data_11034 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for N-terminal DNA Recognition Domain of the Bacillus subtilis transition-state regulator SpoVT ; _BMRB_accession_number 11034 _BMRB_flat_file_name bmr11034.str _Entry_type original _Submission_date 2008-03-13 _Accession_date 2008-03-14 _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 Sullivan Daniel M. . 2 Bobay Benjamin G. . 3 Kojetin Douglas J. . 4 Thompson Richele J. . 5 Rance Mark . . 6 Strauch Mark A. . 7 Cavanagh John . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 303 "13C chemical shifts" 241 "15N chemical shifts" 49 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-12-11 original author . stop_ _Original_release_date 2008-12-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Insights into the nature of DNA-binding of AbrB-like transcription factors' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19000822 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sullivan Daniel M. . 2 Bobay Benjamin G. . 3 Kojetin Douglas J. . 4 Thompson Richele J. . 5 Rance Mark . . 6 Strauch Mark A. . 7 Cavanagh John . . stop_ _Journal_abbreviation Structure _Journal_volume 16 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1702 _Page_last 1713 _Year 2008 _Details . loop_ _Keyword transcription stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'SpoVTN dimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'SpoVTN subunit 1' $SpoVTN 'SpoVTN subunit 2' $SpoVTN stop_ _System_molecular_weight 12753 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function DNA-binding stop_ _Database_query_date . _Details 'SpoVTN dimer' save_ ######################## # Monomeric polymers # ######################## save_SpoVTN _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SpoVTN _Molecular_mass 6376.5 _Mol_thiol_state 'not present' loop_ _Biological_function DNA-binding stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 55 _Mol_residue_sequence ; MKATGIVRRIDDLGRVVIPK EIRRTLRIREGDPLEIFVDR DGEVILKKYSPISEL ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 ALA 4 THR 5 GLY 6 ILE 7 VAL 8 ARG 9 ARG 10 ILE 11 ASP 12 ASP 13 LEU 14 GLY 15 ARG 16 VAL 17 VAL 18 ILE 19 PRO 20 LYS 21 GLU 22 ILE 23 ARG 24 ARG 25 THR 26 LEU 27 ARG 28 ILE 29 ARG 30 GLU 31 GLY 32 ASP 33 PRO 34 LEU 35 GLU 36 ILE 37 PHE 38 VAL 39 ASP 40 ARG 41 ASP 42 GLY 43 GLU 44 VAL 45 ILE 46 LEU 47 LYS 48 LYS 49 TYR 50 SER 51 PRO 52 ILE 53 SER 54 GLU 55 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-17 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 PDB 2RO5 "Rdc-Refined Solution Structure Of The N-Terminal Dna Recognition Domain Of The Bacillus Subtilis Transition-State Regulator Spo" 100.00 55 100.00 100.00 1.32e-27 PDB 2W1T "Crystal Structure Of B. Subtilis Spovt" 100.00 178 100.00 100.00 9.27e-28 DBJ BAA05291 "similar to AbrB [Bacillus subtilis]" 100.00 178 100.00 100.00 9.27e-28 DBJ BAB03789 "stage V sporulation protein T [Bacillus halodurans C-125]" 100.00 179 100.00 100.00 6.25e-28 DBJ BAD42216 "stage V sprulation protein T [Symbiobacterium thermophilum IAM 14863]" 100.00 186 98.18 98.18 1.84e-26 DBJ BAD62627 "transcriptional