data_4905 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N Chemical Shift Assignments for Urea-denatured G88W-110 Fragment of Staphylococcal Nuclease ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ye Keqiong . . 2 Wang Jinfeng . . stop_ _BMRB_accession_number 4905 _BMRB_flat_file_name bmr4905.str _Entry_type new _Submission_date 2000-11-24 _Accession_date 2000-11-27 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 583 '13C chemical shifts' 322 '15N chemical shifts' 104 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Self-association Reaction of Denatured Staphylococcal Nuclease Fragments Characterized by Heteronuclear NMR ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 21140180 _PubMed_ID 11243822 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ye Keqiong . . 2 Wang Jinfeng . . stop_ _Journal_abbreviation "J. Mol. Biol." _Journal_name_full "Journal of Molecular Biology" _Journal_volume 307 _Journal_issue 1 _Page_first 309 _Page_last 322 _Year 2001 loop_ _Keyword "Denatured Protein" Self-association "Staphylococcal Nuclease" stop_ save_ ################################## # Molecular system description # ################################## save_SN-G88W-110 _Saveframe_category molecular_system _Mol_system_name "G88W110 fragment of staphylococcal nuclease" _Abbreviation_common SN-G88W-110 _Enzyme_commission_number 3.1.31.1 loop_ _Mol_system_component_name _Mol_label "SNase G88W110 fragment" $Snase stop_ _System_physical_state denatured _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' save_ ######################## # Monomeric polymers # ######################## save_Snase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "Staphylococcal Nuclease" _Name_variant G88W-110 _Abbreviation_common Snase _Mol_thiol_state 'not present' _Details ; Contains residues 1-110 and mutation Gly88Trp of Staphylococcal Nuclease ; ############################## # Polymer residue sequence # ############################## _Residue_count 110 _Mol_residue_sequence ; ATSTKKLHKEPATLIKAIDG DTVKLMYKGQPMTFRLLLVD TPETKHPKKGVEKYGPEASA FTKKMVENAKKIEVEFDKGQ RTDKYGRWLAYIYADGKMVN EALVRQGLAK ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 THR 3 SER 4 THR 5 LYS 6 LYS 7 LEU 8 HIS 9 LYS 10 GLU 11 PRO 12 ALA 13 THR 14 LEU 15 ILE 16 LYS 17 ALA 18 ILE 19 ASP 20 GLY 21 ASP 22 THR 23 VAL 24 LYS 25 LEU 26 MET 27 TYR 28 LYS 29 GLY 30 GLN 31 PRO 32 MET 33 THR 34 PHE 35 ARG 36 LEU 37 LEU 38 LEU 39 VAL 40 ASP 41 THR 42 PRO 43 GLU 44 THR 45 LYS 46 HIS 47 PRO 48 LYS 49 LYS 50 GLY 51 VAL 52 GLU 53 LYS 54 TYR 55 GLY 56 PRO 57 GLU 58 ALA 59 SER 60 ALA 61 PHE 62 THR 63 LYS 64 LYS 65 MET 66 VAL 67 GLU 68 ASN 69 ALA 70 LYS 71 LYS 72 ILE 73 GLU 74 VAL 75 GLU 76 PHE 77 ASP 78 LYS 79 GLY 80 GLN 81 ARG 82 THR 83 ASP 84 LYS 85 TYR 86 GLY 87 ARG 88 TRP 89 LEU 90 ALA 91 TYR 92 ILE 93 TYR 94 ALA 95 ASP 96 GLY 97 LYS 98 MET 99 VAL 100 ASN 101 GLU 102 ALA 103 LEU 104 VAL 105 ARG 106 GLN 107 GLY 108 LEU 109 ALA 110 LYS stop_ _Sequence_homology_query_date 2009-06-13 _Sequence_homology_query_revised_last_date 2008-12-06 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 136 "micrococcal nuclease" 100.00 156 98.18 99.09 8.07e-56 BMRB 1581 "micrococcal nuclease" 95.45 144 98.10 99.05 3.45e-53 BMRB 1704 "micrococcal nuclease" 100.00 143 99.09 99.09 3.28e-56 BMRB 1874 "micrococcal nuclease" 100.00 143 99.09 99.09 3.28e-56 BMRB 1875 "micrococcal nuclease" 100.00 143 99.09 99.09 3.28e-56 BMRB 1876 "micrococcal nuclease" 100.00 143 99.09 99.09 3.28e-56 BMRB 1877 "micrococcal nuclease" 100.00 143 99.09 99.09 3.28e-56 BMRB 1878 "micrococcal nuclease" 100.00 143 99.09 99.09 3.28e-56 BMRB 188 "micrococcal nuclease" 100.00 156 98.18 99.09 8.07e-56 BMRB 189 "micrococcal nuclease" 100.00 156 98.18 99.09 8.07e-56 BMRB 2784 "micrococcal nuclease" 100.00 156 98.18 99.09 8.07e-56 BMRB 2785 "micrococcal nuclease" 100.00 156 98.18 99.09 8.07e-56 BMRB 4010 SNOB 93.64 103 98.06 99.03 1.11e-51 BMRB 4052 "staphylococcal nuclease" 100.00 149 99.09 99.09 2.33e-56 BMRB 4053 "staphylococcal nuclease" 100.00 149 99.09 99.09 2.33e-56 BMRB 494 "micrococcal nuclease" 100.00 143 99.09 99.09 3.28e-56 BMRB 495 "micrococcal nuclease" 100.00 143 99.09 99.09 3.28e-56 BMRB 496 "micrococcal nuclease" 100.00 143 99.09 99.09 3.28e-56 BMRB 497 "micrococcal nuclease" 100.00 143 99.09 99.09 3.28e-56 BMRB 530 "micrococcal nuclease" 100.00 143 99.09 99.09 3.28e-56 BMRB 5536 "Staphylococcal nuclease" 100.00 110 100.00 100.00 2.27e-57 BMRB 6250 G88W121 100.00 121 100.00 100.00 1.87e-57 BMRB 6251 V66W121 100.00 121 98.18 98.18 6.94e-55 BMRB 644 "micrococcal nuclease" 100.00 156 98.18 99.09 8.07e-56 BMRB 6907 "V66W110 fragment of staphylococcal nuclease" 100.00 110 98.18 98.18 6.18e-55 BMRB 6908 "SNase110 fragment of Staphylococcal Nuclease" 100.00 110 99.09 99.09 3.87e-56 PDB 1A2T "Staphylococcal Nuclease, B-Mercaptoethanol Disulfide To V23c Variant" 100.00 149 98.18 98.18 1.12e-55 PDB 1A2U "Staphylococcal Nuclease, V23c Variant, Complex With 1-N- Butane Thiol And 3',5'-Thymidine Diphosphate" 100.00 149 98.18 98.18 1.12e-55 PDB 1A3T "Staphylococcal Nuclease, V23c Variant, Complex With 2- Fluoroethane Thiol And 3',5'-Thymidine Diphosphate" 100.00 149 98.18 98.18 1.12e-55 PDB 1A3U "Staphylococcal Nuclease, Cyclohexane Thiol Disulfide To V23c Variant" 100.00 149 98.18 98.18 1.12e-55 PDB 1A3V "Staphylococcal Nuclease, Cyclopentane Thiol Disulfide To V23c Variant" 100.00 149 98.18 98.18 1.12e-55 PDB 1AEX "Staphylococcal Nuclease, Methane Thiol Disulfide To V23c Variant" 100.00 149 98.18 98.18 1.12e-55 PDB 1ENA "Crystal Structures Of The Binary Ca2+ And Pdtp Complexes And The Ternary Complex Of The Asp 21->glu Mutant Of Staphylococcal Nuclease. Implications For Catalysis And Ligand Binding" 94.55 135 98.08 99.04 1.37e-52 PDB 1ENC "Crystal Structures Of The Binary Ca2+ And Pdtp Complexes And The Ternary Complex Of The Asp 21->glu Mutant Of Staphylococcal Nuclease. Implications For Catalysis And Ligand Binding" 100.00 149 98.18 99.09 7.67e-56 PDB 1EQV "Simplification Of A Protein Loop In Staphylococcal Nuclease" 95.45 136 99.05 99.05 8.85e-54 PDB 1EY0 "Structure Of Wild-Type S. Nuclease At 1.6 A Resolution" 100.00 149 99.09 99.09 2.57e-56 PDB 1EY4 "Structure Of