data_25618 ####################### # 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, from the Thermosynechococcus elongatus BP-1 cyanobacterial species ; _BMRB_accession_number 25618 _BMRB_flat_file_name bmr25618.str _Entry_type original _Submission_date 2015-05-15 _Accession_date 2015-05-15 _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" 79 "13C chemical shifts" 175 "15N chemical shifts" 79 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' 25619 'N-SasA bound to CI' 25620 'G89A single mutant of dimeric KaiB' 25621 'D91R single mutant of dimeric KaiB' 25622 'D91R single mutant of dimeric KaiB (thioredoxin-like fold)' 25623 'G89A,D91R double mutant of dimeric KaiB' 25624 'G89A,D91R double mutant of KaiB' 25625 'G89A,D91R double mutant of KaiB bound to CI' 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 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label N-SasA $FTeSasA16107P16AF 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_ #################### # 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 ; Concentration: [N15,C13]-FLAG-TeSasA-16-107-P16A-FLAG (450 uM); Buffer: 5 mM Tris, 50 mM NaCl, pH 7.0, 10 uM DSS, 0.02% NaN3, 95% H2O/5% D2O, 0.5X Protease Inhibitor Cocktail; Volume: 350 uL; Tube: shaped tube ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FTeSasA16107P16AF 450 uM '[U-99% 13C; U-98% 15N]' 'Protease Inhibitor Cocktail' 450 uM 'natural abundance' Tris 5 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 . 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_ ####################### # 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 601.129948 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' 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 CA C 54.910 . 1 2 8 8 LYS CB C 32.510 . 1 3 9 9 ALA H H 8.115 . 1 4 9 9 ALA CA C 53.680 . 1 5 9 9 ALA CB C 19.890 . 1 6 9 9 ALA N N 124.500 . 1 7 10 10 LEU H H 7.402 . 1 8 10 10 LEU CA C 53.580 . 1 9 10 10 LEU CB C 44.990 . 1 10 10 10 LEU N N 117.000 . 1 11 11 11 SER H H 8.478 . 1 12 11 11 SER CA C 57.550 . 1 13 11 11 SER CB C 64.620 . 1 14 11 11 SER N N 120.200 . 1 15 12 12 LEU H H 8.808 . 1 16 12 12 LEU CA C 53.160 . 1 17 12 12 LEU CB C 46.340 . 1 18 12 12 LEU N N 126.800 . 1 19 13 13 LEU H H 9.323 . 1 20 13 13 LEU CA C 53.210 . 1 21 13 13 LEU CB C 45.970 . 1 22 13 13 LEU N N 124.500 . 1 23 14 14 LEU H H 9.010 . 1 24 14 14 LEU CA C 53.050 . 1 25 14 14 LEU CB C 44.690 . 1 26 14 14 LEU N N 125.200 . 1 27 15 15 PHE H H 9.686 . 1 28 15 15 PHE CA C 56.970 . 1 29 15 15 PHE CB C 40.910 . 1 30 15 15 PHE N N 127.900 . 1 31 16 16 VAL H H 7.956 . 1 32 16 16 VAL CA C 58.840 . 1 33 16 16 VAL CB C 35.650 . 1 34 16 16 VAL N N 113.900 . 1 35 17 17 ALA H H 9.196 . 1 36 17 17 ALA CA C 51.880 . 1 37 17 17 ALA CB C 19.550 . 1 38 17 17 ALA N N 125.800 . 1 39 18 18 ASN H H 8.289 . 1 40 18 18 ASN CA C 52.890 . 