data_25622 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N chemical shift assignments for the thioredoxin-like fold of the single mutant D91R of dimeric KaiB from the Thermosynechococcus elongatus BP-1 cyanobacterial species ; _BMRB_accession_number 25622 _BMRB_flat_file_name bmr25622.str _Entry_type original _Submission_date 2015-05-16 _Accession_date 2015-05-16 _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" 77 "13C chemical shifts" 244 "15N chemical shifts" 77 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 25616 'KaiB dimer' 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' 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 'D91R single mutant of dimeric KaiB (thioredoxin-like fold)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'KaiB D91R mutant, chain 1' $FTBN94YYD91RF_fs 'KaiB D91R mutant, chain 2' $FTBN94YYD91RF_fs 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_FTBN94YYD91RF_fs _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FTBN94YYD91RF_fs _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 110 _Mol_residue_sequence ; DYKDDDDKMAPLRKTAVLKL YVAGNTPNSVRALKTLNNIL EKEFKGVYALKVIDVLKNPQ LAEEDKILATPTLAKVLPPP VRRIIGDLSNREKVLIGLRL LADYKDDDDK ; 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 ARG 100 100 LEU 101 101 LEU 102 102 ALA 103 103 ASP 104 104 TYR 105 105 LYS 106 106 ASP 107 107 ASP 108 108 ASP 109 109 ASP 110 110 LYS 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 $FTBN94YYD91RF_fs 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 $FTBN94YYD91RF_fs '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]-FLAG-TeKaiB-1-94-Y8A-Y94A-D91R-FLAG (1819 uM); Buffer; 20 mM Tris, 100 mM NaCl, pH 7.0, 10 uM DSS, 0.02% NaN3, 95%H2O/5%D2O; Volume: 320 uL; Tube: shaped ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FTBN94YYD91RF_fs 1819 uM '[U-99% 13C; U-98% 15N]' Tris 20 mM 'natural abundance' NaCl 100 mM 'natural abundance' DSS 10 uM 'natural abundance' NaNa3 0.02 % 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % '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 'data analysis' 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 . 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 equipped with a TCI cryoprobe and z-axis pulsed-field gradient capability' 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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 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' 0.1 . M pH 7.0 . 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 601.1299449 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 HSQC' '3D HNCACB' '3D HN(CO)CACB' '3D HN(CA)CO' '3D 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 'KaiB D91R mutant, 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 14 14 LYS C C 176.400 . 1 2 14 14 LYS CA C 56.140 . 1 3 14 14 LYS CB C 32.940 . 1 4 15 15 THR H H 8.049 . 1 5 15 15 THR C C 173.700 . 