data_19273 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural characterization of E. coli ISC-type Ferredoxin ; _BMRB_accession_number 19273 _BMRB_flat_file_name bmr19273.str _Entry_type original _Submission_date 2013-05-28 _Accession_date 2013-05-28 _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 Adinolfi Salvatore . . 2 Iannuzi Clara . . 3 Kelly Geoff . . 4 Oregioni Alain . . 5 Martin Stephen . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 81 "13C chemical shifts" 241 "15N chemical shifts" 81 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-02-13 original author . stop_ _Original_release_date 2014-02-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Cluster and fold stability of E. coli ISC-type ferredoxin.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24265733 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yan Robert . . 2 Adinolfi Salvatore . . 3 Iannuzzi Clara . . 4 Kelly Geoff . . 5 Oregioni Alain . . 6 Martin Stephen . . 7 Pastore Annalisa . . stop_ _Journal_abbreviation 'PLoS ONE' _Journal_name_full 'PloS one' _Journal_volume 8 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first e78948 _Page_last e78948 _Year 2013 _Details . loop_ _Keyword Ferredoxin 'Fe-S cluster' Frataxin 'Friedreich's Ataxia' 'NMR assignments' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name holo-Ferredoxin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label holo--Ferredoxin $holo-Ferredoxin '2FE 2S' $entity_FES stop_ _System_molecular_weight 12833.92 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details '[2Fe-2S] cluster containing ferredoxin in oxidised state' save_ ######################## # Monomeric polymers # ######################## save_holo-Ferredoxin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common holo-Ferredoxin _Molecular_mass 12658.1 _Mol_thiol_state 'free and other bound' loop_ _Biological_function ; Ferredoxin are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Although the function of this ferredoxin is unknown it is probable that it has a role as a cellular electron transfer protein. Involved in the in vivo assembly of the Fe-S clusters in a wide variety of iron-sulfur proteins. ; stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 115 _Mol_residue_sequence ; QGAMAPKIVILPHQDLCPDG AVLEANSGETILDAALRNGI EIEHACEKSCACTTCHCIVR EGFDSLPESSEQEDDMLDKA WGLEPESRLSCQARVTDEDL VVEIPRYTINHAREH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 GLN 2 -2 GLY 3 -1 ALA 4 0 MET 5 1 ALA 6 2 PRO 7 3 LYS 8 4 ILE 9 5 VAL 10 6 ILE 11 7 LEU 12 8 PRO 13 9 HIS 14 10 GLN 15 11 ASP 16 12 LEU 17 13 CYS 18 14 PRO 19 15 ASP 20 16 GLY 21 17 ALA 22 18 VAL 23 19 LEU 24 20 GLU 25 21 ALA 26 22 ASN 27 23 SER 28 24 GLY 29 25 GLU 30 26 THR 31 27 ILE 32 28 LEU 33 29 ASP 34 30 ALA 35 31 ALA 36 32 LEU 37 33 ARG 38 34 ASN 39 35 GLY 