data_26999 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Adenylate kinase in Apo form ; _BMRB_accession_number 26999 _BMRB_flat_file_name bmr26999.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 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" 190 "15N chemical shifts" 190 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 27000 'Adenylate kinase R119A mutant 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 AdKw _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label AdK $Wild_type 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_Wild_type _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Wild_type _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 214 _Mol_residue_sequence ; MRIILLGAPGAGKGTQAQFI MEKYGIPQISTGDMLRAAVK SGSELGKQAKDIMDAGKLVT DELVIALVKERIAQEDCRNG FLLDGFPRTIPQADAMKEAG INVDYVLEFDVPDELIVDRI 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 ARG 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 $Wild_type '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 $Wild_type 'recombinant technology' . Escherichia coli . pEAK91 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_ApoWT_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Wild_type 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 'chemical shift assignment' '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 $ApoWT_sample 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_AdK_Apo _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $NMRPipe stop_ loop_ _Experiment_label '2D 1H-15N HSQC' stop_ loop_ _Sample_label $ApoWT_sample stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name AdK _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 9.601 0.01 1 2 2 2 ARG N N 127.752 0.02 1 3 3 3 ILE H H 8.513 0.01 1 4 3 3 ILE N N 124.681 0.02 1 5 4 4 ILE H H 8.55 0.01 1 6 4 4 ILE N N 126.041 0.02 1 7 5 5 LEU H H 8.027 0.01 1 8 5 5 LEU N N 128.805 0.02 1 9 6 6 LEU H H 9.394 0.01 1 10 6 6 LEU N N 128.985 0.02 1 11 7 7 GLY H H 8.027 0.01 1 12 7 7 GLY N N 108.418 0.02 1 13 8 8 ALA H H 9.199 0.01 1 14 8 8 ALA N N 126.779 0.02 1 15 10 10 GLY H H 8.248 0.01 1 16 10 10 GLY N N 111.581 0.02 1 17 11 11 ALA H H 8.159 0.01 1 18 11 11 ALA N N 121.25 0.02 1 19 13 13 LYS H H 8.039 0.01 1 20 13 13 LYS N N 120.839 0.02 1 21 16 16 GLN H H 6.926 0.01 1 22 16 16 GLN N N 117.679 0.02 1 23 17 17 ALA H H 7.97 0.01 1 24 17 17 ALA N N 122.556 0.02 1 25 18 18 GLN H H 7.6 0.01 1 26 18 18 GLN N N 114.938 0.02 1 27 19 19 PHE H H 6.91 0.01 1 28 19 19 PHE N N 118.737 0.02 1 29 20 20 ILE H H 7.875 0.01 1 30 20 20 ILE N N 120.16 0.02 1 31 21 21 MET H H 8.335 0.01 1 32 21 21 MET N N 118.258 0.02 1 33 22 22 GLU H H 7.777 0.01 1 34 22 22 GLU N N 117.401 0.02 1 35 23 23 LYS H H 8.2 0.01 1 36 23 23 LYS N N 120.462 0.02 1 37 24 24 TYR H H 7.621 0.01 1 38 24 24 TYR N N 112.409 0.02 1 