data_18991 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignment of [2Fe-2S]-ferredoxin in its oxidized state ; _BMRB_accession_number 18991 _BMRB_flat_file_name bmr18991.str _Entry_type original _Submission_date 2013-01-30 _Accession_date 2013-01-30 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kim 'Jin Hae' . . 2 Markley John L. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 93 "13C chemical shifts" 261 "15N chemical shifts" 89 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-02-14 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 18992 '[2Fe-2S]-ferredoxin, reduced state' stop_ _Original_release_date 2014-02-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title '[2Fe-2S]-Ferredoxin Binds Directly to Cysteine Desulfurase and Supplies an Electron for Iron-Sulfur Cluster Assembly but Is Displaced by the Scaffold Protein or Bacterial Frataxin.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23682711 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kim 'Jin Hae' . . 2 Frederick Ronnie O. . 3 Reinen Nichole M. . 4 Troupis Andrew T. . 5 Markley John L. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 135 _Journal_issue 22 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 8117 _Page_last 8120 _Year 2013 _Details . loop_ _Keyword 'cysteine desulfurase' ferredoxin 'iron-sulfur cluster biogenesis' IscS stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name [2Fe-2S]Fdx _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ferredoxin $ferredoxin '2Fe-2S cluster' $entity_FES stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic yes _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ferredoxin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ferredoxin _Molecular_mass . _Mol_thiol_state 'free and other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 111 _Mol_residue_sequence ; MPKIVILPHQDLCPDGAVLE ANSGETILDAALRNGIEIEH ACEKSCACTTCHCIVREGFD SLPESSEQEDDMLDKAWGLE PESRLSCQARVTDEDLVVEI PRYTINHAREH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 PRO 3 LYS 4 ILE 5 VAL 6 ILE 7 LEU 8 PRO 9 HIS 10 GLN 11 ASP 12 LEU 13 CYS 14 PRO 15 ASP 16 GLY 17 ALA 18 VAL 19 LEU 20 GLU 21 ALA 22 ASN 23 SER 24 GLY 25 GLU 26 THR 27 ILE 28 LEU 29 ASP 30 ALA 31 ALA 32 LEU 33 ARG 34 ASN 35 GLY 36 ILE 37 GLU 38 ILE 39 GLU 40 HIS 41 ALA 42 CYS 43 GLU 44 LYS 45 SER 46 CYS 47 ALA 48 CYS 49 THR 50 THR 51 CYS 52 HIS 53 CYS 54 ILE 55 VAL 56 ARG 57 GLU 58 GLY 59 PHE 60 ASP 61 SER 62 LEU 63 PRO 64 GLU 65 SER 66 SER 67 GLU 68 GLN 69 GLU 70 ASP 71 ASP 72 MET 73 LEU 74 ASP 75 LYS 76 ALA 77 TRP 78 GLY 79 LEU 80 GLU 81 PRO 82 GLU 83 SER 84 ARG 85 LEU 86 SER 87 CYS 88 GLN 89 ALA 90 ARG 91 VAL 92 THR 93 ASP 94 GLU 95 ASP 96 LEU 97 