data_27768 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for the ShkA kinase Rec1 domain from Caulobacter crescentus ; _BMRB_accession_number 27768 _BMRB_flat_file_name bmr27768.str _Entry_type original _Submission_date 2019-01-30 _Accession_date 2019-01-30 _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 Boehm Raphael . . 2 Hiller Sebastian . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 116 "13C chemical shifts" 240 "15N chemical shifts" 116 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-12-12 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 27882 'Different Receiver domain (Rec2) of the same ShkA kinase protein of Caulobacter crescentus' stop_ _Original_release_date 2019-02-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A second-messenger-induced genetic program drives bacterial G1/S transition ; _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Boehm Raphael . . 2 Hiller Sebastian . . 3 Kaczmarczyk Andreas . . 4 Hampel Antje Marie . 5 'von Arx' Christoph . . 6 Nesper Jutta . . 7 Dubey Badri N. . 8 Schirmer Tilman . . 9 Jenal Urs . . stop_ _Journal_abbreviation 'Not known' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword NMR c-di-GMP 'histidine kinase' pseudo-receiver stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name ShkA-Rec1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Rec1 $ShkA-Rec1 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_ShkA-Rec1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ShkA-Rec1 _Molecular_mass 15520 _Mol_thiol_state 'not present' loop_ _Biological_function 'Histine Kinase' Phosphorelay stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 151 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MAPLEGRNVAIASPNAIVRA ATARQIEAAGGRAYAAVDIA SALAGAPADAVLLIDAALSG PRGALKPPAGRRSVVLLTPE QRDRIDRLKAAGFSGYLIKP LRAASLVAQVLQAVTADGVA EDEPAHDDRIA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 SER 4 SER 5 HIS 6 HIS 7 HIS 8 HIS 9 HIS 10 HIS 11 SER 12 SER 13 GLY 14 LEU 15 VAL 16 PRO 17 ARG 18 GLY 19 SER 20 HIS 21 MET 22 ALA 23 PRO 24 LEU 25 GLU 26 GLY 27 ARG 28 ASN 29 VAL 30 ALA 31 ILE 32 ALA 33 SER 34 PRO 35 ASN 36 ALA 37 ILE 38 VAL 39 ARG 40 ALA 41 ALA 42 THR 43 ALA 44 ARG 45 GLN 46 ILE 47 GLU 48 ALA 49 ALA 50 GLY 51 GLY 52 ARG 53 ALA 54 TYR 55 ALA 56 ALA 57 VAL 58 ASP 59 ILE 60 ALA 61 SER 62 ALA 63 LEU 64 ALA 65 GLY 66 ALA 67 PRO 68 ALA 69 ASP 70 ALA 71 VAL 72 LEU 73 LEU 74 ILE 75 ASP 76 ALA 77 ALA 78 LEU 79 SER 80 GLY 81 PRO 82 ARG 83 GLY 84 ALA 85 LEU 86 LYS 87 PRO 88 PRO 89 ALA 90 GLY 91 ARG 92 