data_26727 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N assignment for the C-terminal domain of human Doublecortin ; _BMRB_accession_number 26727 _BMRB_flat_file_name bmr26727.str _Entry_type original _Submission_date 2016-01-10 _Accession_date 2016-01-10 _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 'Di Lello' Paola . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 109 "13C chemical shifts" 417 "15N chemical shifts" 108 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-01-11 update BMRB 'update entry citation' 2016-07-14 original author 'original release' stop_ _Original_release_date 2016-07-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Crystal Structures of the Human Doublecortin C- and N-terminal Domains in Complex with Specific Antibodies ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27226599 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Burger Dominique . . 2 Stihle Martine . . 3 Sharma Ashwani . . 4 'Di Lello' Paola . . 5 Benz Jorg . . 6 D'Arcy Brigitte . . 7 Debulpaep Maja . . 8 Fry David . . 9 Huber Walter . . 10 Kremer Thomas . . 11 Laeremans Toon . . 12 Matile Hugues . . 13 Ross Alfred . . 14 Rufer Arne C. . 15 Schoch Guillaume . . 16 Steinmetz Michel O. . 17 Steyaert Jan . . 18 Rudolph Markus G. . 19 Thoma Ralf . . 20 Ruf Armin . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 291 _Journal_issue 31 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 16292 _Page_last 16306 _Year 2016 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Doublecortin C-terminal domain monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Doublecortin C-terminal domain monomer' $Doublecortin_C-terminal_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details monomer save_ ######################## # Monomeric polymers # ######################## save_Doublecortin_C-terminal_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Doublecortin_C-terminal_domain _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 114 _Mol_residue_sequence ; LVPRGSHMARENKDFVRPKL VTIIRSGVKPRKAVRVLLNK KTAHSFEQVLTDITEAIKLE TGVVKKLYTLDGKQVTCLHD FFGDDDVFIACGPEKFRYAQ DDFSLDENECRVMK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 243 LEU 2 244 VAL 3 245 PRO 4 246 ARG 5 247 GLY 6 248 SER 7 249 HIS 8 250 MET 9 251 ALA 10 252 ARG 11 253 GLU 12 254 ASN 13 255 LYS 14 256 ASP 15 257 PHE 16 258 VAL 17 259 ARG 18 260 PRO 19 261 LYS 20 262 LEU 21 263 VAL 22 264 THR 23 265 ILE 24 266 ILE 25 267 ARG 26 268 SER 27 269 GLY 28 270 VAL 29 271 LYS 30 272 PRO 31 273 ARG 32 274 LYS 33 275 ALA 34 276 VAL 35 277 ARG 36 278 VAL 37 279 LEU 38 280 LEU 39 281 ASN 40 282 LYS 41 283 LYS 42 284 THR 43 285 ALA 44 286 HIS 45 287 SER 46 288 PHE 47 289 GLU 48 290 GLN 49 291 VAL 50 292 LEU 51 293 THR 52 294 ASP 53 295 ILE 54 296 THR 55 297 GLU 56 298 ALA 57 299 ILE 58 300 LYS 59 301 LEU 60 302 GLU 61 303 THR 62 304 GLY 63 305 VAL 64 306 VAL 65 307 LYS 66 308 LYS 67 309 LEU 68 310 TYR 69 311 THR 70 312 LEU 71 313 ASP 72 314 GLY 73 315 LYS 74 316 GLN 75 317 VAL 76 318 THR 77 319 CYS 78 320 LEU 79 321 HIS 80 322 ASP 81 323 PHE 82 324 PHE 83 325 GLY 84 326 ASP 85 327 ASP 86 328 ASP 87 329 VAL 88 330 PHE 89 331 ILE 90 332 ALA 91 333 CYS 92 334 GLY 93 335 