data_28136 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Resonance Assignments for the Rabies Phosphoprotein RavP ; _BMRB_accession_number 28136 _BMRB_flat_file_name bmr28136.str _Entry_type original _Submission_date 2020-07-03 _Accession_date 2020-07-03 _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 Jespersen Nathan . . 2 Leyrat Cedric . . 3 Gerard Francine C. . 4 Bourhis Jean-Marie . . 5 Blondel Danielle . . 6 Jamin Marc . . 7 Barbar Elisar . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 198 "13C chemical shifts" 102 "15N chemical shifts" 198 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-07-29 original BMRB . stop_ _Original_release_date 2020-07-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The LC8-RavP Ensemble Structure Evinces A Role for LC8 in Regulating Lyssavirus Polymerase Functionality ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31634467 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jespersen Nathan . . 2 Leyrat Cedric . . 3 Gerard Francine C. . 4 Bourhis Jean-Marie . . 5 Blondel Danielle . . 6 Jamin Marc . . 7 Barbar Elisar . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 431 _Journal_issue 24 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4959 _Page_last 4977 _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'RavP-FL Dimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'RavP, chain A' $Rabies_Phosphoprotein_(RavP) 'RavP, chain B' $Rabies_Phosphoprotein_(RavP) stop_ _System_molecular_weight 68000 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Rabies_Phosphoprotein_(RavP) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Rabies_Phosphoprotein_(RavP) _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 301 _Mol_residue_sequence ; GAHMMSKIFVNPSAIRAGLA DLEMAEETVDLINRNIEDNQ AHLQGEPIEVDNLPEDMGRL HLDGGKSSNPGEMAKVGEGK YREDFQMDEGEDPSLLFQSY LDNVGVQIVRQIRSGERFLK IWSQTVEEIISYVAVNFPNP PGKSSEDKSTQTTGRELKKE TTPTPSQRESQSSKARMAAQ TASGPPALEWSATNEEDDLS VEAEIAHQIAESFSKKYKFP SRSSGILLYNFEQLKMNLDD IVKEAKNVPGVTRLARDGSK LPLRCVLGWVALANSKKFQL LVESNKLSKIMQDDLNRYTS C ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 GLY 2 -2 ALA 3 -1 HIS 4 0 MET 5 1 MET 6 2 SER 7 3 LYS 8 4 ILE 9 5 PHE 10 6 VAL 11 7 ASN 12 8 PRO 13 9 SER 14 10 ALA 15 11 ILE 16 12 ARG 17 13 ALA 18 14 GLY 19 15 LEU 20 16 ALA 21 17 ASP 22 18 LEU 23 19 GLU 24 20 MET 25 21 ALA 26 22 GLU 27 23 GLU 28 24 THR 29 25 VAL 30 26 ASP 31 27 LEU 32 28 ILE 33 29 ASN 34 30 ARG 35 31 ASN 36 32 ILE 37 33 GLU 38 34 ASP 39 35 ASN 40 36 GLN 41 37 ALA 42 38 HIS 43 39 LEU 44 40 GLN 45 41 GLY 46 42 GLU 47 43 PRO 48 44 ILE 49 45 GLU 50 46 VAL 51 47 ASP 52 48 ASN 53 49 LEU 54 50 PRO 55 51 GLU 56 52 ASP 57 53 MET 58 54 GLY 59 55 ARG 60 56 LEU 61 57 HIS 62 58 LEU 63 59 ASP 64 60 GLY 65 61 GLY 66 62 LYS 67 63 SER 68 64 SER 69 65 ASN 70 66 PRO 71 67 GLY 72 68 GLU 73 69 MET 74 70 ALA 75 71 LYS 76 72 VAL 