data_27000 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Adenylate kinase R119A mutant Apo form ; _BMRB_accession_number 27000 _BMRB_flat_file_name bmr27000.str _Entry_type original _Submission_date 2017-01-19 _Accession_date 2017-01-19 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Adenylate kinase variant R119A in Apo form plus bound to Ap5A, ATP, and AMP' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rogne Per . . 2 Wolf-Watz Magnus . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 162 "15N chemical shifts" 162 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-11-22 update BMRB 'update entry citation' 2019-07-30 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 26999 'Adenylate kinase wild type Apo form' 27001 'Adenylate kinase R119K mutant Apo form' 27004 'Adenylate kinase wild type bound to Ap5A' 27005 'Adenylate kinase wild type bound to ATP' 27006 'Adenylate kinase wild type bound to AMP' 27007 'Adenylate kinase R119A mutant bound to Ap5A' 27008 'Adenylate kinase R119A mutant bound to ATP' 27009 'Adenylate kinase R119A mutant bound to AMP' 27010 'Adenylate kinase R119K mutant bound to Ap5A' stop_ _Original_release_date 2017-01-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Nucleation of an Activating Conformational Change by a Cation-pi Interaction ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31339702 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rogne Per . . 2 Andersson David . . 3 Grundstrom Christin . . 4 Sauer-Eriksson Elisabeth . . 5 Linusson Anna . . 6 Wolf-Watz Magnus . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 58 _Journal_issue 32 _Journal_ISSN 1520-4995 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3408 _Page_last 3412 _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name R119A _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label R119A $R119A 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_R119A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common R119A _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 214 _Mol_residue_sequence ; MRIILLGAPGAGKGTQAQFI MEKYGIPQISTGDMLRAAVK SGSELGKQAKDIMDAGKLVT DELVIALVKERIAQEDCRNG FLLDGFPRTIPQADAMKEAG INVDYVLEFDVPDELIVDAI VGRRVHAPSGRVYHVKFNPP KVEGKDDVTGEELTTRKDDQ EETVRKRLVEYHQMTAPLIG YYSKEAEAGNTKYAKVDGTK PVAEVRADLEKILG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ARG 3 ILE 4 ILE 5 LEU 6 LEU 7 GLY 8 ALA 9 PRO 10 GLY 11 ALA 12 GLY 13 LYS 14 GLY 15 THR 16 GLN 17 ALA 18 GLN 19 PHE 20 ILE 21 MET 22 GLU 23 LYS 24 TYR 25 GLY 26 ILE 27 PRO 28 GLN 29 ILE 30 SER 31 THR 32 GLY 33 ASP 34 MET 35 LEU 36 ARG 37 ALA 38 ALA 39 VAL 40 LYS 41 SER 42 GLY 43 SER 44 GLU 45 LEU 46 GLY 47 