data_25445 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; HN,N,CA,CB assignments of A2A-ct ; _BMRB_accession_number 25445 _BMRB_flat_file_name bmr25445.str _Entry_type original _Submission_date 2015-01-20 _Accession_date 2015-01-20 _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 Tossavainen Helena . . 2 Hellman Maarit . . 3 Permi Perttu . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 111 "13C chemical shifts" 344 "15N chemical shifts" 122 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-06-30 original BMRB . stop_ _Original_release_date 2016-06-30 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; HN, N, CA and CB assignments of the intrinsically disordered C-terminus of human adenosine A2A receptor ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25952762 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tossavainen Helena . . 2 Hellman Maarit . . 3 Piirainen Henni . . 4 Jaakola Veli-Pekka . . 5 Permi Perttu . . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _Journal_volume 9 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 403 _Page_last 406 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name A2A-ct _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label A2A-ct $A2A-ct 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_A2A-ct _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common A2A-ct _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 134 _Mol_residue_sequence ; MREFRQTFRKIIRSHVLRQQ EPFKAAGTSARVLAAHGSDG EQVSLRLNGHPPGVWANGSA PHPERRPNGYALGLVSGGSA QESQGNTGLPDVELLSHELK GVCPEPPGLDDPLAQDGAGV SGLEHHHHHHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 292 MET 2 293 ARG 3 294 GLU 4 295 PHE 5 296 ARG 6 297 GLN 7 298 THR 8 299 PHE 9 300 ARG 10 301 LYS 11 302 ILE 12 303 ILE 13 304 ARG 14 305 SER 15 306 HIS 16 307 VAL 17 308 LEU 18 309 ARG 19 310 GLN 20 311 GLN 21 312 GLU 22 313 PRO 23 314 PHE 24 315 LYS 25 316 ALA 26 317 ALA 27 318 GLY 28 319 THR 29 320 SER 30 321 ALA 31 322 ARG 32 323 VAL 33 324 LEU 34 325 ALA 35 326 ALA 36 327 HIS 37 328 GLY 38 329 SER 39 330 ASP 40 331 GLY 41 332 GLU 42 333 GLN 43 334 VAL 44 335 SER 45 336 LEU 46 337 ARG 47 338 LEU 48 339 ASN 49 340 GLY 50 341 HIS 51 342 PRO 52 343 PRO 53 344 GLY 54 345 VAL 55 346 TRP 56 347 ALA 57 348 ASN 58 349 GLY 59 350 SER 60 351 ALA 61 352 PRO 62 353 HIS 63 354 PRO 64 355 GLU 65 356 ARG 66 357 ARG 67 358 PRO 68 359 ASN 69 360 GLY 70 361 TYR 71 362 ALA 72 363 LEU 73 364 GLY 74 365 LEU 75 366 VAL 76 367 SER 77 368 GLY 78 369 GLY 79 370 SER 80 371 ALA 81 372 GLN 82 373 GLU 83 374 SER 84 375 GLN 85 376 GLY 86 377 ASN 87 378 THR 88 379 GLY 89 380 LEU 90 381 PRO 91 382 ASP 92 383 VAL 93 384 GLU 94 385 LEU 95 386 LEU 96 387 SER 97 388 HIS 98 389 GLU 99 390 LEU 100 391 LYS 101 392 GLY 102 393 VAL 103 394 CYS 104 395 PRO 105 396 GLU 106 397 PRO 107 398 PRO 108 399 GLY 109 400 LEU 110 401 ASP 111 402 ASP 112 403 PRO 113 404 