39 25 25 GLY H H 7.642 0.01 1 40 25 25 GLY N N 111.578 0.02 1 41 28 28 GLN H H 8.21 0.01 1 42 28 28 GLN N N 119.021 0.02 1 43 29 29 ILE H H 9.288 0.01 1 44 29 29 ILE N N 127.061 0.02 1 45 30 30 SER H H 8.206318 0.01 1 46 30 30 SER N N 120.0969 0.02 1 47 31 31 THR H H 9.248 0.01 1 48 31 31 THR N N 118.186 0.02 1 49 32 32 GLY H H 8.631 0.01 1 50 32 32 GLY N N 110.038 0.02 1 51 33 33 ASP H H 7.388 0.01 1 52 33 33 ASP N N 121.517 0.02 1 53 34 34 MET H H 8.104 0.01 1 54 34 34 MET N N 120.486 0.02 1 55 35 35 LEU H H 8.353 0.01 1 56 35 35 LEU N N 121.438 0.02 1 57 36 36 ARG H H 7.615 0.01 1 58 36 36 ARG N N 117.756 0.02 1 59 37 37 ALA H H 7.953 0.01 1 60 37 37 ALA N N 120.205 0.02 1 61 38 38 ALA H H 8.052 0.01 1 62 38 38 ALA N N 122.137 0.02 1 63 39 39 VAL H H 7.995 0.01 1 64 39 39 VAL N N 116.837 0.02 1 65 40 40 LYS H H 7.596 0.01 1 66 40 40 LYS N N 119.233 0.02 1 67 41 41 SER H H 7.846 0.01 1 68 41 41 SER N N 113.646 0.02 1 69 42 42 GLY H H 7.829 0.01 1 70 42 42 GLY N N 109.828 0.02 1 71 43 43 SER H H 7.789 0.01 1 72 43 43 SER N N 115.466 0.02 1 73 44 44 GLU H H 8.892 0.01 1 74 44 44 GLU N N 122.781 0.02 1 75 45 45 LEU H H 8.416 0.01 1 76 45 45 LEU N N 119.329 0.02 1 77 46 46 GLY H H 8.047 0.01 1 78 46 46 GLY N N 108.025 0.02 1 79 47 47 LYS H H 8.304 0.01 1 80 47 47 LYS N N 122.325 0.02 1 81 48 48 GLN H H 7.529 0.01 1 82 48 48 GLN N N 118.77 0.02 1 83 49 49 ALA H H 8.267 0.01 1 84 49 49 ALA N N 120.722 0.02 1 85 50 50 LYS H H 8.376 0.01 1 86 50 50 LYS N N 119.673 0.02 1 87 51 51 ASP H H 7.913 0.01 1 88 51 51 ASP N N 118.418 0.02 1 89 52 52 ILE H H 7.489 0.01 1 90 52 52 ILE N N 121.004 0.02 1 91 53 53 MET H H 8.309 0.01 1 92 53 53 MET N N 119.393 0.02 1 93 54 54 ASP H H 9.201 0.01 1 94 54 54 ASP N N 122.193 0.02 1 95 55 55 ALA H H 7.233 0.01 1 96 55 55 ALA N N 119.829 0.02 1 97 56 56 GLY H H 7.963 0.01 1 98 56 56 GLY N N 107.755 0.02 1 99 57 57 LYS H H 7.464 0.01 1 100 57 57 LYS N N 119.388 0.02 1 101 58 58 LEU H H 7.833 0.01 1 102 58 58 LEU N N 119.386 0.02 1 103 59 59 VAL H H 8.241 0.01 1 104 59 59 VAL N N 121.613 0.02 1 105 60 60 THR H H 6.999 0.01 1 106 60 60 THR N N 116.685 0.02 1 107 61 61 ASP H H 8.866 0.01 1 108 61 61 ASP N N 121.917 0.02 1 109 62 62 GLU H H 8.683 0.01 1 110 62 62 GLU N N 117.232 0.02 1 111 63 63 LEU H H 7.395 0.01 1 112 63 63 LEU N N 122.493 0.02 1 113 65 65 ILE H H 8.303 0.01 1 114 65 65 ILE N N 118.953 0.02 1 115 66 66 ALA H H 7.509 0.01 1 116 66 66 ALA N N 122.565 0.02 1 117 67 67 LEU H H 8.206 0.01 1 118 67 67 LEU N N 119.96 0.02 1 119 68 68 VAL H H 8.464 0.01 1 120 68 68 VAL N N 123.177 0.02 1 121 69 69 LYS H H 8.293 0.01 1 122 69 69 LYS N N 118.667 0.02 1 123 70 70 GLU H H 7.417 0.01 1 124 70 70 GLU N N 117.251 0.02 1 125 71 71 ARG H H 8.12 0.01 1 126 71 71 ARG N N 121.442 0.02 1 127 72 72 ILE H H 8.158 0.01 1 128 72 72 ILE N N 110.689 0.02 1 