S. Nuclease Stabilizing Mutant S59a" 100.00 149 98.18 99.09 5.83e-56 PDB 1EY5 "Structure Of S. Nuclease Stabilizing Mutant T33v" 100.00 149 98.18 98.18 8.27e-56 PDB 1EY6 "Structure Of S. Nuclease Stabilizing Mutant T41i" 100.00 149 98.18 98.18 1.04e-55 PDB 1EY7 "Structure Of S. Nuclease Stabilizing Mutant S128a" 100.00 149 99.09 99.09 2.41e-56 PDB 1EY8 "Structure Of S. Nuclease Stabilizing Triple Mutant P117gH124LS128A" 100.00 149 99.09 99.09 2.31e-56 PDB 1EY9 "Structure Of S. Nuclease Stabilizing Quadruple Mutant T41iP117GH124LS128A" 100.00 149 98.18 98.18 9.61e-56 PDB 1EYD "Structure Of Wild-Type S. Nuclease At 1.7 A Resolution" 100.00 149 99.09 99.09 2.57e-56 PDB 1EZ8 "Structure Of S. Nuclease Stabilizing Mutant T33v" 100.00 149 98.18 98.18 8.27e-56 PDB 1F2M "Simplification Of A Protein Loop In Staphylococcal Nuclease" 100.00 149 99.09 99.09 1.92e-56 PDB 1F2Y "Simplification Of A Protein Loop In Staphylococcal Nuclease" 100.00 149 99.09 99.09 1.71e-56 PDB 1F2Z "Simplification Of A Protein Loop In Staphylococcal Nuclease" 100.00 149 99.09 99.09 1.71e-56 PDB 1JOK "Averaged Structure For Staphylococcal Nuclease-H124l In Ternary Complex With Ca2+ And Thymidine-3',5'-Bisphosphate" 100.00 149 99.09 99.09 2.33e-56 PDB 1JOO "Averaged Structure For Unligated Staphylococcal Nuclease- H124l" 100.00 149 99.09 99.09 2.33e-56 PDB 1JOQ "Ensemble Structures For Staphylococcal Nuclease-H124l In Ternary Complex With Ca2+ And Thymidine-3',5'-Bisphosphate" 100.00 149 99.09 99.09 2.33e-56 PDB 1JOR "Ensemble Structures For Unligated Staphylococcal Nuclease- H124l" 100.00 149 99.09 99.09 2.33e-56 PDB 1KAA "Stress And Strain In Staphylococcal Nuclease" 95.45 136 99.05 99.05 1.56e-53 PDB 1KAB "Stress And Strain In Staphylococcal Nuclease" 95.45 136 99.05 99.05 1.87e-53 PDB 1KDA "Stabilization Of A Strained Protein Loop Conformation Through Protein Engineering" 100.00 149 99.09 99.09 2.51e-56 PDB 1KDB "Stabilization Of A Strained Protein Loop Conformation Through Protein Engineering" 100.00 149 99.09 99.09 2.53e-56 PDB 1KDC "Stabilization Of A Strained Protein Loop Conformation Through Protein Engineering" 100.00 149 99.09 99.09 2.33e-56 PDB 1NSN "The Crystal Structure Of Antibody N10-Staphylococcal Nuclease Complex At 2.9 Angstroms Resolution" 100.00 149 99.09 99.09 2.57e-56 PDB 1NUC "Staphylococcal Nuclease, V23c Variant" 100.00 149 98.18 98.18 6.33e-56 PDB 1RKN "Solution Structure Of 1-110 Fragment Of Staphylococcal Nuclease With G88w Mutation" 100.00 110 100.00 100.00 2.27e-57 PDB 1SNC "The Crystal Structure Of The Ternary Complex Of Staphylococcal Nuclease, Ca2+, And The Inhibitor PdTp, Refined At 1.65 Angstroms" 100.00 149 99.09 99.09 2.57e-56 PDB 1SND "Staphylococcal Nuclease Dimer Containing A Deletion Of Residues 114-119 Complexed With Calcium Chloride And The Competitive Inhibitor Deoxythymidine-3',5'-Diphosphate" 100.00 143 99.09 99.09 2.25e-56 PDB 1SNM "Active Site Mutant Glu-43 (Right Arrow) Asp In Staphylococcal Nuclease Displays Nonlocal Structural Changes" 100.00 149 98.18 99.09 6.77e-56 PDB 1SNO "Protein Stability In Staphylococcal Nuclease" 100.00 149 99.09 99.09 2.33e-56 PDB 1SNP "Protein Stability In Staphylococcal Nuclease" 100.00 149 99.09 99.09 2.19e-56 PDB 1SNQ "Protein Stability In Staphylococcal Nuclease" 100.00 149 98.18 98.18 2.05e-55 PDB 1STB "Accommodation Of Insertion Mutations On The Surface And In The Interior Of Staphylococcal Nuclease" 100.91 150 98.20 98.20 6.02e-55 PDB 1STG "Two Distinctly Different Metal Binding Modes Are Seen In X- Ray Crystal Structures Of Staphylococcal Nuclease- Cobalt(Ii)-Nucleotide Complexes" 100.00 149 99.09 99.09 2.57e-56 PDB 1STH "Two Distinctly Different Metal Binding Modes Are Seen In X- Ray Crystal Structures Of Staphylococcal Nuclease- Cobalt(Ii)-Nucleotide Complexes" 100.00 149 99.09 99.09 2.57e-56 PDB 1STN "The Crystal Structure Of Staphylococcal Nuclease Refined At 1.7 Angstroms Resolution" 100.00 149 99.09 99.09 2.57e-56 PDB 1STY "The Alpha Aneurism: A Structural Motif Revealed In An Insertion Mutant Of Staphylococcal Nuclease" 100.00 150 99.09 99.09 2.91e-56 PDB 1SYC "Engineering Alternative Beta-Turn Types In Staphylococcal Nuclease" 100.00 149 99.09 99.09 2.10e-56 PDB 1SYD "Engineering Alternative Beta-Turn Types In Staphylococcal Nuclease" 100.00 149 99.09 99.09 2.10e-56 PDB 1SYE "Engineering Alternative Beta-Turn Types In Staphylococcal Nuclease" 100.00 149 99.09 99.09 1.84e-56 PDB 1SYF "Engineering Alternative Beta-Turn Types In Staphylococcal Nuclease" 100.00 149 99.09 99.09 1.84e-56 PDB 1SYG "Engineering Alternative Beta-Turn Types In Staphylococcal Nuclease" 100.00 149 99.09 99.09 1.72e-56 PDB 1U9R "Crystal Structure Of Staphylococcal Nuclease Mutant V66eP117GH124LS128A AT ROOM TEMPERATURE" 100.00 149 98.18 98.18 1.39e-55 PDB 2ENB "Crystal Structures Of The Binary Ca2+ And Pdtp Complexes And The Ternary Complex Of The Asp 21->glu Mutant Of Staphylococcal Nuclease. Implications For Catalysis And Ligand Binding" 94.55 135 98.08 99.04 1.37e-52 PDB 2EXZ "Crystal Structure Of Staphylococcal Nuclease Mutant T22c" 100.00 149 98.18 98.18 7.74e-56 PDB 2EY1 "Crystal Structure Of Staphylococcal Nuclease Mutant T22v" 100.00 149 98.18 98.18 8.27e-56 PDB 2EY2 "Crystal Structure Of Staphylococcal Nuclease Mutant T41c" 100.00 149 98.18 98.18 7.74e-56 PDB 2EY5 "Crystal Structure Of Staphylococcal Nuclease Mutant T41s" 100.00 149 98.18 99.09 4.81e-56 PDB 2EY6 "Crystal Structure Of Staphylococcal Nuclease Mutant T41v" 100.00 149 98.18 98.18 8.27e-56 PDB 2EYF "Crystal Structure Of Staphylococcal Nuclease Mutant T44v" 100.00 149 98.18 98.18 8.27e-56 PDB 2EYH "Crystal Structure Of Staphylococcal Nuclease Mutant T62s" 100.00 149 98.18 99.09 4.81e-56 PDB 2EYJ "Crystal Structure Of Staphylococcal Nuclease Mutant T62v" 100.00 149 98.18 98.18 8.27e-56 PDB 2EYL "Crystal Structure Of Staphylococcal Nuclease Mutant T82s" 100.00 149 98.18 99.09 4.81e-56 PDB 2EYM "Crystal Structure Of Staphylococcal Nuclease Mutant T120c" 100.00 149 99.09 99.09 2.55e-56 PDB 2EYO "Crystal Structure Of Staphylococcal Nuclease Mutant T120s" 100.00 149 99.09 99.09 2.16e-56 PDB 2EYP "Crystal Structure Of Staphylococcal Nuclease Mutant T120v" 100.00 149 99.09 99.09 2.35e-56 PDB 