data_25626 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N chemical shift assignments for the double mutant G88A,D90R of KaiB from the Synechococcus elongatus PCC 7942 cyanobacterial species ; _BMRB_accession_number 25626 _BMRB_flat_file_name bmr25626.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" 66 "13C chemical shifts" 208 "15N chemical shifts" 66 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' 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' 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 'G88A,D90R double mutant of KaiB' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'KaiB G88A D90R mutant, chain 1' $SeKaiBGDF 'KaiB G88A D90R mutant, chain 2' $SeKaiBGDF 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_SeKaiBGDF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SeKaiBGDF _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 110 _Mol_residue_sequence ; MSPRKTYILKLYVAGNTPNS VRALKTLKNILEVEFQGVYA LKVIDVLKNPQLAEEDKILA TPTLAKVLPLPVRRIIGDLS DREKVLIALRLLYGELQDSD DFDYKDDDDK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 SER 3 3 PRO 4 4 ARG 5 5 LYS 6 6 THR 7 7 TYR 8 8 ILE 9 9 LEU 10 10 LYS 11 11 LEU 12 12 TYR 13 13 VAL 14 14 ALA 15 15 GLY 16 16 ASN 17 17 THR 18 18 PRO 19 19 ASN 20 20 SER 21 21 VAL 22 22 ARG 23 23 ALA 24 24 LEU 25 25 LYS 26 26 THR 27 27 LEU 28 28 LYS 29 29 ASN 30 30 ILE 31 31 LEU 32 32 GLU 33 33 VAL 34 34 GLU 35 35 PHE 36 36 GLN 37 37 GLY 38 38 VAL 39 39 TYR 40 40 ALA 41 41 LEU 42 42 LYS 43 43 VAL 44 44 ILE 45 45 ASP 46 46 VAL 47 47 LEU 48 48 LYS 49 49 ASN 50 50 PRO 51 51 GLN 52 52 LEU 53 53 ALA 54 54 GLU 55 55 GLU 56 56 ASP 57 57 LYS 58 58 ILE 59 59 LEU 60 60 ALA 61 61 THR 62 62 PRO 63 63 THR 64 64 LEU 65 65 ALA 66 66 LYS 67 67 VAL 68 68 LEU 69 69 PRO 70 70 LEU 71 71 PRO 72 72 VAL 73 73 ARG 74 74 ARG 75 75 ILE 76 76 ILE 77 77 GLY 78 78 ASP 79 79 LEU 80 80 SER 81 81 ASP 82 82 ARG 83 83 GLU 84 84 LYS 85 85 VAL 86 86 LEU 87 87 ILE 88 88 ALA 89 89 LEU 90 90 ARG 91 91 LEU 92 92 LEU 93 93 TYR 94 94 GLY 95 95 GLU 96 96 LEU 97 97 GLN 98 98 ASP 99 99 SER 100 100 ASP 101 101 ASP 102 102 PHE 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 $SeKaiBGDF cyanobacteria 32046 Bacteria . Synechococcus 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 $SeKaiBGDF '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]-SeKaiB-G88A-D90R-FLAG (300 uM); Buffer: 20 mM Tris, 100 mM NaCl, pH 7.0, 10 uM DSS, 0.02% NaN3, 95%H2O/5%D2O; Volume: 350 uL; Tube: shaped ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SeKaiBGDF 300 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 'robust automatic backbone assignment of proteins' 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_HNCO_4 _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 601.129919 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 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 G88A D90R 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 3 3 PRO C C 176.700 . 