314 . 1 1 35 35 GLU HG3 H 1 1.867 . . . . . . . . . . . . 5130 1 315 . 1 1 36 36 SER N N 15 108.082 . . . . . . . . . . . . 5130 1 316 . 1 1 36 36 SER H H 1 7.88 . . . . . . . . . . . . 5130 1 317 . 1 1 36 36 SER CA C 13 58.355 . . . . . . . . . . . . 5130 1 318 . 1 1 36 36 SER HA H 1 4.67 . . . . . . . . . . . . 5130 1 319 . 1 1 36 36 SER CB C 13 68.273 . . . . . . . . . . . . 5130 1 320 . 1 1 36 36 SER HB2 H 1 4.457 . . . . . . . . . . . . 5130 1 321 . 1 1 36 36 SER HB3 H 1 3.577 . . . . . . . . . . . . 5130 1 322 . 1 1 37 37 GLY N N 15 116.085 . . . . . . . . . . . . 5130 1 323 . 1 1 37 37 GLY H H 1 8.112 . . . . . . . . . . . . 5130 1 324 . 1 1 37 37 GLY CA C 13 47.79 . . . . . . . . . . . . 5130 1 325 . 1 1 37 37 GLY HA2 H 1 3.758 . . . . . . . . . . . . 5130 1 326 . 1 1 37 37 GLY HA3 H 1 3.466 . . . . . . . . . . . . 5130 1 327 . 1 1 38 38 TYR N N 15 108.777 . . . . . . . . . . . . 5130 1 328 . 1 1 38 38 TYR H H 1 7.391 . . . . . . . . . . . . 5130 1 329 . 1 1 38 38 TYR CA C 13 56.881 . . . . . . . . . . . . 5130 1 330 . 1 1 38 38 TYR HA H 1 3.701 . . . . . . . . . . . . 5130 1 331 . 1 1 38 38 TYR CB C 13 36.949 . . . . . . . . . . . . 5130 1 332 . 1 1 38 38 TYR HB2 H 1 3.213 . . . . . . . . . . . . 5130 1 333 . 1 1 39 39 ASN N N 15 117.484 . . . . . . . . . . . . 5130 1 334 . 1 1 39 39 ASN H H 1 7.135 . . . . . . . . . . . . 5130 1 335 . 1 1 39 39 ASN CA C 13 51.849 . . . . . . . . . . . . 5130 1 336 . 1 1 39 39 ASN HA H 1 5.518 . . . . . . . . . . . . 5130 1 337 . 1 1 39 39 ASN CB C 13 40.674 . . . . . . . . . . . . 5130 1 338 . 1 1 39 39 ASN HB2 H 1 3.484 . . . . . . . . . . . . 5130 1 339 . 1 1 39 39 ASN HB3 H 1 2.723 . . . . . . . . . . . . 5130 1 340 . 1 1 39 39 ASN HD21 H 1 7.745 . . . . . . . . . . . . 5130 1 341 . 1 1 39 39 ASN HD22 H 1 7.03 . . . . . . . . . . . . 5130 1 342 . 1 1 40 40 THR N N 15 115.424 . . . . . . . . . . . . 5130 1 343 . 1 1 40 40 THR H H 1 9.185 . . . . . . . . . . . . 5130 1 344 . 1 1 40 40 THR CA C 13 64.743 . . . . . . . . . . . . 5130 1 345 . 1 1 40 40 THR HA H 1 4.048 . . . . . . . . . . . . 5130 1 346 . 1 1 40 40 THR CB C 13 69.784 . . . . . . . . . . . . 5130 1 347 . 1 1 40 40 THR HB H 1 4.457 . . . . . . . . . . . . 5130 1 348 . 1 1 40 40 THR HG21 H 1 1.547 . . . . . . . . . . . . 5130 1 349 . 1 1 40 40 THR HG22 H 1 1.547 . . . . . . . . . . . . 5130 1 350 . 1 1 40 40 THR HG23 H 1 1.547 . . . . . . . . . . . . 5130 1 351 . 1 1 41 41 ARG N N 15 114.739 . . . . . . . . . . . . 5130 1 352 . 1 1 41 41 ARG H H 1 7.652 . . . . . . . . . . . . 5130 1 353 . 1 1 41 41 ARG CA C 13 55.258 . . . . . . . . . . . . 5130 1 354 . 1 1 41 41 ARG HA H 1 4.497 . . . . . . . . . . . . 5130 1 355 . 1 1 41 41 ARG CB C 13 30.145 . . . . . . . . . . . . 5130 1 356 . 1 1 41 41 ARG HB2 H 1 2.114 . . . . . . . . . . . . 5130 1 357 . 1 1 41 41 ARG HG2 H 1 1.744 . . . . . . . . . . . . 5130 1 358 . 1 1 41 41 ARG HG3 H 1 1.586 . . . . . . . . . . . . 5130 1 359 . 1 1 41 41 ARG HD2 H 1 3.259 . . . . . . . . . . . . 5130 1 360 . 1 1 42 42 ALA N N 15 122.801 . . . . . . . . . . . . 5130 1 361 . 1 1 42 42 ALA H H 1 6.788 . . . . . . . . . . . . 5130 1 362 . 1 1 42 42 ALA CA C 13 53.804 . . . . . . . . . . . . 5130 1 363 . 1 1 42 42 ALA HA H 1 4.048 . . . . . . . . . . . . 5130 1 364 . 1 1 42 42 ALA CB C 13 19.428 . . . . . . . . . . . . 5130 1 365 . 1 1 42 42 ALA HB1 H 1 1.342 . . . . . . . . . . . . 5130 1 366 . 1 1 42 42 ALA HB2 H 1 1.342 . . . . . . . . . . . . 5130 1 367 . 1 1 42 42 ALA HB3 H 1 1.342 . . . . . . . . . . . . 5130 1 368 . 1 1 43 43 THR N N 15 114.051 . . . . . . . . . . . . 5130 1 369 . 1 1 43 43 THR H H 1 8.225 . . . . . . . . . . . . 5130 1 370 . 1 1 43 43 THR CA C 13 60.553 . . . . . . . . . . . . 5130 1 371 . 1 1 43 43 THR HA H 1 5.274 . . . . . . . . . . . . 5130 1 372 . 1 1 43 43 THR CB C 13 73.115 . . . . . . . . . . . . 5130 1 373 . 1 1 43 43 THR HB H 1 3.788 . . . . . . . . . . . . 5130 1 374 . 1 1 43 43 THR HG21 H 1 1.125 . . . . . . . . . . . . 5130 1 375 . 1 1 43 43 THR HG22 H 1 1.125 . . . . . . . . . . . . 5130 1 376 . 1 1 43 43 THR HG23 H 1 1.125 . . . . . . . . . . . . 5130 1 377 . 1 1 44 44 ASN N N 15 119.321 . . . . . . . . . . . . 5130 1 378 . 1 1 44 44 ASN H H 1 8.115 . . . . . . . . . . . . 5130 1 379 . 1 1 44 44 ASN CA C 13 53.688 . . . . . . . . . . . . 5130 1 380 . 1 1 44 44 ASN HA H 1 5.06 . . . . . . . . . . . . 5130 1 381 . 1 1 44 44 ASN CB C 13 43.54 . . . . . . . . . . . . 5130 1 382 . 1 1 44 44 ASN HB2 H 1 2.797 . . . . . . . . . . . . 5130 1 383 . 1 1 45 45 TYR N N 15 127.64 . . . . . . . . . . . . 5130 1 384 . 1 1 45 45 TYR H H 1 8.944 . . . . . . . . . . . . 5130 1 385 . 1 1 45 45 TYR CA C 13 57.909 . . . . . . . . . . . . 5130 1 386 . 1 1 45 45 TYR HA H 1 4.857 . . . . . . . . . . . . 5130 1 387 . 1 1 45 45 TYR CB C 13 40.029 . . . . . . . . . . . . 5130 1 388 . 1 1 45 45 TYR HB2 H 1 3.048 . . . . . . . . . . . . 5130 1 389 . 1 1 45 45 TYR HB3 H 1 2.845 . . . . . . . . . . . . 5130 1 390 . 1 1 46 46 ASN N N 15 127.927 . . . . . . . . . . . . 5130 1 391 . 1 1 46 46 ASN H H 1 8.875 . . . . . . . . . . . . 5130 1 392 . 1 1 46 46 ASN CA C 13 51.903 . . . . . . . . . . . . 5130 1 393 . 1 1 46 46 ASN HA H 1 4.697 . . . . . . . . . . . . 5130 1 394 . 1 1 46 46 ASN CB C 13 39.287 . . . . . . . . . . . . 5130 1 395 . 1 1 46 46 ASN HB2 H 1 2.756 . . . . . . . . . . . . 5130 1 396 . 1 1 46 46 ASN HD21 H 1 7.998 . . . . . . . . . . . . 5130 1 397 . 1 1 46 46 ASN HD22 H 1 6.926 . . . . . . . . . . . . 5130 1 398 . 1 1 47 47 ALA N N 15 125.556 . . . . . . . . . . . . 5130 1 399 . 1 1 47 47 ALA H H 1 8.421 . . . . . . . . . . . . 5130 1 400 . 1 1 47 47 ALA CA C 13 54.773 . . . . . . . . . . . . 5130 1 401 . 1 1 47 47 ALA HA H 1 3.696 . . . . . . . . . . . . 5130 1 402 . 1 1 47 47 ALA CB C 13 18.771 . . . . . . . . . . . . 5130 1 403 . 1 1 47 47 ALA HB1 H 1 1.465 . . . . . . . . . . . . 5130 1 404 . 1 1 47 47 ALA HB2 H 1 1.465 . . . . . . . . . . . . 5130 1 405 . 1 1 47 47 ALA HB3 H 1 1.465 . . . . . . . . . . . . 5130 1 406 . 1 1 48 48 GLY N N 15 104.336 . . . . . . . . . . . . 5130 1 407 . 1 1 48 48 GLY H H 1 8.521 . . . . . . . . . . . . 5130 1 408 . 1 1 48 48 GLY CA C 13 47.422 . . . . . . . . . . . . 5130 1 409 . 1 1 48 48 GLY HA2 H 1 3.872 . . . . . . . . . . . . 5130 1 410 . 1 1 48 48 GLY HA3 H 1 3.828 . . . . . . . . . . . . 5130 1 411 . 1 1 49 49 ASP N N 15 116.994 . . . . . . . . . . . . 5130 1 412 . 1 1 49 49 ASP H H 1 7.156 . . . . . . . . . . . . 5130 1 413 . 1 1 49 49 ASP CA C 13 52.774 . . . . . . . . . . . . 5130 1 414 . 1 1 49 49 ASP HA H 1 4.736 . . . . . . . . . . . . 