1 41 18 18 ASN CB C 38.590 . 1 42 18 18 ASN N N 117.100 . 1 43 19 19 ARG H H 8.537 . 1 44 19 19 ARG CA C 54.450 . 1 45 19 19 ARG CB C 29.100 . 1 46 19 19 ARG N N 121.800 . 1 47 20 20 PRO CA C 64.890 . 1 48 20 20 PRO CB C 31.430 . 1 49 21 21 GLY H H 9.086 . 1 50 21 21 GLY CA C 45.730 . 1 51 21 21 GLY N N 113.200 . 1 52 22 22 ASP H H 8.253 . 1 53 22 22 ASP CA C 56.030 . 1 54 22 22 ASP CB C 41.070 . 1 55 22 22 ASP N N 121.600 . 1 56 23 23 GLU H H 8.902 . 1 57 23 23 GLU CA C 60.130 . 1 58 23 23 GLU CB C 29.110 . 1 59 23 23 GLU N N 121.700 . 1 60 24 24 GLU H H 8.542 . 1 61 24 24 GLU CA C 59.730 . 1 62 24 24 GLU CB C 29.190 . 1 63 24 24 GLU N N 120.600 . 1 64 25 25 GLU H H 8.082 . 1 65 25 25 GLU CA C 59.370 . 1 66 25 25 GLU CB C 29.880 . 1 67 25 25 GLU N N 122.400 . 1 68 26 26 THR H H 8.474 . 1 69 26 26 THR CA C 67.210 . 1 70 26 26 THR CB C 68.310 . 1 71 26 26 THR N N 117.200 . 1 72 27 27 ALA H H 8.004 . 1 73 27 27 ALA CA C 55.020 . 1 74 27 27 ALA CB C 18.040 . 1 75 27 27 ALA N N 122.700 . 1 76 28 28 ALA H H 7.994 . 1 77 28 28 ALA CA C 55.030 . 1 78 28 28 ALA CB C 18.140 . 1 79 28 28 ALA N N 122.000 . 1 80 29 29 ILE H H 8.423 . 1 81 29 29 ILE CA C 65.650 . 1 82 29 29 ILE CB C 38.420 . 1 83 29 29 ILE N N 120.900 . 1 84 30 30 GLN H H 8.130 . 1 85 30 30 GLN CA C 60.310 . 1 86 30 30 GLN CB C 29.560 . 1 87 30 30 GLN N N 117.800 . 1 88 31 31 ALA H H 8.215 . 1 89 31 31 ALA CA C 54.870 . 1 90 31 31 ALA CB C 18.090 . 1 91 31 31 ALA N N 119.700 . 1 92 32 32 HIS H H 7.926 . 1 93 32 32 HIS CA C 59.620 . 1 94 32 32 HIS CB C 30.540 . 1 95 32 32 HIS N N 116.500 . 1 96 33 33 ILE H H 7.936 . 1 97 33 33 ILE CA C 64.870 . 1 98 33 33 ILE CB C 37.770 . 1 99 33 33 ILE N N 117.300 . 1 100 34 34 GLN H H 8.017 . 1 101 34 34 GLN CA C 58.340 . 1 102 34 34 GLN CB C 28.570 . 1 103 34 34 GLN N N 115.200 . 1 104 35 35 GLN H H 7.113 . 1 105 35 35 GLN CA C 54.940 . 1 106 35 35 GLN CB C 29.150 . 1 107 35 35 GLN N N 113.800 . 1 108 36 36 LEU H H 7.070 . 1 109 36 36 LEU CA C 53.450 . 1 110 36 36 LEU CB C 38.940 . 1 111 36 36 LEU N N 124.300 . 1 112 37 37 PRO CA C 63.230 . 1 113 37 37 PRO CB C 31.650 . 1 114 38 38 SER H H 8.628 . 1 115 38 38 SER CA C 57.180 . 1 116 38 38 SER CB C 65.460 . 1 117 38 38 SER N N 116.900 . 1 118 39 39 ASN H H 8.707 . 1 119 39 39 ASN CA C 53.710 . 1 120 39 39 ASN CB C 39.130 . 1 121 39 39 ASN N N 124.700 . 1 122 40 40 PHE H H 7.878 . 1 123 40 40 PHE CA C 55.740 . 1 124 40 40 PHE CB C 41.890 . 1 125 40 40 PHE N N 116.300 . 1 126 41 41 SER H H 9.012 . 1 127 41 41 SER CA C 58.550 . 1 128 41 41 SER CB C 63.950 . 1 129 41 41 SER N N 118.500 . 1 130 42 42 PHE H H 8.239 . 1 131 42 42 PHE CA C 55.280 . 1 132 42 42 PHE CB C 43.580 . 1 133 42 42 PHE N N 117.300 . 1 134 43 43 GLU H H 8.501 . 1 135 43 43 GLU CA C 54.390 . 1 136 43 43 GLU CB C 33.090 . 1 137 43 43 GLU N N 120.100 . 1 138 44 44 LEU H H 8.748 . 1 139 44 44 LEU CA C 54.220 . 1 140 44 44 LEU CB C 44.670 . 