VAL 98 VAL 99 GLU 100 ILE 101 PRO 102 ARG 103 TYR 104 THR 105 ILE 106 ASN 107 HIS 108 ALA 109 ARG 110 GLU 111 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-19 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 18992 ferredoxin 100.00 111 100.00 100.00 3.97e-74 BMRB 19273 holo-Ferredoxin 99.10 115 100.00 100.00 1.90e-73 PDB 1I7H "Crystal Sturcuture Of Fdx" 100.00 111 100.00 100.00 3.97e-74 DBJ BAA16415 "[2Fe-2S] ferredoxin [Escherichia coli str. K12 substr. W3110]" 100.00 111 100.00 100.00 3.97e-74 DBJ BAB36814 "[2FE-2S] ferredoxin [Escherichia coli O157:H7 str. Sakai]" 100.00 111 100.00 100.00 3.97e-74 DBJ BAG78335 "ferredoxin [Escherichia coli SE11]" 100.00 111 100.00 100.00 3.97e-74 DBJ BAI26770 "[2Fe-2S] ferredoxin [Escherichia coli O26:H11 str. 11368]" 100.00 111 100.00 100.00 3.97e-74 DBJ BAI31799 "[2Fe-2S] ferredoxin [Escherichia coli O103:H2 str. 12009]" 100.00 111 100.00 100.00 3.97e-74 EMBL CAP76977 "2Fe-2S ferredoxin [Escherichia coli LF82]" 100.00 111 99.10 99.10 1.93e-73 EMBL CAQ32898 "reduced ferredoxin [Escherichia coli BL21(DE3)]" 100.00 111 100.00 100.00 3.97e-74 EMBL CAQ88191 "[2Fe-2S] ferredoxin [Escherichia fergusonii ATCC 35469]" 100.00 111 99.10 99.10 1.93e-73 EMBL CAQ99416 "[2Fe-2S] ferredoxin [Escherichia coli IAI1]" 100.00 111 100.00 100.00 3.97e-74 EMBL CAR03967 "[2Fe-2S] ferredoxin [Escherichia coli S88]" 100.00 111 99.10 99.10 1.93e-73 GB AAA23755 "ferredoxin [Escherichia coli]" 100.00 111 100.00 100.00 3.97e-74 GB AAC75578 "[2Fe-2S] ferredoxin [Escherichia coli str. K-12 substr. MG1655]" 100.00 111 100.00 100.00 3.97e-74 GB AAG57639 "[2FE-2S] ferredoxin, electron carrer protein [Escherichia coli O157:H7 str. EDL933]" 100.00 111 100.00 100.00 3.97e-74 GB AAN44071 "[2FE-2S] ferredoxin, electron carrer protein [Shigella flexneri 2a str. 301]" 100.00 111 100.00 100.00 3.97e-74 GB AAN81500 "Ferredoxin, 2Fe-2S [Escherichia coli CFT073]" 100.00 111 98.20 99.10 4.58e-73 REF NP_311418 "[2FE-2S] ferredoxin [Escherichia coli O157:H7 str. Sakai]" 100.00 111 100.00 100.00 3.97e-74 REF NP_417020 "[2Fe-2S] ferredoxin [Escherichia coli str. K-12 substr. MG1655]" 100.00 111 100.00 100.00 3.97e-74 REF NP_708364 "[2FE-2S] ferredoxin electron carrer protein [Shigella flexneri 2a str. 301]" 100.00 111 100.00 100.00 3.97e-74 REF WP_001124467 "MULTISPECIES: (2Fe-2S) ferredoxin [Escherichia]" 100.00 111 99.10 99.10 2.68e-73 REF WP_001124468 "(2Fe-2S) ferredoxin [Escherichia coli]" 100.00 111 98.20 99.10 5.82e-73 SP P0A9R4 "RecName: Full=2Fe-2S ferredoxin" 100.00 111 100.00 100.00 3.97e-74 SP P0A9R5 "RecName: Full=2Fe-2S ferredoxin" 100.00 111 100.00 100.00 3.97e-74 SP P0A9R6 "RecName: Full=2Fe-2S ferredoxin" 100.00 111 100.00 100.00 3.97e-74 stop_ save_ ############# # Ligands # ############# save_FES _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_FES (FE2/S2 (INORGANIC) CLUSTER)" _BMRB_code FES _PDB_code FES _Molecular_mass 175.820 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE1 FE1 FE . 