data_25624 ####################### # 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 from the Thermosynechococcus elongatus BP-1 cyanobacterial species ; _BMRB_accession_number 25624 _BMRB_flat_file_name bmr25624.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" 94 "13C chemical shifts" 309 "15N chemical shifts" 94 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' 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 KaiB' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'KaiB G89A D91R mutant, chain 1' $FTeKaiBGDF 'KaiB G89A D91R mutant, chain 2' $FTeKaiBGDF 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_ #################### # 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]-FALG-TeKaiB-G89A-D91R-FLAG (410 uM); Buffer: 20 mM Tris, 50 mM NaCl, 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 410 uM '[U-13C; U-15N; U-2H]' 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' 'Protease Inhibitor Cocktail' 410 uM '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 protons' MHz 601.129944 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, 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 7 7 ASP C C 176.800 . 1 2 7 7 ASP CA C 54.260 . 1 3 7 7 ASP CB C 40.260 . 1 4 8 8 LYS H H 8.074 . 1 5 8 8 LYS C C 177.000 . 1 6 8 8 LYS CA C 56.280 . 1 7 8 8 LYS CB C 31.500 . 1 8 8 8 LYS N N 121.400 . 1 9 9 9 MET H H 8.103 . 1 10 9 9 MET C C 176.000 . 1 11 9 9 MET CA C 54.710 . 1 12 9 9 MET CB C 31.550 . 1 13 9 9 MET N N 119.900 . 1 14 10 10 ALA H H 7.993 . 1 15 10 10 ALA C C 175.600 . 1 16 10 10 ALA CA C 50.830 . 1 17 10 10 ALA CB C 17.090 . 1 18 10 10 ALA N N 126.700 . 1 19 11 11 PRO CA C 62.820 . 1 20 11 11 PRO CB C 30.870 . 1 21 12 12 LEU H H 8.140 . 1 22 12 12 LEU C C 177.400 . 1 23 12 12 LEU CA C 54.850 . 1 24 12 12 LEU CB C 41.080 . 1 25 12 12 LEU N N 122.100 . 1 26 13 13 ARG H H 8.143 . 1 27 13 13 ARG C C 176.100 . 1 28 13 13 ARG CA C 55.550 . 1 29 13 13 ARG CB C 30.010 . 1 30 13 13 ARG N N 122.400 . 1 31 14 14 LYS H H 8.199 . 1 32 14 14 LYS C C 175.700 . 1 33 14 14 LYS CA C 55.640 . 1 34 14 14 LYS CB C 32.230 . 1 35 14 14 LYS N N 123.200 . 1 36 15 15 THR H H 7.792 . 1 37 15 15 THR C C 173.500 . 1 38 15 15 THR CA C 61.410 . 1 39 15 15 THR CB C 69.860 . 1 40 15 15 THR N N 116.800 . 1 41 16 16 TYR H H 8.108 . 1 42 16 16 TYR C C 175.900 . 1 43 16 16 TYR CA C 55.660 . 1 44 16 16 TYR CB C 39.500 . 1 45 16 16 TYR N N 124.700 . 1 46 17 17 VAL H H 8.961 . 1 47 17 17 VAL C C 175.100 . 1 48 17 17 VAL CA C 62.150 . 1 49 17 17 VAL CB C 33.460 . 1 50 17 17 VAL N N 123.400 . 1 51 18 18 LEU H H 9.001 . 1 52 18 18 LEU C C 175.700 . 1 53 18 18 LEU CA C 52.020 . 1 54 18 18 LEU CB C 43.810 . 