1 2 3 3 PRO CA C 63.190 . 1 3 3 3 PRO CB C 32.040 . 1 4 4 4 ARG H H 8.433 . 1 5 4 4 ARG C C 176.200 . 1 6 4 4 ARG CA C 56.380 . 1 7 4 4 ARG CB C 30.890 . 1 8 4 4 ARG N N 121.600 . 1 9 5 5 LYS H H 8.180 . 1 10 5 5 LYS C C 175.300 . 1 11 5 5 LYS CA C 55.890 . 1 12 5 5 LYS CB C 33.510 . 1 13 5 5 LYS N N 122.400 . 1 14 6 6 THR H H 7.797 . 1 15 6 6 THR C C 173.500 . 1 16 6 6 THR CA C 61.900 . 1 17 6 6 THR CB C 70.280 . 1 18 6 6 THR N N 116.200 . 1 19 7 7 TYR H H 8.292 . 1 20 7 7 TYR C C 175.400 . 1 21 7 7 TYR CA C 55.760 . 1 22 7 7 TYR CB C 39.490 . 1 23 7 7 TYR N N 125.400 . 1 24 8 8 ILE H H 8.911 . 1 25 8 8 ILE C C 175.600 . 1 26 8 8 ILE CA C 60.470 . 1 27 8 8 ILE CB C 38.180 . 1 28 8 8 ILE N N 122.800 . 1 29 9 9 LEU H H 9.014 . 1 30 9 9 LEU C C 175.600 . 1 31 9 9 LEU CA C 52.390 . 1 32 9 9 LEU CB C 44.380 . 1 33 9 9 LEU N N 127.200 . 1 34 10 10 LYS H H 9.319 . 1 35 10 10 LYS C C 173.800 . 1 36 10 10 LYS CA C 54.940 . 1 37 10 10 LYS CB C 36.450 . 1 38 10 10 LYS N N 120.900 . 1 39 11 11 LEU H H 8.459 . 1 40 11 11 LEU C C 173.800 . 1 41 11 11 LEU CA C 52.740 . 1 42 11 11 LEU CB C 45.150 . 1 43 11 11 LEU N N 124.400 . 1 44 12 12 TYR H H 9.547 . 1 45 12 12 TYR C C 175.900 . 1 46 12 12 TYR CA C 56.440 . 1 47 12 12 TYR CB C 39.070 . 1 48 12 12 TYR N N 127.200 . 1 49 13 13 VAL H H 9.193 . 1 50 13 13 VAL C C 173.900 . 1 51 13 13 VAL CA C 58.650 . 1 52 13 13 VAL CB C 36.050 . 1 53 13 13 VAL N N 114.900 . 1 54 14 14 ALA H H 8.347 . 1 55 14 14 ALA C C 176.300 . 1 56 14 14 ALA CA C 50.100 . 1 57 14 14 ALA CB C 18.780 . 1 58 14 14 ALA N N 124.100 . 1 59 15 15 GLY H H 8.644 . 1 60 15 15 GLY C C 172.300 . 1 61 15 15 GLY CA C 47.800 . 1 62 15 15 GLY N N 113.800 . 1 63 16 16 ASN H H 8.474 . 1 64 16 16 ASN C C 175.600 . 1 65 16 16 ASN CA C 51.630 . 1 66 16 16 ASN CB C 38.060 . 1 67 16 16 ASN N N 122.300 . 1 68 17 17 THR H H 7.910 . 1 69 17 17 THR CA C 60.960 . 1 70 17 17 THR CB C 69.200 . 1 71 17 17 THR N N 113.900 . 1 72 20 20 SER C C 174.700 . 1 73 21 21 VAL H H 8.174 . 1 74 21 21 VAL C C 178.700 . 1 75 21 21 VAL CA C 66.610 . 1 76 21 21 VAL CB C 31.920 . 1 77 21 21 VAL N N 122.700 . 1 78 22 22 ARG H H 8.171 . 1 79 22 22 ARG C C 179.300 . 1 80 22 22 ARG CA C 59.470 . 1 81 22 22 ARG CB C 30.630 . 