data_25141 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shift assignment of EL_LovR bound to magnesium chloride ; _BMRB_accession_number 25141 _BMRB_flat_file_name bmr25141.str _Entry_type original _Submission_date 2014-08-11 _Accession_date 2014-08-11 _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 Ocasio Victor J. . 2 Correa Fernando . . 3 Gardner Kevin H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 70 "13C chemical shifts" 232 "15N chemical shifts" 70 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-06-30 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 25140 'apo EL_LovR' stop_ _Original_release_date 2016-06-30 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Ligand-induced folding of a two-component signaling receiver domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25629646 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ocasio Victor J. . 2 Correa Fernando . . 3 Gardner Kevin H. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 54 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1353 _Page_last 1363 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name EL_LovR _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'subunit 1' $entity 'MAGNESIUM ION' $entity_MG 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_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common EL_LovR _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 125 _Mol_residue_sequence ; GAMGMPKVLVLEDEPLIAMN LQYAFEDEGAEVVVAATCEQ ALKSLADNPIDVAVLDVNLG PKSHCGPVADALKQRAIPFI LHTGDLDRHGELLRKIDAPV MAKPADTSDVAKRALEMCGG DKEPA ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ALA 3 MET 4 GLY 5 MET 6 PRO 7 LYS 8 VAL 9 LEU 10 VAL 11 LEU 12 GLU 13 ASP 14 GLU 15 PRO 16 LEU 17 ILE 18 ALA 19 MET 20 ASN 21 LEU 22 GLN 23 TYR 24 ALA 25 PHE 26 GLU 27 ASP 28 GLU 29 GLY 30 ALA 31 GLU 32 VAL 33 VAL 34 VAL 35 ALA 36 ALA 37 THR 38 CYS 39 GLU 40 GLN 41 ALA 42 LEU 43 LYS 44 SER 45 LEU 46 ALA 47 ASP 48 ASN 49 PRO 50 ILE 51 ASP 52 VAL 53 ALA 54 VAL 55 LEU 56 ASP 57 VAL 58 ASN 59 LEU 60 GLY 61 PRO 62 LYS 63 SER 64 HIS 65 CYS 66 GLY 67 PRO 68 VAL 69 ALA 70 ASP 71 ALA 72 LEU 73 LYS 74 GLN 75 ARG 76 ALA 77 ILE 78 PRO 79 PHE 80 ILE 81 LEU 82 HIS 83 THR 84 GLY 85 ASP 86 LEU 87 ASP 88 ARG 89 HIS 90 GLY 91 GLU 92 LEU 93 LEU 94 ARG 95 LYS 96 ILE 97 ASP 98 ALA 99 PRO 100 VAL 101 MET 102 ALA 103 LYS 104 PRO 105 ALA 106 ASP 107 THR 108 SER 109 ASP 110 VAL 111 ALA 112 LYS 113 ARG 114 ALA 115 LEU 116 GLU 117 MET 118 CYS 119 GLY 120 GLY 121 ASP 122 LYS 123 GLU 124 PRO 125 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_MG _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'MAGNESIUM ION' _BMRB_code MG _PDB_code MG _Molecular_mass 24.305 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons MG MG MG . