data_25623 ####################### # 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 dimeric KaiB from the Thermosynechococcus elongatus BP-1 cyanobacterial species ; _BMRB_accession_number 25623 _BMRB_flat_file_name bmr25623.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" 85 "13C chemical shifts" 271 "15N chemical shifts" 85 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)' 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 'G89A,D91R double mutant of dimeric KaiB' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'KaiB G89A D91R mutant, chain 1' $FTeKaiBN94YYGD 'KaiB G89A D91R mutant, chain 2' $FTeKaiBN94YYGD 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_FTeKaiBN94YYGD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FTeKaiBN94YYGD _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 102 _Mol_residue_sequence ; DYKDDDDKMAPLRKTAVLKL YVAGNTPNSVRALKTLNNIL EKEFKGVYALKVIDVLKNPQ LAEEDKILATPTLAKVLPPP VRRIIGDLSNREKVLIALRL LA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ASP 2 2 TYR 3 3 LYS 4 4 ASP 5 5 ASP 6 6 ASP 7 7 ASP 8 8 LYS 9 9 MET 10 10 ALA 11 11 PRO 12 12 LEU 13 13 ARG 14 14 LYS 15 15 THR 16 16 ALA 17 17 VAL 18 18 LEU 19 19 LYS 20 20 LEU 21 21 TYR 22 22 VAL 23 23 ALA 24 24 GLY 25 25 ASN 26 26 THR 27 27 PRO 28 28 ASN 29 29 SER 30 30 VAL 31 31 ARG 32 32 ALA 33 33 LEU 34 34 LYS 35 35 THR 36 36 LEU 37 37 ASN 38 38 ASN 39 39 ILE 40 40 LEU 41 41 GLU 42 42 LYS 43 43 GLU 44 44 PHE 45 45 LYS 46 46 GLY 47 47 VAL 48 48 TYR 49 49 ALA 50 50 LEU 51 51 LYS 52 52 VAL 53 53 ILE 54 54 ASP 55 55 VAL 56 56 LEU 57 57 LYS 58 58 ASN 59 59 PRO 60 60 GLN 61 61 LEU 62 62 ALA 63 63 GLU 64 64 GLU 65 65 ASP 66 66 LYS 67 67 ILE 68 68 LEU 69 69 ALA 70 70 THR 71 71 PRO 72 72 THR 73 73 LEU 74 74 ALA 75 75 LYS 76 76 VAL 77 77 LEU 78 78 PRO 79 79 PRO 80 80 PRO 81 81 VAL 82 82 ARG 83 83 ARG 84 84 ILE 85 85 ILE 86 86 GLY 87 87 ASP 88 88 LEU 89 89 SER 90 90 ASN 91 91 ARG 92 92 GLU 93 93 LYS 94 94 VAL 95 95 LEU 96 96 ILE 97 97 ALA 98 98 LEU 99 99 ARG 100 100 LEU 101 101 LEU 102 102 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $FTeKaiBN94YYGD 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 $FTeKaiBN94YYGD '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-G89A-D91R (800 uM); Buffer: 20 mM Tris, 50 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 $FTeKaiBN94YYGD 800 uM '[U-99% 13C; U-98% 15N]' Tris 20 mM 'natural abundance' NaCl 50 mM 'natural abundance' DSS 10 uM 'natural abundance' NaNa3 0.02 % 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' 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_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' 0.05 . 