data_17837 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The assigned chemical shifts for the structured forms of apo-IscU ; _BMRB_accession_number 17837 _BMRB_flat_file_name bmr17837.str _Entry_type original _Submission_date 2011-08-07 _Accession_date 2011-08-07 _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 Tonelli Marco . . 3 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" 94 "13C chemical shifts" 69 "15N chemical shifts" 91 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-02-28 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 17836 IscU 17844 IscU:IscS stop_ _Original_release_date 2012-02-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22203963 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kim 'Jin Hae' . . 2 Tonelli Marco . . 3 Markley John L. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U. S. A.' _Journal_volume 109 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 454 _Page_last 459 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name IscU _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label IscU $IscU stop_ _System_molecular_weight 13716 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_IscU _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common IscU _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'Iron-sulfur cluster scaffolding protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 128 _Mol_residue_sequence ; MAYSEKVIDHYENPRNVGSF DNNDENVGSGMVGAPACGDV MKLQIKVNDEGIIEDARFKT YGCGSAIASSSLVTEWVKGK SLDEAQAIKNTDIAEELELP PVKIHCSILAEDAIKAAIAD YKSKREAK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ALA 3 3 TYR 4 4 SER 5 5 GLU 6 6 LYS 7 7 VAL 8 8 ILE 9 9 ASP 10 10 HIS 11 11 TYR 12 12 GLU 13 13 ASN 14 14 PRO 15 15 ARG 16 16 ASN 17 17 VAL 18 18 GLY 19 19 SER 20 20 PHE 21 21 ASP 22 22 ASN 23 23 ASN 24 24 ASP 25 25 GLU 26 26 ASN 27 27 VAL 28 28 GLY 29 29 SER 30 30 GLY 31 31 MET 32 32 VAL 33 33 GLY 34 34 ALA 35 35 PRO 36 36 ALA 37 37 CYS 38 38 GLY 39 39 ASP 40 40 VAL 41 41 MET 42 42 LYS 43 43 LEU 44 44 GLN 45 45 ILE 46 46 LYS 47 47 VAL 48 48 ASN 49 49 ASP 50 50 GLU 51 51 GLY 52 52 ILE 53 53 ILE 54 54 GLU 55 55 ASP 56 56 ALA 57 57 ARG 58 58 PHE 59 59 LYS 60 60 THR 61 61 TYR 62 62 GLY 63 63 CYS 64 64 GLY 65 65 SER 66 66 ALA 67 67 ILE 68 68 ALA 69 69 SER 70 70 SER 71 71 SER 72 72 LEU 73 73 VAL 74 74 THR 75 75 GLU 76 76 TRP 77 77 VAL 78 78 LYS 79 79 GLY 80 80 LYS 81 81 SER 82 82 LEU 83 83 ASP 84 84 GLU 85 85 ALA 86 86 GLN 87 87 ALA 88 88 ILE 89 89 LYS 90 90 ASN 91 91 THR 92 92 ASP 93 93 ILE 94 94 ALA 95 95 GLU 96 96 GLU 97 97 LEU 98 98 GLU 99 99 LEU 100 100 PRO 101 101 PRO 102 102 VAL 103 103 LYS 104 104 ILE 105 105 HIS 106 106 CYS 107 107 SER 108 108 ILE 109 109 LEU 110 110 ALA 111 111 GLU 112 112 ASP 113 113 ALA 114 114 ILE 115 115 