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $entity a-proteobacteria 39960 Bacteria . Erythrobacter litoralis HTCC2594 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 $entity 'recombinant technology' . Escherichia coli . pHis-parallel 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 'magnesium chloride' 10 mM 'natural abundance' $entity 500 uM '[U-100% 13C; U-100% 15N]' DTT 1 mM 'natural abundance' 'sodium azide' 3 mM 'natural abundance' HEPES 20 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ 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_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_4 _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' 0.025 . M pH 7.5 . 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' 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 . loop_ _Experiment_label '3D HNCACB' '3D CBCA(CO)NH' '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 'subunit 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 2 2 ALA CA C 52.7552 0.3 1 2 2 2 ALA CB C 19.4736 0.3 1 3 2 2 ALA C C 177.8000 0.3 1 4 3 3 MET N N 119.3600 0.5 1 5 3 3 MET H H 8.5700 0.03 1 6 3 3 MET CA C 55.5437 0.3 1 7 3 3 MET CB C 32.8037 0.3 1 8 3 3 MET C C 176.6000 0.3 1 9 4 4 GLY N N 110.1000 0.5 1 10 4 4 GLY H H 8.3700 0.03 1 11 4 4 GLY CA C 45.2669 0.3 1 12 4 4 GLY C C 173.6000 0.3 1 13 5 5 MET N N 121.5400 0.5 1 14 5 5 MET H H 8.2000 0.03 1 15 5 5 MET CA C 53.6642 0.3 1 16 5 5 MET CB C 33.1390 0.3 1 17 6 6 PRO CA C 62.9690 0.3 1 18 6 6 PRO CB C 32.4605 0.3 1 19 6 6 PRO C C 174.5300 0.3 1 20 7 7 LYS N N 123.3500 0.5 1 21 7 7 LYS H H 9.6800 0.03 1 22 7 7 LYS CA C 54.9686 0.3 1 23 7 7 LYS CB C 33.6722 0.3 1 24 7 7 LYS C C 175.8900 0.3 1 25 8 8 VAL N N 125.8600 0.5 1 26 8 8 VAL H H 8.8500 0.03 1 27 8 8 VAL CA C 59.7552 0.3 1 28 8 8 VAL CB C 34.9190 0.3 1 29 11 11 LEU C C 174.5300 0.3 1 30 12 12 GLU N N 127.9700 0.5 1 31 12 12 GLU H H 8.5600 0.03 1 32 12 12 GLU CA C 56.6046 0.3 1 33 12 12 GLU CB C 31.9425 0.3 1 34 15 15 PRO CA C 65.4202 0.3 1 35 15 15 PRO CB C 32.5400 0.3 1 36 15 15 PRO C C 178.9700 0.3 1 37 16 16 LEU N N 118.1600 0.5 1 38 16 16 LEU H H 8.8900 0.03 1 39 16 16 LEU CA C 58.3500 0.3 1 40 16 16 LEU CB C 41.7991 0.3 1 41 16 16 LEU C C 179.3200 0.3 1 42 17 17 ILE N N 117.6400 0.5 1 43 17 17 ILE H H 6.8300 0.03 1 44 17 17 ILE CA C 63.7724 0.3 1 45 17 17 ILE CB C 36.9394 0.3 1 46 20 20 ASN CA C 56.1808 0.3 1 47 20 20 ASN CB C 38.1171 0.3 1 48 20 20 ASN C C 179.4900 0.3 1 49 21 21 LEU N N 121.6200 0.5 1 50 21 21 LEU H H 8.5800 0.03 1 51 21 21 LEU CA C 58.2881 0.3 1 52 21 21 LEU