0 . ? FE2 FE2 FE . 0 . ? S1 S1 S . 0 . ? S2 S2 S . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING FE1 S1 ? ? SING FE1 S2 ? ? SING FE2 S1 ? ? SING FE2 S2 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $ferredoxin 'E. coli' 562 Bacteria . Escherichia coli K12 fdx stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $ferredoxin 'recombinant technology' . Escherichia coli Rosetta(DE3)pLysS pDEST42 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ferredoxin 1 mM '[U-13C; U-15N]' $entity_FES 1 mM 'natural abundance' TRIS 20 mM 'natural abundance' EDTA 0.5 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' DTT 5 mM 'natural abundance' 'sodium azide' 0.02 % 'natural abundance' DSS 0.7 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _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_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _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_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . 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' 0.15 . M pH 7.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D CBCA(CO)NH' '3D HNCACB' '3D HN(CA)CO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name ferredoxin _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 2 2 PRO C C 171.003 0.05 1 2 2 2 PRO CA C 62.705 0.006 1 3 2 2 PRO CB C 33.066 0.016 1 4 3 3 LYS H H 9.108 0.05 1 5 3 3 LYS C C 175.494 0.05 1 6 3 3 LYS CA C 55.609 0.003 1 7 3 3 LYS CB C 34.462 0.012 1 8 3 3 LYS N N 121.594 0.009 1 9 4 4 ILE H H 8.966 0.001 1 10 4 4 ILE C C 174.554 0.05 1 11 4 4 ILE CA C 60.789 0.008 1 12 4 4 ILE CB C 40.642 0.013 1 13 4 4 ILE N N 119.415 0.008 1 14 5 5 VAL H H 8.672 0.001 1 15 5 5 VAL C C 174.647 0.05 1 16 5 5 VAL CA C 61.825 0.015 1 17 5 5 VAL CB C 33.245 0.013 1 18 5 5 VAL N N 129.082 0.01 1 19 6 6 ILE H H 9.293 0.001 1 20 6 6 ILE C C 176.905 0.05 1 21 6 6 ILE CA C 58.687 0.007 1 22 6 6 ILE CB C 37.302 0.014 1 23 6 6 ILE N N 127.93 0.01 1 24 7 7 LEU H H 8.454 0.001 1 25 7 7 LEU CA C 54.248 0.05 1 26 7 7 LEU CB C 39.817 0.05 1 27 7 7 LEU N N 128.042 0.011 1 28 8 8 PRO C C 175.485 0.05 1 29 8 8 PRO CA C 64.624 0.006 1 30 8 8 PRO CB C 31.816 0.05 1 31 9 9 HIS H H 7.957 0.001 1 32 9 9 HIS C C 176.786 0.05 1 33 9 9 HIS CA C 56.95 0.008 1 34 9 9 HIS CB C 34.085 0.008 1 35 9 9 HIS N N 125.51 0.011 1 36 10 10 GLN H H 8.658 0.001 1 37 10 10 GLN HE21 H 7.641 0.002 2 38 10 10 GLN HE22 H 6.788 0.002 2 39 10 