ARG 93 SER 94 VAL 95 VAL 96 LEU 97 LEU 98 THR 99 PRO 100 GLU 101 GLN 102 ARG 103 ASP 104 ARG 105 ILE 106 ASP 107 ARG 108 LEU 109 LYS 110 ALA 111 ALA 112 GLY 113 PHE 114 SER 115 GLY 116 TYR 117 LEU 118 ILE 119 LYS 120 PRO 121 LEU 122 ARG 123 ALA 124 ALA 125 SER 126 LEU 127 VAL 128 ALA 129 GLN 130 VAL 131 LEU 132 GLN 133 ALA 134 VAL 135 THR 136 ALA 137 ASP 138 GLY 139 VAL 140 ALA 141 GLU 142 ASP 143 GLU 144 PRO 145 ALA 146 HIS 147 ASP 148 ASP 149 ARG 150 ILE 151 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 $ShkA-Rec1 'Caulobacter crescentus' 155892 Bacteria . Caulobacter crescentus 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 $ShkA-Rec1 'recombinant technology' . Escherichia coli . pET stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ShkA-Rec1 0.95 mM '[U-99% 13C; U-99% 15N]' TRIS 25 mM 'natural abundance' 'potassium chloride' 50 mM 'natural abundance' 'magnesium sulfate' 2 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Rochus Keller' . . 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 700 _Details . 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_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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' 78 . mM pH 7.2 . pH pressure 1 . atm temperature 298.15 . 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' ppm 0.00 internal direct . . . 1.000000000 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 'TROSY offset: amide protons.' loop_ _Software_label $CARA stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCACB' 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 Rec1 _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 13 13 GLY CA C 45.047 0.300 1 2 14 14 LEU H H 7.884 0.020 1 3 14 14 LEU CA C 54.859 0.300 1 4 14 14 LEU CB C 42.059 0.300 1 5 14 14 LEU N N 121.963 0.300 1 6 15 15 VAL H H 7.912 0.020 1 7 15 15 VAL CA C 59.557 0.300 1 8 15 15 VAL CB C 32.292 0.300 1 9 15 15 VAL N N 122.835 0.300 1 10 21 21 MET H H 7.950 0.020 1 11 21 21 MET CA C 55.190 0.300 1 12 21 21 MET CB C 32.457 0.300 1 13 21 21 MET N N 121.115 0.300 1 14 22 22 ALA H H 8.351 0.020 1 15 22 22 ALA CA C 50.077 0.300 1 16 22 22 ALA CB C 18.307 0.300 1 17 22 22 ALA N N 125.987 0.300 1 18 23 23 PRO CA C 64.919 0.300 1 19 23 23 PRO CB C 32.070 0.300 1 20 24 24 LEU H H 8.285 0.020 1 21 24 24 LEU CA C 52.537 0.300 1 22 24 24 LEU CB C 39.895 0.300 1 23 24 24 LEU N N 112.956 0.300 1 24 25 25 GLU H H 7.260 0.020 1 25 25 25 GLU CA C 58.231 0.300 1 26 25 25 GLU CB C 29.184 0.300 1 27 25 25 GLU N N 120.434 0.300 1 28 26 26 GLY H