data_26786 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Elk1 C-terminus aa309-429 - 8 phosphorylated sites (pS337-pT354-pT364-pT369-pS384-pS390-pT418-pS423) ; _BMRB_accession_number 26786 _BMRB_flat_file_name bmr26786.str _Entry_type original _Submission_date 2016-04-25 _Accession_date 2016-04-25 _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 Theillet Francois X. . 2 Selenko Philipp . . 3 Mylona Anastasia . . 4 Treisman Richard . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 94 "13C chemical shifts" 318 "15N chemical shifts" 94 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-08-24 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 26762 'Elk1 C-terminus aa309-429 non-phosphorylated' stop_ _Original_release_date 2016-04-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Opposing effects of Elk-1 multisite phosphorylation shape its response to ERK activation ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27738173 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mylona Anastasia . . 2 Theillet Francois-Xavier X. . 3 Foster Charles . . 4 Cheng Tammy M. . 5 Miralles Francesc . . 6 Bates Paul A. . 7 Selenko Philipp . . 8 Treisman Richard . . stop_ _Journal_abbreviation Science _Journal_name_full 'Science (New York, N.Y.)' _Journal_volume 354 _Journal_issue 6309 _Journal_ISSN 1095-9203 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 233 _Page_last 237 _Year 2016 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name pElk1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label pElk1 $pElk1 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_pElk1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common pElk1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 122 _Mol_residue_sequence ; GTQPQKGRKPRDLELPLSPS LLGGQGPERXPGSGTSSGLQ APGPALXPSLLPTHTLXPVL LXPSSLPPSIHFWSTLXPIA PRXPAKLSFQFPSSGSAQVH IPSISVDGLSXPVVLXPGPQ KP ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 308 GLY 2 309 THR 3 310 GLN 4 311 PRO 5 312 GLN 6 313 LYS 7 314 GLY 8 315 ARG 9 316 LYS 10 317 PRO 11 318 ARG 12 319 ASP 13 320 LEU 14 321 GLU 15 322 LEU 16 323 PRO 17 324 LEU 18 325 SER 19 326 PRO 20 327 SER 21 328 LEU 22 329 LEU 23 330 GLY 24 331 GLY 25 332 GLN 26 333 GLY 27 334 PRO 28 335 GLU 29 336 ARG 30 337 SEP 31 338 PRO 32 339 GLY 33 340 SER 34 341 GLY 35 342 THR 36 343 SER 37 344 SER 38 345 GLY 39 346 LEU 40 347 GLN 41 348 ALA 42 349 PRO 43 350 GLY 44 351 PRO 45 352 ALA 46 353 LEU 47 354 TPO 48 355 PRO 49 356 SER 50 357 LEU 51 358 LEU 52 359 PRO 53 360 THR 54 361 HIS 55 362 THR 56 363 LEU 57 364 TPO 58 365 PRO 59 366 VAL 60 367 LEU 61 368 LEU 62 369 TPO 63 370 PRO 64 371 SER 65 372 SER 66 373 LEU 67 374 PRO 68 375 PRO 69 376 SER 70 377 ILE 71 378 HIS 72 379 PHE 73 380 TRP 74 381 SER 75 382 THR 76 383 LEU 77 384 SEP 78 385 PRO 79 386 ILE 80 387 ALA 81 388 PRO 82 389 ARG 83 390 SEP 84 391 PRO 85 392 ALA 86 393 LYS 87 394 LEU 88 395 SER 89 396 PHE 90 397 GLN 91 398 PHE 92 399 PRO 93 400 SER 94 401 SER 95 402 GLY 96 403 SER 97 404 ALA 98 405 GLN 99 406 VAL 100 407 HIS 101 408 ILE 102 409 PRO 103 410 SER 104 411 ILE 105 412 SER 106 413 VAL 107 414 ASP 108 415 GLY 109 416 LEU 110 417 SER 111 418 TPO 112 419 PRO 113 420 VAL 114 421 VAL 115 422 LEU 116 423 SEP 117 424 PRO 118 425 GLY 119 426 PRO 120 427 GLN 121 428 LYS 122 429 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_SEP _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common PHOSPHOSERINE _BMRB_code SEP _PDB_code SEP _Standard_residue_derivative . _Molecular_mass 185.072 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? OG OG O . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HXT HXT H . 0 . ? HOP2 HOP2 H . 0 . ? HOP3 HOP3 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N H2 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB OG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING OG P ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HOP2 ? ? SING O3P HOP3 ? ? stop_ save_ save_chem_comp_TPO _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common PHOSPHOTHREONINE _BMRB_code TPO _PDB_code TPO _Standard_residue_derivative . _Molecular_mass 199.099 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG2 CG2 C . 0 . ? OG1 OG1 O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB HB H . 0 . ? HG21 HG21 H . 0 . ? HG22 HG22 H . 0 . ? HG23 HG23 H . 0 . ? HOP2 HOP2 H . 0 . ? HOP3 HOP3 H . 0 . ? HXT HXT H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H ? ? SING N H2 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB CG2 ? ? SING CB OG1 ? ? SING CB HB ? ? SING CG2 HG21 ? ? SING CG2 HG22 ? ? SING CG2 HG23 ? ? SING OG1 P ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HOP2 ? ? SING O3P HOP3 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $pElk1 Mouse 10090 Eukaryota Metazoa Mus musculus 'Sequence numbering is shifted (+1) according to human Elk1, to be consistent with the related paper.' 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 $pElk1 'recombinant technology' . Escherichia coli . pET-29 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_pElk1 _Saveframe_category sample _Sample_type solution _Details 'phosphate: 10 mM (at pH6.9: (HPO4)2- ~2.5mM and (PO4)3- ~ 7.5 mM' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $pElk1 300 uM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 10 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' ATP 5 mM 'natural abundance' DSS 0.5 mM 'natural abundance' 'magnesium chloride' 5 mM 'natural abundance' 'Erk2 kinase' 0.05 ug 'natural abundance' DTT 2 mM 'natural abundance' glycerol 1 '% v/v' 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_CcpNMR_Analysis _Saveframe_category software _Name CcpNMR_Analysis _Version 2.4 loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _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_pElk1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_pElk1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_pElk1 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' 60 . mM pH 6.9 . pH pressure 1 . atm temperature 277 . 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 '13C chemical shift error: CACB:0.2; C:0.03' loop_ _Software_label $CcpNMR_Analysis stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCACB' stop_ loop_ _Sample_label $sample_pElk1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name pElk1 _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 1 309 2 THR C C 174.645 0.03 1 2 309 2 THR CA C 61.985 0.2 1 3 309 2 THR CB C 69.895 0.2 1 4 310 3 GLN H H 8.735 0.003 1 5 310 3 GLN CA C 53.785 0.2 1 6 310 3 GLN CB C 28.805 0.2 1 7 310 3 GLN N N 124.565 0.03 1 8 311 4 PRO C C 176.845 0.03 1 9 311 4 PRO CA C 62.995 0.2 1 10 311 4 PRO CB C 32.205 0.2 1 11 312 5 GLN H H 8.715 0.003 1 12 312 5 GLN C C 176.155 0.03 1 13 312 5 GLN CA C 55.705 0.2 1 14 312 5 GLN CB C 29.615 0.2 1 15 312 5 GLN N N 121.485 0.03 1 16 313 6 LYS H H 8.615 0.003 1 17 313 6 LYS C C 177.135 0.03 