2F0D "Crystal Structure Of Staphylococcal Nuclease Mutant I92v" 100.00 149 98.18 99.09 3.44e-56 PDB 2F0E "Crystal Structure Of Staphylococcal Nuclease Mutant V23l" 100.00 149 98.18 99.09 5.78e-56 PDB 2F0F "Crystal Structure Of Staphylococcal Nuclease Mutant L25i" 100.00 149 98.18 99.09 4.65e-56 PDB 2F0G "Crystal Structure Of Staphylococcal Nuclease Mutant V66i" 100.00 149 98.18 99.09 3.59e-56 PDB 2F0H "Crystal Structure Of Staphylococcal Nuclease Mutant V66l" 100.00 149 98.18 99.09 5.78e-56 PDB 2F0I "Crystal Structure Of Staphylococcal Nuclease Mutant I72l" 100.00 149 98.18 99.09 5.40e-56 PDB 2F0J "Crystal Structure Of Staphylococcal Nuclease Mutant I72v" 100.00 149 98.18 99.09 3.44e-56 PDB 2F3V "Solution Structure Of 1-110 Fragment Of Staphylococcal Nuclease With V66w Mutation" 100.00 110 98.18 98.18 6.18e-55 PDB 2F3W "Solution Structure Of 1-110 Fragment Of Staphylococcal Nuclease In 2m Tmao" 100.00 110 99.09 99.09 3.87e-56 PDB 2NUC "Staphlococcal Nuclease, Ethane Thiol Disulfide To V23c Variant" 100.00 149 98.18 98.18 1.12e-55 PDB 2OXP "Crystal Structure Of Staphylococcal Nuclease Mutant V66dP117GH124LS128A" 100.00 149 98.18 98.18 1.68e-55 PDB 2PW5 "Crystal Structure Of Staphylococcal Nuclease Variant V66yP117GH124LS128A AT ROOM TEMPERATURE" 100.00 149 98.18 98.18 1.08e-55 PDB 2PW7 "Crystal Structure Of Staphylococcal Nuclease Variant V66yP117GH124LS128A AT 100K" 100.00 149 98.18 98.18 1.08e-55 PDB 2PYK "Crystal Structure Of Staphylococcal Nuclease Variant V66qP117GH124LS128A AT ROOM TEMPERATURE" 100.00 149 98.18 98.18 1.17e-55 PDB 2PZT "Crystal Structure Of Staphylococcal Nuclease Variant V66qP117GH124LS128A AT 100 K" 100.00 149 98.18 98.18 1.17e-55 PDB 2PZU "Crystal Structure Of Staphylococcal Nuclease Variant V66nP117GH124LS128A AT CRYOGENIC TEMPERATURE" 100.00 149 98.18 98.18 1.26e-55 PDB 2PZW "Crystal Structure Of Staphylococcal Nuclease Variant V66nP117GH124LS128A AT ROOM TEMPERATURE" 100.00 149 98.18 98.18 1.26e-55 PDB 2RKS "Crystal Structure Of Staphylococcal Nuclease Variant Phs L38k At Cryogenic Temperature" 100.00 149 98.18 98.18 1.68e-55 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 98.18 98.18 1.55e-55 PDB 2SNS "Staphylococcal Nuclease. Proposed Mechanism Of Action Based On Structure Of Enzyme-Thymidine 3(Prime),5(Prime)- Biphosphate-Calcium Ion Complex At 1.5-Angstroms Resolution" 100.00 149 98.18 99.09 7.18e-56 PDB 2SOB "Sn-Ob, Ob-Fold Sub-Domain Of Staphylococcal Nuclease, Nmr, 10 Structures" 93.64 103 98.06 99.03 1.11e-51 PDB 3D6C "Crystal Structure Of Staphylococcal Nuclease Variant Phs L38e At Cryogenic Temperature" 100.00 149 98.18 98.18 1.57e-55 PDB 3DMU "Crystal Structure Of Staphylococcal Nuclease Variant Phs T62k At Cryogenic Temperature" 100.00 149 98.18 98.18 1.16e-55 PDB 3NUC "Staphlococcal Nuclease, 1-N-Propane Thiol Disulfide To V23c Variant" 100.00 149 98.18 98.18 1.12e-55 PDB 5NUC "Staphylococcal Nuclease, 1-N-Pentane Thiol Disulfide To V23c Variant" 100.00 149 98.18 98.18 1.12e-55 DBJ BAB41979 "staphylococcal nuclease [Staphylococcus aureus subsp. aureus N315]" 100.00 228 98.18 98.18 6.66e-57 DBJ BAB56977 "staphylococcal nuclease [Staphylococcus aureus subsp. aureus Mu50]" 100.00 228 98.18 98.18 6.66e-57 DBJ BAB94634 "staphylococcal nuclease [Staphylococcus aureus subsp. aureus MW2]" 100.00 228 99.09 99.09 2.47e-57 DBJ BAF67032 "thermonuclease precursor [Staphylococcus aureus subsp. aureus str. Newman]" 100.00 228 99.09 99.09 2.51e-57 DBJ BAF77694 "staphylococcal nuclease [Staphylococcus aureus subsp. aureus Mu3]" 100.00 228 98.18 98.18 6.66e-57 EMBL CAA24594 "nuclease [Staphylococcus aureus]" 100.00 231 99.09 99.09 2.42e-57 EMBL CAG39855 "thermonuclease precursor [Staphylococcus aureus subsp. aureus MRSA252]" 100.00 228 99.09 99.09 2.02e-57 EMBL CAG42530 "thermonuclease precursor [Staphylococcus aureus subsp. aureus MSSA476]" 100.00 228 99.09 99.09 2.47e-57 EMBL CAI80436 "staphylococcal thermonuclease precursor [Staphylococcus aureus RF122]" 100.00 228 98.18 99.09 9.61e-57 GenBank AAC14660 "deltaSP-Nuc [Cloning vector pFUN]" 100.00 155 99.09 99.09 2.53e-56 GenBank AAW36415 "thermonuclease precursor [Staphylococcus aureus subsp. aureus COL]" 100.00 228 99.09 99.09 2.51e-57 GenBank ABD22328 "thermonuclease precursor [Staphylococcus aureus subsp. aureus USA300_FPR3757]" 100.00 228 99.09 99.09 2.51e-57 GenBank ABD29945 "thermonuclease precursor [Staphylococcus aureus subsp. aureus NCTC 8325]" 100.00 228 99.09 99.09 2.51e-57 GenBank ABE02272 "nuclease [Staphylococcus aureus]" 100.00 227 98.18 98.18 1.10e-56 PRF 1109959A nuclease,staphylococcal 100.00 242 99.09 99.09 2.36e-57 PRF 710414A nuclease 100.00 149 99.09 99.09 2.57e-56 REF NP_371339 "staphylococcal nuclease [Staphylococcus aureus subsp. aureus Mu50]" 100.00 228 98.18 98.18 6.66e-57 REF NP_374001 "staphylococcal nuclease [Staphylococcus aureus subsp. aureus N315]" 100.00 228 98.18 98.18 6.66e-57 REF NP_645586 "staphylococcal nuclease [Staphylococcus aureus subsp. aureus MW2]" 100.00 228 99.09 99.09 2.47e-57 REF YP_001246194 "micrococcal nuclease [Staphylococcus aureus subsp. aureus JH9]" 100.00 228 98.18 98.18 6.66e-57 REF YP_001315975 "micrococcal nuclease [Staphylococcus aureus subsp. aureus JH1]" 100.00 228 98.18 98.18 6.66e-57 SWISS-PROT P00644 "RecName: Full=Thermonuclease; Short=TNase; AltName: Full=Micrococcal nuclease; AltName: Full=Staphylococcal nuclease; Contains: RecName: Full=Nuclease B; Contains: RecName: Full=Nuclease A; Flags: Precursor" 100.00 231 99.09 99.09 2.42e-57 SWISS-PROT Q5HHM4 "RecName: Full=Thermonuclease; Short=TNase; AltName: Full=Micrococcal nuclease; AltName: Full=Staphylococcal nuclease; Flags: Precursor" 100.00 228 99.09 99.09 2.51e-57 SWISS-PROT Q6GB41 "RecName: Full=Thermonuclease; Short=TNase; AltName: Full=Micrococcal nuclease; AltName: Full=Staphylococcal nuclease; Flags: Precursor" 100.00 228 99.09 99.09 2.47e-57 SWISS-PROT Q6GIK1 "RecName: Full=Thermonuclease; Short=TNase; AltName: Full=Micrococcal nuclease; AltName: Full=Staphylococcal nuclease; Flags: Precursor" 100.00 228 99.09 99.09 2.02e-57 SWISS-PROT Q7A6P2 "RecName: Full=Thermonuclease; Short=TNase; AltName: Full=Micrococcal nuclease; AltName: Full=Staphylococcal nuclease; Flags: Precursor" 100.00 228 98.18 98.18 6.66e-57 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $Snase "S. aureus" 1280 Eubacteria . Staphylococcus aureus foggi stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $Snase 'recombinant technology' "E. coli" Escherichia coli BL21(DE3) plasmid pET3d ; The SN-G88W-110 was mainly expressed in the form of inclusion body. ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Snase 2.5 mM "[U-95% 13C; U-90% 15N]" "acetate buffer" 50 mM "[U-99% 2H]" Urea 6 M . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 98 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details ; HNCACB CBCA(CO)NH HNCO HN(CA)CO H(CCO)NH 3D 1H-15N TOCSY-HSQC 3D 1H-15N NOESY-HSQC 3D 1H-15N/1H-15N HSQC-NOESY-HSQC HNHA 1H-13C CT-HSQC ; save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.9 0.1 n/a temperature 305 0.1 K 'ionic strength' 0.05 0.01 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details "All HD of LYS may be overlapped with HB, and are not distinguished." loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "SNase G88W110 fragment" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 ALA C C 174.4 0.20 1 2 1 ALA CA C 51.9 0.20 1 3 1 ALA CB C 19.5 0.20 1 4 1 ALA HA H 4.19 0.01 1 5 1 ALA HB H 1.56 0.01 1 6 2 THR C C 174.387 0.20 1 7 2 THR CA C 61.968 0.20 1 8 2 THR CB C 69.981 0.20 1 9 2 THR H H 8.624 0.01 1 10 2 THR HA H 4.437 0.01 1 11 2 THR HB H 4.214 0.01 1 12 2 THR HG2 H 1.242 0.01 1 13 2 THR N N 115.439 0.20 1 14 3 SER C C 174.896 0.20 1 15 3 SER CA C 58.077 0.20 1 16 3 SER CB C 64.035 0.20 1 17 3 SER H H 8.476 0.01 1 18 3 SER HA H 4.590 0.01 1 19 3 SER HB2 H 3.867 0.01 2 20 3 SER HB3 H 3.931 0.01 2 21 3 SER N N 118.996 0.20 1 22 4 THR C C 174.555 0.20 1 23 4 THR CA C 61.857 0.20 1 24 4 THR CB C 69.751 0.20 1 25 4 THR H H 8.305 0.01 1 26 4 THR HA H 4.353 0.01 1 27 4 THR HB H 4.233 0.01 1 28 4 THR HG2 H 1.213 0.01 1 29 4 THR N N 117.160 0.20 1 30 5 LYS C C 176.326 0.20 1 31 5 LYS CA C 56.364 0.20 1 32 5 LYS CB C 33.352 0.20 1 33 5 LYS H H 8.306 0.01 1 34 5 LYS HA H 4.309 0.01 1 35 5 LYS HB2 H 1.696 0.01 4 36 5 LYS HB3 H 1.775 0.01 4 37 5 LYS HG2 H 1.380 0.01 4 38 5 LYS HG3 H 1.380 0.01 4 39 5 LYS HE2 H 2.982 0.01 1 40 5 LYS HE3 H 2.982 0.01 1 41 5 LYS N N 124.642 0.20 1 42 6 LYS C C 176.359 0.20 1 43 6 LYS CA C 56.299 0.20 1 44 6 LYS CB C 33.226 0.20 1 45 6 LYS H H 8.386 0.01 1 46 6 LYS HA H 4.307 0.01 1 47 6 LYS HB2 H 1.698 0.01 4 48 6 LYS HB3 H 1.773 0.01 4 49 6 LYS HG2 H 1.375 0.01 4 50 6 LYS HG3 H 1.437 0.01 4 51 6 LYS HE2 H 2.979 0.01 1 52 6 LYS HE3 H 2.979 0.01 1 53 6 LYS N N 123.992 0.20 1 54 7 LEU C C 177.132 0.20 1 55 7 LEU CA C 55.018 0.20 1 56 7 LEU CB C 42.671 0.20 1 57 7 LEU H H 8.325 0.01 1 58 7 LEU HA H 4.309 0.01 1 59 7 LEU HB2 H 1.574 0.01 1 60 7 LEU HB3 H 1.574 0.01 1 61 7 LEU HG H 1.478 0.01 1 62 7 LEU HD1 H 0.913 0.01 2 63 7 LEU HD2 H 0.836 0.01 2 64 7 LEU N N 124.674 0.20 1 65 8 HIS C C 174.198 0.20 1 66 8 HIS CA C 55.140 0.20 1 67 8 HIS CB C 29.494 0.20 1 68 8 HIS H H 8.634 0.01 1 69 8 HIS HA H 4.690 0.01 1 70 8 HIS HB2 H 3.162 0.01 2 71 8 HIS HB3 H 3.247 0.01 2 72 8 HIS N N 120.700 0.20 1 73 9 LYS C C 176.073 0.20 1 74 9 LYS CA C 56.294 0.20 1 75 9 LYS CB C 33.588 0.20 1 76 9 LYS H H 8.455 0.01 1 77 9 LYS HA H 4.322 0.01 1 78 9 LYS HB2 H 1.778 0.01 4 79 9 LYS HB3 H 1.676 0.01 4 80 9 LYS HG2 H 1.387 0.01 4 81 9 LYS HG3 H 1.387 0.01 4 82 9 LYS HE2 H 2.967 0.01 1 83 9 LYS HE3 H 2.967 0.01 1 84 9 LYS N N 124.708 0.20 1 85 10 GLU C C 174.429 0.20 1 86 10 GLU CA C 54.277 0.20 1 87 10 GLU CB C 29.329 0.20 1 88 10 GLU H H 8.602 0.01 1 89 10 GLU HA H 4.593 0.01 1 90 10 GLU HB2 H 1.884 0.01 2 91 10 GLU HB3 H 2.086 0.01 2 92 10 GLU HG2 H 2.369 0.01 1 93 10 GLU HG3 H 2.369 0.01 1 94 10 GLU N N 124.673 0.20 1 95 11 PRO C C 176.535 0.20 1 96 11 PRO CA C 63.103 0.20 1 97 11 PRO CB C 32.306 0.20 1 98 11 PRO HA H 4.412 0.01 1 99 11 PRO HB2 H 1.933 0.01 2 100 11 PRO HB3 H 2.304 0.01 2 101 11 PRO HG2 H 2.038 0.01 1 102 11 PRO HG3 H 2.038 0.01 1 103 11 PRO HD2 H 3.688 0.01 1 104 11 PRO HD3 H 3.688 0.01 1 105 12 ALA C C 177.907 0.20 1 106 12 ALA CA C 52.666 0.20 1 107 12 ALA CB C 19.310 0.20 1 108 12 ALA H H 8.409 0.01 1 109 12 ALA HA H 4.341 0.01 1 110 12 ALA HB H 1.398 0.01 1 111 12 ALA N N 124.966 0.20 1 112 13 THR C C 174.257 0.20 1 113 13 THR CA C 61.798 0.20 1 114 13 THR CB C 69.813 0.20 1 115 13 THR H H 8.066 0.01 1 116 13 THR HA H 4.292 0.01 1 117 13 THR HB H 4.153 0.01 1 118 13 THR HG2 H 1.198 0.01 1 119 13 THR N N 114.212 0.20 1 120 14 LEU C C 176.805 0.20 1 121 14 LEU CA C 55.130 0.20 1 122 14 LEU CB C 42.640 0.20 1 123 14 LEU H H 8.226 0.01 1 124 14 LEU HA H 4.399 0.01 1 125 14 LEU HB2 H 1.587 0.01 1 126 14 LEU HB3 H 1.587 0.01 1 127 14 LEU HD1 H 0.894 0.01 1 128 14 LEU HD2 H 0.894 0.01 1 129 14 LEU N N 125.781 0.20 1 130 15 ILE C C 176.038 0.20 1 131 15 ILE CA C 60.948 0.20 1 132 15 ILE CB C 38.762 0.20 1 133 15 ILE H H 8.207 0.01 1 134 15 ILE HA H 4.136 0.01 1 135 15 ILE HB H 1.820 0.01 1 136 15 ILE HG12 H 1.164 0.01 2 137 15 ILE HG13 H 1.463 0.01 2 138 15 ILE HG2 H 0.878 0.01 1 139 15 ILE N N 123.668 0.20 1 140 16 LYS C C 175.956 0.20 1 141 16 LYS CA C 56.133 0.20 1 142 16 LYS CB C 33.428 0.20 1 143 16 LYS H H 8.393 0.01 1 144 16 LYS HA H 4.317 0.01 1 145 16 LYS HB2 H 1.705 0.01 4 146 16 LYS HB3 H 1.799 0.01 4 147 16 LYS HG2 H 1.414 0.01 4 148 16 LYS HG3 H 1.414 0.01 4 149 16 LYS HE2 H 2.978 0.01 1 150 16 LYS HE3 H 2.978 0.01 1 151 16 LYS N N 127.020 0.20 1 152 17 ALA C C 177.637 0.20 1 153 17 ALA CA C 52.395 0.20 1 154 17 ALA CB C 19.457 0.20 1 155 17 ALA H H 8.346 0.01 1 156 17 ALA HA H 4.353 0.01 1 157 17 ALA HB H 1.370 0.01 1 158 17 ALA N N 126.867 0.20 1 159 18 ILE C C 175.960 0.20 1 160 18 ILE CA C 61.267 0.20 1 161 18 ILE CB C 39.073 0.20 1 162 18 ILE H H 8.179 0.01 1 163 18 ILE HA H 4.153 0.01 1 164 18 ILE HB H 1.851 0.01 1 165 18 ILE HG12 H 1.166 0.01 2 166 18 ILE HG13 H 1.478 0.01 2 167 18 ILE HG2 H 0.898 0.01 1 168 18 ILE N N 120.769 0.20 1 169 19 ASP C C 176.404 0.20 1 170 19 ASP CA C 54.189 0.20 1 171 19 ASP CB C 40.949 0.20 1 172 19 ASP H H 8.354 0.01 1 173 19 ASP HA H 4.653 0.01 1 174 19 ASP HB2 H 2.699 0.01 2 175 19 ASP HB3 H 2.743 0.01 2 176 19 ASP N N 124.306 0.20 1 177 20 GLY C C 173.986 0.20 1 178 20 GLY CA