regulator stage V sporulation protein T [Bacillus clausii KSM-K16]" 100.00 179 100.00 100.00 9.38e-28 DBJ BAD74334 "stage V sporulation protein T (transcriptional regulator) [Geobacillus kaustophilus HTA426]" 100.00 178 100.00 100.00 1.60e-27 EMBL CAB11832 "transcriptional regulator [Bacillus subtilis subsp. subtilis str. 168]" 100.00 178 100.00 100.00 9.27e-28 EMBL CBI41182 "transcriptional regulator [Bacillus amyloliquefaciens DSM 7]" 100.00 178 100.00 100.00 5.73e-28 EMBL CCC82977 "stage V sporulation protein T [Paenibacillus polymyxa M1]" 100.00 180 98.18 98.18 4.98e-27 EMBL CCF03591 "Stage V sporulation protein T [Bacillus methylotrophicus CAU B946]" 100.00 178 100.00 100.00 5.09e-28 EMBL CCF15332 "stage V sporulation protein T [Brevibacillus laterosporus GI-9]" 100.00 179 98.18 98.18 6.99e-27 GB AAP07157 "Stage V sporulation protein T [Bacillus cereus ATCC 14579]" 100.00 178 100.00 100.00 1.02e-27 GB AAP24108 "stage V sporulation protein T [Bacillus anthracis str. Ames]" 100.00 178 100.00 100.00 8.78e-28 GB AAS38988 "stage V sporulation protein T [Bacillus cereus ATCC 10987]" 100.00 178 100.00 100.00 1.02e-27 GB AAT29131 "stage V sporulation protein T [Bacillus anthracis str. 'Ames Ancestor']" 100.00 178 100.00 100.00 8.78e-28 GB AAT52391 "stage V sporulation protein T [Bacillus anthracis str. Sterne]" 100.00 178 100.00 100.00 8.78e-28 REF NP_387937 "stage V sporulation protein T [Bacillus subtilis subsp. subtilis str. 168]" 100.00 178 100.00 100.00 9.27e-28 REF NP_829956 "stage V sporulation protein T [Bacillus cereus ATCC 14579]" 100.00 178 100.00 100.00 1.02e-27 REF NP_842622 "stage V sporulation protein T [Bacillus anthracis str. Ames]" 100.00 178 100.00 100.00 8.78e-28 REF WP_000648302 "MULTISPECIES: stage V sporulation protein T [Bacillus]" 100.00 178 100.00 100.00 1.02e-27 REF WP_000648303 "MULTISPECIES: stage V sporulation protein T [Bacillus cereus group]" 100.00 178 100.00 100.00 8.88e-28 SP P37554 "RecName: Full=Stage V sporulation protein T" 100.00 178 100.00 100.00 9.27e-28 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $SpoVTN 'Bacillus subtilis' 1423 Bacteria . Bacillus subtilis spoVT 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 $SpoVTN 'recombinant technology' . Escherichia coli BL21(DE3) pET21-b 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $SpoVTN . mM 1 2 '[U-99% 13C; U-99% 15N]' $SpoVTN . mM 1 2 '[U-99% 13C; U-99% 15N]' TRIS-HCl 10 mM . . 'natural abundance' 'potassium chloride' 150 mM . . 'natural abundance' EDTA 1 mM . . 'natural abundance' DTT 1 mM . . 'natural abundance' 'sodium azide' 0.02 % . . 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $SpoVTN . mM 1 2 '[U-99% 15N]' $SpoVTN . mM 1 2 '[U-99% 15N]' TRIS-HCl 10 mM . . 'natural abundance' 'potassium chloride' 150 mM . . 'natural abundance' EDTA 1 mM . . 'natural abundance' DTT 1 mM . . 