LEU 114 405 ALA 115 406 GLN 116 407 ASP 117 408 GLY 118 409 ALA 119 410 GLY 120 411 VAL 121 412 SER 122 413 GLY 123 414 LEU 124 415 GLU 125 416 HIS 126 417 HIS 127 418 HIS 128 419 HIS 129 420 HIS 130 421 HIS 131 422 HIS 132 423 HIS 133 424 HIS 134 425 HIS 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 $A2A-ct 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 $A2A-ct 'recombinant technology' . Escherichia coli . pQE-T7-1 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 $A2A-ct 0.6 mM '[U-13C; U-15N]' HEPES 50 mM 'natural abundance' TCEP-HCl 1 mM 'natural abundance' 'sodium chloride' 250 mM 'natural abundance' 'calcium chloride' 5 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % U-2H stop_ save_ ############################ # Computer software used # ############################ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Agilent . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Agilent _Model INOVA _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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_i(HCA)CO(CA)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D i(HCA)CO(CA)NH' _Sample_label $sample_1 save_ save_3D_(HCA)N(CA)CO(N)H_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (HCA)N(CA)CO(N)H' _Sample_label $sample_1 save_ save_3D_(HCA)CON(CAN)H_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (HCA)CON(CAN)H' _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' 300 . mM pH 7.2 . 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 carbon' ppm 0.00 na indirect . . . 0.251449530 water H 1 protons ppm 4.79 internal direct . . . 1 'liquid anhydrous ammonia' N 15 nitrogen 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 HNCACB' '3D CBCA(CO)NH' '3D HNCO' '3D i(HCA)CO(CA)NH' '3D (HCA)N(CA)CO(N)H' '3D (HCA)CON(CAN)H' 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 A2A-ct _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 1 293 2 ARG C C 175.30 0.2 1 2 293 2 ARG CA C 56.40 0.2 1 3 293 2 ARG CB C 30.72 0.2 1 4 293 2 ARG N N 123.72 0.2 1 5 294 3 GLU H H 8.54 0.02 1 6 294 3 GLU C C 175.73 0.2 1 7 294 3 GLU CA C 56.36 0.2 1 8 294 3 GLU CB C 30.47 0.2 1 9 294 3 GLU N N 122.93 0.2 1 10 295 4 PHE H H 8.42 0.02 1 11 295 4 PHE C C 175.32 0.2 1 12 295 4 PHE CA C 57.73 0.2 1 13 295 4 PHE CB C 39.58 0.2 1 14 295 4 PHE N N 122.43 0.2 1 15 296 5 ARG H H 8.25 0.02 1 16 296 5 ARG C C 175.57 0.2 1 17 296 5 ARG CA C 55.88 0.2 1 18 296 5 ARG CB C 30.95 0.2 1 19 296 5 ARG N N 123.23 0.2 1 20 297 6 GLN H H 8.40 0.02 1 21 297 6 GLN C C 175.75 0.2 1 22 297 6 GLN CA C 55.85 0.2 1 23 297 6 GLN CB C 29.50 0.2 1 24 297 6 GLN N N 121.91 0.2 1 25 298 7 THR H H 8.14 0.02 1 26 298 7 THR C C 173.89 0.2 1 27 298 7 THR CA C 61.84 0.2 1 28 298 7 THR CB C 69.80 0.2 1 29 298 7 THR N N 115.65 0.2 1 30 299 8 PHE H H 8.26 0.02 1 31 299 8 PHE C C 175.17 0.2 1 32 299 8 PHE CA C 57.70 0.2 1 33 299 8 PHE CB C 39.59 0.2 1 