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 protons' MHz 601.129947 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 G89A 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 8 8 LYS C C 177.200 . 1 2 8 8 LYS CA C 57.070 . 1 3 8 8 LYS CB C 32.310 . 1 4 9 9 MET H H 8.156 . 1 5 9 9 MET C C 176.100 . 1 6 9 9 MET CA C 55.100 . 1 7 9 9 MET CB C 32.350 . 1 8 9 9 MET N N 118.300 . 1 9 10 10 ALA H H 7.979 . 1 10 10 10 ALA C C 175.700 . 1 11 10 10 ALA CA C 51.940 . 1 12 10 10 ALA CB C 17.740 . 1 13 10 10 ALA N N 125.600 . 1 14 11 11 PRO C C 177.100 . 1 15 11 11 PRO CA C 63.730 . 1 16 11 11 PRO CB C 31.820 . 1 17 12 12 LEU H H 8.121 . 1 18 12 12 LEU C C 177.400 . 1 19 12 12 LEU CA C 55.320 . 1 20 12 12 LEU CB C 42.180 . 1 21 12 12 LEU N N 120.600 . 1 22 13 13 ARG H H 8.147 . 1 23 13 13 ARG C C 176.000 . 1 24 13 13 ARG CA C 56.270 . 1 25 13 13 ARG CB C 30.730 . 1 26 13 13 ARG N N 121.400 . 1 27 14 14 LYS H H 8.277 . 1 28 14 14 LYS C C 176.300 . 1 29 14 14 LYS CA C 56.280 . 1 30 14 14 LYS CB C 32.900 . 1 31 14 14 LYS N N 122.600 . 1 32 15 15 THR H H 7.999 . 1 33 15 15 THR C C 173.700 . 1 34 15 15 THR CA C 62.380 . 1 35 15 15 THR CB C 70.360 . 1 36 15 15 THR N N 116.000 . 1 37 16 16 ALA H H 7.957 . 1 38 16 16 ALA C C 176.600 . 1 39 16 16 ALA CA C 51.880 . 1 40 16 16 ALA CB C 21.160 . 1 41 16 16 ALA N N 126.700 . 1 42 17 17 VAL H H 8.880 . 1 43 17 17 VAL C C 175.000 . 1 44 17 17 VAL CA C 62.490 . 1 45 17 17 VAL CB C 35.030 . 1 46 17 17 VAL N N 121.200 . 1 47 18 18 LEU H H 8.935 . 1 48 18 18 LEU C C 175.700 . 1 49 18 18 LEU CA C 52.460 . 1 50 18 18 LEU CB C 45.160 . 1 51 18 18 LEU N N 126.800 . 1 52 19 19 LYS H H 9.349 . 1 53 19 19 LYS C C 173.800 . 1 54 19 19 LYS CA C 54.990 . 1 55 19 19 LYS CB C 36.410 . 1 56 19 19 LYS N N 120.600 . 1 57 20 20 LEU H H 8.538 . 1 58 20 20 LEU C C 173.800 . 1 59 20 20 LEU CA C 52.850 . 1 60 20 20 LEU CB C 45.000 . 1 61 20 20 LEU N N 124.600 . 1 62 21 21 TYR H H 9.502 . 1 63 21 21 TYR C C 175.800 . 1 64 21 21 TYR CA C 56.520 . 1 65 21 21 TYR CB C 39.010 . 1 66 21 21 TYR N N 127.000 . 1 67 22 22 VAL H H 9.099 . 1 68 22 22 VAL C C 173.900 . 1 69 22 22 VAL CA C 58.660 . 1 70 22 22 VAL CB C 35.840 . 1 71 22 22 VAL N N 114.600 . 1 72 23 23 ALA H H 8.368 . 1 73 23 23 ALA C C 176.300 . 1 74 23 23 ALA CA C 50.450 . 1 75 23 23 ALA CB C 18.660 . 1 76 23 23 ALA N N 124.200 . 1 77 24 24 GLY H H 8.636 . 1 78 24 24 GLY C C 172.400 . 1 79 24 24 GLY CA C 47.580 . 1 80 24 24 GLY N N 113.800 . 1 81 25 25 ASN H H 8.450 . 1 82 25 25 ASN C C 175.500 . 1 83 25 25 ASN CA C 51.920 . 1 84 25 25 ASN CB C 38.080 . 1 85 25 25 ASN N N 121.900 . 1 86 26 26 THR H H 7.839 . 