1 141 44 44 LEU N N 127.100 . 1 142 45 45 LYS H H 8.426 . 1 143 45 45 LYS CA C 54.600 . 1 144 45 45 LYS CB C 34.660 . 1 145 45 45 LYS N N 128.200 . 1 146 46 46 VAL H H 8.712 . 1 147 46 46 VAL CA C 62.230 . 1 148 46 46 VAL CB C 32.090 . 1 149 46 46 VAL N N 126.300 . 1 150 47 47 VAL H H 9.295 . 1 151 47 47 VAL CA C 59.490 . 1 152 47 47 VAL CB C 33.500 . 1 153 47 47 VAL N N 131.400 . 1 154 48 48 PRO CA C 61.380 . 1 155 48 48 PRO CB C 31.680 . 1 156 49 49 ILE H H 8.834 . 1 157 49 49 ILE CA C 62.170 . 1 158 49 49 ILE CB C 38.760 . 1 159 49 49 ILE N N 122.100 . 1 160 50 50 GLY H H 8.625 . 1 161 50 50 GLY CA C 46.180 . 1 162 50 50 GLY N N 110.100 . 1 163 51 51 GLU H H 8.073 . 1 164 51 51 GLU CA C 56.530 . 1 165 51 51 GLU CB C 30.440 . 1 166 51 51 GLU N N 118.400 . 1 167 52 52 GLN H H 7.667 . 1 168 52 52 GLN N N 117.500 . 1 169 53 53 PRO CA C 65.150 . 1 170 53 53 PRO CB C 31.340 . 1 171 54 54 TYR H H 7.637 . 1 172 54 54 TYR CA C 58.710 . 1 173 54 54 TYR CB C 37.190 . 1 174 54 54 TYR N N 117.000 . 1 175 55 55 LEU H H 7.641 . 1 176 55 55 LEU CA C 57.060 . 1 177 55 55 LEU CB C 42.370 . 1 178 55 55 LEU N N 121.800 . 1 179 56 56 LEU CB C 41.270 . 1 180 57 57 GLU H H 7.564 . 1 181 57 57 GLU CA C 58.340 . 1 182 57 57 GLU CB C 29.560 . 1 183 57 57 GLU N N 117.800 . 1 184 58 58 GLU H H 8.000 . 1 185 58 58 GLU CA C 58.720 . 1 186 58 58 GLU CB C 29.670 . 1 187 58 58 GLU N N 120.200 . 1 188 59 59 TYR H H 7.579 . 1 189 59 59 TYR CA C 58.440 . 1 190 59 59 TYR CB C 38.030 . 1 191 59 59 TYR N N 114.700 . 1 192 60 60 LYS H H 7.664 . 1 193 60 60 LYS CA C 56.580 . 1 194 60 60 LYS CB C 29.530 . 1 195 60 60 LYS N N 118.400 . 1 196 61 61 LEU H H 7.978 . 1 197 61 61 LEU CA C 54.270 . 1 198 61 61 LEU CB C 43.380 . 1 199 61 61 LEU N N 119.000 . 1 200 62 62 VAL H H 8.370 . 1 201 62 62 VAL CA C 62.150 . 1 202 62 62 VAL CB C 32.880 . 1 203 62 62 VAL N N 117.600 . 1 204 63 63 ALA H H 7.662 . 1 205 63 63 ALA CA C 51.580 . 1 206 63 63 ALA CB C 21.610 . 1 207 63 63 ALA N N 123.100 . 1 208 64 64 THR H H 7.709 . 1 209 64 64 THR CA C 58.500 . 1 210 64 64 THR CB C 69.430 . 1 211 64 64 THR N N 106.800 . 1 212 65 65 PRO CA C 62.090 . 1 213 65 65 PRO CB C 35.030 . 1 214 66 66 ALA H H 8.784 . 1 215 66 66 ALA CA C 51.370 . 1 216 66 66 ALA CB C 23.910 . 1 217 66 66 ALA N N 122.100 . 1 218 67 67 LEU H H 9.608 . 1 219 67 67 LEU CA C 53.050 . 1 220 67 67 LEU CB C 46.950 . 1 221 67 67 LEU N N 125.300 . 1 222 68 68 ILE H H 9.892 . 1 223 68 68 ILE CA C 59.590 . 1 224 68 68 ILE CB C 40.360 . 1 225 68 68 ILE N N 126.000 . 1 226 69 69 LYS H H 8.948 . 1 227 69 69 LYS CA C 55.740 . 1 228 69 69 LYS CB C 31.590 . 1 229 69 69 LYS N N 130.000 . 1 230 70 70 VAL H H 8.325 . 1 231 70 70 VAL CA C 62.910 . 1 232 70 70 VAL CB C 33.110 . 1 233 70 70 VAL N N 123.000 . 1 234 71 71 ARG H H 7.432 . 1 235 71 71 ARG CA C 53.800 . 1 236 71 71 ARG CB C 34.170 . 1 237 71 71 ARG N N 118.200 . 