40 36 ILE 41 37 GLU 42 38 ILE 43 39 GLU 44 40 HIS 45 41 ALA 46 42 CYS 47 43 GLU 48 44 LYS 49 45 SER 50 46 CYS 51 47 ALA 52 48 CYS 53 49 THR 54 50 THR 55 51 CYS 56 52 HIS 57 53 CYS 58 54 ILE 59 55 VAL 60 56 ARG 61 57 GLU 62 58 GLY 63 59 PHE 64 60 ASP 65 61 SER 66 62 LEU 67 63 PRO 68 64 GLU 69 65 SER 70 66 SER 71 67 GLU 72 68 GLN 73 69 GLU 74 70 ASP 75 71 ASP 76 72 MET 77 73 LEU 78 74 ASP 79 75 LYS 80 76 ALA 81 77 TRP 82 78 GLY 83 79 LEU 84 80 GLU 85 81 PRO 86 82 GLU 87 83 SER 88 84 ARG 89 85 LEU 90 86 SER 91 87 CYS 92 88 GLN 93 89 ALA 94 90 ARG 95 91 VAL 96 92 THR 97 93 ASP 98 94 GLU 99 95 ASP 100 96 LEU 101 97 VAL 102 98 VAL 103 99 GLU 104 100 ILE 105 101 PRO 106 102 ARG 107 103 TYR 108 104 THR 109 105 ILE 110 106 ASN 111 107 HIS 112 108 ALA 113 109 ARG 114 110 GLU 115 111 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 18991 ferredoxin 95.65 111 100.00 100.00 2.11e-73 BMRB 18992 ferredoxin 95.65 111 100.00 100.00 2.11e-73 PDB 1I7H "Crystal Sturcuture Of Fdx" 95.65 111 100.00 100.00 2.11e-73 DBJ BAA16415 "[2Fe-2S] ferredoxin [Escherichia coli str. K12 substr. W3110]" 95.65 111 100.00 100.00 2.11e-73 DBJ BAB36814 "[2FE-2S] ferredoxin [Escherichia coli O157:H7 str. Sakai]" 95.65 111 100.00 100.00 2.11e-73 DBJ BAG78335 "ferredoxin [Escherichia coli SE11]" 95.65 111 100.00 100.00 2.11e-73 DBJ BAI26770 "[2Fe-2S] ferredoxin [Escherichia coli O26:H11 str. 11368]" 95.65 111 100.00 100.00 2.11e-73 DBJ BAI31799 "[2Fe-2S] ferredoxin [Escherichia coli O103:H2 str. 12009]" 95.65 111 100.00 100.00 2.11e-73 EMBL CAP76977 "2Fe-2S ferredoxin [Escherichia coli LF82]" 95.65 111 99.09 99.09 1.08e-72 EMBL CAQ32898 "reduced ferredoxin [Escherichia coli BL21(DE3)]" 95.65 111 100.00 100.00 2.11e-73 EMBL CAQ88191 "[2Fe-2S] ferredoxin [Escherichia fergusonii ATCC 35469]" 95.65 111 99.09 99.09 1.08e-72 EMBL CAQ99416 "[2Fe-2S] ferredoxin [Escherichia coli IAI1]" 95.65 111 100.00 100.00 2.11e-73 EMBL CAR03967 "[2Fe-2S] ferredoxin [Escherichia coli S88]" 95.65 111 99.09 99.09 1.08e-72 GB AAA23755 "ferredoxin [Escherichia coli]" 95.65 111 100.00 100.00 2.11e-73 GB AAC75578 "[2Fe-2S] ferredoxin [Escherichia coli str. K-12 substr. MG1655]" 95.65 111 100.00 100.00 2.11e-73 GB AAG57639 "[2FE-2S] ferredoxin, electron carrer protein [Escherichia coli O157:H7 str. EDL933]" 95.65 111 100.00 100.00 2.11e-73 GB AAN44071 "[2FE-2S] ferredoxin, electron carrer protein [Shigella flexneri 2a str. 301]" 95.65 111 100.00 100.00 2.11e-73 GB AAN81500 "Ferredoxin, 2Fe-2S [Escherichia coli CFT073]" 95.65 111 98.18 99.09 2.54e-72 REF NP_311418 "[2FE-2S] ferredoxin [Escherichia coli O157:H7 str. Sakai]" 95.65 111 100.00 100.00 2.11e-73 REF NP_417020 "[2Fe-2S] ferredoxin [Escherichia coli str. K-12 substr. MG1655]" 95.65 111 100.00 100.00 2.11e-73 REF NP_708364 "[2FE-2S] ferredoxin electron carrer protein [Shigella