1 87 26 26 THR C C 174.300 . 1 88 26 26 THR CA C 60.900 . 1 89 26 26 THR CB C 69.280 . 1 90 26 26 THR N N 113.200 . 1 91 28 28 ASN C C 179.000 . 1 92 28 28 ASN CA C 56.550 . 1 93 28 28 ASN CB C 37.000 . 1 94 29 29 SER H H 7.733 . 1 95 29 29 SER C C 174.800 . 1 96 29 29 SER CA C 64.100 . 1 97 29 29 SER CB C 62.460 . 1 98 29 29 SER N N 119.800 . 1 99 30 30 VAL H H 8.158 . 1 100 30 30 VAL C C 178.600 . 1 101 30 30 VAL CA C 66.930 . 1 102 30 30 VAL CB C 31.840 . 1 103 30 30 VAL N N 122.600 . 1 104 31 31 ARG H H 8.151 . 1 105 31 31 ARG C C 179.200 . 1 106 31 31 ARG CA C 59.790 . 1 107 31 31 ARG CB C 30.680 . 1 108 31 31 ARG N N 118.300 . 1 109 32 32 ALA H H 7.468 . 1 110 32 32 ALA C C 178.700 . 1 111 32 32 ALA CA C 54.810 . 1 112 32 32 ALA CB C 18.850 . 1 113 32 32 ALA N N 122.800 . 1 114 33 33 LEU H H 7.959 . 1 115 33 33 LEU C C 178.200 . 1 116 33 33 LEU CA C 58.390 . 1 117 33 33 LEU CB C 42.280 . 1 118 33 33 LEU N N 118.600 . 1 119 34 34 LYS H H 8.271 . 1 120 34 34 LYS C C 180.000 . 1 121 34 34 LYS CA C 59.970 . 1 122 34 34 LYS CB C 32.490 . 1 123 34 34 LYS N N 117.900 . 1 124 35 35 THR H H 8.070 . 1 125 35 35 THR C C 175.900 . 1 126 35 35 THR CA C 67.160 . 1 127 35 35 THR CB C 68.820 . 1 128 35 35 THR N N 117.200 . 1 129 36 36 LEU H H 8.412 . 1 130 36 36 LEU C C 178.500 . 1 131 36 36 LEU CA C 58.180 . 1 132 36 36 LEU CB C 41.620 . 1 133 36 36 LEU N N 121.600 . 1 134 37 37 ASN H H 8.735 . 1 135 37 37 ASN C C 177.500 . 1 136 37 37 ASN CA C 56.610 . 1 137 37 37 ASN CB C 38.090 . 1 138 37 37 ASN N N 116.400 . 1 139 38 38 ASN H H 7.621 . 1 140 38 38 ASN C C 177.400 . 1 141 38 38 ASN CA C 57.100 . 1 142 38 38 ASN CB C 39.860 . 1 143 38 38 ASN N N 116.800 . 1 144 39 39 ILE H H 7.739 . 1 145 39 39 ILE C C 178.900 . 1 146 39 39 ILE CA C 65.130 . 1 147 39 39 ILE CB C 39.130 . 1 148 39 39 ILE N N 119.200 . 1 149 40 40 LEU H H 8.758 . 1 150 40 40 LEU C C 178.200 . 1 151 40 40 LEU CA C 58.310 . 1 152 40 40 LEU CB C 40.210 . 1 153 40 40 LEU N N 120.100 . 1 154 41 41 GLU H H 7.607 . 1 155 41 41 GLU C C 176.900 . 1 156 41 41 GLU CA C 57.620 . 1 157 41 41 GLU CB C 30.260 . 1 158 41 41 GLU N N 114.800 . 1 159 42 42 LYS H H 7.567 . 1 160 42 42 LYS C C 177.100 . 1 161 42 42 LYS CA C 57.460 . 1 162 42 42 LYS CB C 33.560 . 1 163 42 42 LYS N N 119.100 . 1 164 43 43 GLU H H 9.757 . 1 165 43 43 GLU C C 177.400 . 1 166 43 43 GLU CA C 60.040 . 1 167 43 43 GLU CB C 30.070 . 1 168 43 43 GLU N N 122.100 . 1 169 44 44 PHE H H 7.823 . 1 170 44 44 PHE C C 175.000 . 1 171 44 44 PHE CA C 56.930 . 1 172 44 44 PHE CB C 40.010 . 1 173 44 44 PHE N N 114.400 . 1 174 45 45 LYS H H 7.538 . 1 175 45 45 LYS C C 178.700 . 1 176 45 45 LYS CA C 58.920 . 