'natural abundance' 'sodium azide' 0.02 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_ARIA _Saveframe_category software _Name ARIA _Version . loop_ _Vendor _Address _Electronic_address 'Linge, O'Donoghue and Nilges' . . stop_ loop_ _Task 'structure solution' 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 'data analysis' stop_ _Details . save_ 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_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details 'equipped with triple resonance probe' 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_2 save_ save_3D_C(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_2 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_2 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_2 save_ save_3D_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2 save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_2 save_ save_3D_HN(CA)CO_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_2 save_ save_3D_HCCH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _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' 150 . mM pH 5.8 . pH pressure 1 . atm temperature 305 . 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 TMS C 13 'methyl protons' ppm 0.00 internal indirect . . . 0.25144954 water H 1 protons ppm 4.74 internal direct . . . 1.0 TMS N 15 'methyl protons' ppm 0.00 internal indirect . . . 0.1013291444 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 C(CO)NH' '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' '3D HN(CA)CO' '3D HCCH-TOCSY' 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 'SpoVTN subunit 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 MET CG C 15.937 . 1 2 1 1 MET HG2 H 1.986 . 2 3 2 2 LYS CA C 55.606 . 1 4 2 2 LYS HA H 4.540 . 1 5 2 2 LYS CB C 32.447 . 1 6 2 2 LYS HB2 H 1.865 . 2 7 2 2 LYS CG C 26.595 . 1 8 2 2 LYS HG2 H 1.489 . 2 9 2 2 LYS CD C 28.392 . 1 10 2 2 LYS HD2 H 1.683 . 2 11 2 2 LYS CE C 41.161 . 1 12 2 2 LYS HE2 H 3.000 . 2 13 2 2 LYS C C 177.204 . 1 14 3 3 ALA N N 126.109 . 1 15 3 3 ALA H H 8.553 . 1 16 3 3 ALA CA C 52.218 . 1 17 3 3 ALA HA H 4.342 . 1 18 3 3 ALA CB C 19.245 . 1 19 3 3 ALA HB H 1.408 . 1 20 3 3 ALA C C 179.308 . 1 21 4 4 THR N N 112.465 . 1 22 4 4 THR H H 8.078 . 1 23 4 4 THR CA C 61.583 . 1 24 4 4 THR HA H 4.420 . 1 25 4 4 THR CB C 69.460 . 1 26 4 4 THR HB H 4.204 . 1 27 4 4 THR CG2 C 21.200 . 1 28 4 4 THR HG2 H 1.242 . 1 29 4 4 THR C C 173.474 . 1 30 5 5 GLY N N 111.771 . 1 31 5 5 GLY H H 9.037 . 1 32 5 5 GLY CA C 44.687 . 1 33 5 5 GLY HA3 H 4.058 . 2 34 5 5 GLY HA2 H 3.623 . 2 35 5 5 GLY C C 174.756 . 1 36 6 6 ILE N N 121.234 . 1 37 6 6 ILE H H 8.287 . 1 38 6 6 ILE CA C 60.578 . 1 39 6 6 ILE HA H 4.132 . 1 40 6 6 ILE CB C 38.785 . 1 41 6 6 ILE HB H 1.765 . 1 42 6 6 ILE CG1 C 24.463 . 1 43 6 6 ILE HG13 H 1.574 . 1 44 6 6 ILE HG12 H 1.475 . 1 45 6 6 ILE CD1 C 12.335 . 1 46 6 6 ILE HD1 H 0.862 . 1 47 6 6 ILE CG2 C 17.491 . 1 48 6 6 ILE HG2 H 1.043 . 1 49 6 6 ILE C C 176.395 . 1 50 7 7 VAL N N 126.096 . 1 51 7 7 VAL H H 8.237 . 1 52 7 7 VAL CA C 60.516 . 1 53 7 7 VAL HA H 5.002 . 1 54 7 7 VAL CB C 32.807 . 1 55 7 7 VAL HB H 1.651 . 1 56 7 7 VAL CG2 C 20.233 . 1 57 7 7 VAL HG2 H 0.263 . 2 58 7 7 VAL CG1 C 21.235 . 1 59 7 7 VAL HG1 H 0.514 . 2 60 7 7 VAL C C 179.140 . 1 61 8 8 ARG N N 127.158 . 1 62 8 8 ARG H H 9.070 . 1 63 8 8 ARG CA C 52.551 . 1 64 8 8 ARG HA H 4.805 . 1 65 8 8 ARG CB C 34.444 . 1 66 8 8 ARG HB3 H 2.046 . 