1 238 72 72 PRO CA C 62.240 . 1 239 72 72 PRO CB C 34.090 . 1 240 73 73 GLU H H 8.572 . 1 241 73 73 GLU CA C 56.160 . 1 242 73 73 GLU CB C 28.750 . 1 243 73 73 GLU N N 120.800 . 1 244 74 74 PRO CA C 61.320 . 1 245 74 74 PRO CB C 34.680 . 1 246 75 75 ARG H H 8.406 . 1 247 75 75 ARG CA C 56.440 . 1 248 75 75 ARG CB C 31.120 . 1 249 75 75 ARG N N 122.000 . 1 250 76 76 GLN H H 8.019 . 1 251 76 76 GLN CB C 31.130 . 1 252 76 76 GLN N N 123.000 . 1 253 77 77 THR CA C 62.200 . 1 254 77 77 THR CB C 70.220 . 1 255 78 78 LEU H H 9.593 . 1 256 78 78 LEU CA C 53.550 . 1 257 78 78 LEU CB C 44.200 . 1 258 78 78 LEU N N 128.900 . 1 259 79 79 ALA H H 8.648 . 1 260 79 79 ALA CA C 51.810 . 1 261 79 79 ALA CB C 23.520 . 1 262 79 79 ALA N N 123.800 . 1 263 80 80 GLY H H 8.620 . 1 264 80 80 GLY CA C 44.790 . 1 265 80 80 GLY N N 106.400 . 1 266 81 81 ARG H H 8.588 . 1 267 81 81 ARG N N 119.500 . 1 268 82 82 LYS CA C 55.600 . 1 269 82 82 LYS CB C 30.240 . 1 270 83 83 LEU H H 7.495 . 1 271 83 83 LEU CA C 59.880 . 1 272 83 83 LEU CB C 42.060 . 1 273 83 83 LEU N N 119.900 . 1 274 84 84 LEU H H 8.711 . 1 275 84 84 LEU CA C 58.420 . 1 276 84 84 LEU CB C 40.130 . 1 277 84 84 LEU N N 115.800 . 1 278 85 85 GLN H H 7.574 . 1 279 85 85 GLN CA C 59.650 . 1 280 85 85 GLN CB C 28.380 . 1 281 85 85 GLN N N 118.100 . 1 282 86 86 LYS CA C 59.980 . 1 283 86 86 LYS CB C 33.330 . 1 284 87 87 VAL H H 8.819 . 1 285 87 87 VAL CA C 67.190 . 1 286 87 87 VAL CB C 31.450 . 1 287 87 87 VAL N N 121.500 . 1 288 88 88 ASP H H 8.119 . 1 289 88 88 ASP CA C 57.460 . 1 290 88 88 ASP CB C 39.880 . 1 291 88 88 ASP N N 119.600 . 1 292 89 89 TYR H H 7.503 . 1 293 89 89 TYR CA C 61.240 . 1 294 89 89 TYR CB C 38.580 . 1 295 89 89 TYR N N 119.100 . 1 296 90 90 TRP H H 8.213 . 1 297 90 90 TRP CA C 59.840 . 1 298 90 90 TRP CB C 28.710 . 1 299 90 90 TRP N N 117.600 . 1 300 91 91 TRP H H 9.105 . 1 301 91 91 TRP CA C 63.250 . 1 302 91 91 TRP CB C 26.030 . 1 303 91 91 TRP N N 121.400 . 1 304 92 92 PRO CA C 65.640 . 1 305 92 92 PRO CB C 30.970 . 1 306 93 93 ARG H H 6.904 . 1 307 93 93 ARG CA C 59.190 . 1 308 93 93 ARG CB C 28.790 . 1 309 93 93 ARG N N 119.000 . 1 310 94 94 TRP H H 8.771 . 1 311 94 94 TRP CA C 57.820 . 1 312 94 94 TRP CB C 28.480 . 1 313 94 94 TRP N N 122.600 . 1 314 95 95 GLN H H 7.992 . 1 315 95 95 GLN CA C 58.360 . 1 316 95 95 GLN CB C 28.680 . 1 317 95 95 GLN N N 115.100 . 1 318 96 96 ARG H H 7.344 . 1 319 96 96 ARG CA C 58.380 . 1 320 96 96 ARG CB C 29.780 . 1 321 96 96 ARG N N 118.100 . 1 322 97 97 GLU H H 8.095 . 1 323 97 97 GLU CA C 58.980 . 1 324 97 97 GLU CB C 30.120 . 1 325 97 97 GLU N N 119.100 . 1 326 99 99 ALA H H 7.545 . 1 327 99 99 ALA CA C 53.380 . 1 328 99 99 ALA CB C 19.160 . 1 329 99 99 ALA N N 122.400 . 1 330 100 100 LEU H H 7.898 . 1 331 100 100 LEU CA C 56.320 . 1 332 100 100 LEU CB C 41.810 . 1 333 100 100 LEU N N 118.600 . 1 stop_ save_