data_25619 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N chemical shift assignments for N-SasA, the N-terminal domain of SasA, in complex with the CI domain of KaiC from the Thermosynechococcus elongatus BP-1 cyanobacterial species ; _BMRB_accession_number 25619 _BMRB_flat_file_name bmr25619.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" 69 "13C chemical shifts" 235 "15N chemical shifts" 69 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 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 'N-SasA bound to CI' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label N-SasA $FTeSasA16107P16AF 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_FTeSasA16107P16AF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FTeSasA16107P16AF _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 108 _Mol_residue_sequence ; DYKDDDDKALSLLLFVANRP GDEEETAAIQAHIQQLPSNF SFELKVVPIGEQPYLLEEYK LVATPALIKVRPEPRQTLAG RKLLQKVDYWWPRWQREVAL DYKDDDDK ; 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 LEU 11 11 SER 12 12 LEU 13 13 LEU 14 14 LEU 15 15 PHE 16 16 VAL 17 17 ALA 18 18 ASN 19 19 ARG 20 20 PRO 21 21 GLY 22 22 ASP 23 23 GLU 24 24 GLU 25 25 GLU 26 26 THR 27 27 ALA 28 28 ALA 29 29 ILE 30 30 GLN 31 31 ALA 32 32 HIS 33 33 ILE 34 34 GLN 35 35 GLN 36 36 LEU 37 37 PRO 38 38 SER 39 39 ASN 40 40 PHE 41 41 SER 42 42 PHE 43 43 GLU 44 44 LEU 45 45 LYS 46 46 VAL 47 47 VAL 48 48 PRO 49 49 ILE 50 50 GLY 51 51 GLU 52 52 GLN 53 53 PRO 54 54 TYR 55 55 LEU 56 56 LEU 57 57 GLU 58 58 GLU 59 59 TYR 60 60 LYS 61 61 LEU 62 62 VAL 63 63 ALA 64 64 THR 65 65 PRO 66 66 ALA 67 67 LEU 68 68 ILE 69 69 LYS 70 70 VAL 71 71 ARG 72 72 PRO 73 73 GLU 74 74 PRO 75 75 ARG 76 76 GLN 77 77 THR 78 78 LEU 79 79 ALA 80 80 GLY 81 81 ARG 82 82 LYS 83 83 LEU 84 84 LEU 85 85 GLN 86 86 LYS 87 87 VAL 88 88 ASP 89 89 TYR 90 90 TRP 91 91 TRP 92 92 PRO 93 93 ARG 94 94 TRP 95 95 GLN 96 96 ARG 97 97 GLU 98 98 VAL 99 99 ALA 100 100 LEU 101 101 ASP 102 102 TYR 103 103 LYS 104 104 ASP 105 105 ASP 106 106 ASP 107 107 ASP 108 108 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 $FTeSasA16107P16AF 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 $FTeSasA16107P16AF '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-TeSasA-16-107-P16A-FLAG (570 uM) + FLAG-TeKaiC-17-247-R41A-K173A-FLAG (600 uM); Buffer: 20 mM Tris, 50 mM NaCl, 1 mM MgCl2, 1 mM ADP, pH 7.0, 10 uM DSS, 0.02% NaN3, 95% H2O/5% D2O, 1X Protease Inhibitor Cocktail; Volume: 350 uL; Tube: shaped tube ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FTeSasA16107P16AF 570 uM '[U-13C; U-15N; U-2H]' $FTeCI17247R41AK173AF 600 uM 'natural abundance' 'Protease Inhibitor Cocktail' 570 uM 'natural abundance' Tris 20 mM 'natural abundance' NaCl 50 mM 'natural abundance' MgCl2 1 mM 'natural abundance' ADP 1 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_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' 0.05 . 