77 73 GLY 78 74 GLU 79 75 GLY 80 76 LYS 81 77 TYR 82 78 ARG 83 79 GLU 84 80 ASP 85 81 PHE 86 82 GLN 87 83 MET 88 84 ASP 89 85 GLU 90 86 GLY 91 87 GLU 92 88 ASP 93 89 PRO 94 90 SER 95 91 LEU 96 92 LEU 97 93 PHE 98 94 GLN 99 95 SER 100 96 TYR 101 97 LEU 102 98 ASP 103 99 ASN 104 100 VAL 105 101 GLY 106 102 VAL 107 103 GLN 108 104 ILE 109 105 VAL 110 106 ARG 111 107 GLN 112 108 ILE 113 109 ARG 114 110 SER 115 111 GLY 116 112 GLU 117 113 ARG 118 114 PHE 119 115 LEU 120 116 LYS 121 117 ILE 122 118 TRP 123 119 SER 124 120 GLN 125 121 THR 126 122 VAL 127 123 GLU 128 124 GLU 129 125 ILE 130 126 ILE 131 127 SER 132 128 TYR 133 129 VAL 134 130 ALA 135 131 VAL 136 132 ASN 137 133 PHE 138 134 PRO 139 135 ASN 140 136 PRO 141 137 PRO 142 138 GLY 143 139 LYS 144 140 SER 145 141 SER 146 142 GLU 147 143 ASP 148 144 LYS 149 145 SER 150 146 THR 151 147 GLN 152 148 THR 153 149 THR 154 150 GLY 155 151 ARG 156 152 GLU 157 153 LEU 158 154 LYS 159 155 LYS 160 156 GLU 161 157 THR 162 158 THR 163 159 PRO 164 160 THR 165 161 PRO 166 162 SER 167 163 GLN 168 164 ARG 169 165 GLU 170 166 SER 171 167 GLN 172 168 SER 173 169 SER 174 170 LYS 175 171 ALA 176 172 ARG 177 173 MET 178 174 ALA 179 175 ALA 180 176 GLN 181 177 THR 182 178 ALA 183 179 SER 184 180 GLY 185 181 PRO 186 182 PRO 187 183 ALA 188 184 LEU 189 185 GLU 190 186 TRP 191 187 SER 192 188 ALA 193 189 THR 194 190 ASN 195 191 GLU 196 192 GLU 197 193 ASP 198 194 ASP 199 195 LEU 200 196 SER 201 197 VAL 202 198 GLU 203 199 ALA 204 200 GLU 205 201 ILE 206 202 ALA 207 203 HIS 208 204 GLN 209 205 ILE 210 206 ALA 211 207 GLU 212 208 SER 213 209 PHE 214 210 SER 215 211 LYS 216 212 LYS 217 213 TYR 218 214 LYS 219 215 PHE 220 216 PRO 221 217 SER 222 218 ARG 223 219 SER 224 220 SER 225 221 GLY 226 222 ILE 227 223 LEU 228 224 LEU 229 225 TYR 230 226 ASN 231 227 PHE 232 228 GLU 233 229 GLN 234 230 LEU 235 231 LYS 236 232 MET 237 233 ASN 238 234 LEU 239 235 ASP 240 236 ASP 241 237 ILE 242 238 VAL 243 239 LYS 244 240 GLU 245 241 ALA 246 242 LYS 247 243 ASN 248 244 VAL 249 245 PRO 250 246 GLY 251 247 VAL 252 248 THR 253 249 ARG 254 250 LEU 255 251 ALA 256 252 ARG 257 253 ASP 258 254 GLY 259 255 SER 260 256 LYS 261 257 LEU 262 258 PRO 263 259 LEU 264 260 ARG 265 261 CYS 266 262 VAL 267 263 LEU 268 264 GLY 269 265 TRP 270 266 VAL 271 267 ALA 272 268 LEU 273 269 ALA 274 270 ASN 275 271 SER 276 272 LYS 277 273 LYS 278 274 PHE 279 275 GLN 280 276 LEU 281 277 LEU 282 278 VAL 283 279 GLU 284 280 SER 285 281 ASN 286 282 LYS 287 283 LEU 288 284 SER 289 285 LYS 290 286 ILE 291 287 MET 292 288 GLN 293 289 ASP 294 290 ASP 295 291 LEU 296 292 ASN 297 293 ARG 298 294 TYR 299 295 THR 300 296 SER 301 297 CYS 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 _Strain _Gene_mnemonic $Rabies_Phosphoprotein_(RavP) 'Rabies lyssavirus' 11292 Viruses . Rabies Virus 'Pasteur vaccins' P 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 $Rabies_Phosphoprotein_(RavP) 'recombinant technology' . Escherichia coli 'Rosetta BL21 DE3' pET24d+ 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 $Rabies_Phosphoprotein_(RavP) 150 uM '[U-99% 13C; U-99% 15N]' DSS 100 uM [U-2H] 'sodium azide' 1 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' MES 25 mM 'natural abundance' EDTA 5 mM 'natural abundance' beta-mercaptoethanol 5 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 stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _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_HNCO_2 _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' 100 . mM pH 6.5 . 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 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 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 'RavP, chain A' _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 9 13 SER H H 8.153 0.03 1 2 9 13 SER C C 171.864 0.2 1 3 9 13 SER N N 114.455 0.2 1 4 10 14 ALA H H 7.969 0.03 1 5 10 14 ALA C C 175.141 0.2 1 6 10 14 ALA N N 125.283 0.2 1 7 11 15 ILE H H 7.769 0.03 1 8 11 15 ILE C C 173.836 0.2 1 9 11 15 ILE N N 119.227 0.2 1 10 12 16 ARG H H 8.145 0.03 1 11 12 16 ARG N N 124.096 0.2 1 12 13 17 ALA C C 175.404 0.2 1 13 14 18 GLY H H 8.273 0.03 1 14 14 18 GLY C C 171.612 0.2 1 15 14 18 GLY N N 107.933 0.2 1 16 15 19 LEU H H 7.919 0.03 1 17 15 19 LEU C C 174.622 0.2 1 18 15 19 LEU N N 121.226 0.2 1 19 16 20 ALA H H 8.166 0.03 1 20 16 20 ALA C C 174.794 0.2 1 21 16 20 ALA N N 123.480 0.2 1 22 17 21 ASP H H 8.066 0.03 1 23 17 21 ASP N N 118.686 0.2 1 24 19 23 GLU C C 174.211 0.2 1 25 20 24 MET H H 8.128 0.03 1 26 20 24 MET C C 173.093 0.2 1 27 20 24 MET N N 120.398 0.2 1 28 21 25 ALA H H 8.171 0.03 1 29 21 25 ALA C C 174.950 0.2 1 30 21 25 ALA N N 125.232 0.2 1 31 22 26 GLU H H 8.330 0.03 1 32 22 26 GLU C C 174.058 0.2 1 33 22 26 GLU N N 120.291 0.2 1 34 23 27 GLU H H 8.192 0.03 1 35 23 27 GLU C C 173.932 0.2 1 36 23 27 GLU N N 120.707 0.2 1 37 24 28 THR H H 8.102 0.03 1 38 24 28 THR C C 171.892 0.2 1 39 24 28 THR N N 115.755 0.2 1 40 25 29 VAL H H 8.045 0.03 1 41 25 29 VAL C C 173.523 0.2 1 42 25 29 VAL N N 122.219 0.2 1 43 26 30 ASP H H 8.267 0.03 1 44 26 30 ASP C C 173.267 0.2 1 45 26 30 ASP N N 123.272 0.2 1 46 27 31 LEU H H 8.044 0.03 1 47 27 31 LEU C C 174.907 0.2 1 48 27 31 LEU N N 122.046 0.2 1 49 28 32 ILE H H 7.944 0.03 1 50 28 32 ILE C C 173.499 0.2 1 51 28 32 ILE N N 120.009 0.2 1 52 29 33 ASN H H 8.259 0.03 1 53 29 33 ASN C C 172.521 0.2 1 54 29 33 ASN N N 121.209 0.2 1 55 30 34 ARG H H 8.117 0.03 1 56 30 34 ARG N N 121.317 0.2 1 57 31 35 ASN H H 8.357 0.03 1 58 31 35 ASN C C 172.587 0.2 1 59 31 35 ASN N N 119.631 0.2 1 60 32 36 ILE H H 7.966 0.03 1 61 32 36 ILE C C 173.644 0.2 1 62 32 36 ILE N N 120.823 0.2 1 63 33 37 GLU H H 8.349 0.03 1 64 33 37 GLU C C 173.649 0.2 1 65 33 37 GLU N