LYS 48 GLN 49 ALA 50 LYS 51 ASP 52 ILE 53 MET 54 ASP 55 ALA 56 GLY 57 LYS 58 LEU 59 VAL 60 THR 61 ASP 62 GLU 63 LEU 64 VAL 65 ILE 66 ALA 67 LEU 68 VAL 69 LYS 70 GLU 71 ARG 72 ILE 73 ALA 74 GLN 75 GLU 76 ASP 77 CYS 78 ARG 79 ASN 80 GLY 81 PHE 82 LEU 83 LEU 84 ASP 85 GLY 86 PHE 87 PRO 88 ARG 89 THR 90 ILE 91 PRO 92 GLN 93 ALA 94 ASP 95 ALA 96 MET 97 LYS 98 GLU 99 ALA 100 GLY 101 ILE 102 ASN 103 VAL 104 ASP 105 TYR 106 VAL 107 LEU 108 GLU 109 PHE 110 ASP 111 VAL 112 PRO 113 ASP 114 GLU 115 LEU 116 ILE 117 VAL 118 ASP 119 ALA 120 ILE 121 VAL 122 GLY 123 ARG 124 ARG 125 VAL 126 HIS 127 ALA 128 PRO 129 SER 130 GLY 131 ARG 132 VAL 133 TYR 134 HIS 135 VAL 136 LYS 137 PHE 138 ASN 139 PRO 140 PRO 141 LYS 142 VAL 143 GLU 144 GLY 145 LYS 146 ASP 147 ASP 148 VAL 149 THR 150 GLY 151 GLU 152 GLU 153 LEU 154 THR 155 THR 156 ARG 157 LYS 158 ASP 159 ASP 160 GLN 161 GLU 162 GLU 163 THR 164 VAL 165 ARG 166 LYS 167 ARG 168 LEU 169 VAL 170 GLU 171 TYR 172 HIS 173 GLN 174 MET 175 THR 176 ALA 177 PRO 178 LEU 179 ILE 180 GLY 181 TYR 182 TYR 183 SER 184 LYS 185 GLU 186 ALA 187 GLU 188 ALA 189 GLY 190 ASN 191 THR 192 LYS 193 TYR 194 ALA 195 LYS 196 VAL 197 ASP 198 GLY 199 THR 200 LYS 201 PRO 202 VAL 203 ALA 204 GLU 205 VAL 206 ARG 207 ALA 208 ASP 209 LEU 210 GLU 211 LYS 212 ILE 213 LEU 214 GLY 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 $R119A 'E. coli' 562 Bacteria . Escherichia coli 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 $R119A 'recombinant technology' . Escherichia coli . pEAK91 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_R119A_Apo _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $R119A 200 uM [U-15N] MOPS 30 mM 'natural abundance' NaCl 50 mM 'natural abundance' TMSP 100 uM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.2 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . 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_ANSIG _Saveframe_category software _Name ANSIG _Version . loop_ _Vendor _Address _Electronic_address Kraulis . . stop_ loop_ _Task 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AvanceIIIHD _Field_strength 850 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $R119A_Apo 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' 80 . mM pH 7 . pH pressure 1 . atm temperature 298 . 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 TMSP H 1 'methyl protons' ppm 0 internal direct . . . 