data_28005 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for phosphomimetic mutant of cytoplasmic domain of MapZ protein ; _BMRB_accession_number 28005 _BMRB_flat_file_name bmr28005.str _Entry_type original _Submission_date 2019-08-22 _Accession_date 2019-08-22 _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 Hosek Tomas . . 2 Bougault Catherine M. . 3 Simorre Jean-Pierre . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 150 "13C chemical shifts" 318 "15N chemical shifts" 150 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-04-03 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 28006 'MapZcyto-WT monomer' stop_ _Original_release_date 2019-08-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural features of the interaction of MapZ with FtsZ and membranes in Streptococcus pneumoniae ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32132631 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hosek Tomas . . 2 Bougault Catherine . . 3 Lavergne Jean-Pierre . . 4 Martinez Denis . . 5 Ayala Isabel . . 6 Fenel Daphna . . 7 Restelli Marine . . 8 Morlot Cecile . . 9 Habenstein Birgit . . 10 Grangeasse Christophe . . 11 Simorre Jean-Pierre . . stop_ _Journal_abbreviation 'Sci. Rep.' _Journal_name_full 'Scientific reports' _Journal_volume 10 _Journal_issue 1 _Journal_ISSN 2045-2322 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4051 _Page_last 4051 _Year 2020 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'MapZcyto-2TE monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'cytoplasmic domain' $MapZcyto-2TE stop_ _System_molecular_weight . _System_physical_state 'intrinsically disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MapZcyto-2TE _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common MapZcyto-2TE _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 168 _Mol_residue_sequence ; MSKKRRNRHKKEAQEPQFDF DEAKELTVGQAIRKNEEVEA GVLPEDSILDKYVKQHRDEI EADKFAERQYKKEEFVEEQS LDDLIQEMREAVEKSEASSE EVPSSEDILLPLPLDDEEQG LDPLLLDDENPTEMTEEVEE EQNLSRLDQEDSEKKSKKGL QGENLYFQ ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 LYS 4 LYS 5 ARG 6 ARG 7 ASN 8 ARG 9 HIS 10 LYS 11 LYS 12 GLU 13 ALA 14 GLN 15 GLU 16 PRO 17 GLN 18 PHE 19 ASP 20 PHE 21 ASP 22 GLU 23 ALA 24 LYS 25 GLU 26 LEU 27 THR 28 VAL 29 GLY 30 GLN 31 ALA 32 ILE 33 ARG 34 LYS 35 ASN 36 GLU 37 GLU 38 VAL 39 GLU 40 ALA 41 GLY 42 VAL 43 LEU 44 PRO 45 GLU 46 ASP 47 SER 48 ILE 49 LEU 50 ASP 51 LYS 52 TYR 53 VAL 54 LYS 55 GLN 56 HIS 57 ARG 58 ASP 59 GLU 60 ILE 61 GLU 62 ALA 63 ASP 64 LYS 65 PHE 66 ALA 67 GLU 68 ARG 69 GLN 70 TYR 71 LYS 72 LYS 73 GLU 74 GLU 75 PHE 76 VAL 77 GLU 78 GLU 79 GLN 80 SER 81 LEU 82 ASP 83 ASP 84 LEU 85 ILE 86 GLN 87 GLU 88 MET 89 ARG 90 GLU 91 ALA 92 VAL 93 GLU 94 LYS 95 SER 96 GLU 97 ALA 98 SER 99 SER 100 GLU 101 GLU 102 VAL 103 PRO 104 SER 105 SER 106 GLU 107 ASP 108 ILE 109 LEU 110 LEU 111 PRO 112 LEU 113 PRO 114 LEU 115 ASP 116 ASP 117 GLU 118 GLU 119 GLN 120 GLY 121 LEU 122 ASP 123 PRO 124 LEU 125 LEU 126 LEU 127 ASP 128 ASP 129 GLU 130 ASN 131 PRO 132 THR 133 GLU 134 MET 135 THR 136 GLU 137 GLU 138 VAL 139 GLU 140 GLU 141 GLU 142 GLN 143 ASN 144 LEU 145 SER 146 ARG 147 LEU 148 ASP 149 GLN 150 