H 8.666 0.020 1 29 26 26 GLY CA C 45.295 0.300 1 30 26 26 GLY N N 114.988 0.300 1 31 27 27 ARG H H 8.151 0.020 1 32 27 27 ARG CA C 53.449 0.300 1 33 27 27 ARG CB C 29.684 0.300 1 34 27 27 ARG N N 118.217 0.300 1 35 28 28 ASN H H 8.638 0.020 1 36 28 28 ASN CA C 52.178 0.300 1 37 28 28 ASN CB C 40.117 0.300 1 38 28 28 ASN N N 121.245 0.300 1 39 29 29 VAL H H 9.134 0.020 1 40 29 29 VAL CA C 60.746 0.300 1 41 29 29 VAL CB C 35.223 0.300 1 42 29 29 VAL N N 123.488 0.300 1 43 30 30 ALA H H 9.386 0.020 1 44 30 30 ALA CA C 48.889 0.300 1 45 30 30 ALA CB C 21.360 0.300 1 46 30 30 ALA N N 130.133 0.300 1 47 31 31 ILE H H 8.782 0.020 1 48 31 31 ILE CA C 58.175 0.300 1 49 31 31 ILE CB C 41.615 0.300 1 50 31 31 ILE N N 121.103 0.300 1 51 32 32 ALA H H 8.864 0.020 1 52 32 32 ALA CA C 48.419 0.300 1 53 32 32 ALA CB C 19.306 0.300 1 54 32 32 ALA N N 130.012 0.300 1 55 33 33 SER H H 8.336 0.020 1 56 33 33 SER CA C 55.356 0.300 1 57 33 33 SER CB C 65.367 0.300 1 58 33 33 SER N N 114.466 0.300 1 59 36 36 ALA CA C 55.411 0.300 1 60 36 36 ALA CB C 18.529 0.300 1 61 37 37 ILE H H 7.821 0.020 1 62 37 37 ILE CA C 63.952 0.300 1 63 37 37 ILE CB C 36.510 0.300 1 64 37 37 ILE N N 119.505 0.300 1 65 38 38 VAL H H 7.378 0.020 1 66 38 38 VAL CA C 66.025 0.300 1 67 38 38 VAL CB C 31.349 0.300 1 68 38 38 VAL N N 121.743 0.300 1 69 39 39 ARG H H 8.169 0.020 1 70 39 39 ARG CA C 61.685 0.300 1 71 39 39 ARG CB C 30.572 0.300 1 72 39 39 ARG N N 120.073 0.300 1 73 40 40 ALA H H 7.613 0.020 1 74 40 40 ALA CA C 54.748 0.300 1 75 40 40 ALA CB C 18.307 0.300 1 76 40 40 ALA N N 119.828 0.300 1 77 41 41 ALA H H 8.663 0.020 1 78 41 41 ALA CA C 54.886 0.300 1 79 41 41 ALA CB C 18.196 0.300 1 80 41 41 ALA N N 121.201 0.300 1 81 42 42 THR H H 7.832 0.020 1 82 42 42 THR CA C 66.246 0.300 1 83 42 42 THR CB C 67.698 0.300 1 84 42 42 THR N N 114.731 0.300 1 85 43 43 ALA H H 7.703 0.020 1 86 43 43 ALA CA C 55.743 0.300 1 87 43 43 ALA CB C 17.581 0.300 1 88 43 43 ALA N N 124.131 0.300 1 89 44 44 ARG H H 7.444 0.020 1 90 44 44 ARG CA C 59.115 0.300 1 91 44 44 ARG CB C 29.573 0.300 1 92 44 44 ARG N N 115.878 0.300 1 93 45 45 GLN H H 7.522 0.020 1 94 45 45 GLN CA C 59.115 0.300 1 95 45 45 GLN CB C 29.129 0.300 1 96 45 45 GLN N N 119.455 0.300 1 97 46 46 ILE CA C 64.300 0.300 1 98 46 46 ILE CB C 37.128 0.300 1 99 47 47 GLU H H 8.076 0.020 1 100 47 47 GLU CA C 58.560 0.300 1 101 47 47 GLU CB C 28.545 0.300 1 102 47 47 GLU N N 120.020 0.300 1 103 48 48 ALA H H 8.395 0.020 1 104 48 48 ALA CA C 54.389 0.300 1 105 48 48 ALA CB C 17.581 0.300 1 106 48 48 