data_25625 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N chemical shift assignments for the double mutant G89A,D91R of KaiB in complex with the CI domain of KaiC from the Thermosynechococcus elongatus BP-1 cyanobacterial species ; _BMRB_accession_number 25625 _BMRB_flat_file_name bmr25625.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" 49 "13C chemical shifts" 155 "15N chemical shifts" 49 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' 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 'G89A,D91R double mutant of KaiB bound to CI' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'KaiB G89A D91R mutant, chian 1' $FTeKaiBGDF 'KaiB G89A D91R mutant, chain 2' $FTeKaiBGDF CI $FTeCI17247R41AK173AF 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_FTeKaiBGDF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FTeKaiBGDF _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 124 _Mol_residue_sequence ; DYKDDDDKMAPLRKTYVLKL YVAGNTPNSVRALKTLNNIL EKEFKGVYALKVIDVLKNPQ LAEEDKILATPTLAKVLPPP VRRIIGDLSNREKVLIALRL LYEEIGDQAEDDLGLEDYKD DDDK ; 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 TYR 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 ALA 98 98 LEU 99 99 ARG 100 100 LEU 101 101 LEU 102 102 TYR 103 103 GLU 104 104 GLU 105 105 ILE 106 106 GLY 107 107 ASP 108 108 GLN 109 109 ALA 110 110 GLU 111 111 ASP 112 112 ASP 113 113 LEU 114 114 GLY 115 115 LEU 116 116 GLU 117 117 ASP 118 118 TYR 119 119 LYS 120 120 ASP 121 121 ASP 122 122 ASP 123 123 ASP 124 124 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_FTeCI17247R41AK173AF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FTeCI17247R41AK173AF _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 247 _Mol_residue_sequence ; DYKDDDDKAEVKKIPTMIEG FDDISHGGLPQGATTLVSGT SGTGKTLFAVQFLYNGITIF NEPGIFVTFEESPQDIIKNA LSFGWNLQSLIDQGKLFILD ASPDPDGQEVAGDFDLSALI ERIQYAIRKYKATRVSIDSV TAVFQQYDAASVVRREIFRL AFRLAQLGVTTIMTTERVDE YGPVARFGVEEFVSDNVVIL RNVLEGERRRRTVEILKLRG TTHMKGEYPFTINNGINIFD YKDDDDK ; 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 ALA 10 10 GLU 11 11 VAL 12 12 LYS 13 13 LYS 14 14 ILE 15 15 PRO 16 16 THR 17 17 MET 18 18 ILE 19 19 GLU 20 20 GLY 21 21 PHE 22 22 ASP 23 23 ASP 24 24 ILE 25 25 SER 26 26 HIS 27 27 GLY 28 28 GLY 29 29 LEU 30 30 PRO 31 31 GLN 32 32 GLY 33 33 ALA 34 34 THR 35 35 THR 36 36 LEU 37 37 VAL 38 38 SER 39 39 GLY 40 40 THR 41 41 SER 42 42 GLY 43 43 THR 44 44 GLY 45 45 LYS 46 46 THR 47 47 LEU 48 48 PHE 49 49 ALA 50 50 VAL 51 51 GLN 52 52 PHE 53 53 LEU 54 54 TYR 55 55 ASN 56 56 GLY 57 57 ILE 58 58 THR 59 59 ILE 60 60 PHE 61 61 ASN 62 62 GLU 63 63 PRO 64 64 GLY 65 65 ILE 66 66 PHE 67 67 VAL 68 68 THR 69 69 PHE 70 70 GLU 71 71 GLU 72 72 SER 73 73 PRO 74 74 GLN 75 75 ASP 76 76 ILE 77 77 ILE 78 78 