10 GLN C C 174.931 0.05 1 40 10 10 GLN CA C 59.683 0.017 1 41 10 10 GLN CB C 29.344 0.029 1 42 10 10 GLN CG C 33.485 0.031 1 43 10 10 GLN CD C 179.837 0.016 1 44 10 10 GLN N N 125.332 0.01 1 45 10 10 GLN NE2 N 111.951 0.093 1 46 11 11 ASP H H 8.433 0.003 1 47 11 11 ASP C C 177.259 0.05 1 48 11 11 ASP CA C 55.725 0.004 1 49 11 11 ASP CB C 43.667 0.024 1 50 11 11 ASP N N 114.719 0.017 1 51 12 12 LEU H H 9.206 0.002 1 52 12 12 LEU C C 178.414 0.05 1 53 12 12 LEU CA C 56.764 0.007 1 54 12 12 LEU CB C 44.326 0.053 1 55 12 12 LEU N N 119.643 0.011 1 56 13 13 CYS H H 8.4 0.002 1 57 13 13 CYS CA C 55.078 0.05 1 58 13 13 CYS CB C 25.582 0.05 1 59 13 13 CYS N N 108.984 0.014 1 60 14 14 PRO C C 176.295 0.05 1 61 14 14 PRO CA C 65.837 0.003 1 62 14 14 PRO CB C 32.237 0.013 1 63 15 15 ASP H H 8.692 0.001 1 64 15 15 ASP C C 177.312 0.05 1 65 15 15 ASP CA C 53.742 0.015 1 66 15 15 ASP CB C 42.12 0.034 1 67 15 15 ASP N N 114.977 0.012 1 68 16 16 GLY H H 8.031 0.05 1 69 16 16 GLY C C 171.499 0.05 1 70 16 16 GLY CA C 44.383 0.004 1 71 16 16 GLY N N 108.464 0.008 1 72 17 17 ALA H H 8.627 0.001 1 73 17 17 ALA CA C 52.296 0.006 1 74 17 17 ALA CB C 23.064 0.008 1 75 17 17 ALA N N 119.917 0.008 1 76 18 18 VAL H H 8.447 0.001 1 77 18 18 VAL C C 174.48 0.05 1 78 18 18 VAL CA C 62.178 0.011 1 79 18 18 VAL CB C 33.389 0.01 1 80 18 18 VAL N N 120.213 0.005 1 81 19 19 LEU H H 9.327 0.002 1 82 19 19 LEU C C 175.297 0.05 1 83 19 19 LEU CA C 52.812 0.014 1 84 19 19 LEU CB C 43.462 0.019 1 85 19 19 LEU N N 125.836 0.009 1 86 20 20 GLU H H 8.513 0.05 1 87 20 20 GLU C C 174.599 0.05 1 88 20 20 GLU CA C 55.704 0.002 1 89 20 20 GLU CB C 29.917 0.008 1 90 20 20 GLU N N 121.478 0.009 1 91 21 21 ALA H H 8.694 0.001 1 92 21 21 ALA C C 176.025 0.05 1 93 21 21 ALA CA C 49.906 0.018 1 94 21 21 ALA CB C 22.735 0.008 1 95 21 21 ALA N N 126.933 0.008 1 96 22 22 ASN H H 9.418 0.001 1 97 22 22 ASN HD21 H 7.494 0.05 2 98 22 22 ASN HD22 H 6.974 0.001 2 99 22 22 ASN C C 174.836 0.05 1 100 22 22 ASN CA C 51.761 0.015 1 101 22 22 ASN CB C 39.823 0.017 1 102 22 22 ASN CG C 176.319 0.05 1 103 22 22 ASN N N 120.894 0.009 1 104 22 22 ASN ND2 N 113.84 0.075 1 105 23 23 SER H H 8.793 0.001 1 106 23 23 SER C C 175.821 0.05 1 107 23 23 SER CA C 60.738 0.031 1 108 23 23 SER CB C 62.786 0.01 1 109 23 23 SER N N 116.561 0.008 1 110 24 24 GLY H H 9.104 0.001 1 111 24 24 GLY C C 173.446 0.05 1 112 24 24 GLY CA C 45.275 0.01 1 113 24 24 GLY N N 115.918 0.009 1 114 25 25 GLU H H 7.859 0.001 1 115 25 25 GLU C C 175.41 0.05 1 116 25 25 GLU CA C 55.202 0.005 1 117 25 25 GLU CB C 31.879 0.005 1 118 25 25 GLU N N 122.546 0.009 1 119 26 26 THR H H 8.66 0.002 1 120 26 26 THR C C 175.719 0.05 1 121 26 26 THR CA C 60.669 0.01 