1 TMSP N 15 'methyl protons' ppm 118 internal 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_chemical_shifts_R119A_Apo _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $NMRPipe stop_ loop_ _Experiment_label '2D 1H-15N HSQC' stop_ loop_ _Sample_label $R119A_Apo stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name R119A _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 ARG H H 9.605 0.01 1 2 2 2 ARG N N 127.756 0.02 1 3 4 4 ILE H H 8.56 0.01 1 4 4 4 ILE N N 126.096 0.02 1 5 5 5 LEU H H 8.159 0.01 1 6 5 5 LEU N N 128.854 0.02 1 7 6 6 LEU H H 9.396 0.01 1 8 6 6 LEU N N 128.846 0.02 1 9 7 7 GLY H H 8.036 0.01 1 10 7 7 GLY N N 108.417 0.02 1 11 10 10 GLY H H 8.204 0.01 1 12 10 10 GLY N N 111.147 0.02 1 13 18 18 GLN H H 7.621 0.01 1 14 18 18 GLN N N 115.062 0.02 1 15 20 20 ILE H H 7.89 0.01 1 16 20 20 ILE N N 120.111 0.02 1 17 21 21 MET H H 8.325 0.01 1 18 21 21 MET N N 118.265 0.02 1 19 22 22 GLU H H 7.795 0.01 1 20 22 22 GLU N N 117.43 0.02 1 21 23 23 LYS H H 8.199 0.01 1 22 23 23 LYS N N 120.468 0.02 1 23 24 24 TYR H H 7.62 0.01 1 24 24 24 TYR N N 112.403 0.02 1 25 25 25 GLY H H 7.639 0.01 1 26 25 25 GLY N N 111.591 0.02 1 27 28 28 GLN H H 8.202 0.01 1 28 28 28 GLN N N 119.031 0.02 1 29 29 29 ILE H H 9.291 0.01 1 30 29 29 ILE N N 127.078 0.02 1 31 31 31 THR H H 9.257 0.01 1 32 31 31 THR N N 118.307 0.02 1 33 32 32 GLY H H 8.631 0.01 1 34 32 32 GLY N N 110.012 0.02 1 35 33 33 ASP H H 7.392 0.01 1 36 33 33 ASP N N 121.522 0.02 1 37 34 34 MET H H 8.106 0.01 1 38 34 34 MET N N 120.489 0.02 1 39 35 35 LEU H H 8.344 0.01 1 40 35 35 LEU N N 121.42 0.02 1 41 36 36 ARG H H 7.615 0.01 1 42 36 36 ARG N N 117.774 0.02 1 43 37 37 ALA H H 7.957 0.01 1 44 37 37 ALA N N 120.205 0.02 1 45 39 39 VAL H H 7.993 0.01 1 46 39 39 VAL N N 116.837 0.02 1 47 40 40 LYS H H 7.596 0.01 1 48 40 40 LYS N N 119.226 0.02 1 49 41 41 SER H H 7.845 0.01 1 50 41 41 SER N N 113.652 0.02 1 51 42 42 GLY H H 7.829 0.01 1 52 42 42 GLY N N 109.827 0.02 1 53 43 43 SER H H 7.789 0.01 1 54 43 43 SER N N 115.479 0.02 1 55 44 44 GLU H H 8.89 0.01 1 56 44 44 GLU N N 122.755 0.02 1 57 45 45 LEU H H 8.415 0.01 1 58 45 45 LEU N N 119.32 0.02 1 59 46 46 GLY H H 8.048 0.01 1 60 46 46 GLY N N 108.044 0.02 1 61 47 47 LYS H H 8.307 0.01 1 62 47 47 LYS N N 122.32 0.02 1 63 48 48 GLN H H 7.526 0.01 1 64 48 48 GLN N N 118.769 0.02 1 65 49 49 ALA H H 8.264 0.01 1 66 49 49 ALA N N 120.733 0.02 1 67 50 50 LYS H H 8.375 0.01 1 68 50 50 LYS N N 119.672 0.02 1 69 51 51 ASP H H 7.914 0.01 1 70 51 51 ASP N N 118.423 0.02 1 71 52 52 ILE H H 7.488 0.01 1 72 52 52 ILE N N 120.984 0.02 1 73 53 53 MET H H 8.309 0.01 1 74 53 53 MET N N 119.403 0.02 1 75 54 54 ASP H H 9.201 0.01 1 76 54 54 ASP N N 122.189 0.02 1 77 55 55 ALA H H 7.232 0.01 1 78 55 55 ALA N N 119.841 0.02 1 79 56 56 GLY H H 7.964 0.01 1 80 56 56 GLY N N 107.757 0.02 1 81 57 57 LYS H H 7.463 0.01 1 82 57 57 LYS N N 119.399 0.02 1 83 58 58 LEU H H 7.832 0.01 1 84 58 58 LEU N N 119.387 0.02 