flexneri 2a str. 301]" 95.65 111 100.00 100.00 2.11e-73 REF WP_001124467 "MULTISPECIES: (2Fe-2S) ferredoxin [Escherichia]" 95.65 111 99.09 99.09 1.47e-72 REF WP_001124468 "(2Fe-2S) ferredoxin [Escherichia coli]" 95.65 111 98.18 99.09 3.80e-72 SP P0A9R4 "RecName: Full=2Fe-2S ferredoxin" 95.65 111 100.00 100.00 2.11e-73 SP P0A9R5 "RecName: Full=2Fe-2S ferredoxin" 95.65 111 100.00 100.00 2.11e-73 SP P0A9R6 "RecName: Full=2Fe-2S ferredoxin" 95.65 111 100.00 100.00 2.11e-73 stop_ save_ ############# # Ligands # ############# save_FES _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'FE2/S2 (INORGANIC) CLUSTER' _BMRB_code FES _PDB_code FES _Molecular_mass 175.820 _Mol_charge 0 _Mol_paramagnetic no _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 'not present' _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 $holo-Ferredoxin 'E. coli' 562 Bacteria . Escherichia coli 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 $holo-Ferredoxin 'recombinant technology' . Escherichia coli . pET-24 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 $holo-Ferredoxin 0.5 mM '[U-99% 13C; U-99% 15N]' TRIS 20 mM 'natural abundance' 'sodium chloride' 500 mM 'natural abundance' TCEP 20 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' 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_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_MARS _Saveframe_category software _Name MARS _Version . loop_ _Vendor _Address _Electronic_address 'oung-sang Jung , Markus Zweckstetter' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'Avance 1' _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance3 _Field_strength 700 _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_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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' 500 . mM pH 8 . 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 water C 13 water ppm 4.77 na indirect . . . 0.251449530 water H 1 water ppm 4.77 internal direct . . . 1.000000000 water N 15 water ppm 4.77 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_assignments_fdx _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' '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 holo--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 0 4 MET H H 8.392 . 1 2 0 4 MET C C 175.423 . 1 3 0 4 MET CA C 55.454 . 1 4 0 4 MET CB C 32.864 . 1 5 0 4 MET N N 118.968 . 1 6 1 5 ALA H H 8.213 . 1 7 1 5 ALA C C 174.490 . 1 8 1 5 ALA CA C 50.443 . 1 9 1 5 ALA CB C 18.508 . 1 10 1 5 ALA N N 126.540 . 1 11 3 7 LYS H H 8.600 . 1 12 3 7 LYS C C 176.112 . 1 13 3 7 LYS CA C 54.349 . 1 14 3 7 LYS CB C 34.985 . 1 15 3 7 LYS N N 119.950 . 1 16 4 8 ILE H H 8.882 . 1 17 4 8 ILE C C 174.855 . 1 18 4 8 ILE CA C 60.549 . 1 19 4 8 ILE CB C 41.015 . 1 20 4 8 ILE N N 118.466 . 1 21 5 9 VAL H H 8.780 . 1 22 5 9 VAL C C 174.997 . 