34 299 8 PHE N N 122.57 0.2 1 35 300 9 ARG H H 8.16 0.02 1 36 300 9 ARG C C 175.33 0.2 1 37 300 9 ARG CA C 55.89 0.2 1 38 300 9 ARG CB C 30.98 0.2 1 39 300 9 ARG N N 122.96 0.2 1 40 301 10 LYS H H 8.26 0.02 1 41 301 10 LYS C C 175.95 0.2 1 42 301 10 LYS CA C 56.32 0.2 1 43 301 10 LYS CB C 33.05 0.2 1 44 301 10 LYS N N 123.28 0.2 1 45 302 11 ILE H H 8.23 0.02 1 46 302 11 ILE C C 175.80 0.2 1 47 302 11 ILE CA C 60.85 0.2 1 48 302 11 ILE CB C 38.61 0.2 1 49 302 11 ILE N N 123.59 0.2 1 50 303 12 ILE H H 8.34 0.02 1 51 303 12 ILE C C 175.94 0.2 1 52 303 12 ILE CA C 60.73 0.2 1 53 303 12 ILE CB C 38.43 0.2 1 54 303 12 ILE N N 126.64 0.2 1 55 304 13 ARG H H 8.47 0.02 1 56 304 13 ARG C C 175.90 0.2 1 57 304 13 ARG CA C 56.02 0.2 1 58 304 13 ARG CB C 30.88 0.2 1 59 304 13 ARG N N 126.21 0.2 1 60 305 14 SER H H 8.30 0.02 1 61 305 14 SER C C 174.19 0.2 1 62 305 14 SER CA C 58.24 0.2 1 63 305 14 SER CB C 63.68 0.2 1 64 305 14 SER N N 116.86 0.2 1 65 306 15 HIS C C 174.75 0.2 1 66 306 15 HIS CA C 56.13 0.2 1 67 306 15 HIS CB C 30.23 0.2 1 68 307 16 VAL H H 8.01 0.02 1 69 307 16 VAL C C 175.80 0.2 1 70 307 16 VAL CA C 62.61 0.2 1 71 307 16 VAL CB C 32.63 0.2 1 72 307 16 VAL N N 121.20 0.2 1 73 308 17 LEU H H 8.29 0.02 1 74 308 17 LEU C C 176.97 0.2 1 75 308 17 LEU CA C 55.15 0.2 1 76 308 17 LEU CB C 42.33 0.2 1 77 308 17 LEU N N 125.90 0.2 1 78 309 18 ARG H H 8.31 0.02 1 79 309 18 ARG C C 175.94 0.2 1 80 309 18 ARG CA C 56.16 0.2 1 81 309 18 ARG CB C 30.80 0.2 1 82 309 18 ARG N N 122.18 0.2 1 83 310 19 GLN H H 8.40 0.02 1 84 310 19 GLN C C 175.56 0.2 1 85 310 19 GLN CA C 56.08 0.2 1 86 310 19 GLN CB C 29.72 0.2 1 87 310 19 GLN N N 121.59 0.2 1 88 311 20 GLN H H 8.42 0.02 1 89 311 20 GLN C C 175.47 0.2 1 90 311 20 GLN CA C 55.73 0.2 1 91 311 20 GLN CB C 29.58 0.2 1 92 311 20 GLN N N 121.58 0.2 1 93 312 21 GLU H H 8.47 0.02 1 94 312 21 GLU C C 174.44 0.2 1 95 312 21 GLU CA C 54.58 0.2 1 96 312 21 GLU CB C 29.78 0.2 1 97 312 21 GLU N N 123.71 0.2 1 98 313 22 PRO C C 176.42 0.2 1 99 313 22 PRO CA C 63.24 0.2 1 100 313 22 PRO CB C 31.95 0.2 1 101 313 22 PRO N N 136.96 0.2 1 102 314 23 PHE H H 8.22 0.02 1 103 314 23 PHE C C 175.38 0.2 1 104 314 23 PHE CA C 57.82 0.2 1 105 314 23 PHE CB C 39.35 0.2 1 106 314 23 PHE N N 120.11 0.2 1 107 315 24 LYS H H 8.02 0.02 1 108 315 24 LYS C C 175.42 0.2 1 109 315 24 LYS CA C 55.83 0.2 1 110 315 24 LYS CB C 33.32 0.2 1 111 315 24 LYS N N 124.06 0.2 1 112 316 25 ALA H H 8.21 0.02 1 113 316 25 ALA C C 177.27 0.2 1 114 316 25 ALA CA C 52.42 0.2 1 115 316 25 ALA CB C 19.26 0.2 1 116 316 25 ALA N N 125.85 0.2 1 117 317 26 ALA H H 8.32 0.02 1 118 317 26 ALA C C 178.17 0.2 1 119 317 26 ALA CA C 52.61 0.2 1 120 317 26 ALA CB C 19.29 0.2 1 121 317 26 ALA N N 123.71 0.2 1 122 318 27 GLY H H 8.38 0.02 1 123 318 27 GLY C C 174.39 0.2 1 124 318 27 GLY CA C 45.44 0.2 1 125 318 27 GLY N N 108.15 0.2 1 126 319 28 THR H H 8.07 0.02 1 127 319 