data_50141 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shift assignments of the APO Fowlpox virus resolvase (APO Fpr) ; _BMRB_accession_number 50141 _BMRB_flat_file_name bmr50141.str _Entry_type original _Submission_date 2019-12-24 _Accession_date 2019-12-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone chemical shift assignments of the APO Fowlpox virus resolvase (APO Fpr)' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rao Timsi . . 2 Aihara Hideki . . 3 Li Na . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 132 "13C chemical shifts" 334 "15N chemical shifts" 132 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-03-10 update BMRB 'update entry citation' 2020-02-05 original author 'original release' stop_ _Original_release_date 2020-01-02 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural insights into the promiscuous DNA binding and broad substrate selectivity of fowlpox virus resolvase ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31941902 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Li Na . . 2 Shi Ke . . 3 Rao Timsi . . 4 Banerjee Surajit . . 5 Aihara Hideki . . stop_ _Journal_abbreviation 'Sci. Rep.' _Journal_name_full 'Scientific reports' _Journal_volume 10 _Journal_issue 1 _Journal_ISSN 2045-2322 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 393 _Page_last 393 _Year 2020 _Details . loop_ _Keyword 'DNA binding' 'Fowlpox virus resolvase,' 'Holliday Junction,' stop_ save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'Fowlpox virus resolvase monomer' _Enzyme_commission_number 3.1.22.4 loop_ _Mol_system_component_name _Mol_label Polypeptide $entity_1 stop_ _System_molecular_weight 17478.07 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'Single entity Fowlpox virus resolvase monomer' save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Fowlpox virus resolvase protein, D135N, C-terminal 6 residues deleted' _Molecular_mass 17478.07 _Mol_thiol_state 'all free' loop_ _Biological_function ; Fowlpox virus resolvase (Fpr) is an endonuclease that cleaves a broad range of branched DNA structures, including the Holliday junction (HJ), with little sequence-specificity ; stop_ _Details ; D135N mutation renders the enzyme to be inactive for nuclease activity and therefore was used for studying binding with cognate DNA. Removing last 6 residues of the full length Fpr protein made it less prone to aggregation and hence the 6-residue deleted construct was used for structure elucidation. ; ############################## # Polymer residue sequence # ############################## _Residue_count 150 _Mol_residue_sequence ; MIICSVDIGIKNPAYAIFNY DNTSNTIKLIAIEKSDWTKN WERSVARDLTRYNPDVVILE KQGFKSPNSKIIYFIKGFFY NSNTKVIVRNPTFKGGSYRN RKKQSIDVFIQKISEYTDYK NDILNKYTKLDDIANSFNLG LSYMESLLKK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ILE 3 ILE 4 CYS 5 SER 6 VAL 7 ASP 8 ILE 9 GLY 10 ILE 11 LYS 12 ASN 13 PRO 14 ALA 15 TYR 16 ALA 17 ILE 18 PHE 19 ASN 20 TYR 21 ASP 22 ASN 23 THR 24 SER 25 ASN 26 THR 27 ILE 28 LYS 29 LEU 30 ILE 31 ALA 32 ILE 33 GLU 34 LYS 35 SER 36 ASP 37 TRP 38 THR 39 LYS 40 ASN 41 TRP 42 GLU 43 ARG 44 SER 45 VAL 46 ALA 47 ARG 48 ASP 49 LEU 50 THR 51 ARG 52 TYR 53 ASN 