5130 1 415 . 1 1 49 49 ASP CB C 13 40.958 . . . . . . . . . . . . 5130 1 416 . 1 1 49 49 ASP HB2 H 1 2.91 . . . . . . . . . . . . 5130 1 417 . 1 1 49 49 ASP HB3 H 1 2.449 . . . . . . . . . . . . 5130 1 418 . 1 1 50 50 ARG N N 15 114.264 . . . . . . . . . . . . 5130 1 419 . 1 1 50 50 ARG H H 1 7.88 . . . . . . . . . . . . 5130 1 420 . 1 1 50 50 ARG CA C 13 57.79 . . . . . . . . . . . . 5130 1 421 . 1 1 50 50 ARG HA H 1 3.832 . . . . . . . . . . . . 5130 1 422 . 1 1 50 50 ARG CB C 13 27.468 . . . . . . . . . . . . 5130 1 423 . 1 1 50 50 ARG HB2 H 1 2.247 . . . . . . . . . . . . 5130 1 424 . 1 1 50 50 ARG HB3 H 1 2.1 . . . . . . . . . . . . 5130 1 425 . 1 1 50 50 ARG HG2 H 1 1.726 . . . . . . . . . . . . 5130 1 426 . 1 1 50 50 ARG HG3 H 1 1.639 . . . . . . . . . . . . 5130 1 427 . 1 1 50 50 ARG HD2 H 1 3.262 . . . . . . . . . . . . 5130 1 428 . 1 1 51 51 SER N N 15 114.057 . . . . . . . . . . . . 5130 1 429 . 1 1 51 51 SER H H 1 7.999 . . . . . . . . . . . . 5130 1 430 . 1 1 51 51 SER CA C 13 57.396 . . . . . . . . . . . . 5130 1 431 . 1 1 51 51 SER HA H 1 4.742 . . . . . . . . . . . . 5130 1 432 . 1 1 51 51 SER CB C 13 66.767 . . . . . . . . . . . . 5130 1 433 . 1 1 51 51 SER HB2 H 1 4.16 . . . . . . . . . . . . 5130 1 434 . 1 1 51 51 SER HB3 H 1 3.598 . . . . . . . . . . . . 5130 1 435 . 1 1 52 52 THR N N 15 116.36 . . . . . . . . . . . . 5130 1 436 . 1 1 52 52 THR H H 1 9.053 . . . . . . . . . . . . 5130 1 437 . 1 1 52 52 THR CA C 13 62.072 . . . . . . . . . . . . 5130 1 438 . 1 1 52 52 THR HA H 1 5.061 . . . . . . . . . . . . 5130 1 439 . 1 1 52 52 THR CB C 13 71.735 . . . . . . . . . . . . 5130 1 440 . 1 1 52 52 THR HB H 1 3.844 . . . . . . . . . . . . 5130 1 441 . 1 1 52 52 THR HG21 H 1 0.414 . . . . . . . . . . . . 5130 1 442 . 1 1 52 52 THR HG22 H 1 0.414 . . . . . . . . . . . . 5130 1 443 . 1 1 52 52 THR HG23 H 1 0.414 . . . . . . . . . . . . 5130 1 444 . 1 1 53 53 ASP N N 15 124.539 . . . . . . . . . . . . 5130 1 445 . 1 1 53 53 ASP H H 1 8.888 . . . . . . . . . . . . 5130 1 446 . 1 1 53 53 ASP CA C 13 52.399 . . . . . . . . . . . . 5130 1 447 . 1 1 53 53 ASP HA H 1 5.259 . . . . . . . . . . . . 5130 1 448 . 1 1 53 53 ASP CB C 13 42.306 . . . . . . . . . . . . 5130 1 449 . 1 1 53 53 ASP HB2 H 1 2.773 . . . . . . . . . . . . 5130 1 450 . 1 1 53 53 ASP HB3 H 1 2.061 . . . . . . . . . . . . 5130 1 451 . 1 1 54 54 TYR N N 15 118.503 . . . . . . . . . . . . 5130 1 452 . 1 1 54 54 TYR H H 1 9.134 . . . . . . . . . . . . 5130 1 453 . 1 1 54 54 TYR CA C 13 59.969 . . . . . . . . . . . . 5130 1 454 . 1 1 54 54 TYR HA H 1 4.837 . . . . . . . . . . . . 5130 1 455 . 1 1 54 54 TYR CB C 13 43.436 . . . . . . . . . . . . 5130 1 456 . 1 1 54 54 TYR HB2 H 1 3 . . . . . . . . . . . . 5130 1 457 . 1 1 54 54 TYR HB3 H 1 2.726 . . . . . . . . . . . . 5130 1 458 . 1 1 55 55 GLY N N 15 112.562 . . . . . . . . . . . . 5130 1 459 . 1 1 55 55 GLY H H 1 9.069 . . . . . . . . . . . . 5130 1 460 . 1 1 55 55 GLY CA C 13 46.895 . . . . . . . . . . . . 5130 1 461 . 1 1 55 55 GLY HA2 H 1 4.527 . . . . . . . . . . . . 5130 1 462 . 1 1 55 55 GLY HA3 H 1 4.479 . . . . . . . . . . . . 5130 1 463 . 1 1 56 56 ILE N N 15 121.805 . . . . . . . . . . . . 5130 1 464 . 1 1 56 56 ILE H H 1 9.215 . . . . . . . . . . . . 5130 1 465 . 1 1 56 56 ILE CA C 13 62.615 . . . . . . . . . . . . 5130 1 466 . 1 1 56 56 ILE HA H 1 4.132 . . . . . . . . . . . . 5130 1 467 . 1 1 56 56 ILE CB C 13 39.594 . . . . . . . . . . . . 5130 1 468 . 1 1 56 56 ILE HB H 1 1.746 . . . . . . . . . . . . 5130 1 469 . 1 1 56 56 ILE HG12 H 1 0.571 . . . . . . . . . . . . 5130 1 470 . 1 1 56 56 ILE HG13 H 1 0.391 . . . . . . . . . . . . 5130 1 471 . 1 1 56 56 ILE HG21 H 1 0.055 . . . . . . . . . . . . 5130 1 472 . 1 1 56 56 ILE HG22 H 1 0.055 . . . . . . . . . . . . 5130 1 473 . 1 1 56 56 ILE HG23 H 1 0.055 . . . . . . . . . . . . 5130 1 474 . 1 1 56 56 ILE HD11 H 1 1.206 . . . . . . . . . . . . 5130 1 475 . 1 1 56 56 ILE HD12 H 1 1.206 . . . . . . . . . . . . 5130 1 476 . 1 1 56 56 ILE HD13 H 1 1.206 . . . . . . . . . . . . 5130 1 477 . 1 1 57 57 PHE N N 15 115.646 . . . . . . . . . . . . 5130 1 478 . 1 1 57 57 PHE H H 1 8.296 . . . . . . . . . . . . 5130 1 479 . 1 1 57 57 PHE CA C 13 55.96 . . . . . . . . . . . . 5130 1 480 . 1 1 57 57 PHE HA H 1 4.672 . . . . . . . . . . . . 5130 1 481 . 1 1 57 57 PHE CB C 13 39.992 . . . . . . . . . . . . 5130 1 482 . 1 1 57 57 PHE HB2 H 1 3.478 . . . . . . . . . . . . 5130 1 483 . 1 1 57 57 PHE HB3 H 1 2.71 . . . . . . . . . . . . 5130 1 484 . 1 1 58 58 GLN N N 15 113.982 . . . . . . . . . . . . 5130 1 485 . 1 1 58 58 GLN H H 1 7.916 . . . . . . . . . . . . 5130 1 486 . 1 1 58 58 GLN CA C 13 55.59 . . . . . . . . . . . . 5130 1 487 . 1 1 58 58 GLN HA H 1 3.488 . . . . . . . . . . . . 5130 1 488 . 1 1 58 58 GLN CB C 13 27.331 . . . . . . . . . . . . 5130 1 489 . 1 1 58 58 GLN HB2 H 1 2.579 . . . . . . . . . . . . 5130 1 490 . 1 1 58 58 GLN HB3 H 1 2.599 . . . . . . . . . . . . 5130 1 491 . 1 1 58 58 GLN HG2 H 1 1.966 . . . . . . . . . . . . 5130 1 492 . 1 1 58 58 GLN HG3 H 1 1.991 . . . . . . . . . . . . 5130 1 493 . 1 1 58 58 GLN HE21 H 1 7.821 . . . . . . . . . . . . 5130 1 494 . 1 1 58 58 GLN HE22 H 1 7.245 . . . . . . . . . . . . 5130 1 495 . 1 1 59 59 ILE N N 15 122.23 . . . . . . . . . . . . 5130 1 496 . 1 1 59 59 ILE H H 1 7.881 . . . . . . . . . . . . 5130 1 497 . 1 1 59 59 ILE CA C 13 61.882 . . . . . . . . . . . . 5130 1 498 . 1 1 59 59 ILE HA H 1 4.358 . . . . . . . . . . . . 5130 1 499 . 1 1 59 59 ILE CB C 13 39.655 . . . . . . . . . . . . 5130 1 500 . 1 1 59 59 ILE HB H 1 1.938 . . . . . . . . . . . . 5130 1 501 . 1 1 59 59 ILE HG12 H 1 1.316 . . . . . . . . . . . . 5130 1 502 . 1 1 59 59 ILE HG21 H 1 1.316 . . . . . . . . . . . . 5130 1 503 . 1 1 59 59 ILE HG22 H 1 1.316 . . . . . . . . . . . . 5130 1 504 . 1 1 59 59 ILE HG23 H 1 1.316 . . . . . . . . . . . . 5130 1 505 . 1 1 59 59 ILE HD11 H 1 1.096 . . . . . . . . . . . . 5130 1 506 . 1 1 59 59 ILE HD12 H 1 1.096 . . . . . . . . . . . . 5130 1 507 . 1 1 59 59 ILE HD13 H 1 1.096 . . . . . . . . . . . . 5130 1 508 . 1 1 60 60 ASN N N 15 127.899 . . . . . . . . . . . . 5130 1 509 . 1 1 60 60 ASN H H 1 8.515 . . . . . . . . . . . . 5130 1 510 . 1 1 60 60 ASN CA C 13 56.545 . . . . . . . . . . . . 5130 1 511 . 1 1 60 60 ASN HA H 1 5.73 . . . . . . . . . . . . 5130 1 512 . 1 1 60 60 ASN CB C 13 44.162 . . . . . . . . . . . . 5130 1 513 . 1 1 60 60 ASN HB2 H 1 3.442 . . . . . . . . . . . . 5130 1 514 . 1 1 60 60 ASN HB3 H 1 3.021 . . . . . . . . . . . . 5130 1 515 . 