2 67 8 8 ARG HB2 H 1.613 . 2 68 8 8 ARG CG C 26.603 . 1 69 8 8 ARG HG3 H 1.936 . 2 70 8 8 ARG HG2 H 1.371 . 2 71 8 8 ARG CD C 42.841 . 1 72 8 8 ARG HD3 H 3.605 . 2 73 8 8 ARG HD2 H 3.226 . 2 74 8 8 ARG C C 176.302 . 1 75 9 9 ARG N N 118.729 . 1 76 9 9 ARG H H 8.630 . 1 77 9 9 ARG CA C 54.299 . 1 78 9 9 ARG HA H 5.115 . 1 79 9 9 ARG CB C 31.277 . 1 80 9 9 ARG HB3 H 1.600 . 2 81 9 9 ARG HB2 H 1.474 . 2 82 9 9 ARG CG C 27.724 . 1 83 9 9 ARG HG3 H 1.558 . 2 84 9 9 ARG HG2 H 1.292 . 2 85 9 9 ARG CD C 42.412 . 1 86 9 9 ARG HD2 H 3.190 . 2 87 9 9 ARG C C 178.367 . 1 88 10 10 ILE N N 122.469 . 1 89 10 10 ILE H H 7.962 . 1 90 10 10 ILE CA C 58.715 . 1 91 10 10 ILE HA H 4.541 . 1 92 10 10 ILE CB C 39.300 . 1 93 10 10 ILE HB H 1.634 . 1 94 10 10 ILE CG1 C 22.119 . 1 95 10 10 ILE HG13 H 1.325 . 1 96 10 10 ILE HG12 H 1.248 . 1 97 10 10 ILE CD1 C 13.644 . 1 98 10 10 ILE HD1 H 0.702 . 1 99 10 10 ILE CG2 C 16.201 . 1 100 10 10 ILE HG2 H 1.046 . 1 101 10 10 ILE C C 177.681 . 1 102 11 11 ASP N N 127.298 . 1 103 11 11 ASP H H 8.557 . 1 104 11 11 ASP CA C 52.440 . 1 105 11 11 ASP HA H 4.889 . 1 106 11 11 ASP CB C 40.972 . 1 107 11 11 ASP HB3 H 3.402 . 2 108 11 11 ASP HB2 H 2.832 . 2 109 11 11 ASP C C 178.929 . 1 110 12 12 ASP N N 113.147 . 1 111 12 12 ASP H H 8.506 . 1 112 12 12 ASP CA C 55.100 . 1 113 12 12 ASP HA H 4.054 . 1 114 12 12 ASP CB C 38.734 . 1 115 12 12 ASP HB3 H 2.454 . 2 116 12 12 ASP HB2 H 2.160 . 2 117 12 12 ASP C C 178.444 . 1 118 13 13 LEU N N 120.798 . 1 119 13 13 LEU H H 8.268 . 1 120 13 13 LEU CA C 53.160 . 1 121 13 13 LEU HA H 4.510 . 1 122 13 13 LEU CB C 42.040 . 1 123 13 13 LEU HB3 H 1.777 . 2 124 13 13 LEU HB2 H 1.556 . 2 125 13 13 LEU CG C 26.504 . 1 126 13 13 LEU HG H 1.604 . 1 127 13 13 LEU CD1 C 22.893 . 1 128 13 13 LEU HD1 H 0.836 . 2 129 13 13 LEU CD2 C 24.249 . 1 130 13 13 LEU HD2 H 0.829 . 2 131 13 13 LEU C C 178.487 . 1 132 14 14 GLY N N 106.617 . 1 133 14 14 GLY H H 7.978 . 1 134 14 14 GLY CA C 44.441 . 1 135 14 14 GLY HA3 H 3.380 . 2 136 14 14 GLY HA2 H 4.168 . 2 137 14 14 GLY C C 174.619 . 1 138 15 15 ARG N N 116.828 . 1 139 15 15 ARG H H 8.530 . 1 140 15 15 ARG CA C 54.284 . 1 141 15 15 ARG HA H 5.202 . 1 142 15 15 ARG CB C 31.579 . 1 143 15 15 ARG HB3 H 2.222 . 2 144 15 15 ARG HB2 H 1.234 . 2 145 15 15 ARG CG C 26.559 . 1 146 15 15 ARG HG3 H 1.593 . 2 147 15 15 ARG HG2 H 1.434 . 2 148 15 15 ARG CD C 42.739 . 1 149 15 15 ARG HD3 H 3.285 . 2 150 15 15 ARG HD2 H 2.700 . 2 151 15 15 ARG C C 178.314 . 1 152 16 16 VAL N N 119.216 . 1 153 16 16 VAL H H 8.481 . 1 154 16 16 VAL CA C 58.123 . 1 155 16 16 VAL HA H 4.494 . 1 156 16 16 VAL CB C 36.071 . 1 157 16 16 VAL HB H 1.634 . 1 158 16 16 VAL CG2 C 19.280 . 1 159 16 16 VAL HG2 H 0.723 . 2 160 16 16 VAL CG1 C 20.552 . 1 161 16 16 VAL HG1 H 0.514 . 2 162 16 16 VAL C C 174.742 . 1 163 17 17 VAL N N 125.420 . 1 164 17 17 VAL H H 7.990 . 1 165 17 17 VAL CA C 61.551 . 1 166 17 17 VAL HA H 3.882 . 1 167 17 17 VAL CB C 32.136 . 1 168 17 17 VAL HB H 1.871 . 1 169 17 17 VAL CG2 C 21.636 . 1 170 17 17 VAL HG2 H 0.940 . 2 171 17 17 VAL CG1 C 20.898 . 1 172 17 17 VAL HG1 H 0.829 . 2 173 17 17 VAL C C 176.487 . 