data_25616 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N chemical shift assignments for dimeric KaiB from the Thermosynechococcus elongatus BP-1 cyanobacterial species ; _BMRB_accession_number 25616 _BMRB_flat_file_name bmr25616.str _Entry_type original _Submission_date 2015-05-15 _Accession_date 2015-05-15 _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 Chang Yonggang . . 2 Cohen Susan . . 3 Phong Connie . . 4 Myers William . . 5 Kim Yong-Ick . . 6 Tseng Roger . . 7 Lin Jenny . . 8 Zhang Li . . 9 Boyd Joseph . . 10 Lee Yvonne . . 11 Kang Shannon . . 12 Lee David . . 13 Li Sheng . . 14 Britt R. . . 15 Rust Michael . . 16 Golden Susan . . 17 LiWang Andy . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 89 "13C chemical shifts" 281 "15N chemical shifts" 89 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-08-24 update BMRB 'update entry citation' 2015-07-14 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 25617 'dimeric KaiB bound to CI' 25618 N-SasA 25619 'N-SasA bound to CI' 25620 'G89A single mutant of dimeric KaiB' 25621 'D91R single mutant of dimeric KaiB' 25622 'D91R single mutant of dimeric KaiB (thioredoxin-like fold)' 25623 'G89A,D91R double mutant of dimeric KaiB' 25624 'G89A,D91R double mutant of KaiB' 25625 'G89A,D91R double mutant of KaiB bound to CI' 25626 'G88A,D90R double mutant of KaiB' stop_ _Original_release_date 2015-07-14 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; A Protein Fold Switch Joins the Circadian Oscillator to Clock Output in Cyanobacteria ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26113641 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chang Yonggang . . 2 Cohen Susan . . 3 Phong Connie . . 4 Myers William . . 5 Kim Yong-Ick . . 6 Tseng Roger . . 7 Lin Jenny . . 8 Zhang Li . . 9 Boyd Joseph . . 10 Lee Yvonne . . 11 Kang Shannon . . 12 Lee David . . 13 Li Sheng . . 14 Britt R. . . 15 Rust Michael . . 16 Golden Susan . . 17 LiWang Andy . . stop_ _Journal_abbreviation Science _Journal_volume 349 _Journal_issue 6245 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 324 _Page_last 328 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'KaiB dimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'dimeric KaiB, chain 1' $FTeKaiBN94YY 'dimeric KaiB, chain 2' $FTeKaiBN94YY 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_FTeKaiBN94YY _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FTeKaiBN94YY _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 102 _Mol_residue_sequence ; DYKDDDDKMAPLRKTAVLKL YVAGNTPNSVRALKTLNNIL EKEFKGVYALKVIDVLKNPQ LAEEDKILATPTLAKVLPPP VRRIIGDLSNREKVLIGLDL LA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ASP 2 2 TYR 3 3 LYS 4 4 ASP 5 5 ASP 6 6 ASP 7 7 ASP 8 8 LYS 9 9 MET 10 10 ALA 11 11 PRO 12 12 