1 1 60 60 ASN HD21 H 1 7.658 . . . . . . . . . . . . 5130 1 516 . 1 1 61 61 SER N N 15 119.565 . . . . . . . . . . . . 5130 1 517 . 1 1 61 61 SER H H 1 9.221 . . . . . . . . . . . . 5130 1 518 . 1 1 61 61 SER CA C 13 60.992 . . . . . . . . . . . . 5130 1 519 . 1 1 61 61 SER HA H 1 5.149 . . . . . . . . . . . . 5130 1 520 . 1 1 61 61 SER CB C 13 65.206 . . . . . . . . . . . . 5130 1 521 . 1 1 61 61 SER HB2 H 1 4.473 . . . . . . . . . . . . 5130 1 522 . 1 1 62 62 ARG N N 15 123.956 . . . . . . . . . . . . 5130 1 523 . 1 1 62 62 ARG H H 1 8.747 . . . . . . . . . . . . 5130 1 524 . 1 1 62 62 ARG CA C 13 58.941 . . . . . . . . . . . . 5130 1 525 . 1 1 62 62 ARG HA H 1 4.193 . . . . . . . . . . . . 5130 1 526 . 1 1 62 62 ARG CB C 13 29.982 . . . . . . . . . . . . 5130 1 527 . 1 1 62 62 ARG HB2 H 1 1.766 . . . . . . . . . . . . 5130 1 528 . 1 1 62 62 ARG HB3 H 1 1.459 . . . . . . . . . . . . 5130 1 529 . 1 1 62 62 ARG HG2 H 1 1.198 . . . . . . . . . . . . 5130 1 530 . 1 1 62 62 ARG HG3 H 1 0.825 . . . . . . . . . . . . 5130 1 531 . 1 1 62 62 ARG HD2 H 1 3.096 . . . . . . . . . . . . 5130 1 532 . 1 1 62 62 ARG HD3 H 1 3.009 . . . . . . . . . . . . 5130 1 533 . 1 1 63 63 TYR N N 15 114.62 . . . . . . . . . . . . 5130 1 534 . 1 1 63 63 TYR H H 1 7.315 . . . . . . . . . . . . 5130 1 535 . 1 1 63 63 TYR CA C 13 59.023 . . . . . . . . . . . . 5130 1 536 . 1 1 63 63 TYR HA H 1 4.34 . . . . . . . . . . . . 5130 1 537 . 1 1 63 63 TYR CB C 13 39.996 . . . . . . . . . . . . 5130 1 538 . 1 1 63 63 TYR HB2 H 1 1.611 . . . . . . . . . . . . 5130 1 539 . 1 1 63 63 TYR HB3 H 1 1.631 . . . . . . . . . . . . 5130 1 540 . 1 1 64 64 TRP N N 15 114.706 . . . . . . . . . . . . 5130 1 541 . 1 1 64 64 TRP H H 1 7.235 . . . . . . . . . . . . 5130 1 542 . 1 1 64 64 TRP CA C 13 59.325 . . . . . . . . . . . . 5130 1 543 . 1 1 64 64 TRP HA H 1 5.044 . . . . . . . . . . . . 5130 1 544 . 1 1 64 64 TRP CB C 13 33.939 . . . . . . . . . . . . 5130 1 545 . 1 1 64 64 TRP HB2 H 1 3.397 . . . . . . . . . . . . 5130 1 546 . 1 1 65 65 CYS N N 15 111.294 . . . . . . . . . . . . 5130 1 547 . 1 1 65 65 CYS H H 1 7.462 . . . . . . . . . . . . 5130 1 548 . 1 1 65 65 CYS CA C 13 53.221 . . . . . . . . . . . . 5130 1 549 . 1 1 65 65 CYS HA H 1 5.737 . . . . . . . . . . . . 5130 1 550 . 1 1 65 65 CYS CB C 13 45.849 . . . . . . . . . . . . 5130 1 551 . 1 1 65 65 CYS HB2 H 1 2.891 . . . . . . . . . . . . 5130 1 552 . 1 1 65 65 CYS HB3 H 1 2.517 . . . . . . . . . . . . 5130 1 553 . 1 1 66 66 ASN N N 15 119.416 . . . . . . . . . . . . 5130 1 554 . 1 1 66 66 ASN H H 1 8.709 . . . . . . . . . . . . 5130 1 555 . 1 1 66 66 ASN CA C 13 51.617 . . . . . . . . . . . . 5130 1 556 . 1 1 66 66 ASN HA H 1 5.634 . . . . . . . . . . . . 5130 1 557 . 1 1 66 66 ASN CB C 13 40.889 . . . . . . . . . . . . 5130 1 558 . 1 1 66 66 ASN HB2 H 1 2.899 . . . . . . . . . . . . 5130 1 559 . 1 1 66 66 ASN HB3 H 1 2.439 . . . . . . . . . . . . 5130 1 560 . 1 1 67 67 ASP N N 15 131.536 . . . . . . . . . . . . 5130 1 561 . 1 1 67 67 ASP H H 1 10.354 . . . . . . . . . . . . 5130 1 562 . 1 1 67 67 ASP CA C 13 51.948 . . . . . . . . . . . . 5130 1 563 . 1 1 67 67 ASP HA H 1 4.966 . . . . . . . . . . . . 5130 1 564 . 1 1 67 67 ASP CB C 13 41.528 . . . . . . . . . . . . 5130 1 565 . 1 1 67 67 ASP HB2 H 1 3.264 . . . . . . . . . . . . 5130 1 566 . 1 1 67 67 ASP HB3 H 1 2.294 . . . . . . . . . . . . 5130 1 567 . 1 1 68 68 GLY N N 15 108.663 . . . . . . . . . . . . 5130 1 568 . 1 1 68 68 GLY H H 1 8.252 . . . . . . . . . . . . 5130 1 569 . 1 1 68 68 GLY CA C 13 46.749 . . . . . . . . . . . . 5130 1 570 . 1 1 68 68 GLY HA2 H 1 4.143 . . . . . . . . . . . . 5130 1 571 . 1 1 68 68 GLY HA3 H 1 3.868 . . . . . . . . . . . . 5130 1 572 . 1 1 69 69 LYS N N 15 117.928 . . . . . . . . . . . . 5130 1 573 . 1 1 69 69 LYS H H 1 8.188 . . . . . . . . . . . . 5130 1 574 . 1 1 69 69 LYS CA C 13 55.638 . . . . . . . . . . . . 5130 1 575 . 1 1 69 69 LYS HA H 1 4.797 . . . . . . . . . . . . 5130 1 576 . 1 1 69 69 LYS CB C 13 34.175 . . . . . . . . . . . . 5130 1 577 . 1 1 69 69 LYS HB2 H 1 1.855 . . . . . . . . . . . . 5130 1 578 . 1 1 69 69 LYS HG3 H 1 1.652 . . . . . . . . . . . . 5130 1 579 . 1 1 69 69 LYS HD2 H 1 1.287 . . . . . . . . . . . . 5130 1 580 . 1 1 69 69 LYS HE2 H 1 2.993 . . . . . . . . . . . . 5130 1 581 . 1 1 70 70 THR N N 15 121.014 . . . . . . . . . . . . 5130 1 582 . 1 1 70 70 THR H H 1 8.342 . . . . . . . . . . . . 5130 1 583 . 1 1 70 70 THR CA C 13 60.636 . . . . . . . . . . . . 5130 1 584 . 1 1 70 70 THR HA H 1 4.807 . . . . . . . . . . . . 5130 1 585 . 1 1 70 70 THR CB C 13 70.834 . . . . . . . . . . . . 5130 1 586 . 1 1 70 70 THR HB H 1 4.158 . . . . . . . . . . . . 5130 1 587 . 1 1 70 70 THR HG21 H 1 1.092 . . . . . . . . . . . . 5130 1 588 . 1 1 70 70 THR HG22 H 1 1.092 . . . . . . . . . . . . 5130 1 589 . 1 1 70 70 THR HG23 H 1 1.092 . . . . . . . . . . . . 5130 1 590 . 1 1 71 71 PRO CA C 13 63.496 . . . . . . . . . . . . 5130 1 591 . 1 1 71 71 PRO HA H 1 4.404 . . . . . . . . . . . . 5130 1 592 . 1 1 71 71 PRO CB C 13 32.232 . . . . . . . . . . . . 5130 1 593 . 1 1 71 71 PRO HB2 H 1 2.323 . . . . . . . . . . . . 5130 1 594 . 1 1 71 71 PRO HG2 H 1 2.089 . . . . . . . . . . . . 5130 1 595 . 1 1 71 71 PRO HG3 H 1 1.959 . . . . . . . . . . . . 5130 1 596 . 1 1 71 71 PRO HD2 H 1 4.115 . . . . . . . . . . . . 5130 1 597 . 1 1 71 71 PRO HD3 H 1 3.894 . . . . . . . . . . . . 5130 1 598 . 1 1 72 72 GLY N N 15 110.275 . . . . . . . . . . . . 5130 1 599 . 1 1 72 72 GLY H H 1 8.697 . . . . . . . . . . . . 5130 1 600 . 1 1 72 72 GLY CA C 13 46.424 . . . . . . . . . . . . 5130 1 601 . 1 1 72 72 GLY HA2 H 1 3.867 . . . . . . . . . . . . 5130 1 602 . 1 1 72 72 GLY HA3 H 1 3.751 . . . . . . . . . . . . 5130 1 603 . 1 1 73 73 ALA N N 15 120.953 . . . . . . . . . . . . 5130 1 604 . 1 1 73 73 ALA H H 1 7.115 . . . . . . . . . . . . 5130 1 605 . 1 1 73 73 ALA CA C 13 53.08 . . . . . . . . . . . . 5130 1 606 . 1 1 73 73 ALA HA H 1 4.603 . . . . . . . . . . . . 5130 1 607 . 1 1 73 73 ALA CB C 13 20.925 . . . . . . . . . . . . 5130 1 608 . 1 1 73 73 ALA HB1 H 1 1.562 . . . . . . . . . . . . 5130 1 609 . 1 1 73 73 ALA HB2 H 1 1.562 . . . . . . . . . . . . 5130 1 610 . 1 1 73 73 ALA HB3 H 1 1.562 . . . . . . . . . . . . 5130 1 611 . 1 1 74 74 VAL N N 15 120.346 . . . . . . . . . . . . 5130 1 612 . 1 1 74 74 VAL H H 1 7.816 . . . . . . . . . . . . 5130 1 613 . 1 1 74 74 VAL CA C 13 63.151 . . . . . . . . . . . . 5130 1 614 . 1 1 74 74 VAL HA H 1 3.907 . . . . . . . . . . . . 5130 1 615 . 1 1 74 74 VAL CB C 13 34.081 . . . . . . . . . . . . 