data_495 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 495 _Entry.Title ; Two-Dimensional NMR Studies of Staphylococcal Nuclease. 1. Sequence-Specific Assignments of Hydrogen-1 Signals and Solution Structure of the Nuclease H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-03-25 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Jinfeng Wang . . . 495 2 David LeMaster . M. . 495 3 John Markley . L. . 495 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 495 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 538 495 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 4 . . 2010-06-11 . revision BMRB 'Complete natural source information' 495 3 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 495 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 495 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 495 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 495 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Wang, Jinfeng, LeMaster, David M., Markley, John L., "Two-Dimensional NMR Studies of Staphylococcal Nuclease. 1. Sequence-Specific Assignments of Hydrogen-1 Signals and Solution Structure of the Nuclease H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex," Biochemistry 29, 88-101 (1990). ; _Citation.Title ; Two-Dimensional NMR Studies of Staphylococcal Nuclease. 1. Sequence-Specific Assignments of Hydrogen-1 Signals and Solution Structure of the Nuclease H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 29 _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 88 _Citation.Page_last 101 _Citation.Year 1990 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Jinfeng Wang . . . 495 1 2 David LeMaster . M. . 495 1 3 John Markley . L. . 495 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_micrococcal_nuclease _Assembly.Sf_category assembly _Assembly.Sf_framecode system_micrococcal_nuclease _Assembly.Entry_ID 495 _Assembly.ID 1 _Assembly.Name 'micrococcal nuclease' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic . _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'micrococcal nuclease' 1 $micrococcal_nuclease . . . . . . . . . 495 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'micrococcal nuclease' system 495 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_micrococcal_nuclease _Entity.Sf_category entity _Entity.Sf_framecode micrococcal_nuclease _Entity.Entry_ID 495 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'micrococcal nuclease' _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 ; ATSTKKLHKEPATLIKAIDG DTVKLMYKGQPMTFRLLLVD TPETKHPKKGVEKYGPEASA FTKKMVENAKKIEVEFDKGQ RTDKYGRGLAYIYADGKMVN EALVRQGLAKVAYVYKPNNT HEQLLRKSEAQAKKEKLNIW SED ; _Entity.Polymer_seq_one_letter_code ; ATSTKKLHKEPATLIKAIDG DTVKLMYKGQPMTFRLLLVD TPETKHPKKGVEKYGPEASA FTKKMVENAKKIEVEFDKGQ RTDKYGRGLAYIYADGKMVN EALVRQGLAKVAYVYKPNNT HEQLLRKSEAQAKKEKLNIW SED ; _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 143 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number 3.1.31.1 _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 136 . "micrococcal nuclease" . . . . . 100.00 156 97.90 99.30 5.17e-96 . . . . 495 1 2 no BMRB 1581 . "micrococcal nuclease" . . . . . 96.50 156 97.83 99.28 1.82e-92 . . . . 495 1 3 no BMRB 1582 . "micrococcal nuclease" . . . . . 96.50 156 97.10 99.28 7.45e-92 . . . . 495 1 4 no BMRB 16585 . SNase140 . . . . . 97.90 140 100.00 100.00 2.49e-96 . . . . 495 1 5 no BMRB 1704 . "micrococcal nuclease" . . . . . 100.00 143 100.00 100.00 1.10e-98 . . . . 495 1 6 no BMRB 17718 . Staphylococcal_nuclease . . . . . 100.00 149 100.00 100.00 1.02e-98 . . . . 495 1 7 no BMRB 18013 . SNase_PHS . . . . . 100.00 149 98.60 99.30 9.05e-97 . . . . 495 1 8 no BMRB 1874 . "micrococcal nuclease" . . . . . 100.00 143 100.00 100.00 1.10e-98 . . . . 495 1 9 no BMRB 1875 . "micrococcal nuclease" . . . . . 100.00 143 100.00 100.00 1.10e-98 . . . . 495 1 10 no BMRB 1876 . "micrococcal nuclease" . . . . . 100.00 143 100.00 100.00 1.10e-98 . . . . 495 1 11 no BMRB 1877 . "micrococcal nuclease" . . . . . 100.00 143 100.00 100.00 1.10e-98 . . . . 495 1 12 no BMRB 1878 . "micrococcal nuclease" . . . . . 100.00 143 100.00 100.00 1.10e-98 . . . . 495 1 13 no BMRB 18788 . staph_nuc_E43S . . . . . 100.00 149 99.30 99.30 4.44e-98 . . . . 495 1 14 no BMRB 188 . "micrococcal nuclease" . . . . . 100.00 156 97.90 99.30 5.17e-96 . . . . 495 1 15 no BMRB 189 . "micrococcal nuclease" . . . . . 100.00 156 97.90 99.30 5.17e-96 . . . . 495 1 16 no BMRB 2784 . "micrococcal nuclease" . . . . . 100.00 156 97.90 99.30 5.17e-96 . . . . 495 1 17 no BMRB 2785 . "micrococcal nuclease" . . . . . 100.00 156 97.90 99.30 5.17e-96 . . . . 495 1 18 no BMRB 4010 . SNOB . . . . . 72.03 103 98.06 99.03 3.27e-65 . . . . 495 1 19 no BMRB 4052 . staph-nucl-H124L . . . . . 100.00 149 100.00 100.00 1.02e-98 . . . . 495 1 20 no BMRB 4053 . staph-nucl-H124L . . . . . 100.00 149 100.00 100.00 1.02e-98 . . . . 495 1 21 no BMRB 4905 . Snase . . . . . 76.92 110 99.09 99.09 7.14e-71 . . . . 495 1 22 no BMRB 494 . "micrococcal nuclease" . . . . . 100.00 143 100.00 100.00 1.10e-98 . . . . 495 1 23 no BMRB 496 . "micrococcal nuclease" . . . . . 100.00 143 100.00 100.00 1.10e-98 . . . . 495 1 24 no BMRB 497 . "micrococcal nuclease" . . . . . 100.00 143 100.00 100.00 1.10e-98 . . . . 495 1 25 no BMRB 530 . "micrococcal nuclease" . . . . . 100.00 143 100.00 100.00 1.10e-98 . . . . 495 1 26 no BMRB 5536 . G88W110_Snase . . . . . 76.92 110 99.09 99.09 7.14e-71 . . . . 495 1 27 no BMRB 6250 . G88W121 . . . . . 84.62 121 99.17 99.17 3.37e-80 . . . . 495 1 28 no BMRB 6251 . V66W121 . . . . . 84.62 121 99.17 99.17 2.45e-80 . . . . 495 1 29 no BMRB 644 . "micrococcal nuclease" . . . . . 100.00 156 97.90 99.30 5.17e-96 . . . . 495 1 30 no BMRB 6907 . V66W110_fragment_of_staphylococcal_nuclease . . . . . 76.92 110 99.09 99.09 5.15e-71 . . . . 495 1 31 no BMRB 6908 . SNase110_fragment_of_Staphylococcal_Nuclease . . . . . 76.92 110 100.00 100.00 2.62e-72 . . . . 495 1 32 no PDB 1A2T . "Staphylococcal Nuclease, B-Mercaptoethanol Disulfide To V23c Variant" . . . . . 100.00 149 98.60 98.60 8.57e-97 . . . . 495 1 33 no PDB 1A2U . "Staphylococcal Nuclease, V23c Variant, Complex With 1-N- Butane Thiol And 3',5'-Thymidine Diphosphate" . . . . . 100.00 149 98.60 98.60 8.57e-97 . . . . 495 1 34 no PDB 1A3T . "Staphylococcal Nuclease, V23c Variant, Complex With 2- Fluoroethane Thiol And 3',5'-Thymidine Diphosphate" . . . . . 100.00 149 98.60 98.60 8.57e-97 . . . . 495 1 35 no PDB 1A3U . "Staphylococcal Nuclease, Cyclohexane Thiol Disulfide To V23c Variant" . . . . . 100.00 149 98.60 98.60 8.57e-97 . . . . 495 1 36 no PDB 1A3V . "Staphylococcal Nuclease, Cyclopentane Thiol Disulfide To V23c Variant" . . . . . 100.00 149 98.60 98.60 8.57e-97 . . . . 495 1 37 no PDB 1AEX . "Staphylococcal Nuclease, Methane Thiol Disulfide To V23c Variant" . . . . . 100.00 149 98.60 98.60 8.57e-97 . . . . 495 1 38 no PDB 1ENA . "Crystal Structures Of The Binary Ca2+ And Pdtp Complexes And The Ternary Complex Of The Asp 21->glu Mutant Of Staphylococcal Nu" . . . . . 94.41 135 98.52 99.26 4.10e-91 . . . . 495 1 39 no PDB 1ENC . "Crystal Structures Of The Binary Ca2+ And Pdtp Complexes And The Ternary Complex Of The Asp 21->glu Mutant Of Staphylococcal Nu" . . . . . 100.00 149 98.60 99.30 6.89e-97 . . . . 495 1 40 no PDB 1EY0 . "Structure Of Wild-Type S. Nuclease At 1.6 A Resolution" . . . . . 100.00 149 99.30 99.30 1.46e-97 . . . . 495 1 41 no PDB 1EY4 . "Structure Of S. Nuclease Stabilizing Mutant S59a" . . . . . 100.00 149 98.60 99.30 4.86e-97 . . . . 495 1 42 no PDB 1EY5 . "Structure Of S. Nuclease Stabilizing Mutant T33v" . . . . . 100.00 149 98.60 98.60 7.04e-97 . . . . 495 1 43 no PDB 1EY6 . "Structure Of S. Nuclease Stabilizing Mutant T41i" . . . . . 100.00 149 98.60 98.60 1.03e-96 . . . . 495 1 44 no PDB 1EY7 . "Structure Of S. Nuclease Stabilizing Mutant S128a" . . . . . 100.00 149 98.60 99.30 4.86e-97 . . . . 495 1 45 no PDB 1EY8 . "Structure Of S. Nuclease Stabilizing Triple Mutant P117gH124LS128A" . . . . . 100.00 149 98.60 99.30 9.05e-97 . . . . 495 1 46 no PDB 1EY9 . "Structure Of S. Nuclease Stabilizing Quadruple Mutant T41iP117GH124LS128A" . . . . . 100.00 149 97.90 98.60 6.47e-96 . . . . 495 1 47 no PDB 1EYA . "Structure Of S. Nuclease Stabilizing Quintuple Mutant T33vT41IP117GH124LS128A" . . . . . 100.00 149 97.20 97.90 2.98e-95 . . . . 