C 45.623 0.20 1 179 20 GLY H H 8.281 0.01 1 180 20 GLY HA2 H 3.963 0.01 1 181 20 GLY HA3 H 3.963 0.01 1 182 20 GLY N N 109.765 0.20 1 183 21 ASP C C 176.533 0.20 1 184 21 ASP CA C 54.307 0.20 1 185 21 ASP CB C 40.894 0.20 1 186 21 ASP H H 8.305 0.01 1 187 21 ASP HA H 4.703 0.01 1 188 21 ASP HB2 H 2.763 0.01 2 189 21 ASP HB3 H 2.694 0.01 2 190 21 ASP N N 120.836 0.20 1 191 22 THR C C 174.792 0.20 1 192 22 THR CA C 62.284 0.20 1 193 22 THR CB C 69.770 0.20 1 194 22 THR H H 8.107 0.01 1 195 22 THR HA H 4.318 0.01 1 196 22 THR HB H 4.212 0.01 1 197 22 THR HG2 H 1.201 0.01 1 198 22 THR N N 114.794 0.20 1 199 23 VAL C C 175.973 0.20 1 200 23 VAL CA C 62.724 0.20 1 201 23 VAL CB C 32.841 0.20 1 202 23 VAL H H 8.055 0.01 1 203 23 VAL HA H 4.063 0.01 1 204 23 VAL HB H 2.050 0.01 1 205 23 VAL HG1 H 0.927 0.01 1 206 23 VAL HG2 H 0.927 0.01 1 207 23 VAL N N 123.124 0.20 1 208 24 LYS C C 176.303 0.20 1 209 24 LYS CA C 56.269 0.20 1 210 24 LYS CB C 33.129 0.20 1 211 24 LYS H H 8.291 0.01 1 212 24 LYS HA H 4.336 0.01 1 213 24 LYS HB2 H 1.767 0.01 4 214 24 LYS HB3 H 1.728 0.01 4 215 24 LYS HG2 H 1.368 0.01 4 216 24 LYS HG3 H 1.444 0.01 4 217 24 LYS HE2 H 2.978 0.01 1 218 24 LYS HE3 H 2.978 0.01 1 219 24 LYS N N 125.530 0.20 1 220 25 LEU C C 177.107 0.20 1 221 25 LEU CA C 55.042 0.20 1 222 25 LEU CB C 42.510 0.20 1 223 25 LEU H H 8.226 0.01 1 224 25 LEU HA H 4.325 0.01 1 225 25 LEU HB2 H 1.602 0.01 1 226 25 LEU HB3 H 1.602 0.01 1 227 25 LEU HG H 1.476 0.01 1 228 25 LEU HD1 H 0.903 0.01 2 229 25 LEU HD2 H 0.852 0.01 2 230 25 LEU N N 124.213 0.20 1 231 26 MET C C 175.772 0.20 1 232 26 MET CA C 55.347 0.20 1 233 26 MET CB C 33.410 0.20 1 234 26 MET H H 8.361 0.01 1 235 26 MET HA H 4.451 0.01 1 236 26 MET HB2 H 1.940 0.01 1 237 26 MET HB3 H 1.940 0.01 1 238 26 MET HG2 H 2.417 0.01 2 239 26 MET HG3 H 2.504 0.01 2 240 26 MET N N 121.895 0.20 1 241 27 TYR C C 175.631 0.20 1 242 27 TYR CA C 57.875 0.20 1 243 27 TYR CB C 39.095 0.20 1 244 27 TYR H H 8.263 0.01 1 245 27 TYR HA H 4.610 0.01 1 246 27 TYR HB2 H 2.955 0.01 2 247 27 TYR HB3 H 3.007 0.01 2 248 27 TYR N N 122.402 0.20 1 249 28 LYS C C 176.566 0.20 1 250 28 LYS CA C 56.379 0.20 1 251 28 LYS CB C 33.122 0.20 1 252 28 LYS H H 8.367 0.01 1 253 28 LYS HA H 4.248 0.01 1 254 28 LYS HB2 H 1.663 0.01 4 255 28 LYS HB3 H 1.819 0.01 4 256 28 LYS HG2 H 1.325 0.01 4 257 28 LYS HG3 H 1.325 0.01 4 258 28 LYS HE2 H 2.961 0.01 1 259 28 LYS HE3 H 2.961 0.01 1 260 28 LYS N N 124.785 0.20 1 261 29 GLY C C 173.506 0.20 1 262 29 GLY CA C 45.068 0.20 1 263 29 GLY H H 7.900 0.01 1 264 29 GLY HA2 H 3.907 0.01 1 265 29 GLY HA3 H 3.907 0.01 1 266 29 GLY N N 109.631 0.20 1 267 30 GLN C C 174.080 0.20 1 268 30 GLN CA C 53.745 0.20 1 269 30 GLN CB C 29.289 0.20 1 270 30 GLN H H 8.187 0.01 1 271 30 GLN HA H 4.633 0.01 1 272 30 GLN HB2 H 1.915 0.01 2 273 30 GLN HB3 H 2.084 0.01 2 274 30 GLN HG2 H 2.371 0.01 1 275 30 GLN HG3 H 2.371 0.01 1 276 30 GLN N N 121.146 0.20 1 277 31 PRO C C 176.798 0.20 1 278 31 PRO CA C 63.260 0.20 1 279 31 PRO CB C 32.172 0.20 1 280 31 PRO HA H 4.443 0.01 1 281 31 PRO HB2 H 1.884 0.01 2 282 31 PRO HB3 H 2.258 0.01 2 283 31 PRO HG2 H 1.994 0.01 1 284 31 PRO HG3 H 1.994 0.01 1 285 32 MET C C 176.198 0.20 1 286 32 MET CA C 55.657 0.20 1 287 32 MET CB C 33.386 0.20 1 288 32 MET H H 8.498 0.01 1 289 32 MET HA H 4.464 0.01 1 290 32 MET HB2 H 1.963 0.01 1 291 32 MET HB3 H 1.963 0.01 1 292 32 MET HG2 H 2.524 0.01 1 293 32 MET HG3 H 2.524 0.01 1 294 32 MET N N 121.670 0.20 1 295 33 THR C C 173.977 0.20 1 296 33 THR CA C 61.671 0.20 1 297 33 THR CB C 69.989 0.20 1 298 33 THR H H 8.058 0.01 1 299 33 THR HA H 4.311 0.01 1 300 33 THR HB H 4.120 0.01 1 301 33 THR HG2 H 1.132 0.01 1 302 33 THR N N 115.732 0.20 1 303 34 PHE C C 175.269 0.20 1 304 34 PHE CA C 57.572 0.20 1 305 34 PHE CB C 40.068 0.20 1 306 34 PHE H H 8.258 0.01 1 307 34 PHE HA H 4.636 0.01 1 308 34 PHE HB2 H 2.982 0.01 2 309 34 PHE HB3 H 3.102 0.01 2 310 34 PHE N N 123.259 0.20 1 311 35 ARG C C 175.476 0.20 1 312 35 ARG CA C 55.936 0.20 1 313 35 ARG CB C 31.338 0.20 1 314 35 ARG H H 8.274 0.01 1 315 35 ARG HA H 4.308 0.01 1 316 35 ARG HB2 H 1.669 0.01 2 317 35 ARG HB3 H 1.758 0.01 2 318 35 ARG HG2 H 1.553 0.01 1 319 35 ARG HG3 H 1.553 0.01 1 320 35 ARG HD2 H 3.149 0.01 1 321 35 ARG HD3 H 3.149 0.01 1 322 35 ARG N N 123.769 0.20 1 323 36 LEU C C 176.689 0.20 1 324 36 LEU CA C 55.034 0.20 1 325 36 LEU CB C 42.663 0.20 1 326 36 LEU H H 8.236 0.01 1 327 36 LEU HA H 4.289 0.01 1 328 36 LEU HB2 H 1.568 0.01 1 329 36 LEU HB3 H 1.568 0.01 1 330 36 LEU HD1 H 0.929 0.01 1 331 36 LEU HD2 H 0.929 0.01 1 332 36 LEU N N 124.641 0.20 1 333 37 LEU C C 176.763 0.20 1 334 37 LEU CA C 54.874 0.20 1 335 37 LEU CB C 42.527 0.20 1 336 37 LEU H H 8.342 0.01 1 337 37 LEU HA H 4.383 0.01 1 338 37 LEU HB2 H 1.573 0.01 1 339 37 LEU HB3 H 1.573 0.01 1 340 37 LEU HD1 H 0.895 0.01 1 341 37 LEU HD2 H 0.895 0.01 1 342 37 LEU N N 125.000 0.20 1 343 38 LEU C C 177.016 0.20 1 344 38 LEU CA C 54.893 0.20 1 345 38 LEU CB C 42.435 0.20 1 346 38 LEU H H 8.285 0.01 1 347 38 LEU HA H 4.417 0.01 1 348 38 LEU HB2 H 1.633 0.01 1 349 38 LEU HB3 H 1.633 0.01 1 350 38 LEU HG H 1.559 0.01 1 351 38 LEU HD1 H 0.897 0.01 1 352 38 LEU HD2 H 0.897 0.01 1 353 38 LEU N N 124.815 0.20 1 354 39 VAL C C 175.632 0.20 1 355 39 VAL CA C 61.937 0.20 1 356 39 VAL CB C 33.216 0.20 1 357 39 VAL H H 8.107 0.01 1 358 39 VAL HA H 4.165 0.01 1 359 39 VAL HB H 2.068 0.01 1 360 39 VAL HG1 H 0.916 0.01 1 361 39 VAL HG2 H 0.916 0.01 1 362 39 VAL N N 121.053 0.20 1 363 40 ASP C C 175.720 0.20 1 364 40 ASP CA C 54.005 0.20 1 365 40 ASP CB C 41.060 0.20 1 366 40 ASP H H 8.411 0.01 1 367 40 ASP HA H 4.705 0.01 1 368 40 ASP HB2 H 2.625 0.01 2 369 40 ASP HB3 H 2.724 0.01 2 370 40 ASP N N 124.579 0.20 1 371 41 THR C C 173.132 0.20 1 372 41 THR CA C 59.648 0.20 1 373 41 THR CB C 69.708 0.20 1 374 41 THR H H 8.088 0.01 1 375 41 THR HA H 4.624 0.01 1 376 41 THR HB H 4.232 0.01 1 377 41 THR HG2 H 1.239 0.01 1 378 41 THR N N 116.500 0.20 1 379 42 PRO C C 177.023 0.20 1 380 42 PRO CA C 63.663 0.20 1 381 42 PRO CB C 32.158 0.20 1 382 42 PRO HA H 4.414 0.01 1 383 42 PRO HB2 H 1.918 0.01 2 384 42 PRO HB3 H 2.303 0.01 2 385 42 PRO HG2 H 2.036 0.01 1 386 42 PRO HG3 H 2.036 0.01 1 387 43 GLU