LYS 116 116 ALA 117 117 ALA 118 118 ILE 119 119 ALA 120 120 ASP 121 121 TYR 122 122 LYS 123 123 SER 124 124 LYS 125 125 ARG 126 126 GLU 127 127 ALA 128 128 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-15 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 15967 IscU(D39A) 100.00 128 99.22 99.22 5.74e-86 BMRB 16245 IscU 100.00 130 100.00 100.00 4.22e-87 BMRB 16603 IscU 100.00 128 99.22 99.22 5.74e-86 BMRB 17282 IscU 100.00 128 100.00 100.00 4.36e-87 BMRB 17836 IscU 100.00 128 100.00 100.00 4.36e-87 BMRB 17844 IscU 100.00 128 100.00 100.00 4.36e-87 BMRB 18359 IscU(D39V) 100.00 128 99.22 99.22 8.98e-86 BMRB 18360 IscU(E111A) 100.00 128 99.22 99.22 3.22e-86 BMRB 18361 IscU(N90A) 100.00 128 99.22 99.22 4.82e-86 BMRB 18362 IscU(S107A) 100.00 128 99.22 100.00 1.51e-86 BMRB 18381 IscU 100.00 128 100.00 100.00 4.36e-87 BMRB 18750 IscU 100.00 128 100.00 100.00 4.36e-87 BMRB 18754 IscU 100.00 128 100.00 100.00 4.36e-87 PDB 2KQK "Solution Structure Of Apo-Iscu(D39a)" 100.00 128 99.22 99.22 5.74e-86 PDB 2L4X "Solution Structure Of Apo-Iscu(Wt)" 100.00 128 100.00 100.00 4.36e-87 PDB 3LVL "Crystal Structure Of E.Coli Iscs-Iscu Complex" 99.22 129 100.00 100.00 4.87e-86 DBJ BAA16423 "scaffold protein [Escherichia coli str. K12 substr. W3110]" 100.00 128 100.00 100.00 4.36e-87 DBJ BAB36818 "NifU-like protein [Escherichia coli O157:H7 str. Sakai]" 100.00 128 100.00 100.00 4.36e-87 DBJ BAG78339 "conserved hypothetical protein [Escherichia coli SE11]" 100.00 128 100.00 100.00 4.36e-87 DBJ BAH64655 "hypothetical protein KP1_4113 [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" 100.00 128 97.66 100.00 4.93e-85 DBJ BAI26774 "scaffold protein IscU [Escherichia coli O26:H11 str. 11368]" 100.00 128 100.00 100.00 4.36e-87 EMBL CAD02745 "NifU-like protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 128 98.44 100.00 8.14e-86 EMBL CAP76981 "NifU-like protein [Escherichia coli LF82]" 100.00 128 99.22 99.22 2.64e-86 EMBL CAQ32902 "scaffold protein involved in iron-sulfur cluster assembly [Escherichia coli BL21(DE3)]" 100.00 128 100.00 100.00 4.36e-87 EMBL CAQ88187 "scaffold protein [Escherichia fergusonii ATCC 35469]" 100.00 128 100.00 100.00 4.36e-87 EMBL CAQ99420 "scaffold protein [Escherichia coli IAI1]" 100.00 128 100.00 100.00 4.36e-87 GB AAC75582 "iron-sulfur cluster assembly scaffold protein [Escherichia coli str. K-12 substr. MG1655]" 100.00 128 100.00 100.00 4.36e-87 GB AAG57643 "orf, hypothetical protein [Escherichia coli O157:H7 str. EDL933]" 100.00 128 100.00 100.00 4.36e-87 GB AAL21436 "NifU homolog [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 128 98.44 100.00 8.14e-86 GB AAN44075 "conserved hypothetical protein [Shigella flexneri 2a str. 301]" 100.00 128 100.00 100.00 4.36e-87 GB AAN81505 "NifU-like protein [Escherichia coli CFT073]" 100.00 128 100.00 100.00 4.36e-87 PIR AE0824 "NifU-like protein [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 128 98.44 100.00 8.14e-86 REF NP_311422 "scaffold protein [Escherichia coli O157:H7 str. Sakai]" 100.00 128 100.00 100.00 4.36e-87 REF NP_417024 "iron-sulfur cluster assembly scaffold protein [Escherichia coli str. K-12 substr. MG1655]" 100.00 128 100.00 100.00 4.36e-87 REF NP_457073 "NifU-like protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 128 98.44 100.00 8.14e-86 REF NP_461477 "iron-sulfur cluster assembly scaffold protein [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 128 98.44 100.00 8.14e-86 REF NP_708368 "scaffold protein [Shigella flexneri 2a str. 301]" 100.00 128 100.00 100.00 4.36e-87 SP P0ACD4 "RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU; AltName: Full=Sulfur acceptor protein IscU" 100.00 128 100.00 100.00 4.36e-87 SP P0ACD5 "RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU; AltName: Full=Sulfur acceptor protein IscU" 100.00 128 100.00 100.00 4.36e-87 SP P0ACD6 "RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU; AltName: Full=Sulfur acceptor protein IscU" 100.00 128 100.00 100.00 4.36e-87 SP P0ACD7 "RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU; AltName: Full=Sulfur acceptor protein IscU" 100.00 128 100.00 100.00 4.36e-87 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 _Gene_mnemonic $IscU 'E. coli' 562 Bacteria . Escherichia coli BL21 iscu 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 $IscU 'recombinant technology' . Escherichia coli BL21 pTrc99a 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 $IscU 1.5 mM '[U-13C; U-15N]' TRIS 50 mM 'natural abundance' DTT 5 mM 'natural abundance' DSS 0.7 mM 'natural abundance' EDTA 0.5 mM 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ 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_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection 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_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _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_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_C(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _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' . . 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 CBCA(CO)NH' '3D HNCACB' '3D C(CO)NH' '3D HNCO' '3D HBHA(CO)NH' 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 IscU _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 15 15 ARG H H 9.308 0.030 1 2 15 15 ARG N N 123.347 0.300 1 3 16 16 ASN H H 8.259 0.030 1 4 16 16 ASN N N 109.230 0.300 1 5 18 18 GLY H H 8.555 0.030 1 6 18 18 GLY N N 115.038 0.300 1 7 19 19 SER H H 8.022 0.030 1 8 19 19 SER CA C 