GLU 151 ASP 152 SER 153 GLU 154 LYS 155 LYS 156 SER 157 LYS 158 LYS 159 GLY 160 LEU 161 GLN 162 GLY 163 GLU 164 ASN 165 LEU 166 TYR 167 PHE 168 GLN 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 $MapZcyto-2TE 'Streptococcus pneumoniae' 1313 Bacteria . Streptococcus pneumoniae 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 $MapZcyto-2TE 'recombinant technology' . Escherichia coli . pEtPhos 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 $MapZcyto-2TE 0.2 mM '[U-99% 13C; U-99% 15N]' HEPES 30 mM 'natural abundance' 'potassium chloride' 200 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_CCPN _Saveframe_category software _Name CCPN _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' 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_HBHA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _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' 0.2 . 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 '2D 1H-15N HSQC' '3D HBHA(CO)NH' '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 'cytoplasmic domain' _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 3 3 LYS CA C 56.319 0.011 1 2 3 3 LYS CB C 32.811 0.019 1 3 4 4 LYS H H 8.500 0.004 1 4 4 4 LYS CA C 56.360 0.009 1 5 4 4 LYS CB C 33.001 0.030 1 6 4 4 LYS N N 122.925 0.025 1 7 5 5 ARG H H 8.514 0.004 1 8 5 5 ARG CA C 56.127 0.000 1 9 5 5 ARG CB C 30.866 0.000 1 10 5 5 ARG N N 123.287 0.023 1 11 9 9 HIS CA C 56.488 0.022 1 12 9 9 HIS CB C 31.087 0.049 1 13 10 10 LYS H H 8.244 0.003 1 14 10 10 LYS CA C 56.305 0.001 1 15 10 10 LYS CB C 33.064 0.028 1 16 10 10 LYS N N 123.061 0.011 1 17 11 11 LYS H H 8.625 0.003 1 18 11 11 LYS CA C 56.610 0.028 1 19 11 11 LYS CB C 32.817 0.019 1 20 11 11 LYS N N 123.482 0.006 1 21 12 12 GLU H H 8.583 0.002 1 22 12 12 GLU CA C 56.430 0.022 1 23 12 12 GLU CB C 30.171 0.014 1 24 12 12 GLU N N 122.346 0.036 1 25 13 13 ALA H H 8.439 0.001 1 26 13 13 ALA CA C 52.566 0.018 1 27 13 13 ALA CB C 19.176 0.012 1 28 13 13 ALA N N 124.962 0.015 1 29 14 14 GLN H H 8.421 0.002 1 30 14 14 GLN CA C 55.374 0.022 1 31 14 14 GLN CB C 29.622 0.026 1 32 14 14 GLN N N 119.342 0.028 1 33 15 15 GLU H H 8.516 0.005 1 34 15 15 GLU CA C 54.448 0.000 1 35 15 15 GLU CB C 29.421 0.000 1 36 15 15 GLU N N 123.793 0.016 1 37 16 16 PRO CA C 63.212 0.012 1 38 16 16 PRO CB C 32.047 0.025 1 39 17 17 GLN H H 8.558 0.001 1 40 17 17 GLN CA C 55.392 0.011 1 41 17 17 GLN CB C 29.610 0.021 1 42 17 17 GLN N N 120.583 0.009 1 43 18 18 PHE H H 8.315 0.002 1 44 18 18 PHE CA C 57.363 0.053 1 45 18 18 PHE CB C 39.950 0.007 1 46 18 18 PHE N N 121.407 0.009 1 47 19 19 ASP H H 8.343 0.001 1 48 19 19 ASP CA C 53.868 0.015 1 49 19 19 ASP CB C 41.100 0.023 1 50 19 19 ASP N N 122.128 0.013 1 51 20 20 PHE H H 8.212 0.001 1 52 20 20 PHE CA C 58.069 0.011 1 53 20 20 PHE CB C 39.597 0.027 1 54 20 20 PHE N N 121.195 0.015 1 55 21 21 ASP H H 8.397 0.002 1 56 21 21 ASP CA C 54.230 0.003 1 57 21 21 ASP CB C 41.149 0.017 1 58 21 21 ASP N N 122.389 0.023 1 59 22 22 GLU H H 8.388 0.001 1 60 22 22 GLU CA C 57.136 0.006 1 61 22 22 GLU CB C 30.096 0.012 1 62 22 22 GLU N N 122.532 0.006 1 63 23 23 ALA H H 8.355 0.001 1 64 23 23 ALA CA C 52.815 0.004 1 65 23 23 ALA CB C 