1 23 5 9 VAL CA C 61.908 . 1 24 5 9 VAL CB C 33.031 . 1 25 5 9 VAL N N 129.371 . 1 26 6 10 ILE H H 9.292 . 1 27 6 10 ILE C C 177.268 . 1 28 6 10 ILE CA C 58.766 . 1 29 6 10 ILE CB C 37.278 . 1 30 6 10 ILE N N 128.053 . 1 31 7 11 LEU H H 8.500 . 1 32 7 11 LEU C C 174.389 . 1 33 7 11 LEU CA C 54.434 . 1 34 7 11 LEU CB C 39.826 . 1 35 7 11 LEU N N 128.300 . 1 36 11 15 ASP H H 8.439 . 1 37 11 15 ASP C C 177.593 . 1 38 11 15 ASP CA C 55.878 . 1 39 11 15 ASP CB C 43.648 . 1 40 11 15 ASP N N 114.940 . 1 41 12 16 LEU H H 9.233 . 1 42 12 16 LEU C C 178.749 . 1 43 12 16 LEU CA C 56.643 . 1 44 12 16 LEU CB C 44.242 . 1 45 12 16 LEU N N 119.694 . 1 46 13 17 CYS H H 8.446 . 1 47 13 17 CYS C C 174.903 . 1 48 13 17 CYS CA C 55.266 . 1 49 13 17 CYS CB C 25.370 . 1 50 13 17 CYS N N 109.674 . 1 51 15 19 ASP H H 8.701 . 1 52 15 19 ASP C C 177.694 . 1 53 15 19 ASP CA C 53.840 . 1 54 15 19 ASP CB C 42.034 . 1 55 15 19 ASP N N 115.044 . 1 56 16 20 GLY H H 8.013 . 1 57 16 20 GLY C C 171.671 . 1 58 16 20 GLY CA C 44.582 . 1 59 16 20 GLY N N 108.585 . 1 60 17 21 ALA H H 8.623 . 1 61 17 21 ALA C C 175.119 . 1 62 17 21 ALA CA C 52.566 . 1 63 17 21 ALA CB C 23.006 . 1 64 17 21 ALA N N 120.037 . 1 65 18 22 VAL H H 8.453 . 1 66 18 22 VAL C C 174.794 . 1 67 18 22 VAL CA C 62.418 . 1 68 18 22 VAL CB C 33.116 . 1 69 18 22 VAL N N 120.477 . 1 70 19 23 LEU H H 9.404 . 1 71 19 23 LEU C C 175.894 . 1 72 19 23 LEU CA C 52.906 . 1 73 19 23 LEU CB C 43.053 . 1 74 19 23 LEU N N 126.516 . 1 75 20 24 GLU H H 8.495 . 1 76 20 24 GLU C C 175.180 . 1 77 20 24 GLU CA C 56.218 . 1 78 20 24 GLU CB C 30.144 . 1 79 20 24 GLU N N 121.670 . 1 80 21 25 ALA H H 8.591 . 1 81 21 25 ALA C C 174.713 . 1 82 21 25 ALA CA C 50.443 . 1 83 21 25 ALA CB C 21.820 . 1 84 21 25 ALA N N 128.511 . 1 85 22 26 ASN H H 8.642 . 1 86 22 26 ASN C C 175.038 . 1 87 22 26 ASN CA C 51.462 . 1 88 22 26 ASN CB C 40.421 . 1 89 22 26 ASN N N 116.394 . 1 90 23 27 SER H H 8.703 . 1 91 23 27 SER C C 175.078 . 1 92 23 27 SER CA C 60.974 . 1 93 23 27 SER CB C 62.843 . 1 94 23 27 SER N N 116.554 . 1 95 24 28 GLY H H 9.038 . 1 96 24 28 GLY C C 173.598 . 1 97 24 28 GLY CA C 45.432 . 1 98 24 28 GLY N N 116.154 . 1 99 25 29 GLU H H 7.910 . 1 100 25 29 GLU C C 175.524 . 1 101 25 29 GLU CA C 55.029 . 1 102 25 29 GLU CB C 31.672 . 1 103 25 29 GLU N N 122.813 . 1 104 26 30 THR H H 8.648 . 1 105 26 30 THR C C 176.052 . 1 106 26 30 THR CA C 60.804 . 1 107 26 30 THR CB C 70.741 . 1 108 26 30 THR N N 111.581 . 1 109 27 31 ILE H H 8.269 . 1 110 27 31 ILE C C 177.086 . 1 111 27 31 ILE CA C 65.900 . 1 112 27 31 ILE CB C 38.892 . 1 113 27 31 ILE N N 119.186 . 1 114 28 32 LEU H H 7.682 . 1 115 28 32 LEU C C 177.289 . 1 116 28 32 LEU CA C 58.002 . 1 117 28 32 LEU CB C 40.505 . 1 118 28 32 LEU N N 116.052 . 1 119 29 33 ASP H H 8.230 . 1 120 29 33 ASP C C 179.804 . 