LEU 13 13 ARG 14 14 LYS 15 15 THR 16 16 ALA 17 17 VAL 18 18 LEU 19 19 LYS 20 20 LEU 21 21 TYR 22 22 VAL 23 23 ALA 24 24 GLY 25 25 ASN 26 26 THR 27 27 PRO 28 28 ASN 29 29 SER 30 30 VAL 31 31 ARG 32 32 ALA 33 33 LEU 34 34 LYS 35 35 THR 36 36 LEU 37 37 ASN 38 38 ASN 39 39 ILE 40 40 LEU 41 41 GLU 42 42 LYS 43 43 GLU 44 44 PHE 45 45 LYS 46 46 GLY 47 47 VAL 48 48 TYR 49 49 ALA 50 50 LEU 51 51 LYS 52 52 VAL 53 53 ILE 54 54 ASP 55 55 VAL 56 56 LEU 57 57 LYS 58 58 ASN 59 59 PRO 60 60 GLN 61 61 LEU 62 62 ALA 63 63 GLU 64 64 GLU 65 65 ASP 66 66 LYS 67 67 ILE 68 68 LEU 69 69 ALA 70 70 THR 71 71 PRO 72 72 THR 73 73 LEU 74 74 ALA 75 75 LYS 76 76 VAL 77 77 LEU 78 78 PRO 79 79 PRO 80 80 PRO 81 81 VAL 82 82 ARG 83 83 ARG 84 84 ILE 85 85 ILE 86 86 GLY 87 87 ASP 88 88 LEU 89 89 SER 90 90 ASN 91 91 ARG 92 92 GLU 93 93 LYS 94 94 VAL 95 95 LEU 96 96 ILE 97 97 GLY 98 98 LEU 99 99 ASP 100 100 LEU 101 101 LEU 102 102 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $FTeKaiBN94YY cyanobacteria 146786 Bacteria . Thermosynechococcus elongatus 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 $FTeKaiBN94YY 'recombinant technology' . Escherichia coli . pET-28b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; Sample: [N15,C13,H2]-FLAG-TeKaiB-1-94-Y8A-Y94A (600 uM); Buffer: 5 mM Tris, 50 mM NaCl, pH 7.0, 10 uM DSS, 0.02% NaNa3, 95%H2O/5%D2O, 1X Protease Inhibitor Cocktail; Volume: 350 uL; Tube: shaped ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FTeKaiBN94YY 600 uM '[U-13C; U-15N; U-2H]' Tris 5 mM 'natural abundance' NaCl 50 mM 'natural abundance' DSS 10 uM 'natural abundance' NaNa3 0.02 % 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' 'Protease Inhibitor Cocktail' 600 uM '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_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_Mars _Saveframe_category software _Name Mars _Version . loop_ _Vendor _Address _Electronic_address 'Young-Sang Jung and Markus Zweckstetter' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details 'robust automatic backbone assignment of protein' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'Bruker 600 MHz AVANCE III spectrometer with a TCI cryoprobe and z-axis pulsed-field gradient capability' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N TROSY' _Sample_label $sample_1 save_ save_3D_TROSY_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCACB' _Sample_label $sample_1 save_ save_3D_TROSY_HN(CO)CACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_TROSY_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CA)CO' _Sample_label $sample_1 save_ save_3D_TROSY_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCO' _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' 0.05 . M pH 7 . pH pressure 1 . atm temperature 273 . 