data_17009 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence specific backbone assignment of the C-terminal domain of MqsA ; _BMRB_accession_number 17009 _BMRB_flat_file_name bmr17009.str _Entry_type original _Submission_date 2010-06-19 _Accession_date 2010-06-19 _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 Brown Breann L. . 2 Grigoriu Simina . . 3 Arruda Jennifer . . 4 Page Rebecca . . 5 Peti Wolfgang . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 65 "13C chemical shifts" 288 "15N chemical shifts" 65 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-01-18 update BMRB 'update entry citation' 2010-12-03 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure of the Escherichia coli Antitoxin MqsA (YgiT/b3021) Bound to Its Gene Promoter Reveals Extensive Domain Rearrangements and the Specificity of Transcriptional Regulation.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Brown Breann L. . 2 Wood Thomas K. . 3 Peti Wolfgang . . 4 Page Rebecca . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 286 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2285 _Page_last 2296 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name mqsa_cterm _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'mqsa cterm' $mqsa_c stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_mqsa_c _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common mqsa_c _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 73 _Mol_residue_sequence ; GHMASVNAETVAPEFIVKVR KKLSLTQKEASEIFGGGVNA FSRYEKGNAQPHPSTIKLLR VLDKHPELLNEIR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 59 GLY 2 60 HIS 3 61 MET 4 62 ALA 5 63 SER 6 64 VAL 7 65 ASN 8 66 ALA 9 67 GLU 10 68 THR 11 69 VAL 12 70 ALA 13 71 PRO 14 72 GLU 15 73 PHE 16 74 ILE 17 75 VAL 18 76 LYS 19 77 VAL 20 78 ARG 21 79 LYS 22 80 LYS 23 81 LEU 24 82 SER 25 83 LEU 26 84 THR 27 85 GLN 28 86 LYS 29 87 GLU 30 88 ALA 31 89 SER 32 90 GLU 33 91 ILE 34 92 PHE 35 93 GLY 36 94 GLY 37 95 GLY 38 96 VAL 39 97 ASN 40 98 ALA 41 99 PHE 42 100 SER 43 101 ARG 44 102 TYR 45 103 GLU 46 104 LYS 47 105 GLY 48 106 ASN 49 107 ALA 50 108 GLN 51 109 PRO 52 110 HIS 53 111 PRO 54 112 SER 55 113 THR 56 114 ILE 57 115 LYS 58 116 LEU 59 117 LEU 60 118 ARG 61 119 VAL 62 120 LEU 63 121 ASP 64 122 LYS 65 123 HIS 66 124 PRO 67 125 GLU 68 126 LEU 69 127 LEU 70 128 ASN 71 129 GLU 72 130 ILE 73 131 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-21 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 15446 