1 6 15 15 THR CA C 62.450 . 1 7 15 15 THR CB C 70.340 . 1 8 15 15 THR N N 116.500 . 1 9 16 16 ALA H H 8.016 . 1 10 16 16 ALA C C 176.600 . 1 11 16 16 ALA CA C 51.940 . 1 12 16 16 ALA CB C 21.120 . 1 13 16 16 ALA N N 127.300 . 1 14 17 17 VAL H H 8.985 . 1 15 17 17 VAL C C 175.300 . 1 16 17 17 VAL CA C 62.410 . 1 17 17 17 VAL CB C 35.220 . 1 18 17 17 VAL N N 121.100 . 1 19 18 18 LEU H H 8.972 . 1 20 18 18 LEU C C 175.700 . 1 21 18 18 LEU CA C 52.470 . 1 22 18 18 LEU CB C 44.940 . 1 23 18 18 LEU N N 126.800 . 1 24 19 19 LYS H H 9.349 . 1 25 19 19 LYS C C 173.800 . 1 26 19 19 LYS CA C 55.180 . 1 27 19 19 LYS CB C 36.310 . 1 28 19 19 LYS N N 120.500 . 1 29 20 20 LEU H H 8.390 . 1 30 20 20 LEU C C 173.900 . 1 31 20 20 LEU CA C 52.760 . 1 32 20 20 LEU CB C 44.920 . 1 33 20 20 LEU N N 124.300 . 1 34 21 21 TYR H H 9.530 . 1 35 21 21 TYR C C 175.900 . 1 36 21 21 TYR CA C 56.460 . 1 37 21 21 TYR CB C 39.020 . 1 38 21 21 TYR N N 127.100 . 1 39 22 22 VAL H H 9.160 . 1 40 22 22 VAL C C 173.900 . 1 41 22 22 VAL CA C 58.630 . 1 42 22 22 VAL CB C 35.850 . 1 43 22 22 VAL N N 114.800 . 1 44 23 23 ALA H H 8.354 . 1 45 23 23 ALA C C 176.300 . 1 46 23 23 ALA CA C 50.280 . 1 47 23 23 ALA CB C 18.610 . 1 48 23 23 ALA N N 124.300 . 1 49 24 24 GLY H H 8.617 . 1 50 24 24 GLY C C 172.400 . 1 51 24 24 GLY CA C 47.660 . 1 52 24 24 GLY N N 113.700 . 1 53 25 25 ASN H H 8.463 . 1 54 25 25 ASN C C 175.500 . 1 55 25 25 ASN CA C 51.840 . 1 56 25 25 ASN CB C 38.080 . 1 57 25 25 ASN N N 122.100 . 1 58 26 26 THR H H 7.860 . 1 59 26 26 THR C C 174.400 . 1 60 26 26 THR CA C 60.910 . 1 61 26 26 THR CB C 69.280 . 1 62 26 26 THR N N 113.300 . 1 63 29 29 SER C C 174.800 . 1 64 30 30 VAL H H 8.153 . 1 65 30 30 VAL C C 178.700 . 1 66 30 30 VAL CA C 66.970 . 1 67 30 30 VAL CB C 32.000 . 1 68 30 30 VAL N N 122.600 . 1 69 31 31 ARG H H 8.209 . 1 70 31 31 ARG C C 179.300 . 1 71 31 31 ARG CA C 59.780 . 1 72 31 31 ARG CB C 30.580 . 1 73 31 31 ARG N N 118.200 . 1 74 32 32 ALA H H 7.476 . 1 75 32 32 ALA C C 178.900 . 1 76 32 32 ALA CA C 54.780 . 1 77 32 32 ALA CB C 18.870 . 1 78 32 32 ALA N N 122.700 . 1 79 33 33 LEU H H 7.986 . 1 80 33 33 LEU C C 178.100 . 1 81 33 33 LEU CA C 58.410 . 1 82 33 33 LEU CB C 42.150 . 1 83 33 33 LEU N N 119.200 . 1 84 34 34 LYS H H 8.272 . 1 85 34 34 LYS C C 180.100 . 1 86 34 34 LYS CA C 59.920 . 1 87 34 34 LYS CB C 32.570 . 1 88 34 34 LYS N N 118.000 . 1 89 35 35 THR H H 8.080 . 1 90 35 35 THR CA C 67.250 . 1 91 35 35 THR CB C 68.940 . 1 92 35 35 THR N N 117.500 . 1 93 36 36 LEU H H 8.340 . 1 94 36 36 LEU C C 178.600 . 1 95 36 36 LEU CA C 57.930 . 1 96 36 36 LEU CB C 41.430 . 1 97 36 36 LEU N N 121.700 . 1 98 37 37 ASN H H 8.774 . 1 99 37 37 ASN C C 177.400 . 1 100 37 37 ASN CA C 56.520 . 1 101 37 37 ASN CB C 37.960 . 1 102 37 37 ASN N N 116.600 . 1 103 38 38 ASN H H 7.579 . 1 104 38 38 ASN C C 177.500 . 1 105 38 38 ASN CA C 57.290 . 1 106 38 38 ASN CB C 40.080 . 1 107 38 38 ASN N N 116.900 . 