28 THR C C 174.67 0.2 1 128 319 28 THR CA C 61.99 0.2 1 129 319 28 THR CB C 69.79 0.2 1 130 319 28 THR N N 113.37 0.2 1 131 320 29 SER H H 8.36 0.02 1 132 320 29 SER C C 174.12 0.2 1 133 320 29 SER CA C 58.53 0.2 1 134 320 29 SER CB C 63.75 0.2 1 135 320 29 SER N N 118.16 0.2 1 136 321 30 ALA H H 8.31 0.02 1 137 321 30 ALA C C 177.60 0.2 1 138 321 30 ALA CA C 52.79 0.2 1 139 321 30 ALA CB C 19.22 0.2 1 140 321 30 ALA N N 125.84 0.2 1 141 322 31 ARG H H 8.21 0.02 1 142 322 31 ARG C C 176.21 0.2 1 143 322 31 ARG CA C 56.45 0.2 1 144 322 31 ARG CB C 30.78 0.2 1 145 322 31 ARG N N 120.13 0.2 1 146 323 32 VAL H H 8.11 0.02 1 147 323 32 VAL C C 176.02 0.2 1 148 323 32 VAL CA C 62.63 0.2 1 149 323 32 VAL CB C 32.61 0.2 1 150 323 32 VAL N N 121.88 0.2 1 151 324 33 LEU H H 8.29 0.02 1 152 324 33 LEU C C 176.86 0.2 1 153 324 33 LEU CA C 55.13 0.2 1 154 324 33 LEU CB C 42.34 0.2 1 155 324 33 LEU N N 126.01 0.2 1 156 325 34 ALA H H 8.18 0.02 1 157 325 34 ALA C C 177.13 0.2 1 158 325 34 ALA CA C 52.34 0.2 1 159 325 34 ALA CB C 19.27 0.2 1 160 325 34 ALA N N 124.67 0.2 1 161 326 35 ALA H H 8.19 0.02 1 162 326 35 ALA C C 177.41 0.2 1 163 326 35 ALA CA C 52.52 0.2 1 164 326 35 ALA CB C 19.23 0.2 1 165 326 35 ALA N N 123.11 0.2 1 166 327 36 HIS H H 8.35 0.02 1 167 327 36 HIS C C 175.28 0.2 1 168 327 36 HIS CA C 55.70 0.2 1 169 327 36 HIS CB C 29.87 0.2 1 170 327 36 HIS N N 117.85 0.2 1 171 328 37 GLY H H 8.42 0.02 1 172 328 37 GLY C C 174.18 0.2 1 173 328 37 GLY CA C 45.41 0.2 1 174 328 37 GLY N N 110.24 0.2 1 175 329 38 SER H H 8.38 0.02 1 176 329 38 SER C C 174.39 0.2 1 177 329 38 SER CA C 58.43 0.2 1 178 329 38 SER CB C 63.86 0.2 1 179 329 38 SER N N 115.93 0.2 1 180 330 39 ASP H H 8.49 0.02 1 181 330 39 ASP C C 176.64 0.2 1 182 330 39 ASP CA C 54.67 0.2 1 183 330 39 ASP CB C 41.06 0.2 1 184 330 39 ASP N N 122.21 0.2 1 185 331 40 GLY H H 8.33 0.02 1 186 331 40 GLY C C 174.25 0.2 1 187 331 40 GLY CA C 45.53 0.2 1 188 331 40 GLY N N 108.81 0.2 1 189 332 41 GLU H H 8.26 0.02 1 190 332 41 GLU C C 176.58 0.2 1 191 332 41 GLU CA C 56.71 0.2 1 192 332 41 GLU CB C 30.25 0.2 1 193 332 41 GLU N N 120.66 0.2 1 194 333 42 GLN H H 8.45 0.02 1 195 333 42 GLN C C 176.19 0.2 1 196 333 42 GLN CA C 56.17 0.2 1 197 333 42 GLN CB C 29.18 0.2 1 198 333 42 GLN N N 121.16 0.2 1 199 334 43 VAL H H 8.16 0.02 1 200 334 43 VAL C C 176.22 0.2 1 201 334 43 VAL CA C 62.90 0.2 1 202 334 43 VAL CB C 32.63 0.2 1 203 334 43 VAL N N 121.18 0.2 1 204 335 44 SER H H 8.33 0.02 1 205 335 44 SER C C 174.55 0.2 1 206 335 44 SER CA C 58.65 0.2 1 207 335 44 SER CB C 63.66 0.2 1 208 335 44 SER N N 118.54 0.2 1 209 336 45 LEU H H 8.18 0.02 1 210 336 45 LEU C C 177.20 0.2 1 211 336 45 LEU CA C 55.57 0.2 1 212 336 45 LEU CB C 42.36 0.2 1 213 336 45 LEU N N 124.07 0.2 1 214 337 46 ARG H H 8.18 0.02 1 215 337 46 ARG C C 176.21 0.2 1 216 337 46 ARG CA C 56.18 0.2 1 217 337 46 ARG CB C 30.47 0.2 1 218 337 