54 PRO 55 ASP 56 VAL 57 VAL 58 ILE 59 LEU 60 GLU 61 LYS 62 GLN 63 GLY 64 PHE 65 LYS 66 SER 67 PRO 68 ASN 69 SER 70 LYS 71 ILE 72 ILE 73 TYR 74 PHE 75 ILE 76 LYS 77 GLY 78 PHE 79 PHE 80 TYR 81 ASN 82 SER 83 ASN 84 THR 85 LYS 86 VAL 87 ILE 88 VAL 89 ARG 90 ASN 91 PRO 92 THR 93 PHE 94 LYS 95 GLY 96 GLY 97 SER 98 TYR 99 ARG 100 ASN 101 ARG 102 LYS 103 LYS 104 GLN 105 SER 106 ILE 107 ASP 108 VAL 109 PHE 110 ILE 111 GLN 112 LYS 113 ILE 114 SER 115 GLU 116 TYR 117 THR 118 ASP 119 TYR 120 LYS 121 ASN 122 ASP 123 ILE 124 LEU 125 ASN 126 LYS 127 TYR 128 THR 129 LYS 130 LEU 131 ASP 132 ASP 133 ILE 134 ALA 135 ASN 136 SER 137 PHE 138 ASN 139 LEU 140 GLY 141 LEU 142 SER 143 TYR 144 MET 145 GLU 146 SER 147 LEU 148 LEU 149 LYS 150 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 UNP Q9J546.1 RUVV_FOWPN . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $entity_1 'Avipoxvirus Fowlpox virus' 10261 Virus . Avipoxvirus fowlpox FPV187 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $entity_1 'recombinant technology' . . . BL21 DE3 plasmid pET24a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; The 2H, 15N, 13C-labeled Fpr C151Stop D135N protein was obtained by growing the transformed BL21(DE3) bacterial cells in M9/D2O minimal medium with a final pH of 8.2 (50 mM Na2HPO4, 25 mM KH2PO4, 10 mM NaCl, 5 mM MgSO4, 0.1 mM CaCl2, 1% Thiamine, 0.15% 15NH4Cl, 0.3% Deuterated 13C6 D-glucose). ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 . mM '[U-2H; U-15N; U-13C]' L-Arginine 25 mM 'natural abundance' L-Glutamine 25 mM 'natural abundance' DSS 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CcpNMR _Version 2.4 loop_ _Vendor _Address _Electronic_address 'Bahrami, Markley, Assadi, and Eghbalnia' . . CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 . M pH 7 . pH pressure 1 . atm temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . 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 glucose C 13 'methyl carbon' ppm 0 internal direct . . . 1 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 '[15N] ammonium chloride' N 15 nitrogen ppm 0 internal direct . . . 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_assigned_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $software_1 stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CA)CO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name Polypeptide _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 MET C C 174.463 0.20 1 2 1 1 MET CA C 54.700 0.200 1 3 2 2 ILE H H 10.367 0.02 1 4 2 2 ILE C C 179.204 0.20 1 5 2 2 ILE CA C 58.600 0.200 1 6 2 2 ILE CB C 36.700 0.200 1 7 2 2 ILE N N 128.622 0.20 1 8 3 3 ILE H H 9.354 0.02 1 9 3 3 ILE C C 176.693 0.20 1 10 3 3 ILE CA C 59.200 0.200 1 11 3 3 ILE CB C 40.200 0.200 1 12 3 3 ILE N N 130.282 0.20 1 13 4 4 CYS H H 8.945 0.02 1 14 4 4 CYS C C 175.763 0.20 1 15 4 4 CYS CB C 27.900 0.200 1 16 4 4 CYS N N 127.987 0.20 1 17 5 5 SER H H 9.822 0.02 1 18 5 5 SER C C 176.515 0.20 1 19 5 5 SER CA C 55.400 0.200 1 20 5 5 SER CB C 64.000 0.200 1 21 5 5 SER N N 124.709 0.20 1 22 6 6 VAL H H 8.804 0.02 1 23 6 6 VAL C C 177.141 0.20 1 24 6 6 VAL CA C 60.300 0.200 1 25 6 6 VAL N N 124.853 0.20 1 26 7 7 ASP H H 7.007 0.02 1 27 7 7 ASP