1 121 29 33 ASP CA C 57.832 . 1 122 29 33 ASP CB C 39.656 . 1 123 29 33 ASP N N 119.395 . 1 124 30 34 ALA H H 7.972 . 1 125 30 34 ALA C C 179.743 . 1 126 30 34 ALA CA C 55.369 . 1 127 30 34 ALA CB C 17.913 . 1 128 30 34 ALA N N 122.592 . 1 129 31 35 ALA H H 8.224 . 1 130 31 35 ALA C C 180.392 . 1 131 31 35 ALA CA C 56.133 . 1 132 31 35 ALA CB C 17.489 . 1 133 31 35 ALA N N 122.254 . 1 134 32 36 LEU H H 9.252 . 1 135 32 36 LEU C C 182.318 . 1 136 32 36 LEU CA C 58.171 . 1 137 32 36 LEU CB C 41.270 . 1 138 32 36 LEU N N 118.715 . 1 139 33 37 ARG H H 7.956 . 1 140 33 37 ARG C C 176.579 . 1 141 33 37 ARG CA C 58.766 . 1 142 33 37 ARG CB C 29.549 . 1 143 33 37 ARG N N 118.665 . 1 144 34 38 ASN H H 7.402 . 1 145 34 38 ASN C C 174.105 . 1 146 34 38 ASN CA C 54.180 . 1 147 34 38 ASN CB C 41.694 . 1 148 34 38 ASN N N 116.480 . 1 149 35 39 GLY H H 7.745 . 1 150 35 39 GLY C C 173.679 . 1 151 35 39 GLY CA C 46.706 . 1 152 35 39 GLY N N 106.647 . 1 153 36 40 ILE H H 8.151 . 1 154 36 40 ILE C C 175.200 . 1 155 36 40 ILE CA C 59.700 . 1 156 36 40 ILE CB C 36.089 . 1 157 36 40 ILE N N 122.848 . 1 158 37 41 GLU H H 8.201 . 1 159 37 41 GLU C C 175.180 . 1 160 37 41 GLU CA C 56.048 . 1 161 37 41 GLU CB C 27.341 . 1 162 37 41 GLU N N 127.588 . 1 163 38 42 ILE H H 7.441 . 1 164 38 42 ILE C C 176.396 . 1 165 38 42 ILE CA C 62.843 . 1 166 38 42 ILE CB C 38.807 . 1 167 38 42 ILE N N 125.117 . 1 168 39 43 GLU H H 9.040 . 1 169 39 43 GLU C C 175.484 . 1 170 39 43 GLU CA C 58.426 . 1 171 39 43 GLU CB C 30.568 . 1 172 39 43 GLU N N 132.420 . 1 173 53 57 CYS H H 9.645 . 1 174 53 57 CYS C C 187.591 . 1 175 53 57 CYS CA C 55.793 . 1 176 53 57 CYS CB C 31.842 . 1 177 53 57 CYS N N 122.619 . 1 178 54 58 ILE H H 9.344 . 1 179 54 58 ILE C C 187.551 . 1 180 54 58 ILE CA C 61.229 . 1 181 54 58 ILE CB C 40.166 . 1 182 54 58 ILE N N 119.605 . 1 183 55 59 VAL H H 8.564 . 1 184 55 59 VAL C C 174.084 . 1 185 55 59 VAL CA C 62.503 . 1 186 55 59 VAL CB C 30.059 . 1 187 55 59 VAL N N 129.714 . 1 188 56 60 ARG H H 7.940 . 1 189 56 60 ARG C C 177.451 . 1 190 56 60 ARG CA C 57.832 . 1 191 56 60 ARG CB C 30.229 . 1 192 56 60 ARG N N 126.140 . 1 193 57 61 GLU H H 7.951 . 1 194 57 61 GLU C C 176.356 . 1 195 57 61 GLU CA C 57.577 . 1 196 57 61 GLU CB C 32.862 . 1 197 57 61 GLU N N 116.202 . 1 198 58 62 GLY H H 8.827 . 1 199 58 62 GLY C C 177.066 . 1 200 58 62 GLY CA C 45.092 . 1 201 58 62 GLY N N 109.524 . 1 202 59 63 PHE H H 9.175 . 1 203 59 63 PHE C C 177.410 . 1 204 59 63 PHE CA C 62.843 . 1 205 59 63 PHE CB C 39.826 . 1 206 59 63 PHE N N 125.787 . 1 207 60 64 ASP H H 8.942 . 1 208 60 64 ASP C C 176.254 . 1 209 60 64 ASP CA C 56.218 . 1 210 60 64 ASP CB C 40.166 . 1 211 60 64 ASP N N 115.934 . 1 212 61 65 SER H H 7.922 . 1 213 61 65 SER C C 174.936 . 1 214 61 65 SER CA C 59.530 . 1 215 61 65 SER CB C 64.626 . 