1 85 59 59 VAL H H 8.241 0.01 1 86 59 59 VAL N N 121.602 0.02 1 87 60 60 THR H H 6.992 0.01 1 88 60 60 THR N N 116.644 0.02 1 89 61 61 ASP H H 8.864 0.01 1 90 61 61 ASP N N 121.923 0.02 1 91 62 62 GLU H H 8.684 0.01 1 92 62 62 GLU N N 117.227 0.02 1 93 63 63 LEU H H 7.395 0.01 1 94 63 63 LEU N N 122.487 0.02 1 95 65 65 ILE H H 8.306 0.01 1 96 65 65 ILE N N 118.967 0.02 1 97 66 66 ALA H H 7.511 0.01 1 98 66 66 ALA N N 122.581 0.02 1 99 67 67 LEU H H 8.205 0.01 1 100 67 67 LEU N N 119.964 0.02 1 101 68 68 VAL H H 8.46 0.01 1 102 68 68 VAL N N 123.178 0.02 1 103 69 69 LYS H H 8.291 0.01 1 104 69 69 LYS N N 118.676 0.02 1 105 70 70 GLU H H 7.418 0.01 1 106 70 70 GLU N N 117.255 0.02 1 107 72 72 ILE H H 8.154 0.01 1 108 72 72 ILE N N 110.688 0.02 1 109 73 73 ALA H H 6.996 0.01 1 110 73 73 ALA N N 122.421 0.02 1 111 74 74 GLN H H 7.2 0.01 1 112 74 74 GLN N N 116.821 0.02 1 113 75 75 GLU H H 8.93 0.01 1 114 75 75 GLU N N 122.27 0.02 1 115 76 76 ASP H H 8.425 0.01 1 116 76 76 ASP N N 117.131 0.02 1 117 77 77 CYS H H 7.672 0.01 1 118 77 77 CYS N N 118.142 0.02 1 119 78 78 ARG H H 7.628 0.01 1 120 78 78 ARG N N 122.65 0.02 1 121 80 80 GLY H H 7.648 0.01 1 122 80 80 GLY N N 108.975 0.02 1 123 81 81 PHE H H 7.341 0.01 1 124 81 81 PHE N N 108.467 0.02 1 125 82 82 LEU H H 8.789 0.01 1 126 82 82 LEU N N 122.475 0.02 1 127 83 83 LEU H H 9.458 0.01 1 128 83 83 LEU N N 128.119 0.02 1 129 85 85 GLY H H 8.866 0.01 1 130 85 85 GLY N N 113.146 0.02 1 131 86 86 PHE H H 7.317 0.01 1 132 86 86 PHE N N 120.198 0.02 1 133 88 88 ARG H H 8.554 0.01 1 134 88 88 ARG N N 114.517 0.02 1 135 89 89 THR H H 7.059 0.01 1 136 89 89 THR N N 107.075 0.02 1 137 90 90 ILE H H 8.968 0.01 1 138 90 90 ILE N N 121.533 0.02 1 139 92 92 GLN H H 7.213 0.01 1 140 92 92 GLN N N 116.539 0.02 1 141 93 93 ALA H H 7.683 0.01 1 142 93 93 ALA N N 124.927 0.02 1 143 95 95 ALA H H 8.032 0.01 1 144 95 95 ALA N N 123.06 0.02 1 145 97 97 LYS H H 7.52 0.01 1 146 97 97 LYS N N 120.794 0.02 1 147 98 98 GLU H H 8.413 0.01 1 148 98 98 GLU N N 121.432 0.02 1 149 99 99 ALA H H 7.466 0.01 1 150 99 99 ALA N N 113.186 0.02 1 151 100 100 GLY H H 7.806 0.01 1 152 100 100 GLY N N 106.645 0.02 1 153 101 101 ILE H H 8.025 0.01 1 154 101 101 ILE N N 122.001 0.02 1 155 102 102 ASN H H 7.846 0.01 1 156 102 102 ASN N N 123.598 0.02 1 157 103 103 VAL H H 8.348 0.01 1 158 103 103 VAL N N 113.074 0.02 1 159 105 105 TYR H H 7.563 0.01 1 160 105 105 TYR N N 114.373 0.02 1 161 106 106 VAL H H 8.911 0.01 1 162 106 106 VAL N N 123.428 0.02 1 163 107 107 LEU H H 8.84 0.01 1 164 107 107 LEU N N 124.539 0.02 1 165 108 108 GLU H H 8.743 0.01 1 166 108 108 GLU N N 124.686 0.02 1 167 109 109 PHE H H 9.18 0.01 1 