PRO 94 336 GLU 95 337 LYS 96 338 PHE 97 339 ARG 98 340 TYR 99 341 ALA 100 342 GLN 101 343 ASP 102 344 ASP 103 345 PHE 104 346 SER 105 347 LEU 106 348 ASP 107 349 GLU 108 350 ASN 109 351 GLU 110 352 CYS 111 353 ARG 112 354 VAL 113 355 MET 114 356 LYS 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 $Doublecortin_C-terminal_domain human 9606 Eukaryota Metazoa Homo sapiens 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 $Doublecortin_C-terminal_domain 'recombinant technology' . Escherichia coli . pER2b 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 $Doublecortin_C-terminal_domain 0.5 mM '[U-99% 13C; U-99% 15N]' 'sodium acetate' 20 mM 'natural abundance' TCEP 5 mM 'natural abundance' D2O 5 % 'natural abundance' H2O 95 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 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_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_(HB)CBCA(CO)NNH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (HB)CBCA(CO)NNH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _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' 20 . mM pH 4.0 . pH pressure 1 . atm temperature 300 . 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 external indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 external indirect . . . 1 DSS N 15 'methyl protons' ppm 0 external 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' '3D HNCACB' '3D (HB)CBCA(CO)NNH' '3D C(CO)NH' '3D HNCA' '3D HN(CO)CA' '3D HN(CA)CO' 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 'Doublecortin C-terminal domain monomer' _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 1 243 1 LEU C C 173.500 0.1 1 2 243 1 LEU CA C 54.800 0.1 1 3 243 1 LEU CB C 43.000 0.1 1 4 243 1 LEU CG C 26.800 0.1 1 5 243 1 LEU CD1 C 24.500 0.1 2 6 243 1 LEU CD2 C 24.500 0.1 2 7 244 2 VAL H H 8.560 0.01 1 8 244 2 VAL C C 174.370 0.1 1 9 244 2 VAL CA C 60.300 0.1 1 10 244 2 VAL CB C 32.900 0.1 1 11 244 2 VAL N N 124.800 0.1 1 12 245 3 PRO C C 177.200 0.1 1 13 245 3 PRO CA C 63.300 0.1 1 14 245 3 PRO CB C 32.400 0.1 1 15 245 3 PRO CG C 27.800 0.1 1 16 245 3 PRO CD C 51.400 0.1 1 17 246 4 ARG H H 8.460 0.01 1 18 246 4 ARG C C 177.400 0.1 1 19 246 4 ARG CA C 56.700 0.1 1 20 246 4 ARG CB C 31.200 0.1 1 21 246 4 ARG CG C 27.100 0.1 1 22 246 4 ARG CD C 43.700 0.1 1 23 246 4 ARG N N 122.200 0.1 1 24 247 5 GLY H H 8.460 0.01 1 25 247 5 GLY C C 174.400 0.1 1 26 247 5 GLY CA C 45.500 0.1 1 27 247 5 GLY N N 110.400 0.1 1 28 248 6 SER H H 8.160 0.01 1 29 248 6 SER C C 174.800 0.1 1 30 248 6 SER CA C 58.600 0.1 1 31 248 6 SER CB C 64.200 0.1 1 32 248 6 SER N N 115.400 0.1 1 33 249 7 HIS H H 8.620 0.01 1 34 249 7 HIS C C 174.570 0.1 1 35 249 7 HIS CA C 55.600 0.1 1 36 249 7 HIS CB C 29.200 0.1 1 37 249 7 HIS N N 120.400 0.1 1 38 250 8 MET H H 8.340 0.01 1 39 250 8 MET C C 176.090 0.1 1 40 250 8 MET CA C 55.700 0.1 1 41 250 8 MET CB C 33.400 0.1 1 42 250 8 MET CG C 32.300 0.1 1 43 250 8 MET N N 121.700 0.1 1 44 251 9 ALA H H 8.370 0.01 1 45 251 9 ALA C C 177.880 0.1 1 46 251 9 ALA CA C 52.900 0.1 1 47 251 9 ALA CB C 19.600 0.1 1 48 251 9 ALA N N 126.000 0.1 1 49 252 10 ARG H H 8.300 0.01 1 50 252 10 ARG C C 176.530 0.1 1 51 252 10 ARG CA C 56.400 0.1 1 52 252 