N 123.739 0.2 1 66 34 38 ASP H H 8.202 0.03 1 67 34 38 ASP C C 173.518 0.2 1 68 34 38 ASP N N 121.191 0.2 1 69 35 39 ASN H H 8.271 0.03 1 70 35 39 ASN C C 172.821 0.2 1 71 35 39 ASN N N 119.298 0.2 1 72 36 40 GLN H H 8.271 0.03 1 73 36 40 GLN C C 173.469 0.2 1 74 36 40 GLN N N 119.742 0.2 1 75 37 41 ALA H H 8.081 0.03 1 76 37 41 ALA N N 123.761 0.2 1 77 38 42 HIS C C 172.553 0.2 1 78 39 43 LEU H H 8.028 0.03 1 79 39 43 LEU C C 174.321 0.2 1 80 39 43 LEU N N 123.013 0.2 1 81 40 44 GLN H H 8.290 0.03 1 82 40 44 GLN C C 173.491 0.2 1 83 40 44 GLN N N 120.681 0.2 1 84 41 45 GLY H H 8.244 0.03 1 85 41 45 GLY C C 170.870 0.2 1 86 41 45 GLY N N 109.899 0.2 1 87 42 46 GLU H H 8.120 0.03 1 88 42 46 GLU N N 121.636 0.2 1 89 44 48 ILE H H 8.121 0.03 1 90 44 48 ILE C C 173.368 0.2 1 91 44 48 ILE N N 120.846 0.2 1 92 45 49 GLU H H 8.375 0.03 1 93 45 49 GLU N N 125.221 0.2 1 94 46 50 VAL H H 8.136 0.03 1 95 46 50 VAL C C 172.939 0.2 1 96 46 50 VAL N N 120.738 0.2 1 97 47 51 ASP H H 8.294 0.03 1 98 47 51 ASP C C 172.933 0.2 1 99 47 51 ASP N N 123.051 0.2 1 100 48 52 ASN H H 8.202 0.03 1 101 48 52 ASN C C 171.930 0.2 1 102 48 52 ASN N N 118.564 0.2 1 103 49 53 LEU H H 8.172 0.03 1 104 49 53 LEU N N 123.487 0.2 1 105 50 54 PRO C C 174.509 0.2 1 106 51 55 GLU H H 8.520 0.03 1 107 51 55 GLU C C 173.711 0.2 1 108 51 55 GLU N N 120.641 0.2 1 109 52 56 ASP H H 8.233 0.03 1 110 52 56 ASP C C 173.917 0.2 1 111 52 56 ASP N N 120.352 0.2 1 112 53 57 MET H H 8.238 0.03 1 113 53 57 MET C C 174.423 0.2 1 114 53 57 MET N N 120.773 0.2 1 115 54 58 GLY H H 8.421 0.03 1 116 54 58 GLY C C 171.741 0.2 1 117 54 58 GLY N N 108.917 0.2 1 118 55 59 ARG H H 7.886 0.03 1 119 55 59 ARG C C 173.658 0.2 1 120 55 59 ARG N N 119.697 0.2 1 121 56 60 LEU H H 7.957 0.03 1 122 56 60 LEU N N 121.558 0.2 1 123 58 62 LEU H H 8.127 0.03 1 124 58 62 LEU C C 174.321 0.2 1 125 58 62 LEU N N 123.435 0.2 1 126 59 63 ASP H H 8.305 0.03 1 127 59 63 ASP C C 174.110 0.2 1 128 59 63 ASP N N 120.759 0.2 1 129 60 64 GLY H H 8.287 0.03 1 130 60 64 GLY C C 172.188 0.2 1 131 60 64 GLY N N 109.476 0.2 1 132 61 65 GLY H H 8.252 0.03 1 133 61 65 GLY C C 171.256 0.2 1 134 61 65 GLY N N 108.572 0.2 1 135 62 66 LYS H H 7.987 0.03 1 136 62 66 LYS N N 120.279 0.2 1 137 64 68 SER H H 8.315 0.03 1 138 64 68 SER N N 118.673 0.2 1 139 66 70 PRO C C 174.963 0.2 1 140 67 71 GLY H H 8.374 0.03 1 141 67 71 GLY C C 171.697 0.2 1 142 67 71 GLY N N 108.447 0.2 1 143 68 72 GLU H H 7.939 0.03 1 144 68 72 GLU N N 120.282 0.2 1 145 69 73 MET H H 8.214 0.03 1 146 69 73 MET C C 173.358 0.2 1 147 69 73 MET N N 120.936 0.2 1 148 70 74 ALA H H 8.118 0.03 1 149 70 74 ALA C C 174.847 0.2 1 150 70 74 ALA N N 124.550 0.2 1 151 71 75 LYS H H 8.129 0.03 1 152 71 75 LYS C C 173.946 0.2 1 153 71 75 LYS N N 120.422 0.2 1 154 72 76 VAL H H 8.028 0.03 1 155 72 76 VAL C C 173.956 0.2 1 156 72 76 VAL N N 120.938 