LYS 79 79 ASN 80 80 ALA 81 81 LEU 82 82 SER 83 83 PHE 84 84 GLY 85 85 TRP 86 86 ASN 87 87 LEU 88 88 GLN 89 89 SER 90 90 LEU 91 91 ILE 92 92 ASP 93 93 GLN 94 94 GLY 95 95 LYS 96 96 LEU 97 97 PHE 98 98 ILE 99 99 LEU 100 100 ASP 101 101 ALA 102 102 SER 103 103 PRO 104 104 ASP 105 105 PRO 106 106 ASP 107 107 GLY 108 108 GLN 109 109 GLU 110 110 VAL 111 111 ALA 112 112 GLY 113 113 ASP 114 114 PHE 115 115 ASP 116 116 LEU 117 117 SER 118 118 ALA 119 119 LEU 120 120 ILE 121 121 GLU 122 122 ARG 123 123 ILE 124 124 GLN 125 125 TYR 126 126 ALA 127 127 ILE 128 128 ARG 129 129 LYS 130 130 TYR 131 131 LYS 132 132 ALA 133 133 THR 134 134 ARG 135 135 VAL 136 136 SER 137 137 ILE 138 138 ASP 139 139 SER 140 140 VAL 141 141 THR 142 142 ALA 143 143 VAL 144 144 PHE 145 145 GLN 146 146 GLN 147 147 TYR 148 148 ASP 149 149 ALA 150 150 ALA 151 151 SER 152 152 VAL 153 153 VAL 154 154 ARG 155 155 ARG 156 156 GLU 157 157 ILE 158 158 PHE 159 159 ARG 160 160 LEU 161 161 ALA 162 162 PHE 163 163 ARG 164 164 LEU 165 165 ALA 166 166 GLN 167 167 LEU 168 168 GLY 169 169 VAL 170 170 THR 171 171 THR 172 172 ILE 173 173 MET 174 174 THR 175 175 THR 176 176 GLU 177 177 ARG 178 178 VAL 179 179 ASP 180 180 GLU 181 181 TYR 182 182 GLY 183 183 PRO 184 184 VAL 185 185 ALA 186 186 ARG 187 187 PHE 188 188 GLY 189 189 VAL 190 190 GLU 191 191 GLU 192 192 PHE 193 193 VAL 194 194 SER 195 195 ASP 196 196 ASN 197 197 VAL 198 198 VAL 199 199 ILE 200 200 LEU 201 201 ARG 202 202 ASN 203 203 VAL 204 204 LEU 205 205 GLU 206 206 GLY 207 207 GLU 208 208 ARG 209 209 ARG 210 210 ARG 211 211 ARG 212 212 THR 213 213 VAL 214 214 GLU 215 215 ILE 216 216 LEU 217 217 LYS 218 218 LEU 219 219 ARG 220 220 GLY 221 221 THR 222 222 THR 223 223 HIS 224 224 MET 225 225 LYS 226 226 GLY 227 227 GLU 228 228 TYR 229 229 PRO 230 230 PHE 231 231 THR 232 232 ILE 233 233 ASN 234 234 ASN 235 235 GLY 236 236 ILE 237 237 ASN 238 238 ILE 239 239 PHE 240 240 ASP 241 241 TYR 242 242 LYS 243 243 ASP 244 244 ASP 245 245 ASP 246 246 ASP 247 247 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 $FTeKaiBGDF 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 $FTeKaiBGDF '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-G89A-D91R-FLAG (650 uM) + FLAG-TeKaiC-17-247-R41A-K173A-FLAG (650 uM); Buffer: 25 mM Tris, 64 mM NaCl, 0.8 mM MgCl2, 0.8 mM ADP, pH 7.0, 10 uM DSS, 0.02% NaN3, 95%H2O/5%D2O, 1X Protease Inhibitor Cocktail; Volume: 350 uL; Tube: shaped ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FTeKaiBGDF 650 uM '[U-13C; U-15N; U-2H]' $FTeCI17247R41AK173AF 650 uM 'natural abundance' Tris 25 mM 'natural abundance' NaCl 64 mM 'natural abundance' MgCl2 0.8 mM 'natural abundance' ADP 0.8 mM 'natural abundance' DSS 10 uM 'natural abundance' 'Protease Inhibitor Cocktail' 650 