129 73 73 ALA H H 6.997 0.01 1 130 73 73 ALA N N 122.451 0.02 1 131 74 74 GLN H H 7.198 0.01 1 132 74 74 GLN N N 116.826 0.02 1 133 75 75 GLU H H 8.93 0.01 1 134 75 75 GLU N N 122.269 0.02 1 135 76 76 ASP H H 8.428 0.01 1 136 76 76 ASP N N 117.14 0.02 1 137 77 77 CYS H H 7.673 0.01 1 138 77 77 CYS N N 118.163 0.02 1 139 78 78 ARG H H 7.63 0.01 1 140 78 78 ARG N N 122.67 0.02 1 141 79 79 ASN H H 8.873 0.01 1 142 79 79 ASN N N 115.387 0.02 1 143 80 80 GLY H H 7.649 0.01 1 144 80 80 GLY N N 108.971 0.02 1 145 81 81 PHE H H 7.342 0.01 1 146 81 81 PHE N N 108.454 0.02 1 147 82 82 LEU H H 8.796 0.01 1 148 82 82 LEU N N 122.442 0.02 1 149 83 83 LEU H H 9.435 0.01 1 150 83 83 LEU N N 127.98 0.02 1 151 85 85 GLY H H 8.911 0.01 1 152 85 85 GLY N N 113.201 0.02 1 153 86 86 PHE H H 7.309 0.01 1 154 86 86 PHE N N 120.1 0.02 1 155 88 88 ARG H H 8.567 0.01 1 156 88 88 ARG N N 114.606 0.02 1 157 89 89 THR H H 7.058 0.01 1 158 89 89 THR N N 107.084 0.02 1 159 90 90 ILE H H 8.966 0.01 1 160 90 90 ILE N N 121.544 0.02 1 161 92 92 GLN H H 7.215 0.01 1 162 92 92 GLN N N 116.531 0.02 1 163 93 93 ALA H H 7.682 0.01 1 164 93 93 ALA N N 124.944 0.02 1 165 94 94 ASP H H 8.745 0.01 1 166 94 94 ASP N N 119.561 0.02 1 167 95 95 ALA H H 8.034 0.01 1 168 95 95 ALA N N 123.061 0.02 1 169 97 97 LYS H H 7.521 0.01 1 170 97 97 LYS N N 120.812 0.02 1 171 98 98 GLU H H 8.409 0.01 1 172 98 98 GLU N N 121.416 0.02 1 173 99 99 ALA H H 7.464 0.01 1 174 99 99 ALA N N 113.181 0.02 1 175 100 100 GLY H H 7.807 0.01 1 176 100 100 GLY N N 106.636 0.02 1 177 101 101 ILE H H 8.025 0.01 1 178 101 101 ILE N N 121.986 0.02 1 179 102 102 ASN H H 7.842 0.01 1 180 102 102 ASN N N 123.543 0.02 1 181 103 103 VAL H H 8.329 0.01 1 182 103 103 VAL N N 113.174 0.02 1 183 105 105 TYR H H 7.556 0.01 1 184 105 105 TYR N N 114.35 0.02 1 185 106 106 VAL H H 8.928 0.01 1 186 106 106 VAL N N 123.478 0.02 1 187 107 107 LEU H H 8.847 0.01 1 188 107 107 LEU N N 124.484 0.02 1 189 108 108 GLU H H 8.756 0.01 1 190 108 108 GLU N N 124.638 0.02 1 191 109 109 PHE H H 9.21 0.01 1 192 109 109 PHE N N 130.805 0.02 1 193 110 110 ASP H H 8.666 0.01 1 194 110 110 ASP N N 128.795 0.02 1 195 111 111 VAL H H 7.317 0.01 1 196 111 111 VAL N N 126.064 0.02 1 197 113 113 ASP H H 8.817 0.01 1 198 113 113 ASP N N 124.082 0.02 1 199 114 114 GLU H H 8.939 0.01 1 200 114 114 GLU N N 114.492 0.02 1 201 115 115 LEU H H 7.031 0.01 1 202 115 115 LEU N N 119.216 0.02 1 203 116 116 ILE H H 7.349 0.01 1 204 116 116 ILE N N 120.855 0.02 1 205 117 117 VAL H H 8.237 0.01 1 206 117 117 VAL N N 117.046 0.02 1 207 118 118 ASP H H 7.7 0.01 1 208 118 118 ASP N N 117.168 0.02 1 209 119 119 ARG H H 8.021 0.01 1 210 119 119 ARG N N 116.712 0.02 1 211 120 120 ILE H H 7.96 0.01 1 212 120 120 ILE N N 119.13 0.02 1 213 121 121 VAL H H 8.885 0.01 1 214 121 121 VAL N N 114.995 0.02 1 