N N 115.849 0.20 1 28 10 10 ILE H H 7.856 0.02 1 29 10 10 ILE C C 178.622 0.20 1 30 10 10 ILE CA C 60.300 0.200 1 31 10 10 ILE CB C 38.300 0.200 1 32 10 10 ILE N N 119.952 0.20 1 33 11 11 LYS H H 8.019 0.02 1 34 11 11 LYS C C 179.576 0.20 1 35 11 11 LYS CA C 58.400 0.200 1 36 11 11 LYS CB C 31.800 0.200 1 37 11 11 LYS CE C 42.100 0.200 1 38 11 11 LYS N N 120.063 0.20 1 39 12 12 ASN H H 7.788 0.02 1 40 12 12 ASN CB C 39.000 0.200 1 41 12 12 ASN N N 115.877 0.20 1 42 13 13 PRO C C 177.886 0.20 1 43 13 13 PRO CA C 62.800 0.200 1 44 13 13 PRO CB C 31.400 0.200 1 45 14 14 ALA H H 7.564 0.02 1 46 14 14 ALA C C 177.753 0.20 1 47 14 14 ALA CA C 49.700 0.200 1 48 14 14 ALA N N 123.650 0.20 1 49 15 15 TYR H H 8.495 0.02 1 50 15 15 TYR C C 174.270 0.20 1 51 15 15 TYR CA C 54.600 0.200 1 52 15 15 TYR CB C 41.100 0.200 1 53 15 15 TYR N N 116.236 0.20 1 54 16 16 ALA H H 8.944 0.02 1 55 16 16 ALA C C 177.500 0.20 1 56 16 16 ALA N N 122.341 0.20 1 57 17 17 ILE H H 7.096 0.02 1 58 17 17 ILE C C 179.122 0.20 1 59 17 17 ILE N N 116.554 0.20 1 60 18 18 PHE H H 7.992 0.02 1 61 18 18 PHE C C 177.414 0.20 1 62 18 18 PHE CA C 60.300 0.200 1 63 18 18 PHE N N 120.916 0.20 1 64 19 19 ASN H H 9.134 0.02 1 65 19 19 ASN C C 177.435 0.20 1 66 19 19 ASN CA C 52.000 0.200 1 67 19 19 ASN N N 126.268 0.20 1 68 20 20 TYR H H 9.197 0.02 1 69 20 20 TYR C C 176.284 0.20 1 70 20 20 TYR CA C 55.500 0.200 1 71 20 20 TYR CB C 40.400 0.200 1 72 20 20 TYR N N 127.722 0.20 1 73 21 21 ASP H H 8.119 0.02 1 74 21 21 ASP C C 178.490 0.20 1 75 21 21 ASP CA C 51.900 0.200 1 76 21 21 ASP CB C 41.600 0.200 1 77 21 21 ASP N N 128.805 0.20 1 78 22 22 ASN H H 8.377 0.02 1 79 22 22 ASN C C 179.009 0.20 1 80 22 22 ASN CA C 54.800 0.200 1 81 22 22 ASN CB C 37.500 0.200 1 82 22 22 ASN N N 123.227 0.20 1 83 23 23 THR H H 8.329 0.02 1 84 23 23 THR C C 178.370 0.20 1 85 23 23 THR CA C 64.700 0.200 1 86 23 23 THR CB C 67.900 0.200 1 87 23 23 THR N N 114.752 0.20 1 88 24 24 SER H H 7.462 0.02 1 89 24 24 SER C C 177.574 0.20 1 90 24 24 SER CA C 57.600 0.200 1 91 24 24 SER CB C 63.900 0.200 1 92 24 24 SER N N 114.037 0.20 1 93 25 25 ASN H H 7.965 0.02 1 94 25 25 ASN C C 176.696 0.20 1 95 25 25 ASN CA C 54.100 0.200 1 96 25 25 ASN CB C 36.800 0.200 1 97 25 25 ASN N N 120.213 0.20 1 98 26 26 THR H H 7.268 0.02 1 99 26 26 THR C C 176.462 0.20 1 100 26 26 THR CA C 61.100 0.200 1 101 26 26 THR CB C 70.500 0.200 1 102 26 26 THR N N 110.137 0.20 1 103 27 27 ILE H H 8.670 0.02 1 104 27 27 ILE C C 177.627 0.20 1 105 27 27 ILE CA C 60.600 0.200 1 106 27 27 ILE CB C 40.300 0.200 1 107 27 27 ILE N N 125.630 0.20 1 108 28 28 LYS H H 8.710 0.02 1 109 28 28 LYS C C 178.855 0.20 1 110 28 28 LYS CA C 54.500 0.200 1 111 28 28 LYS CE C 42.100 0.200 1 112 28 28 LYS N N 125.124 0.20 1 113 29 29 LEU H H 9.083 0.02 1 114 29 29 LEU C C 178.236 0.20 1 115 29 29 LEU CA C 54.500 0.200 1 116 29 29 LEU CB C 42.200 0.200 1 117 29 29 LEU N N 126.399 0.20 1 118 30 30 ILE H H 9.071 0.02 1 119 30 30 ILE C C 178.995 0.20 1 120 30 30 ILE CA C 61.200 0.200 1 121 30 30 ILE CB C 37.300 0.200 1 122 30 30 ILE N N 128.162 0.20 1 123 31 31 ALA H H 7.401 0.02 1 124 31 31 ALA C C 177.758 0.20 1 125 31 31 ALA CA C 51.600 0.200 1 126 31 31 ALA N N 