2cxxc_-_Ygit 95.89 131 100.00 100.00 2.92e-41 PDB 2KZ8 "Solution Nmr Structure Of Mqsa, A Protein From E. Coli, Containing A Zinc Finger, N-Terminal And A Helix Turn-Helix C-Terminal " 95.89 131 100.00 100.00 2.92e-41 PDB 3FMY "Structure Of The C-Terminal Domain Of The E. Coli Protein Mqsa (YgitB3021)" 100.00 73 98.63 98.63 1.32e-43 PDB 3GN5 "Structure Of The E. Coli Protein Mqsa (YgitB3021)" 95.89 133 100.00 100.00 3.89e-41 PDB 3O9X "Structure Of The E. Coli Antitoxin Mqsa (YgitB3021) IN COMPLEX WITH Its Gene Promoter" 95.89 133 100.00 100.00 3.89e-41 DBJ BAE77077 "predicted DNA-binding transcriptional regulator [Escherichia coli str. K12 substr. W3110]" 95.89 131 100.00 100.00 2.92e-41 DBJ BAJ44773 "HTH-type transcriptional regulator ygiT [Escherichia coli DH1]" 95.89 131 100.00 100.00 2.92e-41 DBJ BAL39680 "predicted DNA-binding transcriptional regulator [Escherichia coli str. K-12 substr. MDS42]" 95.89 131 100.00 100.00 2.92e-41 EMBL CAQ33360 "MqsA antitoxin of the MqsRA toxin-antitoxin system and DNA transcriptional repressor, subunit of MqsR-MqsA complex DNA binding " 95.89 131 100.00 100.00 2.92e-41 EMBL CAR14662 "putative DNA-binding transcriptional regulator [Escherichia coli UMN026]" 95.89 131 100.00 100.00 2.92e-41 EMBL CAR19632 "putative DNA-binding transcriptional regulator [Escherichia coli IAI39]" 95.89 131 100.00 100.00 2.92e-41 EMBL CBJ02792 "putative DNA-binding HTH regulator [Escherichia coli ETEC H10407]" 95.89 131 100.00 100.00 2.92e-41 EMBL CCJ45634 "hypothetical protein BN17_29491 [Escherichia coli]" 95.89 131 100.00 100.00 2.92e-41 GB AAA69189 "ORF_f131 [Escherichia coli str. K-12 substr. MG1655]" 95.89 131 100.00 100.00 2.92e-41 GB AAC76057 "antitoxin for MqsR toxin; transcriptional repressor [Escherichia coli str. K-12 substr. MG1655]" 95.89 131 100.00 100.00 2.92e-41 GB ABV07432 "transcriptional regulator, Cro/CI family [Escherichia coli HS]" 95.89 131 100.00 100.00 2.92e-41 GB ACA76352 "transcriptional regulator, XRE family [Escherichia coli ATCC 8739]" 95.89 131 100.00 100.00 2.92e-41 GB ACB04106 "predicted DNA-binding transcriptional regulator [Escherichia coli str. K-12 substr. DH10B]" 95.89 131 100.00 100.00 2.92e-41 REF NP_417493 "antitoxin for MqsR toxin; transcriptional repressor [Escherichia coli str. K-12 substr. MG1655]" 95.89 131 100.00 100.00 2.92e-41 REF WP_000650107 "MULTISPECIES: antitoxin [Proteobacteria]" 95.89 131 100.00 100.00 2.92e-41 REF WP_001487520 "antitoxin [Escherichia coli]" 