215 122 122 GLY H H 7.365 0.01 1 216 122 122 GLY N N 106.218 0.02 1 217 123 123 ARG H H 7.624 0.01 1 218 123 123 ARG N N 120.707 0.02 1 219 124 124 ARG H H 8.793 0.01 1 220 124 124 ARG N N 125.626 0.02 1 221 126 126 HIS H H 9.122 0.01 1 222 126 126 HIS N N 126.841 0.02 1 223 127 127 ALA H H 9 0.01 1 224 127 127 ALA N N 129.672 0.02 1 225 129 129 SER H H 6.715 0.01 1 226 129 129 SER N N 107.475 0.02 1 227 130 130 GLY H H 8.537 0.01 1 228 130 130 GLY N N 113.137 0.02 1 229 131 131 ARG H H 8.395 0.01 1 230 131 131 ARG N N 122.203 0.02 1 231 132 132 VAL H H 7.85 0.01 1 232 132 132 VAL N N 120.011 0.02 1 233 133 133 TYR H H 9.162 0.01 1 234 133 133 TYR N N 124.425 0.02 1 235 134 134 HIS H H 8.34 0.01 1 236 134 134 HIS N N 120.859 0.02 1 237 135 135 VAL H H 8.12 0.01 1 238 135 135 VAL N N 120.863 0.02 1 239 136 136 LYS H H 9.467 0.01 1 240 136 136 LYS N N 119.952 0.02 1 241 137 137 PHE H H 8.096 0.01 1 242 137 137 PHE N N 116.9 0.02 1 243 138 138 ASN H H 8.556 0.01 1 244 138 138 ASN N N 114.284 0.02 1 245 141 141 LYS H H 10.033 0.01 1 246 141 141 LYS N N 124.205 0.02 1 247 142 142 VAL H H 8.773 0.01 1 248 142 142 VAL N N 120.69 0.02 1 249 143 143 GLU H H 8.072 0.01 1 250 143 143 GLU N N 125.584 0.02 1 251 144 144 GLY H H 8.827 0.01 1 252 144 144 GLY N N 111.781 0.02 1 253 145 145 LYS H H 7.91 0.01 1 254 145 145 LYS N N 119.315 0.02 1 255 146 146 ASP H H 8.971 0.01 1 256 146 146 ASP N N 119.915 0.02 1 257 147 147 ASP H H 7.811 0.01 1 258 147 147 ASP N N 127.137 0.02 1 259 148 148 VAL H H 6.271 0.01 1 260 148 148 VAL N N 114.981 0.02 1 261 149 149 THR H H 7.404 0.01 1 262 149 149 THR N N 105.493 0.02 1 263 150 150 GLY H H 7.788 0.01 1 264 150 150 GLY N N 111.133 0.02 1 265 151 151 GLU H H 7.503 0.01 1 266 151 151 GLU N N 118.749 0.02 1 267 152 152 GLU H H 8.62 0.01 1 268 152 152 GLU N N 119.615 0.02 1 269 153 153 LEU H H 7.84 0.01 1 270 153 153 LEU N N 120.939 0.02 1 271 154 154 THR H H 9.246 0.01 1 272 154 154 THR N N 114.332 0.02 1 273 155 155 THR H H 8.317 0.01 1 274 155 155 THR N N 115.938 0.02 1 275 156 156 ARG H H 9.738 0.01 1 276 156 156 ARG N N 127.362 0.02 1 277 158 158 ASP H H 8.305 0.01 1 278 158 158 ASP N N 114.548 0.02 1 279 159 159 ASP H H 7.361 0.01 1 280 159 159 ASP N N 116.501 0.02 1 281 160 160 GLN H H 6.964 0.01 1 282 160 160 GLN N N 117.382 0.02 1 283 161 161 GLU H H 9.135 0.01 1 284 161 161 GLU N N 124.535 0.02 1 285 162 162 GLU H H 9.182 0.01 1 286 162 162 GLU N N 116.482 0.02 1 287 163 163 THR H H 7.112 0.01 1 288 163 163 THR N N 116.295 0.02 1 289 164 164 VAL H H 8.167 0.01 1 290 164 164 VAL N N 123.046 0.02 1 291 165 165 ARG H H 8.701 0.01 1 292 165 165 ARG N N 116.814 0.02 1 293 166 166 LYS H H 7.667 0.01 1 294 166 166 LYS N N 120.144 0.02 1 295 167 167 ARG H H 7.969 0.01 1 296 167 167 ARG N N 118.588 0.02 1 297 168 168 LEU H H 8.046 0.01 1 298 168 168 