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' MHz 601.129941 internal direct . . . 1.0 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 TROSY' '3D TROSY HNCACB' '3D TROSY HN(CO)CACB' '3D TROSY HN(CA)CO' '3D TROSY HNCO' 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 'dimeric KaiB, chain 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 6 6 ASP C C 176.500 . 1 2 6 6 ASP CA C 54.640 . 1 3 6 6 ASP CB C 40.570 . 1 4 7 7 ASP H H 8.217 . 1 5 7 7 ASP C C 176.900 . 1 6 7 7 ASP CA C 54.430 . 1 7 7 7 ASP CB C 40.320 . 1 8 7 7 ASP N N 121.200 . 1 9 8 8 LYS H H 8.097 . 1 10 8 8 LYS C C 177.100 . 1 11 8 8 LYS CA C 56.370 . 1 12 8 8 LYS CB C 31.450 . 1 13 8 8 LYS N N 121.500 . 1 14 9 9 MET H H 8.096 . 1 15 9 9 MET C C 176.000 . 1 16 9 9 MET CA C 54.710 . 1 17 9 9 MET CB C 31.520 . 1 18 9 9 MET N N 119.700 . 1 19 10 10 ALA H H 7.971 . 1 20 10 10 ALA C C 175.600 . 1 21 10 10 ALA CA C 50.830 . 1 22 10 10 ALA CB C 17.080 . 1 23 10 10 ALA N N 126.700 . 1 24 11 11 PRO C C 177.000 . 1 25 11 11 PRO CA C 62.760 . 1 26 11 11 PRO CB C 31.020 . 1 27 12 12 LEU H H 8.122 . 1 28 12 12 LEU C C 177.400 . 1 29 12 12 LEU CA C 54.630 . 1 30 12 12 LEU CB C 41.050 . 1 31 12 12 LEU N N 122.100 . 1 32 13 13 ARG H H 8.176 . 1 33 13 13 ARG C C 175.700 . 1 34 13 13 ARG CA C 55.290 . 1 35 13 13 ARG CB C 29.880 . 1 36 13 13 ARG N N 122.900 . 1 37 14 14 LYS H H 8.277 . 1 38 14 14 LYS C C 176.200 . 1 39 14 14 LYS CA C 55.430 . 1 40 14 14 LYS CB C 32.340 . 1 41 14 14 LYS N N 124.200 . 1 42 15 15 THR H H 8.126 . 1 43 15 15 THR C C 173.400 . 1 44 15 15 THR CA C 62.510 . 1 45 15 15 THR CB C 69.470 . 1 46 15 15 THR N N 120.300 . 1 47 16 16 ALA H H 8.007 . 1 48 16 16 ALA C C 176.400 . 1 49 16 16 ALA CA C 51.150 . 1 50 16 16 ALA CB C 19.510 . 1 51 16 16 ALA N N 130.200 . 1 52 17 17 VAL H H 8.595 . 1 53 17 17 VAL C C 174.200 . 1 54 17 17 VAL CA C 61.650 . 1 55 17 17 VAL CB C 32.480 . 1 56 17 17 VAL N N 122.800 . 1 57 18 18 LEU H H 8.946 . 1 58 18 18 LEU C C 173.300 . 1 59 18 18 LEU CA C 53.050 . 1 60 18 18 LEU CB C 42.290 . 1 61 18 18 LEU N N 131.600 . 1 62 19 19 LYS H H 8.898 . 1 63 19 19 LYS C C 174.500 . 1 64 19 19 LYS CA C 54.250 . 1 65 19 19 LYS CB C 33.290 . 1 66 19 19 LYS N N 126.700 . 1 67 20 20 LEU H H 8.440 . 1 68 20 20 LEU C C 174.300 . 1 69 20 20 LEU CA C 53.490 . 1 70 20 20 LEU CB C 42.610 . 1 71 20 20 LEU N N 122.500 . 1 72 21 21 TYR H H 8.060 . 1 73 21 21 TYR C C 175.200 . 1 74 21 21 TYR CA C 56.310 . 1 75 21 21 TYR CB C 38.370 . 1 76 21 21 TYR N N 121.700 . 1 77 22 22 VAL H H 9.273 . 1 78 22 22 VAL C C 174.500 . 1 79 22 22 VAL CA C 57.650 . 1 80 22 22 VAL CB C 33.850 . 1 81 22 22 VAL N N 117.700 . 1 82 23 23 ALA H H 9.112 . 1 83 23 23 ALA C C 175.500 . 1 84 23 23 ALA CA C 49.120 . 1 85 23 23 ALA CB C 16.190 . 1 86 23 23 ALA N N 127.000 . 