CB C 42.5360 0.3 1 53 22 22 GLN CA C 60.5676 0.3 1 54 22 22 GLN CB C 27.1071 0.3 1 55 22 22 GLN C C 178.0600 0.3 1 56 23 23 TYR N N 117.4100 0.5 1 57 23 23 TYR H H 8.4400 0.03 1 58 23 23 TYR CA C 59.4725 0.3 1 59 23 23 TYR CB C 37.0355 0.3 1 60 23 23 TYR C C 178.4400 0.3 1 61 24 24 ALA N N 121.3100 0.5 1 62 24 24 ALA H H 7.8000 0.03 1 63 24 24 ALA CA C 55.0983 0.3 1 64 24 24 ALA CB C 18.2765 0.3 1 65 24 24 ALA C C 180.8600 0.3 1 66 25 25 PHE N N 115.4700 0.5 1 67 25 25 PHE H H 8.3400 0.03 1 68 25 25 PHE CA C 63.4493 0.3 1 69 25 25 PHE CB C 39.5109 0.3 1 70 25 25 PHE C C 179.0600 0.3 1 71 26 26 GLU N N 121.1100 0.5 1 72 26 26 GLU H H 8.8300 0.03 1 73 26 26 GLU CA C 59.7502 0.3 1 74 26 26 GLU CB C 29.0647 0.3 1 75 26 26 GLU C C 181.6600 0.3 1 76 27 27 ASP N N 121.8300 0.5 1 77 27 27 ASP H H 8.4200 0.03 1 78 27 27 ASP CA C 56.7487 0.3 1 79 27 27 ASP CB C 40.7895 0.3 1 80 27 27 ASP C C 177.8900 0.3 1 81 28 28 GLU N N 115.7300 0.5 1 82 28 28 GLU H H 7.1700 0.03 1 83 28 28 GLU CA C 55.4581 0.3 1 84 28 28 GLU CB C 30.3142 0.3 1 85 29 29 GLY CA C 45.6377 0.3 1 86 29 29 GLY C C 173.1300 0.3 1 87 30 30 ALA N N 120.9900 0.5 1 88 30 30 ALA H H 7.7500 0.03 1 89 30 30 ALA CA C 50.6248 0.3 1 90 30 30 ALA CB C 21.9627 0.3 1 91 30 30 ALA C C 175.8900 0.3 1 92 31 31 GLU N N 119.9500 0.5 1 93 31 31 GLU H H 8.6000 0.03 1 94 31 31 GLU CA C 55.1081 0.3 1 95 31 31 GLU CB C 32.2188 0.3 1 96 31 31 GLU C C 175.4300 0.3 1 97 32 32 VAL N N 123.0900 0.5 1 98 32 32 VAL H H 8.8600 0.03 1 99 32 32 VAL CA C 60.7996 0.3 1 100 32 32 VAL CB C 34.9299 0.3 1 101 32 32 VAL C C 175.2600 0.3 1 102 33 33 VAL N N 128.1000 0.5 1 103 33 33 VAL H H 9.0300 0.03 1 104 33 33 VAL CA C 61.0090 0.3 1 105 33 33 VAL CB C 33.8427 0.3 1 106 33 33 VAL C C 173.8800 0.3 1 107 34 34 VAL N N 126.3900 0.5 1 108 34 34 VAL H H 8.5600 0.03 1 109 34 34 VAL CA C 61.2804 0.3 1 110 34 34 VAL CB C 33.1740 0.3 1 111 34 34 VAL C C 175.1300 0.3 1 112 35 35 ALA N N 130.0000 0.5 1 113 35 35 ALA H H 9.3600 0.03 1 114 35 35 ALA CA C 50.1132 0.3 1 115 35 35 ALA CB C 22.7656 0.3 1 116 35 35 ALA C C 176.6100 0.3 1 117 36 36 ALA N N 121.1500 0.5 1 118 36 36 ALA H H 8.5400 0.03 1 119 36 36 ALA CA C 52.6850 0.3 1 120 36 36 ALA CB C 19.3080 0.3 1 121 36 36 ALA C C 176.6100 0.3 1 122 37 37 THR N N 102.8000 0.5 1 123 37 37 THR H H 7.0160 0.03 1 124 37 37 THR CA C 57.6100 0.3 1 125 37 37 THR CB C 72.9800 0.3 1 126 38 38 CYS CA C 63.0297 0.3 1 127 38 38 CYS CB C 26.3964 0.3 1 128 38 38 CYS C C 175.9800 0.3 1 129 39 39 GLU N N 118.5300 0.5 1 130 39 39 GLU H H 8.9800 0.03 1 131 39 39 GLU CA C 60.6165 0.3 1 132 39 39 GLU CB C 28.9849 0.3 1 133 39 39 GLU C C 179.4700 0.3 1 134 40 40 GLN N N 118.6100 0.5 