0.2 1 157 73 77 GLY H H 8.384 0.03 1 158 73 77 GLY C C 171.334 0.2 1 159 73 77 GLY N N 112.297 0.2 1 160 74 78 GLU H H 8.182 0.03 1 161 74 78 GLU N N 120.399 0.2 1 162 75 79 GLY H H 8.423 0.03 1 163 75 79 GLY C C 171.354 0.2 1 164 75 79 GLY N N 109.947 0.2 1 165 76 80 LYS H H 7.974 0.03 1 166 76 80 LYS N N 120.612 0.2 1 167 77 81 TYR H H 8.124 0.03 1 168 77 81 TYR C C 172.814 0.2 1 169 77 81 TYR N N 121.031 0.2 1 170 78 82 ARG H H 7.997 0.03 1 171 78 82 ARG C C 173.147 0.2 1 172 78 82 ARG N N 122.658 0.2 1 173 79 83 GLU H H 8.377 0.03 1 174 79 83 GLU C C 173.304 0.2 1 175 79 83 GLU N N 121.863 0.2 1 176 80 84 ASP H H 8.240 0.03 1 177 80 84 ASP C C 173.072 0.2 1 178 80 84 ASP N N 119.908 0.2 1 179 81 85 PHE H H 7.941 0.03 1 180 81 85 PHE C C 172.495 0.2 1 181 81 85 PHE N N 119.671 0.2 1 182 82 86 GLN H H 8.099 0.03 1 183 82 86 GLN C C 172.617 0.2 1 184 82 86 GLN N N 122.221 0.2 1 185 83 87 MET H H 8.268 0.03 1 186 83 87 MET N N 121.963 0.2 1 187 84 88 ASP H H 8.341 0.03 1 188 84 88 ASP C C 173.485 0.2 1 189 84 88 ASP N N 122.129 0.2 1 190 85 89 GLU H H 8.446 0.03 1 191 85 89 GLU C C 174.201 0.2 1 192 85 89 GLU N N 121.715 0.2 1 193 86 90 GLY H H 8.378 0.03 1 194 86 90 GLY N N 109.236 0.2 1 195 138 142 GLY H H 8.347 0.03 1 196 138 142 GLY C C 171.279 0.2 1 197 138 142 GLY N N 108.843 0.2 1 198 139 143 LYS H H 8.166 0.03 1 199 139 143 LYS N N 120.968 0.2 1 200 140 144 SER H H 8.499 0.03 1 201 140 144 SER N N 117.625 0.2 1 202 141 145 SER H H 8.455 0.03 1 203 141 145 SER C C 171.891 0.2 1 204 141 145 SER N N 117.668 0.2 1 205 142 146 GLU H H 8.324 0.03 1 206 142 146 GLU C C 173.388 0.2 1 207 142 146 GLU N N 122.261 0.2 1 208 143 147 ASP H H 8.240 0.03 1 209 143 147 ASP C C 173.719 0.2 1 210 143 147 ASP N N 121.494 0.2 1 211 144 148 LYS H H 8.288 0.03 1 212 144 148 LYS C C 174.416 0.2 1 213 144 148 LYS N N 122.406 0.2 1 214 145 149 SER H H 8.357 0.03 1 215 145 149 SER N N 116.648 0.2 1 216 146 150 THR H H 8.033 0.03 1 217 146 150 THR N N 115.230 0.2 1 218 147 151 GLN H H 8.206 0.03 1 219 147 151 GLN N N 122.655 0.2 1 220 148 152 THR H H 8.181 0.03 1 221 148 152 THR N N 115.235 0.2 1 222 149 153 THR H H 8.197 0.03 1 223 149 153 THR N N 116.041 0.2 1 224 150 154 GLY H H 8.459 0.03 1 225 150 154 GLY C C 171.492 0.2 1 226 150 154 GLY N N 111.415 0.2 1 227 151 155 ARG H H 8.088 0.03 1 228 151 155 ARG C C 173.505 0.2 1 229 151 155 ARG N N 120.379 0.2 1 230 152 156 GLU H H 8.499 0.03 1 231 152 156 GLU C C 173.531 0.2 1 232 152 156 GLU N N 121.660 0.2 1 233 153 157 LEU H H 8.174 0.03 1 234 153 157 LEU C C 174.374 0.2 1 235 153 157 LEU N N 123.627 0.2 1 236 154 158 LYS H H 8.250 0.03 1 237 154 158 LYS C C 173.523 0.2 1 238 154 158 LYS N N 122.523 0.2 1 239 155 159 LYS H H 8.268 0.03 1 240 155 159 LYS C C 173.696 0.2 1 241 155 159 LYS N N 123.150 0.2 1 242 156 160 GLU H H 8.450 0.03 1 243 156 160 GLU C C 173.802 0.2 1 