10 ARG CB C 31.200 0.1 1 53 252 10 ARG CG C 27.200 0.1 1 54 252 10 ARG CD C 43.700 0.1 1 55 252 10 ARG N N 120.500 0.1 1 56 253 11 GLU H H 8.410 0.01 1 57 253 11 GLU C C 176.210 0.1 1 58 253 11 GLU CA C 56.400 0.1 1 59 253 11 GLU CB C 30.200 0.1 1 60 253 11 GLU CG C 35.100 0.1 1 61 253 11 GLU N N 121.900 0.1 1 62 254 12 ASN H H 8.520 0.01 1 63 254 12 ASN C C 175.570 0.1 1 64 254 12 ASN CA C 53.600 0.1 1 65 254 12 ASN CB C 39.200 0.1 1 66 254 12 ASN N N 121.100 0.1 1 67 255 13 LYS H H 8.350 0.01 1 68 255 13 LYS C C 176.620 0.1 1 69 255 13 LYS CA C 56.600 0.1 1 70 255 13 LYS CB C 33.000 0.1 1 71 255 13 LYS CG C 24.900 0.1 1 72 255 13 LYS CD C 29.500 0.1 1 73 255 13 LYS CE C 42.500 0.1 1 74 255 13 LYS N N 122.000 0.1 1 75 256 14 ASP H H 8.250 0.01 1 76 256 14 ASP C C 175.760 0.1 1 77 256 14 ASP CA C 54.600 0.1 1 78 256 14 ASP CB C 40.600 0.1 1 79 256 14 ASP N N 120.900 0.1 1 80 257 15 PHE H H 7.300 0.01 1 81 257 15 PHE C C 175.360 0.1 1 82 257 15 PHE CA C 57.100 0.1 1 83 257 15 PHE CB C 39.400 0.1 1 84 257 15 PHE N N 117.600 0.1 1 85 258 16 VAL H H 7.380 0.01 1 86 258 16 VAL C C 174.900 0.1 1 87 258 16 VAL CA C 63.900 0.1 1 88 258 16 VAL CB C 31.600 0.1 1 89 258 16 VAL CG1 C 21.500 0.1 2 90 258 16 VAL CG2 C 21.200 0.1 2 91 258 16 VAL N N 123.300 0.1 1 92 259 17 ARG H H 7.300 0.01 1 93 259 17 ARG C C 172.640 0.1 1 94 259 17 ARG CA C 53.300 0.1 1 95 259 17 ARG CB C 31.000 0.1 1 96 259 17 ARG N N 126.900 0.1 1 97 260 18 PRO C C 177.480 0.1 1 98 260 18 PRO CA C 63.500 0.1 1 99 260 18 PRO CB C 32.200 0.1 1 100 260 18 PRO CD C 50.600 0.1 1 101 261 19 LYS H H 9.110 0.01 1 102 261 19 LYS C C 174.150 0.1 1 103 261 19 LYS CA C 56.500 0.1 1 104 261 19 LYS CB C 36.700 0.1 1 105 261 19 LYS N N 124.900 0.1 1 106 262 20 LEU H H 8.630 0.01 1 107 262 20 LEU C C 177.310 0.1 1 108 262 20 LEU CA C 54.500 0.1 1 109 262 20 LEU CB C 43.500 0.1 1 110 262 20 LEU CD1 C 25.200 0.1 2 111 262 20 LEU CD2 C 25.200 0.1 2 112 262 20 LEU N N 128.700 0.1 1 113 263 21 VAL H H 8.950 0.01 1 114 263 21 VAL C C 174.630 0.1 1 115 263 21 VAL CA C 59.600 0.1 1 116 263 21 VAL CB C 34.800 0.1 1 117 263 21 VAL CG1 C 23.200 0.1 2 118 263 21 VAL CG2 C 18.900 0.1 2 119 263 21 VAL N N 119.400 0.1 1 120 264 22 THR H H 8.830 0.01 1 121 264 22 THR C C 173.040 0.1 1 122 264 22 THR CA C 62.700 0.1 1 123 264 22 THR CB C 70.500 0.1 1 124 264 22 THR CG2 C 22.000 0.1 1 125 264 22 THR N N 119.600 0.1 1 126 265 23 ILE H H 9.460 0.01 1 127 265 23 ILE C C 175.360 0.1 1 128 265 23 ILE CA C 57.700 0.1 1 129 265 23 ILE CB C 38.000 0.1 1 130 265 23 ILE N N 126.800 0.1 1 131 266 24 ILE H H 9.130 0.01 1 132 266 24 ILE C C 175.920 0.1 1 133 266 24 ILE CA C 59.900 0.1 1 134 266 24 ILE CB C 40.900 0.1 1 135 266 24 ILE N N 126.500 0.1 1 136 267 25 ARG H H 8.740 0.01 1 137 267 25 ARG C C 175.910 0.1 1 138 267 25 ARG CA C 55.900 0.1 1 139 267 25 ARG CB C 31.400 0.1 1 140 267 25 ARG N N 126.900 0.1 1 141 268 26 SER H H 8.450 0.01 1 142 268 26 SER C C 175.670 0.1 1 143 268 26 SER CA C 59.400 0.1 1 144 268 26 SER CB C 64.400 0.1 1 145 268 26 SER N N 121.300 0.1 1 146 269 27 GLY H H 8.610 0.01 1 147 269 27 GLY C C 173.770 0.1 1 148 269 27 GLY CA C 46.200 0.1 1 149 269 27 GLY N N 111.400 0.1 1 150 270 28 VAL H H 7.320 0.01 1 