1 135 40 40 GLN H H 7.8500 0.03 1 136 40 40 GLN CA C 58.2800 0.3 1 137 40 40 GLN CB C 28.9000 0.3 1 138 41 41 ALA CA C 55.2174 0.3 1 139 41 41 ALA CB C 19.5919 0.3 1 140 41 41 ALA C C 178.4100 0.3 1 141 42 42 LEU N N 116.8000 0.5 1 142 42 42 LEU H H 8.4500 0.03 1 143 42 42 LEU CA C 58.0496 0.3 1 144 42 42 LEU CB C 41.0650 0.3 1 145 42 42 LEU C C 180.0600 0.3 1 146 43 43 LYS N N 121.0200 0.5 1 147 43 43 LYS H H 7.5800 0.03 1 148 43 43 LYS CA C 59.2237 0.3 1 149 43 43 LYS CB C 32.1255 0.3 1 150 43 43 LYS C C 178.4900 0.3 1 151 44 44 SER N N 115.1200 0.5 1 152 44 44 SER H H 8.1500 0.03 1 153 44 44 SER CA C 59.2194 0.3 1 154 44 44 SER CB C 62.8620 0.3 1 155 44 44 SER C C 176.4200 0.3 1 156 45 45 LEU N N 119.9600 0.5 1 157 45 45 LEU H H 8.0400 0.03 1 158 45 45 LEU CA C 56.7404 0.3 1 159 45 45 LEU CB C 42.3379 0.3 1 160 45 45 LEU C C 177.2400 0.3 1 161 46 46 ALA N N 119.9300 0.5 1 162 46 46 ALA H H 7.3700 0.03 1 163 46 46 ALA CA C 54.1950 0.3 1 164 46 46 ALA CB C 18.2904 0.3 1 165 46 46 ALA C C 179.3300 0.3 1 166 47 47 ASP N N 115.1800 0.5 1 167 47 47 ASP H H 7.5900 0.03 1 168 47 47 ASP CA C 55.1278 0.3 1 169 47 47 ASP CB C 42.4124 0.3 1 170 47 47 ASP C C 175.9200 0.3 1 171 48 48 ASN N N 116.8900 0.5 1 172 48 48 ASN H H 7.7100 0.03 1 173 48 48 ASN CA C 51.1295 0.3 1 174 48 48 ASN CB C 42.4534 0.3 1 175 49 49 PRO CA C 62.0576 0.3 1 176 49 49 PRO CB C 30.0104 0.3 1 177 49 49 PRO C C 174.8600 0.3 1 178 50 50 ILE N N 122.4700 0.5 1 179 50 50 ILE H H 7.4200 0.03 1 180 50 50 ILE CA C 58.4251 0.3 1 181 50 50 ILE CB C 38.7702 0.3 1 182 50 50 ILE C C 174.8400 0.3 1 183 51 51 ASP N N 123.7900 0.5 1 184 51 51 ASP H H 9.3100 0.03 1 185 51 51 ASP CA C 56.8604 0.3 1 186 51 51 ASP CB C 44.4167 0.3 1 187 51 51 ASP C C 175.0900 0.3 1 188 52 52 VAL N N 114.3900 0.5 1 189 52 52 VAL H H 7.5700 0.03 1 190 52 52 VAL CA C 59.9174 0.3 1 191 52 52 VAL CB C 32.8740 0.3 1 192 52 52 VAL C C 171.2100 0.3 1 193 53 53 ALA N N 124.6174 0.5 1 194 53 53 ALA H H 7.7850 0.03 1 195 53 53 ALA CA C 49.8524 0.3 1 196 53 53 ALA CB C 25.8039 0.3 1 197 53 53 ALA C C 175.1600 0.3 1 198 54 54 VAL N N 118.8200 0.5 1 199 54 54 VAL H H 8.7000 0.03 1 200 54 54 VAL CA C 61.5051 0.3 1 201 54 54 VAL CB C 34.8124 0.3 1 202 54 54 VAL C C 174.1900 0.3 1 203 55 55 LEU N N 124.7700 0.5 1 204 55 55 LEU H H 9.1800 0.03 1 205 55 55 LEU CA C 53.4626 0.3 1 206 55 55 LEU CB C 43.0626 0.3 1 207 59 59 LEU C C 175.7700 0.3 1 208 60 60 GLY N N 108.7800 0.5 1 209 60 60 GLY H H 7.8900 0.03 1 210 60 60 GLY CA C 44.6511 0.3 1 211 61 61 PRO CA C 64.8891 0.3 1 212 61 61 PRO CB C 32.0304 0.3 1 213 61 61 PRO C C 177.9000 0.3 1 214 62 62 LYS N N 115.9700 0.5 1 215 62 62 LYS H H 8.5900 0.03 