168 109 109 PHE N N 130.69 0.02 1 169 110 110 ASP H H 8.682 0.01 1 170 110 110 ASP N N 128.959 0.02 1 171 111 111 VAL H H 7.351 0.01 1 172 111 111 VAL N N 125.694 0.02 1 173 113 113 ASP H H 8.789 0.01 1 174 113 113 ASP N N 123.861 0.02 1 175 114 114 GLU H H 8.971 0.01 1 176 114 114 GLU N N 114.761 0.02 1 177 121 121 VAL H H 8.877 0.01 1 178 121 121 VAL N N 114.97 0.02 1 179 122 122 GLY H H 7.212 0.01 1 180 122 122 GLY N N 105.267 0.02 1 181 123 123 ARG H H 7.585 0.01 1 182 123 123 ARG N N 120.455 0.02 1 183 124 124 ARG H H 8.785 0.01 1 184 124 124 ARG N N 125.307 0.02 1 185 127 127 ALA H H 9 0.01 1 186 127 127 ALA N N 129.633 0.02 1 187 129 129 SER H H 6.716 0.01 1 188 129 129 SER N N 107.49 0.02 1 189 130 130 GLY H H 8.535 0.01 1 190 130 130 GLY N N 113.121 0.02 1 191 131 131 ARG H H 8.391 0.01 1 192 131 131 ARG N N 122.198 0.02 1 193 132 132 VAL H H 7.852 0.01 1 194 132 132 VAL N N 119.99 0.02 1 195 133 133 TYR H H 9.152 0.01 1 196 133 133 TYR N N 124.373 0.02 1 197 134 134 HIS H H 8.322 0.01 1 198 134 134 HIS N N 120.844 0.02 1 199 136 136 LYS H H 9.396 0.01 1 200 136 136 LYS N N 119.972 0.02 1 201 138 138 ASN H H 8.553 0.01 1 202 138 138 ASN N N 114.182 0.02 1 203 141 141 LYS H H 10.031 0.01 1 204 141 141 LYS N N 124.196 0.02 1 205 143 143 GLU H H 8.071 0.01 1 206 143 143 GLU N N 125.587 0.02 1 207 144 144 GLY H H 8.835 0.01 1 208 144 144 GLY N N 111.79 0.02 1 209 145 145 LYS H H 7.914 0.01 1 210 145 145 LYS N N 119.315 0.02 1 211 146 146 ASP H H 8.974 0.01 1 212 146 146 ASP N N 119.941 0.02 1 213 147 147 ASP H H 7.815 0.01 1 214 147 147 ASP N N 127.151 0.02 1 215 148 148 VAL H H 6.271 0.01 1 216 148 148 VAL N N 114.969 0.02 1 217 149 149 THR H H 7.402 0.01 1 218 149 149 THR N N 105.479 0.02 1 219 150 150 GLY H H 7.789 0.01 1 220 150 150 GLY N N 111.135 0.02 1 221 151 151 GLU H H 7.505 0.01 1 222 151 151 GLU N N 118.756 0.02 1 223 152 152 GLU H H 8.619 0.01 1 224 152 152 GLU N N 119.596 0.02 1 225 153 153 LEU H H 7.841 0.01 1 226 153 153 LEU N N 120.949 0.02 1 227 154 154 THR H H 9.239 0.01 1 228 154 154 THR N N 114.277 0.02 1 229 155 155 THR H H 8.303 0.01 1 230 155 155 THR N N 115.623 0.02 1 231 156 156 ARG H H 9.719 0.01 1 232 156 156 ARG N N 127.203 0.02 1 233 158 158 ASP H H 8.302 0.01 1 234 158 158 ASP N N 114.61 0.02 1 235 161 161 GLU H H 9.123 0.01 1 236 161 161 GLU N N 124.455 0.02 1 237 162 162 GLU H H 9.172 0.01 1 238 162 162 GLU N N 116.499 0.02 1 239 163 163 THR H H 7.115 0.01 1 240 163 163 THR N N 116.298 0.02 1 241 164 164 VAL H H 8.179 0.01 1 242 164 164 VAL N N 123.134 0.02 1 243 165 165 ARG H H 8.712 0.01 1 244 165 165 ARG N N 116.912 0.02 1 245 166 166 LYS H H 7.658 0.01 1 246 166 166 LYS N N 120.071 