1 87 24 24 GLY H H 7.745 . 1 88 24 24 GLY C C 171.300 . 1 89 24 24 GLY CA C 44.420 . 1 90 24 24 GLY N N 109.800 . 1 91 25 25 ASN H H 7.849 . 1 92 25 25 ASN C C 174.100 . 1 93 25 25 ASN CA C 51.740 . 1 94 25 25 ASN CB C 42.350 . 1 95 25 25 ASN N N 112.100 . 1 96 26 26 THR H H 9.071 . 1 97 26 26 THR C C 173.400 . 1 98 26 26 THR CA C 58.320 . 1 99 26 26 THR CB C 69.230 . 1 100 26 26 THR N N 113.700 . 1 101 27 27 PRO C C 180.100 . 1 102 27 27 PRO CA C 65.750 . 1 103 27 27 PRO CB C 30.550 . 1 104 28 28 ASN H H 8.464 . 1 105 28 28 ASN C C 179.000 . 1 106 28 28 ASN CA C 54.640 . 1 107 28 28 ASN CB C 37.020 . 1 108 28 28 ASN N N 113.600 . 1 109 29 29 SER H H 8.937 . 1 110 29 29 SER C C 175.900 . 1 111 29 29 SER CA C 62.310 . 1 112 29 29 SER CB C 61.400 . 1 113 29 29 SER N N 124.200 . 1 114 30 30 VAL H H 8.299 . 1 115 30 30 VAL C C 179.400 . 1 116 30 30 VAL CA C 66.400 . 1 117 30 30 VAL CB C 30.730 . 1 118 30 30 VAL N N 125.200 . 1 119 31 31 ARG H H 7.239 . 1 120 31 31 ARG C C 179.000 . 1 121 31 31 ARG CA C 59.160 . 1 122 31 31 ARG CB C 29.400 . 1 123 31 31 ARG N N 119.900 . 1 124 32 32 ALA H H 8.050 . 1 125 32 32 ALA C C 179.800 . 1 126 32 32 ALA CA C 54.670 . 1 127 32 32 ALA CB C 17.500 . 1 128 32 32 ALA N N 123.800 . 1 129 33 33 LEU H H 8.397 . 1 130 33 33 LEU C C 179.900 . 1 131 33 33 LEU CA C 57.550 . 1 132 33 33 LEU CB C 40.520 . 1 133 33 33 LEU N N 119.000 . 1 134 34 34 LYS H H 7.778 . 1 135 34 34 LYS C C 179.400 . 1 136 34 34 LYS CA C 59.250 . 1 137 34 34 LYS CB C 30.860 . 1 138 34 34 LYS N N 122.700 . 1 139 35 35 THR H H 8.189 . 1 140 35 35 THR C C 176.400 . 1 141 35 35 THR CA C 66.380 . 1 142 35 35 THR CB C 67.890 . 1 143 35 35 THR N N 119.200 . 1 144 36 36 LEU H H 8.725 . 1 145 36 36 LEU C C 177.600 . 1 146 36 36 LEU CA C 57.600 . 1 147 36 36 LEU CB C 40.090 . 1 148 36 36 LEU N N 122.700 . 1 149 37 37 ASN H H 8.168 . 1 150 37 37 ASN C C 177.000 . 1 151 37 37 ASN CA C 57.300 . 1 152 37 37 ASN CB C 38.830 . 1 153 37 37 ASN N N 117.600 . 1 154 38 38 ASN H H 7.991 . 1 155 38 38 ASN C C 177.800 . 1 156 38 38 ASN CA C 56.180 . 1 157 38 38 ASN CB C 37.760 . 1 158 38 38 ASN N N 117.500 . 1 159 39 39 ILE H H 8.389 . 1 160 39 39 ILE C C 178.800 . 1 161 39 39 ILE CA C 64.890 . 1 162 39 39 ILE CB C 37.700 . 1 163 39 39 ILE N N 121.500 . 1 164 40 40 LEU H H 8.366 . 1 165 40 40 LEU C C 179.500 . 1 166 40 40 LEU CA C 58.260 . 1 167 40 40 LEU CB C 39.320 . 1 168 40 40 LEU N N 120.400 . 1 169 41 41 GLU H H 8.065 . 1 170 41 41 GLU C C 177.700 . 1 171 41 41 GLU CA C 58.480 . 1 172 41 41 GLU CB C 29.420 . 1 173 41 41 GLU N N 117.300 . 1 174 42 42 LYS H H 8.008 . 1 175 42 42 LYS C C 178.500 . 1 176 42 42 LYS CA C 57.580 . 1 177 42 42 LYS CB C 32.560 . 1 178 42 42 LYS N N 116.500 . 1 179 43 43 GLU H H 8.495 . 1 180 43 43 GLU C C 177.000 . 