1 216 67 67 PRO CA C 65.3404 0.3 1 217 67 67 PRO CB C 33.0343 0.3 1 218 67 67 PRO C C 179.8300 0.3 1 219 68 68 VAL N N 116.3800 0.5 1 220 68 68 VAL H H 7.4000 0.03 1 221 68 68 VAL CA C 64.9996 0.3 1 222 68 68 VAL CB C 31.3761 0.3 1 223 68 68 VAL C C 176.3400 0.3 1 224 69 69 ALA N N 122.6600 0.5 1 225 69 69 ALA H H 7.8600 0.03 1 226 69 69 ALA CA C 55.1620 0.3 1 227 69 69 ALA CB C 18.3124 0.3 1 228 69 69 ALA C C 179.1700 0.3 1 229 70 70 ASP N N 116.7100 0.5 1 230 70 70 ASP H H 8.3500 0.03 1 231 70 70 ASP CA C 57.5101 0.3 1 232 70 70 ASP CB C 40.5852 0.3 1 233 70 70 ASP C C 178.3300 0.3 1 234 71 71 ALA N N 122.7300 0.5 1 235 71 71 ALA H H 7.1700 0.03 1 236 71 71 ALA CA C 55.0313 0.3 1 237 71 71 ALA CB C 18.6914 0.3 1 238 71 71 ALA C C 180.6900 0.3 1 239 72 72 LEU N N 119.2300 0.5 1 240 72 72 LEU H H 8.2300 0.03 1 241 73 73 LYS C C 178.5400 0.3 1 242 74 74 GLN N N 118.9100 0.5 1 243 74 74 GLN H H 8.0400 0.03 1 244 74 74 GLN CA C 58.8183 0.3 1 245 74 74 GLN CB C 28.5862 0.3 1 246 74 74 GLN C C 177.6000 0.3 1 247 75 75 ARG N N 116.7200 0.5 1 248 75 75 ARG H H 7.2200 0.03 1 249 75 75 ARG CA C 55.9069 0.3 1 250 75 75 ARG CB C 31.8401 0.3 1 251 75 75 ARG C C 174.3000 0.3 1 252 76 76 ALA N N 122.1200 0.5 1 253 76 76 ALA H H 8.0500 0.03 1 254 76 76 ALA CA C 53.0758 0.3 1 255 76 76 ALA CB C 16.6130 0.3 1 256 78 78 PRO CA C 62.7213 0.3 1 257 78 78 PRO CB C 32.8514 0.3 1 258 78 78 PRO C C 174.7300 0.3 1 259 79 79 PHE N N 110.0315 0.5 1 260 79 79 PHE H H 7.5531 0.03 1 261 79 79 PHE CA C 55.5560 0.3 1 262 79 79 PHE CB C 42.4121 0.3 1 263 79 79 PHE C C 172.7000 0.3 1 264 80 80 ILE N N 115.4500 0.5 1 265 80 80 ILE H H 8.0700 0.03 1 266 80 80 ILE CA C 59.0133 0.3 1 267 80 80 ILE CB C 43.2167 0.3 1 268 80 80 ILE C C 174.6000 0.3 1 269 81 81 LEU N N 125.0000 0.5 1 270 81 81 LEU H H 8.9400 0.03 1 271 81 81 LEU CA C 53.4276 0.3 1 272 81 81 LEU CB C 43.1740 0.3 1 273 86 86 LEU C C 178.6100 0.3 1 274 87 87 ASP N N 117.1000 0.5 1 275 87 87 ASP H H 8.3200 0.03 1 276 87 87 ASP CA C 55.9066 0.3 1 277 87 87 ASP CB C 40.5852 0.3 1 278 89 89 HIS C C 175.8660 0.3 1 279 90 90 GLY N N 108.1500 0.5 1 280 90 90 GLY H H 7.9100 0.03 1 281 90 90 GLY CA C 48.1576 0.3 1 282 92 92 LEU C C 178.6600 0.3 1 283 93 93 LEU N N 116.9700 0.5 1 284 93 93 LEU H H 8.1500 0.03 1 285 93 93 LEU CA C 57.7968 0.3 1 286 93 93 LEU CB C 40.6148 0.3 1 287 94 94 ARG CA C 58.2869 0.3 1 288 94 94 ARG CB C 30.4104 0.3 1 289 94 94 ARG C C 177.8100 0.3 1 290 95 95 LYS N N 118.2700 0.5 1 291 95 95 LYS H H 7.6300 0.03 1 292 95 95 LYS CA C 57.6608 0.3 1 293 95 95 LYS CB C 32.9060 0.3 1 294 99 99 PRO C C 179.1400 0.3 1 295 100 100 VAL N N 120.4900 0.5 1 296 100 100 VAL H H 8.2900 0.03 