1 177 45 45 LYS CB C 31.880 . 1 178 45 45 LYS N N 122.900 . 1 179 46 46 GLY H H 9.122 . 1 180 46 46 GLY C C 174.300 . 1 181 46 46 GLY CA C 45.840 . 1 182 46 46 GLY N N 115.200 . 1 183 47 47 VAL H H 8.025 . 1 184 47 47 VAL C C 175.400 . 1 185 47 47 VAL CA C 65.360 . 1 186 47 47 VAL CB C 33.340 . 1 187 47 47 VAL N N 120.500 . 1 188 48 48 TYR H H 8.025 . 1 189 48 48 TYR C C 175.700 . 1 190 48 48 TYR CA C 56.810 . 1 191 48 48 TYR CB C 42.400 . 1 192 48 48 TYR N N 114.500 . 1 193 49 49 ALA H H 8.693 . 1 194 49 49 ALA C C 175.200 . 1 195 49 49 ALA CA C 51.000 . 1 196 49 49 ALA CB C 20.820 . 1 197 49 49 ALA N N 124.500 . 1 198 50 50 LEU H H 8.583 . 1 199 50 50 LEU C C 175.700 . 1 200 50 50 LEU CA C 54.110 . 1 201 50 50 LEU CB C 44.990 . 1 202 50 50 LEU N N 123.100 . 1 203 51 51 LYS H H 8.989 . 1 204 51 51 LYS C C 174.100 . 1 205 51 51 LYS CA C 54.450 . 1 206 51 51 LYS CB C 34.090 . 1 207 51 51 LYS N N 128.900 . 1 208 52 52 VAL H H 8.560 . 1 209 52 52 VAL C C 175.800 . 1 210 52 52 VAL CA C 62.070 . 1 211 52 52 VAL CB C 32.810 . 1 212 52 52 VAL N N 124.900 . 1 213 53 53 ILE H H 9.204 . 1 214 53 53 ILE C C 173.700 . 1 215 53 53 ILE CA C 59.870 . 1 216 53 53 ILE CB C 39.460 . 1 217 53 53 ILE N N 130.900 . 1 218 54 54 ASP H H 8.869 . 1 219 54 54 ASP C C 173.700 . 1 220 54 54 ASP CA C 52.180 . 1 221 54 54 ASP CB C 40.940 . 1 222 54 54 ASP N N 126.800 . 1 223 55 55 VAL H H 9.386 . 1 224 55 55 VAL C C 177.000 . 1 225 55 55 VAL CA C 63.600 . 1 226 55 55 VAL CB C 30.730 . 1 227 55 55 VAL N N 121.200 . 1 228 56 56 LEU H H 8.676 . 1 229 56 56 LEU C C 179.200 . 1 230 56 56 LEU CA C 56.510 . 1 231 56 56 LEU CB C 40.730 . 1 232 56 56 LEU N N 120.200 . 1 233 57 57 LYS H H 7.154 . 1 234 57 57 LYS C C 176.500 . 1 235 57 57 LYS CA C 56.850 . 1 236 57 57 LYS CB C 33.800 . 1 237 57 57 LYS N N 118.000 . 1 238 58 58 ASN H H 7.830 . 1 239 58 58 ASN CA C 51.340 . 1 240 58 58 ASN N N 114.600 . 1 241 59 59 PRO C C 179.500 . 1 242 59 59 PRO CA C 65.420 . 1 243 59 59 PRO CB C 31.300 . 1 244 60 60 GLN H H 8.788 . 1 245 60 60 GLN C C 178.400 . 1 246 60 60 GLN CA C 58.720 . 1 247 60 60 GLN CB C 27.220 . 1 248 60 60 GLN N N 119.500 . 1 249 61 61 LEU H H 7.494 . 1 250 61 61 LEU C C 178.700 . 1 251 61 61 LEU CA C 57.080 . 1 252 61 61 LEU CB C 41.460 . 1 253 61 61 LEU N N 120.000 . 1 254 62 62 ALA H H 7.237 . 1 255 62 62 ALA C C 178.800 . 1 256 62 62 ALA CA C 54.730 . 1 257 62 62 ALA CB C 18.190 . 1 258 62 62 ALA N N 119.700 . 1 259 63 63 GLU H H 7.604 . 1 260 63 63 GLU C C 180.200 . 1 261 63 63 GLU CA C 58.990 . 1 262 63 63 GLU CB C 29.470 . 1 263 63 63 GLU N N 117.100 . 1 264 64 64 GLU H H 8.218 . 1 265 64 64 GLU C C 177.800 . 