1 55 18 18 LEU N N 127.800 . 1 56 19 19 LYS H H 9.282 . 1 57 19 19 LYS C C 173.900 . 1 58 19 19 LYS CA C 54.690 . 1 59 19 19 LYS CB C 35.370 . 1 60 19 19 LYS N N 121.000 . 1 61 20 20 LEU H H 8.434 . 1 62 20 20 LEU C C 173.900 . 1 63 20 20 LEU CA C 52.340 . 1 64 20 20 LEU CB C 43.960 . 1 65 20 20 LEU N N 124.900 . 1 66 21 21 TYR H H 9.438 . 1 67 21 21 TYR C C 175.900 . 1 68 21 21 TYR CA C 56.080 . 1 69 21 21 TYR CB C 38.090 . 1 70 21 21 TYR N N 127.700 . 1 71 22 22 VAL H H 9.075 . 1 72 22 22 VAL C C 173.900 . 1 73 22 22 VAL CA C 58.180 . 1 74 22 22 VAL CB C 34.930 . 1 75 22 22 VAL N N 115.400 . 1 76 23 23 ALA H H 8.179 . 1 77 23 23 ALA C C 176.300 . 1 78 23 23 ALA CA C 49.720 . 1 79 23 23 ALA CB C 17.800 . 1 80 23 23 ALA N N 124.300 . 1 81 24 24 GLY H H 8.585 . 1 82 24 24 GLY C C 172.300 . 1 83 24 24 GLY CA C 47.340 . 1 84 24 24 GLY N N 114.300 . 1 85 25 25 ASN H H 8.374 . 1 86 25 25 ASN C C 175.600 . 1 87 25 25 ASN CA C 51.460 . 1 88 25 25 ASN CB C 37.430 . 1 89 25 25 ASN N N 122.800 . 1 90 26 26 THR H H 7.822 . 1 91 26 26 THR C C 174.600 . 1 92 26 26 THR CA C 60.580 . 1 93 26 26 THR CB C 68.710 . 1 94 26 26 THR N N 114.200 . 1 95 28 28 ASN C C 179.300 . 1 96 28 28 ASN CA C 55.720 . 1 97 28 28 ASN CB C 36.140 . 1 98 29 29 SER H H 7.611 . 1 99 29 29 SER C C 174.700 . 1 100 29 29 SER CA C 64.070 . 1 101 29 29 SER CB C 62.960 . 1 102 29 29 SER N N 120.200 . 1 103 30 30 VAL H H 8.063 . 1 104 30 30 VAL C C 178.700 . 1 105 30 30 VAL CA C 66.140 . 1 106 30 30 VAL CB C 30.870 . 1 107 30 30 VAL N N 123.200 . 1 108 31 31 ARG H H 8.119 . 1 109 31 31 ARG C C 179.300 . 1 110 31 31 ARG CA C 59.090 . 1 111 31 31 ARG CB C 29.590 . 1 112 31 31 ARG N N 118.600 . 1 113 32 32 ALA H H 7.330 . 1 114 32 32 ALA C C 178.800 . 1 115 32 32 ALA CA C 54.300 . 1 116 32 32 ALA CB C 18.160 . 1 117 32 32 ALA N N 123.000 . 1 118 33 33 LEU H H 7.936 . 1 119 33 33 LEU C C 178.100 . 1 120 33 33 LEU CA C 57.850 . 1 121 33 33 LEU CB C 41.100 . 1 122 33 33 LEU N N 119.700 . 1 123 34 34 LYS H H 8.216 . 1 124 34 34 LYS C C 180.200 . 1 125 34 34 LYS CA C 59.280 . 1 126 34 34 LYS CB C 31.460 . 1 127 34 34 LYS N N 118.300 . 1 128 35 35 THR H H 7.915 . 1 129 35 35 THR C C 175.700 . 1 130 35 35 THR CA C 66.580 . 1 131 35 35 THR CB C 68.280 . 1 132 35 35 THR N N 118.100 . 1 133 36 36 LEU H H 8.230 . 1 134 36 36 LEU C C 178.700 . 1 135 36 36 LEU CA C 57.250 . 1 136 36 36 LEU CB C 40.320 . 1 137 36 36 LEU N N 122.100 . 1 138 37 37 ASN H H 8.678 . 1 139 37 37 ASN C C 177.400 . 1 140 37 37 ASN CA C 55.980 . 1 141 37 37 ASN CB C 37.310 . 1 142 37 37 ASN N N 116.900 . 1 143 38 38 ASN H H 7.511 . 1 144 38 38 ASN C C 177.500 . 1 145 38 38 ASN CA C 57.010 . 