95.89 131 100.00 100.00 2.74e-41 REF WP_021572968 "antitoxin [Escherichia coli]" 95.89 131 100.00 100.00 2.80e-41 REF WP_044814339 "hypothetical protein [Escherichia coli]" 69.86 106 100.00 100.00 3.47e-27 SP Q46864 "RecName: Full=Antitoxin MqsA" 95.89 131 100.00 100.00 2.92e-41 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $mqsa_c '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 $mqsa_c 'recombinant technology' . Escherichia coli . RP1B 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 $mqsa_c 0.5 mM '[U-99% 15N]' 'sodium chloride' 50 mM 'natural abundance' TRIS 10 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $mqsa_c 0.5 mM '[U-99% 13C; U-99% 15N]' 'sodium chloride' 50 mM 'natural abundance' TRIS 10 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.8.2 loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_2 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_2 save_ save_3D_C(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_2 save_ save_3D_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_2 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' 60 . mM pH 7.0 . pH pressure 1 . atm temperature 293 . 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 HNCA' '3D HNCACB' '3D CBCA(CO)NH' '3D C(CO)NH' '3D HNCO' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'mqsa cterm' _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 60 2 HIS C C 175.007 0.3 1 2 60 2 HIS CA C 56.249 0.3 1 3 60 2 HIS CB C 30.507 0.3 1 4 61 3 MET H H 8.345 0.02 1 5 61 3 MET C C 175.510 0.3 1 6 61 3 MET CA C 55.238 0.3 1 7 61 3 MET CB C 32.784 0.3 1 8 61 3 MET N N 122.738 0.06 1 9 62 4 ALA H H 8.305 0.02 1 10 62 4 ALA C C 177.616 0.3 1 11 62 4 ALA CA C 52.455 0.3 1 12 62 4 ALA CB C 19.059 0.3 1 13 62 4 ALA N N 125.826 0.06 1 14 63 5 SER H H 8.186 0.02 1 15 63 5 SER CA C 58.147 0.3 1 16 63 5 SER CB C 63.713 0.3 1 17 63 5 SER N N 115.388 0.06 1 18 64 6 VAL H H 8.044 0.02 1 19 64 6 VAL C C 175.839 0.3 1 20 64 6 VAL CA C 62.316 0.3 1 21 64 6 VAL CB C 32.505 0.3 1 22 64 6 VAL CG1 C 20.628 0.3 2 23 64 6 VAL CG2 C 20.309 0.3 2 24 64 6 VAL N N 121.473 0.06 1 25 65 7 ASN H H 8.318 0.02 1 26 65 7 ASN C C 174.781 0.3 1 27 65 7 ASN CA C 53.087 0.3 1 28 65 7 ASN CB C 38.793 0.3 1 29 65 7 ASN N N 122.009 0.06 1 30 66 8 ALA H H 8.127 0.02 1 31 66 8 ALA C C 177.437 0.3 1 32 66 8 ALA CA C 52.644 0.3 1 33 66 8 ALA CB C 19.122 0.3 1 34 66 8 ALA N N 124.421 0.06 1 35 67 9 GLU H H 8.209 0.02 1 36 67 9 GLU C C 176.075 0.3 1 37 67 9 GLU CA C 