ALA N N 124.698 0.300 1 107 49 49 ALA H H 7.032 0.020 1 108 49 49 ALA CA C 51.155 0.300 1 109 49 49 ALA CB C 18.363 0.300 1 110 49 49 ALA N N 118.141 0.300 1 111 50 50 GLY H H 7.797 0.020 1 112 50 50 GLY CA C 44.826 0.300 1 113 50 50 GLY N N 107.191 0.300 1 114 51 51 GLY H H 7.895 0.020 1 115 51 51 GLY CA C 44.273 0.300 1 116 51 51 GLY N N 108.602 0.300 1 117 52 52 ARG H H 8.015 0.020 1 118 52 52 ARG CA C 54.665 0.300 1 119 52 52 ARG CB C 31.071 0.300 1 120 52 52 ARG N N 118.855 0.300 1 121 53 53 ALA H H 8.805 0.020 1 122 53 53 ALA CA C 49.966 0.300 1 123 53 53 ALA CB C 22.469 0.300 1 124 53 53 ALA N N 127.002 0.300 1 125 54 54 TYR H H 8.394 0.020 1 126 54 54 TYR CA C 56.987 0.300 1 127 54 54 TYR CB C 40.283 0.300 1 128 54 54 TYR N N 122.133 0.300 1 129 55 55 ALA H H 8.661 0.020 1 130 55 55 ALA CA C 50.879 0.300 1 131 55 55 ALA CB C 21.304 0.300 1 132 55 55 ALA N N 128.089 0.300 1 133 56 56 ALA H H 9.009 0.020 1 134 56 56 ALA CA C 50.657 0.300 1 135 56 56 ALA CB C 22.858 0.300 1 136 56 56 ALA N N 125.139 0.300 1 137 57 57 VAL H H 7.966 0.020 1 138 57 57 VAL CA C 62.128 0.300 1 139 57 57 VAL CB C 31.599 0.300 1 140 57 57 VAL N N 112.653 0.300 1 141 58 58 ASP H H 7.254 0.020 1 142 58 58 ASP CA C 52.122 0.300 1 143 58 58 ASP CB C 41.005 0.300 1 144 58 58 ASP N N 113.992 0.300 1 145 59 59 ILE H H 8.047 0.020 1 146 59 59 ILE CA C 66.577 0.300 1 147 59 59 ILE CB C 37.564 0.300 1 148 59 59 ILE N N 118.649 0.300 1 149 60 60 ALA H H 8.432 0.020 1 150 60 60 ALA CA C 55.467 0.300 1 151 60 60 ALA CB C 17.752 0.300 1 152 60 60 ALA N N 122.127 0.300 1 153 61 61 SER H H 8.670 0.020 1 154 61 61 SER CA C 61.437 0.300 1 155 61 61 SER CB C 62.481 0.300 1 156 61 61 SER N N 114.194 0.300 1 157 62 62 ALA H H 7.829 0.020 1 158 62 62 ALA CA C 54.859 0.300 1 159 62 62 ALA CB C 17.581 0.300 1 160 62 62 ALA N N 128.212 0.300 1 161 63 63 LEU H H 8.194 0.020 1 162 63 63 LEU CA C 56.793 0.300 1 163 63 63 LEU CB C 41.615 0.300 1 164 63 63 LEU N N 116.175 0.300 1 165 64 64 ALA H H 7.492 0.020 1 166 64 64 ALA CA C 53.725 0.300 1 167 64 64 ALA CB C 18.474 0.300 1 168 64 64 ALA N N 118.511 0.300 1 169 65 65 GLY H H 7.387 0.020 1 170 65 65 GLY CA C 44.798 0.300 1 171 65 65 GLY N N 103.214 0.300 1 172 66 66 ALA H H 7.207 0.020 1 173 66 66 ALA CA C 48.916 0.300 1 174 66 66 ALA CB C 18.474 0.300 1 175 66 66 ALA N N 122.632 0.300 1 176 68 68 ALA CA C 54.002 0.300 1 177 68 68 ALA CB C 18.141 0.300 1 178 69 69 ASP H H 7.566 0.020 1 179 69 69 ASP CA C 52.039 0.300 1 180 69 69 ASP CB C 40.172 0.300 1 181 69 69 ASP N N 112.175 0.300 1 