C C 176.774 0.20 1 388 43 GLU CA C 56.611 0.20 1 389 43 GLU CB C 30.046 0.20 1 390 43 GLU H H 8.474 0.01 1 391 43 GLU HA H 4.296 0.01 1 392 43 GLU HB2 H 1.975 0.01 2 393 43 GLU HB3 H 2.055 0.01 2 394 43 GLU HG2 H 2.342 0.01 1 395 43 GLU HG3 H 2.342 0.01 1 396 43 GLU N N 120.850 0.20 1 397 44 THR C C 174.452 0.20 1 398 44 THR CA C 62.052 0.20 1 399 44 THR CB C 69.718 0.20 1 400 44 THR H H 8.107 0.01 1 401 44 THR HA H 4.275 0.01 1 402 44 THR HB H 4.171 0.01 1 403 44 THR HG2 H 1.162 0.01 1 404 44 THR N N 116.145 0.20 1 405 45 LYS C C 176.113 0.20 1 406 45 LYS CA C 56.208 0.20 1 407 45 LYS CB C 33.198 0.20 1 408 45 LYS H H 8.236 0.01 1 409 45 LYS HA H 4.280 0.01 1 410 45 LYS HB2 H 1.698 0.01 4 411 45 LYS HB3 H 1.698 0.01 4 412 45 LYS HG2 H 1.325 0.01 4 413 45 LYS HG3 H 1.411 0.01 4 414 45 LYS HE2 H 2.948 0.01 1 415 45 LYS HE3 H 2.948 0.01 1 416 45 LYS N N 124.153 0.20 1 417 46 HIS C C 172.389 0.20 1 418 46 HIS CA C 53.187 0.20 1 419 46 HIS CB C 28.804 0.20 1 420 46 HIS H H 8.493 0.01 1 421 46 HIS HA H 4.984 0.01 1 422 46 HIS HB2 H 3.098 0.01 2 423 46 HIS HB3 H 3.218 0.01 2 424 46 HIS N N 120.447 0.20 1 425 47 PRO C C 176.787 0.20 1 426 47 PRO CA C 63.165 0.20 1 427 47 PRO CB C 32.391 0.20 1 428 47 PRO HA H 4.448 0.01 1 429 47 PRO HB2 H 1.900 0.01 2 430 47 PRO HB3 H 2.294 0.01 2 431 47 PRO HG2 H 2.004 0.01 1 432 47 PRO HG3 H 2.004 0.01 1 433 48 LYS C C 176.585 0.20 1 434 48 LYS CA C 56.430 0.20 1 435 48 LYS CB C 33.424 0.20 1 436 48 LYS H H 8.534 0.01 1 437 48 LYS HA H 4.305 0.01 1 438 48 LYS HB2 H 1.731 0.01 4 439 48 LYS HB3 H 1.831 0.01 4 440 48 LYS HG2 H 1.461 0.01 4 441 48 LYS HG3 H 1.461 0.01 4 442 48 LYS HE2 H 2.997 0.01 1 443 48 LYS HE3 H 2.997 0.01 1 444 48 LYS N N 123.120 0.20 1 445 49 LYS C C 176.989 0.20 1 446 49 LYS CA C 56.498 0.20 1 447 49 LYS CB C 33.596 0.20 1 448 49 LYS H H 8.456 0.01 1 449 49 LYS HA H 4.336 0.01 1 450 49 LYS HB2 H 1.756 0.01 4 451 49 LYS HB3 H 1.838 0.01 4 452 49 LYS HG2 H 1.448 0.01 4 453 49 LYS HG3 H 1.448 0.01 4 454 49 LYS HE2 H 2.975 0.01 1 455 49 LYS HE3 H 2.975 0.01 1 456 49 LYS N N 123.956 0.20 1 457 50 GLY C C 173.861 0.20 1 458 50 GLY CA C 45.196 0.20 1 459 50 GLY H H 8.479 0.01 1 460 50 GLY HA2 H 4.042 0.01 2 461 50 GLY HA3 H 3.950 0.01 2 462 50 GLY N N 111.521 0.20 1 463 51 VAL C C 176.192 0.20 1 464 51 VAL CA C 62.116 0.20 1 465 51 VAL CB C 32.941 0.20 1 466 51 VAL H H 8.015 0.01 1 467 51 VAL HA H 4.132 0.01 1 468 51 VAL HB H 2.060 0.01 1 469 51 VAL HG1 H 0.911 0.01 1 470 51 VAL HG2 H 0.911 0.01 1 471 51 VAL N N 119.466 0.20 1 472 52 GLU C C 176.010 0.20 1 473 52 GLU CA C 56.309 0.20 1 474 52 GLU CB C 30.116 0.20 1 475 52 GLU H H 8.506 0.01 1 476 52 GLU HA H 4.274 0.01 1 477 52 GLU HB2 H 1.897 0.01 1 478 52 GLU HB3 H 1.897 0.01 1 479 52 GLU HG2 H 2.276 0.01 1 480 52 GLU HG3 H 2.276 0.01 1 481 52 GLU N N 125.321 0.20 1 482 53 LYS C C 175.964 0.20 1 483 53 LYS CA C 56.312 0.20 1 484 53 LYS CB C 33.584 0.20 1 485 53 LYS H H 8.258 0.01 1 486 53 LYS HA H 4.237 0.01 1 487 53 LYS HB2 H 1.630 0.01 4 488 53 LYS HB3 H 1.630 0.01 4 489 53 LYS HG2 H 1.305 0.01 4 490 53 LYS HG3 H 1.214 0.01 4 491 53 LYS HE2 H 2.929 0.01 1 492 53 LYS HE3 H 2.929 0.01 1 493 53 LYS N N 123.259 0.20 1 494 54 TYR C C 176.046 0.20 1 495 54 TYR CA C 57.419 0.20 1 496 54 TYR CB C 39.400 0.20 1 497 54 TYR H H 8.232 0.01 1 498 54 TYR HA H 4.665 0.01 1 499 54 TYR HB2 H 2.886 0.01 2 500 54 TYR HB3 H 3.117 0.01 2 501 54 TYR N N 121.527 0.20 1 502 55 GLY C C 171.852 0.20 1 503 55 GLY CA C 44.698 0.20 1 504 55 GLY H H 8.256 0.01 1 505 55 GLY HA2 H 4.075 0.01 2 506 55 GLY HA3 H 4.117 0.01 2 507 55 GLY N N 110.928 0.20 1 508 56 PRO C C 177.340 0.20 1 509 56 PRO CA C 63.508 0.20 1 510 56 PRO CB C 32.293 0.20 1 511 56 PRO HA H 4.405 0.01 1 512 56 PRO HB2 H 1.950 0.01 2 513 56 PRO HB3 H 2.274 0.01 2 514 56 PRO HG2 H 1.990 0.01 1 515 56 PRO HG3 H 1.990 0.01 1 516 57 GLU C C 176.433 0.20 1 517 57 GLU CA C 56.566 0.20 1 518 57 GLU CB C 29.762 0.20 1 519 57 GLU H H 8.600 0.01 1 520 57 GLU HA H 4.263 0.01 1 521 57 GLU HB2 H 1.964 0.01 2 522 57 GLU HB3 H 2.086 0.01 2 523 57 GLU HG2 H 2.354 0.01 1 524 57 GLU HG3 H 2.354 0.01 1 525 57 GLU N N 121.189 0.20 1 526 58 ALA C C 177.842 0.20 1 527 58 ALA CA C 52.766 0.20 1 528 58 ALA CB C 19.260 0.20 1 529 58 ALA H H 8.237 0.01 1 530 58 ALA HA H 4.302 0.01 1 531 58 ALA HB H 1.393 0.01 1 532 58 ALA N N 125.445 0.20 1 533 59 SER C C 174.546 0.20 1 534 59 SER CA C 58.370 0.20 1 535 59 SER CB C 63.885 0.20 1 536 59 SER H H 8.180 0.01 1 537 59 SER HA H 4.399 0.01 1 538 59 SER HB2 H 3.883 0.01 2 539 59 SER HB3 H 3.823 0.01 2 540 59 SER N N 115.315 0.20 1 541 60 ALA C C 177.491 0.20 1 542 60 ALA CA C 52.902 0.20 1 543 60 ALA CB C 19.242 0.20 1 544 60 ALA H H 8.209 0.01 1 545 60 ALA HA H 4.248 0.01 1 546 60 ALA HB H 1.269 0.01 1 547 60 ALA N N 126.085 0.20 1 548 61 PHE C C 175.995 0.20 1 549 61 PHE CA C 57.731 0.20 1 550 61 PHE CB C 39.609 0.20 1 551 61 PHE H H 8.068 0.01 1 552 61 PHE HA H 4.654 0.01 1 553 61 PHE HB2 H 3.007 0.01 2 554 61 PHE HB3 H 3.181 0.01 2 555 61 PHE N N 119.074 0.20 1 556 62 THR C C 174.294 0.20 1 557 62 THR CA C 61.833 0.20 1 558 62 THR CB C 69.977 0.20 1 559 62 THR H H 7.954 0.01 1 560 62 THR HA H 4.292 0.01 1 561 62 THR HB H 4.162 0.01 1 562 62 THR HG2 H 1.182 0.01 1 563 62 THR N N 116.150 0.20 1 564 63 LYS C C 176.308 0.20 1 565 63 LYS CA C 56.507 0.20 1 566 63 LYS CB C 33.368 0.20 1 567 63 LYS H H 8.236 0.01 1 568 63 LYS HA H 4.289 0.01 1 569 63 LYS HB2 H 1.708 0.01 4 570 63 LYS HB3 H 1.808 0.01 4 571 63 LYS HG2 H 1.427 0.01 4 572 63 LYS HG3 H 1.427 0.01 4 573 63 LYS HE2 H 2.981 0.01 1 574 63 LYS HE3 H 2.981 0.01 1 575 63 LYS N N 124.641 0.20 1 576 64 LYS C C 176.499 0.20 1 577 64 LYS CA C 56.508 0.20 1 578 64 LYS CB C 33.226 0.20 1 579 64 LYS H H 8.361 0.01 1 580 64 LYS HA H 4.292 0.01 1 581 64 LYS HB2 H 1.771 0.01 4 582 64 LYS HB3 H 1.684 0.01 4 583 64 LYS HG2 H 1.410 0.01 4 584 64 LYS HG3 H 1.410 0.01 4 585 64 LYS HE2 H 2.967 0.01 1 586 64 LYS HE3 H 2.967 0.01 1 587 64 LYS N N 123.801 0.20 1 588 65 MET C C 176.156 0.20 1 589 65 MET CA C 55.586 0.20 1 590 65 MET CB C 33.189 0.20 1 591 65 MET H H 8.460 0.01 1 592 65 MET HA H 4.479 0.01 1 593 65 MET HB2 H 2.005 0.01 1 594 65 MET HB3 H 2.005 0.01 1 595 65 MET HG2 H 2.511 0.01 2 596 65 