56.577 0.3 1 38 67 9 GLU CB C 30.074 0.3 1 39 67 9 GLU CG C 36.131 0.3 1 40 67 9 GLU N N 119.667 0.06 1 41 68 10 THR H H 7.785 0.02 1 42 68 10 THR C C 173.747 0.3 1 43 68 10 THR CA C 60.867 0.3 1 44 68 10 THR CB C 70.670 0.3 1 45 68 10 THR CG2 C 21.226 0.3 1 46 68 10 THR N N 114.692 0.06 1 47 69 11 VAL H H 8.343 0.02 1 48 69 11 VAL C C 173.846 0.3 1 49 69 11 VAL CA C 59.766 0.3 1 50 69 11 VAL CB C 33.979 0.3 1 51 69 11 VAL CG1 C 21.026 0.3 2 52 69 11 VAL CG2 C 20.787 0.3 2 53 69 11 VAL N N 119.432 0.06 1 54 70 12 ALA H H 8.410 0.02 1 55 70 12 ALA CA C 50.178 0.3 1 56 70 12 ALA CB C 18.110 0.3 1 57 70 12 ALA N N 129.100 0.06 1 58 71 13 PRO C C 177.924 0.3 1 59 71 13 PRO CA C 66.116 0.3 1 60 71 13 PRO CB C 31.962 0.3 1 61 71 13 PRO CD C 50.440 0.3 1 62 71 13 PRO CG C 28.041 0.3 1 63 72 14 GLU H H 8.839 0.02 1 64 72 14 GLU C C 178.810 0.3 1 65 72 14 GLU CA C 59.665 0.3 1 66 72 14 GLU CB C 28.609 0.3 1 67 72 14 GLU CG C 36.331 0.3 1 68 72 14 GLU N N 113.402 0.06 1 69 73 15 PHE H H 7.617 0.02 1 70 73 15 PHE C C 175.674 0.3 1 71 73 15 PHE CA C 60.882 0.3 1 72 73 15 PHE CB C 39.160 0.3 1 73 73 15 PHE N N 121.066 0.06 1 74 74 16 ILE H H 7.071 0.02 1 75 74 16 ILE C C 177.000 0.3 1 76 74 16 ILE CA C 65.421 0.3 1 77 74 16 ILE CB C 37.401 0.3 1 78 74 16 ILE CD1 C 13.454 0.3 1 79 74 16 ILE CG1 C 28.280 0.3 1 80 74 16 ILE CG2 C 18.794 0.3 1 81 74 16 ILE N N 118.125 0.06 1 82 75 17 VAL H H 7.590 0.02 1 83 75 17 VAL C C 177.226 0.3 1 84 75 17 VAL CA C 66.369 0.3 1 85 75 17 VAL CB C 31.962 0.3 1 86 75 17 VAL CG1 C 22.063 0.3 2 87 75 17 VAL CG2 C 21.186 0.3 2 88 75 17 VAL N N 116.240 0.06 1 89 76 18 LYS H H 7.427 0.02 1 90 76 18 LYS C C 180.195 0.3 1 91 76 18 LYS CA C 59.855 0.3 1 92 76 18 LYS CB C 31.582 0.3 1 93 76 18 LYS CD C 29.516 0.3 1 94 76 18 LYS CE C 41.950 0.3 1 95 76 18 LYS CG C 25.012 0.3 1 96 76 18 LYS N N 118.015 0.06 1 97 77 19 VAL H H 7.861 0.02 1 98 77 19 VAL C C 177.030 0.3 1 99 77 19 VAL CA C 66.820 0.3 1 100 77 19 VAL CB C 31.508 0.3 1 101 77 19 VAL CG1 C 22.939 0.3 2 102 77 19 VAL CG2 C 22.421 0.3 2 103 77 19 VAL N N 119.671 0.06 1 104 78 20 ARG H H 8.368 0.02 1 105 78 20 ARG C C 178.952 0.3 1 106 78 20 ARG CA C 62.064 0.3 1 107 78 20 ARG CB C 29.179 0.3 1 108 78 20 ARG CD C 41.592 0.3 1 109 78 20 ARG CG C 28.798 0.3 1 110 78 20 ARG N N 120.025 0.06 1 111 79 21 LYS H H 8.375 0.02 1 112 79 21 LYS C C 181.129 0.3 1 113 79 21 LYS CA C 59.791 0.3 1 114 79 21 LYS CB C 31.962 0.3 1 115 79 21 LYS CD C 29.356 0.3 1 116 79 21 LYS CE C 41.871 