1 18 313 6 LYS CA C 56.535 0.2 1 19 313 6 LYS CB C 33.055 0.2 1 20 313 6 LYS N N 123.605 0.03 1 21 314 7 GLY H H 8.645 0.003 1 22 314 7 GLY C C 173.835 0.03 1 23 314 7 GLY CA C 45.135 0.2 1 24 314 7 GLY N N 110.795 0.03 1 25 315 8 ARG H H 8.315 0.003 1 26 315 8 ARG C C 176.285 0.03 1 27 315 8 ARG CA C 55.825 0.2 1 28 315 8 ARG CB C 31.045 0.2 1 29 315 8 ARG N N 120.805 0.03 1 30 316 9 LYS H H 8.685 0.003 1 31 316 9 LYS CA C 54.365 0.2 1 32 316 9 LYS CB C 32.465 0.2 1 33 316 9 LYS N N 125.195 0.03 1 34 317 10 PRO C C 177.025 0.03 1 35 317 10 PRO CA C 63.415 0.2 1 36 317 10 PRO CB C 32.315 0.2 1 37 318 11 ARG H H 8.575 0.003 1 38 318 11 ARG C C 176.295 0.03 1 39 318 11 ARG CA C 56.365 0.2 1 40 318 11 ARG CB C 30.675 0.2 1 41 318 11 ARG N N 121.045 0.03 1 42 319 12 ASP H H 8.435 0.003 1 43 319 12 ASP C C 176.335 0.03 1 44 319 12 ASP CA C 54.665 0.2 1 45 319 12 ASP CB C 41.025 0.2 1 46 319 12 ASP N N 121.575 0.03 1 47 320 13 LEU H H 8.295 0.003 1 48 320 13 LEU C C 177.315 0.03 1 49 320 13 LEU CA C 55.275 0.2 1 50 320 13 LEU CB C 42.265 0.2 1 51 320 13 LEU N N 122.135 0.03 1 52 321 14 GLU H H 8.395 0.003 1 53 321 14 GLU C C 176.165 0.03 1 54 321 14 GLU CA C 56.115 0.2 1 55 321 14 GLU CB C 30.175 0.2 1 56 321 14 GLU N N 121.505 0.03 1 57 322 15 LEU H H 8.325 0.003 1 58 322 15 LEU CA C 52.955 0.2 1 59 322 15 LEU CB C 41.645 0.2 1 60 322 15 LEU N N 124.915 0.03 1 61 323 16 PRO C C 176.785 0.03 1 62 323 16 PRO CA C 62.735 0.2 1 63 323 16 PRO CB C 32.335 0.2 1 64 324 17 LEU H H 8.505 0.003 1 65 324 17 LEU C C 177.435 0.03 1 66 324 17 LEU CA C 55.335 0.2 1 67 324 17 LEU CB C 42.535 0.2 1 68 324 17 LEU N N 122.685 0.03 1 69 325 18 SER H H 8.435 0.003 1 70 325 18 SER CA C 56.085 0.2 1 71 325 18 SER CB C 63.485 0.2 1 72 325 18 SER N N 118.335 0.03 1 73 326 19 PRO C C 177.215 0.03 1 74 326 19 PRO CB C 32.155 0.2 1 75 327 20 SER H H 8.455 0.003 1 76 327 20 SER C C 174.985 0.03 1 77 327 20 SER CA C 58.555 0.2 1 78 327 20 SER CB C 63.605 0.2 1 79 327 20 SER N N 115.665 0.03 1 80 328 21 LEU H H 8.395 0.003 1 81 328 21 LEU C C 177.675 0.03 1 82 328 21 LEU CA C 55.305 0.2 1 83 328 21 LEU CB C 42.105 0.2 1 84 328 21 LEU N N 124.565 0.03 1 85 329 22 LEU H H 8.265 0.003 1 86 329 22 LEU C C 178.075 0.03 1 87 329 22 LEU CA C 55.295 0.2 1 88 329 22 LEU CB C 42.055 0.2 1 89 329 22 LEU N N 122.215 0.03 1 90 330 23 GLY H H 8.485 0.003 1 91 330 23 GLY C C 174.915 0.03 1 92 330 23 GLY CA C 45.455 0.2 1 93 330 23 GLY N N 109.625 0.03 1 94 331 24 GLY H H 8.395 0.003 1 95 331 24 GLY C C 174.255 0.03 1 96 331 24 GLY CA C 45.325 0.2 1 97 331 24 GLY N N 108.805 0.03 1 98 332 25 GLN H H 8.445 0.003 1 99 332 25 GLN C C 176.275 0.03 1 100 332 25 GLN CA C 55.635 0.2 1 101 332 25 GLN CB C 29.805 0.2 1 102 332 25 GLN N N 119.615 0.03 1 103 333 26 GLY H H 8.515 0.003 1 104 333 26 GLY CA C 44.615 0.2 1 105 333 26 GLY N N 110.625 0.03 1 106 334 27 PRO C C 177.155 0.03 1 107 334 27 PRO CA C 63.215 0.2 1 108 334 27 PRO CB C 32.185 0.2 1 109 335 28 GLU H H 8.725 0.003 1 110 335 28 GLU C C 176.835 0.03 1 111 335 28 GLU CA C 56.755 0.2 1 112 335 28 GLU CB C 30.055 0.2 1 113 335 28 GLU N N 121.235 0.03 1 114 336 29 ARG H H 8.505 0.003 1 115 336 29 ARG C C 176.045 0.03 1 116 336 29 ARG CA C 55.515 0.2 1 117 336 29 ARG CB C 31.245 0.2 1 118 336 29 ARG N N 122.675 0.03 1 119 337 30 SEP H H 9.275 0.003 1 120 337 30 SEP CA C 60.875 0.2 1 121 337 30 SEP CB C 72.065 0.2 1 122 337 30 SEP N N 120.915 0.03 1 123 338 31 PRO C C 177.825 0.03 1 124 338 31 PRO CA C 