495 1 48 no PDB 1EYC . "Structure Of S. Nuclease Stabilizing Quintuple Mutant T41iS59AP117GH124LS128A" . . . . . 100.00 149 97.20 98.60 1.42e-95 . . . . 495 1 49 no PDB 1EYD . "Structure Of Wild-Type S. Nuclease At 1.7 A Resolution" . . . . . 100.00 149 99.30 99.30 1.46e-97 . . . . 495 1 50 no PDB 1EZ8 . "Structure Of S. Nuclease Stabilizing Mutant T33v" . . . . . 100.00 149 98.60 98.60 7.04e-97 . . . . 495 1 51 no PDB 1F2M . "Simplification Of A Protein Loop In Staphylococcal Nuclease" . . . . . 100.00 149 97.90 97.90 3.51e-96 . . . . 495 1 52 no PDB 1F2Y . "Simplification Of A Protein Loop In Staphylococcal Nuclease" . . . . . 100.00 149 97.90 97.90 1.23e-95 . . . . 495 1 53 no PDB 1F2Z . "Simplification Of A Protein Loop In Staphylococcal Nuclease" . . . . . 100.00 149 97.90 97.90 1.23e-95 . . . . 495 1 54 no PDB 1JOK . "Averaged Structure For Staphylococcal Nuclease-H124l In Ternary Complex With Ca2+ And Thymidine-3',5'-Bisphosphate" . . . . . 100.00 149 100.00 100.00 1.02e-98 . . . . 495 1 55 no PDB 1JOO . "Averaged Structure For Unligated Staphylococcal Nuclease- H124l" . . . . . 100.00 149 100.00 100.00 1.02e-98 . . . . 495 1 56 no PDB 1JOQ . "Ensemble Structures For Staphylococcal Nuclease-H124l In Ternary Complex With Ca2+ And Thymidine-3',5'-Bisphosphate" . . . . . 100.00 149 100.00 100.00 1.02e-98 . . . . 495 1 57 no PDB 1JOR . "Ensemble Structures For Unligated Staphylococcal Nuclease- H124l" . . . . . 100.00 149 100.00 100.00 1.02e-98 . . . . 495 1 58 no PDB 1KAA . "Stress And Strain In Staphylococcal Nuclease" . . . . . 95.10 136 98.53 98.53 1.21e-91 . . . . 495 1 59 no PDB 1KAB . "Stress And Strain In Staphylococcal Nuclease" . . . . . 95.10 136 98.53 98.53 2.54e-91 . . . . 495 1 60 no PDB 1KDA . "Stabilization Of A Strained Protein Loop Conformation Through Protein Engineering" . . . . . 100.00 149 97.90 98.60 4.36e-96 . . . . 495 1 61 no PDB 1KDB . "Stabilization Of A Strained Protein Loop Conformation Through Protein Engineering" . . . . . 100.00 149 97.90 99.30 2.95e-96 . . . . 495 1 62 no PDB 1KDC . "Stabilization Of A Strained Protein Loop Conformation Through Protein Engineering" . . . . . 100.00 149 97.90 98.60 3.29e-96 . . . . 495 1 63 no PDB 1NSN . "The Crystal Structure Of Antibody N10-Staphylococcal Nuclease Complex At 2.9 Angstroms Resolution" . . . . . 100.00 149 98.60 99.30 7.85e-97 . . . . 495 1 64 no PDB 1NUC . "Staphylococcal Nuclease, V23c Variant" . . . . . 100.00 149 98.60 98.60 4.45e-97 . . . . 495 1 65 no PDB 1RKN . "Solution Structure Of 1-110 Fragment Of Staphylococcal Nuclease With G88w Mutation" . . . . . 76.92 110 99.09 99.09 7.14e-71 . . . . 495 1 66 no PDB 1SNC . "The Crystal Structure Of The Ternary Complex Of Staphylococcal Nuclease, Ca2+, And The Inhibitor PdTp, Refined At 1.65 Angstrom" . . . . . 100.00 149 99.30 99.30 1.46e-97 . . . . 495 1 67 no PDB 1SNM . "Active Site Mutant Glu-43 (Right Arrow) Asp In Staphylococcal Nuclease Displays Nonlocal Structural Changes" . . . . . 100.00 149 98.60 99.30 5.42e-97 . . . . 495 1 68 no PDB 1SNO . "Protein Stability In Staphylococcal Nuclease" . . . . . 100.00 149 100.00 100.00 1.02e-98 . . . . 495 1 69 no PDB 1SNP . "Protein Stability In Staphylococcal Nuclease" . . . . . 100.00 149 99.30 99.30 2.88e-97 . . . . 495 1 70 no PDB 1SNQ . "Protein Stability In Staphylococcal Nuclease" . . . . . 100.00 149 98.60 98.60 3.66e-96 . . . . 495 1 71 no PDB 1STA . "Accommodation Of Insertion Mutations On The Surface And In The Interior Of Staphylococcal Nuclease" . . . . . 101.40 151 97.93 97.93 2.30e-95 . . . . 495 1 72 no PDB 1STB . "Accommodation Of Insertion Mutations On The Surface And In The Interior Of Staphylococcal Nuclease" . . . . . 100.70 150 98.61 98.61 1.21e-95 . . . . 495 1 73 no PDB 1STG . "Two Distinctly Different Metal Binding Modes Are Seen In X- Ray Crystal Structures Of Staphylococcal Nuclease- Cobalt(Ii)-Nucle" . . . . . 100.00 149 99.30 99.30 1.46e-97 . . . . 495 1 74 no PDB 1STH . "Two Distinctly Different Metal Binding Modes Are Seen In X- Ray Crystal Structures Of Staphylococcal Nuclease- Cobalt(Ii)-Nucle" . . . . . 100.00 149 99.30 99.30 1.46e-97 . . . . 495 1 75 no PDB 1STN . "The Crystal Structure Of Staphylococcal Nuclease Refined At 1.7 Angstroms Resolution" . . . . . 100.00 149 99.30 99.30 1.46e-97 . . . . 495 1 76 no PDB 1STY . "The Alpha Aneurism: A Structural Motif Revealed In An Insertion Mutant Of Staphylococcal Nuclease" . . . . . 100.70 150 98.61 98.61 1.32e-95 . . . . 495 1 77 no PDB 1SYC . "Engineering Alternative Beta-Turn Types In Staphylococcal Nuclease" . . . . . 100.00 149 98.60 98.60 3.75e-96 . . . . 495 1 78 no PDB 1SYD . "Engineering Alternative Beta-Turn Types In Staphylococcal Nuclease" . . . . . 100.00 149 98.60 98.60 3.75e-96 . . . . 495 1 79 no PDB 1SYE . "Engineering Alternative Beta-Turn Types In Staphylococcal Nuclease" . . . . . 100.00 149 98.60 98.60 2.05e-96 . . . . 495 1 80 no PDB 1SYF . "Engineering Alternative Beta-Turn Types In Staphylococcal Nuclease" . . . . . 100.00 149 98.60 98.60 2.05e-96 . . . . 495 1 81 no PDB 1SYG . "Engineering Alternative Beta-Turn Types In Staphylococcal Nuclease" . . . . . 100.00 149 98.60 98.60 1.69e-96 . . . . 495 1 82 no PDB 1U9R . "Crystal Structure Of Staphylococcal Nuclease Mutant V66eP117GH124LS128A AT ROOM TEMPERATURE" . . . . . 100.00 149 97.90 98.60 9.48e-96 . . . . 495 1 83 no PDB 2ENB . "Crystal Structures Of The Binary Ca2+ And Pdtp Complexes And The Ternary Complex Of The Asp 21->glu Mutant Of Staphylococcal Nu" . . . . . 94.41 135 98.52 99.26 4.10e-91 . . . . 495 1 84 no PDB 2EXZ . "Crystal Structure Of Staphylococcal Nuclease Mutant T22c" . . . . . 100.00 149 98.60 98.60 5.07e-97 . . . . 495 1 85 no PDB 2EY1 . "Crystal Structure Of Staphylococcal Nuclease Mutant T22v" . . . . . 100.00 149 98.60 98.60 7.04e-97 . . . . 495 1 86 no PDB 2EY2 . "Crystal Structure Of Staphylococcal Nuclease Mutant T41c" . . . . . 100.00 149 98.60 98.60 5.07e-97 . . . . 495 1 87 no PDB 2EY5 . "Crystal Structure Of Staphylococcal Nuclease Mutant T41s" . . . . . 100.00 149 98.60 99.30 3.70e-97 . . . . 495 1 88 no PDB 2EY6 . "Crystal Structure Of Staphylococcal Nuclease Mutant T41v" . . . . . 100.00 149 98.60 98.60 7.04e-97 . . . . 495 1 89 no PDB 2EYF . "Crystal Structure Of Staphylococcal Nuclease Mutant T44v" . . . . . 100.00 149 98.60 98.60 7.04e-97 . . . . 495 1 90 no PDB 2EYH . "Crystal Structure Of Staphylococcal Nuclease Mutant T62s" . . . . . 100.00 149 98.60 99.30 3.70e-97 . . . . 495 1 91 no PDB 2EYJ . "Crystal Structure Of Staphylococcal Nuclease Mutant T62v" . . . . . 100.00 149 98.60 98.60 7.04e-97 . . . . 495 1 92 no PDB 2EYL . "Crystal Structure Of Staphylococcal Nuclease Mutant T82s" . . . . . 100.00 149 98.60 99.30 3.70e-97 . . . . 495 1 93 no PDB 2EYM . "Crystal Structure Of Staphylococcal Nuclease Mutant T120c" . . . . . 100.00 149 98.60 98.60 5.07e-97 . . . . 495 1 94 no PDB 2EYO . "Crystal Structure Of Staphylococcal Nuclease Mutant T120s" . . . . . 100.00 149 98.60 99.30 3.70e-97 . . . . 495 1 95 no PDB 2EYP . "Crystal Structure Of Staphylococcal Nuclease Mutant T120v" . . . . . 100.00 149 98.60 98.60 7.04e-97 . . . . 495 1 96 no PDB 2F0D . "Crystal Structure Of Staphylococcal Nuclease Mutant I92v" . . . . . 100.00 149 98.60 99.30 2.47e-97 . . . . 495 1 97 no PDB 2F0E . "Crystal Structure Of Staphylococcal Nuclease Mutant V23l" . . . . . 100.00 149 98.60 99.30 5.24e-97 . . . . 495 1 98 no PDB 2F0F . "Crystal Structure Of Staphylococcal Nuclease Mutant L25i" . . . . . 100.00 149 98.60 99.30 2.91e-97 . . . . 495 1 99 no PDB 2F0G . "Crystal Structure Of Staphylococcal Nuclease Mutant V66i" . . . . . 100.00 149 98.60 99.30 2.19e-97 . . . . 495 1 100 no PDB 2F0H . "Crystal Structure Of Staphylococcal Nuclease Mutant V66l" . . . . . 100.00 149 98.60 99.30 5.24e-97 . . . . 495 1 101 no PDB 2F0I . "Crystal Structure Of Staphylococcal Nuclease Mutant I72l" . . . . . 100.00 149 98.60 99.30 3.78e-97 . . . . 495 1 102 no PDB 2F0J . "Crystal Structure Of Staphylococcal Nuclease Mutant I72v" . . . . . 100.00 149 98.60 99.30 2.47e-97 . . . . 495 1 103 no PDB 2F0K . "Crystal Structure Of Staphylococcal Nuclease Mutant V23iL25I" . . . . . 100.00 149 97.90 99.30 5.13e-97 . . . . 495 1 104 no PDB 2F0L . "Crystal Structure Of Staphylococcal Nuclease Mutant V23lI72L" . . . . . 100.00 149 97.90 99.30 1.42e-96 . . . . 495 1 105 no PDB 2F0M . "Crystal Structure Of Staphylococcal Nuclease Mutant V23lI72V" . . . . . 