1 122 26 26 THR CB C 70.567 0.019 1 123 26 26 THR N N 111.68 0.008 1 124 27 27 ILE H H 8.214 0.001 1 125 27 27 ILE C C 176.812 0.05 1 126 27 27 ILE CA C 66.005 0.005 1 127 27 27 ILE CB C 39.003 0.003 1 128 27 27 ILE N N 118.983 0.012 1 129 28 28 LEU H H 7.648 0.001 1 130 28 28 LEU C C 177.027 0.05 1 131 28 28 LEU CA C 57.997 0.002 1 132 28 28 LEU CB C 40.562 0.011 1 133 28 28 LEU N N 115.72 0.026 1 134 29 29 ASP H H 8.226 0.001 1 135 29 29 ASP C C 179.594 0.05 1 136 29 29 ASP CA C 57.769 0.021 1 137 29 29 ASP CB C 39.461 0.039 1 138 29 29 ASP N N 119.248 0.034 1 139 30 30 ALA H H 7.984 0.001 1 140 30 30 ALA C C 179.307 0.05 1 141 30 30 ALA CA C 55.267 0.006 1 142 30 30 ALA CB C 18.158 0.008 1 143 30 30 ALA N N 122.266 0.009 1 144 31 31 ALA H H 8.226 0.001 1 145 31 31 ALA C C 180.018 0.05 1 146 31 31 ALA CA C 56.202 0.035 1 147 31 31 ALA CB C 17.457 0.051 1 148 31 31 ALA N N 122.162 0.018 1 149 32 32 LEU H H 9.218 0.002 1 150 32 32 LEU C C 181.917 0.05 1 151 32 32 LEU CA C 58.093 0.001 1 152 32 32 LEU CB C 41.238 0.008 1 153 32 32 LEU N N 118.492 0.04 1 154 33 33 ARG H H 7.893 0.05 1 155 33 33 ARG C C 176.252 0.05 1 156 33 33 ARG CA C 58.521 0.03 1 157 33 33 ARG CB C 29.48 0.009 1 158 33 33 ARG N N 118.079 0.006 1 159 34 34 ASN H H 7.399 0.001 1 160 34 34 ASN HD21 H 8.371 0.001 2 161 34 34 ASN HD22 H 7.102 0.001 2 162 34 34 ASN C C 173.788 0.05 1 163 34 34 ASN CA C 53.874 0.033 1 164 34 34 ASN CB C 41.665 0.026 1 165 34 34 ASN CG C 178.44 0.05 1 166 34 34 ASN N N 116.607 0.007 1 167 34 34 ASN ND2 N 115.218 0.063 1 168 35 35 GLY H H 7.71 0.003 1 169 35 35 GLY C C 173.451 0.05 1 170 35 35 GLY CA C 46.592 0.019 1 171 35 35 GLY N N 106.319 0.006 1 172 36 36 ILE H H 8.107 0.001 1 173 36 36 ILE C C 174.916 0.05 1 174 36 36 ILE CA C 59.546 0.009 1 175 36 36 ILE CB C 35.935 0.016 1 176 36 36 ILE N N 122.565 0.012 1 177 37 37 GLU H H 8.18 0.001 1 178 37 37 GLU C C 174.91 0.05 1 179 37 37 GLU CA C 55.702 0.029 1 180 37 37 GLU CB C 27.406 0.006 1 181 37 37 GLU N N 127.535 0.024 1 182 38 38 ILE H H 7.403 0.003 1 183 38 38 ILE C C 176.096 0.05 1 184 38 38 ILE CA C 62.729 0.009 1 185 38 38 ILE CB C 38.905 0.011 1 186 38 38 ILE N N 124.921 0.036 1 187 39 39 GLU H H 9.05 0.011 1 188 39 39 GLU CA C 58.522 0.05 1 189 39 39 GLU CB C 30.52 0.05 1 190 39 39 GLU N N 132.311 0.039 1 191 52 52 HIS C C 172.24 0.05 1 192 52 52 HIS CA C 55.658 0.05 1 193 52 52 HIS CB C 30.693 0.046 1 194 53 53 CYS H H 9.634 0.001 1 195 53 53 CYS C C 169.301 0.05 1 196 53 53 CYS CA C 55.555 0.008 1 197 53 53 CYS CB C 31.924 0.007 1 198 53 53 CYS N N 122.447 0.02 1 199 54 54 ILE H H 9.335 0.001 1 200 54 54 ILE C C 175.361 0.05 1 201 54 54 ILE CA C 61.203 0.015 1 202 54 54 ILE CB C 40.151 