18.754 0.028 1 66 23 23 ALA N N 124.102 0.011 1 67 24 24 LYS H H 8.102 0.001 1 68 24 24 LYS CA C 56.488 0.022 1 69 24 24 LYS CB C 32.938 0.031 1 70 24 24 LYS N N 120.300 0.003 1 71 25 25 GLU H H 8.389 0.001 1 72 25 25 GLU CA C 56.626 0.015 1 73 25 25 GLU CB C 30.042 0.013 1 74 25 25 GLU N N 121.391 0.009 1 75 26 26 LEU H H 8.356 0.001 1 76 26 26 LEU CA C 55.270 0.009 1 77 26 26 LEU CB C 42.253 0.025 1 78 26 26 LEU N N 123.140 0.008 1 79 27 27 THR H H 8.253 0.001 1 80 27 27 THR CA C 61.905 0.014 1 81 27 27 THR CB C 69.827 0.025 1 82 27 27 THR N N 115.461 0.012 1 83 28 28 VAL H H 8.292 0.001 1 84 28 28 VAL CA C 62.962 0.022 1 85 28 28 VAL CB C 32.549 0.026 1 86 28 28 VAL N N 122.954 0.007 1 87 29 29 GLY H H 8.626 0.000 1 88 29 29 GLY CA C 45.284 0.022 1 89 29 29 GLY N N 112.478 0.017 1 90 30 30 GLN H H 8.231 0.003 1 91 30 30 GLN CA C 55.809 0.008 1 92 30 30 GLN CB C 29.573 0.026 1 93 30 30 GLN N N 120.023 0.009 1 94 31 31 ALA H H 8.446 0.001 1 95 31 31 ALA CA C 52.612 0.015 1 96 31 31 ALA CB C 18.961 0.022 1 97 31 31 ALA N N 125.454 0.008 1 98 32 32 ILE H H 8.233 0.001 1 99 32 32 ILE CA C 61.268 0.020 1 100 32 32 ILE CB C 38.504 0.038 1 101 32 32 ILE N N 120.851 0.006 1 102 33 33 ARG H H 8.479 0.001 1 103 33 33 ARG CA C 56.016 0.008 1 104 33 33 ARG CB C 30.725 0.017 1 105 33 33 ARG N N 125.987 0.018 1 106 34 34 LYS H H 8.557 0.001 1 107 34 34 LYS CA C 56.410 0.019 1 108 34 34 LYS CB C 33.044 0.057 1 109 34 34 LYS N N 123.650 0.017 1 110 35 35 ASN H H 8.629 0.003 1 111 35 35 ASN CA C 53.607 0.002 1 112 35 35 ASN CB C 38.613 0.014 1 113 35 35 ASN N N 120.230 0.015 1 114 36 36 GLU H H 8.549 0.002 1 115 36 36 GLU CA C 56.684 0.019 1 116 36 36 GLU CB C 30.140 0.009 1 117 36 36 GLU N N 121.229 0.004 1 118 37 37 GLU H H 8.431 0.001 1 119 37 37 GLU CA C 56.609 0.007 1 120 37 37 GLU CB C 30.118 0.026 1 121 37 37 GLU N N 121.838 0.006 1 122 38 38 VAL H H 8.252 0.001 1 123 38 38 VAL CA C 62.393 0.018 1 124 38 38 VAL CB C 32.835 0.032 1 125 38 38 VAL N N 121.507 0.009 1 126 39 39 GLU H H 8.582 0.000 1 127 39 39 GLU CA C 56.466 0.021 1 128 39 39 GLU CB C 30.148 0.008 1 129 39 39 GLU N N 125.184 0.005 1 130 40 40 ALA H H 8.486 0.001 1 131 40 40 ALA CA C 52.747 0.008 1 132 40 40 ALA CB C 19.175 0.011 1 133 40 40 ALA N N 125.757 0.009 1 134 41 41 GLY H H 8.476 0.001 1 135 41 41 GLY CA C 45.135 0.002 1 136 41 41 GLY N N 108.507 0.011 1 137 42 42 VAL H H 8.011 0.000 1 138 42 42 VAL CA C 62.070 0.003 1 139 42 42 VAL CB C 32.724 0.020 1 140 42 42 VAL N N 119.855 0.011 1 141 43 43 LEU H H 8.637 0.001 1 142 43 43 LEU CA C 52.816 0.000 1 143 43 43 LEU CB C 41.372 0.000 1 144 43 43 LEU N N 128.524 0.017 1 145 44 44 PRO CA C 63.265 0.023 1 146 44 44 PRO CB C 32.036 0.011 1 147 45 45 GLU H H 8.771 0.001 1 148 45 45 GLU CA C 56.969 0.019 1 149 45 45 GLU CB C 29.915 0.018 1 150 45 45 GLU N N 120.662 0.005 1 151 46 46 ASP H H 8.396 0.001 1 152 46 46 ASP CA C 54.584 0.032 1 153 46 46 ASP CB C 41.057 0.008 1 154 46 46 ASP N N 121.158 0.011 1 155 47 47 SER H H 8.283 0.001 1 156 47 47 SER CA C 58.569 0.003 1 157 47 47 SER CB C 63.791 0.022 1 158 47 47 SER N N 116.167 0.009 1 159 48 48 ILE H H 8.218 0.001 1 160 48 48 ILE CA C 61.819 0.008 1 161 48 48 