1 181 43 43 GLU CA C 57.200 . 1 182 43 43 GLU CB C 30.070 . 1 183 43 43 GLU N N 117.700 . 1 184 44 44 PHE H H 7.529 . 1 185 44 44 PHE C C 175.700 . 1 186 44 44 PHE CA C 56.540 . 1 187 44 44 PHE CB C 39.150 . 1 188 44 44 PHE N N 116.800 . 1 189 45 45 LYS H H 7.619 . 1 190 45 45 LYS C C 178.500 . 1 191 45 45 LYS CA C 58.300 . 1 192 45 45 LYS CB C 30.330 . 1 193 45 45 LYS N N 122.400 . 1 194 46 46 GLY H H 9.112 . 1 195 46 46 GLY C C 174.400 . 1 196 46 46 GLY CA C 45.310 . 1 197 46 46 GLY N N 114.100 . 1 198 47 47 VAL H H 8.222 . 1 199 47 47 VAL C C 176.100 . 1 200 47 47 VAL CA C 64.540 . 1 201 47 47 VAL CB C 31.790 . 1 202 47 47 VAL N N 122.000 . 1 203 48 48 TYR H H 7.837 . 1 204 48 48 TYR C C 174.900 . 1 205 48 48 TYR CA C 55.760 . 1 206 48 48 TYR CB C 42.390 . 1 207 48 48 TYR N N 115.300 . 1 208 49 49 ALA H H 8.703 . 1 209 49 49 ALA C C 175.200 . 1 210 49 49 ALA CA C 50.260 . 1 211 49 49 ALA CB C 20.310 . 1 212 49 49 ALA N N 125.100 . 1 213 50 50 LEU H H 8.658 . 1 214 50 50 LEU C C 176.400 . 1 215 50 50 LEU CA C 53.890 . 1 216 50 50 LEU CB C 43.440 . 1 217 50 50 LEU N N 124.000 . 1 218 51 51 LYS H H 8.997 . 1 219 51 51 LYS C C 173.500 . 1 220 51 51 LYS CA C 54.910 . 1 221 51 51 LYS CB C 34.740 . 1 222 51 51 LYS N N 129.000 . 1 223 52 52 VAL H H 8.509 . 1 224 52 52 VAL C C 175.500 . 1 225 52 52 VAL CA C 61.150 . 1 226 52 52 VAL CB C 32.030 . 1 227 52 52 VAL N N 125.600 . 1 228 53 53 ILE H H 9.129 . 1 229 53 53 ILE C C 173.700 . 1 230 53 53 ILE CA C 60.650 . 1 231 53 53 ILE CB C 38.310 . 1 232 53 53 ILE N N 132.600 . 1 233 54 54 ASP H H 8.582 . 1 234 54 54 ASP C C 178.300 . 1 235 54 54 ASP CA C 51.430 . 1 236 54 54 ASP CB C 39.990 . 1 237 54 54 ASP N N 127.200 . 1 238 55 55 VAL H H 8.993 . 1 239 55 55 VAL C C 175.600 . 1 240 55 55 VAL CA C 62.800 . 1 241 55 55 VAL CB C 30.720 . 1 242 55 55 VAL N N 124.500 . 1 243 56 56 LEU H H 8.265 . 1 244 56 56 LEU C C 179.200 . 1 245 56 56 LEU CA C 56.090 . 1 246 56 56 LEU CB C 39.280 . 1 247 56 56 LEU N N 116.600 . 1 248 57 57 LYS H H 7.104 . 1 249 57 57 LYS C C 176.800 . 1 250 57 57 LYS CA C 56.430 . 1 251 57 57 LYS CB C 32.800 . 1 252 57 57 LYS N N 118.000 . 1 253 58 58 ASN H H 7.881 . 1 254 58 58 ASN C C 171.200 . 1 255 58 58 ASN CA C 51.140 . 1 256 58 58 ASN CB C 39.370 . 1 257 58 58 ASN N N 115.900 . 1 258 59 59 PRO C C 176.500 . 1 259 59 59 PRO CA C 64.900 . 1 260 59 59 PRO CB C 31.160 . 1 261 60 60 GLN H H 7.343 . 1 262 60 60 GLN C C 177.500 . 1 263 60 60 GLN CA C 56.810 . 1 264 60 60 GLN CB C 28.450 . 1 265 60 60 GLN N N 112.900 . 1 266 61 61 LEU H H 7.962 . 1 267 61 61 LEU C C 177.700 . 1 268 61 61 LEU CA C 55.000 . 1 269 61 61 LEU CB C 40.850 . 1 270 61 61 LEU N N 127.600 . 1 271 62 62 ALA H H 9.032 . 1 272 62 62 ALA C C 177.100 . 1 273 62 62 ALA CA C 50.800 . 