100.00 149 97.90 99.30 8.03e-97 . . . . 495 1 106 no PDB 2F0N . "Crystal Structure Of Staphylococcal Nuclease Mutant L25iI72L" . . . . . 100.00 149 97.90 99.30 9.05e-97 . . . . 495 1 107 no PDB 2F0O . "Crystal Structure Of Staphylococcal Nuclease Mutant V66iI72V" . . . . . 100.00 149 97.90 99.30 4.03e-97 . . . . 495 1 108 no PDB 2F0P . "Crystal Structure Of Staphylococcal Nuclease Mutant V66iV99I" . . . . . 100.00 149 97.90 99.30 3.62e-97 . . . . 495 1 109 no PDB 2F0Q . "Crystal Structure Of Staphylococcal Nuclease Mutant V66lI92L" . . . . . 100.00 149 97.90 99.30 1.42e-96 . . . . 495 1 110 no PDB 2F0S . "Crystal Structure Of Staphylococcal Nuclease Mutant V66lI92V" . . . . . 100.00 149 97.90 99.30 8.03e-97 . . . . 495 1 111 no PDB 2F0T . "Crystal Structure Of Staphylococcal Nuclease Mutant V66lV99I" . . . . . 100.00 149 97.90 99.30 7.94e-97 . . . . 495 1 112 no PDB 2F0U . "Crystal Structure Of Staphylococcal Nuclease Mutant V23iL25II72V" . . . . . 100.00 149 97.20 99.30 8.12e-97 . . . . 495 1 113 no PDB 2F0V . "Crystal Structure Of Staphylococcal Nuclease Mutant V23lV66LI72L" . . . . . 100.00 149 97.20 99.30 4.22e-96 . . . . 495 1 114 no PDB 2F3V . "Solution Structure Of 1-110 Fragment Of Staphylococcal Nuclease With V66w Mutation" . . . . . 76.92 110 99.09 99.09 5.15e-71 . . . . 495 1 115 no PDB 2F3W . "Solution Structure Of 1-110 Fragment Of Staphylococcal Nuclease In 2m Tmao" . . . . . 76.92 110 100.00 100.00 2.62e-72 . . . . 495 1 116 no PDB 2KHS . "Solution Structure Of Snase121:snase(111-143) Complex" . . . . . 84.62 121 100.00 100.00 1.02e-81 . . . . 495 1 117 no PDB 2KQ3 . "Solution Structure Of Snase140" . . . . . 97.90 140 100.00 100.00 2.49e-96 . . . . 495 1 118 no PDB 2LKV . "Staphylococcal Nuclease Phs Variant" . . . . . 100.00 149 98.60 99.30 9.05e-97 . . . . 495 1 119 no PDB 2M00 . "Solution Structure Of Staphylococcal Nuclease E43s Mutant In The Presence Of Ssdna And Cd2+" . . . . . 100.00 149 99.30 99.30 4.44e-98 . . . . 495 1 120 no PDB 2NUC . "Staphlococcal Nuclease, Ethane Thiol Disulfide To V23c Variant" . . . . . 100.00 149 98.60 98.60 8.57e-97 . . . . 495 1 121 no PDB 2OXP . "Crystal Structure Of Staphylococcal Nuclease Mutant V66dP117GH124LS128A" . . . . . 100.00 149 97.90 98.60 1.10e-95 . . . . 495 1 122 no PDB 2PW5 . "Crystal Structure Of Staphylococcal Nuclease Variant V66yP117GH124LS128A AT ROOM TEMPERATURE" . . . . . 100.00 149 97.90 98.60 8.05e-96 . . . . 495 1 123 no PDB 2PW7 . "Crystal Structure Of Staphylococcal Nuclease Variant V66yP117GH124LS128A AT 100K" . . . . . 100.00 149 97.90 98.60 8.05e-96 . . . . 495 1 124 no PDB 2PYK . "Crystal Structure Of Staphylococcal Nuclease Variant V66qP117GH124LS128A AT ROOM TEMPERATURE" . . . . . 100.00 149 97.90 98.60 7.96e-96 . . . . 495 1 125 no PDB 2PZT . "Crystal Structure Of Staphylococcal Nuclease Variant V66qP117GH124LS128A AT 100 K" . . . . . 100.00 149 97.90 98.60 7.96e-96 . . . . 495 1 126 no PDB 2PZU . "Crystal Structure Of Staphylococcal Nuclease Variant V66nP117GH124LS128A AT CRYOGENIC TEMPERATURE" . . . . . 100.00 149 97.90 98.60 9.17e-96 . . . . 495 1 127 no PDB 2PZW . "Crystal Structure Of Staphylococcal Nuclease Variant V66nP117GH124LS128A AT ROOM TEMPERATURE" . . . . . 100.00 149 97.90 98.60 9.17e-96 . . . . 495 1 128 no PDB 2RKS . "Crystal Structure Of Staphylococcal Nuclease Variant Phs L38k At Cryogenic Temperature" . . . . . 100.00 149 97.90 98.60 1.19e-95 . . . . 495 1 129 no PDB 2SNM . "In A Staphylococcal Nuclease Mutant The Side-chain Of A Lysine Replacing Valine 66 Is Fully Buried In The Hydrophobic Core" . . . . . 100.00 149 98.60 98.60 1.88e-96 . . . . 495 1 130 no PDB 2SNS . "Staphylococcal Nuclease. Proposed Mechanism Of Action Based On Structure Of Enzyme-Thymidine 3(Prime),5(Prime)-Biphosphate-Calc" . . . . . 100.00 149 97.90 99.30 3.66e-96 . . . . 495 1 131 no PDB 2SOB . "Sn-Ob, Ob-Fold Sub-Domain Of Staphylococcal Nuclease, Nmr, 10 Structures" . . . . . 72.03 103 98.06 99.03 3.27e-65 . . . . 495 1 132 no PDB 3D6C . "Crystal Structure Of Staphylococcal Nuclease Variant Phs L38e At Cryogenic Temperature" . . . . . 100.00 149 97.90 98.60 1.21e-95 . . . . 495 1 133 no PDB 3DMU . "Crystal Structure Of Staphylococcal Nuclease Variant Phs T62k At Cryogenic Temperature" . . . . . 100.00 149 97.90 98.60 8.50e-96 . . . . 495 1 134 no PDB 3NUC . "Staphlococcal Nuclease, 1-N-Propane Thiol Disulfide To V23c Variant" . . . . . 100.00 149 98.60 98.60 8.57e-97 . . . . 495 1 135 no PDB 4G57 . "Staphylococcal Nuclease Double Mutant I72l, I92l" . . . . . 94.41 135 97.78 99.26 6.56e-91 . . . . 495 1 136 no PDB 4H7B . "Crystal Structure Of Staphylococcal Nuclease Mutant I72vV99L" . . . . . 100.00 149 97.90 99.30 8.03e-97 . . . . 495 1 137 no PDB 4ID6 . "Crystal Structure Of Staphylococcal Nuclease Mutant V23i/i72l" . . . . . 100.00 149 97.90 99.30 6.89e-97 . . . . 495 1 138 no PDB 4K14 . "Crystal Structure Of Staphylococcal Nuclease Mutant V66i/v99l" . . . . . 95.10 136 97.79 99.26 1.30e-91 . . . . 495 1 139 no PDB 4K5W . "Crystal Structure Of Staphylococcal Nuclease Variant V23m/l25f/t62f At Cryogenic Temperature" . . . . . 100.00 149 97.20 97.90 1.83e-95 . . . . 495 1 140 no PDB 4K5X . "Crystal Structure Of Staphylococcal Nuclease Variant V23m/l36f At Cryogenic Temperature" . . . . . 100.00 149 97.90 98.60 1.65e-96 . . . . 495 1 141 no PDB 4K6D . "Crystal Structure Of Staphylococcal Nuclease Variant V23m/t62f At Cryogenic Temperature" . . . . . 100.00 149 97.90 98.60 6.06e-96 . . . . 495 1 142 no PDB 4K8I . "Crystal Structure Of Staphylococcal Nuclease Mutant I92v/v99l" . . . . . 94.41 135 97.78 99.26 5.10e-91 . . . . 495 1 143 no PDB 4K8J . "Crystal Structure Of Staphylococcal Nuclease Mutant V23l/v66i" . . . . . 94.41 135 97.78 99.26 4.67e-91 . . . . 495 1 144 no PDB 4QB4 . "Crystal Structure Of Staphylococcal Nuclease Mutant V23l/l25v/v66l" . . . . . 95.10 136 97.06 99.26 8.16e-91 . . . . 495 1 145 no PDB 4QF4 . "Crystal Structure Of Staphylococcal Nuclease Variant V23m At Cryogenic Temperature" . . . . . 100.00 149 97.20 97.90 6.84e-95 . . . . 495 1 146 no PDB 4WOR . "Staphylococcal Nuclease In Complex With Ca2+ And Thymidine-3'-5'- Diphosphate (pdtp) At Room Temperature" . . . . . 100.00 149 99.30 99.30 1.46e-97 . . . . 495 1 147 no PDB 5NUC . "Staphylococcal Nuclease, 1-N-Pentane Thiol Disulfide To V23c Variant" . . . . . 100.00 149 98.60 98.60 8.57e-97 . . . . 495 1 148 no DBJ BAB41979 . "staphylococcal nuclease [Staphylococcus aureus subsp. aureus N315]" . . . . . 100.00 228 99.30 99.30 9.86e-99 . . . . 495 1 149 no DBJ BAB56977 . "staphylococcal nuclease [Staphylococcus aureus subsp. aureus Mu50]" . . . . . 100.00 228 99.30 99.30 9.86e-99 . . . . 495 1 150 no DBJ BAB94634 . "staphylococcal nuclease [Staphylococcus aureus subsp. aureus MW2]" . . . . . 100.00 228 100.00 100.00 3.21e-99 . . . . 495 1 151 no DBJ BAF67032 . "thermonuclease precursor [Staphylococcus aureus subsp. aureus str. Newman]" . . . . . 100.00 228 100.00 100.00 3.04e-99 . . . . 495 1 152 no DBJ BAF77694 . "staphylococcal nuclease [Staphylococcus aureus subsp. aureus Mu3]" . . . . . 100.00 228 99.30 99.30 9.86e-99 . . . . 495 1 153 no EMBL CAA24594 . "nuclease [Staphylococcus aureus]" . . . . . 100.00 231 99.30 99.30 5.97e-98 . . . . 495 1 154 no EMBL CAG39855 . "thermonuclease precursor [Staphylococcus aureus subsp. aureus MRSA252]" . . . . . 100.00 228 100.00 100.00 2.36e-99 . . . . 495 1 155 no EMBL CAG42530 . "thermonuclease precursor [Staphylococcus aureus subsp. aureus MSSA476]" . . . . . 100.00 228 100.00 100.00 3.21e-99 . . . . 495 1 156 no EMBL CAI80436 . "staphylococcal thermonuclease precursor [Staphylococcus aureus RF122]" . . . . . 100.00 228 99.30 100.00 1.61e-98 . . . . 495 1 157 no EMBL CAQ49298 . "thermonuclease (TNase) (Micrococcal nuclease)(Staphylococcal nuclease) [Staphylococcus aureus subsp. aureus ST398]" . . . . . 100.00 228 100.00 100.00 2.34e-99 . . . . 495 1 158 no GB AAC14660 . "deltaSP-Nuc [Cloning vector pFUN]" . . . . . 100.00 155 99.30 99.30 1.97e-97 . . . . 495 1 159 no GB AAW36415 . "thermonuclease precursor [Staphylococcus aureus subsp. aureus COL]" . . . . . 100.00 228 100.00 100.00 3.04e-99 . . . . 495 1 160 no GB ABD22328 . "thermonuclease precursor [Staphylococcus aureus subsp. aureus USA300_FPR3757]" . . . . . 100.00 228 100.00 100.00 3.04e-99 . . . . 495 1 161 no GB ABD29945 . "thermonuclease precursor [Staphylococcus aureus subsp. aureus NCTC 8325]" . . . . . 