ILE CB C 38.235 0.016 1 162 48 48 ILE N N 122.546 0.005 1 163 49 49 LEU H H 8.219 0.001 1 164 49 49 LEU CA C 55.577 0.051 1 165 49 49 LEU CB C 42.081 0.013 1 166 49 49 LEU N N 124.695 0.009 1 167 50 50 ASP H H 8.252 0.001 1 168 50 50 ASP CA C 54.953 0.042 1 169 50 50 ASP CB C 41.022 0.011 1 170 50 50 ASP N N 120.873 0.006 1 171 51 51 LYS H H 8.146 0.001 1 172 51 51 LYS CA C 57.223 0.036 1 173 51 51 LYS CB C 32.651 0.057 1 174 51 51 LYS N N 120.770 0.006 1 175 52 52 TYR H H 8.213 0.001 1 176 52 52 TYR CA C 58.585 0.012 1 177 52 52 TYR CB C 38.360 0.024 1 178 52 52 TYR N N 120.655 0.014 1 179 53 53 VAL H H 7.984 0.002 1 180 53 53 VAL CA C 63.025 0.051 1 181 53 53 VAL CB C 32.637 0.019 1 182 53 53 VAL N N 122.829 0.015 1 183 54 54 LYS H H 8.314 0.002 1 184 54 54 LYS CA C 57.117 0.000 1 185 54 54 LYS CB C 32.891 0.000 1 186 54 54 LYS N N 124.505 0.026 1 187 56 56 HIS CA C 56.651 0.017 1 188 56 56 HIS CB C 30.601 0.007 1 189 57 57 ARG H H 8.299 0.001 1 190 57 57 ARG CA C 56.823 0.015 1 191 57 57 ARG CB C 30.696 0.027 1 192 57 57 ARG N N 122.706 0.006 1 193 58 58 ASP H H 8.718 0.004 1 194 58 58 ASP CA C 55.090 0.046 1 195 58 58 ASP CB C 40.780 0.016 1 196 58 58 ASP N N 121.385 0.014 1 197 59 59 GLU H H 8.359 0.002 1 198 59 59 GLU CA C 57.197 0.022 1 199 59 59 GLU CB C 30.053 0.037 1 200 59 59 GLU N N 121.335 0.005 1 201 60 60 ILE H H 8.159 0.002 1 202 60 60 ILE CA C 61.900 0.037 1 203 60 60 ILE CB C 38.368 0.038 1 204 60 60 ILE N N 121.504 0.012 1 205 61 61 GLU H H 8.481 0.001 1 206 61 61 GLU CA C 57.185 0.002 1 207 61 61 GLU CB C 29.849 0.017 1 208 61 61 GLU N N 124.037 0.003 1 209 62 62 ALA H H 8.324 0.001 1 210 62 62 ALA CA C 53.358 0.039 1 211 62 62 ALA CB C 18.905 0.029 1 212 62 62 ALA N N 124.386 0.012 1 213 63 63 ASP H H 8.321 0.003 1 214 63 63 ASP CA C 54.974 0.004 1 215 63 63 ASP CB C 40.771 0.057 1 216 63 63 ASP N N 119.373 0.007 1 217 64 64 LYS H H 8.148 0.001 1 218 64 64 LYS CA C 57.211 0.009 1 219 64 64 LYS CB C 32.371 0.029 1 220 64 64 LYS N N 121.523 0.007 1 221 65 65 PHE H H 8.251 0.002 1 222 65 65 PHE CA C 58.528 0.004 1 223 65 65 PHE CB C 39.016 0.024 1 224 65 65 PHE N N 120.000 0.008 1 225 66 66 ALA H H 8.050 0.001 1 226 66 66 ALA CA C 53.157 0.042 1 227 66 66 ALA CB C 18.942 0.009 1 228 66 66 ALA N N 123.929 0.012 1 229 67 67 GLU H H 8.293 0.003 1 230 67 67 GLU CA C 56.913 0.027 1 231 67 67 GLU CB C 29.929 0.045 1 232 67 67 GLU N N 119.340 0.005 1 233 68 68 ARG H H 8.214 0.000 1 234 68 68 ARG CA C 56.529 0.033 1 235 68 68 ARG CB C 30.460 0.048 1 236 68 68 ARG N N 121.335 0.007 1 237 69 69 GLN H H 8.305 0.001 1 238 69 69 GLN CA C 55.779 0.010 1 239 69 69 GLN CB C 29.257 0.050 1 240 69 69 GLN N N 120.695 0.011 1 241 70 70 TYR H H 8.243 0.001 1 242 70 70 TYR CA C 57.921 0.007 1 243 70 70 TYR CB C 38.774 0.023 1 244 70 70 TYR N N 121.418 0.005 1 245 71 71 LYS H H 8.225 0.001 1 246 71 71 LYS CA C 55.893 0.032 1 247 71 71 LYS CB C 33.189 0.013 1 248 71 71 LYS N N 123.885 0.017 1 249 72 72 LYS H H 8.423 0.001 1 250 72 72 LYS CA C 56.756 0.068 1 251 72 72 LYS CB C 32.841 0.016 1 252 72 72 LYS N N 124.049 0.018 1 253 73 73 GLU H H 8.632 0.003 1 254 73 73 GLU CA C 56.628 0.052 1 255 73 73 GLU CB C 30.097 0.019 1 