46 ARG N N 121.05 0.2 1 219 338 47 LEU H H 8.22 0.02 1 220 338 47 LEU C C 177.06 0.2 1 221 338 47 LEU CA C 55.21 0.2 1 222 338 47 LEU CB C 42.22 0.2 1 223 338 47 LEU N N 122.72 0.2 1 224 339 48 ASN H H 8.39 0.02 1 225 339 48 ASN C C 175.36 0.2 1 226 339 48 ASN CA C 53.30 0.2 1 227 339 48 ASN CB C 38.90 0.2 1 228 339 48 ASN N N 118.82 0.2 1 229 340 49 GLY H H 8.27 0.02 1 230 340 49 GLY C C 173.30 0.2 1 231 340 49 GLY CA C 45.21 0.2 1 232 340 49 GLY N N 108.45 0.2 1 233 341 50 HIS H H 8.11 0.02 1 234 341 50 HIS C C 172.26 0.2 1 235 341 50 HIS CA C 53.60 0.2 1 236 341 50 HIS CB C 29.36 0.2 1 237 341 50 HIS N N 119.10 0.2 1 238 342 51 PRO N N 139.07 0.2 1 239 343 52 PRO C C 177.26 0.2 1 240 343 52 PRO CA C 63.26 0.2 1 241 343 52 PRO CB C 32.07 0.2 1 242 343 52 PRO N N 135.17 0.2 1 243 344 53 GLY H H 8.36 0.02 1 244 344 53 GLY C C 173.79 0.2 1 245 344 53 GLY CA C 45.22 0.2 1 246 344 53 GLY N N 108.88 0.2 1 247 345 54 VAL H H 7.77 0.02 1 248 345 54 VAL C C 175.58 0.2 1 249 345 54 VAL CA C 62.33 0.2 1 250 345 54 VAL CB C 32.64 0.2 1 251 345 54 VAL N N 118.96 0.2 1 252 346 55 TRP H H 8.21 0.02 1 253 346 55 TRP HE1 H 10.08 0.02 1 254 346 55 TRP C C 175.85 0.2 1 255 346 55 TRP CA C 56.75 0.2 1 256 346 55 TRP CB C 29.58 0.2 1 257 346 55 TRP N N 124.52 0.2 1 258 346 55 TRP NE1 N 129.24 0.2 1 259 347 56 ALA H H 8.15 0.02 1 260 347 56 ALA C C 177.12 0.2 1 261 347 56 ALA CA C 52.58 0.2 1 262 347 56 ALA CB C 19.28 0.2 1 263 347 56 ALA N N 125.85 0.2 1 264 348 57 ASN H H 8.22 0.02 1 265 348 57 ASN C C 175.67 0.2 1 266 348 57 ASN CA C 53.46 0.2 1 267 348 57 ASN CB C 38.66 0.2 1 268 348 57 ASN N N 117.53 0.2 1 269 349 58 GLY H H 8.33 0.02 1 270 349 58 GLY C C 173.99 0.2 1 271 349 58 GLY CA C 45.56 0.2 1 272 349 58 GLY N N 109.31 0.2 1 273 350 59 SER H H 8.09 0.02 1 274 350 59 SER C C 173.41 0.2 1 275 350 59 SER CA C 58.11 0.2 1 276 350 59 SER CB C 64.10 0.2 1 277 350 59 SER N N 115.45 0.2 1 278 351 60 ALA H H 8.15 0.02 1 279 351 60 ALA C C 175.17 0.2 1 280 351 60 ALA CA C 50.55 0.2 1 281 351 60 ALA CB C 18.25 0.2 1 282 351 60 ALA N N 126.63 0.2 1 283 352 61 PRO C C 176.20 0.2 1 284 352 61 PRO CA C 62.94 0.2 1 285 352 61 PRO CB C 32.05 0.2 1 286 352 61 PRO N N 135.17 0.2 1 287 353 62 HIS H H 8.38 0.02 1 288 353 62 HIS C C 172.93 0.2 1 289 353 62 HIS CA C 53.66 0.2 1 290 353 62 HIS CB C 29.31 0.2 1 291 353 62 HIS N N 119.12 0.2 1 292 354 63 PRO C C 176.75 0.2 1 293 354 63 PRO CA C 63.43 0.2 1 294 354 63 PRO CB C 31.95 0.2 1 295 354 63 PRO N N 137.46 0.2 1 296 355 64 GLU H H 8.89 0.02 1 297 355 64 GLU C C 176.17 0.2 1 298 355 64 GLU CA C 56.65 0.2 1 299 355 64 GLU CB C 29.99 0.2 1 300 355 64 GLU N N 121.35 0.2 1 301 356 65 ARG H H 8.30 0.02 1 302 356 65 ARG C C 175.69 0.2 1 303 356 65 ARG CA C 55.89 0.2 1 304 356 65 ARG CB C 30.83 0.2 1 305 356 65 ARG N N 122.33 0.2 1 306 357 66 ARG H H 8.37 0.02 1 307 357 66 ARG C C 174.17 0.2 1 308 357 66 ARG CA C 53.78 0.2 1 