1 266 64 64 GLU CA C 59.480 . 1 267 64 64 GLU CB C 29.590 . 1 268 64 64 GLU N N 121.000 . 1 269 65 65 ASP H H 7.739 . 1 270 65 65 ASP C C 174.400 . 1 271 65 65 ASP CA C 54.200 . 1 272 65 65 ASP CB C 39.670 . 1 273 65 65 ASP N N 116.500 . 1 274 66 66 LYS H H 7.633 . 1 275 66 66 LYS C C 175.200 . 1 276 66 66 LYS CA C 54.640 . 1 277 66 66 LYS CB C 28.880 . 1 278 66 66 LYS N N 117.400 . 1 279 67 67 ILE H H 8.116 . 1 280 67 67 ILE C C 176.000 . 1 281 67 67 ILE CA C 58.440 . 1 282 67 67 ILE CB C 35.160 . 1 283 67 67 ILE N N 120.200 . 1 284 68 68 LEU H H 8.419 . 1 285 68 68 LEU C C 176.100 . 1 286 68 68 LEU CA C 55.020 . 1 287 68 68 LEU CB C 43.150 . 1 288 68 68 LEU N N 128.300 . 1 289 69 69 ALA H H 7.634 . 1 290 69 69 ALA C C 175.600 . 1 291 69 69 ALA CA C 51.190 . 1 292 69 69 ALA CB C 21.790 . 1 293 69 69 ALA N N 121.300 . 1 294 70 70 THR H H 8.258 . 1 295 70 70 THR C C 172.300 . 1 296 70 70 THR CA C 58.090 . 1 297 70 70 THR CB C 71.020 . 1 298 70 70 THR N N 108.700 . 1 299 71 71 PRO C C 176.300 . 1 300 71 71 PRO CA C 62.210 . 1 301 71 71 PRO CB C 33.950 . 1 302 72 72 THR H H 8.413 . 1 303 72 72 THR C C 171.300 . 1 304 72 72 THR CA C 62.840 . 1 305 72 72 THR CB C 73.220 . 1 306 72 72 THR N N 117.400 . 1 307 73 73 LEU H H 9.303 . 1 308 73 73 LEU C C 173.200 . 1 309 73 73 LEU CA C 53.310 . 1 310 73 73 LEU CB C 45.840 . 1 311 73 73 LEU N N 130.500 . 1 312 74 74 ALA H H 9.570 . 1 313 74 74 ALA C C 175.200 . 1 314 74 74 ALA CA C 50.370 . 1 315 74 74 ALA CB C 22.850 . 1 316 74 74 ALA N N 128.200 . 1 317 75 75 LYS H H 9.061 . 1 318 75 75 LYS C C 175.700 . 1 319 75 75 LYS CA C 56.500 . 1 320 75 75 LYS CB C 32.370 . 1 321 75 75 LYS N N 125.100 . 1 322 76 76 VAL H H 8.470 . 1 323 76 76 VAL C C 174.000 . 1 324 76 76 VAL CA C 62.000 . 1 325 76 76 VAL CB C 32.490 . 1 326 76 76 VAL N N 118.600 . 1 327 77 77 LEU H H 7.391 . 1 328 77 77 LEU C C 174.800 . 1 329 77 77 LEU CA C 52.790 . 1 330 77 77 LEU CB C 46.470 . 1 331 77 77 LEU N N 120.100 . 1 332 80 80 PRO C C 175.400 . 1 333 80 80 PRO CA C 61.740 . 1 334 80 80 PRO CB C 35.010 . 1 335 81 81 VAL H H 8.441 . 1 336 81 81 VAL C C 177.100 . 1 337 81 81 VAL CA C 63.440 . 1 338 81 81 VAL CB C 31.710 . 1 339 81 81 VAL N N 120.900 . 1 340 82 82 ARG H H 8.658 . 1 341 82 82 ARG C C 174.700 . 1 342 82 82 ARG CA C 54.400 . 1 343 82 82 ARG CB C 34.450 . 1 344 82 82 ARG N N 126.900 . 1 345 83 83 ARG H H 8.786 . 1 346 83 83 ARG C C 175.300 . 1 347 83 83 ARG CA C 55.800 . 1 348 83 83 ARG CB C 32.380 . 1 349 83 83 ARG N N 122.200 . 1 350 84 84 ILE H H 8.945 . 1 351 84 84 ILE C C 174.400 . 1 352 84 84 ILE CA C 60.510 . 1 353 84 84 ILE CB C 39.290 . 1 354 84 84 ILE N N 124.500 . 