256 73 73 GLU N N 122.633 0.008 1 257 74 74 GLU H H 8.405 0.001 1 258 74 74 GLU CA C 56.339 0.011 1 259 74 74 GLU CB C 30.401 0.029 1 260 74 74 GLU N N 122.063 0.004 1 261 75 75 PHE H H 8.399 0.002 1 262 75 75 PHE CA C 57.704 0.006 1 263 75 75 PHE CB C 39.629 0.004 1 264 75 75 PHE N N 121.865 0.005 1 265 76 76 VAL H H 8.111 0.000 1 266 76 76 VAL CA C 61.912 0.013 1 267 76 76 VAL CB C 33.090 0.016 1 268 76 76 VAL N N 124.165 0.010 1 269 77 77 GLU H H 8.535 0.001 1 270 77 77 GLU CA C 56.383 0.008 1 271 77 77 GLU CB C 30.291 0.011 1 272 77 77 GLU N N 125.544 0.005 1 273 78 78 GLU H H 8.638 0.001 1 274 78 78 GLU CA C 56.533 0.006 1 275 78 78 GLU CB C 30.371 0.003 1 276 78 78 GLU N N 123.283 0.008 1 277 79 79 GLN H H 8.590 0.006 1 278 79 79 GLN CA C 55.698 0.020 1 279 79 79 GLN CB C 29.854 0.028 1 280 79 79 GLN N N 122.386 0.066 1 281 80 80 SER H H 8.776 0.003 1 282 80 80 SER CA C 57.934 0.004 1 283 80 80 SER CB C 63.976 0.003 1 284 80 80 SER N N 118.858 0.017 1 285 81 81 LEU H H 8.608 0.001 1 286 81 81 LEU CA C 56.102 0.003 1 287 81 81 LEU CB C 41.815 0.019 1 288 81 81 LEU N N 124.750 0.016 1 289 82 82 ASP H H 8.285 0.001 1 290 82 82 ASP CA C 55.559 0.021 1 291 82 82 ASP CB C 40.925 0.042 1 292 82 82 ASP N N 119.638 0.032 1 293 83 83 ASP H H 8.195 0.001 1 294 83 83 ASP CA C 55.364 0.036 1 295 83 83 ASP CB C 40.681 0.053 1 296 83 83 ASP N N 120.592 0.008 1 297 84 84 LEU H H 8.081 0.001 1 298 84 84 LEU CA C 56.360 0.038 1 299 84 84 LEU CB C 41.887 0.014 1 300 84 84 LEU N N 122.005 0.009 1 301 85 85 ILE H H 8.175 0.001 1 302 85 85 ILE CA C 62.472 0.014 1 303 85 85 ILE CB C 37.993 0.031 1 304 85 85 ILE N N 121.477 0.017 1 305 86 86 GLN H H 8.331 0.002 1 306 86 86 GLN CA C 56.917 0.042 1 307 86 86 GLN CB C 28.727 0.028 1 308 86 86 GLN N N 123.103 0.022 1 309 87 87 GLU H H 8.426 0.003 1 310 87 87 GLU CA C 57.680 0.020 1 311 87 87 GLU CB C 29.958 0.075 1 312 87 87 GLU N N 121.532 0.021 1 313 88 88 MET H H 8.387 0.001 1 314 88 88 MET CA C 56.486 0.081 1 315 88 88 MET CB C 32.486 0.025 1 316 88 88 MET N N 120.878 0.013 1 317 89 89 ARG H H 8.321 0.002 1 318 89 89 ARG CA C 57.201 0.058 1 319 89 89 ARG CB C 30.644 0.082 1 320 89 89 ARG N N 122.180 0.012 1 321 90 90 GLU H H 8.448 0.001 1 322 90 90 GLU CA C 57.087 0.023 1 323 90 90 GLU CB C 29.966 0.024 1 324 90 90 GLU N N 121.135 0.015 1 325 91 91 ALA H H 8.236 0.003 1 326 91 91 ALA CA C 53.059 0.024 1 327 91 91 ALA CB C 18.805 0.015 1 328 91 91 ALA N N 124.437 0.025 1 329 92 92 VAL H H 8.105 0.001 1 330 92 92 VAL CA C 63.045 0.036 1 331 92 92 VAL CB C 32.618 0.040 1 332 92 92 VAL N N 119.766 0.010 1 333 93 93 GLU H H 8.491 0.002 1 334 93 93 GLU CA C 56.956 0.055 1 335 93 93 GLU CB C 30.096 0.076 1 336 93 93 GLU N N 124.189 0.028 1 337 94 94 LYS H H 8.437 0.002 1 338 94 94 LYS CA C 56.664 0.021 1 339 94 94 LYS CB C 32.925 0.016 1 340 94 94 LYS N N 122.601 0.023 1 341 95 95 SER H H 8.420 0.003 1 342 95 95 SER CA C 58.637 0.024 1 343 95 95 SER CB C 63.724 0.019 1 344 95 95 SER N N 117.569 0.020 1 345 96 96 GLU H H 8.547 0.002 1 346 96 96 GLU CA C 56.554 0.020 1 347 96 96 GLU CB C 30.185 0.038 1 348 96 96 GLU N N 123.048 0.017 1 349 97 97 ALA H H 8.355 0.003 1 350 97 97 ALA CA C 52.603 