1 146 38 38 ASN CB C 39.600 . 1 147 38 38 ASN N N 117.500 . 1 148 39 39 ILE H H 7.613 . 1 149 39 39 ILE C C 179.000 . 1 150 39 39 ILE CA C 64.620 . 1 151 39 39 ILE CB C 38.200 . 1 152 39 39 ILE N N 119.500 . 1 153 40 40 LEU H H 8.563 . 1 154 40 40 LEU C C 177.900 . 1 155 40 40 LEU CA C 57.380 . 1 156 40 40 LEU CB C 38.880 . 1 157 40 40 LEU N N 120.700 . 1 158 41 41 GLU H H 7.459 . 1 159 41 41 GLU C C 176.800 . 1 160 41 41 GLU CA C 56.520 . 1 161 41 41 GLU CB C 29.490 . 1 162 41 41 GLU N N 115.700 . 1 163 42 42 LYS H H 7.406 . 1 164 42 42 LYS C C 176.600 . 1 165 42 42 LYS CA C 56.630 . 1 166 42 42 LYS CB C 32.460 . 1 167 42 42 LYS N N 121.100 . 1 168 43 43 GLU C C 177.700 . 1 169 43 43 GLU CA C 59.990 . 1 170 43 43 GLU CB C 28.920 . 1 171 44 44 PHE H H 7.761 . 1 172 44 44 PHE C C 174.600 . 1 173 44 44 PHE CA C 57.130 . 1 174 44 44 PHE CB C 39.000 . 1 175 44 44 PHE N N 113.300 . 1 176 45 45 LYS H H 7.235 . 1 177 45 45 LYS C C 178.500 . 1 178 45 45 LYS CA C 58.130 . 1 179 45 45 LYS CB C 30.960 . 1 180 45 45 LYS N N 122.800 . 1 181 46 46 GLY H H 8.977 . 1 182 46 46 GLY C C 174.300 . 1 183 46 46 GLY CA C 45.410 . 1 184 46 46 GLY N N 116.000 . 1 185 47 47 VAL H H 7.868 . 1 186 47 47 VAL C C 175.000 . 1 187 47 47 VAL CA C 64.080 . 1 188 47 47 VAL CB C 38.120 . 1 189 47 47 VAL N N 120.500 . 1 190 48 48 TYR H H 7.293 . 1 191 48 48 TYR C C 175.300 . 1 192 48 48 TYR CA C 56.170 . 1 193 48 48 TYR CB C 41.350 . 1 194 48 48 TYR N N 114.300 . 1 195 49 49 ALA H H 8.691 . 1 196 49 49 ALA C C 175.300 . 1 197 49 49 ALA CA C 50.290 . 1 198 49 49 ALA CB C 20.350 . 1 199 49 49 ALA N N 125.000 . 1 200 50 50 LEU H H 8.538 . 1 201 50 50 LEU C C 175.700 . 1 202 50 50 LEU CA C 53.470 . 1 203 50 50 LEU CB C 44.270 . 1 204 50 50 LEU N N 123.400 . 1 205 51 51 LYS H H 8.906 . 1 206 51 51 LYS C C 174.200 . 1 207 51 51 LYS CA C 53.950 . 1 208 51 51 LYS CB C 32.880 . 1 209 51 51 LYS N N 129.200 . 1 210 52 52 VAL H H 8.495 . 1 211 52 52 VAL C C 175.800 . 1 212 52 52 VAL CA C 61.500 . 1 213 52 52 VAL CB C 31.720 . 1 214 52 52 VAL N N 125.500 . 1 215 53 53 ILE H H 9.079 . 1 216 53 53 ILE C C 173.800 . 1 217 53 53 ILE CA C 58.950 . 1 218 53 53 ILE CB C 38.270 . 1 219 53 53 ILE N N 131.400 . 1 220 54 54 ASP H H 8.826 . 1 221 54 54 ASP C C 178.700 . 1 222 54 54 ASP CA C 51.700 . 1 223 54 54 ASP CB C 40.280 . 1 224 54 54 ASP N N 127.400 . 1 225 55 55 VAL H H 9.313 . 1 226 55 55 VAL C C 177.100 . 1 227 55 55 VAL CA C 62.860 . 1 228 55 55 VAL CB C 29.860 . 1 229 55 55 VAL N N 122.100 . 1 230 56 56 LEU H H 8.585 . 1 231 56 56 LEU C C 179.300 . 1 232 56 56 LEU CA C 56.020 . 1 233 56 56 LEU CB C 39.570 . 1 234 56 56 LEU N N 120.800 . 