100.00 228 100.00 100.00 3.04e-99 . . . . 495 1 162 no GB ABE02272 . "nuclease [Staphylococcus aureus]" . . . . . 100.00 227 99.30 99.30 1.43e-98 . . . . 495 1 163 no PRF 1109959A . nuclease,staphylococcal . . . . . 100.00 242 99.30 99.30 6.92e-98 . . . . 495 1 164 no PRF 710414A . nuclease . . . . . 100.00 149 99.30 99.30 1.46e-97 . . . . 495 1 165 no REF NP_371339 . "nuclease [Staphylococcus aureus subsp. aureus Mu50]" . . . . . 100.00 228 99.30 99.30 9.86e-99 . . . . 495 1 166 no REF NP_374001 . "nuclease [Staphylococcus aureus subsp. aureus N315]" . . . . . 100.00 228 99.30 99.30 9.86e-99 . . . . 495 1 167 no REF NP_645586 . "nuclease [Staphylococcus aureus subsp. aureus MW2]" . . . . . 100.00 228 100.00 100.00 3.21e-99 . . . . 495 1 168 no REF WP_000141556 . "thermonuclease [Staphylococcus aureus]" . . . . . 100.00 228 100.00 100.00 3.42e-99 . . . . 495 1 169 no REF WP_000141557 . "thermonuclease [Staphylococcus aureus]" . . . . . 100.00 228 99.30 99.30 9.86e-99 . . . . 495 1 170 no SP P00644 . "RecName: Full=Thermonuclease; Short=TNase; AltName: Full=Micrococcal nuclease; AltName: Full=Staphylococcal nuclease; Contains:" . . . . . 100.00 231 99.30 99.30 5.97e-98 . . . . 495 1 171 no SP Q5HHM4 . "RecName: Full=Thermonuclease; Short=TNase; AltName: Full=Micrococcal nuclease; AltName: Full=Staphylococcal nuclease; Flags: Pr" . . . . . 100.00 228 100.00 100.00 3.04e-99 . . . . 495 1 172 no SP Q6GB41 . "RecName: Full=Thermonuclease; Short=TNase; AltName: Full=Micrococcal nuclease; AltName: Full=Staphylococcal nuclease; Flags: Pr" . . . . . 100.00 228 100.00 100.00 3.21e-99 . . . . 495 1 173 no SP Q6GIK1 . "RecName: Full=Thermonuclease; Short=TNase; AltName: Full=Micrococcal nuclease; AltName: Full=Staphylococcal nuclease; Flags: Pr" . . . . . 100.00 228 100.00 100.00 2.36e-99 . . . . 495 1 174 no SP Q7A6P2 . "RecName: Full=Thermonuclease; Short=TNase; AltName: Full=Micrococcal nuclease; AltName: Full=Staphylococcal nuclease; Flags: Pr" . . . . . 100.00 228 99.30 99.30 9.86e-99 . . . . 495 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID H124L variant 495 1 'micrococcal nuclease' common 495 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 . ALA . 495 1 2 . THR . 495 1 3 . SER . 495 1 4 . THR . 495 1 5 . LYS . 495 1 6 . LYS . 495 1 7 . LEU . 495 1 8 . HIS . 495 1 9 . LYS . 495 1 10 . GLU . 495 1 11 . PRO . 495 1 12 . ALA . 495 1 13 . THR . 495 1 14 . LEU . 495 1 15 . ILE . 495 1 16 . LYS . 495 1 17 . ALA . 495 1 18 . ILE . 495 1 19 . ASP . 495 1 20 . GLY . 495 1 21 . ASP . 495 1 22 . THR . 495 1 23 . VAL . 495 1 24 . LYS . 495 1 25 . LEU . 495 1 26 . MET . 495 1 27 . TYR . 495 1 28 . LYS . 495 1 29 . GLY . 495 1 30 . GLN . 495 1 31 . PRO . 495 1 32 . MET . 495 1 33 . THR . 495 1 34 . PHE . 495 1 35 . ARG . 495 1 36 . LEU . 495 1 37 . LEU . 495 1 38 . LEU . 495 1 39 . VAL . 495 1 40 . ASP . 495 1 41 . THR . 495 1 42 . PRO . 495 1 43 . GLU . 495 1 44 . THR . 495 1 45 . LYS . 495 1 46 . HIS . 495 1 47 . PRO . 495 1 48 . LYS . 495 1 49 . LYS . 495 1 50 . GLY . 495 1 51 . VAL . 495 1 52 . GLU . 495 1 53 . LYS . 495 1 54 . TYR . 495 1 55 . GLY . 495 1 56 . PRO . 495 1 57 . GLU . 495 1 58 . ALA . 495 1 59 . SER . 495 1 60 . ALA . 495 1 61 . PHE . 495 1 62 . THR . 495 1 63 . LYS . 495 1 64 . LYS . 495 1 65 . MET . 495 1 66 . VAL . 495 1 67 . GLU . 495 1 68 . ASN . 495 1 69 . ALA . 495 1 70 . LYS . 495 1 71 . LYS . 495 1 72 . ILE . 495 1 73 . GLU . 495 1 74 . VAL . 495 1 75 . GLU . 495 1 76 . PHE . 495 1 77 . ASP . 495 1 78 . LYS . 495 1 79 . GLY . 495 1 80 . GLN . 495 1 81 . ARG . 495 1 82 . THR . 495 1 83 . ASP . 495 1 84 . LYS . 495 1 85 . TYR . 495 1 86 . GLY . 495 1 87 . ARG . 495 1 88 . GLY . 495 1 89 . LEU . 495 1 90 . ALA . 495 1 91 . TYR . 495 1 92 . ILE . 495 1 93 . TYR . 495 1 94 . ALA . 495 1 95 . ASP . 495 1 96 . GLY . 495 1 97 . LYS . 495 1 98 . MET . 495 1 99 . VAL . 495 1 100 . ASN . 495 1 101 . GLU . 495 1 102 . ALA . 495 1 103 . LEU . 495 1 104 . VAL . 495 1 105 . ARG . 495 1 106 . GLN . 495 1 107 . GLY . 495 1 108 . LEU . 495 1 109 . ALA . 495 1 110 . LYS . 495 1 111 . VAL . 495 1 112 . ALA . 495 1 113 . TYR . 495 1 114 . VAL . 495 1 115 . TYR . 495 1 116 . LYS . 495 1 117 . PRO . 495 1 118 . ASN . 495 1 119 . ASN . 495 1 120 . THR . 495 1 121 . HIS . 495 1 122 . GLU . 495 1 123 . GLN . 495 1 124 . LEU . 495 1 125 . LEU . 495 1 126 . ARG . 495 1 127 . LYS . 495 1 128 . SER . 495 1 129 . GLU . 495 1 130 . ALA . 495 1 131 . GLN . 495 1 132 . ALA . 495 1 133 . LYS . 495 1 134 . LYS . 495 1 135 . GLU . 495 1 136 . LYS . 495 1 137 . LEU . 495 1 138 . ASN . 495 1 139 . ILE . 495 1 140 . TRP . 495 1 141 . SER . 495 1 142 . GLU . 495 1 143 . ASP . 495 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 . ALA 1 1 495 1 . THR 2 2 495 1 . SER 3 3 495 1 . THR 4 4 495 1 . LYS 5 5 495 1 . LYS 6 6 495 1 . LEU 7 7 495 1 . HIS 8 8 495 1 . LYS 9 9 495 1 . GLU 10 10 495 1 . PRO 11 11 495 1 . ALA 12 12 495 1 . THR 13 13 495 1 . LEU 14 14 495 1 . ILE 15 15 495 1 . LYS 16 16 495 1 . ALA 17 17 495 1 . ILE 18 18 495 1 . ASP 19 19 495 1 . GLY 20 20 495 1 . ASP 21 21 495 1 . THR 22 22 495 1 . VAL 23 23 495 1 . LYS 24 24 495 1 . LEU 25 25 495 1 . MET 26 26 495 1 . TYR 27 27 495 1 . LYS 28 28 495 1 . GLY 29 29 495 1 . GLN 30 30 495 1 . PRO 31 31 495 1 . MET 32 32 495 1 . THR 33 33 495 1 . PHE 34 34 495 1 . ARG 35 35 495 1 . LEU 36 36 495 1 . LEU 37 37 495 1 . LEU 38 38 495 1 . VAL 39 39 495 1 . ASP 40 40 495 1 . THR 41 41 495 1 . PRO 42 42 495 1 . GLU 43 43 495 1 . THR 44 44 495 1 . LYS 45 45 495 1 . HIS 46 46 495 1 . PRO 47 47 495 1 . LYS 48 48 495 1 . LYS 49 49 495 1 . GLY 50 50 495 1 . VAL 51 51 495 1 . GLU 52 52 495 1 . LYS 53 53 495 1 . TYR 54 54 495 1 . GLY 55 55 495 1 . PRO 56 56 495 1 . GLU 57 57 495 1 . ALA 58 58 495 1 . SER 59 59 495 1 . ALA 60 60 495 1 . PHE 61 61 495 1 . THR 62 62 495 1 . LYS 63 63 495 1 . LYS 64 64 495 1 . MET 65 65 495 1 . VAL 66 66 495 1 . GLU 67 67 495 1 . ASN 68 68 495 1 . ALA 69 69 495 1 . LYS 70 70 495 1 . LYS 71 71 495 1 . ILE 72 72 495 1 . GLU 73 73 495 1 . VAL 74 74 495 1 . GLU 75 75 495 1 . PHE 76 76 495 1 . ASP 77 77 495 1 . LYS 78 78 495 1 . GLY 79 79 495 1 . GLN 80 80 495 1 . ARG 81 81 495 1 . THR 82 82 495 1 . ASP 83 83 495 1 . LYS 84 84 495 1 . TYR 85 85 495 1 . GLY 86 86 495 1 . ARG 87 87 495 1 . GLY 88 88 495 1 . LEU 89 89 495 1 . ALA 90 90 495 1 . TYR 91 91 495 1 . ILE 92 92 495 1 . TYR 93 93 495 1 . ALA 94 94 495 1 . ASP 95 95 495 1 . GLY 96 96 495 1 . LYS 97 97 495 1 . MET 98 98 495 1 . VAL 99 99 495 1 . ASN 100 100 495 1 . GLU 101 101 495 1 . ALA 102 102 495 1 . LEU 103 103 495 1 . VAL 104 104 495 1 . ARG 105 105 495 1 . GLN 106 106 495 1 . GLY 107 107 495 1 . LEU 108 108 495 1 . ALA 109 109 495 1 . LYS 110 110 495 1 . VAL 111 111 495 1 . ALA 112 112 495 1 . TYR 113 113 495 1 . VAL 114 114 495 1 . TYR 115 115 495 1 . LYS 116 116 495 1 . PRO 117 117 495 1 . ASN 118 118 495 1 . ASN 119 119 495 1 . THR 120 120 495 1 . HIS 121 121 495 1 . GLU 122 122 495 1 . GLN 123 123 495 1 . LEU 124 124 495 1 . LEU 125 125 495 1 . ARG 126 126 495 1 . LYS 127 127 495 1 . SER 128 128 495 1 . GLU 129 129 495 1 . ALA 130 130 495 1 . GLN 131 131 495 1 . ALA 132 132 495 1 . LYS 133 133 495 1 . LYS 134 134 495 1 . GLU 135 135 495 1 . LYS 136 136 495 1 . LEU 137 137 495 1 . ASN 138 138 495 1 . ILE 139 139 495 1 . TRP 140 140 495 1 . SER 141 141 495 1 . GLU 142 142 495 1 . ASP 143 143 495 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 495 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $micrococcal_nuclease . 1280 organism . 'Staphylococcus aureus' . . . Bacteria . Staphylococcus aureus . . . . . . . . . . . . . . . . . . . . . 495 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 495 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $micrococcal_nuclease . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 495 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 495 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_condition_set_one _Sample_condition_list.Entry_ID 495 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 5.5 . na 495 1 temperature 318 . K 495 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 495 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 495 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 unknown unknown . 0 'spectrometer information not available' . . 