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_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_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCA' _Sample_label $sample_1 save_ save_3D_TROSY_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CO)CA' _Sample_label $sample_1 save_ save_3D_TROSY_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CA)CO' _Sample_label $sample_1 save_ save_3D_TROSY_HNCO_7 _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' 0.064 . 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 601.129942 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 HNCA' '3D TROSY HN(CO)CA' '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 'KaiB G89A D91R mutant, chian 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 7 7 ASP C C 176.900 . 1 2 7 7 ASP CA C 54.350 . 1 3 7 7 ASP CB C 40.270 . 1 4 8 8 LYS H H 8.079 . 1 5 8 8 LYS C C 177.000 . 1 6 8 8 LYS CA C 56.320 . 1 7 8 8 LYS CB C 31.510 . 1 8 8 8 LYS N N 121.400 . 1 9 9 9 MET H H 8.109 . 1 10 9 9 MET C C 176.000 . 1 11 9 9 MET CA C 54.730 . 1 12 9 9 MET CB C 31.590 . 1 13 9 9 MET N N 119.900 . 1 14 10 10 ALA H H 7.998 . 1 15 10 10 ALA C C 175.600 . 1 16 10 10 ALA CA C 50.890 . 1 17 10 10 ALA CB C 17.070 . 1 18 10 10 ALA N N 126.700 . 1 19 16 16 TYR C C 175.700 . 1 20 16 16 TYR CA C 56.260 . 1 21 16 16 TYR CB C 38.900 . 1 22 17 17 VAL H H 8.830 . 1 23 17 17 VAL C C 175.300 . 1 24 17 17 VAL CA C 62.530 . 1 25 17 17 VAL CB C 33.130 . 1 26 17 17 VAL N N 124.600 . 1 27 18 18 LEU H H 8.822 . 1 28 18 18 LEU CA C 52.550 . 1 29 18 18 LEU CB C 44.050 . 1 30 18 18 LEU N N 128.800 . 1 31 19 19 LYS C C 173.900 . 1 32 19 19 LYS CA C 54.430 . 1 33 19 19 LYS CB C 35.270 . 1 34 20 20 LEU H H 8.668 . 1 35 20 20 LEU C C 173.900 . 1 36 20 20 LEU CA C 52.560 . 1 37 20 20 LEU CB C 44.120 . 1 38 20 20 LEU N N 125.300 . 1 39 21 21 TYR H H 9.668 . 1 40 21 21 TYR C C 176.500 . 1 41 21 21 TYR CA C 56.480 . 1 42 21 21 TYR CB C 38.300 . 1 43 21 21 TYR N N 127.700 . 1 44 22 22 VAL H H 9.074 . 1 45 22 22 VAL C C 174.100 . 1 46 22 22 VAL CA C 58.350 . 1 47 22 22 VAL CB C 34.690 . 1 48 22 22 VAL N N 116.300 . 1 49 23 23 ALA H H 8.437 . 1 50 23 23 ALA C C 175.800 . 1 51 23 23 ALA CA C 49.730 . 1 52 23 23 ALA CB C 18.010 . 1 53 23 23 ALA N N 124.000 . 1 54 24 24 GLY H H 8.759 . 1 55 24 24 GLY C C 172.300 . 1 56 24 24 GLY CA C 47.360 . 1 57 24 24 GLY N N 114.700 . 1 58 25 25 ASN H H 8.441 . 1 59 25 25 ASN C C 175.400 . 1 60 25 25 ASN CA C 51.410 . 1 61 25 25 ASN N N 123.200 . 1 62 26 26 THR H H 7.600 . 1 63 26 26 THR CA C 60.320 . 1 64 26 26 THR CB C 68.510 . 1 65 26 26 THR N N 112.100 . 1 66 31 31 ARG C C 179.000 . 1 67 31 31 ARG CA C 59.550 . 1 68 32 32 ALA H H 7.794 . 1 69 32 32 ALA C C 178.900 . 1 70 32 32 ALA CA C 55.030 . 