LEU N N 121.51 0.02 1 299 171 171 TYR H H 8.105 0.01 1 300 171 171 TYR N N 120.114 0.02 1 301 172 172 HIS H H 8.781714 0.01 1 302 172 172 HIS N N 120.8233 0.02 1 303 173 173 GLN H H 8.462 0.01 1 304 173 173 GLN N N 118.884 0.02 1 305 174 174 MET H H 7.672 0.01 1 306 174 174 MET N N 115.455 0.02 1 307 175 175 THR H H 8.16 0.01 1 308 175 175 THR N N 113.558 0.02 1 309 176 176 ALA H H 8.407 0.01 1 310 176 176 ALA N N 126.082 0.02 1 311 178 178 LEU H H 6.838 0.01 1 312 178 178 LEU N N 119.118 0.02 1 313 179 179 ILE H H 8.388 0.01 1 314 179 179 ILE N N 121.069 0.02 1 315 180 180 GLY H H 7.815 0.01 1 316 180 180 GLY N N 107.651 0.02 1 317 181 181 TYR H H 7.867 0.01 1 318 181 181 TYR N N 123.742 0.02 1 319 182 182 TYR H H 8.854 0.01 1 320 182 182 TYR N N 118.771 0.02 1 321 184 184 LYS H H 7.357 0.01 1 322 184 184 LYS N N 123.53 0.02 1 323 185 185 GLU H H 7.936 0.01 1 324 185 185 GLU N N 120.884 0.02 1 325 186 186 ALA H H 8.295 0.01 1 326 186 186 ALA N N 122.845 0.02 1 327 187 187 GLU H H 7.896 0.01 1 328 187 187 GLU N N 122.054 0.02 1 329 188 188 ALA H H 7.413 0.01 1 330 188 188 ALA N N 118.728 0.02 1 331 189 189 GLY H H 7.744 0.01 1 332 189 189 GLY N N 105.259 0.02 1 333 190 190 ASN H H 8.094 0.01 1 334 190 190 ASN N N 117.216 0.02 1 335 191 191 THR H H 7.444 0.01 1 336 191 191 THR N N 113.706 0.02 1 337 192 192 LYS H H 7.776 0.01 1 338 192 192 LYS N N 122.555 0.02 1 339 193 193 TYR H H 8.227 0.01 1 340 193 193 TYR N N 123.758 0.02 1 341 194 194 ALA H H 8.18 0.01 1 342 194 194 ALA N N 130.051 0.02 1 343 195 195 LYS H H 8.262 0.01 1 344 195 195 LYS N N 122.644 0.02 1 345 196 196 VAL H H 9.027 0.01 1 346 196 196 VAL N N 125.236 0.02 1 347 197 197 ASP H H 8.677 0.01 1 348 197 197 ASP N N 124.577 0.02 1 349 198 198 GLY H H 8.345 0.01 1 350 198 198 GLY N N 112.051 0.02 1 351 199 199 THR H H 8.597 0.01 1 352 199 199 THR N N 111.885 0.02 1 353 200 200 LYS H H 6.508 0.01 1 354 200 200 LYS N N 121.631 0.02 1 355 202 202 VAL H H 8.383 0.01 1 356 202 202 VAL N N 123.467 0.02 1 357 203 203 ALA H H 8.77 0.01 1 358 203 203 ALA N N 119.561 0.02 1 359 204 204 GLU H H 7.333 0.01 1 360 204 204 GLU N N 117.822 0.02 1 361 205 205 VAL H H 7.787 0.01 1 362 205 205 VAL N N 121.099 0.02 1 363 206 206 ARG H H 7.879 0.01 1 364 206 206 ARG N N 118.588 0.02 1 365 207 207 ALA H H 7.162 0.01 1 366 207 207 ALA N N 120.417 0.02 1 367 208 208 ASP H H 8.194 0.01 1 368 208 208 ASP N N 121.315 0.02 1 369 209 209 LEU H H 8.461 0.01 1 370 209 209 LEU N N 120.58 0.02 1 371 210 210 GLU H H 8.394 0.01 1 372 210 210 GLU N N 118.962 0.02 1 373 211 211 LYS H H 7.595 0.01 1 374 211 211 LYS N N 118.856 0.02 1 375 212 212 ILE H H 7.524 0.01 1 376 212 212 ILE N N 119.293 0.02 1 377 213 213 LEU H H 8.05 0.01 1 378 213 213 LEU N N 117.117 0.02 1 379 214 214 GLY H H 7.556 0.01 1 380 214 214 GLY N N 112.519 0.02 1 stop_ save_