495 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 495 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_condition_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 495 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_par_set_one _Chem_shift_reference.Entry_ID 495 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H . TSP . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 495 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_data_set_one _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode 'chemical_shift_assignment_data_set_one' _Assigned_chem_shift_list.Entry_ID 495 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_condition_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_par_set_one _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 495 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 8 8 HIS HA H 1 5.04 . . 1 . . . . . . . . 495 1 2 . 1 1 8 8 HIS HB2 H 1 3.26 . . 2 . . . . . . . . 495 1 3 . 1 1 8 8 HIS HB3 H 1 3.33 . . 2 . . . . . . . . 495 1 4 . 1 1 8 8 HIS HD2 H 1 7.34 . . 1 . . . . . . . . 495 1 5 . 1 1 8 8 HIS HE1 H 1 8.66 . . 1 . . . . . . . . 495 1 6 . 1 1 9 9 LYS HA H 1 4.82 . . 1 . . . . . . . . 495 1 7 . 1 1 9 9 LYS HB2 H 1 1.53 . . 1 . . . . . . . . 495 1 8 . 1 1 9 9 LYS HB3 H 1 1.53 . . 1 . . . . . . . . 495 1 9 . 1 1 10 10 GLU HA H 1 5.06 . . 1 . . . . . . . . 495 1 10 . 1 1 10 10 GLU HB2 H 1 2.16 . . 1 . . . . . . . . 495 1 11 . 1 1 10 10 GLU HB3 H 1 2.16 . . 1 . . . . . . . . 495 1 12 . 1 1 11 11 PRO HA H 1 4.94 . . 1 . . . . . . . . 495 1 13 . 1 1 11 11 PRO HD2 H 1 3.57 . . 2 . . . . . . . . 495 1 14 . 1 1 11 11 PRO HD3 H 1 3.92 . . 2 . . . . . . . . 495 1 15 . 1 1 12 12 ALA HA H 1 5.01 . . 1 . . . . . . . . 495 1 16 . 1 1 12 12 ALA HB1 H 1 1.34 . . 1 . . . . . . . . 495 1 17 . 1 1 12 12 ALA HB2 H 1 1.34 . . 1 . . . . . . . . 495 1 18 . 1 1 12 12 ALA HB3 H 1 1.34 . . 1 . . . . . . . . 495 1 19 . 1 1 13 13 THR HA H 1 4.73 . . 1 . . . . . . . . 495 1 20 . 1 1 13 13 THR HB H 1 4.12 . . 1 . . . . . . . . 495 1 21 . 1 1 13 13 THR HG21 H 1 1.28 . . 1 . . . . . . . . 495 1 22 . 1 1 13 13 THR HG22 H 1 1.28 . . 1 . . . . . . . . 495 1 23 . 1 1 13 13 THR HG23 H 1 1.28 . . 1 . . . . . . . . 495 1 24 . 1 1 14 14 LEU HA H 1 4.13 . . 1 . . . . . . . . 495 1 25 . 1 1 14 14 LEU HB2 H 1 1.93 . . 1 . . . . . . . . 495 1 26 . 1 1 14 14 LEU HB3 H 1 1.93 . . 1 . . . . . . . . 495 1 27 . 1 1 15 15 ILE HA H 1 4.25 . . 1 . . . . . . . . 495 1 28 . 1 1 15 15 ILE HB H 1 1.33 . . 1 . . . . . . . . 495 1 29 . 1 1 15 15 ILE HG12 H 1 1.35 . . 1 . . . . . . . . 495 1 30 . 1 1 15 15 ILE HG13 H 1 1.35 . . 1 . . . . . . . . 495 1 31 . 1 1 15 15 ILE HG21 H 1 .9 . . 1 . . . . . . . . 495 1 32 . 1 1 15 15 ILE HG22 H 1 .9 . . 1 . . . . . . . . 495 1 33 . 1 1 15 15 ILE HG23 H 1 .9 . . 1 . . . . . . . . 495 1 34 . 1 1 15 15 ILE HD11 H 1 .83 . . 1 . . . . . . . . 495 1 35 . 1 1 15 15 ILE HD12 H 1 .83 . . 1 . . . . . . . . 495 1 36 . 1 1 15 15 ILE HD13 H 1 .83 . . 1 . . . . . . . . 495 1 37 . 1 1 16 16 LYS HA H 1 4.46 . . 1 . . . . . . . . 495 1 38 . 1 1 16 16 LYS HB2 H 1 1.84 . . 1 . . . . . . . . 495 1 39 . 1 1 16 16 LYS HB3 H 1 1.84 . . 1 . . . . . . . . 495 1 40 . 1 1 17 17 ALA HA H 1 4.45 . . 1 . . . . . . . . 495 1 41 . 1 1 17 17 ALA HB1 H 1 1.37 . . 1 . . . . . . . . 495 1 42 . 1 1 17 17 ALA HB2 H 1 1.37 . . 1 . . . . . . . . 495 1 43 . 1 1 17 17 ALA HB3 H 1 1.37 . . 1 . . . . . . . . 495 1 44 . 1 1 18 18 ILE HA H 1 4.06 . . 1 . . . . . . . . 495 1 45 . 1 1 18 18 ILE HB H 1 1.58 . . 1 . . . . . . . . 495 1 46 . 1 1 18 18 ILE HG12 H 1 1.11 . . 2 . . . . . . . . 495 1 47 . 1 1 18 18 ILE HG13 H 1 1.44 . . 2 . . . . . . . . 495 1 48 . 1 1 18 18 ILE HG21 H 1 .87 . . 1 . . . . . . . . 495 1 49 . 1 1 18 18 ILE HG22 H 1 .87 . . 1 . . . . . . . . 495 1 50 . 1 1 18 18 ILE HG23 H 1 .87 . . 1 . . . . . . . . 495 1 51 . 1 1 18 18 ILE HD11 H 1 .78 . . 1 . . . . . . . . 495 1 52 . 1 1 18 18 ILE HD12 H 1 .78 . . 1 . . . . . . . . 495 1 53 . 1 1 18 18 ILE HD13 H 1 .78 . . 1 . . . . . . . . 495 1 54 . 1 1 19 19 ASP HA H 1 4.67 . . 1 . . . . . . . . 495 1 55 . 1 1 21 21 ASP HA H 1 4.89 . . 1 . . . . . . . . 495 1 56 . 1 1 22 22 THR HA H 1 5.64 . . 1 . . . . . . . . 495 1 57 . 1 1 22 22 THR HB H 1 3.97 . . 1 . . . . . . . . 495 1 58 . 1 1 22 22 THR HG21 H 1 1.16 . . 1 . . . . . . . . 495 1 59 . 1 1 22 22 THR HG22 H 1 1.16 . . 1 . . . . . . . . 495 1 60 . 1 1 22 22 THR HG23 H 1 1.16 . . 1 . . . . . . . . 495 1 61 . 1 1 23 23 VAL HA H 1 4.65 . . 1 . . . . . . . . 495 1 62 . 1 1 23 23 VAL HB H 1 1.93 . . 1 . . . . . . . . 495 1 63 . 1 1 23 23 VAL HG11 H 1 .78 . . 2 . . . . . . . . 495 1 64 . 1 1 23 23 VAL HG12 H 1 .78 . . 2 . . . . . . . . 495 1 65 . 1 1 23 23 VAL HG13 H 1 .78 . . 2 . . . . . . . . 495 1 66 . 1 1 23 23 VAL HG21 H 1 .84 . . 2 . . . . . . . . 495 1 67 . 1 1 23 23 VAL HG22 H 1 .84 . . 2 . . . . . . . . 495 1 68 . 1 1 23 23 VAL HG23 H 1 .84 . . 2 . . . . . . . . 495 1 69 . 1 1 24 24 LYS HA H 1 5.44 . . 1 . . . . . . . . 495 1 70 . 1 1 24 24 LYS HB2 H 1 2.02 . . 1 . . . . . . . . 495 1 71 . 1 1 24 24 LYS HB3 H 1 2.02 . . 1 . . . . . . . . 495 1 72 . 1 1 25 25 LEU HA H 1 5.21 . . 1 . . . . . . . . 495 1 73 . 1 1 25 25 LEU HB2 H 1 1.78 . . 1 . . . . . . . . 495 1 74 . 1 1 25 25 LEU HB3 H 1 1.78 . . 1 . . . . . . . . 495 1 75 . 1 1 26 26 MET HA H 1 4.88 . . 1 . . . . . . . . 495 1 76 . 1 1 26 26 MET HB2 H 1 2.28 . . 2 . . . . . . . . 495 1 77 . 1 1 26 26 MET HB3 H 1 1.75 . . 2 . . . . . . . . 495 1 78 . 1 1 26 26 MET HG2 H 1 2.5 . . 1 . . . . . . . . 495 1 79 . 1 1 26 26 MET HG3 H 1 2.5 . . 1 . . . . . . . . 495 1 80 . 1 1 26 26 MET HE1 H 1 1.97 . . 1 . . . . . . . . 495 1 81 . 1 1 26 26 MET HE2 H 1 1.97 . . 1 . . . . . . . . 495 1 82 . 1 1 26 26 MET HE3 H 1 1.97 . . 1 . . . . . . . . 495 1 83 . 1 1 27 27 TYR HA H 1 5.06 . . 1 . . . . . . . . 495 1 84 . 1 1 27 27 TYR HB2 H 1 3.01 . . 2 . . . . . . . . 495 1 85 . 1 1 27 27 TYR HB3 H 1 3.19 . . 2 . . . . . . . . 495 1 86 . 1 1 27 27 TYR HD1 H 1 7.34 . . 1 . . . . . . . . 495 1 87 . 1 1 27 27 TYR HD2 H 1 7.34 . . 1 . . . . . . . . 495 1 88 . 1 1 27 27 TYR HE1 H 1 6.92 . . 1 . . . . . . . . 495 1 89 . 1 1 27 27 TYR HE2 H 1 6.92 . . 1 . . . . . . . . 495 1 90 . 1 1 28 28 LYS HA H 1 3.6 . . 1 . . . . . . . . 495 1 91 . 1 1 28 28 LYS HB2 H 1 1.38 . . 1 . . . . . . . . 495 1 92 . 1 1 28 28 LYS HB3 H 1 1.38 . . 1 . . . . . . . . 495 1 93 . 1 1 29 29 GLY HA2 H 1 3.51 . . 2 . . . . . . . . 495 1 94 . 1 1 29 29 GLY HA3 H 1 4.14 . . 2 . . . . . . . . 495 1 95 . 1 1 30 30 GLN HA H 1 5.04 . . 1 . . . . . . . . 495 1 96 . 1 1 30 30 GLN HB2 H 1 2.08 . . 1 . . . . . . . . 495 1 97 . 1 1 30 30 GLN HB3 H 1 2.08 . . 1 . . . . . . . . 495 1 98 . 1 1 31 31 PRO HA H 1 4.84 . . 1 . . . . . . . . 495 1 99 . 1 1 31 31 PRO HD2 H 1 3.2 . . 2 . . . . . . . . 495 1 100 . 1 1 31 31 PRO HD3 H 1 3.8 . . 2 . . . . . . . . 495 1 101 . 1 1 32 32 MET HA H 1 4.65 . . 1 . . . . . . . . 495 1 102 . 1 1 32 32 MET HB2 H 1 2.1 . . 2 . . . . . . . . 495 1 103 . 1 1 32 32 MET HB3 H 1 1.98 . . 2 . . . . . . . . 495 1 104 . 1 1 32 32 MET HG2 H 1 2.44 . . 1 . . . . . . . . 495 1 105 . 1 1 32 32 MET HG3 H 1 2.44 . . 1 . . . . . . . . 495 1 106 . 1 1 32 32 MET HE1 H 1 1.9 . . 1 . . . . . . . . 495 1 107 . 1 1 32 32 MET HE2 H 1 1.9 . . 1 . . . . . . . . 495 1 108 . 1 1 32 32 MET HE3 H 1 1.9 . . 1 . . . . . . . . 495 1 109 . 1 1 33 33 THR HA H 1 4.49 . . 1 . . . . . . . . 495 1 110 . 1 1 33 33 THR HB H 1 3.98 . . 1 . . . . . . . . 495 1 111 . 1 1 33 33 THR HG21 H 1 .95 . . 1 . . . . . . . . 495 1 112 . 1 1 33 33 THR HG22 H 1 .95 . . 1 . . . . . . . . 495 1 113 . 1 1 33 33 THR HG23 H 1 .95 . . 1 . . . . . . . . 495 1 114 . 1 1 34 34 PHE HA H 1 4.94 . . 1 . . . . . . . . 495 1 115 . 1 1 34 34 PHE HB2 H 1 2.37 . . 2 . . . . . . . . 495 1 116 . 1 1 34 34 PHE HB3 H 1 2.89 . . 2 . . . . . . . . 495 1 117 . 1 1 34 34 PHE HD1 H 1 6.91 . . 1 . . . . . . . . 495 1 118 . 1 1 34 34 PHE HD2 H 1 6.91 . . 1 . . . . . . . . 495 1 119 . 1 1 34 34 PHE HE1 H 1 6.91 . . 1 . . . . . . . . 495 1 120 . 1 1 34 34 PHE HE2 H 1 6.91 . . 1 . . . . . . . . 495 1 121 . 1 1 34 34 PHE HZ H 1 6.64 . . 1 . . . . . . . . 495 1 122 . 1 1 35 35 ARG HA H 1 4.99 . . 1 . . . . . . . . 495 1 123 . 1 1 35 35 ARG HB2 H 1 1.92 . . 1 . . . . . . . . 495 1 124 . 1 1 35 35 ARG HB3 H 1 1.92 . . 1 . . . . . . . . 495 1 125 . 1 1 37 37 LEU HA H 1 3.92 . . 1 . . . . . . . . 495 1 126 . 1 1 38 38 LEU HA H 1 4.31 . . 1 . . . . . . . . 495 1 127 . 1 1 38 38 LEU HB2 H 1 1.91 . . 1 . . . . . . . . 495 1 128 . 1 1 38 38 LEU HB3 H 1 1.91 . . 1 . . . . . . . . 495 1 129 . 