1 235 57 57 LYS H H 7.126 . 1 236 57 57 LYS C C 176.600 . 1 237 57 57 LYS CA C 56.460 . 1 238 57 57 LYS CB C 32.740 . 1 239 57 57 LYS N N 118.500 . 1 240 58 58 ASN H H 7.775 . 1 241 58 58 ASN C C 172.000 . 1 242 58 58 ASN CA C 51.000 . 1 243 58 58 ASN CB C 39.390 . 1 244 58 58 ASN N N 115.200 . 1 245 59 59 PRO C C 179.500 . 1 246 59 59 PRO CA C 64.830 . 1 247 59 59 PRO CB C 30.450 . 1 248 60 60 GLN H H 8.695 . 1 249 60 60 GLN C C 178.400 . 1 250 60 60 GLN CA C 58.180 . 1 251 60 60 GLN CB C 26.520 . 1 252 60 60 GLN N N 119.900 . 1 253 61 61 LEU H H 7.428 . 1 254 61 61 LEU C C 178.700 . 1 255 61 61 LEU CA C 56.630 . 1 256 61 61 LEU CB C 40.300 . 1 257 61 61 LEU N N 120.500 . 1 258 62 62 ALA H H 7.147 . 1 259 62 62 ALA C C 178.800 . 1 260 62 62 ALA CA C 54.060 . 1 261 62 62 ALA CB C 17.280 . 1 262 62 62 ALA N N 120.100 . 1 263 63 63 GLU H H 7.528 . 1 264 63 63 GLU C C 180.100 . 1 265 63 63 GLU CA C 58.440 . 1 266 63 63 GLU N N 117.700 . 1 267 64 64 GLU C C 177.800 . 1 268 64 64 GLU CA C 58.820 . 1 269 64 64 GLU CB C 28.630 . 1 270 65 65 ASP H H 7.637 . 1 271 65 65 ASP C C 174.500 . 1 272 65 65 ASP CA C 53.700 . 1 273 65 65 ASP CB C 39.020 . 1 274 65 65 ASP N N 117.200 . 1 275 66 66 LYS H H 7.545 . 1 276 66 66 LYS C C 175.300 . 1 277 66 66 LYS CA C 56.130 . 1 278 66 66 LYS CB C 27.970 . 1 279 66 66 LYS N N 117.800 . 1 280 67 67 ILE H H 8.027 . 1 281 67 67 ILE C C 176.000 . 1 282 67 67 ILE CA C 57.950 . 1 283 67 67 ILE CB C 34.320 . 1 284 67 67 ILE N N 120.800 . 1 285 68 68 LEU H H 8.302 . 1 286 68 68 LEU C C 176.200 . 1 287 68 68 LEU CA C 54.690 . 1 288 68 68 LEU CB C 41.960 . 1 289 68 68 LEU N N 128.500 . 1 290 69 69 ALA H H 7.586 . 1 291 69 69 ALA C C 175.900 . 1 292 69 69 ALA CA C 50.840 . 1 293 69 69 ALA CB C 20.750 . 1 294 69 69 ALA N N 122.000 . 1 295 70 70 THR H H 8.196 . 1 296 70 70 THR C C 172.300 . 1 297 70 70 THR CA C 57.510 . 1 298 70 70 THR CB C 70.520 . 1 299 70 70 THR N N 109.600 . 1 300 71 71 PRO C C 176.200 . 1 301 71 71 PRO CA C 61.680 . 1 302 71 71 PRO CB C 33.090 . 1 303 72 72 THR H H 8.378 . 1 304 72 72 THR C C 171.100 . 1 305 72 72 THR CA C 62.310 . 1 306 72 72 THR CB C 72.630 . 1 307 72 72 THR N N 117.700 . 1 308 73 73 LEU H H 9.280 . 1 309 73 73 LEU C C 173.300 . 1 310 73 73 LEU CA C 52.920 . 1 311 73 73 LEU CB C 44.950 . 1 312 73 73 LEU N N 131.300 . 1 313 74 74 ALA H H 9.407 . 1 314 74 74 ALA C C 175.600 . 1 315 74 74 ALA CA C 49.990 . 1 316 74 74 ALA CB C 21.530 . 1 317 74 74 ALA N N 128.000 . 1 318 75 75 LYS H H 9.055 . 1 319 75 75 LYS C C 175.600 . 1 320 75 75 LYS CA C 56.050 . 1 321 75 75 LYS CB C 30.340 . 1 322 75 75 LYS N N 125.100 . 1 323 76 76 VAL H H 8.676 . 