0.02 1 247 168 168 LEU H H 8.058 0.01 1 248 168 168 LEU N N 121.533 0.02 1 249 171 171 TYR H H 8.118 0.01 1 250 171 171 TYR N N 120.219 0.02 1 251 173 173 GLN H H 8.463 0.01 1 252 173 173 GLN N N 118.888 0.02 1 253 174 174 MET H H 7.724 0.01 1 254 174 174 MET N N 115.617 0.02 1 255 175 175 THR H H 8.128 0.01 1 256 175 175 THR N N 113.484 0.02 1 257 176 176 ALA H H 8.35 0.01 1 258 176 176 ALA N N 125.997 0.02 1 259 178 178 LEU H H 6.861 0.01 1 260 178 178 LEU N N 119.157 0.02 1 261 179 179 ILE H H 8.371 0.01 1 262 179 179 ILE N N 121.081 0.02 1 263 180 180 GLY H H 7.803 0.01 1 264 180 180 GLY N N 107.613 0.02 1 265 181 181 TYR H H 7.875 0.01 1 266 181 181 TYR N N 123.709 0.02 1 267 182 182 TYR H H 8.848 0.01 1 268 182 182 TYR N N 118.745 0.02 1 269 184 184 LYS H H 7.364 0.01 1 270 184 184 LYS N N 123.517 0.02 1 271 185 185 GLU H H 7.927 0.01 1 272 185 185 GLU N N 120.868 0.02 1 273 186 186 ALA H H 8.285 0.01 1 274 186 186 ALA N N 122.805 0.02 1 275 187 187 GLU H H 7.898 0.01 1 276 187 187 GLU N N 122.059 0.02 1 277 188 188 ALA H H 7.417 0.01 1 278 188 188 ALA N N 118.725 0.02 1 279 189 189 GLY H H 7.744 0.01 1 280 189 189 GLY N N 105.252 0.02 1 281 190 190 ASN H H 8.09 0.01 1 282 190 190 ASN N N 117.214 0.02 1 283 191 191 THR H H 7.448 0.01 1 284 191 191 THR N N 113.716 0.02 1 285 192 192 LYS H H 7.769 0.01 1 286 192 192 LYS N N 122.559 0.02 1 287 193 193 TYR H H 8.237 0.01 1 288 193 193 TYR N N 123.782 0.02 1 289 194 194 ALA H H 8.195 0.01 1 290 194 194 ALA N N 130.136 0.02 1 291 195 195 LYS H H 8.256 0.01 1 292 195 195 LYS N N 122.626 0.02 1 293 196 196 VAL H H 9.022 0.01 1 294 196 196 VAL N N 125.537 0.02 1 295 197 197 ASP H H 8.645 0.01 1 296 197 197 ASP N N 124.755 0.02 1 297 198 198 GLY H H 8.325 0.01 1 298 198 198 GLY N N 112.077 0.02 1 299 199 199 THR H H 8.545 0.01 1 300 199 199 THR N N 111.35 0.02 1 301 200 200 LYS H H 6.518 0.01 1 302 200 200 LYS N N 121.628 0.02 1 303 202 202 VAL H H 8.395 0.01 1 304 202 202 VAL N N 123.499 0.02 1 305 204 204 GLU H H 7.351 0.01 1 306 204 204 GLU N N 117.804 0.02 1 307 205 205 VAL H H 7.801 0.01 1 308 205 205 VAL N N 121.191 0.02 1 309 206 206 ARG H H 7.875 0.01 1 310 206 206 ARG N N 118.572 0.02 1 311 207 207 ALA H H 7.181 0.01 1 312 207 207 ALA N N 120.45 0.02 1 313 208 208 ASP H H 8.21 0.01 1 314 208 208 ASP N N 121.333 0.02 1 315 209 209 LEU H H 8.451 0.01 1 316 209 209 LEU N N 120.518 0.02 1 317 210 210 GLU H H 8.381 0.01 1 318 210 210 GLU N N 118.895 0.02 1 319 212 212 ILE H H 7.546 0.01 1 320 212 212 ILE N N 119.257 0.02 1 321 213 213 LEU H H 8.049 0.01 1 322 213 213 LEU N N 117.1 0.02 1 323 214 214 GLY H H 7.556 0.01 1 324 214 214 GLY N N 112.535 0.02 1 stop_ save_