151 270 28 VAL C C 175.020 0.1 1 152 270 28 VAL CA C 61.500 0.1 1 153 270 28 VAL CB C 34.100 0.1 1 154 270 28 VAL CG1 C 21.700 0.1 2 155 270 28 VAL CG2 C 20.700 0.1 2 156 270 28 VAL N N 116.900 0.1 1 157 271 29 LYS H H 8.320 0.01 1 158 271 29 LYS C C 175.110 0.1 1 159 271 29 LYS CA C 54.400 0.1 1 160 271 29 LYS CB C 34.300 0.1 1 161 271 29 LYS N N 124.500 0.1 1 162 272 30 PRO C C 176.020 0.1 1 163 272 30 PRO CA C 62.700 0.1 1 164 272 30 PRO CB C 34.700 0.1 1 165 273 31 ARG H H 8.690 0.01 1 166 273 31 ARG C C 176.230 0.1 1 167 273 31 ARG CA C 57.000 0.1 1 168 273 31 ARG CB C 31.100 0.1 1 169 273 31 ARG CD C 44.000 0.1 1 170 273 31 ARG N N 122.200 0.1 1 171 274 32 LYS H H 8.330 0.01 1 172 274 32 LYS C C 174.200 0.1 1 173 274 32 LYS CA C 55.600 0.1 1 174 274 32 LYS CB C 34.700 0.1 1 175 274 32 LYS CE C 42.600 0.1 1 176 274 32 LYS N N 125.500 0.1 1 177 275 33 ALA H H 8.490 0.01 1 178 275 33 ALA C C 177.130 0.1 1 179 275 33 ALA CA C 50.800 0.1 1 180 275 33 ALA CB C 22.400 0.1 1 181 275 33 ALA N N 127.300 0.1 1 182 276 34 VAL H H 8.880 0.01 1 183 276 34 VAL C C 174.180 0.1 1 184 276 34 VAL CA C 60.300 0.1 1 185 276 34 VAL CB C 35.600 0.1 1 186 276 34 VAL CG1 C 21.700 0.1 2 187 276 34 VAL CG2 C 20.500 0.1 2 188 276 34 VAL N N 118.200 0.1 1 189 277 35 ARG H H 8.550 0.01 1 190 277 35 ARG C C 176.460 0.1 1 191 277 35 ARG CA C 55.000 0.1 1 192 277 35 ARG CB C 32.100 0.1 1 193 277 35 ARG CD C 44.000 0.1 1 194 277 35 ARG N N 123.500 0.1 1 195 278 36 VAL H H 9.000 0.01 1 196 278 36 VAL C C 173.720 0.1 1 197 278 36 VAL CA C 61.000 0.1 1 198 278 36 VAL CB C 35.900 0.1 1 199 278 36 VAL CG1 C 21.600 0.1 2 200 278 36 VAL CG2 C 21.600 0.1 2 201 278 36 VAL N N 122.500 0.1 1 202 279 37 LEU H H 8.380 0.01 1 203 279 37 LEU C C 176.010 0.1 1 204 279 37 LEU CA C 54.700 0.1 1 205 279 37 LEU CB C 42.800 0.1 1 206 279 37 LEU CD1 C 23.300 0.1 2 207 279 37 LEU CD2 C 23.300 0.1 2 208 279 37 LEU N N 127.900 0.1 1 209 280 38 LEU H H 9.190 0.01 1 210 280 38 LEU C C 174.460 0.1 1 211 280 38 LEU CA C 53.600 0.1 1 212 280 38 LEU CB C 42.900 0.1 1 213 280 38 LEU CG C 27.100 0.1 1 214 280 38 LEU CD1 C 23.700 0.1 2 215 280 38 LEU CD2 C 23.700 0.1 2 216 280 38 LEU N N 128.900 0.1 1 217 281 39 ASN H H 7.960 0.01 1 218 281 39 ASN C C 174.870 0.1 1 219 281 39 ASN CA C 52.300 0.1 1 220 281 39 ASN CB C 39.000 0.1 1 221 281 39 ASN N N 118.500 0.1 1 222 282 40 LYS H H 8.710 0.01 1 223 282 40 LYS C C 177.820 0.1 1 224 282 40 LYS CA C 59.900 0.1 1 225 282 40 LYS CB C 32.600 0.1 1 226 282 40 LYS CD C 25.800 0.1 1 227 282 40 LYS CE C 42.400 0.1 1 228 282 40 LYS N N 118.000 0.1 1 229 283 41 LYS H H 7.910 0.01 1 230 283 41 LYS C C 178.710 0.1 1 231 283 41 LYS CA C 58.500 0.1 1 232 283 41 LYS CB C 33.100 0.1 1 233 283 41 LYS CD C 25.600 0.1 1 234 283 41 LYS CE C 42.300 0.1 1 235 283 41 LYS N N 116.500 0.1 1 236 284 42 THR H H 7.850 0.01 1 237 284 42 THR C C 175.200 0.1 1 238 284 42 THR CA C 61.600 0.1 1 239 284 42 THR CB C 70.100 0.1 1 240 284 42 THR CG2 C 22.100 0.1 1 241 284 42 THR N N 108.100 0.1 1 242 285 43 ALA H H 7.900 0.01 1 243 285 43 ALA C C 175.080 0.1 1 244 285 43 ALA CA C 50.900 0.1 1 245 285 43 ALA CB C 19.100 0.1 1 246 285 43 ALA N N 125.600 0.1 1 247 286 44 HIS H H 8.680 0.01 1 248 