0.3 1 117 79 21 LYS CG C 25.929 0.3 1 118 79 21 LYS N N 115.379 0.06 1 119 80 22 LYS H H 7.947 0.02 1 120 80 22 LYS C C 178.078 0.3 1 121 80 22 LYS CA C 59.349 0.3 1 122 80 22 LYS CB C 31.582 0.3 1 123 80 22 LYS CD C 30.233 0.3 1 124 80 22 LYS CE C 41.791 0.3 1 125 80 22 LYS CG C 24.773 0.3 1 126 80 22 LYS N N 123.352 0.06 1 127 81 23 LEU H H 7.533 0.02 1 128 81 23 LEU C C 175.120 0.3 1 129 81 23 LEU CA C 54.226 0.3 1 130 81 23 LEU CB C 41.702 0.3 1 131 81 23 LEU CD1 C 25.889 0.3 2 132 81 23 LEU CD2 C 21.823 0.3 2 133 81 23 LEU CG C 26.845 0.3 1 134 81 23 LEU N N 117.389 0.06 1 135 82 24 SER H H 7.832 0.02 1 136 82 24 SER C C 173.527 0.3 1 137 82 24 SER CA C 58.463 0.3 1 138 82 24 SER CB C 61.373 0.3 1 139 82 24 SER N N 112.640 0.06 1 140 83 25 LEU H H 7.105 0.02 1 141 83 25 LEU C C 178.674 0.3 1 142 83 25 LEU CA C 52.295 0.3 1 143 83 25 LEU CB C 45.307 0.3 1 144 83 25 LEU CD1 C 25.331 0.3 2 145 83 25 LEU CD2 C 22.939 0.3 2 146 83 25 LEU CG C 26.686 0.3 1 147 83 25 LEU N N 116.226 0.06 1 148 84 26 THR H H 9.101 0.02 1 149 84 26 THR C C 176.044 0.3 1 150 84 26 THR CA C 61.056 0.3 1 151 84 26 THR CB C 70.923 0.3 1 152 84 26 THR CG2 C 21.664 0.3 1 153 84 26 THR N N 114.720 0.06 1 154 85 27 GLN H H 9.189 0.02 1 155 85 27 GLN C C 179.106 0.3 1 156 85 27 GLN CA C 61.014 0.3 1 157 85 27 GLN CB C 27.598 0.3 1 158 85 27 GLN CG C 34.179 0.3 1 159 85 27 GLN N N 120.605 0.06 1 160 86 28 LYS H H 8.511 0.02 1 161 86 28 LYS C C 178.829 0.3 1 162 86 28 LYS CA C 59.981 0.3 1 163 86 28 LYS CB C 32.847 0.3 1 164 86 28 LYS CD C 29.635 0.3 1 165 86 28 LYS CE C 42.030 0.3 1 166 86 28 LYS CG C 24.852 0.3 1 167 86 28 LYS N N 122.013 0.06 1 168 87 29 GLU H H 7.761 0.02 1 169 87 29 GLU C C 179.444 0.3 1 170 87 29 GLU CA C 58.690 0.3 1 171 87 29 GLU CB C 31.070 0.3 1 172 87 29 GLU CG C 37.048 0.3 1 173 87 29 GLU N N 119.325 0.06 1 174 88 30 ALA H H 8.309 0.02 1 175 88 30 ALA C C 178.356 0.3 1 176 88 30 ALA CA C 55.103 0.3 1 177 88 30 ALA CB C 15.207 0.3 1 178 88 30 ALA N N 119.276 0.06 1 179 89 31 SER H H 7.945 0.02 1 180 89 31 SER C C 176.531 0.3 1 181 89 31 SER CA C 62.827 0.3 1 182 89 31 SER CB C 63.015 0.3 1 183 89 31 SER N N 114.927 0.06 1 184 90 32 GLU H H 7.655 0.02 1 185 90 32 GLU C C 178.389 0.3 1 186 90 32 GLU CA C 59.145 0.3 1 187 90 32 GLU CB C 29.396 0.3 1 188 90 32 GLU CG C 36.291 0.3 1 189 90 32 GLU N N 122.247 0.06 1 190 91 33 ILE H H 7.919 0.02 1 191 91 33 ILE C C 177.030 0.3 1 192 91 33 ILE CA C 64.588 0.3 1 193 91 33 ILE CB C 39.519 0.3 