56.930 0.300 1 9 19 19 SER CB C 66.014 0.300 1 10 19 19 SER N N 112.032 0.300 1 11 20 20 PHE H H 8.778 0.030 1 12 20 20 PHE C C 175.698 0.300 1 13 20 20 PHE CA C 55.475 0.300 1 14 20 20 PHE CB C 41.899 0.300 1 15 20 20 PHE N N 120.566 0.300 1 16 21 21 ASP H H 8.885 0.030 1 17 21 21 ASP N N 122.880 0.300 1 18 22 22 ASN H H 8.485 0.030 1 19 22 22 ASN CA C 54.963 0.300 1 20 22 22 ASN CB C 41.501 0.300 1 21 22 22 ASN N N 122.118 0.300 1 22 24 24 ASP H H 7.510 0.030 1 23 24 24 ASP N N 122.185 0.300 1 24 25 25 GLU H H 9.015 0.030 1 25 25 25 GLU N N 125.006 0.300 1 26 26 26 ASN H H 8.699 0.030 1 27 26 26 ASN N N 115.852 0.300 1 28 27 27 VAL H H 7.327 0.030 1 29 27 27 VAL N N 118.843 0.300 1 30 28 28 GLY H H 8.804 0.030 1 31 28 28 GLY N N 112.418 0.300 1 32 29 29 SER H H 10.402 0.030 1 33 29 29 SER CA C 57.644 0.300 1 34 29 29 SER CB C 64.837 0.300 1 35 29 29 SER N N 120.916 0.300 1 36 30 30 GLY H H 9.502 0.030 1 37 30 30 GLY N N 112.775 0.300 1 38 31 31 MET H H 8.689 0.030 1 39 31 31 MET N N 125.417 0.300 1 40 32 32 VAL H H 8.874 0.030 1 41 32 32 VAL N N 120.212 0.300 1 42 33 33 GLY H H 8.375 0.030 1 43 33 33 GLY N N 108.623 0.300 1 44 34 34 ALA H H 8.393 0.030 1 45 34 34 ALA N N 123.601 0.300 1 46 35 35 PRO C C 177.963 0.300 1 47 35 35 PRO CA C 64.697 0.300 1 48 35 35 PRO CB C 31.758 0.300 1 49 36 36 ALA H H 8.421 0.030 1 50 36 36 ALA CA C 53.836 0.300 1 51 36 36 ALA CB C 18.488 0.300 1 52 36 36 ALA N N 118.723 0.300 1 53 37 37 CYS H H 7.612 0.030 1 54 37 37 CYS CA C 58.074 0.300 1 55 37 37 CYS CB C 29.172 0.300 1 56 37 37 CYS N N 112.779 0.300 1 57 38 38 GLY H H 8.092 0.030 1 58 38 38 GLY CA C 45.708 0.300 1 59 38 38 GLY N N 109.425 0.300 1 60 41 41 MET H H 8.866 0.030 1 61 41 41 MET N N 126.505 0.300 1 62 43 43 LEU H H 8.971 0.030 1 63 43 43 LEU N N 126.606 0.300 1 64 44 44 GLN H H 9.359 0.030 1 65 44 44 GLN N N 120.574 0.300 1 66 45 45 ILE H H 9.226 0.030 1 67 45 45 ILE N N 113.049 0.300 1 68 46 46 LYS H H 8.285 0.030 1 69 46 46 LYS N N 123.792 0.300 1 70 47 47 VAL H H 8.502 0.030 1 71 47 47 VAL N N 128.517 0.300 1 72 48 48 ASN H H 8.917 0.030 1 73 48 48 ASN N N 126.343 0.300 1 74 49 49 ASP H H 8.394 0.030 1 75 49 49 ASP N N 116.903 0.300 1 76 50 50 GLU H H 7.803 0.030 1 77 50 50 GLU CA C 56.016 0.300 1 78 50 50 GLU CB C 29.951 0.300 1 79 50 50 GLU CG C 36.833 0.300 1 80 50 50 GLU N N 117.824 0.300 1 81 51 51 GLY H H 8.053 0.030 1 82 51 51 GLY CA C 45.710 0.300 1 83 51 51 GLY N N 107.788 0.300 1 84 52 52 ILE H H 7.517 0.030 1 85 52 52 ILE CA C 57.786 0.300 1 86 52 52 ILE CB C 37.723 0.300 1 87 52 52 ILE N N 119.922 0.300 1 88 53 53 ILE H H 8.705 0.030 1 89 53 53 ILE N N 127.101 0.300 1 90 54 54 GLU H H 8.903 0.030 1 91 54 54 GLU N N 130.296 0.300 1 92 55 55 ASP H H 8.015 0.030 1 93 55 55 ASP N N 115.918 0.300 1 94 56 