1 174 18 18 ILE N N 125.876 . 1 175 18 18 ILE H H 8.527 . 1 176 18 18 ILE CA C 56.210 . 1 177 18 18 ILE HA H 4.332 . 1 178 18 18 ILE CB C 35.827 . 1 179 18 18 ILE HB H 1.971 . 1 180 18 18 ILE CG1 C 29.192 . 1 181 18 18 ILE HG13 H 2.141 . 1 182 18 18 ILE HG12 H 1.280 . 1 183 18 18 ILE CD1 C 17.683 . 1 184 18 18 ILE HD1 H 0.927 . 1 185 18 18 ILE CG2 C 21.236 . 1 186 18 18 ILE HG2 H 0.960 . 1 187 18 18 ILE C C 176.060 . 1 188 19 19 PRO CA C 62.944 . 1 189 19 19 PRO HA H 4.549 . 1 190 19 19 PRO CB C 32.802 . 1 191 19 19 PRO HB3 H 2.689 . 2 192 19 19 PRO HB2 H 1.834 . 2 193 19 19 PRO CG C 27.694 . 1 194 19 19 PRO HG3 H 1.967 . 2 195 19 19 PRO HG2 H 1.921 . 2 196 19 19 PRO CD C 50.785 . 1 197 19 19 PRO HD3 H 3.364 . 2 198 19 19 PRO HD2 H 4.437 . 2 199 19 19 PRO C C 178.970 . 1 200 20 20 LYS N N 126.618 . 1 201 20 20 LYS H H 9.014 . 1 202 20 20 LYS CA C 59.765 . 1 203 20 20 LYS HA H 3.756 . 1 204 20 20 LYS CB C 31.684 . 1 205 20 20 LYS HB3 H 1.955 . 2 206 20 20 LYS HB2 H 1.895 . 2 207 20 20 LYS CG C 23.878 . 1 208 20 20 LYS HG3 H 1.597 . 2 209 20 20 LYS HG2 H 1.487 . 2 210 20 20 LYS CD C 28.912 . 1 211 20 20 LYS HD3 H 1.708 . 2 212 20 20 LYS HD2 H 1.165 . 2 213 20 20 LYS CE C 41.096 . 1 214 20 20 LYS HE2 H 3.035 . 2 215 20 20 LYS C C 179.313 . 1 216 21 21 GLU N N 117.455 . 1 217 21 21 GLU H H 9.856 . 1 218 21 21 GLU CA C 59.771 . 1 219 21 21 GLU HA H 4.110 . 1 220 21 21 GLU CB C 28.626 . 1 221 21 21 GLU HB2 H 2.023 . 2 222 21 21 GLU CG C 36.095 . 1 223 21 21 GLU HG3 H 2.391 . 2 224 21 21 GLU HG2 H 2.326 . 2 225 21 21 GLU C C 180.774 . 1 226 22 22 ILE N N 118.288 . 1 227 22 22 ILE H H 7.074 . 1 228 22 22 ILE CA C 63.046 . 1 229 22 22 ILE HA H 3.849 . 1 230 22 22 ILE CB C 36.466 . 1 231 22 22 ILE HB H 1.950 . 1 232 22 22 ILE CG1 C 27.784 . 1 233 22 22 ILE HG13 H 1.556 . 1 234 22 22 ILE HG12 H 1.233 . 1 235 22 22 ILE CD1 C 11.927 . 1 236 22 22 ILE HD1 H 0.799 . 1 237 22 22 ILE CG2 C 17.235 . 1 238 22 22 ILE HG2 H 0.714 . 1 239 22 22 ILE C C 179.924 . 1 240 23 23 ARG N N 117.382 . 1 241 23 23 ARG H H 7.830 . 1 242 23 23 ARG CA C 60.379 . 1 243 23 23 ARG HA H 3.764 . 1 244 23 23 ARG CB C 28.923 . 1 245 23 23 ARG HB3 H 2.157 . 2 246 23 23 ARG HB2 H 1.718 . 2 247 23 23 ARG HG3 H 1.587 . 2 248 23 23 ARG HG2 H 1.168 . 2 249 23 23 ARG CD C 43.987 . 1 250 23 23 ARG HD3 H 3.363 . 2 251 23 23 ARG HD2 H 3.157 . 2 252 23 23 ARG C C 180.110 . 1 253 24 24 ARG N N 115.785 . 1 254 24 24 ARG H H 8.431 . 1 255 24 24 ARG CA C 58.531 . 1 256 24 24 ARG HA H 4.183 . 1 257 24 24 ARG CB C 29.763 . 1 258 24 24 ARG HB3 H 1.924 . 2 259 24 24 ARG HB2 H 2.128 . 2 260 24 24 ARG CG C 26.173 . 1 261 24 24 ARG HG3 H 1.783 . 2 262 24 24 ARG HG2 H 1.651 . 2 263 24 24 ARG CD C 42.396 . 1 264 24 24 ARG HD2 H 3.260 . 2 265 24 24 ARG C C 181.515 . 1 266 25 25 THR N N 115.618 . 1 267 25 25 THR H H 7.733 . 1 268 25 25 THR CA C 65.778 . 1 269 25 25 THR HA H 3.994 . 1 270 25 25 THR CB C 68.590 . 1 271 25 25 THR HB H 4.256 . 1 272 25 25 THR CG2 C 21.714 . 1 273 25 25 THR HG2 H 1.328 . 1 274 25 25 THR C C 177.350 . 1 275 26 26 LEU N N 117.244 . 1 276 26 26 LEU H H 7.796 . 1 277 26 26 LEU CA C 54.352 . 1 278 26 26 LEU HA H 4.368 . 