1 71 32 32 ALA CB C 18.130 . 1 72 32 32 ALA N N 122.700 . 1 73 33 33 LEU H H 7.866 . 1 74 33 33 LEU C C 178.400 . 1 75 33 33 LEU CA C 57.840 . 1 76 33 33 LEU N N 118.200 . 1 77 34 34 LYS H H 7.878 . 1 78 34 34 LYS C C 180.300 . 1 79 34 34 LYS CA C 59.250 . 1 80 34 34 LYS N N 119.100 . 1 81 35 35 THR H H 8.387 . 1 82 35 35 THR C C 176.400 . 1 83 35 35 THR CA C 66.280 . 1 84 35 35 THR N N 118.100 . 1 85 36 36 LEU H H 8.855 . 1 86 36 36 LEU C C 178.300 . 1 87 36 36 LEU CA C 57.340 . 1 88 36 36 LEU N N 122.600 . 1 89 37 37 ASN H H 8.444 . 1 90 37 37 ASN C C 177.600 . 1 91 37 37 ASN CA C 56.360 . 1 92 37 37 ASN CB C 37.510 . 1 93 37 37 ASN N N 117.000 . 1 94 38 38 ASN H H 7.432 . 1 95 38 38 ASN C C 177.400 . 1 96 38 38 ASN CA C 56.580 . 1 97 38 38 ASN CB C 38.920 . 1 98 38 38 ASN N N 117.800 . 1 99 48 48 TYR C C 175.600 . 1 100 48 48 TYR CA C 56.450 . 1 101 49 49 ALA H H 8.727 . 1 102 49 49 ALA C C 175.300 . 1 103 49 49 ALA CA C 50.360 . 1 104 49 49 ALA CB C 20.020 . 1 105 49 49 ALA N N 125.300 . 1 106 50 50 LEU H H 8.528 . 1 107 50 50 LEU C C 175.600 . 1 108 50 50 LEU CA C 53.750 . 1 109 50 50 LEU CB C 43.570 . 1 110 50 50 LEU N N 124.100 . 1 111 51 51 LYS H H 8.804 . 1 112 51 51 LYS C C 173.900 . 1 113 51 51 LYS CA C 54.160 . 1 114 51 51 LYS CB C 33.270 . 1 115 51 51 LYS N N 129.700 . 1 116 52 52 VAL H H 8.525 . 1 117 52 52 VAL C C 176.000 . 1 118 52 52 VAL CA C 61.420 . 1 119 52 52 VAL CB C 31.510 . 1 120 52 52 VAL N N 126.500 . 1 121 53 53 ILE H H 9.135 . 1 122 53 53 ILE C C 173.500 . 1 123 53 53 ILE CA C 60.020 . 1 124 53 53 ILE CB C 39.510 . 1 125 53 53 ILE N N 131.500 . 1 126 54 54 ASP H H 8.981 . 1 127 54 54 ASP C C 179.000 . 1 128 54 54 ASP CA C 51.730 . 1 129 54 54 ASP CB C 40.450 . 1 130 54 54 ASP N N 127.700 . 1 131 55 55 VAL H H 9.459 . 1 132 55 55 VAL CA C 63.340 . 1 133 55 55 VAL N N 122.600 . 1 134 71 71 PRO C C 176.800 . 1 135 71 71 PRO CA C 62.740 . 1 136 71 71 PRO CB C 32.130 . 1 137 72 72 THR H H 8.384 . 1 138 72 72 THR C C 171.500 . 1 139 72 72 THR CA C 63.570 . 1 140 72 72 THR CB C 72.450 . 1 141 72 72 THR N N 116.400 . 1 142 73 73 LEU H H 9.673 . 1 143 73 73 LEU C C 173.300 . 1 144 73 73 LEU CA C 52.980 . 1 145 73 73 LEU N N 131.400 . 1 146 74 74 ALA H H 9.901 . 1 147 74 74 ALA C C 175.200 . 1 148 74 74 ALA CA C 49.940 . 1 149 74 74 ALA CB C 20.930 . 1 150 74 74 ALA N N 130.700 . 1 151 75 75 LYS H H 8.882 . 1 152 75 75 LYS C C 175.100 . 1 153 75 75 LYS CA C 55.380 . 1 154 75 75 LYS CB C 31.010 . 1 155 75 75 LYS N N 128.300 . 1 156 81 81 VAL C C 177.000 . 1 157 81 81 VAL CA C 62.330 . 1 158 81 81 VAL CB C 30.850 . 1 159 82 82 ARG H H 8.516 . 1 160 82 82 ARG C C 174.900 . 1 161 82 82 ARG CA C 53.470 . 1 162 82 82 ARG CB C 33.470 . 1 163 82 82 ARG N N 125.300 . 1 164 83 83 ARG H H 8.589 . 