1 194 91 33 ILE CD1 C 15.048 0.3 1 195 91 33 ILE CG1 C 28.838 0.3 1 196 91 33 ILE CG2 C 15.885 0.3 1 197 91 33 ILE N N 118.848 0.06 1 198 92 34 PHE H H 8.455 0.02 1 199 92 34 PHE C C 177.318 0.3 1 200 92 34 PHE CA C 59.538 0.3 1 201 92 34 PHE CB C 39.201 0.3 1 202 92 34 PHE N N 112.724 0.06 1 203 93 35 GLY H H 7.496 0.02 1 204 93 35 GLY C C 171.956 0.3 1 205 93 35 GLY CA C 44.422 0.3 1 206 93 35 GLY N N 107.707 0.06 1 207 94 36 GLY H H 8.248 0.02 1 208 94 36 GLY C C 175.715 0.3 1 209 94 36 GLY CA C 44.512 0.3 1 210 94 36 GLY N N 102.334 0.06 1 211 95 37 GLY H H 8.304 0.02 1 212 95 37 GLY C C 174.246 0.3 1 213 95 37 GLY CA C 43.726 0.3 1 214 95 37 GLY N N 111.519 0.06 1 215 96 38 VAL H H 8.108 0.02 1 216 96 38 VAL CA C 64.725 0.3 1 217 96 38 VAL CB C 31.582 0.3 1 218 96 38 VAL N N 117.516 0.06 1 219 97 39 ASN C C 176.078 0.3 1 220 97 39 ASN CA C 53.269 0.3 1 221 97 39 ASN CB C 38.005 0.3 1 222 98 40 ALA H H 7.585 0.02 1 223 98 40 ALA CA C 56.099 0.3 1 224 98 40 ALA CB C 18.396 0.3 1 225 98 40 ALA N N 122.193 0.06 1 226 99 41 PHE H H 8.091 0.02 1 227 99 41 PHE C C 177.924 0.3 1 228 99 41 PHE CA C 62.385 0.3 1 229 99 41 PHE CB C 37.022 0.3 1 230 99 41 PHE N N 113.468 0.06 1 231 100 42 SER H H 7.649 0.02 1 232 100 42 SER C C 177.174 0.3 1 233 100 42 SER CA C 61.120 0.3 1 234 100 42 SER CB C 61.942 0.3 1 235 100 42 SER N N 114.100 0.06 1 236 101 43 ARG H H 7.160 0.02 1 237 101 43 ARG C C 180.279 0.3 1 238 101 43 ARG CA C 59.311 0.3 1 239 101 43 ARG CB C 30.317 0.3 1 240 101 43 ARG CD C 43.545 0.3 1 241 101 43 ARG CG C 27.762 0.3 1 242 101 43 ARG N N 118.645 0.06 1 243 102 44 TYR H H 8.606 0.02 1 244 102 44 TYR C C 181.037 0.3 1 245 102 44 TYR CA C 56.936 0.3 1 246 102 44 TYR CB C 37.447 0.3 1 247 102 44 TYR N N 119.042 0.06 1 248 103 45 GLU H H 8.415 0.02 1 249 103 45 GLU C C 176.907 0.3 1 250 103 45 GLU CA C 59.349 0.3 1 251 103 45 GLU CB C 28.609 0.3 1 252 103 45 GLU CG C 38.682 0.3 1 253 103 45 GLU N N 117.026 0.06 1 254 104 46 LYS H H 7.153 0.02 1 255 104 46 LYS C C 176.989 0.3 1 256 104 46 LYS CA C 56.123 0.3 1 257 104 46 LYS CB C 33.669 0.3 1 258 104 46 LYS CD C 28.997 0.3 1 259 104 46 LYS CE C 41.990 0.3 1 260 104 46 LYS CG C 25.331 0.3 1 261 104 46 LYS N N 116.805 0.06 1 262 105 47 GLY H H 7.566 0.02 1 263 105 47 GLY C C 174.329 0.3 1 264 105 47 GLY CA C 45.491 0.3 1 265 105 47 GLY N N 105.423 0.06 1 266 106 48 ASN H H 7.996 0.02 1 267 106 48 ASN C C 173.866 0.3 1 268 106 48 ASN CA C 53.720 0.3 1 269 106 48 ASN CB C 39.615 0.3 