0.012 1 203 54 54 ILE N N 119.436 0.007 1 204 55 55 VAL H H 8.558 0.001 1 205 55 55 VAL C C 173.776 0.05 1 206 55 55 VAL CA C 62.386 0.005 1 207 55 55 VAL CB C 30.284 0.014 1 208 55 55 VAL N N 129.517 0.012 1 209 56 56 ARG H H 7.883 0.002 1 210 56 56 ARG C C 177.053 0.05 1 211 56 56 ARG CA C 57.748 0.007 1 212 56 56 ARG CB C 30.507 0.041 1 213 56 56 ARG N N 125.963 0.016 1 214 57 57 GLU H H 7.928 0.001 1 215 57 57 GLU C C 176.101 0.05 1 216 57 57 GLU CA C 57.392 0.028 1 217 57 57 GLU CB C 33.002 0.007 1 218 57 57 GLU N N 116.148 0.013 1 219 58 58 GLY H H 8.82 0.001 1 220 58 58 GLY C C 176.759 0.05 1 221 58 58 GLY CA C 45.058 0.012 1 222 58 58 GLY N N 109.488 0.007 1 223 59 59 PHE H H 9.184 0.001 1 224 59 59 PHE C C 177.026 0.05 1 225 59 59 PHE CA C 62.913 0.011 1 226 59 59 PHE CB C 39.795 0.014 1 227 59 59 PHE N N 125.775 0.014 1 228 60 60 ASP H H 8.916 0.001 1 229 60 60 ASP C C 175.875 0.05 1 230 60 60 ASP CA C 55.954 0.01 1 231 60 60 ASP CB C 40.026 0.012 1 232 60 60 ASP N N 115.633 0.009 1 233 61 61 SER H H 7.897 0.001 1 234 61 61 SER C C 174.615 0.05 1 235 61 61 SER CA C 59.426 0.007 1 236 61 61 SER CB C 64.645 0.031 1 237 61 61 SER N N 114.946 0.009 1 238 62 62 LEU H H 7.205 0.05 1 239 62 62 LEU CA C 52.4 0.05 1 240 62 62 LEU CB C 40.597 0.05 1 241 62 62 LEU N N 124.875 0.01 1 242 63 63 PRO C C 176.694 0.05 1 243 63 63 PRO CA C 63.075 0.017 1 244 63 63 PRO CB C 31.49 0.05 1 245 64 64 GLU H H 8.697 0.001 1 246 64 64 GLU C C 176.936 0.05 1 247 64 64 GLU CA C 57.071 0.004 1 248 64 64 GLU CB C 30.418 0.01 1 249 64 64 GLU N N 124.021 0.009 1 250 65 65 SER H H 8.553 0.001 1 251 65 65 SER C C 174.506 0.05 1 252 65 65 SER CA C 58.733 0.017 1 253 65 65 SER CB C 63.398 0.012 1 254 65 65 SER N N 118.991 0.006 1 255 66 66 SER H H 8.424 0.001 1 256 66 66 SER C C 173.991 0.05 1 257 66 66 SER CA C 56.878 0.005 1 258 66 66 SER CB C 66.034 0.022 1 259 66 66 SER N N 118.302 0.008 1 260 67 67 GLU H H 8.91 0.001 1 261 67 67 GLU C C 178.176 0.05 1 262 67 67 GLU CA C 59.777 0.005 1 263 67 67 GLU CB C 29.534 0.014 1 264 67 67 GLU N N 120.467 0.007 1 265 68 68 GLN H H 8.138 0.001 1 266 68 68 GLN HE21 H 7.547 0.002 2 267 68 68 GLN HE22 H 6.902 0.001 2 268 68 68 GLN C C 178.08 0.05 1 269 68 68 GLN CA C 59.288 0.044 1 270 68 68 GLN CB C 28.17 0.021 1 271 68 68 GLN CG C 34.262 0.01 1 272 68 68 GLN CD C 180.351 0.05 1 273 68 68 GLN N N 117.988 0.011 1 274 68 68 GLN NE2 N 111.409 0.067 1 275 69 69 GLU H H 7.754 0.001 1 276 69 69 GLU C C 177.369 0.05 1 277 69 69 GLU CA C 59.48 0.009 1 278 69 69 GLU CB C 28.945 0.016 1 279 69 69 GLU N N 122.454 0.013 1 280 70 70 ASP H H 8.476 0.001 1 281 70 70 ASP C C 178.318 0.05 1 282 70 70 ASP CA C 57.931 0.005 1 283 70 70 ASP CB C 39.604 