1 279 26 26 LEU CB C 42.330 . 1 280 26 26 LEU HB2 H 1.608 . 2 281 26 26 LEU CG C 25.107 . 1 282 26 26 LEU HG H 2.311 . 1 283 26 26 LEU CD1 C 21.914 . 1 284 26 26 LEU HD1 H 0.871 . 2 285 26 26 LEU CD2 C 17.448 . 1 286 26 26 LEU HD2 H 0.774 . 2 287 26 26 LEU C C 177.163 . 1 288 27 27 ARG N N 116.574 . 1 289 27 27 ARG H H 7.720 . 1 290 27 27 ARG CA C 56.737 . 1 291 27 27 ARG HA H 3.872 . 1 292 27 27 ARG CB C 25.656 . 1 293 27 27 ARG HB3 H 2.085 . 2 294 27 27 ARG HB2 H 1.927 . 2 295 27 27 ARG HG2 H 1.650 . 2 296 27 27 ARG CD C 42.720 . 1 297 27 27 ARG HD2 H 3.277 . 2 298 27 27 ARG C C 176.893 . 1 299 28 28 ILE N N 116.788 . 1 300 28 28 ILE H H 8.332 . 1 301 28 28 ILE CA C 60.527 . 1 302 28 28 ILE HA H 4.465 . 1 303 28 28 ILE CB C 39.882 . 1 304 28 28 ILE HB H 1.562 . 1 305 28 28 ILE CG1 C 23.121 . 1 306 28 28 ILE CD1 C 13.281 . 1 307 28 28 ILE HD1 H 0.760 . 1 308 28 28 ILE CG2 C 18.214 . 1 309 28 28 ILE HG2 H 0.926 . 1 310 28 28 ILE C C 176.976 . 1 311 29 29 ARG N N 128.150 . 1 312 29 29 ARG H H 9.187 . 1 313 29 29 ARG CA C 53.925 . 1 314 29 29 ARG HA H 4.472 . 1 315 29 29 ARG CB C 31.701 . 1 316 29 29 ARG HB3 H 1.842 . 2 317 29 29 ARG HB2 H 1.739 . 2 318 29 29 ARG CG C 25.886 . 1 319 29 29 ARG HG3 H 1.679 . 2 320 29 29 ARG HG2 H 1.608 . 2 321 29 29 ARG CD C 42.435 . 1 322 29 29 ARG HD2 H 3.221 . 2 323 29 29 ARG C C 176.397 . 1 324 30 30 GLU N N 119.127 . 1 325 30 30 GLU H H 8.813 . 1 326 30 30 GLU CA C 58.715 . 1 327 30 30 GLU HA H 3.642 . 1 328 30 30 GLU CB C 27.910 . 1 329 30 30 GLU HB2 H 1.952 . 2 330 30 30 GLU CG C 35.599 . 1 331 30 30 GLU HG3 H 2.156 . 2 332 30 30 GLU HG2 H 2.441 . 2 333 30 30 GLU C C 178.085 . 1 334 31 31 GLY N N 113.446 . 1 335 31 31 GLY H H 8.365 . 1 336 31 31 GLY CA C 44.684 . 1 337 31 31 GLY HA3 H 4.401 . 2 338 31 31 GLY HA2 H 3.749 . 2 339 31 31 GLY C C 175.765 . 1 340 32 32 ASP N N 121.874 . 1 341 32 32 ASP H H 8.288 . 1 342 32 32 ASP CA C 52.900 . 1 343 32 32 ASP HA H 4.973 . 1 344 32 32 ASP CB C 39.908 . 1 345 32 32 ASP HB3 H 3.008 . 2 346 32 32 ASP HB2 H 2.610 . 2 347 32 32 ASP C C 176.423 . 1 348 33 33 PRO CA C 61.096 . 1 349 33 33 PRO HA H 4.774 . 1 350 33 33 PRO CB C 31.074 . 1 351 33 33 PRO HB3 H 2.119 . 2 352 33 33 PRO HB2 H 1.855 . 2 353 33 33 PRO CG C 28.577 . 1 354 33 33 PRO HG3 H 1.984 . 2 355 33 33 PRO HG2 H 1.862 . 2 356 33 33 PRO CD C 50.276 . 1 357 33 33 PRO HD3 H 4.079 . 2 358 33 33 PRO HD2 H 3.998 . 2 359 33 33 PRO C C 177.497 . 1 360 34 34 LEU N N 123.101 . 1 361 34 34 LEU H H 9.067 . 1 362 34 34 LEU CA C 52.842 . 1 363 34 34 LEU HA H 5.052 . 1 364 34 34 LEU CB C 44.012 . 1 365 34 34 LEU HB3 H 1.728 . 2 366 34 34 LEU HB2 H 1.237 . 2 367 34 34 LEU CG C 26.452 . 1 368 34 34 LEU HG H 1.719 . 1 369 34 34 LEU CD1 C 23.143 . 1 370 34 34 LEU HD1 H 0.786 . 2 371 34 34 LEU C C 176.051 . 1 372 35 35 GLU N N 122.921 . 1 373 35 35 GLU H H 9.535 . 1 374 35 35 GLU CA C 54.656 . 1 375 35 35 GLU HA H 4.218 . 1 376 35 35 GLU CB C 32.760 . 1 377 35 35 GLU HB3 H 2.180 . 2 378 35 35 GLU HB2 H 1.950 . 2 379 35 35 GLU CG C 36.096 . 1 380 35 35 GLU HG3 H 2.600 . 2 381 35 35 GLU HG2 H 2.485 . 2 382 35 35 GLU C C 177.010 . 1 383 36 36 ILE N N 122.970 . 