1 324 76 76 VAL C C 173.900 . 1 325 76 76 VAL CA C 61.300 . 1 326 76 76 VAL CB C 31.740 . 1 327 76 76 VAL N N 119.900 . 1 328 77 77 LEU H H 7.337 . 1 329 77 77 LEU C C 174.900 . 1 330 77 77 LEU CA C 52.200 . 1 331 77 77 LEU CB C 45.180 . 1 332 77 77 LEU N N 120.400 . 1 333 80 80 PRO C C 175.800 . 1 334 80 80 PRO CA C 61.170 . 1 335 80 80 PRO CB C 34.300 . 1 336 81 81 VAL H H 8.433 . 1 337 81 81 VAL C C 177.000 . 1 338 81 81 VAL CA C 62.660 . 1 339 81 81 VAL CB C 30.660 . 1 340 81 81 VAL N N 121.900 . 1 341 82 82 ARG H H 8.701 . 1 342 82 82 ARG C C 175.000 . 1 343 82 82 ARG CA C 53.630 . 1 344 82 82 ARG CB C 33.220 . 1 345 82 82 ARG N N 127.100 . 1 346 83 83 ARG H H 8.904 . 1 347 83 83 ARG C C 175.300 . 1 348 83 83 ARG CA C 55.550 . 1 349 83 83 ARG CB C 30.360 . 1 350 83 83 ARG N N 124.700 . 1 351 84 84 ILE H H 8.693 . 1 352 84 84 ILE C C 174.800 . 1 353 84 84 ILE CA C 60.260 . 1 354 84 84 ILE CB C 37.320 . 1 355 84 84 ILE N N 125.800 . 1 356 85 85 ILE H H 8.295 . 1 357 85 85 ILE C C 175.600 . 1 358 85 85 ILE CA C 59.710 . 1 359 85 85 ILE CB C 38.440 . 1 360 85 85 ILE N N 125.600 . 1 361 86 86 GLY H H 8.039 . 1 362 86 86 GLY C C 172.300 . 1 363 86 86 GLY CA C 43.790 . 1 364 86 86 GLY N N 112.000 . 1 365 87 87 ASP C C 176.700 . 1 366 87 87 ASP CA C 53.360 . 1 367 87 87 ASP CB C 39.590 . 1 368 88 88 LEU H H 8.267 . 1 369 88 88 LEU C C 175.100 . 1 370 88 88 LEU CA C 54.700 . 1 371 88 88 LEU CB C 40.110 . 1 372 88 88 LEU N N 125.800 . 1 373 89 89 SER H H 8.009 . 1 374 89 89 SER C C 174.000 . 1 375 89 89 SER CA C 58.190 . 1 376 89 89 SER CB C 63.660 . 1 377 89 89 SER N N 110.100 . 1 378 90 90 ASN H H 7.393 . 1 379 90 90 ASN C C 173.700 . 1 380 90 90 ASN CA C 51.940 . 1 381 90 90 ASN CB C 38.050 . 1 382 90 90 ASN N N 122.600 . 1 383 91 91 ARG H H 8.486 . 1 384 91 91 ARG C C 176.900 . 1 385 91 91 ARG CA C 59.820 . 1 386 91 91 ARG CB C 29.490 . 1 387 91 91 ARG N N 127.400 . 1 388 92 92 GLU H H 8.067 . 1 389 92 92 GLU C C 179.200 . 1 390 92 92 GLU CA C 59.600 . 1 391 92 92 GLU CB C 28.370 . 1 392 92 92 GLU N N 116.500 . 1 393 93 93 LYS H H 7.643 . 1 394 93 93 LYS C C 179.900 . 1 395 93 93 LYS CA C 58.520 . 1 396 93 93 LYS CB C 31.510 . 1 397 93 93 LYS N N 117.700 . 1 398 94 94 VAL H H 8.154 . 1 399 94 94 VAL C C 177.200 . 1 400 94 94 VAL CA C 66.550 . 1 401 94 94 VAL CB C 30.290 . 1 402 94 94 VAL N N 122.400 . 1 403 95 95 LEU H H 8.327 . 1 404 95 95 LEU C C 178.900 . 1 405 95 95 LEU CA C 58.800 . 1 406 95 95 LEU CB C 41.120 . 1 407 95 95 LEU N N 121.300 . 1 408 96 96 ILE H H 7.593 . 1 409 96 96 ILE C C 178.200 . 1 410 96 96 ILE CA C 64.820 . 1 411 96 96 ILE CB C 37.310 . 1 412 96 96 ILE N N 118.400 . 1 413 97 97 ALA H H 7.664 . 