244 156 160 GLU N N 122.510 0.2 1 245 157 161 THR H H 8.218 0.03 1 246 157 161 THR C C 171.672 0.2 1 247 157 161 THR N N 115.713 0.2 1 248 158 162 THR H H 8.168 0.03 1 249 158 162 THR N N 119.519 0.2 1 250 159 163 PRO C C 174.053 0.2 1 251 160 164 THR H H 8.284 0.03 1 252 160 164 THR N N 117.233 0.2 1 253 162 166 SER H H 8.335 0.03 1 254 162 166 SER N N 115.726 0.2 1 255 163 167 GLN H H 8.323 0.03 1 256 163 167 GLN C C 173.624 0.2 1 257 163 167 GLN N N 122.456 0.2 1 258 164 168 ARG H H 8.249 0.03 1 259 164 168 ARG C C 174.022 0.2 1 260 164 168 ARG N N 121.455 0.2 1 261 165 169 GLU H H 8.333 0.03 1 262 165 169 GLU C C 174.166 0.2 1 263 165 169 GLU N N 121.519 0.2 1 264 166 170 SER H H 8.305 0.03 1 265 166 170 SER N N 116.678 0.2 1 266 168 172 SER H H 8.270 0.03 1 267 168 172 SER N N 116.710 0.2 1 268 169 173 SER H H 8.280 0.03 1 269 169 173 SER N N 118.146 0.2 1 270 170 174 LYS H H 8.128 0.03 1 271 170 174 LYS N N 122.817 0.2 1 272 171 175 ALA H H 8.026 0.03 1 273 171 175 ALA N N 123.758 0.2 1 274 172 176 ARG H H 8.065 0.03 1 275 172 176 ARG C C 174.215 0.2 1 276 172 176 ARG N N 119.708 0.2 1 277 173 177 MET H H 8.159 0.03 1 278 173 177 MET C C 173.763 0.2 1 279 173 177 MET N N 120.685 0.2 1 280 174 178 ALA H H 8.111 0.03 1 281 174 178 ALA C C 174.982 0.2 1 282 174 178 ALA N N 124.483 0.2 1 283 175 179 ALA H H 8.036 0.03 1 284 175 179 ALA C C 175.283 0.2 1 285 175 179 ALA N N 122.164 0.2 1 286 176 180 GLN H H 8.171 0.03 1 287 176 180 GLN N N 119.047 0.2 1 288 177 181 THR H H 8.025 0.03 1 289 177 181 THR N N 114.888 0.2 1 290 178 182 ALA H H 8.226 0.03 1 291 178 182 ALA N N 126.367 0.2 1 292 179 183 SER H H 8.188 0.03 1 293 179 183 SER C C 171.734 0.2 1 294 179 183 SER N N 115.080 0.2 1 295 180 184 GLY H H 8.058 0.03 1 296 180 184 GLY N N 110.505 0.2 1 297 182 186 PRO C C 173.768 0.2 1 298 183 187 ALA H H 8.203 0.03 1 299 183 187 ALA C C 174.844 0.2 1 300 183 187 ALA N N 123.714 0.2 1 301 184 188 LEU H H 8.055 0.03 1 302 184 188 LEU C C 174.492 0.2 1 303 184 188 LEU N N 121.131 0.2 1 304 185 189 GLU H H 8.261 0.03 1 305 185 189 GLU C C 173.308 0.2 1 306 185 189 GLU N N 121.254 0.2 1 307 186 190 TRP H H 8.106 0.03 1 308 186 190 TRP C C 173.172 0.2 1 309 186 190 TRP N N 122.462 0.2 1 310 187 191 SER H H 7.792 0.03 1 311 187 191 SER C C 170.777 0.2 1 312 187 191 SER N N 117.849 0.2 1 313 188 192 ALA H H 8.062 0.03 1 314 188 192 ALA C C 175.196 0.2 1 315 188 192 ALA N N 125.867 0.2 1 316 189 193 THR H H 8.036 0.03 1 317 189 193 THR N N 112.619 0.2 1 318 190 194 ASN H H 8.334 0.03 1 319 190 194 ASN N N 120.934 0.2 1 320 191 195 GLU H H 8.412 0.03 1 321 191 195 GLU C C 174.232 0.2 1 322 191 195 GLU N N 121.728 0.2 1 323 192 196 GLU H H 8.345 0.03 1 324 192 196 GLU C C 174.264 0.2 1 325 192 196 GLU N N 120.401 0.2 1 326 193 197 ASP H H 8.184 0.03 1 327 193 197 ASP C C 173.715 0.2 1 328 193 197 ASP N N 120.929 0.2 1 