1 384 36 36 ILE H H 8.514 . 1 385 36 36 ILE CA C 60.838 . 1 386 36 36 ILE HA H 4.184 . 1 387 36 36 ILE CB C 38.529 . 1 388 36 36 ILE HB H 1.888 . 1 389 36 36 ILE CG1 C 26.978 . 1 390 36 36 ILE HG13 H 1.491 . 1 391 36 36 ILE HG12 H 1.212 . 1 392 36 36 ILE CD1 C 13.447 . 1 393 36 36 ILE HD1 H 0.890 . 1 394 36 36 ILE CG2 C 17.458 . 1 395 36 36 ILE HG2 H 0.937 . 1 396 36 36 ILE C C 177.618 . 1 397 37 37 PHE N N 125.834 . 1 398 37 37 PHE H H 9.392 . 1 399 37 37 PHE CA C 55.662 . 1 400 37 37 PHE HA H 5.087 . 1 401 37 37 PHE CB C 42.260 . 1 402 37 37 PHE HB3 H 3.094 . 2 403 37 37 PHE HB2 H 3.023 . 2 404 37 37 PHE C C 175.006 . 1 405 38 38 VAL N N 116.642 . 1 406 38 38 VAL H H 8.519 . 1 407 38 38 VAL CA C 60.289 . 1 408 38 38 VAL HA H 5.154 . 1 409 38 38 VAL CB C 34.258 . 1 410 38 38 VAL HB H 2.065 . 1 411 38 38 VAL CG2 C 21.315 . 1 412 38 38 VAL HG2 H 1.049 . 2 413 38 38 VAL CG1 C 20.617 . 1 414 38 38 VAL HG1 H 0.772 . 2 415 38 38 VAL C C 177.654 . 1 416 39 39 ASP N N 124.423 . 1 417 39 39 ASP H H 8.720 . 1 418 39 39 ASP CA C 51.372 . 1 419 39 39 ASP HA H 5.014 . 1 420 39 39 ASP CB C 42.446 . 1 421 39 39 ASP HB3 H 2.827 . 2 422 39 39 ASP HB2 H 3.017 . 2 423 39 39 ASP C C 178.788 . 1 424 40 40 ARG N N 117.971 . 1 425 40 40 ARG H H 8.601 . 1 426 40 40 ARG CA C 57.264 . 1 427 40 40 ARG HA H 4.174 . 1 428 40 40 ARG CB C 29.007 . 1 429 40 40 ARG HB2 H 1.914 . 2 430 40 40 ARG CG C 25.857 . 1 431 40 40 ARG HG3 H 1.725 . 2 432 40 40 ARG HG2 H 1.625 . 2 433 40 40 ARG CD C 42.461 . 1 434 40 40 ARG HD2 H 3.232 . 2 435 40 40 ARG C C 177.916 . 1 436 41 41 ASP N N 117.798 . 1 437 41 41 ASP H H 8.138 . 1 438 41 41 ASP CA C 53.578 . 1 439 41 41 ASP HA H 4.723 . 1 440 41 41 ASP CB C 39.947 . 1 441 41 41 ASP HB3 H 2.551 . 2 442 41 41 ASP HB2 H 2.875 . 2 443 41 41 ASP C C 178.048 . 1 444 42 42 GLY N N 106.809 . 1 445 42 42 GLY H H 8.125 . 1 446 42 42 GLY CA C 46.017 . 1 447 42 42 GLY HA3 H 4.156 . 2 448 42 42 GLY HA2 H 3.647 . 2 449 42 42 GLY C C 174.932 . 1 450 43 43 GLU N N 116.783 . 1 451 43 43 GLU H H 7.909 . 1 452 43 43 GLU CA C 53.603 . 1 453 43 43 GLU HA H 4.741 . 1 454 43 43 GLU CB C 29.813 . 1 455 43 43 GLU HB3 H 1.973 . 2 456 43 43 GLU HB2 H 1.875 . 2 457 43 43 GLU CG C 35.230 . 1 458 43 43 GLU HG3 H 2.135 . 2 459 43 43 GLU HG2 H 2.310 . 2 460 43 43 GLU C C 176.455 . 1 461 44 44 VAL N N 120.785 . 1 462 44 44 VAL H H 8.635 . 1 463 44 44 VAL CA C 61.231 . 1 464 44 44 VAL HA H 4.503 . 1 465 44 44 VAL CB C 32.334 . 1 466 44 44 VAL HB H 2.033 . 1 467 44 44 VAL CG2 C 21.031 . 1 468 44 44 VAL HG2 H 0.799 . 2 469 44 44 VAL CG1 C 21.246 . 1 470 44 44 VAL HG1 H 0.961 . 2 471 44 44 VAL C C 175.366 . 1 472 45 45 ILE N N 126.640 . 1 473 45 45 ILE H H 8.972 . 1 474 45 45 ILE CA C 59.456 . 1 475 45 45 ILE HA H 4.889 . 1 476 45 45 ILE CB C 38.628 . 1 477 45 45 ILE HB H 1.633 . 1 478 45 45 ILE CG1 C 27.488 . 1 479 45 45 ILE HG13 H 1.077 . 1 480 45 45 ILE HG12 H 1.323 . 1 481 45 45 ILE CD1 C 13.126 . 1 482 45 45 ILE HD1 H 0.764 . 1 483 45 45 ILE CG2 C 17.860 . 1 484 45 45 ILE HG2 H 0.664 . 1 485 45 45 ILE C C 176.485 . 1 486 46 46 LEU N N 123.557 . 1 487 46 46 LEU H H 9.340 . 1 488 46 46 LEU CA C 52.946 . 