182 70 70 ALA H H 7.338 0.020 1 183 70 70 ALA CA C 52.150 0.300 1 184 70 70 ALA CB C 18.307 0.300 1 185 70 70 ALA N N 122.277 0.300 1 186 71 71 VAL H H 7.849 0.020 1 187 71 71 VAL CA C 62.542 0.300 1 188 71 71 VAL CB C 33.014 0.300 1 189 71 71 VAL N N 125.671 0.300 1 190 72 72 LEU H H 8.767 0.020 1 191 72 72 LEU CA C 54.195 0.300 1 192 72 72 LEU CB C 42.670 0.300 1 193 72 72 LEU N N 128.174 0.300 1 194 73 73 LEU H H 9.163 0.020 1 195 73 73 LEU CA C 53.034 0.300 1 196 73 73 LEU CB C 41.504 0.300 1 197 73 73 LEU N N 126.010 0.300 1 198 74 74 ILE H H 8.971 0.020 1 199 74 74 ILE CA C 60.303 0.300 1 200 74 74 ILE CB C 40.172 0.300 1 201 74 74 ILE N N 122.816 0.300 1 202 75 75 ASP H H 8.498 0.020 1 203 75 75 ASP CA C 54.306 0.300 1 204 75 75 ASP CB C 42.836 0.300 1 205 75 75 ASP N N 128.268 0.300 1 206 76 76 ALA H H 9.151 0.020 1 207 76 76 ALA CA C 54.361 0.300 1 208 76 76 ALA CB C 16.966 0.300 1 209 76 76 ALA N N 131.168 0.300 1 210 77 77 ALA H H 8.561 0.020 1 211 77 77 ALA CA C 54.140 0.300 1 212 77 77 ALA CB C 18.751 0.300 1 213 77 77 ALA N N 124.852 0.300 1 214 78 78 LEU H H 8.012 0.020 1 215 78 78 LEU CA C 55.190 0.300 1 216 78 78 LEU CB C 41.171 0.300 1 217 78 78 LEU N N 116.850 0.300 1 218 79 79 SER H H 7.629 0.020 1 219 79 79 SER CA C 59.806 0.300 1 220 79 79 SER CB C 64.313 0.300 1 221 79 79 SER N N 115.784 0.300 1 222 80 80 GLY H H 8.607 0.020 1 223 80 80 GLY CA C 44.383 0.300 1 224 80 80 GLY N N 110.773 0.300 1 225 81 81 PRO CA C 62.874 0.300 1 226 81 81 PRO CB C 31.682 0.300 1 227 82 82 ARG H H 8.332 0.020 1 228 82 82 ARG CA C 56.047 0.300 1 229 82 82 ARG CB C 30.683 0.300 1 230 82 82 ARG N N 122.342 0.300 1 231 83 83 GLY H H 7.953 0.020 1 232 83 83 GLY CA C 45.461 0.300 1 233 83 83 GLY N N 107.686 0.300 1 234 84 84 ALA H H 7.451 0.020 1 235 84 84 ALA CA C 52.786 0.300 1 236 84 84 ALA CB C 19.084 0.300 1 237 84 84 ALA N N 124.625 0.300 1 238 85 85 LEU H H 7.912 0.020 1 239 85 85 LEU CA C 55.163 0.300 1 240 85 85 LEU CB C 43.391 0.300 1 241 85 85 LEU N N 125.220 0.300 1 242 86 86 LYS H H 8.341 0.020 1 243 86 86 LYS CA C 52.205 0.300 1 244 86 86 LYS CB C 33.679 0.300 1 245 86 86 LYS N N 127.713 0.300 1 246 90 90 GLY CA C 45.572 0.300 1 247 91 91 ARG H H 6.930 0.020 1 248 91 91 ARG CA C 51.044 0.300 1 249 91 91 ARG CB C 30.516 0.300 1 250 91 91 ARG N N 116.520 0.300 1 251 92 92 ARG H H 9.041 0.020 1 252 92 92 ARG CA C 54.859 0.300 1 253 92 92 ARG CB C 30.239 0.300 1 254 92 92 ARG N N 125.307 0.300 1 255 93 93 SER H H 8.793 0.020 1 256 93 93 SER CA C 57.567 0.300 1 257 93 93 SER CB C 67.088 