1 216 61 65 SER N N 115.179 . 1 217 62 66 LEU H H 7.230 . 1 218 62 66 LEU C C 175.159 . 1 219 62 66 LEU CA C 52.566 . 1 220 62 66 LEU CB C 40.675 . 1 221 62 66 LEU N N 125.082 . 1 222 63 67 PRO C C 176.944 . 1 223 63 67 PRO CA C 63.097 . 1 224 63 67 PRO CB C 31.418 . 1 225 64 68 GLU H H 8.695 . 1 226 64 68 GLU C C 177.228 . 1 227 64 68 GLU CA C 57.237 . 1 228 64 68 GLU CB C 30.398 . 1 229 64 68 GLU N N 124.269 . 1 230 65 69 SER H H 8.586 . 1 231 65 69 SER C C 174.977 . 1 232 65 69 SER CA C 58.936 . 1 233 65 69 SER CB C 63.607 . 1 234 65 69 SER N N 119.340 . 1 235 66 70 SER H H 8.479 . 1 236 66 70 SER C C 174.267 . 1 237 66 70 SER CA C 57.152 . 1 238 66 70 SER CB C 66.070 . 1 239 66 70 SER N N 118.625 . 1 240 67 71 GLU H H 8.916 . 1 241 67 71 GLU C C 178.485 . 1 242 67 71 GLU CA C 59.700 . 1 243 67 71 GLU CB C 29.464 . 1 244 67 71 GLU N N 120.717 . 1 245 68 72 GLN H H 8.163 . 1 246 68 72 GLN C C 178.364 . 1 247 68 72 GLN CA C 59.360 . 1 248 68 72 GLN CB C 28.105 . 1 249 68 72 GLN N N 118.136 . 1 250 69 73 GLU H H 7.781 . 1 251 69 73 GLU C C 177.694 . 1 252 69 73 GLU CA C 59.530 . 1 253 69 73 GLU CB C 28.700 . 1 254 69 73 GLU N N 122.580 . 1 255 70 74 ASP H H 8.480 . 1 256 70 74 ASP C C 178.769 . 1 257 70 74 ASP CA C 58.002 . 1 258 70 74 ASP CB C 39.826 . 1 259 70 74 ASP N N 121.204 . 1 260 71 75 ASP H H 8.140 . 1 261 71 75 ASP C C 178.891 . 1 262 71 75 ASP CA C 57.322 . 1 263 71 75 ASP CB C 41.100 . 1 264 71 75 ASP N N 119.184 . 1 265 72 76 MET H H 7.485 . 1 266 72 76 MET C C 179.013 . 1 267 72 76 MET CA C 56.218 . 1 268 72 76 MET CB C 32.267 . 1 269 72 76 MET N N 117.937 . 1 270 73 77 LEU H H 8.774 . 1 271 73 77 LEU C C 177.958 . 1 272 73 77 LEU CA C 57.747 . 1 273 73 77 LEU CB C 41.100 . 1 274 73 77 LEU N N 119.926 . 1 275 74 78 ASP H H 7.358 . 1 276 74 78 ASP C C 177.532 . 1 277 74 78 ASP CA C 57.237 . 1 278 74 78 ASP CB C 42.119 . 1 279 74 78 ASP N N 114.756 . 1 280 75 79 LYS H H 7.629 . 1 281 75 79 LYS C C 176.903 . 1 282 75 79 LYS CA C 55.284 . 1 283 75 79 LYS CB C 32.522 . 1 284 75 79 LYS N N 115.640 . 1 285 76 80 ALA H H 8.059 . 1 286 76 80 ALA C C 177.127 . 1 287 76 80 ALA CA C 52.566 . 1 288 76 80 ALA CB C 18.083 . 1 289 76 80 ALA N N 124.747 . 1 290 77 81 TRP H H 8.484 . 1 291 77 81 TRP HE1 H 10.112 . 3 292 77 81 TRP C C 177.329 . 1 293 77 81 TRP CA C 58.256 . 1 294 77 81 TRP CB C 29.125 . 1 295 77 81 TRP N N 124.359 . 1 296 77 81 TRP NE1 N 129.453 . 1 297 78 82 GLY H H 8.222 . 1 298 78 82 GLY C C 174.064 . 1 299 78 82 GLY CA C 46.366 . 1 300 78 82 GLY N N 113.596 . 1 301 79 83 LEU H H 6.798 . 1 302 79 83 LEU C C 176.275 . 1 303 79 83 LEU CA C 56.218 . 1 304 79 83 LEU CB C 43.053 . 1 305 79 83 LEU N N 118.596 . 1 306 80 84 GLU H H 9.870 . 1 307 80 84 GLU C C 175.808 . 1 308 80 84 GLU CA C 54.859 . 1 309 80 84 GLU CB C 32.267 . 1 310 80 84 GLU N N 128.778 . 1 311 81 85 PRO C C 178.283 . 