1 489 46 46 LEU HA H 5.384 . 1 490 46 46 LEU CB C 42.721 . 1 491 46 46 LEU HB3 H 1.334 . 2 492 46 46 LEU HB2 H 1.725 . 2 493 46 46 LEU CG C 25.180 . 1 494 46 46 LEU HG H 1.638 . 1 495 46 46 LEU CD1 C 18.620 . 1 496 46 46 LEU CD2 C 25.292 . 1 497 46 46 LEU HD2 H 0.719 . 2 498 46 46 LEU C C 177.393 . 1 499 47 47 LYS N N 119.462 . 1 500 47 47 LYS H H 8.909 . 1 501 47 47 LYS CA C 53.220 . 1 502 47 47 LYS HA H 4.959 . 1 503 47 47 LYS CB C 35.877 . 1 504 47 47 LYS HB3 H 2.039 . 2 505 47 47 LYS HB2 H 1.846 . 2 506 47 47 LYS CD C 26.326 . 1 507 47 47 LYS HD3 H 1.613 . 2 508 47 47 LYS HD2 H 1.744 . 2 509 47 47 LYS CE C 40.718 . 1 510 47 47 LYS HE3 H 2.926 . 2 511 47 47 LYS HE2 H 2.836 . 2 512 48 48 LYS CA C 58.654 . 1 513 48 48 LYS HA H 4.251 . 1 514 48 48 LYS CB C 31.479 . 1 515 48 48 LYS HB3 H 2.224 . 2 516 48 48 LYS HB2 H 1.947 . 2 517 48 48 LYS CG C 24.477 . 1 518 48 48 LYS HG3 H 1.608 . 2 519 48 48 LYS HG2 H 1.463 . 2 520 48 48 LYS CD C 28.437 . 1 521 48 48 LYS HD3 H 1.825 . 2 522 48 48 LYS HD2 H 1.748 . 2 523 48 48 LYS CE C 41.197 . 1 524 48 48 LYS HE2 H 3.026 . 2 525 48 48 LYS C C 178.183 . 1 526 49 49 TYR N N 125.460 . 1 527 49 49 TYR H H 8.189 . 1 528 49 49 TYR CA C 57.281 . 1 529 49 49 TYR HA H 4.762 . 1 530 49 49 TYR CB C 38.697 . 1 531 49 49 TYR HB3 H 2.867 . 2 532 49 49 TYR HB2 H 2.714 . 2 533 49 49 TYR C C 176.094 . 1 534 50 50 SER N N 122.040 . 1 535 50 50 SER H H 8.045 . 1 536 50 50 SER CA C 54.280 . 1 537 50 50 SER HA H 4.635 . 1 538 50 50 SER CB C 62.402 . 1 539 50 50 SER HB3 H 3.717 . 2 540 50 50 SER HB2 H 3.601 . 2 541 51 51 PRO CA C 62.488 . 1 542 51 51 PRO HA H 4.298 . 1 543 51 51 PRO CB C 31.121 . 1 544 51 51 PRO HB3 H 1.952 . 2 545 51 51 PRO HB2 H 2.215 . 2 546 51 51 PRO CG C 26.012 . 1 547 51 51 PRO CD C 50.211 . 1 548 51 51 PRO HD3 H 3.551 . 2 549 51 51 PRO HD2 H 3.100 . 2 550 51 51 PRO C C 178.546 . 1 551 52 52 ILE N N 118.973 . 1 552 52 52 ILE H H 7.963 . 1 553 52 52 ILE CA C 60.234 . 1 554 52 52 ILE HA H 4.198 . 1 555 52 52 ILE CB C 37.863 . 1 556 52 52 ILE HB H 1.917 . 1 557 52 52 ILE CG1 C 26.407 . 1 558 52 52 ILE HG13 H 1.475 . 1 559 52 52 ILE HG12 H 1.210 . 1 560 52 52 ILE CD1 C 12.056 . 1 561 52 52 ILE HD1 H 0.900 . 1 562 52 52 ILE CG2 C 16.688 . 1 563 52 52 ILE HG2 H 0.930 . 1 564 52 52 ILE C C 177.929 . 1 565 53 53 SER N N 118.194 . 1 566 53 53 SER H H 8.203 . 1 567 53 53 SER CA C 57.318 . 1 568 53 53 SER HA H 4.480 . 1 569 53 53 SER CB C 63.124 . 1 570 53 53 SER HB2 H 3.862 . 2 571 53 53 SER C C 175.932 . 1 572 54 54 GLU N N 122.542 . 1 573 54 54 GLU H H 8.347 . 1 574 54 54 GLU CA C 55.560 . 1 575 54 54 GLU HA H 4.387 . 1 576 54 54 GLU CB C 29.438 . 1 577 54 54 GLU HB3 H 2.149 . 2 578 54 54 GLU HB2 H 1.931 . 2 579 54 54 GLU CG C 35.270 . 1 580 54 54 GLU HG2 H 2.307 . 2 581 54 54 GLU C C 176.980 . 1 582 55 55 LEU N N 127.380 . 1 583 55 55 LEU H H 7.789 . 1 584 55 55 LEU CA C 54.472 . 1 585 55 55 LEU HA H 4.332 . 1 586 55 55 LEU CB C 29.388 . 1 587 55 55 LEU HB3 H 1.475 . 2 588 55 55 LEU HB2 H 1.298 . 2 589 55 55 LEU HG H 1.983 . 1 590 55 55 LEU HD1 H 0.809 . 2 591 55 55 LEU CD2 C 9.860 . 1 592 55 55 LEU HD2 H 0.617 . 2 593 55 55 LEU C C 174.095 . 1 stop_ save_