1 270 106 48 ASN N N 115.784 0.06 1 271 107 49 ALA H H 7.233 0.02 1 272 107 49 ALA C C 175.459 0.3 1 273 107 49 ALA CA C 51.316 0.3 1 274 107 49 ALA CB C 22.221 0.3 1 275 107 49 ALA N N 118.116 0.06 1 276 108 50 GLN H H 8.806 0.02 1 277 108 50 GLN CA C 52.012 0.3 1 278 108 50 GLN CB C 29.811 0.3 1 279 108 50 GLN N N 120.781 0.06 1 280 109 51 PRO C C 179.784 0.3 1 281 109 51 PRO CA C 66.243 0.3 1 282 109 51 PRO CB C 32.088 0.3 1 283 109 51 PRO CD C 50.200 0.3 1 284 109 51 PRO CG C 27.802 0.3 1 285 110 52 HIS H H 11.815 0.02 1 286 110 52 HIS CA C 63.523 0.3 1 287 110 52 HIS CB C 31.936 0.3 1 288 110 52 HIS N N 116.325 0.06 1 289 112 54 SER C C 176.622 0.3 1 290 112 54 SER CA C 63.733 0.3 1 291 112 54 SER CB C 63.273 0.3 1 292 113 55 THR H H 7.885 0.02 1 293 113 55 THR C C 175.463 0.3 1 294 113 55 THR CA C 67.003 0.3 1 295 113 55 THR CB C 67.617 0.3 1 296 113 55 THR CG2 C 22.381 0.3 1 297 113 55 THR N N 120.424 0.06 1 298 114 56 ILE H H 7.472 0.02 1 299 114 56 ILE C C 177.380 0.3 1 300 114 56 ILE CA C 65.835 0.3 1 301 114 56 ILE CB C 37.208 0.3 1 302 114 56 ILE CD1 C 12.896 0.3 1 303 114 56 ILE CG1 C 28.679 0.3 1 304 114 56 ILE CG2 C 17.121 0.3 1 305 114 56 ILE N N 119.618 0.06 1 306 115 57 LYS H H 7.957 0.02 1 307 115 57 LYS C C 178.000 0.3 1 308 115 57 LYS CA C 60.297 0.3 1 309 115 57 LYS CB C 32.847 0.3 1 310 115 57 LYS CD C 28.798 0.3 1 311 115 57 LYS CE C 42.468 0.3 1 312 115 57 LYS CG C 27.045 0.3 1 313 115 57 LYS N N 116.556 0.06 1 314 116 58 LEU H H 8.156 0.02 1 315 116 58 LEU C C 178.479 0.3 1 316 116 58 LEU CA C 57.932 0.3 1 317 116 58 LEU CB C 42.309 0.3 1 318 116 58 LEU CD1 C 23.258 0.3 2 319 116 58 LEU CD2 C 26.606 0.3 2 320 116 58 LEU CG C 26.845 0.3 1 321 116 58 LEU N N 119.140 0.06 1 322 117 59 LEU H H 8.441 0.02 1 323 117 59 LEU C C 178.613 0.3 1 324 117 59 LEU CA C 58.490 0.3 1 325 117 59 LEU CB C 41.632 0.3 1 326 117 59 LEU CD1 C 26.247 0.3 2 327 117 59 LEU CD2 C 21.903 0.3 2 328 117 59 LEU CG C 26.487 0.3 1 329 117 59 LEU N N 118.939 0.06 1 330 118 60 ARG H H 8.147 0.02 1 331 118 60 ARG C C 180.363 0.3 1 332 118 60 ARG CA C 60.550 0.3 1 333 118 60 ARG CB C 30.001 0.3 1 334 118 60 ARG CD C 43.943 0.3 1 335 118 60 ARG CG C 28.400 0.3 1 336 118 60 ARG N N 117.478 0.06 1 337 119 61 VAL H H 7.986 0.02 1 338 119 61 VAL C C 177.893 0.3 1 339 119 61 VAL CA C 66.541 0.3 1 340 119 61 VAL CB C 31.987 0.3 1 341 119 61 VAL CG1 C 23.139 0.3 2 342 119 61 VAL CG2 C 22.342 0.3 2 343 119 61 VAL N N 120.420 0.06 1 344 120 62 LEU H H 