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 carbons' 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 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 N-SasA _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 8 8 LYS C C 176.200 . 1 2 8 8 LYS CA C 54.450 . 1 3 8 8 LYS CB C 31.400 . 1 4 9 9 ALA H H 8.029 . 1 5 9 9 ALA C C 176.200 . 1 6 9 9 ALA CA C 53.180 . 1 7 9 9 ALA CB C 18.870 . 1 8 9 9 ALA N N 125.000 . 1 9 10 10 LEU H H 7.268 . 1 10 10 10 LEU C C 175.400 . 1 11 10 10 LEU CA C 53.200 . 1 12 10 10 LEU CB C 43.730 . 1 13 10 10 LEU N N 117.700 . 1 14 11 11 SER C C 172.800 . 1 15 11 11 SER CA C 56.910 . 1 16 11 11 SER CB C 63.820 . 1 17 12 12 LEU H H 8.674 . 1 18 12 12 LEU C C 175.900 . 1 19 12 12 LEU CA C 52.700 . 1 20 12 12 LEU CB C 44.980 . 1 21 12 12 LEU N N 127.200 . 1 22 13 13 LEU H H 9.176 . 1 23 13 13 LEU C C 174.400 . 1 24 13 13 LEU CA C 52.910 . 1 25 13 13 LEU CB C 45.010 . 1 26 13 13 LEU N N 124.700 . 1 27 14 14 LEU H H 8.868 . 1 28 14 14 LEU C C 173.600 . 1 29 14 14 LEU CA C 52.780 . 1 30 14 14 LEU CB C 43.540 . 1 31 14 14 LEU N N 125.600 . 1 32 15 15 PHE H H 9.809 . 1 33 15 15 PHE C C 175.800 . 1 34 15 15 PHE CA C 56.980 . 1 35 15 15 PHE CB C 39.710 . 1 36 15 15 PHE N N 128.300 . 1 37 16 16 VAL H H 7.687 . 1 38 16 16 VAL C C 175.100 . 1 39 16 16 VAL CA C 58.160 . 1 40 16 16 VAL CB C 34.770 . 1 41 16 16 VAL N N 114.100 . 1 42 17 17 ALA H H 9.439 . 1 43 17 17 ALA C C 176.800 . 1 44 17 17 ALA CA C 51.630 . 1 45 17 17 ALA CB C 18.470 . 1 46 17 17 ALA N N 126.800 . 1 47 18 18 ASN H H 8.276 . 1 48 18 18 ASN C C 175.600 . 1 49 18 18 ASN CA C 52.590 . 1 50 18 18 ASN CB C 37.760 . 1 51 18 18 ASN N N 117.200 . 1 52 19 19 ARG H H 8.505 . 1 53 19 19 ARG C C 174.800 . 1 54 19 19 ARG CA C 54.200 . 1 55 19 19 ARG CB C 27.770 . 1 56 19 19 ARG N N 122.200 . 1 57 20 20 PRO C C 178.000 . 1 58 20 20 PRO CA C 64.630 . 1 59 20 20 PRO CB C 30.360 . 1 60 21 21 GLY H H 9.033 . 1 61 21 21 GLY C C 175.700 . 1 62 21 21 GLY CA C 45.190 . 1 63 21 21 GLY N N 114.400 . 1 64 22 22 ASP C C 178.100 . 1 65 22 22 ASP CA C 55.700 . 1 66 22 22 ASP CB C 40.430 . 1 67 23 23 GLU H H 8.917 . 1 68 23 23 GLU C C 179.200 . 1 69 23 23 GLU CA C 59.920 . 1 70 23 23 GLU CB C 28.070 . 1 71 23 23 GLU N N 122.400 . 1 72 24 24 GLU H H 8.520 . 1 73 24 24 GLU C C 179.300 . 1 74 24 24 GLU CA C 59.120 . 1 75 24 24 GLU CB C 28.160 . 1 76 24 24 GLU N N 121.000 . 1 77 25 25 GLU H H 7.919 . 1 78 25 25 GLU C C 178.900 . 1 79 25 25 GLU CA C 58.860 . 1 80 25 25 GLU CB C 28.910 . 1 81 25 25 GLU N N 122.500 . 1 82 26 26 THR H H 8.367 . 1 83 26 26 THR C C 176.100 . 1 84 26 26 THR CA C 66.740 . 1 85 26 26 THR CB C 67.750 . 1 86 26 26 THR N N 118.200 . 1 87 27 27 ALA H H 7.925 . 1 88 27 27 ALA C C 180.500 . 1 89 27 27 ALA CA C 54.570 . 