286 44 HIS C C 175.150 0.1 1 249 286 44 HIS CA C 57.300 0.1 1 250 286 44 HIS CB C 29.200 0.1 1 251 286 44 HIS N N 115.900 0.1 1 252 287 45 SER H H 7.730 0.01 1 253 287 45 SER C C 173.940 0.1 1 254 287 45 SER CA C 56.800 0.1 1 255 287 45 SER CB C 66.700 0.1 1 256 287 45 SER N N 109.800 0.1 1 257 288 46 PHE H H 9.630 0.01 1 258 288 46 PHE C C 176.320 0.1 1 259 288 46 PHE CA C 62.200 0.1 1 260 288 46 PHE CB C 40.000 0.1 1 261 288 46 PHE N N 124.400 0.1 1 262 289 47 GLU H H 9.000 0.01 1 263 289 47 GLU C C 179.070 0.1 1 264 289 47 GLU CA C 60.300 0.1 1 265 289 47 GLU CB C 28.500 0.1 1 266 289 47 GLU CG C 35.900 0.1 1 267 289 47 GLU N N 117.100 0.1 1 268 290 48 GLN H H 7.900 0.01 1 269 290 48 GLN C C 178.370 0.1 1 270 290 48 GLN CA C 59.100 0.1 1 271 290 48 GLN CB C 28.300 0.1 1 272 290 48 GLN CG C 33.600 0.1 1 273 290 48 GLN N N 121.200 0.1 1 274 291 49 VAL H H 7.590 0.01 1 275 291 49 VAL C C 178.420 0.1 1 276 291 49 VAL CA C 66.800 0.1 1 277 291 49 VAL CB C 31.000 0.1 1 278 291 49 VAL N N 120.500 0.1 1 279 292 50 LEU H H 7.930 0.01 1 280 292 50 LEU C C 181.150 0.1 1 281 292 50 LEU CA C 58.600 0.1 1 282 292 50 LEU CB C 40.500 0.1 1 283 292 50 LEU CD1 C 24.900 0.1 2 284 292 50 LEU CD2 C 24.900 0.1 2 285 292 50 LEU N N 119.400 0.1 1 286 293 51 THR H H 8.150 0.01 1 287 293 51 THR C C 176.000 0.1 1 288 293 51 THR CA C 67.500 0.1 1 289 293 51 THR CB C 68.500 0.1 1 290 293 51 THR CG2 C 22.100 0.1 1 291 293 51 THR N N 119.800 0.1 1 292 294 52 ASP H H 8.520 0.01 1 293 294 52 ASP C C 179.440 0.1 1 294 294 52 ASP CA C 56.500 0.1 1 295 294 52 ASP CB C 37.900 0.1 1 296 294 52 ASP N N 122.700 0.1 1 297 295 53 ILE H H 8.610 0.01 1 298 295 53 ILE C C 176.900 0.1 1 299 295 53 ILE CA C 66.300 0.1 1 300 295 53 ILE CB C 38.400 0.1 1 301 295 53 ILE N N 120.400 0.1 1 302 296 54 THR H H 8.280 0.01 1 303 296 54 THR C C 176.610 0.1 1 304 296 54 THR CA C 68.000 0.1 1 305 296 54 THR CB C 69.600 0.1 1 306 296 54 THR N N 117.000 0.1 1 307 297 55 GLU H H 8.000 0.01 1 308 297 55 GLU C C 178.770 0.1 1 309 297 55 GLU CA C 58.700 0.1 1 310 297 55 GLU CB C 28.800 0.1 1 311 297 55 GLU CG C 34.500 0.1 1 312 297 55 GLU N N 118.800 0.1 1 313 298 56 ALA H H 7.810 0.01 1 314 298 56 ALA C C 179.590 0.1 1 315 298 56 ALA CA C 54.900 0.1 1 316 298 56 ALA CB C 19.600 0.1 1 317 298 56 ALA N N 121.700 0.1 1 318 299 57 ILE H H 7.990 0.01 1 319 299 57 ILE C C 174.930 0.1 1 320 299 57 ILE CA C 61.600 0.1 1 321 299 57 ILE CB C 38.900 0.1 1 322 299 57 ILE CG2 C 17.800 0.1 1 323 299 57 ILE CD1 C 14.600 0.1 1 324 299 57 ILE N N 111.900 0.1 1 325 300 58 LYS H H 7.650 0.01 1 326 300 58 LYS C C 176.470 0.1 1 327 300 58 LYS CA C 57.100 0.1 1 328 300 58 LYS CB C 30.000 0.1 1 329 300 58 LYS CE C 42.800 0.1 1 330 300 58 LYS N N 118.700 0.1 1 331 301 59 LEU H H 7.910 0.01 1 332 301 59 LEU C C 178.320 0.1 1 333 301 59 LEU CA C 55.400 0.1 1 334 301 59 LEU CB C 43.100 0.1 1 335 301 59 LEU N N 120.300 0.1 1 336 302 60 GLU H H 8.890 0.01 1 337 302 60 GLU C C 177.030 0.1 1 338 302 60 GLU CA C 58.100 0.1 1 339 302 60 GLU CB C 29.600 0.1 1 340 302 60 GLU CG C 35.400 0.1 1 341 302 60 GLU N N 122.800 0.1 1 342 303 61 THR H H 7.570 0.01 1 343 303 61 THR C C 174.570 0.1 1 344 303 61 THR CA C 62.000 0.1 1 345 303 61 THR CB C 