119.111 0.20 1 127 32 32 ILE H H 8.207 0.02 1 128 32 32 ILE C C 176.603 0.20 1 129 32 32 ILE CA C 60.700 0.200 1 130 32 32 ILE CB C 39.900 0.200 1 131 32 32 ILE N N 119.405 0.20 1 132 33 33 GLU H H 8.430 0.02 1 133 33 33 GLU CA C 53.900 0.200 1 134 33 33 GLU N N 124.596 0.20 1 135 34 34 LYS H H 7.892 0.02 1 136 34 34 LYS CA C 55.100 0.200 1 137 34 34 LYS CB C 32.700 0.200 1 138 34 34 LYS CE C 42.100 0.200 1 139 34 34 LYS N N 120.043 0.20 1 140 35 35 SER C C 175.950 0.20 1 141 35 35 SER CA C 57.300 0.200 1 142 35 35 SER CB C 63.700 0.200 1 143 36 36 ASP H H 8.401 0.02 1 144 36 36 ASP C C 179.579 0.20 1 145 36 36 ASP CB C 40.300 0.200 1 146 36 36 ASP N N 119.319 0.20 1 147 37 37 TRP H H 8.801 0.02 1 148 37 37 TRP C C 178.951 0.20 1 149 37 37 TRP CA C 53.500 0.200 1 150 37 37 TRP CB C 28.100 0.200 1 151 37 37 TRP N N 126.368 0.20 1 152 38 38 THR H H 8.157 0.02 1 153 38 38 THR C C 178.297 0.20 1 154 38 38 THR CA C 63.400 0.200 1 155 38 38 THR CB C 69.300 0.200 1 156 38 38 THR N N 111.832 0.20 1 157 39 39 LYS H H 8.204 0.02 1 158 39 39 LYS C C 179.183 0.20 1 159 39 39 LYS CB C 32.000 0.200 1 160 39 39 LYS CE C 42.100 0.200 1 161 39 39 LYS N N 122.476 0.20 1 162 40 40 ASN H H 7.471 0.02 1 163 40 40 ASN C C 180.690 0.20 1 164 40 40 ASN CA C 55.600 0.200 1 165 40 40 ASN N N 116.010 0.20 1 166 41 41 TRP H H 7.694 0.02 1 167 41 41 TRP CA C 57.300 0.200 1 168 41 41 TRP CB C 28.500 0.200 1 169 41 41 TRP N N 119.867 0.20 1 170 42 42 GLU H H 8.126 0.02 1 171 42 42 GLU C C 179.534 0.20 1 172 42 42 GLU CA C 59.900 0.200 1 173 42 42 GLU CB C 29.500 0.200 1 174 42 42 GLU N N 123.482 0.20 1 175 43 43 ARG H H 6.838 0.02 1 176 43 43 ARG CA C 57.500 0.200 1 177 43 43 ARG CD C 43.300 0.200 1 178 43 43 ARG N N 115.494 0.20 1 179 44 44 SER C C 177.601 0.20 1 180 44 44 SER CB C 62.700 0.200 1 181 45 45 VAL H H 8.197 0.02 1 182 45 45 VAL C C 180.065 0.20 1 183 45 45 VAL CA C 65.500 0.200 1 184 45 45 VAL N N 123.020 0.20 1 185 46 46 ALA H H 7.244 0.02 1 186 46 46 ALA C C 183.030 0.20 1 187 46 46 ALA CA C 54.600 0.200 1 188 46 46 ALA CB C 18.100 0.200 1 189 46 46 ALA N N 119.186 0.20 1 190 47 47 ARG H H 7.912 0.02 1 191 47 47 ARG C C 177.584 0.20 1 192 47 47 ARG CA C 58.300 0.200 1 193 47 47 ARG CD C 43.300 0.200 1 194 47 47 ARG N N 118.633 0.20 1 195 48 48 ASP H H 7.826 0.02 1 196 48 48 ASP CA C 53.200 0.200 1 197 48 48 ASP N N 114.644 0.20 1 198 49 49 LEU C C 180.394 0.20 1 199 50 50 THR H H 7.676 0.02 1 200 50 50 THR CA C 60.200 0.200 1 201 50 50 THR N N 122.115 0.20 1 202 51 51 ARG H H 8.269 0.02 1 203 51 51 ARG CD C 43.300 0.200 1 204 51 51 ARG N N 118.415 0.20 1 205 52 52 TYR H H 7.977 0.02 1 206 52 52 TYR CA C 57.000 0.200 1 207 52 52 TYR N N 118.490 0.20 1 208 53 53 ASN H H 8.103 0.02 1 209 53 53 ASN N N 118.823 0.20 1 210 54 54 PRO C C 180.483 0.20 1 211 54 54 PRO CA C 62.300 0.200 1 212 55 55 ASP H H 8.178 0.02 1 213 55 55 ASP N N 120.676 0.20 1 214 56 56 VAL CA C 63.000 0.200 1 215 57 57 VAL CA C 59.300 0.200 1 216 58 58 ILE H H 8.104 0.02 1 217 58 58 ILE CA C 63.000 0.200 1 218 58 58 ILE N N 122.890 0.20 1 219 59 59 LEU H H 8.118 0.02 1 220 59 59 LEU C C 181.736 0.20 1 221 59 59 LEU CA C 56.600 0.200 1 222 59 59 LEU N N 121.069 0.20 1 223 60 60 GLU H H 