MET HG3 H 2.571 0.01 2 597 65 MET N N 123.395 0.20 1 598 66 VAL C C 176.074 0.20 1 599 66 VAL CA C 62.308 0.20 1 600 66 VAL CB C 32.917 0.20 1 601 66 VAL H H 8.217 0.01 1 602 66 VAL HA H 4.106 0.01 1 603 66 VAL HB H 2.053 0.01 1 604 66 VAL HG1 H 0.928 0.01 1 605 66 VAL HG2 H 0.928 0.01 1 606 66 VAL N N 122.456 0.20 1 607 67 GLU C C 176.090 0.20 1 608 67 GLU CA C 56.309 0.20 1 609 67 GLU CB C 30.116 0.20 1 610 67 GLU H H 8.485 0.01 1 611 67 GLU HA H 4.308 0.01 1 612 67 GLU HB2 H 1.931 0.01 2 613 67 GLU HB3 H 2.040 0.01 2 614 67 GLU HG2 H 2.302 0.01 1 615 67 GLU HG3 H 2.302 0.01 1 616 67 GLU N N 125.258 0.20 1 617 68 ASN C C 174.933 0.20 1 618 68 ASN CA C 53.300 0.20 1 619 68 ASN CB C 39.058 0.20 1 620 68 ASN H H 8.486 0.01 1 621 68 ASN HA H 4.672 0.01 1 622 68 ASN HB2 H 2.740 0.01 2 623 68 ASN HB3 H 2.822 0.01 2 624 68 ASN N N 120.995 0.20 1 625 69 ALA C C 177.586 0.20 1 626 69 ALA CA C 52.727 0.20 1 627 69 ALA CB C 19.424 0.20 1 628 69 ALA H H 8.239 0.01 1 629 69 ALA HA H 4.281 0.01 1 630 69 ALA HB H 1.382 0.01 1 631 69 ALA N N 125.016 0.20 1 632 70 LYS C C 176.441 0.20 1 633 70 LYS CA C 56.308 0.20 1 634 70 LYS CB C 33.381 0.20 1 635 70 LYS H H 8.240 0.01 1 636 70 LYS HA H 4.275 0.01 1 637 70 LYS HB2 H 1.725 0.01 4 638 70 LYS HB3 H 1.790 0.01 4 639 70 LYS HG2 H 1.431 0.01 4 640 70 LYS HG3 H 1.431 0.01 4 641 70 LYS HE2 H 2.980 0.01 1 642 70 LYS HE3 H 2.980 0.01 1 643 70 LYS N N 121.352 0.20 1 644 71 LYS C C 176.404 0.20 1 645 71 LYS CA C 56.315 0.20 1 646 71 LYS CB C 33.279 0.20 1 647 71 LYS H H 8.337 0.01 1 648 71 LYS HA H 4.323 0.01 1 649 71 LYS HB2 H 1.710 0.01 4 650 71 LYS HB3 H 1.776 0.01 4 651 71 LYS HG2 H 1.355 0.01 4 652 71 LYS HG3 H 1.414 0.01 4 653 71 LYS HE2 H 2.983 0.01 1 654 71 LYS HE3 H 2.983 0.01 1 655 71 LYS N N 124.132 0.20 1 656 72 ILE C C 176.073 0.20 1 657 72 ILE CA C 61.053 0.20 1 658 72 ILE CB C 38.844 0.20 1 659 72 ILE H H 8.260 0.01 1 660 72 ILE HA H 4.151 0.01 1 661 72 ILE HB H 1.818 0.01 1 662 72 ILE HG12 H 1.164 0.01 2 663 72 ILE HG13 H 1.462 0.01 2 664 72 ILE HG2 H 0.876 0.01 1 665 72 ILE N N 123.780 0.20 1 666 73 GLU C C 177.801 0.20 1 667 73 GLU CA C 56.091 0.20 1 668 73 GLU CB C 30.100 0.20 1 669 73 GLU H H 8.480 0.01 1 670 73 GLU HA H 4.387 0.01 1 671 73 GLU HB2 H 1.916 0.01 2 672 73 GLU HB3 H 2.036 0.01 2 673 73 GLU HG2 H 2.293 0.01 1 674 73 GLU HG3 H 2.293 0.01 1 675 73 GLU N N 126.211 0.20 1 676 74 VAL C C 175.831 0.20 1 677 74 VAL CA C 62.243 0.20 1 678 74 VAL CB C 33.091 0.20 1 679 74 VAL H H 8.155 0.01 1 680 74 VAL HA H 4.075 0.01 1 681 74 VAL HB H 1.980 0.01 1 682 74 VAL HG1 H 0.895 0.01 2 683 74 VAL HG2 H 0.821 0.01 2 684 74 VAL N N 121.969 0.20 1 685 75 GLU C C 175.929 0.20 1 686 75 GLU CA C 56.132 0.20 1 687 75 GLU CB C 30.056 0.20 1 688 75 GLU H H 8.372 0.01 1 689 75 GLU HA H 4.294 0.01 1 690 75 GLU HB2 H 1.867 0.01 2 691 75 GLU HB3 H 1.948 0.01 2 692 75 GLU HG2 H 2.259 0.01 1 693 75 GLU HG3 H 2.259 0.01 1 694 75 GLU N N 124.625 0.20 1 695 76 PHE C C 175.490 0.20 1 696 76 PHE CA C 57.744 0.20 1 697 76 PHE CB C 39.839 0.20 1 698 76 PHE H H 8.236 0.01 1 699 76 PHE HA H 4.608 0.01 1 700 76 PHE HB2 H 2.976 0.01 2 701 76 PHE HB3 H 3.122 0.01 2 702 76 PHE N N 122.065 0.20 1 703 77 ASP C C 176.180 0.20 1 704 77 ASP CA C 54.076 0.20 1 705 77 ASP CB C 41.051 0.20 1 706 77 ASP H H 8.375 0.01 1 707 77 ASP HA H 4.593 0.01 1 708 77 ASP HB2 H 2.723 0.01 1 709 77 ASP HB3 H 2.723 0.01 1 710 77 ASP N N 122.382 0.20 1 711 78 LYS C C 177.146 0.20 1 712 78 LYS CA C 56.810 0.20 1 713 78 LYS CB C 32.924 0.20 1 714 78 LYS H H 8.248 0.01 1 715 78 LYS HA H 4.258 0.01 1 716 78 LYS HB2 H 1.742 0.01 4 717 78 LYS HB3 H 1.890 0.01 4 718 78 LYS HG2 H 1.416 0.01 4 719 78 LYS HG3 H 1.416 0.01 4 720 78 LYS HE2 H 2.967 0.01 1 721 78 LYS HE3 H 2.967 0.01 1 722 78 LYS N N 122.751 0.20 1 723 79 GLY C C 174.097 0.20 1 724 79 GLY CA C 45.411 0.20 1 725 79 GLY H H 8.405 0.01 1 726 79 GLY HA2 H 3.933 0.01 1 727 79 GLY HA3 H 3.933 0.01 1 728 79 GLY N N 109.544 0.20 1 729 80 GLN C C 176.060 0.20 1 730 80 GLN CA C 55.871 0.20 1 731 80 GLN CB C 29.810 0.20 1 732 80 GLN H H 8.141 0.01 1 733 80 GLN HA H 4.338 0.01 1 734 80 GLN HB2 H 1.943 0.01 2 735 80 GLN HB3 H 2.073 0.01 2 736 80 GLN HG2 H 2.303 0.01 1 737 80 GLN HG3 H 2.303 0.01 1 738 80 GLN N N 120.264 0.20 1 739 81 ARG C C 176.368 0.20 1 740 81 ARG CA C 56.093 0.20 1 741 81 ARG CB C 31.283 0.20 1 742 81 ARG H H 8.477 0.01 1 743 81 ARG HA H 4.428 0.01 1 744 81 ARG HB2 H 1.748 0.01 2 745 81 ARG HB3 H 1.867 0.01 2 746 81 ARG HG2 H 1.593 0.01 2 747 81 ARG HG3 H 1.643 0.01 2 748 81 ARG HD2 H 3.138 0.01 1 749 81 ARG HD3 H 3.138 0.01 1 750 81 ARG N N 122.817 0.20 1 751 82 THR C C 174.443 0.20 1 752 82 THR CA C 61.057 0.20 1 753 82 THR CB C 70.476 0.20 1 754 82 THR H H 8.163 0.01 1 755 82 THR HA H 4.544 0.01 1 756 82 THR HB H 4.150 0.01 1 757 82 THR HG2 H 1.053 0.01 1 758 82 THR N N 114.444 0.20 1 759 83 ASP C C 176.997 0.20 1 760 83 ASP CA C 53.549 0.20 1 761 83 ASP CB C 41.349 0.20 1 762 83 ASP H H 8.451 0.01 1 763 83 ASP HA H 4.652 0.01 1 764 83 ASP HB2 H 2.695 0.01 2 765 83 ASP HB3 H 2.881 0.01 2 766 83 ASP N N 122.685 0.20 1 767 84 LYS C C 176.441 0.20 1 768 84 LYS CA C 57.414 0.20 1 769 84 LYS CB C 32.710 0.20 1 770 84 LYS H H 8.242 0.01 1 771 84 LYS HA H 4.110 0.01 1 772 84 LYS HB2 H 1.583 0.01 4 773 84 LYS HB3 H 1.583 0.01 4 774 84 LYS HG2 H 0.990 0.01 4 775 84 LYS HG3 H 1.072 0.01 4 776 84 LYS HE2 H 2.852 0.01 1 777 84 LYS HE3 H 2.852 0.01 1 778 84 LYS N N 120.961 0.20 1 779 85 TYR C C 176.338 0.20 1 780 85 TYR CA C 57.665 0.20 1 781 85 TYR CB C 38.754 0.20 1 782 85 TYR H H 8.092 0.01 1 783 85 TYR HA H 4.593 0.01 1 784 85 TYR HB2 H 2.897 0.01 2 785 85 TYR HB3 H 3.199 0.01 2 786 85 TYR N N 119.890 0.20 1 787 86 GLY C C 174.069 0.20 1 788 86 GLY CA C 45.500 0.20 1 789 86 GLY H H 8.095 0.01 1 790 86 GLY HA2 H 3.930 0.01 2 791 86 GLY HA3 H 3.777 0.01 2 792 86 GLY N N 109.834 0.20 1 793 87 ARG C C 176.180 0.20 1 794 87 ARG CA C 56.350 0.20 1 795 87 ARG CB C 30.780 0.20 1 796 87 ARG H H 8.232 0.01 1 797 87 ARG HA H 4.306 0.01 1 798 87 ARG HB2 H 1.726 0.01 1 799 87 ARG HB3 H 1.726 0.01 1 800 87 ARG HG2 H 1.493 0.01 1 801 87 ARG HG3 H 1.493 0.01 1 802 87 ARG HD2 H 3.103 0.01 1 803 87 ARG HD3 H 3.103 0.01 1 804 87 ARG N N 121.527 0.20 1 