1 1 39 39 VAL HA H 1 5.74 . . 1 . . . . . . . . 495 1 130 . 1 1 39 39 VAL HB H 1 1.87 . . 1 . . . . . . . . 495 1 131 . 1 1 39 39 VAL HG11 H 1 .73 . . 2 . . . . . . . . 495 1 132 . 1 1 39 39 VAL HG12 H 1 .73 . . 2 . . . . . . . . 495 1 133 . 1 1 39 39 VAL HG13 H 1 .73 . . 2 . . . . . . . . 495 1 134 . 1 1 39 39 VAL HG21 H 1 1.02 . . 2 . . . . . . . . 495 1 135 . 1 1 39 39 VAL HG22 H 1 1.02 . . 2 . . . . . . . . 495 1 136 . 1 1 39 39 VAL HG23 H 1 1.02 . . 2 . . . . . . . . 495 1 137 . 1 1 40 40 ASP HA H 1 5.22 . . 1 . . . . . . . . 495 1 138 . 1 1 40 40 ASP HB2 H 1 2.48 . . 1 . . . . . . . . 495 1 139 . 1 1 40 40 ASP HB3 H 1 2.48 . . 1 . . . . . . . . 495 1 140 . 1 1 41 41 THR HA H 1 5.14 . . 1 . . . . . . . . 495 1 141 . 1 1 41 41 THR HB H 1 4.23 . . 1 . . . . . . . . 495 1 142 . 1 1 41 41 THR HG21 H 1 1.18 . . 1 . . . . . . . . 495 1 143 . 1 1 41 41 THR HG22 H 1 1.18 . . 1 . . . . . . . . 495 1 144 . 1 1 41 41 THR HG23 H 1 1.18 . . 1 . . . . . . . . 495 1 145 . 1 1 42 42 PRO HD2 H 1 3.54 . . 2 . . . . . . . . 495 1 146 . 1 1 42 42 PRO HD3 H 1 3.71 . . 2 . . . . . . . . 495 1 147 . 1 1 44 44 THR HA H 1 4.38 . . 1 . . . . . . . . 495 1 148 . 1 1 44 44 THR HB H 1 4.29 . . 1 . . . . . . . . 495 1 149 . 1 1 44 44 THR HG21 H 1 1.14 . . 1 . . . . . . . . 495 1 150 . 1 1 44 44 THR HG22 H 1 1.14 . . 1 . . . . . . . . 495 1 151 . 1 1 44 44 THR HG23 H 1 1.14 . . 1 . . . . . . . . 495 1 152 . 1 1 45 45 LYS HA H 1 4.24 . . 1 . . . . . . . . 495 1 153 . 1 1 46 46 HIS HA H 1 4.89 . . 1 . . . . . . . . 495 1 154 . 1 1 46 46 HIS HB2 H 1 3.12 . . 2 . . . . . . . . 495 1 155 . 1 1 46 46 HIS HB3 H 1 3.17 . . 2 . . . . . . . . 495 1 156 . 1 1 46 46 HIS HD2 H 1 7.3 . . 1 . . . . . . . . 495 1 157 . 1 1 46 46 HIS HE1 H 1 8.29 . . 1 . . . . . . . . 495 1 158 . 1 1 50 50 GLY HA2 H 1 3.84 . . 2 . . . . . . . . 495 1 159 . 1 1 50 50 GLY HA3 H 1 4.14 . . 2 . . . . . . . . 495 1 160 . 1 1 51 51 VAL HA H 1 4.1 . . 1 . . . . . . . . 495 1 161 . 1 1 51 51 VAL HB H 1 2.08 . . 1 . . . . . . . . 495 1 162 . 1 1 51 51 VAL HG11 H 1 .95 . . 2 . . . . . . . . 495 1 163 . 1 1 51 51 VAL HG12 H 1 .95 . . 2 . . . . . . . . 495 1 164 . 1 1 51 51 VAL HG13 H 1 .95 . . 2 . . . . . . . . 495 1 165 . 1 1 51 51 VAL HG21 H 1 1 . . 2 . . . . . . . . 495 1 166 . 1 1 51 51 VAL HG22 H 1 1 . . 2 . . . . . . . . 495 1 167 . 1 1 51 51 VAL HG23 H 1 1 . . 2 . . . . . . . . 495 1 168 . 1 1 52 52 GLU HA H 1 4.29 . . 1 . . . . . . . . 495 1 169 . 1 1 52 52 GLU HB2 H 1 1.73 . . 1 . . . . . . . . 495 1 170 . 1 1 52 52 GLU HB3 H 1 1.73 . . 1 . . . . . . . . 495 1 171 . 1 1 54 54 TYR HA H 1 4.39 . . 1 . . . . . . . . 495 1 172 . 1 1 54 54 TYR HB2 H 1 3.18 . . 1 . . . . . . . . 495 1 173 . 1 1 54 54 TYR HB3 H 1 3.18 . . 1 . . . . . . . . 495 1 174 . 1 1 54 54 TYR HD1 H 1 6.82 . . 1 . . . . . . . . 495 1 175 . 1 1 54 54 TYR HD2 H 1 6.82 . . 1 . . . . . . . . 495 1 176 . 1 1 54 54 TYR HE1 H 1 6.73 . . 1 . . . . . . . . 495 1 177 . 1 1 54 54 TYR HE2 H 1 6.73 . . 1 . . . . . . . . 495 1 178 . 1 1 55 55 GLY HA2 H 1 3.8 . . 2 . . . . . . . . 495 1 179 . 1 1 55 55 GLY HA3 H 1 3.9 . . 2 . . . . . . . . 495 1 180 . 1 1 56 56 PRO HD2 H 1 3.56 . . 2 . . . . . . . . 495 1 181 . 1 1 56 56 PRO HD3 H 1 3.63 . . 2 . . . . . . . . 495 1 182 . 1 1 58 58 ALA HA H 1 4.17 . . 1 . . . . . . . . 495 1 183 . 1 1 58 58 ALA HB1 H 1 1.72 . . 1 . . . . . . . . 495 1 184 . 1 1 58 58 ALA HB2 H 1 1.72 . . 1 . . . . . . . . 495 1 185 . 1 1 58 58 ALA HB3 H 1 1.72 . . 1 . . . . . . . . 495 1 186 . 1 1 59 59 SER HA H 1 3.98 . . 1 . . . . . . . . 495 1 187 . 1 1 59 59 SER HB2 H 1 3.74 . . 1 . . . . . . . . 495 1 188 . 1 1 59 59 SER HB3 H 1 3.74 . . 1 . . . . . . . . 495 1 189 . 1 1 60 60 ALA HA H 1 4.05 . . 1 . . . . . . . . 495 1 190 . 1 1 60 60 ALA HB1 H 1 1.51 . . 1 . . . . . . . . 495 1 191 . 1 1 60 60 ALA HB2 H 1 1.51 . . 1 . . . . . . . . 495 1 192 . 1 1 60 60 ALA HB3 H 1 1.51 . . 1 . . . . . . . . 495 1 193 . 1 1 61 61 PHE HA H 1 4.05 . . 1 . . . . . . . . 495 1 194 . 1 1 61 61 PHE HB2 H 1 3.14 . . 2 . . . . . . . . 495 1 195 . 1 1 61 61 PHE HB3 H 1 3.33 . . 2 . . . . . . . . 495 1 196 . 1 1 61 61 PHE HD1 H 1 7.13 . . 1 . . . . . . . . 495 1 197 . 1 1 61 61 PHE HD2 H 1 7.13 . . 1 . . . . . . . . 495 1 198 . 1 1 61 61 PHE HE1 H 1 7.22 . . 1 . . . . . . . . 495 1 199 . 1 1 61 61 PHE HE2 H 1 7.22 . . 1 . . . . . . . . 495 1 200 . 1 1 61 61 PHE HZ H 1 7.21 . . 1 . . . . . . . . 495 1 201 . 1 1 62 62 THR HA H 1 3.6 . . 1 . . . . . . . . 495 1 202 . 1 1 62 62 THR HB H 1 4.12 . . 1 . . . . . . . . 495 1 203 . 1 1 62 62 THR HG21 H 1 1.01 . . 1 . . . . . . . . 495 1 204 . 1 1 62 62 THR HG22 H 1 1.01 . . 1 . . . . . . . . 495 1 205 . 1 1 62 62 THR HG23 H 1 1.01 . . 1 . . . . . . . . 495 1 206 . 1 1 63 63 LYS HA H 1 3.58 . . 1 . . . . . . . . 495 1 207 . 1 1 63 63 LYS HB2 H 1 1.77 . . 1 . . . . . . . . 495 1 208 . 1 1 63 63 LYS HB3 H 1 1.77 . . 1 . . . . . . . . 495 1 209 . 1 1 64 64 LYS HA H 1 3.93 . . 1 . . . . . . . . 495 1 210 . 1 1 64 64 LYS HB2 H 1 1.74 . . 1 . . . . . . . . 495 1 211 . 1 1 64 64 LYS HB3 H 1 1.74 . . 1 . . . . . . . . 495 1 212 . 1 1 65 65 MET HA H 1 3.92 . . 1 . . . . . . . . 495 1 213 . 1 1 65 65 MET HB2 H 1 1.8 . . 2 . . . . . . . . 495 1 214 . 1 1 65 65 MET HB3 H 1 2.16 . . 2 . . . . . . . . 495 1 215 . 1 1 65 65 MET HG2 H 1 2.46 . . 1 . . . . . . . . 495 1 216 . 1 1 65 65 MET HG3 H 1 2.46 . . 1 . . . . . . . . 495 1 217 . 1 1 65 65 MET HE1 H 1 1.94 . . 1 . . . . . . . . 495 1 218 . 1 1 65 65 MET HE2 H 1 1.94 . . 1 . . . . . . . . 495 1 219 . 1 1 65 65 MET HE3 H 1 1.94 . . 1 . . . . . . . . 495 1 220 . 1 1 66 66 VAL HA H 1 4.17 . . 1 . . . . . . . . 495 1 221 . 1 1 66 66 VAL HB H 1 2.15 . . 1 . . . . . . . . 495 1 222 . 1 1 66 66 VAL HG11 H 1 .89 . . 2 . . . . . . . . 495 1 223 . 1 1 66 66 VAL HG12 H 1 .89 . . 2 . . . . . . . . 495 1 224 . 1 1 66 66 VAL HG13 H 1 .89 . . 2 . . . . . . . . 495 1 225 . 1 1 66 66 VAL HG21 H 1 1.15 . . 2 . . . . . . . . 495 1 226 . 1 1 66 66 VAL HG22 H 1 1.15 . . 2 . . . . . . . . 495 1 227 . 1 1 66 66 VAL HG23 H 1 1.15 . . 2 . . . . . . . . 495 1 228 . 1 1 67 67 GLU HA H 1 3.98 . . 1 . . . . . . . . 495 1 229 . 1 1 67 67 GLU HB2 H 1 2.06 . . 1 . . . . . . . . 495 1 230 . 1 1 67 67 GLU HB3 H 1 2.06 . . 1 . . . . . . . . 495 1 231 . 1 1 68 68 ASN HA H 1 4.69 . . 1 . . . . . . . . 495 1 232 . 1 1 68 68 ASN HB2 H 1 2.78 . . 2 . . . . . . . . 495 1 233 . 1 1 68 68 ASN HB3 H 1 2.81 . . 2 . . . . . . . . 495 1 234 . 1 1 69 69 ALA HA H 1 4.52 . . 1 . . . . . . . . 495 1 235 . 1 1 69 69 ALA HB1 H 1 1.32 . . 1 . . . . . . . . 495 1 236 . 1 1 69 69 ALA HB2 H 1 1.32 . . 1 . . . . . . . . 495 1 237 . 1 1 69 69 ALA HB3 H 1 1.32 . . 1 . . . . . . . . 495 1 238 . 1 1 70 70 LYS HA H 1 4.35 . . 1 . . . . . . . . 495 1 239 . 1 1 70 70 LYS HB2 H 1 2.03 . . 1 . . . . . . . . 495 1 240 . 1 1 70 70 LYS HB3 H 1 2.03 . . 1 . . . . . . . . 495 1 241 . 1 1 71 71 LYS HA H 1 4.66 . . 1 . . . . . . . . 495 1 242 . 1 1 71 71 LYS HB2 H 1 1.74 . . 1 . . . . . . . . 495 1 243 . 1 1 71 71 LYS HB3 H 1 1.74 . . 1 . . . . . . . . 495 1 244 . 1 1 72 72 ILE HA H 1 5.23 . . 1 . . . . . . . . 495 1 245 . 1 1 72 72 ILE HB H 1 1.89 . . 1 . . . . . . . . 495 1 246 . 1 1 72 72 ILE HG12 H 1 1.15 . . 2 . . . . . . . . 495 1 247 . 1 1 72 72 ILE HG13 H 1 1.33 . . 2 . . . . . . . . 495 1 248 . 1 1 72 72 ILE HG21 H 1 .64 . . 1 . . . . . . . . 495 1 249 . 1 1 72 72 ILE HG22 H 1 .64 . . 1 . . . . . . . . 495 1 250 . 1 1 72 72 ILE HG23 H 1 .64 . . 1 . . . . . . . . 495 1 251 . 1 1 72 72 ILE HD11 H 1 .89 . . 1 . . . . . . . . 495 1 252 . 1 1 72 72 ILE HD12 H 1 .89 . . 1 . . . . . . . . 495 1 253 . 1 1 72 72 ILE HD13 H 1 .89 . . 1 . . . . . . . . 495 1 254 . 1 1 73 73 GLU HA H 1 5.27 . . 1 . . . . . . . . 495 1 255 . 1 1 73 73 GLU HB2 H 1 1.74 . . 1 . . . . . . . . 495 1 256 . 1 1 73 73 GLU HB3 H 1 1.74 . . 1 . . . . . . . . 495 1 257 . 1 1 74 74 VAL HA H 1 4.62 . . 1 . . . . . . . . 495 1 258 . 1 1 74 74 VAL HB H 1 1.29 . . 1 . . . . . . . . 495 1 259 . 1 1 74 74 VAL HG11 H 1 .14 . . 2 . . . . . . . . 495 1 260 . 1 1 74 74 VAL HG12 H 1 .14 . . 2 . . . . . . . . 495 1 261 . 1 1 74 74 VAL HG13 H 1 .14 . . 2 . . . . . . . . 495 1 262 . 1 1 74 74 VAL HG21 H 1 .3 . . 2 . . . . . . . . 495 1 263 . 1 1 74 74 VAL HG22 H 1 .3 . . 2 . . . . . . . . 495 1 264 . 1 1 74 74 VAL HG23 H 1 .3 . . 2 . . . . . . . . 495 1 265 . 1 1 75 75 GLU HA H 1 5.15 . . 1 . . . . . . . . 495 1 266 . 1 1 75 75 GLU HB2 H 1 2.91 . . 1 . . . . . . . . 495 1 267 . 1 1 75 75 GLU HB3 H 1 2.91 . . 