7.750 0.02 1 224 60 60 GLU C C 179.122 0.20 1 225 60 60 GLU N N 119.745 0.20 1 226 61 61 LYS H H 7.998 0.02 1 227 61 61 LYS C C 179.399 0.20 1 228 61 61 LYS CA C 52.700 0.200 1 229 61 61 LYS CE C 42.100 0.200 1 230 61 61 LYS N N 120.984 0.20 1 231 62 62 GLN H H 7.535 0.02 1 232 62 62 GLN C C 178.675 0.20 1 233 62 62 GLN CA C 60.300 0.200 1 234 62 62 GLN N N 120.788 0.20 1 235 63 63 GLY H H 8.082 0.02 1 236 63 63 GLY C C 180.176 0.20 1 237 63 63 GLY CA C 45.100 0.200 1 238 63 63 GLY N N 109.991 0.20 1 239 64 64 PHE H H 7.697 0.02 1 240 64 64 PHE C C 180.840 0.20 1 241 64 64 PHE CA C 57.000 0.200 1 242 64 64 PHE N N 113.953 0.20 1 243 65 65 LYS H H 7.855 0.02 1 244 65 65 LYS C C 177.384 0.20 1 245 65 65 LYS CA C 56.600 0.200 1 246 65 65 LYS CE C 42.100 0.200 1 247 65 65 LYS N N 119.164 0.20 1 248 66 66 SER H H 8.079 0.02 1 249 66 66 SER N N 116.177 0.20 1 250 67 67 PRO C C 180.270 0.20 1 251 67 67 PRO CA C 63.900 0.200 1 252 68 68 ASN H H 8.033 0.02 1 253 68 68 ASN C C 179.476 0.20 1 254 68 68 ASN CA C 52.500 0.200 1 255 68 68 ASN CB C 37.700 0.200 1 256 68 68 ASN N N 114.049 0.20 1 257 69 69 SER H H 7.819 0.02 1 258 69 69 SER C C 178.634 0.20 1 259 69 69 SER CA C 62.000 0.200 1 260 69 69 SER N N 118.653 0.20 1 261 70 70 LYS H H 7.625 0.02 1 262 70 70 LYS C C 178.860 0.20 1 263 70 70 LYS CA C 58.400 0.200 1 264 70 70 LYS CE C 42.100 0.200 1 265 70 70 LYS N N 118.610 0.20 1 266 71 71 ILE H H 6.904 0.02 1 267 71 71 ILE C C 181.156 0.20 1 268 71 71 ILE CA C 63.900 0.200 1 269 71 71 ILE CB C 36.400 0.200 1 270 71 71 ILE N N 118.623 0.20 1 271 72 72 ILE H H 7.034 0.02 1 272 72 72 ILE C C 180.477 0.20 1 273 72 72 ILE CA C 65.100 0.200 1 274 72 72 ILE CB C 38.400 0.200 1 275 72 72 ILE N N 118.300 0.20 1 276 73 73 TYR H H 7.024 0.02 1 277 73 73 TYR CB C 38.500 0.200 1 278 73 73 TYR N N 116.547 0.20 1 279 74 74 PHE H H 8.208 0.02 1 280 74 74 PHE C C 180.206 0.20 1 281 74 74 PHE CA C 61.500 0.200 1 282 74 74 PHE CB C 39.900 0.200 1 283 74 74 PHE N N 120.417 0.20 1 284 75 75 ILE H H 8.541 0.02 1 285 75 75 ILE C C 180.490 0.20 1 286 75 75 ILE CA C 66.100 0.200 1 287 75 75 ILE CB C 36.700 0.200 1 288 75 75 ILE N N 120.453 0.20 1 289 76 76 LYS H H 8.334 0.02 1 290 76 76 LYS CA C 59.300 0.200 1 291 76 76 LYS CE C 42.100 0.200 1 292 76 76 LYS N N 117.769 0.20 1 293 77 77 GLY C C 177.279 0.20 1 294 77 77 GLY CA C 46.900 0.200 1 295 78 78 PHE H H 8.577 0.02 1 296 78 78 PHE C C 179.787 0.20 1 297 78 78 PHE CA C 60.000 0.200 1 298 78 78 PHE CB C 38.900 0.200 1 299 78 78 PHE N N 123.425 0.20 1 300 79 79 PHE H H 7.422 0.02 1 301 79 79 PHE C C 180.011 0.20 1 302 79 79 PHE CA C 57.100 0.200 1 303 79 79 PHE N N 110.915 0.20 1 304 80 80 TYR H H 7.506 0.02 1 305 80 80 TYR C C 179.734 0.20 1 306 80 80 TYR CA C 63.300 0.200 1 307 80 80 TYR CB C 38.300 0.200 1 308 80 80 TYR N N 125.609 0.20 1 309 81 81 ASN H H 8.668 0.02 1 310 81 81 ASN C C 177.038 0.20 1 311 81 81 ASN CA C 52.000 0.200 1 312 81 81 ASN CB C 36.900 0.200 1 313 81 81 ASN N N 116.955 0.20 1 314 82 82 SER H H 7.659 0.02 1 315 82 82 SER C C 176.237 0.20 1 316 82 82 SER CA C 57.500 0.200 1 317 82 82 SER CB C 66.100 0.200 1 318 82 82 SER N N 116.601 0.20 1 319 83 83 ASN H H 8.604 0.02 1 320 83 83 ASN C C 178.277 