1 108 39 39 ILE H H 7.684 . 1 109 39 39 ILE C C 179.100 . 1 110 39 39 ILE CA C 65.260 . 1 111 39 39 ILE CB C 39.250 . 1 112 39 39 ILE N N 119.200 . 1 113 40 40 LEU H H 8.771 . 1 114 40 40 LEU C C 177.900 . 1 115 40 40 LEU CA C 57.880 . 1 116 40 40 LEU CB C 40.200 . 1 117 40 40 LEU N N 119.900 . 1 118 41 41 GLU H H 7.534 . 1 119 41 41 GLU C C 176.800 . 1 120 41 41 GLU CA C 56.980 . 1 121 41 41 GLU CB C 30.380 . 1 122 41 41 GLU N N 114.900 . 1 123 42 42 LYS H H 7.540 . 1 124 42 42 LYS C C 176.700 . 1 125 42 42 LYS CA C 57.120 . 1 126 42 42 LYS CB C 33.530 . 1 127 42 42 LYS N N 120.500 . 1 128 43 43 GLU H H 10.130 . 1 129 43 43 GLU C C 177.600 . 1 130 43 43 GLU CA C 60.600 . 1 131 43 43 GLU CB C 29.780 . 1 132 43 43 GLU N N 123.900 . 1 133 44 44 PHE H H 7.923 . 1 134 44 44 PHE C C 174.700 . 1 135 44 44 PHE CA C 57.460 . 1 136 44 44 PHE CB C 39.840 . 1 137 44 44 PHE N N 113.500 . 1 138 45 45 LYS H H 7.406 . 1 139 45 45 LYS C C 178.600 . 1 140 45 45 LYS CA C 58.750 . 1 141 45 45 LYS CB C 32.040 . 1 142 45 45 LYS N N 122.700 . 1 143 46 46 GLY H H 9.124 . 1 144 46 46 GLY C C 174.300 . 1 145 46 46 GLY CA C 45.850 . 1 146 46 46 GLY N N 115.400 . 1 147 47 47 VAL H H 7.991 . 1 148 47 47 VAL C C 175.300 . 1 149 47 47 VAL CA C 65.210 . 1 150 47 47 VAL CB C 33.310 . 1 151 47 47 VAL N N 120.500 . 1 152 48 48 TYR H H 7.976 . 1 153 48 48 TYR C C 175.700 . 1 154 48 48 TYR CA C 56.800 . 1 155 48 48 TYR CB C 42.660 . 1 156 48 48 TYR N N 114.300 . 1 157 49 49 ALA H H 8.743 . 1 158 49 49 ALA C C 175.300 . 1 159 49 49 ALA CA C 50.890 . 1 160 49 49 ALA CB C 20.880 . 1 161 49 49 ALA N N 124.500 . 1 162 50 50 LEU H H 8.588 . 1 163 50 50 LEU C C 175.800 . 1 164 50 50 LEU CA C 54.050 . 1 165 50 50 LEU CB C 45.070 . 1 166 50 50 LEU N N 122.900 . 1 167 51 51 LYS H H 9.010 . 1 168 51 51 LYS C C 174.000 . 1 169 51 51 LYS CA C 54.380 . 1 170 51 51 LYS CB C 34.160 . 1 171 51 51 LYS N N 128.700 . 1 172 52 52 VAL H H 8.561 . 1 173 52 52 VAL C C 175.800 . 1 174 52 52 VAL CA C 62.030 . 1 175 52 52 VAL CB C 32.650 . 1 176 52 52 VAL N N 124.900 . 1 177 53 53 ILE H H 9.193 . 1 178 53 53 ILE C C 173.700 . 1 179 53 53 ILE CA C 59.350 . 1 180 53 53 ILE CB C 39.150 . 1 181 53 53 ILE N N 130.900 . 1 182 54 54 ASP H H 8.894 . 1 183 54 54 ASP C C 178.700 . 1 184 54 54 ASP CA C 52.170 . 1 185 54 54 ASP CB C 40.910 . 1 186 54 54 ASP N N 126.800 . 1 187 55 55 VAL H H 9.393 . 1 188 55 55 VAL C C 177.100 . 1 189 55 55 VAL CA C 63.460 . 1 190 55 55 VAL CB C 30.820 . 1 191 55 55 VAL N N 121.300 . 1 192 56 56 LEU H H 8.680 . 1 193 56 56 LEU C C 179.200 . 1 194 56 56 LEU CA C 56.490 . 1 195 56 56 LEU CB C 40.800 . 1 196 56 56 LEU N N 120.300 . 1 197 57 57 LYS H H 7.171 . 1 198 57 57 LYS C C 176.600 . 1 199 57 57 LYS CA C 56.890 . 1 200 57 57 LYS CB C 33.840 . 1 201 57 57 LYS N N 118.000 . 1 202 58 58 ASN H H 7.850 . 1 203 58 58 ASN CA C 51.360 . 1 204 58 58 ASN CB C 40.040 . 1 205 58 58 ASN N N 114.600 . 