1 274 62 62 ALA CB C 18.900 . 1 275 62 62 ALA N N 128.000 . 1 276 63 63 GLU H H 8.475 . 1 277 63 63 GLU C C 176.900 . 1 278 63 63 GLU CA C 59.840 . 1 279 63 63 GLU CB C 28.700 . 1 280 63 63 GLU N N 117.800 . 1 281 64 64 GLU H H 8.372 . 1 282 64 64 GLU C C 176.200 . 1 283 64 64 GLU CA C 56.750 . 1 284 64 64 GLU CB C 28.210 . 1 285 64 64 GLU N N 115.200 . 1 286 65 65 ASP H H 8.209 . 1 287 65 65 ASP C C 174.300 . 1 288 65 65 ASP CA C 54.280 . 1 289 65 65 ASP CB C 43.140 . 1 290 65 65 ASP N N 123.500 . 1 291 66 66 LYS H H 8.295 . 1 292 66 66 LYS C C 172.400 . 1 293 66 66 LYS CA C 54.400 . 1 294 66 66 LYS CB C 35.080 . 1 295 66 66 LYS N N 117.600 . 1 296 67 67 ILE H H 8.483 . 1 297 67 67 ILE C C 174.200 . 1 298 67 67 ILE CA C 60.890 . 1 299 67 67 ILE CB C 37.290 . 1 300 67 67 ILE N N 117.200 . 1 301 68 68 LEU H H 8.605 . 1 302 68 68 LEU C C 176.500 . 1 303 68 68 LEU CA C 52.190 . 1 304 68 68 LEU CB C 41.850 . 1 305 68 68 LEU N N 125.300 . 1 306 69 69 ALA H H 7.928 . 1 307 69 69 ALA C C 179.100 . 1 308 69 69 ALA CA C 52.480 . 1 309 69 69 ALA CB C 19.560 . 1 310 69 69 ALA N N 121.600 . 1 311 70 70 THR H H 9.099 . 1 312 70 70 THR C C 173.700 . 1 313 70 70 THR CA C 67.220 . 1 314 70 70 THR CB C 65.780 . 1 315 70 70 THR N N 120.900 . 1 316 71 71 PRO C C 178.200 . 1 317 71 71 PRO CA C 64.860 . 1 318 71 71 PRO CB C 30.280 . 1 319 72 72 THR H H 7.546 . 1 320 72 72 THR C C 175.400 . 1 321 72 72 THR CA C 64.920 . 1 322 72 72 THR CB C 68.210 . 1 323 72 72 THR N N 112.200 . 1 324 73 73 LEU H H 6.922 . 1 325 73 73 LEU C C 177.700 . 1 326 73 73 LEU CA C 54.240 . 1 327 73 73 LEU CB C 43.790 . 1 328 73 73 LEU N N 118.900 . 1 329 74 74 ALA H H 8.400 . 1 330 74 74 ALA C C 178.600 . 1 331 74 74 ALA CA C 55.490 . 1 332 74 74 ALA CB C 17.150 . 1 333 74 74 ALA N N 121.500 . 1 334 75 75 LYS H H 7.216 . 1 335 75 75 LYS C C 177.300 . 1 336 75 75 LYS CA C 57.700 . 1 337 75 75 LYS CB C 31.140 . 1 338 75 75 LYS N N 110.400 . 1 339 76 76 VAL H H 7.275 . 1 340 76 76 VAL C C 176.200 . 1 341 76 76 VAL CA C 60.930 . 1 342 76 76 VAL CB C 30.790 . 1 343 76 76 VAL N N 112.900 . 1 344 77 77 LEU H H 7.273 . 1 345 77 77 LEU C C 173.700 . 1 346 77 77 LEU CA C 51.650 . 1 347 77 77 LEU CB C 39.890 . 1 348 77 77 LEU N N 122.400 . 1 349 80 80 PRO C C 179.100 . 1 350 80 80 PRO CA C 65.580 . 1 351 80 80 PRO CB C 30.790 . 1 352 81 81 VAL H H 6.838 . 1 353 81 81 VAL C C 176.900 . 1 354 81 81 VAL CA C 64.340 . 1 355 81 81 VAL CB C 30.640 . 1 356 81 81 VAL N N 116.000 . 1 357 82 82 ARG H H 8.086 . 1 358 82 82 ARG C C 178.900 . 1 359 82 82 ARG CA C 59.620 . 1 360 82 82 ARG CB C 29.570 . 1 361 82 82 ARG N N 119.900 . 1 362 83 83 ARG H H 7.951 . 1 363 83 83 ARG C C 178.400 . 1 364 83 83 ARG CA C 59.060 . 1 365 83 83 ARG CB C 29.170 . 1 366 83 83 ARG N N 118.800 . 1 367 84 84 ILE H H 6.809 . 