0.023 1 351 97 97 ALA CB C 19.128 0.005 1 352 97 97 ALA N N 124.972 0.017 1 353 98 98 SER H H 8.420 0.001 1 354 98 98 SER CA C 58.282 0.022 1 355 98 98 SER CB C 63.810 0.049 1 356 98 98 SER N N 115.595 0.013 1 357 99 99 SER H H 8.499 0.002 1 358 99 99 SER CA C 58.411 0.038 1 359 99 99 SER CB C 63.777 0.015 1 360 99 99 SER N N 118.348 0.010 1 361 100 100 GLU H H 8.463 0.001 1 362 100 100 GLU CA C 56.298 0.016 1 363 100 100 GLU CB C 30.367 0.005 1 364 100 100 GLU N N 122.615 0.010 1 365 101 101 GLU H H 8.478 0.002 1 366 101 101 GLU CA C 56.242 0.024 1 367 101 101 GLU CB C 30.229 0.045 1 368 101 101 GLU N N 122.604 0.019 1 369 102 102 VAL H H 8.469 0.002 1 370 102 102 VAL CA C 59.845 0.000 1 371 102 102 VAL CB C 32.525 0.000 1 372 102 102 VAL N N 124.253 0.012 1 373 103 103 PRO CA C 63.032 0.034 1 374 103 103 PRO CB C 32.230 0.010 1 375 104 104 SER H H 8.689 0.001 1 376 104 104 SER CA C 58.173 0.026 1 377 104 104 SER CB C 63.921 0.064 1 378 104 104 SER N N 117.149 0.011 1 379 105 105 SER H H 8.599 0.001 1 380 105 105 SER CA C 58.539 0.021 1 381 105 105 SER CB C 63.715 0.011 1 382 105 105 SER N N 118.519 0.010 1 383 106 106 GLU H H 8.521 0.001 1 384 106 106 GLU CA C 56.478 0.005 1 385 106 106 GLU CB C 30.213 0.019 1 386 106 106 GLU N N 122.380 0.013 1 387 107 107 ASP H H 8.366 0.002 1 388 107 107 ASP CA C 54.445 0.003 1 389 107 107 ASP CB C 40.955 0.023 1 390 107 107 ASP N N 121.695 0.013 1 391 108 108 ILE H H 8.109 0.001 1 392 108 108 ILE CA C 61.034 0.014 1 393 108 108 ILE CB C 38.622 0.017 1 394 108 108 ILE N N 121.333 0.008 1 395 109 109 LEU H H 8.407 0.000 1 396 109 109 LEU CA C 54.668 0.006 1 397 109 109 LEU CB C 42.101 0.007 1 398 109 109 LEU N N 127.047 0.011 1 399 110 110 LEU H H 8.312 0.001 1 400 110 110 LEU CA C 52.706 0.000 1 401 110 110 LEU CB C 41.639 0.000 1 402 110 110 LEU N N 125.672 0.022 1 403 111 111 PRO CA C 62.622 0.011 1 404 111 111 PRO CB C 31.971 0.030 1 405 112 112 LEU H H 8.415 0.000 1 406 112 112 LEU CA C 52.930 0.000 1 407 112 112 LEU CB C 41.349 0.000 1 408 112 112 LEU N N 124.132 0.005 1 409 113 113 PRO CA C 62.816 0.025 1 410 113 113 PRO CB C 32.030 0.022 1 411 114 114 LEU H H 8.488 0.000 1 412 114 114 LEU CA C 54.880 0.035 1 413 114 114 LEU CB C 42.324 0.053 1 414 114 114 LEU N N 122.932 0.011 1 415 115 115 ASP H H 8.464 0.001 1 416 115 115 ASP CA C 54.287 0.025 1 417 115 115 ASP CB C 41.190 0.036 1 418 115 115 ASP N N 121.514 0.013 1 419 116 116 ASP H H 8.389 0.002 1 420 116 116 ASP CA C 54.447 0.013 1 421 116 116 ASP CB C 41.140 0.019 1 422 116 116 ASP N N 120.865 0.011 1 423 117 117 GLU H H 8.459 0.002 1 424 117 117 GLU CA C 56.677 0.016 1 425 117 117 GLU CB C 30.201 0.024 1 426 117 117 GLU N N 121.175 0.017 1 427 118 118 GLU H H 8.521 0.001 1 428 118 118 GLU CA C 56.738 0.031 1 429 118 118 GLU CB C 29.850 0.023 1 430 118 118 GLU N N 122.014 0.018 1 431 119 119 GLN H H 8.521 0.001 1 432 119 119 GLN CA C 55.918 0.012 1 433 119 119 GLN CB C 29.495 0.011 1 434 119 119 GLN N N 121.762 0.002 1 435 120 120 GLY H H 8.558 0.001 1 436 120 120 GLY CA C 45.184 0.017 1 437 120 120 GLY N N 110.143 0.019 1 438 121 121 LEU H H 8.197 0.003 1 439 121 121 LEU CA C 54.663 0.011 1 440 121 121 LEU CB C 