1 206 59 59 PRO C C 179.500 . 1 207 59 59 PRO CA C 65.380 . 1 208 59 59 PRO CB C 31.390 . 1 209 60 60 GLN H H 8.820 . 1 210 60 60 GLN C C 178.400 . 1 211 60 60 GLN CA C 58.710 . 1 212 60 60 GLN CB C 27.320 . 1 213 60 60 GLN N N 119.500 . 1 214 61 61 LEU H H 7.521 . 1 215 61 61 LEU C C 178.700 . 1 216 61 61 LEU CA C 57.010 . 1 217 61 61 LEU CB C 41.430 . 1 218 61 61 LEU N N 120.000 . 1 219 62 62 ALA H H 7.226 . 1 220 62 62 ALA C C 178.800 . 1 221 62 62 ALA CA C 54.720 . 1 222 62 62 ALA CB C 18.200 . 1 223 62 62 ALA N N 119.700 . 1 224 63 63 GLU H H 7.611 . 1 225 63 63 GLU C C 180.100 . 1 226 63 63 GLU CA C 59.010 . 1 227 63 63 GLU CB C 29.430 . 1 228 63 63 GLU N N 117.100 . 1 229 66 66 LYS C C 175.300 . 1 230 66 66 LYS CB C 28.820 . 1 231 67 67 ILE H H 8.130 . 1 232 67 67 ILE C C 176.000 . 1 233 67 67 ILE CA C 58.320 . 1 234 67 67 ILE CB C 35.260 . 1 235 67 67 ILE N N 120.300 . 1 236 68 68 LEU H H 8.398 . 1 237 68 68 LEU C C 176.100 . 1 238 68 68 LEU CA C 55.060 . 1 239 68 68 LEU CB C 43.000 . 1 240 68 68 LEU N N 128.100 . 1 241 69 69 ALA H H 7.648 . 1 242 69 69 ALA C C 175.800 . 1 243 69 69 ALA CA C 51.230 . 1 244 69 69 ALA CB C 21.750 . 1 245 69 69 ALA N N 121.400 . 1 246 70 70 THR H H 8.289 . 1 247 70 70 THR C C 172.300 . 1 248 70 70 THR CA C 58.000 . 1 249 70 70 THR CB C 71.000 . 1 250 70 70 THR N N 109.000 . 1 251 71 71 PRO C C 176.100 . 1 252 71 71 PRO CA C 62.120 . 1 253 71 71 PRO CB C 33.980 . 1 254 72 72 THR H H 8.458 . 1 255 72 72 THR C C 171.000 . 1 256 72 72 THR CA C 62.850 . 1 257 72 72 THR CB C 73.370 . 1 258 72 72 THR N N 117.400 . 1 259 73 73 LEU H H 9.415 . 1 260 73 73 LEU C C 173.300 . 1 261 73 73 LEU CA C 53.400 . 1 262 73 73 LEU CB C 46.080 . 1 263 73 73 LEU N N 130.700 . 1 264 74 74 ALA H H 9.392 . 1 265 74 74 ALA C C 175.100 . 1 266 74 74 ALA CA C 50.450 . 1 267 74 74 ALA CB C 22.770 . 1 268 74 74 ALA N N 127.800 . 1 269 75 75 LYS H H 9.086 . 1 270 75 75 LYS C C 175.900 . 1 271 75 75 LYS CA C 56.570 . 1 272 75 75 LYS CB C 31.660 . 1 273 75 75 LYS N N 124.900 . 1 274 76 76 VAL H H 8.562 . 1 275 76 76 VAL C C 173.900 . 1 276 76 76 VAL CA C 61.920 . 1 277 76 76 VAL CB C 32.570 . 1 278 76 76 VAL N N 118.500 . 1 279 77 77 LEU H H 7.366 . 1 280 77 77 LEU C C 174.800 . 1 281 77 77 LEU CA C 52.700 . 1 282 77 77 LEU CB C 46.450 . 1 283 77 77 LEU N N 120.300 . 1 284 80 80 PRO C C 175.500 . 1 285 80 80 PRO CA C 61.640 . 1 286 80 80 PRO CB C 35.190 . 1 287 81 81 VAL H H 8.456 . 1 288 81 81 VAL C C 177.300 . 1 289 81 81 VAL CA C 63.370 . 1 290 81 81 VAL CB C 31.530 . 1 291 81 81 VAL N N 120.900 . 1 292 82 82 ARG H H 8.727 . 1 293 82 82 ARG C C 174.800 . 1 294 82 82 ARG CA C 54.250 . 1 295 82 82 ARG CB C 34.380 . 1 296 82 82 ARG N N 126.800 . 1 297 83 83 ARG H H 8.817 . 1 298 83 83 ARG C C 175.800 . 1 299 83 83 ARG CA C 55.840 . 1 300 83 83 ARG CB C 31.950 . 1 301 83 83 ARG N N 122.700 . 1 302 84 84 ILE H H 8.619 . 1 303 84 84 ILE C C 174.900 . 