1 . . . . . . . . 495 1 268 . 1 1 76 76 PHE HA H 1 4.77 . . 1 . . . . . . . . 495 1 269 . 1 1 76 76 PHE HB2 H 1 2.92 . . 2 . . . . . . . . 495 1 270 . 1 1 76 76 PHE HB3 H 1 3.55 . . 2 . . . . . . . . 495 1 271 . 1 1 76 76 PHE HD1 H 1 7.69 . . 1 . . . . . . . . 495 1 272 . 1 1 76 76 PHE HD2 H 1 7.69 . . 1 . . . . . . . . 495 1 273 . 1 1 76 76 PHE HE1 H 1 7.27 . . 1 . . . . . . . . 495 1 274 . 1 1 76 76 PHE HE2 H 1 7.27 . . 1 . . . . . . . . 495 1 275 . 1 1 76 76 PHE HZ H 1 6.79 . . 1 . . . . . . . . 495 1 276 . 1 1 77 77 ASP HA H 1 5.32 . . 1 . . . . . . . . 495 1 277 . 1 1 77 77 ASP HB2 H 1 3.83 . . 1 . . . . . . . . 495 1 278 . 1 1 77 77 ASP HB3 H 1 3.83 . . 1 . . . . . . . . 495 1 279 . 1 1 78 78 LYS HA H 1 4.24 . . 1 . . . . . . . . 495 1 280 . 1 1 78 78 LYS HB2 H 1 1.91 . . 1 . . . . . . . . 495 1 281 . 1 1 78 78 LYS HB3 H 1 1.91 . . 1 . . . . . . . . 495 1 282 . 1 1 79 79 GLY HA2 H 1 3.33 . . 2 . . . . . . . . 495 1 283 . 1 1 79 79 GLY HA3 H 1 4.42 . . 2 . . . . . . . . 495 1 284 . 1 1 80 80 GLN HA H 1 4.14 . . 1 . . . . . . . . 495 1 285 . 1 1 80 80 GLN HB2 H 1 2 . . 1 . . . . . . . . 495 1 286 . 1 1 80 80 GLN HB3 H 1 2 . . 1 . . . . . . . . 495 1 287 . 1 1 81 81 ARG HA H 1 4.16 . . 1 . . . . . . . . 495 1 288 . 1 1 81 81 ARG HB2 H 1 2.05 . . 1 . . . . . . . . 495 1 289 . 1 1 81 81 ARG HB3 H 1 2.05 . . 1 . . . . . . . . 495 1 290 . 1 1 82 82 THR HA H 1 5.56 . . 1 . . . . . . . . 495 1 291 . 1 1 82 82 THR HB H 1 3.84 . . 1 . . . . . . . . 495 1 292 . 1 1 82 82 THR HG21 H 1 .96 . . 1 . . . . . . . . 495 1 293 . 1 1 82 82 THR HG22 H 1 .96 . . 1 . . . . . . . . 495 1 294 . 1 1 82 82 THR HG23 H 1 .96 . . 1 . . . . . . . . 495 1 295 . 1 1 83 83 ASP HA H 1 4.64 . . 1 . . . . . . . . 495 1 296 . 1 1 83 83 ASP HB2 H 1 2.36 . . 1 . . . . . . . . 495 1 297 . 1 1 83 83 ASP HB3 H 1 2.36 . . 1 . . . . . . . . 495 1 298 . 1 1 85 85 TYR HA H 1 4.65 . . 1 . . . . . . . . 495 1 299 . 1 1 85 85 TYR HB2 H 1 2.88 . . 2 . . . . . . . . 495 1 300 . 1 1 85 85 TYR HB3 H 1 3.39 . . 2 . . . . . . . . 495 1 301 . 1 1 85 85 TYR HD1 H 1 7.02 . . 1 . . . . . . . . 495 1 302 . 1 1 85 85 TYR HD2 H 1 7.02 . . 1 . . . . . . . . 495 1 303 . 1 1 85 85 TYR HE1 H 1 6.91 . . 1 . . . . . . . . 495 1 304 . 1 1 85 85 TYR HE2 H 1 6.91 . . 1 . . . . . . . . 495 1 305 . 1 1 86 86 GLY HA2 H 1 3.61 . . 2 . . . . . . . . 495 1 306 . 1 1 86 86 GLY HA3 H 1 4.21 . . 2 . . . . . . . . 495 1 307 . 1 1 87 87 ARG HA H 1 4.39 . . 1 . . . . . . . . 495 1 308 . 1 1 87 87 ARG HB2 H 1 1.99 . . 1 . . . . . . . . 495 1 309 . 1 1 87 87 ARG HB3 H 1 1.99 . . 1 . . . . . . . . 495 1 310 . 1 1 88 88 GLY HA2 H 1 2.68 . . 2 . . . . . . . . 495 1 311 . 1 1 88 88 GLY HA3 H 1 4.46 . . 2 . . . . . . . . 495 1 312 . 1 1 89 89 LEU HA H 1 5.21 . . 1 . . . . . . . . 495 1 313 . 1 1 89 89 LEU HB2 H 1 1.7 . . 1 . . . . . . . . 495 1 314 . 1 1 89 89 LEU HB3 H 1 1.7 . . 1 . . . . . . . . 495 1 315 . 1 1 90 90 ALA HA H 1 4.81 . . 1 . . . . . . . . 495 1 316 . 1 1 90 90 ALA HB1 H 1 .75 . . 1 . . . . . . . . 495 1 317 . 1 1 90 90 ALA HB2 H 1 .75 . . 1 . . . . . . . . 495 1 318 . 1 1 90 90 ALA HB3 H 1 .75 . . 1 . . . . . . . . 495 1 319 . 1 1 91 91 TYR HA H 1 4.63 . . 1 . . . . . . . . 495 1 320 . 1 1 91 91 TYR HB2 H 1 3.4 . . 1 . . . . . . . . 495 1 321 . 1 1 91 91 TYR HB3 H 1 3.4 . . 1 . . . . . . . . 495 1 322 . 1 1 91 91 TYR HE1 H 1 6.58 . . 1 . . . . . . . . 495 1 323 . 1 1 91 91 TYR HE2 H 1 6.58 . . 1 . . . . . . . . 495 1 324 . 1 1 92 92 ILE HA H 1 4.97 . . 1 . . . . . . . . 495 1 325 . 1 1 92 92 ILE HB H 1 1.46 . . 1 . . . . . . . . 495 1 326 . 1 1 92 92 ILE HG12 H 1 .98 . . 2 . . . . . . . . 495 1 327 . 1 1 92 92 ILE HG13 H 1 1.17 . . 2 . . . . . . . . 495 1 328 . 1 1 92 92 ILE HG21 H 1 .64 . . 1 . . . . . . . . 495 1 329 . 1 1 92 92 ILE HG22 H 1 .64 . . 1 . . . . . . . . 495 1 330 . 1 1 92 92 ILE HG23 H 1 .64 . . 1 . . . . . . . . 495 1 331 . 1 1 92 92 ILE HD11 H 1 .34 . . 1 . . . . . . . . 495 1 332 . 1 1 92 92 ILE HD12 H 1 .34 . . 1 . . . . . . . . 495 1 333 . 1 1 92 92 ILE HD13 H 1 .34 . . 1 . . . . . . . . 495 1 334 . 1 1 93 93 TYR HA H 1 5.11 . . 1 . . . . . . . . 495 1 335 . 1 1 93 93 TYR HB2 H 1 2.84 . . 1 . . . . . . . . 495 1 336 . 1 1 93 93 TYR HB3 H 1 2.84 . . 1 . . . . . . . . 495 1 337 . 1 1 93 93 TYR HD1 H 1 6.63 . . 1 . . . . . . . . 495 1 338 . 1 1 93 93 TYR HD2 H 1 6.63 . . 1 . . . . . . . . 495 1 339 . 1 1 93 93 TYR HE1 H 1 6.73 . . 1 . . . . . . . . 495 1 340 . 1 1 93 93 TYR HE2 H 1 6.73 . . 1 . . . . . . . . 495 1 341 . 1 1 94 94 ALA HA H 1 4.98 . . 1 . . . . . . . . 495 1 342 . 1 1 94 94 ALA HB1 H 1 1.13 . . 1 . . . . . . . . 495 1 343 . 1 1 94 94 ALA HB2 H 1 1.13 . . 1 . . . . . . . . 495 1 344 . 1 1 94 94 ALA HB3 H 1 1.13 . . 1 . . . . . . . . 495 1 345 . 1 1 95 95 ASP HA H 1 4.43 . . 1 . . . . . . . . 495 1 346 . 1 1 95 95 ASP HB2 H 1 2.74 . . 1 . . . . . . . . 495 1 347 . 1 1 95 95 ASP HB3 H 1 2.74 . . 1 . . . . . . . . 495 1 348 . 1 1 96 96 GLY HA2 H 1 3.67 . . 2 . . . . . . . . 495 1 349 . 1 1 96 96 GLY HA3 H 1 4.25 . . 2 . . . . . . . . 495 1 350 . 1 1 97 97 LYS HA H 1 4.66 . . 1 . . . . . . . . 495 1 351 . 1 1 97 97 LYS HB2 H 1 1.85 . . 1 . . . . . . . . 495 1 352 . 1 1 97 97 LYS HB3 H 1 1.85 . . 1 . . . . . . . . 495 1 353 . 1 1 98 98 MET HA H 1 3.83 . . 1 . . . . . . . . 495 1 354 . 1 1 98 98 MET HB2 H 1 1.49 . . 2 . . . . . . . . 495 1 355 . 1 1 98 98 MET HB3 H 1 1.98 . . 2 . . . . . . . . 495 1 356 . 1 1 98 98 MET HG2 H 1 2.11 . . 1 . . . . . . . . 495 1 357 . 1 1 98 98 MET HG3 H 1 2.11 . . 1 . . . . . . . . 495 1 358 . 1 1 98 98 MET HE1 H 1 1.44 . . 1 . . . . . . . . 495 1 359 . 1 1 98 98 MET HE2 H 1 1.44 . . 1 . . . . . . . . 495 1 360 . 1 1 98 98 MET HE3 H 1 1.44 . . 1 . . . . . . . . 495 1 361 . 1 1 99 99 VAL HA H 1 3.7 . . 1 . . . . . . . . 495 1 362 . 1 1 99 99 VAL HB H 1 1.83 . . 1 . . . . . . . . 495 1 363 . 1 1 99 99 VAL HG11 H 1 .98 . . 2 . . . . . . . . 495 1 364 . 1 1 99 99 VAL HG12 H 1 .98 . . 2 . . . . . . . . 495 1 365 . 1 1 99 99 VAL HG13 H 1 .98 . . 2 . . . . . . . . 495 1 366 . 1 1 99 99 VAL HG21 H 1 1.05 . . 2 . . . . . . . . 495 1 367 . 1 1 99 99 VAL HG22 H 1 1.05 . . 2 . . . . . . . . 495 1 368 . 1 1 99 99 VAL HG23 H 1 1.05 . . 2 . . . . . . . . 495 1 369 . 1 1 100 100 ASN HA H 1 4.07 . . 1 . . . . . . . . 495 1 370 . 1 1 100 100 ASN HB2 H 1 2.79 . . 2 . . . . . . . . 495 1 371 . 1 1 100 100 ASN HB3 H 1 2.93 . . 2 . . . . . . . . 495 1 372 . 1 1 101 101 GLU HA H 1 3.69 . . 1 . . . . . . . . 495 1 373 . 1 1 101 101 GLU HB2 H 1 2.25 . . 1 . . . . . . . . 495 1 374 . 1 1 101 101 GLU HB3 H 1 2.25 . . 1 . . . . . . . . 495 1 375 . 1 1 102 102 ALA HA H 1 4.08 . . 1 . . . . . . . . 495 1 376 . 1 1 102 102 ALA HB1 H 1 1.69 . . 1 . . . . . . . . 495 1 377 . 1 1 102 102 ALA HB2 H 1 1.69 . . 1 . . . . . . . . 495 1 378 . 1 1 102 102 ALA HB3 H 1 1.69 . . 1 . . . . . . . . 495 1 379 . 1 1 103 103 LEU HA H 1 3.34 . . 1 . . . . . . . . 495 1 380 . 1 1 103 103 LEU HB2 H 1 1.72 . . 1 . . . . . . . . 495 1 381 . 1 1 103 103 LEU HB3 H 1 1.72 . . 1 . . . . . . . . 495 1 382 . 1 1 104 104 VAL HA H 1 3.98 . . 1 . . . . . . . . 495 1 383 . 1 1 104 104 VAL HB H 1 2.1 . . 1 . . . . . . . . 495 1 384 . 1 1 104 104 VAL HG11 H 1 1.05 . . 1 . . . . . . . . 495 1 385 . 1 1 104 104 VAL HG12 H 1 1.05 . . 1 . . . . . . . . 495 1 386 . 1 1 104 104 VAL HG13 H 1 1.05 . . 1 . . . . . . . . 495 1 387 . 1 1 104 104 VAL HG21 H 1 1.05 . . 1 . . . . . . . . 495 1 388 . 1 1 104 104 VAL HG22 H 1 1.05 . . 1 . . . . . . . . 495 1 389 . 1 1 104 104 VAL HG23 H 1 1.05 . . 1 . . . . . . . . 495 1 390 . 1 1 105 105 ARG HA H 1 4.03 . . 1 . . . . . . . . 495 1 391 . 1 1 105 105 ARG HB2 H 1 1.98 . . 1 . . . . . . . . 495 1 392 . 1 1 105 105 ARG HB3 H 1 1.98 . . 1 . . . . . . . . 495 1 393 . 1 1 106 106 GLN HA H 1 4.3 . . 1 . . . . . . . . 495 1 394 . 1 1 106 106 GLN HB2 H 1 1.49 . . 1 . . . . . . . . 495 1 395 . 1 1 106 106 GLN HB3 H 1 1.49 . . 1 . . . . . . . . 495 1 396 . 1 1 107 107 GLY HA2 H 1 4.01 . . 2 . . . . . . . . 495 1 397 . 1 1 107 107 GLY HA3 H 1 4.28 . . 2 . . . . . . . . 495 1 398 . 1 1 108 108 LEU HA H 1 4.33 . . 1 . . . . . . . . 495 1 399 . 1 1 108 108 LEU HB2 H 1 1.99 . . 1 . . . . . . . . 495 1 400 . 1 1 108 108 LEU HB3 H 1 1.99 . . 1 . . . . . . . . 495 1 401 . 1 1 109 109 ALA HA H 1 4.53 . . 1 . . . . . . . . 495 1 402 . 1 1 109 109 ALA HB1 H 1 1.03 . . 1 . . . . . . . . 495 1 403 . 1 1 109 109 ALA HB2 H 1 1.03 . . 1 . . . . . . . . 495 1 404 . 1 1 109 109 ALA HB3 H 1 1.03 . . 