1 297 100 100 VAL CA C 60.4047 0.3 1 298 100 100 VAL CB C 34.9997 0.3 1 299 100 100 VAL C C 176.6900 0.3 1 300 101 101 MET N N 126.6900 0.5 1 301 101 101 MET H H 9.1200 0.03 1 302 101 101 MET CA C 54.7391 0.3 1 303 101 101 MET CB C 34.8295 0.3 1 304 104 104 PRO CA C 62.1713 0.3 1 305 104 104 PRO CB C 32.7723 0.3 1 306 104 104 PRO C C 175.7400 0.3 1 307 105 105 ALA N N 128.3894 0.5 1 308 105 105 ALA H H 8.3730 0.03 1 309 105 105 ALA CA C 52.4490 0.3 1 310 105 105 ALA CB C 19.3532 0.3 1 311 109 109 ASP CA C 56.9735 0.3 1 312 109 109 ASP CB C 40.8064 0.3 1 313 109 109 ASP C C 178.4200 0.3 1 314 110 110 VAL N N 119.9300 0.5 1 315 110 110 VAL H H 7.5500 0.03 1 316 110 110 VAL CA C 66.1980 0.3 1 317 110 110 VAL CB C 31.4651 0.3 1 318 110 110 VAL C C 176.4900 0.3 1 319 111 111 ALA N N 118.8500 0.5 1 320 111 111 ALA H H 7.5800 0.03 1 321 111 111 ALA CA C 54.6111 0.3 1 322 111 111 ALA CB C 16.5200 0.3 1 323 111 111 ALA C C 178.9500 0.3 1 324 112 112 LYS N N 115.7300 0.5 1 325 112 112 LYS H H 7.8100 0.03 1 326 112 112 LYS CA C 59.9597 0.3 1 327 112 112 LYS CB C 32.7224 0.3 1 328 112 112 LYS C C 172.2500 0.3 1 329 113 113 ARG N N 118.8500 0.5 1 330 113 113 ARG H H 7.8900 0.03 1 331 113 113 ARG CA C 58.2503 0.3 1 332 113 113 ARG CB C 29.6230 0.3 1 333 114 114 ALA CA C 55.1629 0.3 1 334 114 114 ALA CB C 18.1798 0.3 1 335 114 114 ALA C C 179.1700 0.3 1 336 115 115 LEU N N 116.3700 0.5 1 337 115 115 LEU H H 8.3300 0.03 1 338 115 115 LEU CA C 57.5101 0.3 1 339 115 115 LEU CB C 40.5852 0.3 1 340 115 115 LEU C C 180.5200 0.3 1 341 116 116 GLU N N 119.9300 0.5 1 342 116 116 GLU H H 7.8900 0.03 1 343 116 116 GLU CA C 58.7092 0.3 1 344 116 116 GLU CB C 29.5733 0.3 1 345 116 116 GLU C C 178.8700 0.3 1 346 117 117 MET N N 116.4200 0.5 1 347 117 117 MET H H 7.7000 0.03 1 348 117 117 MET CA C 57.7056 0.3 1 349 117 117 MET CB C 33.6080 0.3 1 350 117 117 MET C C 176.8800 0.3 1 351 118 118 CYS N N 114.1400 0.5 1 352 118 118 CYS H H 7.4300 0.03 1 353 118 118 CYS CA C 58.5300 0.3 1 354 118 118 CYS CB C 28.6083 0.3 1 355 118 118 CYS C C 174.7600 0.3 1 356 119 119 GLY N N 109.8000 0.5 1 357 119 119 GLY H H 8.0400 0.03 1 358 119 119 GLY CA C 45.7555 0.3 1 359 119 119 GLY C C 174.6800 0.3 1 360 120 120 GLY N N 108.8100 0.5 1 361 120 120 GLY H H 8.3000 0.03 1 362 120 120 GLY CA C 45.3648 0.3 1 363 121 121 ASP N N 120.8300 0.5 1 364 121 121 ASP H H 8.4200 0.03 1 365 121 121 ASP CA C 56.7487 0.3 1 366 121 121 ASP CB C 41.1310 0.3 1 367 124 124 PRO CA C 63.3520 0.3 1 368 124 124 PRO CB C 31.9875 0.3 1 369 124 124 PRO C C 175.7700 0.3 1 370 125 125 ALA N N 130.2800 0.5 1 371 125 125 ALA H H 8.0000 0.03 1 372 125 125 ALA CA C 53.7994 0.3 1 stop_ save_