0.025 1 284 70 70 ASP N N 121.035 0.016 1 285 71 71 ASP H H 8.099 0.002 1 286 71 71 ASP C C 178.47 0.05 1 287 71 71 ASP CA C 57.119 0.028 1 288 71 71 ASP CB C 40.999 0.015 1 289 71 71 ASP N N 118.916 0.01 1 290 72 72 MET H H 7.44 0.001 1 291 72 72 MET C C 178.693 0.05 1 292 72 72 MET CA C 56.048 0.043 1 293 72 72 MET CB C 32.506 0.043 1 294 72 72 MET N N 117.595 0.003 1 295 73 73 LEU H H 8.753 0.002 1 296 73 73 LEU C C 177.619 0.05 1 297 73 73 LEU CA C 57.627 0.009 1 298 73 73 LEU CB C 41.077 0.002 1 299 73 73 LEU N N 119.802 0.019 1 300 74 74 ASP H H 7.35 0.002 1 301 74 74 ASP C C 177.138 0.05 1 302 74 74 ASP CA C 57.005 0.045 1 303 74 74 ASP CB C 41.936 0.012 1 304 74 74 ASP N N 114.573 0.01 1 305 75 75 LYS H H 7.598 0.001 1 306 75 75 LYS C C 176.698 0.05 1 307 75 75 LYS CA C 55.176 0.013 1 308 75 75 LYS CB C 32.513 0.016 1 309 75 75 LYS N N 115.372 0.018 1 310 76 76 ALA H H 8.054 0.001 1 311 76 76 ALA C C 176.827 0.05 1 312 76 76 ALA CA C 52.381 0.007 1 313 76 76 ALA CB C 18.156 0.001 1 314 76 76 ALA N N 124.67 0.02 1 315 77 77 TRP H H 8.463 0.003 1 316 77 77 TRP HE1 H 10.095 0.05 1 317 77 77 TRP C C 177.025 0.05 1 318 77 77 TRP CA C 58.246 0.004 1 319 77 77 TRP CB C 29.189 0.009 1 320 77 77 TRP N N 124.163 0.011 1 321 77 77 TRP NE1 N 129.236 0.05 1 322 78 78 GLY H H 8.204 0.001 1 323 78 78 GLY C C 173.754 0.05 1 324 78 78 GLY CA C 46.247 0.024 1 325 78 78 GLY N N 113.45 0.01 1 326 79 79 LEU H H 6.777 0.006 1 327 79 79 LEU C C 175.981 0.05 1 328 79 79 LEU CA C 56.208 0.026 1 329 79 79 LEU CB C 43.115 0.021 1 330 79 79 LEU N N 118.442 0.007 1 331 80 80 GLU H H 9.854 0.001 1 332 80 80 GLU CA C 54.713 0.05 1 333 80 80 GLU CB C 32.291 0.05 1 334 80 80 GLU N N 128.557 0.033 1 335 81 81 PRO C C 178.002 0.05 1 336 81 81 PRO CA C 65.636 0.014 1 337 81 81 PRO CB C 31.358 0.002 1 338 82 82 GLU H H 7.312 0.002 1 339 82 82 GLU C C 175.826 0.05 1 340 82 82 GLU CA C 56.392 0.024 1 341 82 82 GLU CB C 27.437 0.013 1 342 82 82 GLU N N 112.827 0.01 1 343 83 83 SER H H 7.887 0.001 1 344 83 83 SER C C 174.475 0.05 1 345 83 83 SER CA C 62.359 0.02 1 346 83 83 SER CB C 64.422 0.012 1 347 83 83 SER N N 120.056 0.009 1 348 84 84 ARG H H 9.57 0.001 1 349 84 84 ARG C C 176.282 0.05 1 350 84 84 ARG CA C 52.445 0.034 1 351 84 84 ARG CB C 34.537 0.024 1 352 84 84 ARG N N 117.396 0.008 1 353 85 85 LEU H H 9.648 0.003 1 354 85 85 LEU N N 121.814 0.057 1 355 88 88 GLN C C 176.019 0.05 1 356 88 88 GLN CA C 54.183 0.008 1 357 88 88 GLN CB C 32.122 0.05 1 358 89 89 ALA H H 7.081 0.004 1 359 89 89 ALA C C 173.955 0.05 1 360 89 89 ALA CA C 51.977 0.013 1 361 89 89 ALA CB C 19.631 0.01 1 362 89 89 ALA N N 122.735 0.011 1 363 90 90 ARG H H 7.83 0.001 1 364 90 90 ARG CA C 55.473 0.007 