805 88 TRP C C 176.187 0.20 1 806 88 TRP CA C 57.401 0.20 1 807 88 TRP CB C 29.557 0.20 1 808 88 TRP H H 8.264 0.01 1 809 88 TRP HA H 4.670 0.01 1 810 88 TRP HB2 H 3.180 0.01 2 811 88 TRP HB3 H 3.291 0.01 2 812 88 TRP N N 122.840 0.20 1 813 89 LEU C C 176.510 0.20 1 814 89 LEU CA C 54.989 0.20 1 815 89 LEU CB C 42.695 0.20 1 816 89 LEU H H 8.040 0.01 1 817 89 LEU HA H 4.234 0.01 1 818 89 LEU HB2 H 1.472 0.01 1 819 89 LEU HB3 H 1.472 0.01 1 820 89 LEU HG H 1.398 0.01 1 821 89 LEU HD1 H 0.807 0.01 1 822 89 LEU HD2 H 0.807 0.01 1 823 89 LEU N N 124.898 0.20 1 824 90 ALA C C 177.232 0.20 1 825 90 ALA CA C 52.542 0.20 1 826 90 ALA CB C 19.461 0.20 1 827 90 ALA H H 8.022 0.01 1 828 90 ALA HA H 4.149 0.01 1 829 90 ALA HB H 1.269 0.01 1 830 90 ALA N N 124.471 0.20 1 831 91 TYR C C 175.398 0.20 1 832 91 TYR CA C 57.818 0.20 1 833 91 TYR CB C 39.076 0.20 1 834 91 TYR H H 7.955 0.01 1 835 91 TYR HA H 4.511 0.01 1 836 91 TYR HB2 H 2.887 0.01 1 837 91 TYR HB3 H 2.887 0.01 1 838 91 TYR N N 119.602 0.20 1 839 92 ILE C C 175.579 0.20 1 840 92 ILE CA C 60.923 0.20 1 841 92 ILE CB C 39.017 0.20 1 842 92 ILE H H 7.877 0.01 1 843 92 ILE HA H 4.091 0.01 1 844 92 ILE HB H 1.663 0.01 1 845 92 ILE HG12 H 0.991 0.01 2 846 92 ILE HG13 H 1.227 0.01 2 847 92 ILE HG2 H 0.710 0.01 1 848 92 ILE N N 122.533 0.20 1 849 93 TYR C C 175.724 0.20 1 850 93 TYR CA C 57.705 0.20 1 851 93 TYR CB C 39.061 0.20 1 852 93 TYR H H 8.119 0.01 1 853 93 TYR HA H 4.591 0.01 1 854 93 TYR HB2 H 2.857 0.01 2 855 93 TYR HB3 H 3.045 0.01 2 856 93 TYR N N 124.477 0.20 1 857 94 ALA C C 177.044 0.20 1 858 94 ALA CA C 52.517 0.20 1 859 94 ALA CB C 19.434 0.20 1 860 94 ALA H H 8.252 0.01 1 861 94 ALA HA H 4.308 0.01 1 862 94 ALA HB H 1.350 0.01 1 863 94 ALA N N 126.230 0.20 1 864 95 ASP C C 176.633 0.20 1 865 95 ASP CA C 54.212 0.20 1 866 95 ASP CB C 40.825 0.20 1 867 95 ASP H H 8.237 0.01 1 868 95 ASP HA H 4.549 0.01 1 869 95 ASP HB2 H 2.730 0.01 1 870 95 ASP HB3 H 2.730 0.01 1 871 95 ASP N N 119.854 0.20 1 872 96 GLY C C 174.194 0.20 1 873 96 GLY CA C 45.671 0.20 1 874 96 GLY H H 8.246 0.01 1 875 96 GLY HA2 H 3.887 0.01 2 876 96 GLY HA3 H 3.977 0.01 2 877 96 GLY N N 109.013 0.20 1 878 97 LYS C C 176.413 0.20 1 879 97 LYS CA C 56.337 0.20 1 880 97 LYS CB C 33.387 0.20 1 881 97 LYS H H 8.037 0.01 1 882 97 LYS HA H 4.336 0.01 1 883 97 LYS HB2 H 1.775 0.01 4 884 97 LYS HB3 H 1.775 0.01 4 885 97 LYS HG2 H 1.382 0.01 4 886 97 LYS HG3 H 1.382 0.01 4 887 97 LYS HE2 H 2.961 0.01 1 888 97 LYS HE3 H 2.961 0.01 1 889 97 LYS N N 121.033 0.20 1 890 98 MET C C 176.236 0.20 1 891 98 MET CA C 55.604 0.20 1 892 98 MET CB C 33.223 0.20 1 893 98 MET H H 8.385 0.01 1 894 98 MET HA H 4.479 0.01 1 895 98 MET HB2 H 2.020 0.01 1 896 98 MET HB3 H 2.020 0.01 1 897 98 MET HG2 H 2.536 0.01 1 898 98 MET HG3 H 2.536 0.01 1 899 98 MET N N 121.972 0.20 1 900 99 VAL C C 175.633 0.20 1 901 99 VAL CA C 62.308 0.20 1 902 99 VAL CB C 33.196 0.20 1 903 99 VAL H H 8.202 0.01 1 904 99 VAL HA H 4.106 0.01 1 905 99 VAL HB H 2.053 0.01 1 906 99 VAL HG1 H 0.899 0.01 1 907 99 VAL HG2 H 0.899 0.01 1 908 99 VAL N N 122.120 0.20 1 909 100 ASN C C 175.507 0.20 1 910 100 ASN CA C 53.272 0.20 1 911 100 ASN CB C 38.893 0.20 1 912 100 ASN H H 8.485 0.01 1 913 100 ASN HA H 4.700 0.01 1 914 100 ASN HB2 H 2.725 0.01 2 915 100 ASN HB3 H 2.851 0.01 2 916 100 ASN N N 123.022 0.20 1 917 101 GLU C C 176.153 0.20 1 918 101 GLU CA C 56.824 0.20 1 919 101 GLU CB C 29.803 0.20 1 920 101 GLU H H 8.454 0.01 1 921 101 GLU HA H 4.220 0.01 1 922 101 GLU HB2 H 1.958 0.01 1 923 101 GLU HB3 H 1.958 0.01 1 924 101 GLU HG2 H 2.341 0.01 1 925 101 GLU HG3 H 2.341 0.01 1 926 101 GLU N N 122.958 0.20 1 927 102 ALA C C 177.886 0.20 1 928 102 ALA CA C 52.959 0.20 1 929 102 ALA CB C 19.009 0.20 1 930 102 ALA H H 8.226 0.01 1 931 102 ALA HA H 4.260 0.01 1 932 102 ALA HB H 1.382 0.01 1 933 102 ALA N N 124.213 0.20 1 934 103 LEU C C 177.563 0.20 1 935 103 LEU CA C 55.417 0.20 1 936 103 LEU CB C 42.403 0.20 1 937 103 LEU H H 7.930 0.01 1 938 103 LEU HA H 4.311 0.01 1 939 103 LEU HB2 H 1.635 0.01 1 940 103 LEU HB3 H 1.635 0.01 1 941 103 LEU HD1 H 0.847 0.01 2 942 103 LEU HD2 H 0.915 0.01 2 943 103 LEU N N 120.816 0.20 1 944 104 VAL C C 176.424 0.20 1 945 104 VAL CA C 62.700 0.20 1 946 104 VAL CB C 32.830 0.20 1 947 104 VAL H H 7.956 0.01 1 948 104 VAL HA H 4.056 0.01 1 949 104 VAL HB H 2.053 0.01 1 950 104 VAL HG1 H 0.917 0.01 1 951 104 VAL HG2 H 0.917 0.01 1 952 104 VAL N N 121.455 0.20 1 953 105 ARG C C 176.300 0.20 1 954 105 ARG CA C 56.327 0.20 1 955 105 ARG CB C 30.859 0.20 1 956 105 ARG H H 8.342 0.01 1 957 105 ARG HA H 4.322 0.01 1 958 105 ARG HB2 H 1.838 0.01 2 959 105 ARG HB3 H 1.759 0.01 2 960 105 ARG HG2 H 1.644 0.01 1 961 105 ARG HG3 H 1.644 0.01 1 962 105 ARG HD2 H 3.180 0.01 1 963 105 ARG HD3 H 3.180 0.01 1 964 105 ARG N N 125.026 0.20 1 965 106 GLN C C 176.417 0.20 1 966 106 GLN CA C 56.125 0.20 1 967 106 GLN CB C 29.832 0.20 1 968 106 GLN H H 8.360 0.01 1 969 106 GLN HA H 4.334 0.01 1 970 106 GLN HB2 H 1.995 0.01 2 971 106 GLN HB3 H 2.115 0.01 2 972 106 GLN HG2 H 2.384 0.01 1 973 106 GLN HG3 H 2.384 0.01 1 974 106 GLN N N 122.090 0.20 1 975 107 GLY C C 173.847 0.20 1 976 107 GLY CA C 45.326 0.20 1 977 107 GLY H H 8.388 0.01 1 978 107 GLY HA2 H 3.962 0.01 1 979 107 GLY HA3 H 3.962 0.01 1 980 107 GLY N N 110.578 0.20 1 981 108 LEU C C 177.007 0.20 1 982 108 LEU CA C 55.018 0.20 1 983 108 LEU CB C 42.872 0.20 1 984 108 LEU H H 8.052 0.01 1 985 108 LEU HA H 4.358 0.01 1 986 108 LEU HB2 H 1.601 0.01 1 987 108 LEU HB3 H 1.601 0.01 1 988 108 LEU HD1 H 0.900 0.01 1 989 108 LEU HD2 H 0.900 0.01 1 990 108 LEU N N 122.127 0.20 1 991 109 ALA C C 176.663 0.20 1 992 109 ALA CA C 52.517 0.20 1 993 109 ALA CB C 19.434 0.20 1 994 109 ALA H H 8.270 0.01 1 995 109 ALA HA H 4.324 0.01 1 996 109 ALA HB H 1.382 0.01 1 997 109 ALA N N 126.038 0.20 1 998 110 LYS C C 181.232 0.20 1 999 110 LYS CA C 57.729 0.20 1 1000 110 LYS CB C 33.935 0.20 1 1001 110 LYS H H 7.910 0.01 1 1002 110 LYS HA H 4.138 0.01 1 1003 110 LYS HB2 H 1.695 0.01 4 1004 110 LYS HB3 H 1.818 0.01 4 1005 110 LYS HG2 H 1.398 0.01 4 1006 110 LYS HG3 H 1.398 0.01 4 1007 110 LYS HE2 H 2.980 0.01 1 1008 110 LYS HE3 H 2.980 0.01 1 1009 110 LYS N N 126.434 0.20 1 stop_ save_