5130 1 616 . 1 1 74 74 VAL HB H 1 1.975 . . . . . . . . . . . . 5130 1 617 . 1 1 74 74 VAL HG11 H 1 0.959 . . . . . . . . . . . . 5130 1 618 . 1 1 74 74 VAL HG12 H 1 0.959 . . . . . . . . . . . . 5130 1 619 . 1 1 74 74 VAL HG13 H 1 0.959 . . . . . . . . . . . . 5130 1 620 . 1 1 74 74 VAL HG21 H 1 0.751 . . . . . . . . . . . . 5130 1 621 . 1 1 74 74 VAL HG22 H 1 0.751 . . . . . . . . . . . . 5130 1 622 . 1 1 74 74 VAL HG23 H 1 0.751 . . . . . . . . . . . . 5130 1 623 . 1 1 75 75 ASN N N 15 119.028 . . . . . . . . . . . . 5130 1 624 . 1 1 75 75 ASN H H 1 8.727 . . . . . . . . . . . . 5130 1 625 . 1 1 75 75 ASN CA C 13 51.962 . . . . . . . . . . . . 5130 1 626 . 1 1 75 75 ASN HA H 1 3.808 . . . . . . . . . . . . 5130 1 627 . 1 1 75 75 ASN CB C 13 37.535 . . . . . . . . . . . . 5130 1 628 . 1 1 75 75 ASN HB2 H 1 3.116 . . . . . . . . . . . . 5130 1 629 . 1 1 75 75 ASN HB3 H 1 1.978 . . . . . . . . . . . . 5130 1 630 . 1 1 75 75 ASN HD21 H 1 7.748 . . . . . . . . . . . . 5130 1 631 . 1 1 75 75 ASN HD22 H 1 7.146 . . . . . . . . . . . . 5130 1 632 . 1 1 76 76 ALA N N 15 120.577 . . . . . . . . . . . . 5130 1 633 . 1 1 76 76 ALA H H 1 8.359 . . . . . . . . . . . . 5130 1 634 . 1 1 76 76 ALA CA C 13 55.371 . . . . . . . . . . . . 5130 1 635 . 1 1 76 76 ALA HA H 1 4.062 . . . . . . . . . . . . 5130 1 636 . 1 1 76 76 ALA CB C 13 19.461 . . . . . . . . . . . . 5130 1 637 . 1 1 76 76 ALA HB1 H 1 1.477 . . . . . . . . . . . . 5130 1 638 . 1 1 76 76 ALA HB2 H 1 1.477 . . . . . . . . . . . . 5130 1 639 . 1 1 76 76 ALA HB3 H 1 1.477 . . . . . . . . . . . . 5130 1 640 . 1 1 77 77 CYS N N 15 111.151 . . . . . . . . . . . . 5130 1 641 . 1 1 77 77 CYS H H 1 9.38 . . . . . . . . . . . . 5130 1 642 . 1 1 77 77 CYS CA C 13 56.449 . . . . . . . . . . . . 5130 1 643 . 1 1 77 77 CYS HA H 1 4.383 . . . . . . . . . . . . 5130 1 644 . 1 1 77 77 CYS CB C 13 39.917 . . . . . . . . . . . . 5130 1 645 . 1 1 77 77 CYS HB2 H 1 3.51 . . . . . . . . . . . . 5130 1 646 . 1 1 77 77 CYS HB3 H 1 3.807 . . . . . . . . . . . . 5130 1 647 . 1 1 78 78 HIS N N 15 118.023 . . . . . . . . . . . . 5130 1 648 . 1 1 78 78 HIS H H 1 7.817 . . . . . . . . . . . . 5130 1 649 . 1 1 78 78 HIS CA C 13 56.204 . . . . . . . . . . . . 5130 1 650 . 1 1 78 78 HIS HA H 1 3.982 . . . . . . . . . . . . 5130 1 651 . 1 1 78 78 HIS CB C 13 26.112 . . . . . . . . . . . . 5130 1 652 . 1 1 78 78 HIS HB2 H 1 3.388 . . . . . . . . . . . . 5130 1 653 . 1 1 79 79 LEU N N 15 118.528 . . . . . . . . . . . . 5130 1 654 . 1 1 79 79 LEU H H 1 8.72 . . . . . . . . . . . . 5130 1 655 . 1 1 79 79 LEU CA C 13 54.196 . . . . . . . . . . . . 5130 1 656 . 1 1 79 79 LEU HA H 1 4.703 . . . . . . . . . . . . 5130 1 657 . 1 1 79 79 LEU CB C 13 47.372 . . . . . . . . . . . . 5130 1 658 . 1 1 79 79 LEU HB2 H 1 1.664 . . . . . . . . . . . . 5130 1 659 . 1 1 79 79 LEU HD11 H 1 1.25 . . . . . . . . . . . . 5130 1 660 . 1 1 79 79 LEU HD12 H 1 1.25 . . . . . . . . . . . . 5130 1 661 . 1 1 79 79 LEU HD13 H 1 1.25 . . . . . . . . . . . . 5130 1 662 . 1 1 79 79 LEU HD21 H 1 0.812 . . . . . . . . . . . . 5130 1 663 . 1 1 79 79 LEU HD22 H 1 0.812 . . . . . . . . . . . . 5130 1 664 . 1 1 79 79 LEU HD23 H 1 0.812 . . . . . . . . . . . . 5130 1 665 . 1 1 80 80 SER N N 15 117.653 . . . . . . . . . . . . 5130 1 666 . 1 1 80 80 SER H H 1 8.639 . . . . . . . . . . . . 5130 1 667 . 1 1 80 80 SER CA C 13 57.722 . . . . . . . . . . . . 5130 1 668 . 1 1 80 80 SER HA H 1 5.005 . . . . . . . . . . . . 5130 1 669 . 1 1 80 80 SER CB C 13 63.871 . . . . . . . . . . . . 5130 1 670 . 1 1 80 80 SER HB2 H 1 3.963 . . . . . . . . . . . . 5130 1 671 . 1 1 81 81 CYS N N 15 125.91 . . . . . . . . . . . . 5130 1 672 . 1 1 81 81 CYS H H 1 8.5 . . . . . . . . . . . . 5130 1 673 . 1 1 81 81 CYS CA C 13 57.323 . . . . . . . . . . . . 5130 1 674 . 1 1 81 81 CYS HA H 1 3.947 . . . . . . . . . . . . 5130 1 675 . 1 1 81 81 CYS CB C 13 37.891 . . . . . . . . . . . . 5130 1 676 . 1 1 81 81 CYS HB2 H 1 1.861 . . . . . . . . . . . . 5130 1 677 . 1 1 81 81 CYS HB3 H 1 1.181 . . . . . . . . . . . . 5130 1 678 . 1 1 82 82 SER N N 15 114.672 . . . . . . . . . . . . 5130 1 679 . 1 1 82 82 SER H H 1 8.378 . . . . . . . . . . . . 5130 1 680 . 1 1 82 82 SER CA C 13 61.683 . . . . . . . . . . . . 5130 1 681 . 1 1 82 82 SER HA H 1 3.903 . . . . . . . . . . . . 5130 1 682 . 1 1 82 82 SER HB2 H 1 1.683 . . . . . . . . . . . . 5130 1 683 . 1 1 83 83 ALA N N 15 125.947 . . . . . . . . . . . . 5130 1 684 . 1 1 83 83 ALA H H 1 7.81 . . . . . . . . . . . . 5130 1 685 . 1 1 83 83 ALA CA C 13 54.553 . . . . . . . . . . . . 5130 1 686 . 1 1 83 83 ALA HA H 1 4.35 . . . . . . . . . . . . 5130 1 687 . 1 1 83 83 ALA CB C 13 18.496 . . . . . . . . . . . . 5130 1 688 . 1 1 83 83 ALA HB1 H 1 1.679 . . . . . . . . . . . . 5130 1 689 . 1 1 83 83 ALA HB2 H 1 1.679 . . . . . . . . . . . . 5130 1 690 . 1 1 83 83 ALA HB3 H 1 1.679 . . . . . . . . . . . . 5130 1 691 . 1 1 84 84 LEU N N 15 116.688 . . . . . . . . . . . . 5130 1 692 . 1 1 84 84 LEU H H 1 7.876 . . . . . . . . . . . . 5130 1 693 . 1 1 84 84 LEU CA C 13 54.5 . . . . . . . . . . . . 5130 1 694 . 1 1 84 84 LEU HA H 1 4.338 . . . . . . . . . . . . 5130 1 695 . 1 1 84 84 LEU CB C 13 40.948 . . . . . . . . . . . . 5130 1 696 . 1 1 84 84 LEU HB2 H 1 2.228 . . . . . . . . . . . . 5130 1 697 . 1 1 84 84 LEU HB3 H 1 1.753 . . . . . . . . . . . . 5130 1 698 . 1 1 84 84 LEU HG H 1 1.735 . . . . . . . . . . . . 5130 1 699 . 1 1 84 84 LEU HD11 H 1 1.041 . . . . . . . . . . . . 5130 1 700 . 1 1 84 84 LEU HD12 H 1 1.041 . . . . . . . . . . . . 5130 1 701 . 1 1 84 84 LEU HD13 H 1 1.041 . . . . . . . . . . . . 5130 1 702 . 1 1 84 84 LEU HD21 H 1 0.802 . . . . . . . . . . . . 5130 1 703 . 1 1 84 84 LEU HD22 H 1 0.802 . . . . . . . . . . . . 5130 1 704 . 1 1 84 84 LEU HD23 H 1 0.802 . . . . . . . . . . . . 5130 1 705 . 1 1 85 85 LEU N N 15 117.659 . . . . . . . . . . . . 5130 1 706 . 1 1 85 85 LEU H H 1 7.164 . . . . . . . . . . . . 5130 1 707 . 1 1 85 85 LEU CA C 13 53.654 . . . . . . . . . . . . 5130 1 708 . 1 1 85 85 LEU HA H 1 5.633 . . . . . . . . . . . . 5130 1 709 . 1 1 85 85 LEU CB C 13 43.228 . . . . . . . . . . . . 5130 1 710 . 1 1 85 85 LEU HB2 H 1 1.777 . . . . . . . . . . . . 5130 1 711 . 1 1 85 85 LEU HG H 1 1.119 . . . . . . . . . . . . 5130 1 712 . 1 1 85 85 LEU HD11 H 1 1.04 . . . . . . . . . . . . 5130 1 713 . 1 1 85 85 LEU HD12 H 1 1.04 . . . . . . . . . . . . 5130 1 714 . 1 1 85 85 LEU HD13 H 1 1.04 . . . . . . . . . . . . 5130 1 715 . 1 1 85 85 LEU HD21 H 1 1.04 . . . . . . . . . . . . 5130 1 716 . 