0.20 1 321 83 83 ASN CA C 53.200 0.200 1 322 83 83 ASN CB C 38.100 0.200 1 323 83 83 ASN N N 116.788 0.20 1 324 84 84 THR H H 8.629 0.02 1 325 84 84 THR C C 176.387 0.20 1 326 84 84 THR CA C 63.200 0.200 1 327 84 84 THR CB C 69.000 0.200 1 328 84 84 THR N N 121.328 0.20 1 329 85 85 LYS H H 7.736 0.02 1 330 85 85 LYS C C 177.559 0.20 1 331 85 85 LYS CA C 54.500 0.200 1 332 85 85 LYS CB C 32.800 0.200 1 333 85 85 LYS CE C 42.100 0.200 1 334 85 85 LYS N N 127.582 0.20 1 335 86 86 VAL H H 8.352 0.02 1 336 86 86 VAL C C 178.226 0.20 1 337 86 86 VAL CA C 61.000 0.200 1 338 86 86 VAL CB C 31.100 0.200 1 339 86 86 VAL N N 124.199 0.20 1 340 87 87 ILE H H 9.173 0.02 1 341 87 87 ILE C C 176.594 0.20 1 342 87 87 ILE CA C 59.300 0.200 1 343 87 87 ILE CB C 38.900 0.200 1 344 87 87 ILE N N 131.117 0.20 1 345 88 88 VAL H H 8.362 0.02 1 346 88 88 VAL C C 179.455 0.20 1 347 88 88 VAL CA C 60.300 0.200 1 348 88 88 VAL CB C 31.300 0.200 1 349 88 88 VAL N N 126.301 0.20 1 350 89 89 ARG H H 9.006 0.02 1 351 89 89 ARG C C 178.437 0.20 1 352 89 89 ARG CA C 53.900 0.200 1 353 89 89 ARG CB C 31.300 0.200 1 354 89 89 ARG CD C 43.300 0.200 1 355 89 89 ARG N N 127.215 0.20 1 356 90 90 ASN H H 8.802 0.02 1 357 90 90 ASN CA C 51.000 0.200 1 358 90 90 ASN CB C 37.500 0.200 1 359 90 90 ASN N N 121.792 0.20 1 360 91 91 PRO C C 179.494 0.20 1 361 91 91 PRO CA C 62.700 0.200 1 362 91 91 PRO CB C 31.100 0.200 1 363 92 92 THR H H 8.160 0.02 1 364 92 92 THR C C 177.193 0.20 1 365 92 92 THR CA C 61.500 0.200 1 366 92 92 THR CB C 69.400 0.200 1 367 92 92 THR N N 115.394 0.20 1 368 93 93 PHE H H 8.211 0.02 1 369 93 93 PHE C C 178.493 0.20 1 370 93 93 PHE CA C 57.200 0.200 1 371 93 93 PHE CB C 38.900 0.200 1 372 93 93 PHE N N 123.096 0.20 1 373 94 94 LYS H H 8.298 0.02 1 374 94 94 LYS CB C 31.900 0.200 1 375 94 94 LYS CE C 42.100 0.200 1 376 94 94 LYS N N 124.480 0.20 1 377 95 95 GLY C C 180.068 0.20 1 378 96 96 GLY H H 8.449 0.02 1 379 96 96 GLY C C 177.253 0.20 1 380 96 96 GLY CA C 44.900 0.200 1 381 96 96 GLY N N 108.858 0.20 1 382 97 97 SER H H 8.208 0.02 1 383 97 97 SER C C 177.729 0.20 1 384 97 97 SER CA C 57.800 0.200 1 385 97 97 SER CB C 63.200 0.200 1 386 97 97 SER N N 116.180 0.20 1 387 98 98 TYR H H 8.258 0.02 1 388 98 98 TYR C C 179.378 0.20 1 389 98 98 TYR CA C 58.600 0.200 1 390 98 98 TYR N N 123.010 0.20 1 391 99 99 ARG H H 8.066 0.02 1 392 99 99 ARG C C 179.462 0.20 1 393 99 99 ARG CA C 56.700 0.200 1 394 99 99 ARG CB C 29.300 0.200 1 395 99 99 ARG CD C 43.300 0.200 1 396 99 99 ARG N N 121.061 0.20 1 397 100 100 ASN H H 8.021 0.02 1 398 100 100 ASN C C 178.465 0.20 1 399 100 100 ASN CA C 53.200 0.200 1 400 100 100 ASN CB C 37.800 0.200 1 401 100 100 ASN N N 118.405 0.20 1 402 101 101 ARG H H 8.023 0.02 1 403 101 101 ARG C C 179.931 0.20 1 404 101 101 ARG CA C 54.300 0.200 1 405 101 101 ARG CB C 29.400 0.200 1 406 101 101 ARG CD C 43.300 0.200 1 407 101 101 ARG N N 121.447 0.20 1 408 102 102 LYS H H 8.141 0.02 1 409 102 102 LYS CA C 57.200 0.200 1 410 102 102 LYS CE C 42.100 0.200 1 411 102 102 LYS N N 121.774 0.20 1 412 103 103 LYS H H 7.682 0.02 1 413 103 103 LYS C C 179.586 0.20 1 414 103 103 LYS CA C 55.800 0.200 1 415 103 103 LYS CB C 31.900 0.200 1 416 