1 365 90 90 ARG CB C 31.864 0.002 1 366 90 90 ARG N N 124.683 0.011 1 367 91 91 VAL H H 8.173 0.05 1 368 91 91 VAL C C 177.363 0.05 1 369 91 91 VAL CA C 62.854 0.006 1 370 91 91 VAL CB C 32.356 0.008 1 371 91 91 VAL N N 118.679 0.006 1 372 92 92 THR H H 9.072 0.001 1 373 92 92 THR C C 174.066 0.05 1 374 92 92 THR CA C 60.214 0.025 1 375 92 92 THR CB C 68.499 0.009 1 376 92 92 THR N N 119.639 0.014 1 377 93 93 ASP H H 8.793 0.002 1 378 93 93 ASP C C 175.48 0.05 1 379 93 93 ASP CA C 53.195 0.03 1 380 93 93 ASP CB C 41.898 0.019 1 381 93 93 ASP N N 120.651 0.01 1 382 94 94 GLU H H 7.693 0.001 1 383 94 94 GLU C C 174.768 0.05 1 384 94 94 GLU CA C 55.06 0.003 1 385 94 94 GLU CB C 32.552 0.007 1 386 94 94 GLU N N 120.29 0.01 1 387 95 95 ASP H H 8.404 0.001 1 388 95 95 ASP C C 175.56 0.05 1 389 95 95 ASP CA C 54.721 0.074 1 390 95 95 ASP CB C 41.164 0.05 1 391 95 95 ASP N N 122.712 0.009 1 392 96 96 LEU H H 8.588 0.001 1 393 96 96 LEU C C 178.182 0.05 1 394 96 96 LEU CA C 52.828 0.019 1 395 96 96 LEU CB C 48.004 0.04 1 396 96 96 LEU N N 116.662 0.01 1 397 97 97 VAL H H 8.177 0.001 1 398 97 97 VAL C C 175.15 0.05 1 399 97 97 VAL CA C 62.641 0.008 1 400 97 97 VAL CB C 33.728 0.011 1 401 97 97 VAL N N 122.198 0.011 1 402 98 98 VAL H H 9.678 0.001 1 403 98 98 VAL C C 172.124 0.05 1 404 98 98 VAL CA C 60.413 0.003 1 405 98 98 VAL CB C 36.091 0.002 1 406 98 98 VAL N N 126.161 0.008 1 407 99 99 GLU H H 9.497 0.001 1 408 99 99 GLU C C 174.778 0.05 1 409 99 99 GLU CA C 53.644 0.014 1 410 99 99 GLU CB C 34.218 0.016 1 411 99 99 GLU N N 126.631 0.008 1 412 100 100 ILE H H 9.687 0.001 1 413 100 100 ILE CA C 57.324 0.05 1 414 100 100 ILE CB C 37.404 0.05 1 415 100 100 ILE N N 130.349 0.005 1 416 103 103 TYR CA C 57.292 0.05 1 417 103 103 TYR CB C 38.819 0.05 1 418 104 104 THR H H 7.71 0.004 1 419 104 104 THR CA C 60.816 0.041 1 420 104 104 THR CB C 70.494 0.018 1 421 104 104 THR N N 116.126 0.067 1 422 105 105 ILE H H 7.921 0.001 1 423 105 105 ILE CA C 61.061 0.05 1 424 105 105 ILE CB C 38.993 0.05 1 425 105 105 ILE N N 121.553 0.01 1 426 107 107 HIS CA C 56.746 0.05 1 427 107 107 HIS CB C 30.969 0.05 1 428 108 108 ALA H H 8.122 0.005 1 429 108 108 ALA CA C 52.523 0.008 1 430 108 108 ALA CB C 19.143 0.008 1 431 108 108 ALA N N 124.481 0.01 1 432 109 109 ARG H H 8.178 0.003 1 433 109 109 ARG CA C 56.057 0.013 1 434 109 109 ARG CB C 31.005 0.01 1 435 109 109 ARG N N 119.96 0.029 1 436 110 110 GLU H H 8.39 0.002 1 437 110 110 GLU CA C 56.663 0.056 1 438 110 110 GLU CB C 30.521 0.054 1 439 110 110 GLU N N 122.171 0.021 1 440 111 111 HIS H H 7.871 0.001 1 441 111 111 HIS CA C 57.299 0.05 1 442 111 111 HIS CB C 30.878 0.05 1 443 111 111 HIS N N 124.638 0.014 1 stop_ save_