1 1 85 85 LEU HD22 H 1 1.04 . . . . . . . . . . . . 5130 1 717 . 1 1 85 85 LEU HD23 H 1 1.04 . . . . . . . . . . . . 5130 1 718 . 1 1 86 86 GLN N N 15 116.628 . . . . . . . . . . . . 5130 1 719 . 1 1 86 86 GLN H H 1 6.754 . . . . . . . . . . . . 5130 1 720 . 1 1 86 86 GLN CA C 13 55.093 . . . . . . . . . . . . 5130 1 721 . 1 1 86 86 GLN HA H 1 4.424 . . . . . . . . . . . . 5130 1 722 . 1 1 86 86 GLN CB C 13 31.27 . . . . . . . . . . . . 5130 1 723 . 1 1 86 86 GLN HB2 H 1 2.67 . . . . . . . . . . . . 5130 1 724 . 1 1 86 86 GLN HB3 H 1 2.495 . . . . . . . . . . . . 5130 1 725 . 1 1 86 86 GLN HG2 H 1 2.063 . . . . . . . . . . . . 5130 1 726 . 1 1 86 86 GLN HG3 H 1 2.073 . . . . . . . . . . . . 5130 1 727 . 1 1 87 87 ASP N N 15 120.244 . . . . . . . . . . . . 5130 1 728 . 1 1 87 87 ASP H H 1 8.698 . . . . . . . . . . . . 5130 1 729 . 1 1 87 87 ASP CA C 13 57.394 . . . . . . . . . . . . 5130 1 730 . 1 1 87 87 ASP HA H 1 4.222 . . . . . . . . . . . . 5130 1 731 . 1 1 87 87 ASP CB C 13 40.499 . . . . . . . . . . . . 5130 1 732 . 1 1 87 87 ASP HB2 H 1 2.641 . . . . . . . . . . . . 5130 1 733 . 1 1 87 87 ASP HB3 H 1 2.506 . . . . . . . . . . . . 5130 1 734 . 1 1 88 88 ASN N N 15 114.457 . . . . . . . . . . . . 5130 1 735 . 1 1 88 88 ASN H H 1 7.396 . . . . . . . . . . . . 5130 1 736 . 1 1 88 88 ASN CA C 13 52.516 . . . . . . . . . . . . 5130 1 737 . 1 1 88 88 ASN HA H 1 4.895 . . . . . . . . . . . . 5130 1 738 . 1 1 88 88 ASN CB C 13 38.579 . . . . . . . . . . . . 5130 1 739 . 1 1 88 88 ASN HB2 H 1 3.018 . . . . . . . . . . . . 5130 1 740 . 1 1 88 88 ASN HB3 H 1 2.834 . . . . . . . . . . . . 5130 1 741 . 1 1 89 89 ILE N N 15 118.83 . . . . . . . . . . . . 5130 1 742 . 1 1 89 89 ILE H H 1 8.248 . . . . . . . . . . . . 5130 1 743 . 1 1 89 89 ILE CA C 13 61.865 . . . . . . . . . . . . 5130 1 744 . 1 1 89 89 ILE HA H 1 4.623 . . . . . . . . . . . . 5130 1 745 . 1 1 89 89 ILE CB C 13 39.009 . . . . . . . . . . . . 5130 1 746 . 1 1 89 89 ILE HB H 1 2.106 . . . . . . . . . . . . 5130 1 747 . 1 1 89 89 ILE HG12 H 1 1.303 . . . . . . . . . . . . 5130 1 748 . 1 1 89 89 ILE HG21 H 1 1.003 . . . . . . . . . . . . 5130 1 749 . 1 1 89 89 ILE HG22 H 1 1.003 . . . . . . . . . . . . 5130 1 750 . 1 1 89 89 ILE HG23 H 1 1.003 . . . . . . . . . . . . 5130 1 751 . 1 1 89 89 ILE HD11 H 1 0.284 . . . . . . . . . . . . 5130 1 752 . 1 1 89 89 ILE HD12 H 1 0.284 . . . . . . . . . . . . 5130 1 753 . 1 1 89 89 ILE HD13 H 1 0.284 . . . . . . . . . . . . 5130 1 754 . 1 1 90 90 ALA N N 15 126.104 . . . . . . . . . . . . 5130 1 755 . 1 1 90 90 ALA H H 1 8.192 . . . . . . . . . . . . 5130 1 756 . 1 1 90 90 ALA CA C 13 57.269 . . . . . . . . . . . . 5130 1 757 . 1 1 90 90 ALA HA H 1 3.869 . . . . . . . . . . . . 5130 1 758 . 1 1 90 90 ALA CB C 13 18.091 . . . . . . . . . . . . 5130 1 759 . 1 1 90 90 ALA HB1 H 1 1.463 . . . . . . . . . . . . 5130 1 760 . 1 1 90 90 ALA HB2 H 1 1.463 . . . . . . . . . . . . 5130 1 761 . 1 1 90 90 ALA HB3 H 1 1.463 . . . . . . . . . . . . 5130 1 762 . 1 1 91 91 ASP N N 15 118.493 . . . . . . . . . . . . 5130 1 763 . 1 1 91 91 ASP H H 1 9.038 . . . . . . . . . . . . 5130 1 764 . 1 1 91 91 ASP CA C 13 57.019 . . . . . . . . . . . . 5130 1 765 . 1 1 91 91 ASP HA H 1 4.515 . . . . . . . . . . . . 5130 1 766 . 1 1 91 91 ASP CB C 13 38.611 . . . . . . . . . . . . 5130 1 767 . 1 1 91 91 ASP HB2 H 1 2.692 . . . . . . . . . . . . 5130 1 768 . 1 1 91 91 ASP HB3 H 1 2.482 . . . . . . . . . . . . 5130 1 769 . 1 1 92 92 ALA N N 15 123.204 . . . . . . . . . . . . 5130 1 770 . 1 1 92 92 ALA H H 1 7.679 . . . . . . . . . . . . 5130 1 771 . 1 1 92 92 ALA CA C 13 55.91 . . . . . . . . . . . . 5130 1 772 . 1 1 92 92 ALA HA H 1 3.986 . . . . . . . . . . . . 5130 1 773 . 1 1 92 92 ALA CB C 13 17.996 . . . . . . . . . . . . 5130 1 774 . 1 1 92 92 ALA HB1 H 1 1.582 . . . . . . . . . . . . 5130 1 775 . 1 1 92 92 ALA HB2 H 1 1.582 . . . . . . . . . . . . 5130 1 776 . 1 1 92 92 ALA HB3 H 1 1.582 . . . . . . . . . . . . 5130 1 777 . 1 1 93 93 VAL N N 15 118.291 . . . . . . . . . . . . 5130 1 778 . 1 1 93 93 VAL H H 1 8.623 . . . . . . . . . . . . 5130 1 779 . 1 1 93 93 VAL CA C 13 67.225 . . . . . . . . . . . . 5130 1 780 . 1 1 93 93 VAL HA H 1 3.269 . . . . . . . . . . . . 5130 1 781 . 1 1 93 93 VAL CB C 13 31.357 . . . . . . . . . . . . 5130 1 782 . 1 1 93 93 VAL HB H 1 2.179 . . . . . . . . . . . . 5130 1 783 . 1 1 93 93 VAL HG11 H 1 0.853 . . . . . . . . . . . . 5130 1 784 . 1 1 93 93 VAL HG12 H 1 0.853 . . . . . . . . . . . . 5130 1 785 . 1 1 93 93 VAL HG13 H 1 0.853 . . . . . . . . . . . . 5130 1 786 . 1 1 93 93 VAL HG21 H 1 0.853 . . . . . . . . . . . . 5130 1 787 . 1 1 93 93 VAL HG22 H 1 0.853 . . . . . . . . . . . . 5130 1 788 . 1 1 93 93 VAL HG23 H 1 0.853 . . . . . . . . . . . . 5130 1 789 . 1 1 94 94 ALA N N 15 121.62 . . . . . . . . . . . . 5130 1 790 . 1 1 94 94 ALA H H 1 8.03 . . . . . . . . . . . . 5130 1 791 . 1 1 94 94 ALA CA C 13 55.839 . . . . . . . . . . . . 5130 1 792 . 1 1 94 94 ALA HA H 1 3.883 . . . . . . . . . . . . 5130 1 793 . 1 1 94 94 ALA CB C 13 18.139 . . . . . . . . . . . . 5130 1 794 . 1 1 94 94 ALA HB1 H 1 1.552 . . . . . . . . . . . . 5130 1 795 . 1 1 94 94 ALA HB2 H 1 1.552 . . . . . . . . . . . . 5130 1 796 . 1 1 94 94 ALA HB3 H 1 1.552 . . . . . . . . . . . . 5130 1 797 . 1 1 95 95 CYS N N 15 115.939 . . . . . . . . . . . . 5130 1 798 . 1 1 95 95 CYS H H 1 8.307 . . . . . . . . . . . . 5130 1 799 . 1 1 95 95 CYS CA C 13 55.344 . . . . . . . . . . . . 5130 1 800 . 1 1 95 95 CYS HA H 1 4.962 . . . . . . . . . . . . 5130 1 801 . 1 1 95 95 CYS CB C 13 35.337 . . . . . . . . . . . . 5130 1 802 . 1 1 95 95 CYS HB2 H 1 3.345 . . . . . . . . . . . . 5130 1 803 . 1 1 95 95 CYS HB3 H 1 2.684 . . . . . . . . . . . . 5130 1 804 . 1 1 96 96 ALA N N 15 124.455 . . . . . . . . . . . . 5130 1 805 . 1 1 96 96 ALA H H 1 8.826 . . . . . . . . . . . . 5130 1 806 . 1 1 96 96 ALA CA C 13 56.369 . . . . . . . . . . . . 5130 1 807 . 1 1 96 96 ALA HA H 1 3.794 . . . . . . . . . . . . 5130 1 808 . 1 1 96 96 ALA CB C 13 17.731 . . . . . . . . . . . . 5130 1 809 . 1 1 96 96 ALA HB1 H 1 0.872 . . . . . . . . . . . . 5130 1 810 . 1 1 96 96 ALA HB2 H 1 0.872 . . . . . . . . . . . . 5130 1 811 . 1 1 96 96 ALA HB3 H 1 0.872 . . . . . . . . . . . . 5130 1 812 . 1 1 97 97 LYS N N 15 114.307 . . . . . . . . . . . . 5130 1 813 . 1 1 97 97 LYS H H 1 7.968 . . . . . . . . . . . . 5130 1 814 . 1 1 97 97 LYS CA C 13 60.219 . . . . . . . . . . . . 5130 1 815 . 1 1 97 97 LYS HA H 1 3.646 . . . . . . . . . . . . 5130 1 816 . 1 1 97 97 LYS CB C 13 33.231 . . . . . . . . . . . . 