69.700 0.1 1 346 303 61 THR CG2 C 21.900 0.1 1 347 303 61 THR N N 110.400 0.1 1 348 304 62 GLY H H 8.110 0.01 1 349 304 62 GLY C C 173.080 0.1 1 350 304 62 GLY CA C 45.300 0.1 1 351 304 62 GLY N N 111.200 0.1 1 352 305 63 VAL H H 7.680 0.01 1 353 305 63 VAL C C 176.020 0.1 1 354 305 63 VAL CA C 61.300 0.1 1 355 305 63 VAL CB C 34.300 0.1 1 356 305 63 VAL CG1 C 20.900 0.1 2 357 305 63 VAL CG2 C 20.900 0.1 2 358 305 63 VAL N N 115.700 0.1 1 359 306 64 VAL H H 7.800 0.01 1 360 306 64 VAL C C 174.930 0.1 1 361 306 64 VAL CA C 63.800 0.1 1 362 306 64 VAL CB C 32.100 0.1 1 363 306 64 VAL N N 122.400 0.1 1 364 307 65 LYS H H 8.600 0.01 1 365 307 65 LYS C C 176.790 0.1 1 366 307 65 LYS CA C 56.000 0.1 1 367 307 65 LYS CB C 35.000 0.1 1 368 307 65 LYS CE C 42.300 0.1 1 369 307 65 LYS N N 124.600 0.1 1 370 308 66 LYS H H 7.850 0.01 1 371 308 66 LYS C C 173.560 0.1 1 372 308 66 LYS CA C 55.400 0.1 1 373 308 66 LYS CB C 37.500 0.1 1 374 308 66 LYS CE C 42.700 0.1 1 375 308 66 LYS N N 117.600 0.1 1 376 309 67 LEU H H 8.560 0.01 1 377 309 67 LEU C C 175.230 0.1 1 378 309 67 LEU CA C 53.400 0.1 1 379 309 67 LEU CB C 47.100 0.1 1 380 309 67 LEU N N 122.200 0.1 1 381 310 68 TYR H H 9.060 0.01 1 382 310 68 TYR C C 177.400 0.1 1 383 310 68 TYR CA C 56.700 0.1 1 384 310 68 TYR CB C 44.200 0.1 1 385 310 68 TYR N N 119.500 0.1 1 386 311 69 THR H H 9.150 0.01 1 387 311 69 THR C C 177.010 0.1 1 388 311 69 THR CA C 61.400 0.1 1 389 311 69 THR CB C 70.900 0.1 1 390 311 69 THR CG2 C 23.300 0.1 1 391 311 69 THR N N 111.200 0.1 1 392 312 70 LEU H H 8.940 0.01 1 393 312 70 LEU C C 177.990 0.1 1 394 312 70 LEU CA C 58.000 0.1 1 395 312 70 LEU CB C 41.700 0.1 1 396 312 70 LEU CD1 C 25.500 0.1 2 397 312 70 LEU CD2 C 25.500 0.1 2 398 312 70 LEU N N 119.900 0.1 1 399 313 71 ASP H H 7.820 0.01 1 400 313 71 ASP C C 176.700 0.1 1 401 313 71 ASP CA C 53.200 0.1 1 402 313 71 ASP CB C 39.800 0.1 1 403 313 71 ASP N N 112.900 0.1 1 404 314 72 GLY H H 8.050 0.01 1 405 314 72 GLY C C 174.160 0.1 1 406 314 72 GLY CA C 46.100 0.1 1 407 314 72 GLY N N 108.200 0.1 1 408 315 73 LYS H H 7.630 0.01 1 409 315 73 LYS C C 176.550 0.1 1 410 315 73 LYS CA C 56.000 0.1 1 411 315 73 LYS CB C 33.000 0.1 1 412 315 73 LYS CG C 25.200 0.1 1 413 315 73 LYS CD C 29.400 0.1 1 414 315 73 LYS CE C 42.600 0.1 1 415 315 73 LYS N N 121.500 0.1 1 416 316 74 GLN H H 8.870 0.01 1 417 316 74 GLN C C 176.150 0.1 1 418 316 74 GLN CA C 56.300 0.1 1 419 316 74 GLN CB C 29.000 0.1 1 420 316 74 GLN CG C 34.200 0.1 1 421 316 74 GLN N N 125.800 0.1 1 422 317 75 VAL H H 8.500 0.01 1 423 317 75 VAL C C 176.470 0.1 1 424 317 75 VAL CA C 62.800 0.1 1 425 317 75 VAL N N 128.900 0.1 1 426 318 76 THR H H 8.910 0.01 1 427 318 76 THR C C 173.500 0.1 1 428 318 76 THR CA C 61.600 0.1 1 429 318 76 THR CB C 71.600 0.1 1 430 318 76 THR CG2 C 21.400 0.1 1 431 318 76 THR N N 115.300 0.1 1 432 319 77 CYS H H 7.560 0.01 1 433 319 77 CYS C C 174.050 0.1 1 434 319 77 CYS CA C 55.800 0.1 1 435 319 77 CYS CB C 31.100 0.1 1 436 319 77 CYS N N 115.900 0.1 1 437 320 78 LEU H H 9.090 0.01 1 438 320 78 LEU C C 179.030 0.1 1 439 320 78 LEU CA C 58.500 0.1 1 440 320 78 LEU CB C 43.200 0.1 1 441 320 78 LEU CG C 27.700 0.1 1 442 320 78 LEU CD1 C 25.100 0.1 