309 357 66 ARG CB C 30.34 0.2 1 310 357 66 ARG N N 123.58 0.2 1 311 358 67 PRO C C 176.55 0.2 1 312 358 67 PRO CA C 63.26 0.2 1 313 358 67 PRO CB C 31.99 0.2 1 314 358 67 PRO N N 137.08 0.2 1 315 359 68 ASN H H 8.52 0.02 1 316 359 68 ASN C C 175.65 0.2 1 317 359 68 ASN CA C 53.54 0.2 1 318 359 68 ASN CB C 38.81 0.2 1 319 359 68 ASN N N 118.55 0.2 1 320 360 69 GLY H H 8.36 0.02 1 321 360 69 GLY C C 173.93 0.2 1 322 360 69 GLY CA C 45.56 0.2 1 323 360 69 GLY N N 109.09 0.2 1 324 361 70 TYR H H 8.00 0.02 1 325 361 70 TYR C C 175.62 0.2 1 326 361 70 TYR CA C 58.20 0.2 1 327 361 70 TYR CB C 38.76 0.2 1 328 361 70 TYR N N 120.28 0.2 1 329 362 71 ALA H H 8.19 0.02 1 330 362 71 ALA C C 177.32 0.2 1 331 362 71 ALA CA C 52.59 0.2 1 332 362 71 ALA CB C 19.20 0.2 1 333 362 71 ALA N N 125.18 0.2 1 334 363 72 LEU H H 8.00 0.02 1 335 363 72 LEU C C 177.76 0.2 1 336 363 72 LEU CA C 55.53 0.2 1 337 363 72 LEU CB C 42.34 0.2 1 338 363 72 LEU N N 120.63 0.2 1 339 364 73 GLY H H 8.27 0.02 1 340 364 73 GLY C C 173.89 0.2 1 341 364 73 GLY CA C 45.43 0.2 1 342 364 73 GLY N N 108.90 0.2 1 343 365 74 LEU H H 7.97 0.02 1 344 365 74 LEU C C 177.34 0.2 1 345 365 74 LEU CA C 55.17 0.2 1 346 365 74 LEU CB C 42.43 0.2 1 347 365 74 LEU N N 121.38 0.2 1 348 366 75 VAL H H 8.12 0.02 1 349 366 75 VAL C C 176.07 0.2 1 350 366 75 VAL CA C 62.19 0.2 1 351 366 75 VAL CB C 32.80 0.2 1 352 366 75 VAL N N 120.62 0.2 1 353 367 76 SER H H 8.38 0.02 1 354 367 76 SER C C 174.89 0.2 1 355 367 76 SER CA C 58.19 0.2 1 356 367 76 SER CB C 63.70 0.2 1 357 367 76 SER N N 119.40 0.2 1 358 368 77 GLY H H 8.46 0.02 1 359 368 77 GLY C C 174.52 0.2 1 360 368 77 GLY CA C 45.48 0.2 1 361 368 77 GLY N N 111.19 0.2 1 362 369 78 GLY H H 8.30 0.02 1 363 369 78 GLY C C 174.07 0.2 1 364 369 78 GLY CA C 45.32 0.2 1 365 369 78 GLY N N 108.75 0.2 1 366 370 79 SER H H 8.28 0.02 1 367 370 79 SER C C 174.40 0.2 1 368 370 79 SER CA C 58.23 0.2 1 369 370 79 SER CB C 64.01 0.2 1 370 370 79 SER N N 115.74 0.2 1 371 371 80 ALA H H 8.45 0.02 1 372 371 80 ALA C C 177.72 0.2 1 373 371 80 ALA CA C 52.85 0.2 1 374 371 80 ALA CB C 19.06 0.2 1 375 371 80 ALA N N 125.96 0.2 1 376 372 81 GLN H H 8.31 0.02 1 377 372 81 GLN C C 176.12 0.2 1 378 372 81 GLN CA C 56.14 0.2 1 379 372 81 GLN CB C 29.39 0.2 1 380 372 81 GLN N N 119.01 0.2 1 381 373 82 GLU H H 8.40 0.02 1 382 373 82 GLU C C 176.53 0.2 1 383 373 82 GLU CA C 56.85 0.2 1 384 373 82 GLU CB C 30.27 0.2 1 385 373 82 GLU N N 121.76 0.2 1 386 374 83 SER H H 8.33 0.02 1 387 374 83 SER C C 174.54 0.2 1 388 374 83 SER CA C 58.48 0.2 1 389 374 83 SER CB C 63.74 0.2 1 390 374 83 SER N N 116.47 0.2 1 391 375 84 GLN H H 8.43 0.02 1 392 375 84 GLN C C 176.30 0.2 1 393 375 84 GLN CA C 56.10 0.2 1 394 375 84 GLN CB C 29.39 0.2 1 395 375 84 GLN N N 122.06 0.2 1 396 376 85 GLY H H 8.40 0.02 1 397 376 85 GLY C C 173.75 0.2 1 398 376 85 GLY CA C 45.44 0.2 1 399 376 85 GLY N N 109.47 0.2 