1 82 22 22 ARG N N 118.300 . 1 83 23 23 ALA H H 7.469 . 1 84 23 23 ALA C C 178.800 . 1 85 23 23 ALA CA C 54.860 . 1 86 23 23 ALA CB C 19.240 . 1 87 23 23 ALA N N 122.600 . 1 88 24 24 LEU H H 8.091 . 1 89 24 24 LEU C C 177.900 . 1 90 24 24 LEU CA C 58.580 . 1 91 24 24 LEU CB C 42.000 . 1 92 24 24 LEU N N 118.800 . 1 93 25 25 LYS H H 8.226 . 1 94 25 25 LYS C C 179.900 . 1 95 25 25 LYS CA C 59.900 . 1 96 25 25 LYS CB C 32.630 . 1 97 25 25 LYS N N 117.500 . 1 98 26 26 THR H H 8.053 . 1 99 26 26 THR C C 175.700 . 1 100 26 26 THR CA C 67.000 . 1 101 26 26 THR CB C 68.860 . 1 102 26 26 THR N N 117.100 . 1 103 27 27 LEU H H 8.332 . 1 104 27 27 LEU C C 178.600 . 1 105 27 27 LEU CA C 57.540 . 1 106 27 27 LEU CB C 41.380 . 1 107 27 27 LEU N N 121.600 . 1 108 28 28 LYS H H 8.687 . 1 109 28 28 LYS C C 178.800 . 1 110 28 28 LYS CA C 60.610 . 1 111 28 28 LYS CB C 32.030 . 1 112 28 28 LYS N N 116.900 . 1 113 29 29 ASN H H 7.490 . 1 114 29 29 ASN C C 177.200 . 1 115 29 29 ASN CA C 57.250 . 1 116 29 29 ASN CB C 40.140 . 1 117 29 29 ASN N N 115.500 . 1 118 30 30 ILE H H 7.839 . 1 119 30 30 ILE C C 178.300 . 1 120 30 30 ILE CA C 65.430 . 1 121 30 30 ILE CB C 38.810 . 1 122 30 30 ILE N N 119.000 . 1 123 31 31 LEU H H 8.512 . 1 124 31 31 LEU CA C 58.130 . 1 125 31 31 LEU CB C 40.090 . 1 126 31 31 LEU N N 118.400 . 1 127 39 39 TYR CA C 56.040 . 1 128 39 39 TYR CB C 42.330 . 1 129 40 40 ALA H H 8.795 . 1 130 40 40 ALA C C 174.900 . 1 131 40 40 ALA CA C 50.910 . 1 132 40 40 ALA CB C 21.350 . 1 133 40 40 ALA N N 124.700 . 1 134 41 41 LEU H H 8.602 . 1 135 41 41 LEU C C 175.800 . 1 136 41 41 LEU CA C 53.810 . 1 137 41 41 LEU CB C 45.280 . 1 138 41 41 LEU N N 122.800 . 1 139 42 42 LYS H H 9.041 . 1 140 42 42 LYS C C 174.100 . 1 141 42 42 LYS CA C 54.470 . 1 142 42 42 LYS CB C 34.130 . 1 143 42 42 LYS N N 128.700 . 1 144 43 43 VAL H H 8.582 . 1 145 43 43 VAL C C 175.700 . 1 146 43 43 VAL CA C 61.970 . 1 147 43 43 VAL CB C 32.840 . 1 148 43 43 VAL N N 124.700 . 1 149 44 44 ILE H H 9.159 . 1 150 44 44 ILE C C 173.700 . 1 151 44 44 ILE CA C 58.870 . 1 152 44 44 ILE CB C 39.170 . 1 153 44 44 ILE N N 130.800 . 1 154 45 45 ASP H H 8.949 . 1 155 45 45 ASP C C 178.700 . 1 156 45 45 ASP CA C 51.900 . 1 157 45 45 ASP CB C 40.960 . 1 158 45 45 ASP N N 126.900 . 1 159 46 46 VAL H H 9.403 . 1 160 46 46 VAL C C 177.100 . 1 161 46 46 VAL CA C 63.070 . 1 162 46 46 VAL CB C 30.820 . 1 163 46 46 VAL N N 121.200 . 1 164 47 47 LEU H H 8.676 . 1 165 47 47 LEU C C 179.200 . 1 166 47 47 LEU CA C 56.370 . 1 167 47 47 LEU CB C 40.920 . 1 168 47 47 LEU N N 120.300 . 1 169 48 48 LYS H H 7.191 . 