56 ALA H H 8.941 0.030 1 95 56 56 ALA N N 123.762 0.300 1 96 57 57 ARG H H 8.826 0.030 1 97 57 57 ARG N N 117.760 0.300 1 98 58 58 PHE H H 8.481 0.030 1 99 58 58 PHE N N 116.790 0.300 1 100 59 59 LYS H H 8.732 0.030 1 101 59 59 LYS N N 119.999 0.300 1 102 73 73 VAL H H 7.566 0.030 1 103 73 73 VAL N N 113.718 0.300 1 104 74 74 THR H H 7.766 0.030 1 105 74 74 THR N N 109.670 0.300 1 106 75 75 GLU H H 7.259 0.030 1 107 75 75 GLU N N 117.541 0.300 1 108 76 76 TRP H H 8.638 0.030 1 109 76 76 TRP N N 120.102 0.300 1 110 77 77 VAL H H 8.092 0.030 1 111 77 77 VAL N N 107.825 0.300 1 112 78 78 LYS H H 6.685 0.030 1 113 78 78 LYS N N 118.042 0.300 1 114 79 79 GLY H H 9.423 0.030 1 115 79 79 GLY N N 112.501 0.300 1 116 80 80 LYS H H 7.887 0.030 1 117 80 80 LYS N N 120.231 0.300 1 118 81 81 SER H H 8.982 0.030 1 119 81 81 SER N N 116.217 0.300 1 120 82 82 LEU H H 8.012 0.030 1 121 82 82 LEU N N 118.521 0.300 1 122 83 83 ASP H H 8.112 0.030 1 123 83 83 ASP N N 116.064 0.300 1 124 84 84 GLU H H 7.793 0.030 1 125 84 84 GLU N N 120.789 0.300 1 126 85 85 ALA H H 8.670 0.030 1 127 85 85 ALA N N 122.605 0.300 1 128 86 86 GLN H H 7.841 0.030 1 129 86 86 GLN CA C 57.514 0.300 1 130 86 86 GLN CB C 28.719 0.300 1 131 86 86 GLN CG C 34.323 0.300 1 132 86 86 GLN N N 115.297 0.300 1 133 87 87 ALA H H 7.095 0.030 1 134 87 87 ALA C C 177.711 0.300 1 135 87 87 ALA CA C 51.819 0.300 1 136 87 87 ALA CB C 18.877 0.300 1 137 87 87 ALA N N 117.938 0.300 1 138 88 88 ILE H H 7.096 0.030 1 139 88 88 ILE CA C 62.858 0.300 1 140 88 88 ILE CB C 37.742 0.300 1 141 88 88 ILE N N 120.667 0.300 1 142 89 89 LYS H H 8.399 0.030 1 143 89 89 LYS CA C 53.973 0.300 1 144 89 89 LYS CB C 35.706 0.300 1 145 89 89 LYS N N 125.098 0.300 1 146 90 90 ASN H H 9.397 0.030 1 147 90 90 ASN N N 121.356 0.300 1 148 91 91 THR H H 7.164 0.030 1 149 91 91 THR CA C 64.622 0.300 1 150 91 91 THR CB C 67.450 0.300 1 151 91 91 THR N N 109.907 0.300 1 152 92 92 ASP H H 7.085 0.030 1 153 92 92 ASP C C 178.752 0.300 1 154 92 92 ASP CA C 57.503 0.300 1 155 92 92 ASP N N 121.928 0.300 1 156 93 93 ILE H H 7.111 0.030 1 157 93 93 ILE CA C 64.389 0.300 1 158 93 93 ILE N N 120.541 0.300 1 159 94 94 ALA H H 8.188 0.030 1 160 94 94 ALA N N 118.602 0.300 1 161 95 95 GLU H H 8.012 0.030 1 162 95 95 GLU N N 116.370 0.300 1 163 96 96 GLU H H 7.711 0.030 1 164 96 96 GLU N N 120.521 0.300 1 165 97 97 LEU H H 7.278 0.030 1 166 97 97 LEU N N 112.621 0.300 1 167 98 98 GLU HA H 4.210 0.030 1 168 98 98 GLU C C 174.486 0.300 1 169 98 98 GLU CA C 56.318 0.300 1 170 98 98 GLU CB C 30.344 0.300 1 171 99 99 LEU H H 7.902 0.030 1 172 99 99 LEU CA C 51.964 0.300 1 173 99 99 LEU N N 122.822 0.300 1 174 102 102 VAL H H 7.568 0.030 1 175 102 102 VAL N N 110.118 0.300 1 176 103 103 LYS H H 8.104 0.030 1 177 103 