5130 1 817 . 1 1 97 97 LYS HB2 H 1 1.647 . . . . . . . . . . . . 5130 1 818 . 1 1 97 97 LYS HG2 H 1 1.309 . . . . . . . . . . . . 5130 1 819 . 1 1 97 97 LYS HG3 H 1 1.123 . . . . . . . . . . . . 5130 1 820 . 1 1 97 97 LYS HD2 H 1 2.221 . . . . . . . . . . . . 5130 1 821 . 1 1 97 97 LYS HD3 H 1 1.964 . . . . . . . . . . . . 5130 1 822 . 1 1 97 97 LYS HE2 H 1 -0.42 . . . . . . . . . . . . 5130 1 823 . 1 1 97 97 LYS HE3 H 1 0.008 . . . . . . . . . . . . 5130 1 824 . 1 1 98 98 ARG N N 15 118.441 . . . . . . . . . . . . 5130 1 825 . 1 1 98 98 ARG H H 1 7.142 . . . . . . . . . . . . 5130 1 826 . 1 1 98 98 ARG CA C 13 58.468 . . . . . . . . . . . . 5130 1 827 . 1 1 98 98 ARG HA H 1 4.089 . . . . . . . . . . . . 5130 1 828 . 1 1 98 98 ARG CB C 13 28.768 . . . . . . . . . . . . 5130 1 829 . 1 1 98 98 ARG HB2 H 1 1.812 . . . . . . . . . . . . 5130 1 830 . 1 1 98 98 ARG HB3 H 1 1.683 . . . . . . . . . . . . 5130 1 831 . 1 1 98 98 ARG HG3 H 1 2.014 . . . . . . . . . . . . 5130 1 832 . 1 1 98 98 ARG HD2 H 1 2.62 . . . . . . . . . . . . 5130 1 833 . 1 1 98 98 ARG HD3 H 1 2.477 . . . . . . . . . . . . 5130 1 834 . 1 1 99 99 VAL N N 15 123.427 . . . . . . . . . . . . 5130 1 835 . 1 1 99 99 VAL H H 1 8.303 . . . . . . . . . . . . 5130 1 836 . 1 1 99 99 VAL CA C 13 66.072 . . . . . . . . . . . . 5130 1 837 . 1 1 99 99 VAL HA H 1 2.483 . . . . . . . . . . . . 5130 1 838 . 1 1 99 99 VAL CB C 13 30.96 . . . . . . . . . . . . 5130 1 839 . 1 1 99 99 VAL HB H 1 1.886 . . . . . . . . . . . . 5130 1 840 . 1 1 99 99 VAL HG11 H 1 -0.343 . . . . . . . . . . . . 5130 1 841 . 1 1 99 99 VAL HG12 H 1 -0.343 . . . . . . . . . . . . 5130 1 842 . 1 1 99 99 VAL HG13 H 1 -0.343 . . . . . . . . . . . . 5130 1 843 . 1 1 99 99 VAL HG21 H 1 -0.576 . . . . . . . . . . . . 5130 1 844 . 1 1 99 99 VAL HG22 H 1 -0.576 . . . . . . . . . . . . 5130 1 845 . 1 1 99 99 VAL HG23 H 1 -0.576 . . . . . . . . . . . . 5130 1 846 . 1 1 100 100 VAL N N 15 108.312 . . . . . . . . . . . . 5130 1 847 . 1 1 100 100 VAL H H 1 7.462 . . . . . . . . . . . . 5130 1 848 . 1 1 100 100 VAL CA C 13 63.527 . . . . . . . . . . . . 5130 1 849 . 1 1 100 100 VAL HA H 1 3.915 . . . . . . . . . . . . 5130 1 850 . 1 1 100 100 VAL CB C 13 31.444 . . . . . . . . . . . . 5130 1 851 . 1 1 100 100 VAL HB H 1 2.45 . . . . . . . . . . . . 5130 1 852 . 1 1 100 100 VAL HG11 H 1 1.39 . . . . . . . . . . . . 5130 1 853 . 1 1 100 100 VAL HG12 H 1 1.39 . . . . . . . . . . . . 5130 1 854 . 1 1 100 100 VAL HG13 H 1 1.39 . . . . . . . . . . . . 5130 1 855 . 1 1 100 100 VAL HG21 H 1 1.111 . . . . . . . . . . . . 5130 1 856 . 1 1 100 100 VAL HG22 H 1 1.111 . . . . . . . . . . . . 5130 1 857 . 1 1 100 100 VAL HG23 H 1 1.111 . . . . . . . . . . . . 5130 1 858 . 1 1 101 101 ARG N N 15 119.387 . . . . . . . . . . . . 5130 1 859 . 1 1 101 101 ARG H H 1 7.55 . . . . . . . . . . . . 5130 1 860 . 1 1 101 101 ARG CA C 13 58.566 . . . . . . . . . . . . 5130 1 861 . 1 1 101 101 ARG HA H 1 4.176 . . . . . . . . . . . . 5130 1 862 . 1 1 101 101 ARG CB C 13 31.165 . . . . . . . . . . . . 5130 1 863 . 1 1 101 101 ARG HB2 H 1 2.474 . . . . . . . . . . . . 5130 1 864 . 1 1 101 101 ARG HB3 H 1 2.087 . . . . . . . . . . . . 5130 1 865 . 1 1 101 101 ARG HG2 H 1 2.138 . . . . . . . . . . . . 5130 1 866 . 1 1 101 101 ARG HG3 H 1 1.481 . . . . . . . . . . . . 5130 1 867 . 1 1 101 101 ARG HD2 H 1 3.46 . . . . . . . . . . . . 5130 1 868 . 1 1 101 101 ARG HD3 H 1 3.332 . . . . . . . . . . . . 5130 1 869 . 1 1 102 102 ASP N N 15 121.469 . . . . . . . . . . . . 5130 1 870 . 1 1 102 102 ASP H H 1 7.4 . . . . . . . . . . . . 5130 1 871 . 1 1 102 102 ASP CA C 13 54.023 . . . . . . . . . . . . 5130 1 872 . 1 1 102 102 ASP HA H 1 4.926 . . . . . . . . . . . . 5130 1 873 . 1 1 102 102 ASP CB C 13 39.787 . . . . . . . . . . . . 5130 1 874 . 1 1 102 102 ASP HB2 H 1 3.026 . . . . . . . . . . . . 5130 1 875 . 1 1 103 103 PRO CA C 13 66.494 . . . . . . . . . . . . 5130 1 876 . 1 1 103 103 PRO HA H 1 4.228 . . . . . . . . . . . . 5130 1 877 . 1 1 103 103 PRO CB C 13 32.443 . . . . . . . . . . . . 5130 1 878 . 1 1 103 103 PRO HB2 H 1 2.408 . . . . . . . . . . . . 5130 1 879 . 1 1 103 103 PRO HG2 H 1 2.123 . . . . . . . . . . . . 5130 1 880 . 1 1 103 103 PRO HG3 H 1 1.894 . . . . . . . . . . . . 5130 1 881 . 1 1 103 103 PRO HD2 H 1 3.837 . . . . . . . . . . . . 5130 1 882 . 1 1 104 104 GLN N N 15 113.753 . . . . . . . . . . . . 5130 1 883 . 1 1 104 104 GLN H H 1 8.468 . . . . . . . . . . . . 5130 1 884 . 1 1 104 104 GLN CA C 13 57.718 . . . . . . . . . . . . 5130 1 885 . 1 1 104 104 GLN HA H 1 4.13 . . . . . . . . . . . . 5130 1 886 . 1 1 104 104 GLN CB C 13 29.178 . . . . . . . . . . . . 5130 1 887 . 1 1 104 104 GLN HB2 H 1 2.319 . . . . . . . . . . . . 5130 1 888 . 1 1 104 104 GLN HG3 H 1 2.564 . . . . . . . . . . . . 5130 1 889 . 1 1 105 105 GLY N N 15 108.837 . . . . . . . . . . . . 5130 1 890 . 1 1 105 105 GLY H H 1 8.086 . . . . . . . . . . . . 5130 1 891 . 1 1 105 105 GLY CA C 13 46.378 . . . . . . . . . . . . 5130 1 892 . 1 1 105 105 GLY HA2 H 1 4.011 . . . . . . . . . . . . 5130 1 893 . 1 1 105 105 GLY HA3 H 1 4.001 . . . . . . . . . . . . 5130 1 894 . 1 1 106 106 ILE N N 15 126.629 . . . . . . . . . . . . 5130 1 895 . 1 1 106 106 ILE H H 1 8.483 . . . . . . . . . . . . 5130 1 896 . 1 1 106 106 ILE CA C 13 62.856 . . . . . . . . . . . . 5130 1 897 . 1 1 106 106 ILE HA H 1 3.994 . . . . . . . . . . . . 5130 1 898 . 1 1 106 106 ILE CB C 13 39.17 . . . . . . . . . . . . 5130 1 899 . 1 1 106 106 ILE HB H 1 0.916 . . . . . . . . . . . . 5130 1 900 . 1 1 106 106 ILE HG12 H 1 0.195 . . . . . . . . . . . . 5130 1 901 . 1 1 106 106 ILE HG21 H 1 -0.451 . . . . . . . . . . . . 5130 1 902 . 1 1 106 106 ILE HG22 H 1 -0.451 . . . . . . . . . . . . 5130 1 903 . 1 1 106 106 ILE HG23 H 1 -0.451 . . . . . . . . . . . . 5130 1 904 . 1 1 106 106 ILE HD11 H 1 -0.629 . . . . . . . . . . . . 5130 1 905 . 1 1 106 106 ILE HD12 H 1 -0.629 . . . . . . . . . . . . 5130 1 906 . 1 1 106 106 ILE HD13 H 1 -0.629 . . . . . . . . . . . . 5130 1 907 . 1 1 107 107 ARG N N 15 116.868 . . . . . . . . . . . . 5130 1 908 . 1 1 107 107 ARG H H 1 7.315 . . . . . . . . . . . . 5130 1 909 . 1 1 107 107 ARG CA C 13 58.042 . . . . . . . . . . . . 5130 1 910 . 1 1 107 107 ARG HA H 1 4.113 . . . . . . . . . . . . 5130 1 911 . 1 1 107 107 ARG CB C 13 29.497 . . . . . . . . . . . . 5130 1 912 . 1 1 107 107 ARG HB2 H 1 2.112 . . . . . . . . . . . . 5130 1 913 . 1 1 107 107 ARG HB3 H 1 2.067 . . . . . . . . . . . . 5130 1 914 . 1 1 107 107 ARG HG3 H 1 1.818 . . . . . . . . . . . . 