2 443 320 78 LEU CD2 C 25.100 0.1 2 444 320 78 LEU N N 122.300 0.1 1 445 321 79 HIS H H 8.940 0.01 1 446 321 79 HIS C C 177.110 0.1 1 447 321 79 HIS CA C 59.300 0.1 1 448 321 79 HIS CB C 28.100 0.1 1 449 321 79 HIS N N 115.700 0.1 1 450 322 80 ASP H H 7.500 0.01 1 451 322 80 ASP C C 178.260 0.1 1 452 322 80 ASP CA C 57.100 0.1 1 453 322 80 ASP CB C 41.900 0.1 1 454 322 80 ASP N N 115.900 0.1 1 455 323 81 PHE H H 7.700 0.01 1 456 323 81 PHE C C 176.140 0.1 1 457 323 81 PHE CA C 60.700 0.1 1 458 323 81 PHE CB C 39.700 0.1 1 459 324 82 PHE H H 7.590 0.01 1 460 324 82 PHE C C 175.260 0.1 1 461 324 82 PHE CA C 59.200 0.1 1 462 324 82 PHE CB C 39.700 0.1 1 463 324 82 PHE N N 117.200 0.1 1 464 325 83 GLY H H 8.030 0.01 1 465 325 83 GLY C C 174.630 0.1 1 466 325 83 GLY CA C 45.300 0.1 1 467 325 83 GLY N N 111.100 0.1 1 468 326 84 ASP H H 8.630 0.01 1 469 326 84 ASP C C 176.520 0.1 1 470 326 84 ASP CA C 55.400 0.1 1 471 326 84 ASP CB C 40.500 0.1 1 472 326 84 ASP N N 120.900 0.1 1 473 327 85 ASP H H 7.910 0.01 1 474 327 85 ASP C C 176.280 0.1 1 475 327 85 ASP CA C 55.000 0.1 1 476 327 85 ASP CB C 42.400 0.1 1 477 327 85 ASP N N 117.600 0.1 1 478 328 86 ASP H H 9.050 0.01 1 479 328 86 ASP C C 173.300 0.1 1 480 328 86 ASP CA C 53.400 0.1 1 481 328 86 ASP CB C 41.600 0.1 1 482 328 86 ASP N N 120.200 0.1 1 483 329 87 VAL H H 6.900 0.01 1 484 329 87 VAL C C 173.730 0.1 1 485 329 87 VAL CA C 61.100 0.1 1 486 329 87 VAL CB C 34.300 0.1 1 487 329 87 VAL N N 120.800 0.1 1 488 330 88 PHE H H 8.900 0.01 1 489 330 88 PHE C C 173.820 0.1 1 490 330 88 PHE CA C 55.900 0.1 1 491 330 88 PHE CB C 43.500 0.1 1 492 330 88 PHE N N 122.800 0.1 1 493 331 89 ILE H H 9.790 0.01 1 494 331 89 ILE C C 175.780 0.1 1 495 331 89 ILE CA C 59.800 0.1 1 496 331 89 ILE CB C 40.500 0.1 1 497 331 89 ILE N N 122.100 0.1 1 498 332 90 ALA H H 9.050 0.01 1 499 332 90 ALA C C 176.690 0.1 1 500 332 90 ALA CA C 50.900 0.1 1 501 332 90 ALA CB C 21.500 0.1 1 502 332 90 ALA N N 128.400 0.1 1 503 333 91 CYS H H 8.840 0.01 1 504 333 91 CYS C C 175.140 0.1 1 505 333 91 CYS CA C 58.700 0.1 1 506 333 91 CYS CB C 31.000 0.1 1 507 333 91 CYS N N 120.400 0.1 1 508 334 92 GLY H H 8.640 0.01 1 509 334 92 GLY C C 171.600 0.1 1 510 334 92 GLY CA C 44.900 0.1 1 511 334 92 GLY N N 112.700 0.1 1 512 335 93 PRO C C 176.910 0.1 1 513 335 93 PRO CA C 63.700 0.1 1 514 335 93 PRO CB C 32.400 0.1 1 515 336 94 GLU H H 8.920 0.01 1 516 336 94 GLU C C 175.910 0.1 1 517 336 94 GLU CA C 56.600 0.1 1 518 336 94 GLU CB C 29.700 0.1 1 519 336 94 GLU CG C 35.200 0.1 1 520 336 94 GLU N N 121.300 0.1 1 521 337 95 LYS H H 8.210 0.01 1 522 337 95 LYS C C 176.570 0.1 1 523 337 95 LYS CA C 56.800 0.1 1 524 337 95 LYS CB C 33.200 0.1 1 525 337 95 LYS CG C 25.200 0.1 1 526 337 95 LYS CD C 29.800 0.1 1 527 337 95 LYS CE C 42.400 0.1 1 528 337 95 LYS N N 121.300 0.1 1 529 338 96 PHE H H 8.170 0.01 1 530 338 96 PHE C C 175.260 0.1 1 531 338 96 PHE CA C 58.200 0.1 1 532 338 96 PHE CB C 40.000 0.1 1 533 338 96 PHE N N 123.000 0.1 1 534 339 97 ARG H H 7.760 0.01 1 535 339 97 ARG C C 175.070 0.1 1 536 339 97 ARG CA C 55.700 0.1 1 537 339 97 ARG CB C 31.500 0.1 1 538 339 97 ARG CD C 43.700 0.1 1 539 339 97 ARG N N 125.000 0.1 1 540 340 98 TYR