1 304 84 84 ILE CA C 60.630 . 1 305 84 84 ILE CB C 38.290 . 1 306 84 84 ILE N N 124.400 . 1 307 85 85 ILE H H 8.332 . 1 308 85 85 ILE C C 175.800 . 1 309 85 85 ILE CA C 60.480 . 1 310 85 85 ILE CB C 39.330 . 1 311 85 85 ILE N N 125.100 . 1 312 86 86 GLY H H 8.116 . 1 313 86 86 GLY C C 172.400 . 1 314 86 86 GLY CA C 44.130 . 1 315 86 86 GLY N N 111.400 . 1 316 88 88 LEU C C 175.400 . 1 317 88 88 LEU CA C 55.120 . 1 318 88 88 LEU CB C 41.130 . 1 319 89 89 SER H H 8.106 . 1 320 89 89 SER C C 173.900 . 1 321 89 89 SER CA C 58.600 . 1 322 89 89 SER CB C 64.300 . 1 323 89 89 SER N N 109.600 . 1 324 90 90 ASN H H 7.608 . 1 325 90 90 ASN C C 173.900 . 1 326 90 90 ASN CA C 52.320 . 1 327 90 90 ASN CB C 39.350 . 1 328 90 90 ASN N N 121.900 . 1 329 91 91 ARG H H 8.724 . 1 330 91 91 ARG C C 176.900 . 1 331 91 91 ARG CA C 60.250 . 1 332 91 91 ARG CB C 30.550 . 1 333 91 91 ARG N N 126.800 . 1 334 92 92 GLU H H 8.102 . 1 335 92 92 GLU C C 179.000 . 1 336 92 92 GLU CA C 60.190 . 1 337 92 92 GLU CB C 29.250 . 1 338 92 92 GLU N N 116.200 . 1 339 93 93 LYS H H 7.790 . 1 340 93 93 LYS C C 180.200 . 1 341 93 93 LYS CA C 58.670 . 1 342 93 93 LYS CB C 32.120 . 1 343 93 93 LYS N N 117.700 . 1 344 94 94 VAL H H 8.163 . 1 345 94 94 VAL C C 177.100 . 1 346 94 94 VAL N N 122.500 . 1 347 95 95 LEU C C 179.100 . 1 348 95 95 LEU CA C 59.270 . 1 349 95 95 LEU CB C 42.230 . 1 350 96 96 ILE H H 7.895 . 1 351 96 96 ILE C C 178.600 . 1 352 96 96 ILE CA C 65.390 . 1 353 96 96 ILE CB C 38.420 . 1 354 96 96 ILE N N 118.000 . 1 355 97 97 GLY H H 7.956 . 1 356 97 97 GLY C C 176.100 . 1 357 97 97 GLY CA C 47.410 . 1 358 97 97 GLY N N 107.500 . 1 359 98 98 LEU H H 8.587 . 1 360 98 98 LEU C C 180.200 . 1 361 98 98 LEU CA C 57.450 . 1 362 98 98 LEU CB C 41.700 . 1 363 98 98 LEU N N 120.700 . 1 364 99 99 ARG H H 8.436 . 1 365 99 99 ARG C C 179.100 . 1 366 99 99 ARG CA C 60.090 . 1 367 99 99 ARG CB C 30.060 . 1 368 99 99 ARG N N 121.200 . 1 369 100 100 LEU H H 8.081 . 1 370 100 100 LEU C C 179.400 . 1 371 100 100 LEU CA C 57.490 . 1 372 100 100 LEU CB C 41.870 . 1 373 100 100 LEU N N 119.700 . 1 374 101 101 LEU H H 7.548 . 1 375 101 101 LEU C C 178.200 . 1 376 101 101 LEU CA C 56.810 . 1 377 101 101 LEU CB C 41.860 . 1 378 101 101 LEU N N 117.400 . 1 379 102 102 ALA H H 7.529 . 1 380 102 102 ALA C C 177.700 . 1 381 102 102 ALA CA C 53.380 . 1 382 102 102 ALA CB C 18.670 . 1 383 102 102 ALA N N 120.500 . 1 384 103 103 ASP H H 7.861 . 1 385 103 103 ASP C C 176.100 . 1 386 103 103 ASP CA C 54.850 . 1 387 103 103 ASP CB C 41.060 . 1 388 103 103 ASP N N 118.000 . 1 389 104 104 TYR H H 7.732 . 1 390 104 104 TYR C C 175.500 . 1 391 104 104 TYR CA C 58.410 . 1 392 104 104 TYR CB C 38.780 . 1 393 104 104 TYR N N 119.800 . 1 394 105 105 LYS H H 8.143 . 1 395 105 105 LYS C C 176.000 . 1 396 105 105 LYS CA C 56.260 . 1 397 105 105 LYS CB C 33.200 . 1 398 105 105 LYS N N 123.500 . 1 stop_ save_