5130 1 915 . 1 1 107 107 ARG HD2 H 1 3.383 . . . . . . . . . . . . 5130 1 916 . 1 1 108 108 ALA N N 15 120.306 . . . . . . . . . . . . 5130 1 917 . 1 1 108 108 ALA H H 1 7.231 . . . . . . . . . . . . 5130 1 918 . 1 1 108 108 ALA CA C 13 54.444 . . . . . . . . . . . . 5130 1 919 . 1 1 108 108 ALA HA H 1 3.846 . . . . . . . . . . . . 5130 1 920 . 1 1 108 108 ALA CB C 13 19.106 . . . . . . . . . . . . 5130 1 921 . 1 1 108 108 ALA HB1 H 1 0.914 . . . . . . . . . . . . 5130 1 922 . 1 1 108 108 ALA HB2 H 1 0.914 . . . . . . . . . . . . 5130 1 923 . 1 1 108 108 ALA HB3 H 1 0.914 . . . . . . . . . . . . 5130 1 924 . 1 1 109 109 TRP N N 15 116.299 . . . . . . . . . . . . 5130 1 925 . 1 1 109 109 TRP H H 1 7.492 . . . . . . . . . . . . 5130 1 926 . 1 1 109 109 TRP CA C 13 59.694 . . . . . . . . . . . . 5130 1 927 . 1 1 109 109 TRP HA H 1 4.842 . . . . . . . . . . . . 5130 1 928 . 1 1 109 109 TRP CB C 13 30.121 . . . . . . . . . . . . 5130 1 929 . 1 1 109 109 TRP HB2 H 1 3.254 . . . . . . . . . . . . 5130 1 930 . 1 1 110 110 VAL N N 15 128.39 . . . . . . . . . . . . 5130 1 931 . 1 1 110 110 VAL H H 1 8.823 . . . . . . . . . . . . 5130 1 932 . 1 1 110 110 VAL CA C 13 66.665 . . . . . . . . . . . . 5130 1 933 . 1 1 110 110 VAL HA H 1 3.657 . . . . . . . . . . . . 5130 1 934 . 1 1 110 110 VAL CB C 13 31.966 . . . . . . . . . . . . 5130 1 935 . 1 1 110 110 VAL HB H 1 2.193 . . . . . . . . . . . . 5130 1 936 . 1 1 110 110 VAL HG11 H 1 1.161 . . . . . . . . . . . . 5130 1 937 . 1 1 110 110 VAL HG12 H 1 1.161 . . . . . . . . . . . . 5130 1 938 . 1 1 110 110 VAL HG13 H 1 1.161 . . . . . . . . . . . . 5130 1 939 . 1 1 110 110 VAL HG21 H 1 1.059 . . . . . . . . . . . . 5130 1 940 . 1 1 110 110 VAL HG22 H 1 1.059 . . . . . . . . . . . . 5130 1 941 . 1 1 110 110 VAL HG23 H 1 1.059 . . . . . . . . . . . . 5130 1 942 . 1 1 111 111 ALA N N 15 119.562 . . . . . . . . . . . . 5130 1 943 . 1 1 111 111 ALA H H 1 8.648 . . . . . . . . . . . . 5130 1 944 . 1 1 111 111 ALA CA C 13 55.54 . . . . . . . . . . . . 5130 1 945 . 1 1 111 111 ALA HA H 1 4.229 . . . . . . . . . . . . 5130 1 946 . 1 1 111 111 ALA CB C 13 18.463 . . . . . . . . . . . . 5130 1 947 . 1 1 111 111 ALA HB1 H 1 1.436 . . . . . . . . . . . . 5130 1 948 . 1 1 111 111 ALA HB2 H 1 1.436 . . . . . . . . . . . . 5130 1 949 . 1 1 111 111 ALA HB3 H 1 1.436 . . . . . . . . . . . . 5130 1 950 . 1 1 112 112 TRP N N 15 114.721 . . . . . . . . . . . . 5130 1 951 . 1 1 112 112 TRP H H 1 7.379 . . . . . . . . . . . . 5130 1 952 . 1 1 112 112 TRP CA C 13 62.98 . . . . . . . . . . . . 5130 1 953 . 1 1 112 112 TRP HA H 1 3.792 . . . . . . . . . . . . 5130 1 954 . 1 1 112 112 TRP CB C 13 29.029 . . . . . . . . . . . . 5130 1 955 . 1 1 112 112 TRP HB2 H 1 3.109 . . . . . . . . . . . . 5130 1 956 . 1 1 112 112 TRP HB3 H 1 2.836 . . . . . . . . . . . . 5130 1 957 . 1 1 113 113 ARG N N 15 119.275 . . . . . . . . . . . . 5130 1 958 . 1 1 113 113 ARG H H 1 7.747 . . . . . . . . . . . . 5130 1 959 . 1 1 113 113 ARG CA C 13 59.952 . . . . . . . . . . . . 5130 1 960 . 1 1 113 113 ARG HA H 1 3.776 . . . . . . . . . . . . 5130 1 961 . 1 1 113 113 ARG CB C 13 30.63 . . . . . . . . . . . . 5130 1 962 . 1 1 113 113 ARG HB2 H 1 2.206 . . . . . . . . . . . . 5130 1 963 . 1 1 113 113 ARG HG2 H 1 1.945 . . . . . . . . . . . . 5130 1 964 . 1 1 113 113 ARG HG3 H 1 1.743 . . . . . . . . . . . . 5130 1 965 . 1 1 113 113 ARG HD2 H 1 3.578 . . . . . . . . . . . . 5130 1 966 . 1 1 113 113 ARG HD3 H 1 3.334 . . . . . . . . . . . . 5130 1 967 . 1 1 114 114 ASN N N 15 113.165 . . . . . . . . . . . . 5130 1 968 . 1 1 114 114 ASN H H 1 7.859 . . . . . . . . . . . . 5130 1 969 . 1 1 114 114 ASN CA C 13 54.858 . . . . . . . . . . . . 5130 1 970 . 1 1 114 114 ASN HA H 1 4.482 . . . . . . . . . . . . 5130 1 971 . 1 1 114 114 ASN CB C 13 39.477 . . . . . . . . . . . . 5130 1 972 . 1 1 114 114 ASN HB2 H 1 2.627 . . . . . . . . . . . . 5130 1 973 . 1 1 114 114 ASN HB3 H 1 2.798 . . . . . . . . . . . . 5130 1 974 . 1 1 115 115 ARG N N 15 114.016 . . . . . . . . . . . . 5130 1 975 . 1 1 115 115 ARG H H 1 7.787 . . . . . . . . . . . . 5130 1 976 . 1 1 115 115 ARG CA C 13 54.919 . . . . . . . . . . . . 5130 1 977 . 1 1 115 115 ARG HA H 1 4.009 . . . . . . . . . . . . 5130 1 978 . 1 1 115 115 ARG CB C 13 31.767 . . . . . . . . . . . . 5130 1 979 . 1 1 115 115 ARG HB2 H 1 1.325 . . . . . . . . . . . . 5130 1 980 . 1 1 115 115 ARG HB3 H 1 1.043 . . . . . . . . . . . . 5130 1 981 . 1 1 115 115 ARG HG2 H 1 0.619 . . . . . . . . . . . . 5130 1 982 . 1 1 115 115 ARG HG3 H 1 0.258 . . . . . . . . . . . . 5130 1 983 . 1 1 115 115 ARG HD2 H 1 2.205 . . . . . . . . . . . . 5130 1 984 . 1 1 116 116 CYS N N 15 114.709 . . . . . . . . . . . . 5130 1 985 . 1 1 116 116 CYS H H 1 7.313 . . . . . . . . . . . . 5130 1 986 . 1 1 116 116 CYS CA C 13 55.082 . . . . . . . . . . . . 5130 1 987 . 1 1 116 116 CYS HA H 1 4.368 . . . . . . . . . . . . 5130 1 988 . 1 1 116 116 CYS CB C 13 44.394 . . . . . . . . . . . . 5130 1 989 . 1 1 116 116 CYS HB2 H 1 2.518 . . . . . . . . . . . . 5130 1 990 . 1 1 116 116 CYS HB3 H 1 1.692 . . . . . . . . . . . . 5130 1 991 . 1 1 117 117 GLN N N 15 121.003 . . . . . . . . . . . . 5130 1 992 . 1 1 117 117 GLN H H 1 6.652 . . . . . . . . . . . . 5130 1 993 . 1 1 117 117 GLN CA C 13 57.576 . . . . . . . . . . . . 5130 1 994 . 1 1 117 117 GLN HA H 1 3.159 . . . . . . . . . . . . 5130 1 995 . 1 1 117 117 GLN CB C 13 28.754 . . . . . . . . . . . . 5130 1 996 . 1 1 117 117 GLN HB2 H 1 1.655 . . . . . . . . . . . . 5130 1 997 . 1 1 117 117 GLN HG3 H 1 0.698 . . . . . . . . . . . . 5130 1 998 . 1 1 118 118 ASN N N 15 119.82 . . . . . . . . . . . . 5130 1 999 . 1 1 118 118 ASN H H 1 9.082 . . . . . . . . . . . . 5130 1 1000 . 1 1 118 118 ASN CA C 13 54.885 . . . . . . . . . . . . 5130 1 1001 . 1 1 118 118 ASN HA H 1 4.423 . . . . . . . . . . . . 5130 1 1002 . 1 1 118 118 ASN CB C 13 37.657 . . . . . . . . . . . . 5130 1 1003 . 1 1 118 118 ASN HB2 H 1 3.052 . . . . . . . . . . . . 5130 1 1004 . 1 1 118 118 ASN HB3 H 1 2.9 . . . . . . . . . . . . 5130 1 1005 . 1 1 119 119 ARG N N 15 116.716 . . . . . . . . . . . . 5130 1 1006 . 1 1 119 119 ARG H H 1 7.444 . . . . . . . . . . . . 5130 1 1007 . 1 1 119 119 ARG CA C 13 54.01 . . . . . . . . . . . . 5130 1 1008 . 1 1 119 119 ARG HA H 1 4.585 . . . . . . . . . . . . 5130 1 1009 . 1 1 119 119 ARG CB C 13 32.581 . . . . . . . . . . . . 5130 1 1010 . 1 1 119 119 ARG HB2 H 1 2.936 . . . . . . . . . . . . 5130 1 1011 . 1 1 119 119 ARG HB3 H 1 2.766 . . . . . . . . . . . . 5130 1 1012 . 