1 90 27 27 ALA CB C 16.960 . 1 91 27 27 ALA N N 123.300 . 1 92 28 28 ALA H H 7.879 . 1 93 28 28 ALA C C 181.400 . 1 94 28 28 ALA CA C 54.540 . 1 95 28 28 ALA CB C 17.120 . 1 96 28 28 ALA N N 122.200 . 1 97 29 29 ILE C C 177.700 . 1 98 29 29 ILE CA C 65.270 . 1 99 29 29 ILE CB C 37.200 . 1 100 30 30 GLN H H 8.058 . 1 101 30 30 GLN C C 177.500 . 1 102 30 30 GLN CA C 59.290 . 1 103 30 30 GLN CB C 28.480 . 1 104 30 30 GLN N N 118.200 . 1 105 31 31 ALA H H 8.207 . 1 106 31 31 ALA C C 179.800 . 1 107 31 31 ALA CA C 54.330 . 1 108 31 31 ALA CB C 17.170 . 1 109 31 31 ALA N N 120.000 . 1 110 32 32 HIS H H 7.799 . 1 111 32 32 HIS C C 178.200 . 1 112 32 32 HIS CA C 58.660 . 1 113 32 32 HIS CB C 29.580 . 1 114 32 32 HIS N N 116.200 . 1 115 33 33 ILE H H 7.841 . 1 116 33 33 ILE C C 177.200 . 1 117 33 33 ILE CA C 64.460 . 1 118 33 33 ILE CB C 36.470 . 1 119 33 33 ILE N N 118.000 . 1 120 34 34 GLN H H 8.023 . 1 121 34 34 GLN C C 176.800 . 1 122 34 34 GLN CA C 57.910 . 1 123 34 34 GLN CB C 27.620 . 1 124 34 34 GLN N N 115.300 . 1 125 35 35 GLN H H 7.004 . 1 126 35 35 GLN C C 176.100 . 1 127 35 35 GLN CA C 54.520 . 1 128 35 35 GLN CB C 28.430 . 1 129 35 35 GLN N N 114.400 . 1 130 36 36 LEU H H 7.070 . 1 131 36 36 LEU C C 174.900 . 1 132 36 36 LEU CA C 53.130 . 1 133 36 36 LEU CB C 37.700 . 1 134 36 36 LEU N N 125.200 . 1 135 37 37 PRO C C 177.700 . 1 136 37 37 PRO CA C 62.680 . 1 137 37 37 PRO CB C 30.730 . 1 138 38 38 SER H H 8.510 . 1 139 38 38 SER C C 174.300 . 1 140 38 38 SER CA C 56.700 . 1 141 38 38 SER CB C 64.720 . 1 142 38 38 SER N N 116.900 . 1 143 39 39 ASN H H 8.628 . 1 144 39 39 ASN C C 173.600 . 1 145 39 39 ASN CA C 53.310 . 1 146 39 39 ASN CB C 38.240 . 1 147 39 39 ASN N N 125.300 . 1 148 40 40 PHE H H 7.719 . 1 149 40 40 PHE C C 175.500 . 1 150 40 40 PHE CA C 55.120 . 1 151 40 40 PHE CB C 40.880 . 1 152 40 40 PHE N N 116.800 . 1 153 41 41 SER H H 8.940 . 1 154 41 41 SER C C 173.400 . 1 155 41 41 SER CA C 58.210 . 1 156 41 41 SER CB C 63.380 . 1 157 41 41 SER N N 118.900 . 1 158 42 42 PHE H H 8.218 . 1 159 42 42 PHE C C 173.000 . 1 160 42 42 PHE CA C 55.110 . 1 161 42 42 PHE CB C 42.740 . 1 162 42 42 PHE N N 118.500 . 1 163 43 43 GLU H H 8.375 . 1 164 43 43 GLU C C 173.300 . 1 165 43 43 GLU CA C 53.800 . 1 166 43 43 GLU CB C 32.320 . 1 167 43 43 GLU N N 120.200 . 1 168 44 44 LEU H H 8.599 . 1 169 44 44 LEU C C 174.800 . 1 170 44 44 LEU CA C 53.640 . 1 171 44 44 LEU CB C 43.310 . 1 172 44 44 LEU N N 126.900 . 1 173 45 45 LYS H H 8.363 . 1 174 45 45 LYS C C 174.200 . 1 175 45 45 LYS CA C 54.150 . 1 176 45 45 LYS CB C 33.590 . 1 177 45 45 LYS N N 128.200 . 1 178 46 46 VAL H H 8.635 . 1 179 46 46 VAL C C 175.600 . 1 180 46 46 VAL CA C 61.880 . 1 181 46 46 VAL CB C 31.000 . 1 182 46 46 VAL N N 126.300 . 1 183 47 47 VAL H H 9.342 . 1 184 47 47 VAL C C 172.800 . 1 185 47 47 VAL CA C 58.630 . 