1 170 48 48 LYS CA C 56.880 . 1 171 48 48 LYS CB C 33.890 . 1 172 48 48 LYS N N 118.100 . 1 173 50 50 PRO C C 179.500 . 1 174 50 50 PRO CA C 65.280 . 1 175 50 50 PRO CB C 31.340 . 1 176 51 51 GLN H H 8.839 . 1 177 51 51 GLN C C 178.400 . 1 178 51 51 GLN CA C 58.650 . 1 179 51 51 GLN CB C 27.360 . 1 180 51 51 GLN N N 119.600 . 1 181 52 52 LEU H H 7.525 . 1 182 52 52 LEU C C 178.700 . 1 183 52 52 LEU CA C 56.970 . 1 184 52 52 LEU CB C 41.350 . 1 185 52 52 LEU N N 120.000 . 1 186 53 53 ALA H H 7.222 . 1 187 53 53 ALA C C 178.800 . 1 188 53 53 ALA CA C 54.670 . 1 189 53 53 ALA CB C 18.290 . 1 190 53 53 ALA N N 119.700 . 1 191 54 54 GLU H H 7.624 . 1 192 54 54 GLU C C 180.100 . 1 193 54 54 GLU CA C 58.930 . 1 194 54 54 GLU CB C 29.520 . 1 195 54 54 GLU N N 117.200 . 1 196 55 55 GLU H H 8.236 . 1 197 55 55 GLU C C 177.800 . 1 198 55 55 GLU CA C 59.160 . 1 199 55 55 GLU CB C 29.620 . 1 200 55 55 GLU N N 120.900 . 1 201 56 56 ASP H H 7.697 . 1 202 56 56 ASP C C 174.400 . 1 203 56 56 ASP CA C 53.980 . 1 204 56 56 ASP CB C 39.770 . 1 205 56 56 ASP N N 116.700 . 1 206 57 57 LYS H H 7.643 . 1 207 57 57 LYS C C 175.300 . 1 208 57 57 LYS CA C 56.640 . 1 209 57 57 LYS CB C 29.070 . 1 210 57 57 LYS N N 117.200 . 1 211 58 58 ILE H H 8.134 . 1 212 58 58 ILE C C 176.000 . 1 213 58 58 ILE CA C 58.340 . 1 214 58 58 ILE CB C 35.370 . 1 215 58 58 ILE N N 120.200 . 1 216 59 59 LEU H H 8.424 . 1 217 59 59 LEU C C 176.200 . 1 218 59 59 LEU CA C 54.990 . 1 219 59 59 LEU CB C 42.850 . 1 220 59 59 LEU N N 128.100 . 1 221 60 60 ALA H H 7.654 . 1 222 60 60 ALA C C 175.900 . 1 223 60 60 ALA CA C 51.250 . 1 224 60 60 ALA CB C 21.790 . 1 225 60 60 ALA N N 121.500 . 1 226 61 61 THR H H 8.310 . 1 227 61 61 THR CA C 57.950 . 1 228 61 61 THR CB C 70.990 . 1 229 61 61 THR N N 109.100 . 1 230 63 63 THR C C 171.000 . 1 231 63 63 THR CA C 62.830 . 1 232 63 63 THR CB C 73.370 . 1 233 64 64 LEU H H 9.505 . 1 234 64 64 LEU C C 173.500 . 1 235 64 64 LEU CA C 53.320 . 1 236 64 64 LEU CB C 46.120 . 1 237 64 64 LEU N N 130.800 . 1 238 65 65 ALA H H 9.395 . 1 239 65 65 ALA C C 175.300 . 1 240 65 65 ALA CA C 50.520 . 1 241 65 65 ALA CB C 22.730 . 1 242 65 65 ALA N N 127.400 . 1 243 66 66 LYS H H 9.039 . 1 244 66 66 LYS C C 176.000 . 1 245 66 66 LYS CA C 56.330 . 1 246 66 66 LYS CB C 31.020 . 1 247 66 66 LYS N N 124.200 . 1 248 67 67 VAL H H 8.796 . 1 249 67 67 VAL C C 173.600 . 1 250 67 67 VAL CA C 61.440 . 1 251 67 67 VAL CB C 32.260 . 1 252 67 67 VAL N N 118.900 . 1 253 68 68 LEU H H 7.295 . 1 254 68 68 LEU CA C 52.950 . 1 255 68 68 LEU CB C 47.020 . 1 256 68 68 LEU N N 120.300 . 