42.491 0.015 1 441 121 121 LEU N N 121.584 0.009 1 442 122 122 ASP H H 8.499 0.001 1 443 122 122 ASP CA C 52.174 0.000 1 444 122 122 ASP CB C 40.917 0.000 1 445 122 122 ASP N N 123.629 0.017 1 446 123 123 PRO CA C 63.419 0.011 1 447 123 123 PRO CB C 32.173 0.008 1 448 124 124 LEU H H 8.447 0.001 1 449 124 124 LEU CA C 55.329 0.024 1 450 124 124 LEU CB C 41.595 0.021 1 451 124 124 LEU N N 120.896 0.022 1 452 125 125 LEU H H 8.040 0.002 1 453 125 125 LEU CA C 54.791 0.004 1 454 125 125 LEU CB C 41.956 0.003 1 455 125 125 LEU N N 122.372 0.021 1 456 126 126 LEU H H 8.153 0.001 1 457 126 126 LEU CA C 54.770 0.030 1 458 126 126 LEU CB C 42.319 0.045 1 459 126 126 LEU N N 123.196 0.015 1 460 127 127 ASP H H 8.387 0.001 1 461 127 127 ASP CA C 54.278 0.021 1 462 127 127 ASP CB C 41.221 0.035 1 463 127 127 ASP N N 121.519 0.010 1 464 128 128 ASP H H 8.370 0.001 1 465 128 128 ASP CA C 54.253 0.021 1 466 128 128 ASP CB C 41.164 0.017 1 467 128 128 ASP N N 121.157 0.013 1 468 129 129 GLU H H 8.406 0.003 1 469 129 129 GLU CA C 56.477 0.018 1 470 129 129 GLU CB C 30.314 0.039 1 471 129 129 GLU N N 120.833 0.009 1 472 130 130 ASN H H 8.568 0.001 1 473 130 130 ASN CA C 51.355 0.000 1 474 130 130 ASN CB C 38.852 0.000 1 475 130 130 ASN N N 120.461 0.018 1 476 131 131 PRO CA C 63.264 0.022 1 477 131 131 PRO CB C 32.174 0.039 1 478 132 132 THR H H 8.403 0.001 1 479 132 132 THR CA C 62.161 0.003 1 480 132 132 THR CB C 69.739 0.013 1 481 132 132 THR N N 115.208 0.020 1 482 133 133 GLU H H 8.481 0.001 1 483 133 133 GLU CA C 56.381 0.028 1 484 133 133 GLU CB C 30.276 0.039 1 485 133 133 GLU N N 123.773 0.014 1 486 134 134 MET H H 8.580 0.002 1 487 134 134 MET CA C 55.269 0.010 1 488 134 134 MET CB C 32.831 0.028 1 489 134 134 MET N N 122.566 0.041 1 490 135 135 THR H H 8.351 0.001 1 491 135 135 THR CA C 61.791 0.008 1 492 135 135 THR CB C 69.887 0.011 1 493 135 135 THR N N 116.672 0.015 1 494 136 136 GLU H H 8.590 0.001 1 495 136 136 GLU CA C 56.470 0.058 1 496 136 136 GLU CB C 30.461 0.023 1 497 136 136 GLU N N 123.711 0.015 1 498 137 137 GLU H H 8.612 0.001 1 499 137 137 GLU CA C 56.427 0.042 1 500 137 137 GLU CB C 30.192 0.035 1 501 137 137 GLU N N 123.043 0.013 1 502 138 138 VAL H H 8.396 0.002 1 503 138 138 VAL CA C 62.153 0.003 1 504 138 138 VAL CB C 32.936 0.017 1 505 138 138 VAL N N 122.459 0.004 1 506 139 139 GLU H H 8.646 0.000 1 507 139 139 GLU CA C 56.620 0.006 1 508 139 139 GLU CB C 30.334 0.013 1 509 139 139 GLU N N 125.750 0.011 1 510 140 140 GLU H H 8.635 0.002 1 511 140 140 GLU CA C 56.750 0.026 1 512 140 140 GLU CB C 30.187 0.066 1 513 140 140 GLU N N 123.035 0.009 1 514 141 141 GLU H H 8.602 0.001 1 515 141 141 GLU CA C 56.981 0.024 1 516 141 141 GLU CB C 30.071 0.036 1 517 141 141 GLU N N 122.736 0.012 1 518 142 142 GLN H H 8.594 0.000 1 519 142 142 GLN CA C 56.082 0.003 1 520 142 142 GLN CB C 29.344 0.022 1 521 142 142 GLN N N 121.527 0.005 1 522 143 143 ASN H H 8.635 0.001 1 523 143 143 ASN CA C 53.370 0.006 1 524 143 143 ASN CB C 38.541 0.015 1 525 143 143 ASN N N 119.945 0.009 1 526 144 144 LEU H H 8.397 0.001 1 527 144 144 LEU CA C 55.625 0.035 1 528 144 144 LEU CB C 41.974 0.020 1 529 144 144 LEU N N 122.839 0.007 