329 194 198 ASP H H 8.085 0.03 1 330 194 198 ASP C C 174.630 0.2 1 331 194 198 ASP N N 120.435 0.2 1 332 195 199 LEU H H 8.217 0.03 1 333 195 199 LEU N N 121.426 0.2 1 334 196 200 SER H H 8.245 0.03 1 335 196 200 SER N N 116.426 0.2 1 336 197 201 VAL H H 7.846 0.03 1 337 197 201 VAL C C 174.768 0.2 1 338 197 201 VAL N N 123.666 0.2 1 339 198 202 GLU H H 8.148 0.03 1 340 198 202 GLU C C 175.132 0.2 1 341 198 202 GLU N N 118.717 0.2 1 342 199 203 ALA H H 7.947 0.03 1 343 199 203 ALA N N 119.961 0.2 1 344 200 204 GLU H H 7.551 0.03 1 345 200 204 GLU N N 119.958 0.2 1 346 201 205 ILE H H 7.907 0.03 1 347 201 205 ILE N N 118.489 0.2 1 348 202 206 ALA H H 8.472 0.03 1 349 202 206 ALA N N 119.524 0.2 1 350 203 207 HIS H H 8.091 0.03 1 351 203 207 HIS N N 115.796 0.2 1 352 204 208 GLN H H 7.914 0.03 1 353 204 208 GLN N N 116.942 0.2 1 354 207 211 GLU H H 7.774 0.03 1 355 207 211 GLU N N 116.420 0.2 1 356 208 212 SER H H 7.245 0.03 1 357 208 212 SER N N 113.712 0.2 1 358 209 213 PHE H H 7.274 0.03 1 359 209 213 PHE N N 125.540 0.2 1 360 210 214 SER H H 8.448 0.03 1 361 210 214 SER N N 106.081 0.2 1 362 211 215 LYS H H 7.278 0.03 1 363 211 215 LYS N N 127.228 0.2 1 364 212 216 LYS H H 8.466 0.03 1 365 212 216 LYS N N 125.006 0.2 1 366 213 217 TYR H H 8.780 0.03 1 367 213 217 TYR N N 125.341 0.2 1 368 214 218 LYS H H 8.232 0.03 1 369 214 218 LYS N N 118.063 0.2 1 370 215 219 PHE H H 8.982 0.03 1 371 215 219 PHE N N 119.641 0.2 1 372 217 221 SER C C 173.392 0.2 1 373 218 222 ARG H H 8.360 0.03 1 374 218 222 ARG N N 123.524 0.2 1 375 221 225 GLY H H 7.844 0.03 1 376 221 225 GLY N N 109.463 0.2 1 377 222 226 ILE H H 8.434 0.03 1 378 222 226 ILE N N 122.862 0.2 1 379 223 227 LEU H H 9.197 0.03 1 380 223 227 LEU N N 129.952 0.2 1 381 224 228 LEU H H 8.582 0.03 1 382 224 228 LEU N N 126.807 0.2 1 383 225 229 TYR H H 9.177 0.03 1 384 225 229 TYR N N 125.914 0.2 1 385 226 230 ASN H H 6.924 0.03 1 386 226 230 ASN N N 118.590 0.2 1 387 227 231 PHE H H 9.075 0.03 1 388 227 231 PHE N N 115.633 0.2 1 389 228 232 GLU H H 7.091 0.03 1 390 228 232 GLU C C 175.471 0.2 1 391 228 232 GLU N N 121.023 0.2 1 392 229 233 GLN H H 7.603 0.03 1 393 229 233 GLN N N 116.380 0.2 1 394 230 234 LEU H H 7.397 0.03 1 395 230 234 LEU N N 117.442 0.2 1 396 232 236 MET H H 8.206 0.03 1 397 232 236 MET N N 116.897 0.2 1 398 233 237 ASN H H 9.066 0.03 1 399 233 237 ASN N N 120.889 0.2 1 400 234 238 LEU H H 8.866 0.03 1 401 234 238 LEU C C 174.983 0.2 1 402 234 238 LEU N N 124.962 0.2 1 403 235 239 ASP H H 8.462 0.03 1 404 235 239 ASP N N 115.828 0.2 1 405 236 240 ASP H H 7.438 0.03 1 406 236 240 ASP N N 119.107 0.2 1 407 237 241 ILE H H 7.855 0.03 1 408 237 241 ILE N N 121.623 0.2 1 409 238 242 VAL H H 8.426 0.03 1 410 238 242 VAL N N 120.033 0.2 1 411 239 243 LYS H H 7.454 0.03 1 412 239 243 LYS C C 176.344 0.2 1 413 239 243 LYS N N 116.121 0.2 1 414 