1 1 119 119 ARG HG2 H 1 1.769 . . . . . . . . . . . . 5130 1 1013 . 1 1 119 119 ARG HG3 H 1 1.78 . . . . . . . . . . . . 5130 1 1014 . 1 1 119 119 ARG HD2 H 1 4.288 . . . . . . . . . . . . 5130 1 1015 . 1 1 120 120 ASP N N 15 119.358 . . . . . . . . . . . . 5130 1 1016 . 1 1 120 120 ASP H H 1 8.445 . . . . . . . . . . . . 5130 1 1017 . 1 1 120 120 ASP CA C 13 54.423 . . . . . . . . . . . . 5130 1 1018 . 1 1 120 120 ASP HA H 1 4.736 . . . . . . . . . . . . 5130 1 1019 . 1 1 120 120 ASP CB C 13 40.171 . . . . . . . . . . . . 5130 1 1020 . 1 1 120 120 ASP HB2 H 1 2.918 . . . . . . . . . . . . 5130 1 1021 . 1 1 120 120 ASP HB3 H 1 2.725 . . . . . . . . . . . . 5130 1 1022 . 1 1 121 121 VAL N N 15 119.071 . . . . . . . . . . . . 5130 1 1023 . 1 1 121 121 VAL H H 1 8.514 . . . . . . . . . . . . 5130 1 1024 . 1 1 121 121 VAL CA C 13 61.644 . . . . . . . . . . . . 5130 1 1025 . 1 1 121 121 VAL HA H 1 4.819 . . . . . . . . . . . . 5130 1 1026 . 1 1 121 121 VAL CB C 13 32.396 . . . . . . . . . . . . 5130 1 1027 . 1 1 121 121 VAL HB H 1 2.702 . . . . . . . . . . . . 5130 1 1028 . 1 1 121 121 VAL HG11 H 1 1.173 . . . . . . . . . . . . 5130 1 1029 . 1 1 121 121 VAL HG12 H 1 1.173 . . . . . . . . . . . . 5130 1 1030 . 1 1 121 121 VAL HG13 H 1 1.173 . . . . . . . . . . . . 5130 1 1031 . 1 1 121 121 VAL HG21 H 1 0.889 . . . . . . . . . . . . 5130 1 1032 . 1 1 121 121 VAL HG22 H 1 0.889 . . . . . . . . . . . . 5130 1 1033 . 1 1 121 121 VAL HG23 H 1 0.889 . . . . . . . . . . . . 5130 1 1034 . 1 1 122 122 ARG N N 15 123.27 . . . . . . . . . . . . 5130 1 1035 . 1 1 122 122 ARG H H 1 8.28 . . . . . . . . . . . . 5130 1 1036 . 1 1 122 122 ARG CA C 13 60 . . . . . . . . . . . . 5130 1 1037 . 1 1 122 122 ARG HA H 1 3.96 . . . . . . . . . . . . 5130 1 1038 . 1 1 122 122 ARG CB C 13 29.879 . . . . . . . . . . . . 5130 1 1039 . 1 1 122 122 ARG HB2 H 1 2.011 . . . . . . . . . . . . 5130 1 1040 . 1 1 122 122 ARG HB3 H 1 1.956 . . . . . . . . . . . . 5130 1 1041 . 1 1 122 122 ARG HG3 H 1 1.825 . . . . . . . . . . . . 5130 1 1042 . 1 1 122 122 ARG HD2 H 1 3.257 . . . . . . . . . . . . 5130 1 1043 . 1 1 122 122 ARG HD3 H 1 3.298 . . . . . . . . . . . . 5130 1 1044 . 1 1 123 123 GLN N N 15 116.049 . . . . . . . . . . . . 5130 1 1045 . 1 1 123 123 GLN H H 1 8.715 . . . . . . . . . . . . 5130 1 1046 . 1 1 123 123 GLN CA C 13 58.076 . . . . . . . . . . . . 5130 1 1047 . 1 1 123 123 GLN HA H 1 4.085 . . . . . . . . . . . . 5130 1 1048 . 1 1 123 123 GLN CB C 13 27.985 . . . . . . . . . . . . 5130 1 1049 . 1 1 123 123 GLN HB2 H 1 1.828 . . . . . . . . . . . . 5130 1 1050 . 1 1 123 123 GLN HG3 H 1 1.363 . . . . . . . . . . . . 5130 1 1051 . 1 1 124 124 TYR N N 15 116.751 . . . . . . . . . . . . 5130 1 1052 . 1 1 124 124 TYR H H 1 7.585 . . . . . . . . . . . . 5130 1 1053 . 1 1 124 124 TYR CA C 13 62.537 . . . . . . . . . . . . 5130 1 1054 . 1 1 124 124 TYR HA H 1 4.167 . . . . . . . . . . . . 5130 1 1055 . 1 1 124 124 TYR CB C 13 39.13 . . . . . . . . . . . . 5130 1 1056 . 1 1 124 124 TYR HB2 H 1 3.233 . . . . . . . . . . . . 5130 1 1057 . 1 1 124 124 TYR HB3 H 1 2.982 . . . . . . . . . . . . 5130 1 1058 . 1 1 125 125 VAL N N 15 104.745 . . . . . . . . . . . . 5130 1 1059 . 1 1 125 125 VAL H H 1 7.272 . . . . . . . . . . . . 5130 1 1060 . 1 1 125 125 VAL CA C 13 60.341 . . . . . . . . . . . . 5130 1 1061 . 1 1 125 125 VAL HA H 1 4.531 . . . . . . . . . . . . 5130 1 1062 . 1 1 125 125 VAL CB C 13 33.316 . . . . . . . . . . . . 5130 1 1063 . 1 1 125 125 VAL HB H 1 2.344 . . . . . . . . . . . . 5130 1 1064 . 1 1 125 125 VAL HG11 H 1 0.964 . . . . . . . . . . . . 5130 1 1065 . 1 1 125 125 VAL HG12 H 1 0.964 . . . . . . . . . . . . 5130 1 1066 . 1 1 125 125 VAL HG13 H 1 0.964 . . . . . . . . . . . . 5130 1 1067 . 1 1 125 125 VAL HG21 H 1 0.826 . . . . . . . . . . . . 5130 1 1068 . 1 1 125 125 VAL HG22 H 1 0.826 . . . . . . . . . . . . 5130 1 1069 . 1 1 125 125 VAL HG23 H 1 0.826 . . . . . . . . . . . . 5130 1 1070 . 1 1 126 126 GLN N N 15 124.589 . . . . . . . . . . . . 5130 1 1071 . 1 1 126 126 GLN H H 1 7.38 . . . . . . . . . . . . 5130 1 1072 . 1 1 126 126 GLN CA C 13 57.851 . . . . . . . . . . . . 5130 1 1073 . 1 1 126 126 GLN HA H 1 4.205 . . . . . . . . . . . . 5130 1 1074 . 1 1 126 126 GLN CB C 13 28.821 . . . . . . . . . . . . 5130 1 1075 . 1 1 126 126 GLN HB2 H 1 2.103 . . . . . . . . . . . . 5130 1 1076 . 1 1 126 126 GLN HB3 H 1 2.002 . . . . . . . . . . . . 5130 1 1077 . 1 1 126 126 GLN HG2 H 1 2.415 . . . . . . . . . . . . 5130 1 1078 . 1 1 126 126 GLN HG3 H 1 2.401 . . . . . . . . . . . . 5130 1 1079 . 1 1 127 127 GLY N N 15 113.537 . . . . . . . . . . . . 5130 1 1080 . 1 1 127 127 GLY H H 1 9.138 . . . . . . . . . . . . 5130 1 1081 . 1 1 127 127 GLY CA C 13 46.078 . . . . . . . . . . . . 5130 1 1082 . 1 1 127 127 GLY HA2 H 1 4.303 . . . . . . . . . . . . 5130 1 1083 . 1 1 127 127 GLY HA3 H 1 3.875 . . . . . . . . . . . . 5130 1 1084 . 1 1 128 128 CYS N N 15 114.401 . . . . . . . . . . . . 5130 1 1085 . 1 1 128 128 CYS H H 1 7.645 . . . . . . . . . . . . 5130 1 1086 . 1 1 128 128 CYS CA C 13 52.34 . . . . . . . . . . . . 5130 1 1087 . 1 1 128 128 CYS HA H 1 4.946 . . . . . . . . . . . . 5130 1 1088 . 1 1 128 128 CYS CB C 13 35.395 . . . . . . . . . . . . 5130 1 1089 . 1 1 128 128 CYS HB2 H 1 3.215 . . . . . . . . . . . . 5130 1 1090 . 1 1 128 128 CYS HB3 H 1 2.707 . . . . . . . . . . . . 5130 1 1091 . 1 1 129 129 GLY N N 15 111.709 . . . . . . . . . . . . 5130 1 1092 . 1 1 129 129 GLY H H 1 8.874 . . . . . . . . . . . . 5130 1 1093 . 1 1 129 129 GLY CA C 13 47.212 . . . . . . . . . . . . 5130 1 1094 . 1 1 129 129 GLY HA2 H 1 3.975 . . . . . . . . . . . . 5130 1 1095 . 1 1 129 129 GLY HA3 H 1 3.924 . . . . . . . . . . . . 5130 1 1096 . 1 1 130 130 VAL N N 15 116.635 . . . . . . . . . . . . 5130 1 1097 . 1 1 130 130 VAL H H 1 7.454 . . . . . . . . . . . . 5130 1 1098 . 1 1 130 130 VAL CA C 13 61.647 . . . . . . . . . . . . 5130 1 1099 . 1 1 130 130 VAL HA H 1 4.304 . . . . . . . . . . . . 5130 1 1100 . 1 1 130 130 VAL CB C 13 33.79 . . . . . . . . . . . . 5130 1 1101 . 1 1 130 130 VAL HB H 1 2.192 . . . . . . . . . . . . 5130 1 1102 . 1 1 130 130 VAL HG11 H 1 1.474 . . . . . . . . . . . . 5130 1 1103 . 1 1 130 130 VAL HG12 H 1 1.474 . . . . . . . . . . . . 5130 1 1104 . 1 1 130 130 VAL HG13 H 1 1.474 . . . . . . . . . . . . 5130 1 1105 . 1 1 130 130 VAL HG21 H 1 1.347 . . . . . . . . . . . . 5130 1 1106 . 1 1 130 130 VAL HG22 H 1 1.347 . . . . . . . . . . . . 5130 1 1107 . 1 1 130 130 VAL HG23 H 1 1.347 . . . . . . . . . . . . 5130 1 stop_ save_