1 165 83 83 ARG C C 175.000 . 1 166 83 83 ARG CA C 54.790 . 1 167 83 83 ARG CB C 32.110 . 1 168 83 83 ARG N N 122.400 . 1 169 84 84 ILE H H 9.322 . 1 170 84 84 ILE C C 174.800 . 1 171 84 84 ILE CA C 59.070 . 1 172 84 84 ILE CB C 39.650 . 1 173 84 84 ILE N N 124.400 . 1 174 85 85 ILE H H 9.086 . 1 175 85 85 ILE C C 175.600 . 1 176 85 85 ILE CA C 59.160 . 1 177 85 85 ILE N N 124.500 . 1 178 86 86 GLY H H 8.375 . 1 179 86 86 GLY CA C 43.580 . 1 180 86 86 GLY N N 109.100 . 1 181 87 87 ASP H H 8.071 . 1 182 87 87 ASP CA C 54.660 . 1 183 87 87 ASP N N 116.900 . 1 184 89 89 SER C C 176.300 . 1 185 89 89 SER CA C 60.170 . 1 186 90 90 ASN H H 7.801 . 1 187 90 90 ASN C C 174.300 . 1 188 90 90 ASN CA C 51.140 . 1 189 90 90 ASN CB C 35.670 . 1 190 90 90 ASN N N 120.700 . 1 191 91 91 ARG H H 7.780 . 1 192 91 91 ARG C C 178.000 . 1 193 91 91 ARG CA C 59.320 . 1 194 91 91 ARG CB C 29.730 . 1 195 91 91 ARG N N 125.100 . 1 196 92 92 GLU H H 8.534 . 1 197 92 92 GLU C C 178.700 . 1 198 92 92 GLU CA C 59.470 . 1 199 92 92 GLU CB C 28.360 . 1 200 92 92 GLU N N 118.100 . 1 201 93 93 LYS H H 7.226 . 1 202 93 93 LYS CA C 58.710 . 1 203 93 93 LYS CB C 32.160 . 1 204 93 93 LYS N N 116.500 . 1 205 104 104 GLU C C 176.800 . 1 206 104 104 GLU CA C 56.220 . 1 207 104 104 GLU CB C 29.360 . 1 208 105 105 ILE H H 8.029 . 1 209 105 105 ILE C C 176.900 . 1 210 105 105 ILE CA C 61.410 . 1 211 105 105 ILE CB C 37.750 . 1 212 105 105 ILE N N 121.900 . 1 213 106 106 GLY H H 8.208 . 1 214 106 106 GLY C C 173.900 . 1 215 106 106 GLY CA C 44.870 . 1 216 106 106 GLY N N 112.200 . 1 217 113 113 LEU C C 178.300 . 1 218 113 113 LEU CA C 55.220 . 1 219 113 113 LEU CB C 41.100 . 1 220 114 114 GLY H H 8.416 . 1 221 114 114 GLY C C 174.500 . 1 222 114 114 GLY CA C 45.280 . 1 223 114 114 GLY N N 109.700 . 1 224 115 115 LEU H H 7.953 . 1 225 115 115 LEU C C 177.800 . 1 226 115 115 LEU CA C 54.920 . 1 227 115 115 LEU CB C 41.270 . 1 228 115 115 LEU N N 121.700 . 1 229 116 116 GLU H H 8.353 . 1 230 116 116 GLU C C 176.100 . 1 231 116 116 GLU CA C 56.160 . 1 232 116 116 GLU CB C 29.280 . 1 233 116 116 GLU N N 121.700 . 1 234 117 117 ASP H H 8.137 . 1 235 117 117 ASP C C 175.700 . 1 236 117 117 ASP CA C 53.900 . 1 237 117 117 ASP CB C 40.590 . 1 238 117 117 ASP N N 121.700 . 1 239 118 118 TYR H H 7.996 . 1 240 118 118 TYR C C 175.400 . 1 241 118 118 TYR CA C 57.690 . 1 242 118 118 TYR CB C 37.860 . 1 243 118 118 TYR N N 121.600 . 1 244 119 119 LYS H H 7.952 . 1 245 119 119 LYS C C 175.700 . 1 246 119 119 LYS CA C 55.310 . 1 247 119 119 LYS CB C 32.540 . 1 248 119 119 LYS N N 124.800 . 1 249 120 120 ASP H H 8.232 . 1 250 120 120 ASP C C 176.100 . 1 251 120 120 ASP CA C 53.950 . 1 252 120 120 ASP CB C 40.810 . 1 253 120 120 ASP N N 122.800 . 1 stop_ save_