1 414 97 97 ALA C C 180.400 . 1 415 97 97 ALA CA C 54.920 . 1 416 97 97 ALA CB C 17.390 . 1 417 97 97 ALA N N 122.300 . 1 418 98 98 LEU H H 8.460 . 1 419 98 98 LEU C C 180.400 . 1 420 98 98 LEU CA C 56.850 . 1 421 98 98 LEU CB C 40.040 . 1 422 98 98 LEU N N 117.200 . 1 423 99 99 ARG H H 8.428 . 1 424 99 99 ARG C C 178.300 . 1 425 99 99 ARG CA C 59.610 . 1 426 99 99 ARG CB C 28.700 . 1 427 99 99 ARG N N 123.500 . 1 428 100 100 LEU C C 180.500 . 1 429 100 100 LEU CA C 57.710 . 1 430 100 100 LEU CB C 40.490 . 1 431 101 101 LEU H H 7.907 . 1 432 101 101 LEU C C 178.200 . 1 433 101 101 LEU CA C 56.920 . 1 434 101 101 LEU CB C 41.040 . 1 435 101 101 LEU N N 118.800 . 1 436 102 102 TYR H H 7.521 . 1 437 102 102 TYR C C 177.200 . 1 438 102 102 TYR CA C 60.130 . 1 439 102 102 TYR CB C 38.160 . 1 440 102 102 TYR N N 120.200 . 1 441 103 103 GLU H H 7.918 . 1 442 103 103 GLU C C 177.400 . 1 443 103 103 GLU CA C 57.050 . 1 444 103 103 GLU CB C 29.100 . 1 445 103 103 GLU N N 117.900 . 1 446 104 104 GLU H H 7.669 . 1 447 104 104 GLU C C 177.300 . 1 448 104 104 GLU CA C 57.220 . 1 449 104 104 GLU CB C 28.820 . 1 450 104 104 GLU N N 120.100 . 1 451 105 105 ILE H H 8.033 . 1 452 105 105 ILE C C 177.300 . 1 453 105 105 ILE CA C 61.750 . 1 454 105 105 ILE CB C 37.720 . 1 455 105 105 ILE N N 121.500 . 1 456 106 106 GLY H H 8.109 . 1 457 106 106 GLY C C 174.100 . 1 458 106 106 GLY CA C 45.060 . 1 459 106 106 GLY N N 111.300 . 1 460 107 107 ASP CA C 54.130 . 1 461 108 108 GLN H H 8.191 . 1 462 108 108 GLN C C 175.700 . 1 463 108 108 GLN CA C 55.340 . 1 464 108 108 GLN CB C 28.510 . 1 465 108 108 GLN N N 120.600 . 1 466 109 109 ALA H H 8.197 . 1 467 109 109 ALA C C 177.700 . 1 468 109 109 ALA CA C 52.230 . 1 469 109 109 ALA CB C 18.500 . 1 470 109 109 ALA N N 125.500 . 1 471 110 110 GLU H H 8.325 . 1 472 110 110 GLU C C 176.300 . 1 473 110 110 GLU CA C 55.990 . 1 474 110 110 GLU CB C 29.690 . 1 475 110 110 GLU N N 119.900 . 1 476 112 112 ASP C C 176.300 . 1 477 112 112 ASP CA C 54.080 . 1 478 112 112 ASP CB C 40.580 . 1 479 113 113 LEU H H 8.387 . 1 480 113 113 LEU C C 177.400 . 1 481 113 113 LEU CA C 55.030 . 1 482 113 113 LEU CB C 41.260 . 1 483 113 113 LEU N N 123.900 . 1 484 114 114 GLY H H 8.444 . 1 485 114 114 GLY C C 174.500 . 1 486 114 114 GLY CA C 45.030 . 1 487 114 114 GLY N N 110.300 . 1 488 115 115 LEU H H 8.054 . 1 489 115 115 LEU C C 177.700 . 1 490 115 115 LEU CA C 54.930 . 1 491 115 115 LEU CB C 41.130 . 1 492 115 115 LEU N N 122.100 . 1 493 116 116 GLU H H 8.365 . 1 494 116 116 GLU C C 176.100 . 1 495 116 116 GLU CA C 56.210 . 1 496 116 116 GLU CB C 29.330 . 1 497 116 116 GLU N N 121.100 . 1 stop_ save_