1 257 75 75 ILE C C 174.700 . 1 258 75 75 ILE CA C 60.970 . 1 259 75 75 ILE CB C 37.590 . 1 260 76 76 ILE H H 8.243 . 1 261 76 76 ILE C C 175.600 . 1 262 76 76 ILE CA C 60.470 . 1 263 76 76 ILE CB C 39.060 . 1 264 76 76 ILE N N 125.300 . 1 265 77 77 GLY H H 8.101 . 1 266 77 77 GLY C C 172.200 . 1 267 77 77 GLY CA C 44.120 . 1 268 77 77 GLY N N 111.800 . 1 269 78 78 ASP H H 8.033 . 1 270 78 78 ASP CA C 53.590 . 1 271 78 78 ASP CB C 40.830 . 1 272 78 78 ASP N N 118.700 . 1 273 85 85 VAL C C 177.200 . 1 274 85 85 VAL CA C 67.230 . 1 275 86 86 LEU H H 8.421 . 1 276 86 86 LEU C C 178.800 . 1 277 86 86 LEU CA C 59.230 . 1 278 86 86 LEU CB C 42.040 . 1 279 86 86 LEU N N 121.200 . 1 280 87 87 ILE H H 7.991 . 1 281 87 87 ILE C C 178.400 . 1 282 87 87 ILE CA C 65.430 . 1 283 87 87 ILE CB C 38.350 . 1 284 87 87 ILE N N 118.200 . 1 285 88 88 ALA H H 7.812 . 1 286 88 88 ALA C C 181.400 . 1 287 88 88 ALA CA C 55.380 . 1 288 88 88 ALA CB C 18.250 . 1 289 88 88 ALA N N 121.800 . 1 290 89 89 LEU H H 8.701 . 1 291 89 89 LEU CA C 57.310 . 1 292 89 89 LEU CB C 41.680 . 1 293 89 89 LEU N N 118.000 . 1 294 96 96 LEU C C 178.600 . 1 295 97 97 GLN H H 8.030 . 1 296 97 97 GLN C C 176.700 . 1 297 97 97 GLN CA C 56.970 . 1 298 97 97 GLN CB C 29.290 . 1 299 97 97 GLN N N 118.900 . 1 300 98 98 ASP H H 7.953 . 1 301 98 98 ASP C C 175.200 . 1 302 98 98 ASP CA C 55.010 . 1 303 98 98 ASP CB C 41.060 . 1 304 98 98 ASP N N 119.700 . 1 305 99 99 SER H H 8.181 . 1 306 99 99 SER C C 174.400 . 1 307 99 99 SER CA C 58.590 . 1 308 99 99 SER CB C 64.270 . 1 309 99 99 SER N N 109.800 . 1 310 100 100 ASP H H 8.325 . 1 311 100 100 ASP CA C 54.700 . 1 312 100 100 ASP CB C 41.330 . 1 313 100 100 ASP N N 122.700 . 1 314 101 101 ASP C C 176.000 . 1 315 101 101 ASP CA C 54.310 . 1 316 101 101 ASP CB C 41.040 . 1 317 102 102 PHE H H 8.079 . 1 318 102 102 PHE C C 175.200 . 1 319 102 102 PHE CA C 57.850 . 1 320 102 102 PHE CB C 39.700 . 1 321 102 102 PHE N N 120.400 . 1 322 103 103 ASP H H 8.214 . 1 323 103 103 ASP C C 175.400 . 1 324 103 103 ASP CA C 53.920 . 1 325 103 103 ASP CB C 41.220 . 1 326 103 103 ASP N N 121.700 . 1 327 104 104 TYR H H 7.977 . 1 328 104 104 TYR C C 175.300 . 1 329 104 104 TYR CA C 58.180 . 1 330 104 104 TYR CB C 38.800 . 1 331 104 104 TYR N N 121.200 . 1 332 105 105 LYS H H 8.122 . 1 333 105 105 LYS C C 175.700 . 1 334 105 105 LYS CA C 55.720 . 1 335 105 105 LYS CB C 33.540 . 1 336 105 105 LYS N N 123.800 . 1 337 106 106 ASP H H 8.361 . 1 338 106 106 ASP CA C 54.330 . 1 339 106 106 ASP CB C 41.420 . 1 340 106 106 ASP N N 122.200 . 1 stop_ save_