0.300 1 258 93 93 SER N N 118.733 0.300 1 259 94 94 VAL H H 9.365 0.020 1 260 94 94 VAL CA C 60.331 0.300 1 261 94 94 VAL CB C 35.338 0.300 1 262 94 94 VAL N N 126.293 0.300 1 263 95 95 VAL H H 7.929 0.020 1 264 95 95 VAL CA C 58.617 0.300 1 265 95 95 VAL CB C 31.904 0.300 1 266 95 95 VAL N N 127.005 0.300 1 267 96 96 LEU H H 8.291 0.020 1 268 96 96 LEU CA C 52.509 0.300 1 269 96 96 LEU CB C 41.973 0.300 1 270 96 96 LEU N N 125.943 0.300 1 271 97 97 LEU H H 8.931 0.020 1 272 97 97 LEU CA C 53.034 0.300 1 273 97 97 LEU CB C 45.555 0.300 1 274 97 97 LEU N N 124.537 0.300 1 275 98 98 THR H H 8.353 0.020 1 276 98 98 THR CA C 60.027 0.300 1 277 98 98 THR CB C 67.199 0.300 1 278 98 98 THR N N 112.338 0.300 1 279 99 99 PRO CA C 65.914 0.300 1 280 100 100 GLU H H 8.279 0.020 1 281 100 100 GLU CA C 58.396 0.300 1 282 100 100 GLU CB C 28.130 0.300 1 283 100 100 GLU N N 115.380 0.300 1 284 101 101 GLN H H 7.698 0.020 1 285 101 101 GLN CA C 54.776 0.300 1 286 101 101 GLN CB C 29.073 0.300 1 287 101 101 GLN N N 118.534 0.300 1 288 102 102 ARG H H 7.276 0.020 1 289 102 102 ARG CA C 59.143 0.300 1 290 102 102 ARG CB C 29.517 0.300 1 291 102 102 ARG N N 119.655 0.300 1 292 103 103 ASP H H 8.351 0.020 1 293 103 103 ASP CA C 55.301 0.300 1 294 103 103 ASP CB C 38.896 0.300 1 295 103 103 ASP N N 118.635 0.300 1 296 104 104 ARG H H 7.749 0.020 1 297 104 104 ARG CA C 56.075 0.300 1 298 104 104 ARG CB C 30.849 0.300 1 299 104 104 ARG N N 118.609 0.300 1 300 105 105 ILE H H 7.137 0.020 1 301 105 105 ILE CA C 67.075 0.300 1 302 105 105 ILE CB C 37.842 0.300 1 303 105 105 ILE N N 119.028 0.300 1 304 106 106 ASP H H 8.324 0.020 1 305 106 106 ASP CA C 57.982 0.300 1 306 106 106 ASP CB C 39.340 0.300 1 307 106 106 ASP N N 119.165 0.300 1 308 107 107 ARG H H 8.174 0.020 1 309 107 107 ARG CA C 58.452 0.300 1 310 107 107 ARG CB C 29.462 0.300 1 311 107 107 ARG N N 121.929 0.300 1 312 108 108 LEU H H 8.194 0.020 1 313 108 108 LEU CA C 57.733 0.300 1 314 108 108 LEU CB C 40.339 0.300 1 315 108 108 LEU N N 122.666 0.300 1 316 109 109 LYS H H 8.664 0.020 1 317 109 109 LYS CA C 59.336 0.300 1 318 109 109 LYS CB C 31.127 0.300 1 319 109 109 LYS N N 122.665 0.300 1 320 110 110 ALA H H 7.944 0.020 1 321 110 110 ALA CA C 54.416 0.300 1 322 110 110 ALA CB C 17.354 0.300 1 323 110 110 ALA N N 123.451 0.300 1 324 111 111 ALA H H 7.614 0.020 1 325 111 111 ALA CA C 52.647 0.300 1 326 111 111 ALA CB C 18.696 0.300 1 327 111 111 ALA N N 118.849 0.300 1 328 112 112 GLY H H 7.604 0.020 1 329 112 112 GLY CA C 44.328 0.300 1 330 112 112 GLY