103 103 LYS CE C 42.100 0.200 1 417 103 103 LYS N N 118.422 0.20 1 418 104 104 GLN H H 7.804 0.02 1 419 104 104 GLN C C 177.500 0.20 1 420 104 104 GLN N N 109.693 0.20 1 421 105 105 SER H H 7.096 0.02 1 422 105 105 SER C C 179.549 0.20 1 423 105 105 SER CA C 56.600 0.200 1 424 105 105 SER N N 116.554 0.20 1 425 106 106 ILE H H 7.677 0.02 1 426 106 106 ILE C C 176.660 0.20 1 427 106 106 ILE CA C 61.100 0.200 1 428 106 106 ILE CB C 37.800 0.200 1 429 106 106 ILE N N 118.674 0.20 1 430 107 107 ASP H H 8.842 0.02 1 431 107 107 ASP C C 176.297 0.20 1 432 107 107 ASP CA C 59.900 0.200 1 433 107 107 ASP N N 128.496 0.20 1 434 108 108 VAL H H 8.967 0.02 1 435 108 108 VAL CA C 58.000 0.200 1 436 108 108 VAL N N 126.349 0.20 1 437 109 109 PHE H H 8.296 0.02 1 438 109 109 PHE C C 180.225 0.20 1 439 109 109 PHE N N 117.723 0.20 1 440 110 110 ILE H H 7.310 0.02 1 441 110 110 ILE C C 180.840 0.20 1 442 110 110 ILE CA C 60.700 0.200 1 443 110 110 ILE CB C 37.800 0.200 1 444 110 110 ILE N N 121.319 0.20 1 445 111 111 GLN H H 7.867 0.02 1 446 111 111 GLN C C 181.795 0.20 1 447 111 111 GLN CA C 58.400 0.200 1 448 111 111 GLN CB C 29.200 0.200 1 449 111 111 GLN N N 119.082 0.20 1 450 112 112 LYS H H 8.372 0.02 1 451 112 112 LYS C C 181.303 0.20 1 452 112 112 LYS CA C 57.200 0.200 1 453 112 112 LYS CE C 42.100 0.200 1 454 112 112 LYS N N 120.312 0.20 1 455 113 113 ILE H H 8.269 0.02 1 456 113 113 ILE C C 182.332 0.20 1 457 113 113 ILE N N 115.592 0.20 1 458 114 114 SER H H 7.542 0.02 1 459 114 114 SER C C 179.726 0.20 1 460 114 114 SER CA C 63.900 0.200 1 461 114 114 SER N N 109.206 0.20 1 462 115 115 GLU H H 7.296 0.02 1 463 115 115 GLU CA C 58.900 0.200 1 464 115 115 GLU CB C 29.000 0.200 1 465 115 115 GLU N N 122.987 0.20 1 466 116 116 TYR H H 8.208 0.02 1 467 116 116 TYR C C 177.384 0.20 1 468 116 116 TYR CA C 56.600 0.200 1 469 116 116 TYR N N 120.417 0.20 1 470 117 117 THR H H 8.079 0.02 1 471 117 117 THR CA C 63.000 0.200 1 472 117 117 THR N N 116.177 0.20 1 473 118 118 ASP CA C 58.100 0.200 1 474 119 119 TYR H H 8.578 0.02 1 475 119 119 TYR C C 177.914 0.20 1 476 119 119 TYR CA C 52.700 0.200 1 477 119 119 TYR N N 124.132 0.20 1 478 120 120 LYS H H 8.757 0.02 1 479 120 120 LYS CA C 54.700 0.200 1 480 120 120 LYS CB C 32.300 0.200 1 481 120 120 LYS CE C 42.100 0.200 1 482 120 120 LYS N N 120.685 0.20 1 483 121 121 ASN H H 8.168 0.02 1 484 121 121 ASN N N 124.054 0.20 1 485 122 122 ASP C C 177.727 0.20 1 486 122 122 ASP CA C 49.500 0.200 1 487 123 123 ILE H H 8.635 0.02 1 488 123 123 ILE C C 178.090 0.20 1 489 123 123 ILE CA C 57.200 0.200 1 490 123 123 ILE CB C 36.200 0.200 1 491 123 123 ILE N N 120.586 0.20 1 492 124 124 LEU H H 9.588 0.02 1 493 124 124 LEU C C 177.614 0.20 1 494 124 124 LEU CA C 55.500 0.200 1 495 124 124 LEU CB C 42.500 0.200 1 496 124 124 LEU N N 124.455 0.20 1 497 125 125 ASN H H 9.547 0.02 1 498 125 125 ASN CA C 52.000 0.200 1 499 125 125 ASN CB C 37.500 0.200 1 500 125 125 ASN N N 120.103 0.20 1 501 126 126 LYS H H 7.607 0.02 1 502 126 126 LYS CA C 54.700 0.200 1 503 126 126 LYS CE C 42.100 0.200 1 504 126 126 LYS N N 112.931 0.20 1 505 127 127 TYR H H 8.458 0.02 1 506 127 127 TYR CA C 56.100 0.200 1 507 127 127 TYR N N 123.850 