1 186 47 47 VAL CB C 32.330 . 1 187 47 47 VAL N N 131.900 . 1 188 49 49 ILE C C 176.100 . 1 189 50 50 GLY H H 8.540 . 1 190 50 50 GLY C C 175.400 . 1 191 50 50 GLY CA C 44.560 . 1 192 50 50 GLY N N 106.600 . 1 193 51 51 GLU H H 7.601 . 1 194 51 51 GLU CA C 57.020 . 1 195 51 51 GLU CB C 30.390 . 1 196 51 51 GLU N N 118.600 . 1 197 53 53 PRO C C 178.100 . 1 198 53 53 PRO CA C 64.700 . 1 199 54 54 TYR H H 7.249 . 1 200 54 54 TYR C C 178.400 . 1 201 54 54 TYR CA C 58.820 . 1 202 54 54 TYR CB C 35.750 . 1 203 54 54 TYR N N 115.900 . 1 204 55 55 LEU H H 7.210 . 1 205 55 55 LEU CA C 56.560 . 1 206 55 55 LEU CB C 41.560 . 1 207 55 55 LEU N N 121.900 . 1 208 56 56 LEU C C 178.800 . 1 209 57 57 GLU H H 6.962 . 1 210 57 57 GLU C C 178.800 . 1 211 57 57 GLU CA C 57.600 . 1 212 57 57 GLU N N 116.000 . 1 213 58 58 GLU H H 7.699 . 1 214 58 58 GLU C C 177.900 . 1 215 58 58 GLU CA C 58.760 . 1 216 58 58 GLU CB C 28.610 . 1 217 58 58 GLU N N 121.200 . 1 218 59 59 TYR H H 7.310 . 1 219 59 59 TYR C C 173.400 . 1 220 59 59 TYR CA C 57.180 . 1 221 59 59 TYR CB C 36.840 . 1 222 59 59 TYR N N 113.100 . 1 223 60 60 LYS H H 7.439 . 1 224 60 60 LYS C C 175.100 . 1 225 60 60 LYS CA C 56.470 . 1 226 60 60 LYS CB C 28.430 . 1 227 60 60 LYS N N 119.300 . 1 228 61 61 LEU H H 7.585 . 1 229 61 61 LEU CA C 55.160 . 1 230 61 61 LEU CB C 42.590 . 1 231 61 61 LEU N N 119.100 . 1 232 66 66 ALA C C 173.700 . 1 233 66 66 ALA CA C 51.550 . 1 234 66 66 ALA CB C 22.150 . 1 235 67 67 LEU H H 9.635 . 1 236 67 67 LEU C C 174.400 . 1 237 67 67 LEU CA C 52.630 . 1 238 67 67 LEU CB C 44.860 . 1 239 67 67 LEU N N 126.800 . 1 240 68 68 ILE H H 9.871 . 1 241 68 68 ILE C C 175.600 . 1 242 68 68 ILE CA C 58.800 . 1 243 68 68 ILE CB C 39.260 . 1 244 68 68 ILE N N 126.800 . 1 245 69 69 LYS H H 8.847 . 1 246 69 69 LYS C C 174.400 . 1 247 69 69 LYS CA C 54.960 . 1 248 69 69 LYS CB C 30.990 . 1 249 69 69 LYS N N 131.100 . 1 250 70 70 VAL H H 8.181 . 1 251 70 70 VAL C C 175.500 . 1 252 70 70 VAL CA C 62.670 . 1 253 70 70 VAL CB C 31.760 . 1 254 70 70 VAL N N 123.800 . 1 255 72 72 PRO C C 175.600 . 1 256 72 72 PRO CA C 61.770 . 1 257 72 72 PRO CB C 33.090 . 1 258 73 73 GLU H H 8.398 . 1 259 73 73 GLU C C 174.700 . 1 260 73 73 GLU CA C 55.590 . 1 261 73 73 GLU CB C 27.510 . 1 262 73 73 GLU N N 120.900 . 1 263 74 74 PRO C C 175.200 . 1 264 74 74 PRO CA C 61.000 . 1 265 74 74 PRO CB C 33.750 . 1 266 75 75 ARG H H 8.315 . 1 267 75 75 ARG C C 176.700 . 1 268 75 75 ARG CA C 55.940 . 1 269 75 75 ARG CB C 29.950 . 1 270 75 75 ARG N N 122.100 . 1 271 76 76 GLN H H 7.787 . 1 272 76 76 GLN C C 173.800 . 1 273 76 76 GLN CA C 54.920 . 1 274 76 76 GLN CB C 33.910 . 1 275 76 76 GLN N N 122.000 . 1 276 77 77 THR H H 8.613 . 1 277 77 77 THR C C 173.100 . 1 278 77 77 THR CA C 61.980 . 1 279 77 77 THR CB C 69.670 . 1 280 77 77 THR N N 121.400 . 