8.399 0.02 1 345 120 62 LEU C C 176.661 0.3 1 346 120 62 LEU CA C 56.566 0.3 1 347 120 62 LEU CB C 41.576 0.3 1 348 120 62 LEU CD1 C 23.418 0.3 2 349 120 62 LEU CD2 C 15.247 0.3 2 350 120 62 LEU CG C 27.363 0.3 1 351 120 62 LEU N N 120.527 0.06 1 352 121 63 ASP H H 7.929 0.02 1 353 121 63 ASP C C 177.616 0.3 1 354 121 63 ASP CA C 56.882 0.3 1 355 121 63 ASP CB C 42.524 0.3 1 356 121 63 ASP N N 114.946 0.06 1 357 122 64 LYS H H 6.605 0.02 1 358 122 64 LYS C C 176.671 0.3 1 359 122 64 LYS CA C 56.685 0.3 1 360 122 64 LYS CB C 33.922 0.3 1 361 122 64 LYS CD C 28.360 0.3 1 362 122 64 LYS CE C 42.070 0.3 1 363 122 64 LYS CG C 25.410 0.3 1 364 122 64 LYS N N 113.081 0.06 1 365 123 65 HIS H H 8.083 0.02 1 366 123 65 HIS CA C 52.075 0.3 1 367 123 65 HIS CB C 27.850 0.3 1 368 123 65 HIS N N 116.396 0.06 1 369 124 66 PRO C C 179.065 0.3 1 370 124 66 PRO CA C 65.610 0.3 1 371 124 66 PRO CB C 31.392 0.3 1 372 124 66 PRO CD C 49.682 0.3 1 373 124 66 PRO CG C 27.403 0.3 1 374 125 67 GLU H H 10.056 0.02 1 375 125 67 GLU C C 178.143 0.3 1 376 125 67 GLU CA C 58.147 0.3 1 377 125 67 GLU CB C 26.902 0.3 1 378 125 67 GLU CG C 34.976 0.3 1 379 125 67 GLU N N 121.524 0.06 1 380 126 68 LEU H H 7.887 0.02 1 381 126 68 LEU C C 178.078 0.3 1 382 126 68 LEU CA C 55.940 0.3 1 383 126 68 LEU CB C 40.795 0.3 1 384 126 68 LEU CD1 C 26.487 0.3 2 385 126 68 LEU CD2 C 21.823 0.3 2 386 126 68 LEU CG C 28.240 0.3 1 387 126 68 LEU N N 120.922 0.06 1 388 127 69 LEU H H 7.573 0.02 1 389 127 69 LEU C C 177.729 0.3 1 390 127 69 LEU CA C 57.853 0.3 1 391 127 69 LEU CB C 41.552 0.3 1 392 127 69 LEU CD1 C 22.860 0.3 2 393 127 69 LEU CD2 C 26.726 0.3 2 394 127 69 LEU CG C 26.965 0.3 1 395 127 69 LEU N N 120.671 0.06 1 396 128 70 ASN H H 7.543 0.02 1 397 128 70 ASN C C 176.733 0.3 1 398 128 70 ASN CA C 55.491 0.3 1 399 128 70 ASN CB C 37.970 0.3 1 400 128 70 ASN N N 112.176 0.06 1 401 129 71 GLU H H 7.635 0.02 1 402 129 71 GLU C C 177.863 0.3 1 403 129 71 GLU CA C 57.767 0.3 1 404 129 71 GLU CB C 30.191 0.3 1 405 129 71 GLU CG C 36.490 0.3 1 406 129 71 GLU N N 115.982 0.06 1 407 130 72 ILE H H 7.149 0.02 1 408 130 72 ILE C C 174.062 0.3 1 409 130 72 ILE CA C 60.740 0.3 1 410 130 72 ILE CB C 39.488 0.3 1 411 130 72 ILE CD1 C 15.486 0.3 1 412 130 72 ILE CG1 C 26.128 0.3 1 413 130 72 ILE CG2 C 18.595 0.3 1 414 130 72 ILE N N 108.895 0.06 1 415 131 73 ARG H H 7.044 0.02 1 416 131 73 ARG CA C 58.400 0.3 1 417 131 73 ARG CB C 31.013 0.3 1 418 131 73 ARG N N 126.079 0.06 1 stop_ save_