0.20 1 508 128 128 THR CA C 63.000 0.200 1 509 129 129 LYS C C 178.676 0.20 1 510 129 129 LYS CA C 62.400 0.200 1 511 129 129 LYS CE C 42.100 0.200 1 512 130 130 LEU H H 9.110 0.02 1 513 130 130 LEU C C 181.294 0.20 1 514 130 130 LEU CB C 42.800 0.200 1 515 130 130 LEU N N 120.225 0.20 1 516 131 131 ASP H H 7.751 0.02 1 517 131 131 ASP C C 180.070 0.20 1 518 131 131 ASP CB C 39.700 0.200 1 519 131 131 ASP N N 119.471 0.20 1 520 132 132 ASP H H 7.917 0.02 1 521 132 132 ASP C C 177.974 0.20 1 522 132 132 ASP CA C 55.600 0.200 1 523 132 132 ASP CB C 39.800 0.200 1 524 132 132 ASP N N 117.380 0.20 1 525 133 133 ILE H H 7.677 0.02 1 526 133 133 ILE C C 179.938 0.20 1 527 133 133 ILE CA C 60.800 0.200 1 528 133 133 ILE N N 119.857 0.20 1 529 134 134 ALA H H 7.575 0.02 1 530 134 134 ALA C C 181.614 0.20 1 531 134 134 ALA CA C 55.300 0.200 1 532 134 134 ALA N N 124.611 0.20 1 533 135 135 ASN H H 8.432 0.02 1 534 135 135 ASN C C 181.032 0.20 1 535 135 135 ASN CA C 55.900 0.200 1 536 135 135 ASN N N 115.741 0.20 1 537 136 136 SER H H 8.384 0.02 1 538 136 136 SER N N 116.702 0.20 1 539 137 137 PHE H H 7.196 0.02 1 540 137 137 PHE C C 178.882 0.20 1 541 137 137 PHE CA C 60.600 0.200 1 542 137 137 PHE N N 125.518 0.20 1 543 138 138 ASN H H 8.591 0.02 1 544 138 138 ASN C C 181.258 0.20 1 545 138 138 ASN CA C 55.600 0.200 1 546 138 138 ASN CB C 37.600 0.200 1 547 138 138 ASN N N 119.137 0.20 1 548 139 139 LEU H H 8.525 0.02 1 549 139 139 LEU CA C 57.500 0.200 1 550 139 139 LEU N N 122.389 0.20 1 551 140 140 GLY H H 7.131 0.02 1 552 140 140 GLY C C 177.699 0.20 1 553 140 140 GLY CA C 46.600 0.200 1 554 140 140 GLY N N 106.097 0.20 1 555 141 141 LEU H H 7.851 0.02 1 556 141 141 LEU C C 181.755 0.20 1 557 141 141 LEU CA C 57.600 0.200 1 558 141 141 LEU N N 122.681 0.20 1 559 142 142 SER H H 8.009 0.02 1 560 142 142 SER C C 177.425 0.20 1 561 142 142 SER CA C 60.800 0.200 1 562 142 142 SER N N 113.237 0.20 1 563 143 143 TYR H H 8.184 0.02 1 564 143 143 TYR C C 178.465 0.20 1 565 143 143 TYR CA C 55.200 0.200 1 566 143 143 TYR CB C 37.800 0.200 1 567 143 143 TYR N N 108.882 0.20 1 568 144 144 MET H H 8.008 0.02 1 569 144 144 MET C C 181.082 0.20 1 570 144 144 MET CA C 50.500 0.200 1 571 144 144 MET N N 121.615 0.20 1 572 145 145 GLU H H 8.132 0.02 1 573 145 145 GLU C C 181.435 0.20 1 574 145 145 GLU CA C 58.900 0.200 1 575 145 145 GLU CB C 28.400 0.200 1 576 145 145 GLU N N 118.306 0.20 1 577 146 146 SER H H 7.254 0.02 1 578 146 146 SER C C 177.821 0.20 1 579 146 146 SER CA C 59.900 0.200 1 580 146 146 SER CB C 62.700 0.200 1 581 146 146 SER N N 114.188 0.20 1 582 147 147 LEU H H 7.044 0.02 1 583 147 147 LEU C C 180.706 0.20 1 584 147 147 LEU CA C 58.300 0.200 1 585 147 147 LEU N N 121.902 0.20 1 586 148 148 LEU H H 7.062 0.02 1 587 148 148 LEU C C 180.048 0.20 1 588 148 148 LEU CA C 54.900 0.200 1 589 148 148 LEU CB C 41.400 0.200 1 590 148 148 LEU N N 118.627 0.20 1 591 149 149 LYS H H 7.787 0.02 1 592 149 149 LYS C C 178.366 0.20 1 593 149 149 LYS CA C 55.900 0.200 1 594 149 149 LYS CB C 31.600 0.200 1 595 149 149 LYS CE C 42.100 0.200 1 596 149 149 LYS N N 122.084 0.20 1 597 150 150 LYS H H 7.829 0.02 1 598 150 150 LYS N N 128.796 0.20 1 stop_ save_