N N 102.492 0.300 1 331 113 113 PHE H H 7.986 0.020 1 332 113 113 PHE CA C 61.298 0.300 1 333 113 113 PHE CB C 38.119 0.300 1 334 113 113 PHE N N 120.337 0.300 1 335 114 114 SER H H 9.069 0.020 1 336 114 114 SER CA C 60.221 0.300 1 337 114 114 SER CB C 63.869 0.300 1 338 114 114 SER N N 118.572 0.300 1 339 115 115 GLY H H 7.426 0.020 1 340 115 115 GLY CA C 44.549 0.300 1 341 115 115 GLY N N 103.953 0.300 1 342 116 116 TYR H H 7.533 0.020 1 343 116 116 TYR CA C 54.886 0.300 1 344 116 116 TYR CB C 42.392 0.300 1 345 116 116 TYR N N 116.480 0.300 1 346 117 117 LEU H H 8.685 0.020 1 347 117 117 LEU CA C 52.786 0.300 1 348 117 117 LEU CB C 47.609 0.300 1 349 117 117 LEU N N 120.739 0.300 1 350 118 118 ILE H H 8.453 0.020 1 351 118 118 ILE CA C 57.236 0.300 1 352 118 118 ILE CB C 36.232 0.300 1 353 118 118 ILE N N 122.718 0.300 1 354 119 119 LYS H H 8.559 0.020 1 355 119 119 LYS CA C 54.665 0.300 1 356 119 119 LYS CB C 32.570 0.300 1 357 119 119 LYS N N 126.563 0.300 1 358 120 120 PRO CA C 61.547 0.300 1 359 120 120 PRO CB C 33.624 0.300 1 360 121 121 LEU H H 8.395 0.020 1 361 121 121 LEU CA C 55.798 0.300 1 362 121 121 LEU CB C 41.282 0.300 1 363 121 121 LEU N N 123.388 0.300 1 364 122 122 ARG H H 8.437 0.020 1 365 122 122 ARG CA C 53.919 0.300 1 366 122 122 ARG CB C 31.071 0.300 1 367 122 122 ARG N N 124.213 0.300 1 368 123 123 ALA CA C 56.268 0.300 1 369 123 123 ALA CB C 16.739 0.300 1 370 124 124 ALA H H 8.705 0.020 1 371 124 124 ALA CA C 55.190 0.300 1 372 124 124 ALA CB C 17.974 0.300 1 373 124 124 ALA N N 117.407 0.300 1 374 125 125 SER H H 6.939 0.020 1 375 125 125 SER CA C 60.856 0.300 1 376 125 125 SER CB C 62.426 0.300 1 377 125 125 SER N N 113.855 0.300 1 378 126 126 LEU H H 7.975 0.020 1 379 126 126 LEU CA C 58.977 0.300 1 380 126 126 LEU CB C 41.282 0.300 1 381 126 126 LEU N N 124.828 0.300 1 382 127 127 VAL H H 8.135 0.020 1 383 127 127 VAL CA C 67.213 0.300 1 384 127 127 VAL CB C 31.626 0.300 1 385 127 127 VAL N N 118.120 0.300 1 386 128 128 ALA H H 7.258 0.020 1 387 128 128 ALA CA C 55.135 0.300 1 388 128 128 ALA CB C 17.919 0.300 1 389 128 128 ALA N N 119.119 0.300 1 390 129 129 GLN H H 8.158 0.020 1 391 129 129 GLN CA C 57.622 0.300 1 392 129 129 GLN CB C 28.019 0.300 1 393 129 129 GLN N N 115.305 0.300 1 394 130 130 VAL H H 8.155 0.020 1 395 130 130 VAL CA C 67.324 0.300 1 396 130 130 VAL CB C 30.849 0.300 1 397 130 130 VAL N N 120.741 0.300 1 398 131 131 LEU H H 8.011 0.020 1 399 131 131 LEU CA C 57.208 0.300 1 400 131 131 LEU CB C 40.727 0.300 1 401 131 131 LEU N N 117.471 