1 355 85 85 ILE H H 8.321 . 1 356 85 85 ILE C C 175.900 . 1 357 85 85 ILE CA C 60.480 . 1 358 85 85 ILE CB C 39.460 . 1 359 85 85 ILE N N 125.900 . 1 360 86 86 GLY H H 8.071 . 1 361 86 86 GLY C C 172.000 . 1 362 86 86 GLY CA C 44.560 . 1 363 86 86 GLY N N 112.300 . 1 364 87 87 ASP C C 176.700 . 1 365 87 87 ASP CA C 54.400 . 1 366 87 87 ASP CB C 40.790 . 1 367 88 88 LEU H H 8.443 . 1 368 88 88 LEU C C 175.300 . 1 369 88 88 LEU CA C 54.820 . 1 370 88 88 LEU CB C 41.150 . 1 371 88 88 LEU N N 124.100 . 1 372 89 89 SER H H 7.850 . 1 373 89 89 SER C C 174.000 . 1 374 89 89 SER CA C 59.320 . 1 375 89 89 SER CB C 64.240 . 1 376 89 89 SER N N 108.800 . 1 377 90 90 ASN H H 7.504 . 1 378 90 90 ASN C C 173.900 . 1 379 90 90 ASN CA C 52.340 . 1 380 90 90 ASN CB C 39.340 . 1 381 90 90 ASN N N 120.000 . 1 382 91 91 ARG H H 8.643 . 1 383 91 91 ARG C C 176.800 . 1 384 91 91 ARG CA C 60.330 . 1 385 91 91 ARG CB C 30.520 . 1 386 91 91 ARG N N 124.900 . 1 387 92 92 GLU H H 8.201 . 1 388 92 92 GLU C C 179.100 . 1 389 92 92 GLU CA C 60.270 . 1 390 92 92 GLU CB C 29.230 . 1 391 92 92 GLU N N 116.900 . 1 392 93 93 LYS H H 7.881 . 1 393 93 93 LYS C C 180.000 . 1 394 93 93 LYS CA C 59.000 . 1 395 93 93 LYS CB C 32.480 . 1 396 93 93 LYS N N 117.200 . 1 397 94 94 VAL H H 8.092 . 1 398 94 94 VAL C C 176.900 . 1 399 94 94 VAL CA C 67.320 . 1 400 94 94 VAL CB C 31.180 . 1 401 94 94 VAL N N 121.500 . 1 402 95 95 LEU H H 8.368 . 1 403 95 95 LEU C C 179.300 . 1 404 95 95 LEU CA C 59.180 . 1 405 95 95 LEU CB C 41.910 . 1 406 95 95 LEU N N 120.200 . 1 407 96 96 ILE H H 7.750 . 1 408 96 96 ILE C C 178.000 . 1 409 96 96 ILE CA C 65.470 . 1 410 96 96 ILE CB C 38.390 . 1 411 96 96 ILE N N 117.900 . 1 412 97 97 ALA H H 7.637 . 1 413 97 97 ALA C C 180.100 . 1 414 97 97 ALA CA C 55.200 . 1 415 97 97 ALA CB C 18.350 . 1 416 97 97 ALA N N 121.500 . 1 417 98 98 LEU H H 8.391 . 1 418 98 98 LEU C C 180.300 . 1 419 98 98 LEU CA C 57.460 . 1 420 98 98 LEU CB C 41.350 . 1 421 98 98 LEU N N 115.600 . 1 422 99 99 ARG H H 8.134 . 1 423 99 99 ARG C C 178.800 . 1 424 99 99 ARG CA C 59.540 . 1 425 99 99 ARG CB C 29.920 . 1 426 99 99 ARG N N 120.200 . 1 427 100 100 LEU H H 7.819 . 1 428 100 100 LEU C C 178.400 . 1 429 100 100 LEU CA C 56.510 . 1 430 100 100 LEU CB C 42.220 . 1 431 100 100 LEU N N 119.000 . 1 432 101 101 LEU H H 7.425 . 1 433 101 101 LEU C C 175.800 . 1 434 101 101 LEU CA C 55.400 . 1 435 101 101 LEU CB C 42.450 . 1 436 101 101 LEU N N 119.000 . 1 437 102 102 ALA H H 7.214 . 1 438 102 102 ALA C C 182.700 . 1 439 102 102 ALA CA C 54.700 . 1 440 102 102 ALA CB C 19.790 . 1 441 102 102 ALA N N 127.600 . 1 stop_ save_