1 281 78 78 LEU H H 9.559 . 1 282 78 78 LEU C C 174.300 . 1 283 78 78 LEU CA C 52.950 . 1 284 78 78 LEU CB C 42.550 . 1 285 78 78 LEU N N 129.800 . 1 286 79 79 ALA H H 8.932 . 1 287 79 79 ALA C C 177.100 . 1 288 79 79 ALA CA C 50.320 . 1 289 79 79 ALA CB C 22.100 . 1 290 79 79 ALA N N 125.200 . 1 291 80 80 GLY H H 8.389 . 1 292 80 80 GLY CA C 43.450 . 1 293 80 80 GLY N N 105.800 . 1 294 87 87 VAL CA C 66.750 . 1 295 88 88 ASP H H 8.032 . 1 296 88 88 ASP CA C 57.080 . 1 297 88 88 ASP CB C 39.010 . 1 298 88 88 ASP N N 118.900 . 1 299 89 89 TYR C C 176.800 . 1 300 89 89 TYR CA C 60.310 . 1 301 89 89 TYR CB C 37.520 . 1 302 90 90 TRP H H 8.044 . 1 303 90 90 TRP C C 177.400 . 1 304 90 90 TRP CA C 59.250 . 1 305 90 90 TRP CB C 28.200 . 1 306 90 90 TRP N N 118.400 . 1 307 91 91 TRP H H 8.908 . 1 308 91 91 TRP C C 174.500 . 1 309 91 91 TRP CA C 62.580 . 1 310 91 91 TRP CB C 25.380 . 1 311 91 91 TRP N N 121.700 . 1 312 92 92 PRO C C 180.100 . 1 313 92 92 PRO CA C 65.220 . 1 314 93 93 ARG H H 6.930 . 1 315 93 93 ARG C C 179.500 . 1 316 93 93 ARG CA C 58.740 . 1 317 93 93 ARG CB C 27.450 . 1 318 93 93 ARG N N 119.200 . 1 319 94 94 TRP H H 8.685 . 1 320 94 94 TRP C C 178.800 . 1 321 94 94 TRP CA C 57.220 . 1 322 94 94 TRP CB C 27.620 . 1 323 94 94 TRP N N 123.400 . 1 324 95 95 GLN H H 7.977 . 1 325 95 95 GLN C C 178.200 . 1 326 95 95 GLN CA C 57.870 . 1 327 95 95 GLN CB C 27.780 . 1 328 95 95 GLN N N 115.500 . 1 329 96 96 ARG H H 7.252 . 1 330 96 96 ARG C C 178.000 . 1 331 96 96 ARG CA C 57.890 . 1 332 96 96 ARG CB C 28.970 . 1 333 96 96 ARG N N 118.400 . 1 334 97 97 GLU H H 7.928 . 1 335 97 97 GLU C C 178.900 . 1 336 97 97 GLU CA C 58.220 . 1 337 97 97 GLU CB C 29.150 . 1 338 97 97 GLU N N 119.700 . 1 339 98 98 VAL H H 7.566 . 1 340 98 98 VAL C C 176.500 . 1 341 98 98 VAL CA C 63.550 . 1 342 98 98 VAL CB C 30.950 . 1 343 98 98 VAL N N 117.800 . 1 344 99 99 ALA H H 7.504 . 1 345 99 99 ALA C C 178.300 . 1 346 99 99 ALA CA C 52.730 . 1 347 99 99 ALA CB C 18.190 . 1 348 99 99 ALA N N 122.900 . 1 349 100 100 LEU H H 7.763 . 1 350 100 100 LEU C C 177.400 . 1 351 100 100 LEU CA C 55.580 . 1 352 100 100 LEU CB C 40.870 . 1 353 100 100 LEU N N 119.700 . 1 354 101 101 ASP H H 7.889 . 1 355 101 101 ASP C C 175.800 . 1 356 101 101 ASP CA C 53.870 . 1 357 101 101 ASP CB C 40.560 . 1 358 101 101 ASP N N 119.700 . 1 359 102 102 TYR H H 7.775 . 1 360 102 102 TYR C C 175.500 . 1 361 102 102 TYR CA C 57.880 . 1 362 102 102 TYR CB C 38.010 . 1 363 102 102 TYR N N 121.000 . 1 364 103 103 LYS H H 7.913 . 1 365 103 103 LYS C C 175.700 . 1 366 103 103 LYS CA C 55.440 . 1 367 103 103 LYS CB C 32.470 . 1 368 103 103 LYS N N 124.600 . 1 369 104 104 ASP H H 8.244 . 1 370 104 104 ASP C C 176.100 . 1 371 104 104 ASP CA C 53.980 . 1 372 104 104 ASP CB C 40.790 . 1 373 104 104 ASP N N 122.900 . 1 stop_ save_