1 312 81 85 PRO CA C 65.730 . 1 313 81 85 PRO CB C 31.163 . 1 314 82 86 GLU H H 7.350 . 1 315 82 86 GLU C C 176.133 . 1 316 82 86 GLU CA C 56.388 . 1 317 82 86 GLU CB C 27.341 . 1 318 82 86 GLU N N 113.106 . 1 319 83 87 SER H H 7.909 . 1 320 83 87 SER C C 176.133 . 1 321 83 87 SER CA C 62.503 . 1 322 83 87 SER CB C 64.456 . 1 323 83 87 SER N N 120.207 . 1 324 89 93 ALA H H 7.113 . 1 325 89 93 ALA C C 174.348 . 1 326 89 93 ALA CA C 52.056 . 1 327 89 93 ALA CB C 19.612 . 1 328 89 93 ALA N N 122.960 . 1 329 90 94 ARG H H 7.761 . 1 330 90 94 ARG C C 173.293 . 1 331 90 94 ARG CA C 55.623 . 1 332 90 94 ARG CB C 31.842 . 1 333 90 94 ARG N N 124.452 . 1 334 91 95 VAL H H 8.114 . 1 335 91 95 VAL C C 177.593 . 1 336 91 95 VAL CA C 62.843 . 1 337 91 95 VAL CB C 32.607 . 1 338 91 95 VAL N N 118.964 . 1 339 92 96 THR H H 9.131 . 1 340 92 96 THR C C 174.571 . 1 341 92 96 THR CA C 60.465 . 1 342 92 96 THR CB C 68.958 . 1 343 92 96 THR N N 119.308 . 1 344 93 97 ASP H H 8.950 . 1 345 93 97 ASP C C 175.403 . 1 346 93 97 ASP CA C 53.075 . 1 347 93 97 ASP CB C 41.864 . 1 348 93 97 ASP N N 121.170 . 1 349 94 98 GLU H H 7.798 . 1 350 94 98 GLU C C 174.794 . 1 351 94 98 GLU CA C 55.114 . 1 352 94 98 GLU CB C 33.201 . 1 353 94 98 GLU N N 119.795 . 1 354 95 99 ASP H H 8.272 . 1 355 95 99 ASP C C 176.133 . 1 356 95 99 ASP CA C 54.774 . 1 357 95 99 ASP CB C 41.185 . 1 358 95 99 ASP N N 122.327 . 1 359 96 100 LEU H H 8.639 . 1 360 96 100 LEU C C 178.384 . 1 361 96 100 LEU CA C 52.906 . 1 362 96 100 LEU CB C 47.979 . 1 363 96 100 LEU N N 116.770 . 1 364 97 101 VAL H H 8.206 . 1 365 97 101 VAL C C 175.524 . 1 366 97 101 VAL CA C 62.673 . 1 367 97 101 VAL CB C 33.541 . 1 368 97 101 VAL N N 122.292 . 1 369 98 102 VAL H H 9.703 . 1 370 98 102 VAL C C 172.462 . 1 371 98 102 VAL CA C 60.634 . 1 372 98 102 VAL CB C 35.919 . 1 373 98 102 VAL N N 126.408 . 1 374 99 103 GLU H H 9.515 . 1 375 99 103 GLU C C 175.078 . 1 376 99 103 GLU CA C 53.755 . 1 377 99 103 GLU CB C 34.136 . 1 378 99 103 GLU N N 126.881 . 1 379 100 104 ILE H H 9.703 . 1 380 100 104 ILE C C 174.024 . 1 381 100 104 ILE CA C 57.577 . 1 382 100 104 ILE CB C 37.448 . 1 383 100 104 ILE N N 130.573 . 1 384 108 112 ALA H H 8.132 . 1 385 108 112 ALA C C 177.532 . 1 386 108 112 ALA CA C 52.821 . 1 387 108 112 ALA CB C 19.018 . 1 388 108 112 ALA N N 124.623 . 1 389 109 113 ARG H H 8.181 . 1 390 109 113 ARG C C 176.214 . 1 391 109 113 ARG CA C 56.218 . 1 392 109 113 ARG CB C 30.908 . 1 393 109 113 ARG N N 120.095 . 1 394 110 114 GLU H H 8.386 . 1 395 110 114 GLU C C 175.443 . 1 396 110 114 GLU CA C 56.643 . 1 397 110 114 GLU CB C 30.483 . 1 398 110 114 GLU N N 122.307 . 1 399 111 115 HIS H H 7.902 . 1 400 111 115 HIS C C 179.641 . 1 401 111 115 HIS CA C 57.577 . 1 402 111 115 HIS CB C 30.823 . 1 403 111 115 HIS N N 124.902 . 1 stop_ save_