1 530 145 145 SER H H 8.433 0.001 1 531 145 145 SER CA C 58.784 0.054 1 532 145 145 SER CB C 63.469 0.023 1 533 145 145 SER N N 116.447 0.004 1 534 146 146 ARG H H 8.308 0.001 1 535 146 146 ARG CA C 56.501 0.022 1 536 146 146 ARG CB C 30.455 0.018 1 537 146 146 ARG N N 122.869 0.010 1 538 147 147 LEU H H 8.272 0.001 1 539 147 147 LEU CA C 55.680 0.029 1 540 147 147 LEU CB C 42.019 0.046 1 541 147 147 LEU N N 122.425 0.013 1 542 148 148 ASP H H 8.370 0.001 1 543 148 148 ASP CA C 54.733 0.003 1 544 148 148 ASP CB C 40.804 0.020 1 545 148 148 ASP N N 120.499 0.009 1 546 149 149 GLN H H 8.286 0.001 1 547 149 149 GLN CA C 56.212 0.029 1 548 149 149 GLN CB C 29.413 0.043 1 549 149 149 GLN N N 120.280 0.010 1 550 150 150 GLU H H 8.506 0.001 1 551 150 150 GLU CA C 57.147 0.032 1 552 150 150 GLU CB C 29.956 0.033 1 553 150 150 GLU N N 121.747 0.000 1 554 151 151 ASP H H 8.491 0.001 1 555 151 151 ASP CA C 54.835 0.028 1 556 151 151 ASP CB C 41.082 0.018 1 557 151 151 ASP N N 121.598 0.001 1 558 152 152 SER H H 8.413 0.002 1 559 152 152 SER CA C 59.882 0.033 1 560 152 152 SER CB C 63.387 0.011 1 561 152 152 SER N N 116.958 0.016 1 562 153 153 GLU H H 8.444 0.002 1 563 153 153 GLU CA C 57.323 0.036 1 564 153 153 GLU CB C 29.687 0.014 1 565 153 153 GLU N N 122.325 0.012 1 566 154 154 LYS H H 8.134 0.002 1 567 154 154 LYS CA C 57.144 0.040 1 568 154 154 LYS CB C 32.539 0.008 1 569 154 154 LYS N N 121.122 0.016 1 570 155 155 LYS H H 8.229 0.002 1 571 155 155 LYS CA C 56.841 0.015 1 572 155 155 LYS CB C 32.851 0.006 1 573 155 155 LYS N N 121.147 0.020 1 574 156 156 SER H H 8.303 0.002 1 575 156 156 SER CA C 58.628 0.024 1 576 156 156 SER CB C 63.646 0.045 1 577 156 156 SER N N 116.389 0.012 1 578 157 157 LYS H H 8.378 0.003 1 579 157 157 LYS CA C 56.441 0.001 1 580 157 157 LYS CB C 32.671 0.002 1 581 157 157 LYS N N 123.323 0.010 1 582 158 158 LYS H H 8.311 0.001 1 583 158 158 LYS CA C 56.774 0.034 1 584 158 158 LYS CB C 32.927 0.024 1 585 158 158 LYS N N 122.253 0.001 1 586 159 159 GLY H H 8.506 0.002 1 587 159 159 GLY CA C 45.179 0.005 1 588 159 159 GLY N N 110.058 0.015 1 589 160 160 LEU H H 8.187 0.001 1 590 160 160 LEU CA C 55.358 0.026 1 591 160 160 LEU CB C 42.295 0.022 1 592 160 160 LEU N N 121.615 0.011 1 593 161 161 GLN H H 8.510 0.001 1 594 161 161 GLN CA C 55.820 0.000 1 595 161 161 GLN CB C 29.147 0.000 1 596 161 161 GLN N N 121.012 0.015 1 597 163 163 GLU CA C 56.872 0.011 1 598 163 163 GLU CB C 30.287 0.038 1 599 164 164 ASN H H 8.518 0.001 1 600 164 164 ASN CA C 53.184 0.024 1 601 164 164 ASN CB C 38.617 0.010 1 602 164 164 ASN N N 119.249 0.013 1 603 165 165 LEU H H 8.156 0.000 1 604 165 165 LEU CA C 55.230 0.004 1 605 165 165 LEU CB C 42.217 0.026 1 606 165 165 LEU N N 122.151 0.015 1 607 166 166 TYR H H 8.075 0.001 1 608 166 166 TYR CA C 57.618 0.023 1 609 166 166 TYR CB C 38.704 0.020 1 610 166 166 TYR N N 119.734 0.013 1 611 167 167 PHE H H 8.093 0.002 1 612 167 167 PHE CA C 57.536 0.020 1 613 167 167 PHE CB C 39.573 0.017 1 614 167 167 PHE N N 121.625 0.027 1 615 168 168 GLN H H 7.847 0.001 1 616 168 168 GLN CA C 57.292 0.000 1 617 168 168 GLN CB C 30.440 0.000 1 618 168 168 GLN N N 126.248 0.009 1 stop_ save_