103 LYS N N 116.493 0.300 1 178 104 104 ILE H H 7.591 0.030 1 179 104 104 ILE N N 122.907 0.300 1 180 105 105 HIS C C 177.041 0.300 1 181 105 105 HIS CA C 59.776 0.300 1 182 106 106 CYS H H 7.484 0.030 1 183 106 106 CYS CB C 26.764 0.300 1 184 106 106 CYS N N 120.067 0.300 1 185 107 107 SER H H 7.472 0.030 1 186 107 107 SER N N 113.653 0.300 1 187 108 108 ILE H H 6.719 0.030 1 188 108 108 ILE N N 126.554 0.300 1 189 109 109 LEU H H 7.991 0.030 1 190 109 109 LEU N N 119.295 0.300 1 191 110 110 ALA H H 7.075 0.030 1 192 110 110 ALA N N 117.451 0.300 1 193 111 111 GLU H H 7.353 0.030 1 194 111 111 GLU N N 118.025 0.300 1 195 112 112 ASP H H 8.756 0.030 1 196 112 112 ASP CA C 57.332 0.300 1 197 112 112 ASP CB C 39.767 0.300 1 198 112 112 ASP N N 119.393 0.300 1 199 113 113 ALA H H 8.955 0.030 1 200 113 113 ALA CA C 55.801 0.300 1 201 113 113 ALA CB C 18.120 0.300 1 202 113 113 ALA N N 124.614 0.300 1 203 114 114 ILE H H 7.853 0.030 1 204 114 114 ILE N N 118.134 0.300 1 205 115 115 LYS H H 7.968 0.030 1 206 115 115 LYS CA C 61.071 0.300 1 207 115 115 LYS N N 119.562 0.300 1 208 116 116 ALA H H 8.535 0.030 1 209 116 116 ALA CA C 54.836 0.300 1 210 116 116 ALA CB C 17.966 0.300 1 211 116 116 ALA N N 122.721 0.300 1 212 117 117 ALA H H 8.415 0.030 1 213 117 117 ALA CA C 55.436 0.300 1 214 117 117 ALA CB C 17.918 0.300 1 215 117 117 ALA N N 124.589 0.300 1 216 118 118 ILE H H 8.235 0.030 1 217 118 118 ILE C C 177.403 0.300 1 218 118 118 ILE CA C 66.289 0.300 1 219 118 118 ILE N N 118.709 0.300 1 220 119 119 ALA H H 8.105 0.030 1 221 119 119 ALA CA C 55.300 0.300 1 222 119 119 ALA CB C 17.840 0.300 1 223 119 119 ALA N N 121.507 0.300 1 224 120 120 ASP H H 8.257 0.030 1 225 120 120 ASP N N 119.721 0.300 1 226 121 121 TYR H H 8.209 0.030 1 227 121 121 TYR N N 119.478 0.300 1 228 122 122 LYS H H 8.675 0.030 1 229 122 122 LYS C C 179.464 0.300 1 230 122 122 LYS CA C 60.449 0.300 1 231 122 122 LYS CB C 32.426 0.300 1 232 122 122 LYS N N 117.570 0.300 1 233 123 123 SER H H 8.200 0.030 1 234 123 123 SER CA C 61.272 0.300 1 235 123 123 SER CB C 62.943 0.300 1 236 123 123 SER N N 114.978 0.300 1 237 124 124 LYS H H 7.508 0.030 1 238 124 124 LYS N N 121.360 0.300 1 239 125 125 ARG H H 7.427 0.030 1 240 125 125 ARG CB C 29.973 0.300 1 241 125 125 ARG N N 117.566 0.300 1 242 126 126 GLU H H 7.718 0.030 1 243 126 126 GLU N N 119.611 0.300 1 244 127 127 ALA H H 7.959 0.030 1 245 127 127 ALA HA H 4.315 0.030 1 246 127 127 ALA HB H 1.387 0.030 1 247 127 127 ALA C C 176.640 0.300 1 248 127 127 ALA CA C 52.497 0.300 1 249 127 127 ALA CB C 18.974 0.300 1 250 127 127 ALA N N 124.753 0.300 1 251 128 128 LYS H H 7.760 0.030 1 252 128 128 LYS CA C 57.565 0.300 1 253 128 128 LYS CB C 33.717 0.300 1 254 128 128 LYS N N 126.161 0.300 1 stop_ save_