1 400 377 86 ASN H H 8.38 0.02 1 401 377 86 ASN C C 175.51 0.2 1 402 377 86 ASN CA C 53.19 0.2 1 403 377 86 ASN CB C 38.95 0.2 1 404 377 86 ASN N N 118.88 0.2 1 405 378 87 THR H H 8.23 0.02 1 406 378 87 THR C C 174.97 0.2 1 407 378 87 THR CA C 62.14 0.2 1 408 378 87 THR CB C 69.75 0.2 1 409 378 87 THR N N 113.76 0.2 1 410 379 88 GLY H H 8.43 0.02 1 411 379 88 GLY C C 173.52 0.2 1 412 379 88 GLY CA C 45.09 0.2 1 413 379 88 GLY N N 111.02 0.2 1 414 380 89 LEU H H 8.08 0.02 1 415 380 89 LEU C C 175.17 0.2 1 416 380 89 LEU CA C 53.07 0.2 1 417 380 89 LEU CB C 41.68 0.2 1 418 380 89 LEU N N 122.93 0.2 1 419 381 90 PRO C C 176.40 0.2 1 420 381 90 PRO CA C 63.13 0.2 1 421 381 90 PRO CB C 32.05 0.2 1 422 381 90 PRO N N 136.05 0.2 1 423 382 91 ASP H H 8.38 0.02 1 424 382 91 ASP C C 176.43 0.2 1 425 382 91 ASP CA C 54.56 0.2 1 426 382 91 ASP CB C 41.01 0.2 1 427 382 91 ASP N N 120.57 0.2 1 428 383 92 VAL H H 8.03 0.02 1 429 383 92 VAL C C 176.27 0.2 1 430 383 92 VAL CA C 62.74 0.2 1 431 383 92 VAL CB C 32.62 0.2 1 432 383 92 VAL N N 119.67 0.2 1 433 384 93 GLU H H 8.41 0.02 1 434 384 93 GLU C C 176.57 0.2 1 435 384 93 GLU CA C 57.02 0.2 1 436 384 93 GLU CB C 29.99 0.2 1 437 384 93 GLU N N 123.55 0.2 1 438 385 94 LEU H H 8.12 0.02 1 439 385 94 LEU C C 177.43 0.2 1 440 385 94 LEU CA C 55.58 0.2 1 441 385 94 LEU CB C 42.16 0.2 1 442 385 94 LEU N N 122.75 0.2 1 443 386 95 LEU H H 8.13 0.02 1 444 386 95 LEU C C 177.40 0.2 1 445 386 95 LEU CA C 55.32 0.2 1 446 386 95 LEU CB C 42.19 0.2 1 447 386 95 LEU N N 121.85 0.2 1 448 387 96 SER H H 8.14 0.02 1 449 387 96 SER C C 174.64 0.2 1 450 387 96 SER CA C 58.66 0.2 1 451 387 96 SER CB C 63.67 0.2 1 452 387 96 SER N N 115.58 0.2 1 453 388 97 HIS H H 8.34 0.02 1 454 388 97 HIS C C 174.77 0.2 1 455 388 97 HIS CA C 56.14 0.2 1 456 388 97 HIS CB C 29.70 0.2 1 457 388 97 HIS N N 120.58 0.2 1 458 389 98 GLU H H 8.32 0.02 1 459 389 98 GLU C C 176.27 0.2 1 460 389 98 GLU CA C 56.79 0.2 1 461 389 98 GLU CB C 30.22 0.2 1 462 389 98 GLU N N 121.21 0.2 1 463 390 99 LEU H H 8.25 0.02 1 464 390 99 LEU C C 177.12 0.2 1 465 390 99 LEU CA C 55.22 0.2 1 466 390 99 LEU CB C 42.13 0.2 1 467 390 99 LEU N N 123.10 0.2 1 468 391 100 LYS H H 8.25 0.02 1 469 391 100 LYS C C 176.85 0.2 1 470 391 100 LYS CA C 56.36 0.2 1 471 391 100 LYS CB C 32.96 0.2 1 472 391 100 LYS N N 122.11 0.2 1 473 392 101 GLY H H 8.37 0.02 1 474 392 101 GLY C C 173.74 0.2 1 475 392 101 GLY CA C 45.21 0.2 1 476 392 101 GLY N N 109.99 0.2 1 477 393 102 VAL H H 7.96 0.02 1 478 393 102 VAL C C 175.80 0.2 1 479 393 102 VAL CA C 62.15 0.2 1 480 393 102 VAL CB C 32.83 0.2 1 481 393 102 VAL N N 119.05 0.2 1 482 394 103 CYS H H 8.51 0.02 1 483 394 103 CYS C C 172.48 0.2 1 484 394 103 CYS CA C 56.52 0.2 1 485 394 103 CYS CB C 27.47 0.2 1 486 394 103 CYS N N 124.90 0.2 1 487 395 104 PRO CA C 63.52 0.2 1 488 395 104 PRO CB C 32.11 0.2 1 489 395 104 PRO N N 138.65 0.2 1 490 