240 244 GLU H H 7.264 0.03 1 415 240 244 GLU N N 117.177 0.2 1 416 241 245 ALA H H 8.765 0.03 1 417 241 245 ALA N N 122.063 0.2 1 418 242 246 LYS H H 7.307 0.03 1 419 242 246 LYS C C 174.174 0.2 1 420 242 246 LYS N N 111.828 0.2 1 421 243 247 ASN H H 7.542 0.03 1 422 243 247 ASN N N 115.184 0.2 1 423 244 248 VAL H H 7.169 0.03 1 424 244 248 VAL N N 124.175 0.2 1 425 247 251 VAL H H 7.408 0.03 1 426 247 251 VAL N N 120.540 0.2 1 427 248 252 THR H H 8.854 0.03 1 428 248 252 THR N N 113.081 0.2 1 429 249 253 ARG H H 7.523 0.03 1 430 249 253 ARG N N 121.858 0.2 1 431 251 255 ALA H H 8.446 0.03 1 432 251 255 ALA N N 119.535 0.2 1 433 252 256 ARG H H 8.082 0.03 1 434 252 256 ARG N N 119.813 0.2 1 435 253 257 ASP H H 7.299 0.03 1 436 253 257 ASP N N 116.082 0.2 1 437 254 258 GLY H H 7.849 0.03 1 438 254 258 GLY N N 109.096 0.2 1 439 255 259 SER H H 7.972 0.03 1 440 255 259 SER C C 170.275 0.2 1 441 255 259 SER N N 117.282 0.2 1 442 256 260 LYS H H 8.237 0.03 1 443 256 260 LYS N N 121.208 0.2 1 444 259 263 LEU H H 7.514 0.03 1 445 259 263 LEU N N 124.630 0.2 1 446 262 266 VAL H H 8.152 0.03 1 447 262 266 VAL N N 118.173 0.2 1 448 263 267 LEU H H 8.689 0.03 1 449 263 267 LEU N N 119.773 0.2 1 450 264 268 GLY H H 8.519 0.03 1 451 264 268 GLY N N 104.821 0.2 1 452 265 269 TRP H H 8.583 0.03 1 453 265 269 TRP N N 121.685 0.2 1 454 266 270 VAL H H 8.742 0.03 1 455 266 270 VAL N N 118.127 0.2 1 456 267 271 ALA H H 9.210 0.03 1 457 267 271 ALA N N 124.339 0.2 1 458 269 273 ALA H H 6.941 0.03 1 459 269 273 ALA C C 176.387 0.2 1 460 269 273 ALA N N 115.947 0.2 1 461 270 274 ASN H H 7.376 0.03 1 462 270 274 ASN N N 112.348 0.2 1 463 271 275 SER H H 8.802 0.03 1 464 271 275 SER N N 115.348 0.2 1 465 272 276 LYS H H 8.896 0.03 1 466 272 276 LYS N N 132.037 0.2 1 467 273 277 LYS H H 8.118 0.03 1 468 273 277 LYS N N 118.163 0.2 1 469 274 278 PHE H H 7.703 0.03 1 470 274 278 PHE N N 119.289 0.2 1 471 275 279 GLN H H 7.898 0.03 1 472 275 279 GLN N N 114.380 0.2 1 473 276 280 LEU H H 7.475 0.03 1 474 276 280 LEU C C 175.672 0.2 1 475 276 280 LEU N N 116.191 0.2 1 476 277 281 LEU H H 7.364 0.03 1 477 277 281 LEU C C 175.248 0.2 1 478 277 281 LEU N N 117.134 0.2 1 479 278 282 VAL H H 7.571 0.03 1 480 278 282 VAL N N 120.002 0.2 1 481 279 283 GLU H H 7.660 0.03 1 482 279 283 GLU N N 128.122 0.2 1 483 282 286 LYS H H 8.650 0.03 1 484 282 286 LYS N N 121.879 0.2 1 485 283 287 LEU H H 8.540 0.03 1 486 283 287 LEU N N 119.588 0.2 1 487 284 288 SER H H 7.953 0.03 1 488 284 288 SER N N 114.399 0.2 1 489 285 289 LYS H H 7.084 0.03 1 490 285 289 LYS N N 121.022 0.2 1 491 286 290 ILE H H 7.800 0.03 1 492 286 290 ILE N N 119.203 0.2 1 493 294 298 TYR H H 8.134 0.03 1 494 294 298 TYR N N 116.644 0.2 1 495 296 300 SER H H 7.820 0.03 1 496 296 300 SER N N 117.780 0.2 1 497 297 301 CYS H H 7.927 0.03 1 498 297 301 CYS N N 125.624 0.2 1 stop_ save_