1 . . . . . . . . 495 1 405 . 1 1 110 110 LYS HA H 1 5.11 . . 1 . . . . . . . . 495 1 406 . 1 1 110 110 LYS HB2 H 1 1.83 . . 1 . . . . . . . . 495 1 407 . 1 1 110 110 LYS HB3 H 1 1.83 . . 1 . . . . . . . . 495 1 408 . 1 1 111 111 VAL HA H 1 4.71 . . 1 . . . . . . . . 495 1 409 . 1 1 111 111 VAL HB H 1 1.99 . . 1 . . . . . . . . 495 1 410 . 1 1 111 111 VAL HG11 H 1 .85 . . 2 . . . . . . . . 495 1 411 . 1 1 111 111 VAL HG12 H 1 .85 . . 2 . . . . . . . . 495 1 412 . 1 1 111 111 VAL HG13 H 1 .85 . . 2 . . . . . . . . 495 1 413 . 1 1 111 111 VAL HG21 H 1 .9 . . 2 . . . . . . . . 495 1 414 . 1 1 111 111 VAL HG22 H 1 .9 . . 2 . . . . . . . . 495 1 415 . 1 1 111 111 VAL HG23 H 1 .9 . . 2 . . . . . . . . 495 1 416 . 1 1 112 112 ALA HA H 1 4.17 . . 1 . . . . . . . . 495 1 417 . 1 1 112 112 ALA HB1 H 1 .8 . . 1 . . . . . . . . 495 1 418 . 1 1 112 112 ALA HB2 H 1 .8 . . 1 . . . . . . . . 495 1 419 . 1 1 112 112 ALA HB3 H 1 .8 . . 1 . . . . . . . . 495 1 420 . 1 1 113 113 TYR HA H 1 3.44 . . 1 . . . . . . . . 495 1 421 . 1 1 113 113 TYR HB2 H 1 2.57 . . 2 . . . . . . . . 495 1 422 . 1 1 113 113 TYR HB3 H 1 2.97 . . 2 . . . . . . . . 495 1 423 . 1 1 113 113 TYR HD1 H 1 6.98 . . 1 . . . . . . . . 495 1 424 . 1 1 113 113 TYR HD2 H 1 6.98 . . 1 . . . . . . . . 495 1 425 . 1 1 113 113 TYR HE1 H 1 6.74 . . 1 . . . . . . . . 495 1 426 . 1 1 113 113 TYR HE2 H 1 6.74 . . 1 . . . . . . . . 495 1 427 . 1 1 114 114 VAL HA H 1 3.6 . . 1 . . . . . . . . 495 1 428 . 1 1 114 114 VAL HB H 1 1.93 . . 1 . . . . . . . . 495 1 429 . 1 1 114 114 VAL HG11 H 1 .58 . . 2 . . . . . . . . 495 1 430 . 1 1 114 114 VAL HG12 H 1 .58 . . 2 . . . . . . . . 495 1 431 . 1 1 114 114 VAL HG13 H 1 .58 . . 2 . . . . . . . . 495 1 432 . 1 1 114 114 VAL HG21 H 1 .71 . . 2 . . . . . . . . 495 1 433 . 1 1 114 114 VAL HG22 H 1 .71 . . 2 . . . . . . . . 495 1 434 . 1 1 114 114 VAL HG23 H 1 .71 . . 2 . . . . . . . . 495 1 435 . 1 1 115 115 TYR HA H 1 5.03 . . 1 . . . . . . . . 495 1 436 . 1 1 115 115 TYR HB2 H 1 3 . . 2 . . . . . . . . 495 1 437 . 1 1 115 115 TYR HB3 H 1 3.11 . . 2 . . . . . . . . 495 1 438 . 1 1 115 115 TYR HD1 H 1 7.15 . . 1 . . . . . . . . 495 1 439 . 1 1 115 115 TYR HD2 H 1 7.15 . . 1 . . . . . . . . 495 1 440 . 1 1 115 115 TYR HE1 H 1 6.6 . . 1 . . . . . . . . 495 1 441 . 1 1 115 115 TYR HE2 H 1 6.6 . . 1 . . . . . . . . 495 1 442 . 1 1 116 116 LYS HA H 1 4.01 . . 1 . . . . . . . . 495 1 443 . 1 1 116 116 LYS HB2 H 1 1.76 . . 1 . . . . . . . . 495 1 444 . 1 1 116 116 LYS HB3 H 1 1.76 . . 1 . . . . . . . . 495 1 445 . 1 1 118 118 ASN HA H 1 5.32 . . 1 . . . . . . . . 495 1 446 . 1 1 118 118 ASN HB2 H 1 3.12 . . 1 . . . . . . . . 495 1 447 . 1 1 118 118 ASN HB3 H 1 3.12 . . 1 . . . . . . . . 495 1 448 . 1 1 119 119 ASN HA H 1 5.04 . . 1 . . . . . . . . 495 1 449 . 1 1 119 119 ASN HB2 H 1 2.18 . . 1 . . . . . . . . 495 1 450 . 1 1 119 119 ASN HB3 H 1 2.18 . . 1 . . . . . . . . 495 1 451 . 1 1 120 120 THR HA H 1 3.91 . . 1 . . . . . . . . 495 1 452 . 1 1 120 120 THR HB H 1 3.81 . . 1 . . . . . . . . 495 1 453 . 1 1 120 120 THR HG21 H 1 .77 . . 1 . . . . . . . . 495 1 454 . 1 1 120 120 THR HG22 H 1 .77 . . 1 . . . . . . . . 495 1 455 . 1 1 120 120 THR HG23 H 1 .77 . . 1 . . . . . . . . 495 1 456 . 1 1 121 121 HIS HA H 1 5.47 . . 1 . . . . . . . . 495 1 457 . 1 1 121 121 HIS HB2 H 1 2.35 . . 2 . . . . . . . . 495 1 458 . 1 1 121 121 HIS HB3 H 1 3.28 . . 2 . . . . . . . . 495 1 459 . 1 1 122 122 GLU HA H 1 3.71 . . 1 . . . . . . . . 495 1 460 . 1 1 122 122 GLU HB2 H 1 2.19 . . 1 . . . . . . . . 495 1 461 . 1 1 122 122 GLU HB3 H 1 2.19 . . 1 . . . . . . . . 495 1 462 . 1 1 123 123 GLN HA H 1 4 . . 1 . . . . . . . . 495 1 463 . 1 1 123 123 GLN HB2 H 1 2.14 . . 1 . . . . . . . . 495 1 464 . 1 1 123 123 GLN HB3 H 1 2.14 . . 1 . . . . . . . . 495 1 465 . 1 1 124 124 LEU HA H 1 4.12 . . 1 . . . . . . . . 495 1 466 . 1 1 124 124 LEU HB2 H 1 1.78 . . 1 . . . . . . . . 495 1 467 . 1 1 124 124 LEU HB3 H 1 1.78 . . 1 . . . . . . . . 495 1 468 . 1 1 125 125 LEU HA H 1 4.03 . . 1 . . . . . . . . 495 1 469 . 1 1 125 125 LEU HB2 H 1 1.9 . . 1 . . . . . . . . 495 1 470 . 1 1 125 125 LEU HB3 H 1 1.9 . . 1 . . . . . . . . 495 1 471 . 1 1 126 126 ARG HA H 1 4 . . 1 . . . . . . . . 495 1 472 . 1 1 126 126 ARG HB2 H 1 1.98 . . 1 . . . . . . . . 495 1 473 . 1 1 126 126 ARG HB3 H 1 1.98 . . 1 . . . . . . . . 495 1 474 . 1 1 127 127 LYS HA H 1 4.16 . . 1 . . . . . . . . 495 1 475 . 1 1 127 127 LYS HB2 H 1 2.02 . . 1 . . . . . . . . 495 1 476 . 1 1 127 127 LYS HB3 H 1 2.02 . . 1 . . . . . . . . 495 1 477 . 1 1 128 128 SER HA H 1 4.33 . . 1 . . . . . . . . 495 1 478 . 1 1 128 128 SER HB2 H 1 4.1 . . 1 . . . . . . . . 495 1 479 . 1 1 128 128 SER HB3 H 1 4.1 . . 1 . . . . . . . . 495 1 480 . 1 1 129 129 GLU HA H 1 3.9 . . 1 . . . . . . . . 495 1 481 . 1 1 129 129 GLU HB2 H 1 2.2 . . 1 . . . . . . . . 495 1 482 . 1 1 129 129 GLU HB3 H 1 2.2 . . 1 . . . . . . . . 495 1 483 . 1 1 130 130 ALA HA H 1 3.84 . . 1 . . . . . . . . 495 1 484 . 1 1 130 130 ALA HB1 H 1 1.48 . . 1 . . . . . . . . 495 1 485 . 1 1 130 130 ALA HB2 H 1 1.48 . . 1 . . . . . . . . 495 1 486 . 1 1 130 130 ALA HB3 H 1 1.48 . . 1 . . . . . . . . 495 1 487 . 1 1 131 131 GLN HA H 1 4 . . 1 . . . . . . . . 495 1 488 . 1 1 131 131 GLN HB2 H 1 2.2 . . 1 . . . . . . . . 495 1 489 . 1 1 131 131 GLN HB3 H 1 2.2 . . 1 . . . . . . . . 495 1 490 . 1 1 132 132 ALA HA H 1 3.96 . . 1 . . . . . . . . 495 1 491 . 1 1 132 132 ALA HB1 H 1 1.75 . . 1 . . . . . . . . 495 1 492 . 1 1 132 132 ALA HB2 H 1 1.75 . . 1 . . . . . . . . 495 1 493 . 1 1 132 132 ALA HB3 H 1 1.75 . . 1 . . . . . . . . 495 1 494 . 1 1 133 133 LYS HA H 1 3.41 . . 1 . . . . . . . . 495 1 495 . 1 1 133 133 LYS HB2 H 1 1.25 . . 1 . . . . . . . . 495 1 496 . 1 1 133 133 LYS HB3 H 1 1.25 . . 1 . . . . . . . . 495 1 497 . 1 1 134 134 LYS HA H 1 3.97 . . 1 . . . . . . . . 495 1 498 . 1 1 134 134 LYS HB2 H 1 1.95 . . 1 . . . . . . . . 495 1 499 . 1 1 134 134 LYS HB3 H 1 1.95 . . 1 . . . . . . . . 495 1 500 . 1 1 135 135 GLU HA H 1 4.06 . . 1 . . . . . . . . 495 1 501 . 1 1 135 135 GLU HB2 H 1 2.03 . . 1 . . . . . . . . 495 1 502 . 1 1 135 135 GLU HB3 H 1 2.03 . . 1 . . . . . . . . 495 1 503 . 1 1 136 136 LYS HA H 1 3.54 . . 1 . . . . . . . . 495 1 504 . 1 1 136 136 LYS HB2 H 1 2.06 . . 1 . . . . . . . . 495 1 505 . 1 1 136 136 LYS HB3 H 1 2.06 . . 1 . . . . . . . . 495 1 506 . 1 1 137 137 LEU HA H 1 4.19 . . 1 . . . . . . . . 495 1 507 . 1 1 137 137 LEU HB2 H 1 1.52 . . 1 . . . . . . . . 495 1 508 . 1 1 137 137 LEU HB3 H 1 1.52 . . 1 . . . . . . . . 495 1 509 . 1 1 138 138 ASN HA H 1 3.86 . . 1 . . . . . . . . 495 1 510 . 1 1 138 138 ASN HB2 H 1 2.77 . . 1 . . . . . . . . 495 1 511 . 1 1 138 138 ASN HB3 H 1 2.77 . . 1 . . . . . . . . 495 1 512 . 1 1 139 139 ILE HA H 1 3.32 . . 1 . . . . . . . . 495 1 513 . 1 1 139 139 ILE HB H 1 1.05 . . 1 . . . . . . . . 495 1 514 . 1 1 139 139 ILE HG12 H 1 .5 . . 1 . . . . . . . . 495 1 515 . 1 1 139 139 ILE HG13 H 1 .5 . . 1 . . . . . . . . 495 1 516 . 1 1 139 139 ILE HG21 H 1 .12 . . 1 . . . . . . . . 495 1 517 . 1 1 139 139 ILE HG22 H 1 .12 . . 1 . . . . . . . . 495 1 518 . 1 1 139 139 ILE HG23 H 1 .12 . . 1 . . . . . . . . 495 1 519 . 1 1 139 139 ILE HD11 H 1 .06 . . 1 . . . . . . . . 495 1 520 . 1 1 139 139 ILE HD12 H 1 .06 . . 1 . . . . . . . . 495 1 521 . 1 1 139 139 ILE HD13 H 1 .06 . . 1 . . . . . . . . 495 1 522 . 1 1 140 140 TRP HA H 1 4.91 . . 1 . . . . . . . . 495 1 523 . 1 1 140 140 TRP HB2 H 1 2.83 . . 2 . . . . . . . . 495 1 524 . 1 1 140 140 TRP HB3 H 1 3.71 . . 2 . . . . . . . . 495 1 525 . 1 1 140 140 TRP HD1 H 1 7 . . 1 . . . . . . . . 495 1 526 . 1 1 140 140 TRP HE3 H 1 7.66 . . 1 . . . . . . . . 495 1 527 . 1 1 140 140 TRP HZ2 H 1 7.54 . . 1 . . . . . . . . 495 1 528 . 1 1 140 140 TRP HZ3 H 1 7.06 . . 1 . . . . . . . . 495 1 529 . 1 1 140 140 TRP HH2 H 1 7.12 . . 1 . . . . . . . . 495 1 530 . 1 1 141 141 SER HA H 1 4.19 . . 1 . . . . . . . . 495 1 531 . 1 1 141 141 SER HB2 H 1 3.81 . . 2 . . . . . . . . 495 1 532 . 1 1 141 141 SER HB3 H 1 3.87 . . 2 . . . . . . . . 495 1 533 . 1 1 142 142 GLU HA H 1 4.43 . . 1 . . . . . . . . 495 1 534 . 1 1 142 142 GLU HB2 H 1 1.97 . . 2 . . . . . . . . 495 1 535 . 1 1 142 142 GLU HB3 H 1 2.19 . . 2 . . . . . . . . 495 1 536 . 1 1 143 143 ASP HA H 1 4.64 . . 1 . . . . . . . . 495 1 537 . 1 1 143 143 ASP HB2 H 1 2.68 . . 2 . . . . . . . . 495 1 538 . 1 1 143 143 ASP HB3 H 1 2.78 . . 2 . . . . . . . . 495 1 stop_ save_