1 368 84 84 ILE C C 178.300 . 1 369 84 84 ILE CA C 64.030 . 1 370 84 84 ILE CB C 36.980 . 1 371 84 84 ILE N N 119.700 . 1 372 85 85 ILE H H 7.916 . 1 373 85 85 ILE C C 177.900 . 1 374 85 85 ILE CA C 64.540 . 1 375 85 85 ILE CB C 35.820 . 1 376 85 85 ILE N N 120.400 . 1 377 86 86 GLY H H 8.259 . 1 378 86 86 GLY C C 176.000 . 1 379 86 86 GLY CA C 46.800 . 1 380 86 86 GLY N N 108.700 . 1 381 87 87 ASP H H 7.765 . 1 382 87 87 ASP C C 179.900 . 1 383 87 87 ASP CA C 57.350 . 1 384 87 87 ASP CB C 39.450 . 1 385 87 87 ASP N N 124.100 . 1 386 88 88 LEU H H 8.420 . 1 387 88 88 LEU C C 177.700 . 1 388 88 88 LEU CA C 57.570 . 1 389 88 88 LEU CB C 42.130 . 1 390 88 88 LEU N N 121.200 . 1 391 89 89 SER H H 8.110 . 1 392 89 89 SER C C 174.900 . 1 393 89 89 SER CA C 60.450 . 1 394 89 89 SER CB C 63.450 . 1 395 89 89 SER N N 113.100 . 1 396 90 90 ASN H H 8.621 . 1 397 90 90 ASN C C 175.900 . 1 398 90 90 ASN CA C 54.940 . 1 399 90 90 ASN CB C 39.440 . 1 400 90 90 ASN N N 114.400 . 1 401 91 91 ARG H H 7.944 . 1 402 91 91 ARG C C 177.200 . 1 403 91 91 ARG CA C 57.570 . 1 404 91 91 ARG CB C 29.630 . 1 405 91 91 ARG N N 119.100 . 1 406 92 92 GLU H H 8.129 . 1 407 92 92 GLU C C 175.900 . 1 408 92 92 GLU CA C 55.660 . 1 409 92 92 GLU CB C 29.000 . 1 410 92 92 GLU N N 114.700 . 1 411 93 93 LYS H H 6.707 . 1 412 93 93 LYS C C 175.900 . 1 413 93 93 LYS CA C 56.970 . 1 414 93 93 LYS CB C 28.450 . 1 415 93 93 LYS N N 110.200 . 1 416 94 94 VAL H H 7.253 . 1 417 94 94 VAL C C 175.600 . 1 418 94 94 VAL CA C 60.340 . 1 419 94 94 VAL CB C 32.420 . 1 420 94 94 VAL N N 106.200 . 1 421 95 95 LEU H H 7.166 . 1 422 95 95 LEU C C 175.900 . 1 423 95 95 LEU CA C 54.840 . 1 424 95 95 LEU CB C 42.910 . 1 425 95 95 LEU N N 122.200 . 1 426 96 96 ILE H H 9.467 . 1 427 96 96 ILE C C 177.000 . 1 428 96 96 ILE CA C 61.920 . 1 429 96 96 ILE CB C 39.460 . 1 430 96 96 ILE N N 134.300 . 1 431 97 97 GLY H H 7.249 . 1 432 97 97 GLY C C 171.000 . 1 433 97 97 GLY CA C 44.570 . 1 434 97 97 GLY N N 102.900 . 1 435 98 98 LEU H H 9.160 . 1 436 98 98 LEU C C 175.500 . 1 437 98 98 LEU CA C 53.740 . 1 438 98 98 LEU CB C 47.130 . 1 439 98 98 LEU N N 118.600 . 1 440 99 99 ASP H H 8.946 . 1 441 99 99 ASP C C 174.100 . 1 442 99 99 ASP CA C 53.850 . 1 443 99 99 ASP CB C 43.690 . 1 444 99 99 ASP N N 115.000 . 1 445 100 100 LEU H H 8.128 . 1 446 100 100 LEU C C 175.000 . 1 447 100 100 LEU CA C 53.580 . 1 448 100 100 LEU CB C 44.710 . 1 449 100 100 LEU N N 124.900 . 1 450 101 101 LEU H H 9.225 . 1 451 101 101 LEU C C 175.000 . 1 452 101 101 LEU CA C 53.760 . 1 453 101 101 LEU CB C 41.030 . 1 454 101 101 LEU N N 130.900 . 1 455 102 102 ALA H H 8.054 . 1 456 102 102 ALA C C 182.200 . 1 457 102 102 ALA CA C 52.860 . 1 458 102 102 ALA CB C 19.800 . 1 459 102 102 ALA N N 133.700 . 1 stop_ save_