398 107 PRO C C 177.31 0.2 1 491 398 107 PRO CA C 63.10 0.2 1 492 398 107 PRO CB C 32.08 0.2 1 493 398 107 PRO N N 135.13 0.2 1 494 399 108 GLY H H 8.44 0.02 1 495 399 108 GLY C C 174.03 0.2 1 496 399 108 GLY CA C 45.15 0.2 1 497 399 108 GLY N N 108.86 0.2 1 498 400 109 LEU H H 8.15 0.02 1 499 400 109 LEU C C 176.95 0.2 1 500 400 109 LEU CA C 55.20 0.2 1 501 400 109 LEU CB C 42.47 0.2 1 502 400 109 LEU N N 121.63 0.2 1 503 401 110 ASP H H 8.37 0.02 1 504 401 110 ASP C C 175.30 0.2 1 505 401 110 ASP CA C 54.16 0.2 1 506 401 110 ASP CB C 41.09 0.2 1 507 401 110 ASP N N 120.45 0.2 1 508 402 111 ASP H H 8.09 0.02 1 509 402 111 ASP C C 174.92 0.2 1 510 402 111 ASP CA C 52.05 0.2 1 511 402 111 ASP CB C 41.42 0.2 1 512 402 111 ASP N N 121.51 0.2 1 513 403 112 PRO C C 177.23 0.2 1 514 403 112 PRO CA C 63.76 0.2 1 515 403 112 PRO CB C 32.21 0.2 1 516 403 112 PRO N N 137.91 0.2 1 517 404 113 LEU H H 8.30 0.02 1 518 404 113 LEU C C 177.36 0.2 1 519 404 113 LEU CA C 55.08 0.2 1 520 404 113 LEU CB C 41.52 0.2 1 521 404 113 LEU N N 119.57 0.2 1 522 405 114 ALA H H 7.87 0.02 1 523 405 114 ALA C C 177.68 0.2 1 524 405 114 ALA CA C 52.63 0.2 1 525 405 114 ALA CB C 19.18 0.2 1 526 405 114 ALA N N 123.73 0.2 1 527 406 115 GLN H H 8.21 0.02 1 528 406 115 GLN C C 175.72 0.2 1 529 406 115 GLN CA C 55.76 0.2 1 530 406 115 GLN CB C 29.45 0.2 1 531 406 115 GLN N N 118.99 0.2 1 532 407 116 ASP H H 8.36 0.02 1 533 407 116 ASP C C 176.68 0.2 1 534 407 116 ASP CA C 54.58 0.2 1 535 407 116 ASP CB C 41.20 0.2 1 536 407 116 ASP N N 121.18 0.2 1 537 408 117 GLY H H 8.34 0.02 1 538 408 117 GLY C C 174.04 0.2 1 539 408 117 GLY CA C 45.55 0.2 1 540 408 117 GLY N N 109.51 0.2 1 541 409 118 ALA H H 8.18 0.02 1 542 409 118 ALA C C 178.19 0.2 1 543 409 118 ALA CA C 52.68 0.2 1 544 409 118 ALA CB C 19.29 0.2 1 545 409 118 ALA N N 123.46 0.2 1 546 410 119 GLY H H 8.39 0.02 1 547 410 119 GLY C C 174.24 0.2 1 548 410 119 GLY CA C 45.44 0.2 1 549 410 119 GLY N N 107.95 0.2 1 550 411 120 VAL H H 7.99 0.02 1 551 411 120 VAL C C 176.35 0.2 1 552 411 120 VAL CA C 62.27 0.2 1 553 411 120 VAL CB C 32.65 0.2 1 554 411 120 VAL N N 118.85 0.2 1 555 412 121 SER H H 8.48 0.02 1 556 412 121 SER C C 175.04 0.2 1 557 412 121 SER CA C 58.67 0.2 1 558 412 121 SER CB C 63.77 0.2 1 559 412 121 SER N N 119.12 0.2 1 560 413 122 GLY H H 8.46 0.02 1 561 413 122 GLY C C 174.16 0.2 1 562 413 122 GLY CA C 45.53 0.2 1 563 413 122 GLY N N 111.06 0.2 1 564 414 123 LEU H H 8.05 0.02 1 565 414 123 LEU C C 177.41 0.2 1 566 414 123 LEU CA C 55.30 0.2 1 567 414 123 LEU CB C 42.37 0.2 1 568 414 123 LEU N N 121.19 0.2 1 569 415 124 GLU H H 8.43 0.02 1 570 415 124 GLU C C 176.22 0.2 1 571 415 124 GLU CA C 56.85 0.2 1 572 415 124 GLU CB C 29.91 0.2 1 573 415 124 GLU N N 120.67 0.2 1 574 416 125 HIS H H 8.28 0.02 1 575 416 125 HIS CA C 55.95 0.2 1 576 416 125 HIS CB C 29.86 0.2 1 577 416 125 HIS N N 119.27 0.2 1 stop_ save_