H H 7.830 0.01 1 541 340 98 TYR C C 175.350 0.1 1 542 340 98 TYR CA C 58.600 0.1 1 543 340 98 TYR CB C 39.100 0.1 1 544 340 98 TYR N N 122.200 0.1 1 545 341 99 ALA H H 7.970 0.01 1 546 341 99 ALA C C 177.430 0.1 1 547 341 99 ALA CA C 52.400 0.1 1 548 341 99 ALA CB C 19.900 0.1 1 549 341 99 ALA N N 126.100 0.1 1 550 342 100 GLN H H 8.200 0.01 1 551 342 100 GLN C C 176.440 0.1 1 552 342 100 GLN CA C 57.100 0.1 1 553 342 100 GLN CB C 29.300 0.1 1 554 342 100 GLN CG C 34.100 0.1 1 555 342 100 GLN N N 119.300 0.1 1 556 343 101 ASP H H 8.230 0.01 1 557 343 101 ASP C C 175.890 0.1 1 558 343 101 ASP CA C 54.400 0.1 1 559 343 101 ASP CB C 40.200 0.1 1 560 343 101 ASP N N 118.700 0.1 1 561 344 102 ASP H H 7.990 0.01 1 562 344 102 ASP C C 175.960 0.1 1 563 344 102 ASP CA C 54.400 0.1 1 564 344 102 ASP CB C 40.200 0.1 1 565 344 102 ASP N N 119.200 0.1 1 566 345 103 PHE H H 7.950 0.01 1 567 345 103 PHE C C 175.910 0.1 1 568 345 103 PHE CA C 58.200 0.1 1 569 345 103 PHE CB C 39.700 0.1 1 570 345 103 PHE N N 119.600 0.1 1 571 346 104 SER H H 7.990 0.01 1 572 346 104 SER C C 174.920 0.1 1 573 346 104 SER CA C 58.900 0.1 1 574 346 104 SER CB C 64.000 0.1 1 575 346 104 SER N N 116.000 0.1 1 576 347 105 LEU H H 8.130 0.01 1 577 347 105 LEU C C 177.530 0.1 1 578 347 105 LEU CA C 55.800 0.1 1 579 347 105 LEU CB C 42.700 0.1 1 580 347 105 LEU CG C 27.400 0.1 1 581 347 105 LEU CD1 C 25.400 0.1 2 582 347 105 LEU CD2 C 25.400 0.1 2 583 347 105 LEU N N 123.400 0.1 1 584 348 106 ASP H H 8.240 0.01 1 585 348 106 ASP C C 176.580 0.1 1 586 348 106 ASP CA C 54.200 0.1 1 587 348 106 ASP CB C 40.300 0.1 1 588 348 106 ASP N N 119.800 0.1 1 589 349 107 GLU H H 8.330 0.01 1 590 349 107 GLU C C 176.800 0.1 1 591 349 107 GLU CA C 57.300 0.1 1 592 349 107 GLU CB C 29.100 0.1 1 593 349 107 GLU CG C 34.100 0.1 1 594 349 107 GLU N N 120.700 0.1 1 595 350 108 ASN H H 8.350 0.01 1 596 350 108 ASN C C 176.050 0.1 1 597 350 108 ASN CA C 54.400 0.1 1 598 350 108 ASN CB C 39.100 0.1 1 599 350 108 ASN N N 118.200 0.1 1 600 351 109 GLU H H 8.170 0.01 1 601 351 109 GLU C C 176.630 0.1 1 602 351 109 GLU CA C 57.000 0.1 1 603 351 109 GLU CB C 29.400 0.1 1 604 351 109 GLU CG C 34.400 0.1 1 605 351 109 GLU N N 119.700 0.1 1 606 352 110 CYS H H 8.190 0.01 1 607 352 110 CYS C C 174.830 0.1 1 608 352 110 CYS CA C 59.400 0.1 1 609 352 110 CYS CB C 28.100 0.1 1 610 352 110 CYS N N 118.900 0.1 1 611 353 111 ARG H H 8.180 0.01 1 612 353 111 ARG C C 176.310 0.1 1 613 353 111 ARG CA C 56.700 0.1 1 614 353 111 ARG CB C 31.200 0.1 1 615 353 111 ARG CD C 43.700 0.1 1 616 353 111 ARG N N 122.900 0.1 1 617 354 112 VAL H H 8.040 0.01 1 618 354 112 VAL C C 176.240 0.1 1 619 354 112 VAL CA C 62.600 0.1 1 620 354 112 VAL CB C 33.000 0.1 1 621 354 112 VAL CG1 C 21.600 0.1 2 622 354 112 VAL CG2 C 21.200 0.1 2 623 354 112 VAL N N 120.900 0.1 1 624 355 113 MET H H 8.360 0.01 1 625 355 113 MET C C 175.410 0.1 1 626 355 113 MET CA C 55.600 0.1 1 627 355 113 MET CB C 33.200 0.1 1 628 355 113 MET CG C 32.400 0.1 1 629 355 113 MET N N 125.100 0.1 1 630 356 114 LYS H H 7.950 0.01 1 631 356 114 LYS C C 180.810 0.1 1 632 356 114 LYS CA C 57.700 0.1 1 633 356 114 LYS CB C 33.900 0.1 1 634 356 114 LYS N N 127.300 0.1 1 stop_ save_