0.300 1 402 132 132 GLN H H 7.859 0.020 1 403 132 132 GLN CA C 57.595 0.300 1 404 132 132 GLN CB C 28.185 0.300 1 405 132 132 GLN N N 118.630 0.300 1 406 133 133 ALA H H 7.572 0.020 1 407 133 133 ALA CA C 53.808 0.300 1 408 133 133 ALA CB C 18.307 0.300 1 409 133 133 ALA N N 121.848 0.300 1 410 134 134 VAL H H 7.644 0.020 1 411 134 134 VAL CA C 62.321 0.300 1 412 134 134 VAL CB C 32.292 0.300 1 413 134 134 VAL N N 112.959 0.300 1 414 135 135 THR H H 7.637 0.020 1 415 135 135 THR CA C 62.238 0.300 1 416 135 135 THR CB C 69.696 0.300 1 417 135 135 THR N N 114.857 0.300 1 418 136 136 ALA H H 7.956 0.020 1 419 136 136 ALA CA C 52.482 0.300 1 420 136 136 ALA CB C 18.862 0.300 1 421 136 136 ALA N N 126.753 0.300 1 422 137 137 ASP H H 8.188 0.020 1 423 137 137 ASP CA C 54.306 0.300 1 424 137 137 ASP CB C 41.060 0.300 1 425 137 137 ASP N N 120.215 0.300 1 426 138 138 GLY H H 8.147 0.020 1 427 138 138 GLY CA C 45.074 0.300 1 428 138 138 GLY N N 109.430 0.300 1 429 139 139 VAL H H 7.795 0.020 1 430 139 139 VAL CA C 61.879 0.300 1 431 139 139 VAL CB C 32.625 0.300 1 432 139 139 VAL N N 119.907 0.300 1 433 140 140 ALA H H 8.323 0.020 1 434 140 140 ALA CA C 52.067 0.300 1 435 140 140 ALA CB C 19.084 0.300 1 436 140 140 ALA N N 128.935 0.300 1 437 141 141 GLU H H 8.303 0.020 1 438 141 141 GLU CA C 56.268 0.300 1 439 141 141 GLU CB C 30.183 0.300 1 440 141 141 GLU N N 121.235 0.300 1 441 142 142 ASP H H 8.218 0.020 1 442 142 142 ASP CA C 53.974 0.300 1 443 142 142 ASP CB C 40.949 0.300 1 444 142 142 ASP N N 121.751 0.300 1 445 143 143 GLU H H 8.099 0.020 1 446 143 143 GLU CA C 54.029 0.300 1 447 143 143 GLU CB C 29.573 0.300 1 448 143 143 GLU N N 122.804 0.300 1 449 144 144 PRO CA C 62.846 0.300 1 450 144 144 PRO CB C 31.737 0.300 1 451 145 145 ALA H H 8.257 0.020 1 452 145 145 ALA CA C 51.956 0.300 1 453 145 145 ALA CB C 18.862 0.300 1 454 145 145 ALA N N 124.698 0.300 1 455 146 146 HIS H H 8.154 0.020 1 456 146 146 HIS CA C 55.396 0.300 1 457 146 146 HIS N N 119.782 0.300 1 458 147 147 ASP CA C 54.076 0.300 1 459 148 148 ASP H H 8.265 0.020 1 460 148 148 ASP CA C 54.195 0.300 1 461 148 148 ASP CB C 40.727 0.300 1 462 148 148 ASP N N 122.256 0.300 1 463 149 149 ARG H H 8.057 0.020 1 464 149 149 ARG CA C 56.158 0.300 1 465 149 149 ARG CB C 30.405 0.300 1 466 149 149 ARG N N 120.915 0.300 1 467 150 150 ILE H H 7.936 0.020 1 468 150 150 ILE CA C 60.912 0.300 1 469 150 150 ILE CB C 38.341 0.300 1 470 150 150 ILE N N 121.748 0.300 1 471 151 151 ALA H H 7.753 0.020 1 472 151 151 ALA N N 133.842 0.300 1 stop_ save_