64.415 0.2 1 125 338 31 PRO CB C 32.265 0.2 1 126 339 32 GLY H H 9.125 0.003 1 127 339 32 GLY C C 174.845 0.03 1 128 339 32 GLY CA C 45.505 0.2 1 129 339 32 GLY N N 110.525 0.03 1 130 340 33 SER H H 8.385 0.003 1 131 340 33 SER C C 175.465 0.03 1 132 340 33 SER CA C 58.875 0.2 1 133 340 33 SER CB C 63.935 0.2 1 134 340 33 SER N N 115.895 0.03 1 135 341 34 GLY H H 8.705 0.003 1 136 341 34 GLY C C 174.585 0.03 1 137 341 34 GLY CA C 45.385 0.2 1 138 341 34 GLY N N 111.295 0.03 1 139 342 35 THR H H 8.245 0.003 1 140 342 35 THR C C 175.015 0.03 1 141 342 35 THR CA C 61.785 0.2 1 142 342 35 THR CB C 69.975 0.2 1 143 342 35 THR N N 113.695 0.03 1 144 343 36 SER H H 8.585 0.003 1 145 343 36 SER C C 174.845 0.03 1 146 343 36 SER CA C 58.495 0.2 1 147 343 36 SER CB C 63.805 0.2 1 148 343 36 SER N N 118.475 0.03 1 149 344 37 SER H H 8.545 0.003 1 150 344 37 SER C C 175.115 0.03 1 151 344 37 SER CA C 58.745 0.2 1 152 344 37 SER CB C 63.875 0.2 1 153 344 37 SER N N 118.175 0.03 1 154 345 38 GLY H H 8.495 0.003 1 155 345 38 GLY C C 174.065 0.03 1 156 345 38 GLY CA C 45.265 0.2 1 157 345 38 GLY N N 110.855 0.03 1 158 346 39 LEU H H 8.185 0.003 1 159 346 39 LEU C C 177.445 0.03 1 160 346 39 LEU CA C 55.045 0.2 1 161 346 39 LEU CB C 42.445 0.2 1 162 346 39 LEU N N 121.695 0.03 1 163 347 40 GLN H H 8.525 0.003 1 164 347 40 GLN C C 175.315 0.03 1 165 347 40 GLN CA C 55.105 0.2 1 166 347 40 GLN CB C 29.575 0.2 1 167 347 40 GLN N N 121.935 0.03 1 168 348 41 ALA H H 8.535 0.003 1 169 348 41 ALA CA C 50.575 0.2 1 170 348 41 ALA CB C 18.005 0.2 1 171 348 41 ALA N N 127.675 0.03 1 172 349 42 PRO C C 177.255 0.03 1 173 349 42 PRO CA C 63.215 0.2 1 174 349 42 PRO CB C 32.365 0.2 1 175 350 43 GLY H H 8.425 0.003 1 176 350 43 GLY CA C 44.385 0.2 1 177 350 43 GLY N N 109.485 0.03 1 178 351 44 PRO C C 176.535 0.03 1 179 351 44 PRO CA C 62.885 0.2 1 180 351 44 PRO CB C 32.285 0.2 1 181 352 45 ALA H H 8.555 0.003 1 182 352 45 ALA C C 177.605 0.03 1 183 352 45 ALA CA C 52.135 0.2 1 184 352 45 ALA CB C 19.085 0.2 1 185 352 45 ALA N N 124.735 0.03 1 186 353 46 LEU H H 8.425 0.003 1 187 353 46 LEU C C 177.285 0.03 1 188 353 46 LEU CA C 54.655 0.2 1 189 353 46 LEU CB C 42.695 0.2 1 190 353 46 LEU N N 122.845 0.03 1 191 354 47 TPO H H 8.965 0.003 1 192 354 47 TPO CA C 60.285 0.2 1 193 354 47 TPO CB C 72.295 0.2 1 194 354 47 TPO N N 121.405 0.03 1 195 355 48 PRO C C 177.235 0.03 1 196 355 48 PRO CA C 62.635 0.2 1 197 355 48 PRO CB C 32.335 0.2 1 198 356 49 SER H H 8.375 0.003 1 199 356 49 SER C C 174.735 0.03 1 200 356 49 SER CA C 59.135 0.2 1 201 356 49 SER CB C 63.435 0.2 1 202 356 49 SER N N 115.445 0.03 1 203 357 50 LEU H H 8.385 0.003 1 204 357 50 LEU C C 177.135 0.03 1 205 357 50 LEU CA C 54.785 0.2 1 206 357 50 LEU CB C 42.385 0.2 1 207 357 50 LEU N N 124.135 0.03 1 208 358 51 LEU H H 8.245 0.003 1 209 358 51 LEU CA C 53.035 0.2 1 210 358 51 LEU CB C 41.635 0.2 1 211 358 51 LEU N N 124.385 0.03 1 212 359 52 PRO C C 177.135 0.03 1 213 359 52 PRO CA C 63.075 0.2 1 214 359 52 PRO CB C 32.225 0.2 1 215 360 53 THR H H 8.410 0.003 1 216 360 53 THR CA C 61.935 0.2 1 217 360 53 THR CB C 70.025 0.2 1 218 360 53 THR N N 114.965 0.03 1 219 362 55 THR C C 173.785 0.03 1 220 362 55 THR CA C 61.925 0.2 1 221 362 55 THR CB C 69.715 0.2 1 222 363 56 LEU H H 8.445 0.003 1 223 363 56 LEU C C 177.105 0.03 1 224 363 56 LEU CA C 55.335 0.2 1 225 363 56 LEU CB C 42.455 0.2 1 226 363 56 LEU N N 125.675 0.03 1 227 364 57 TPO H H 9.595 0.003 1 228 364 57 TPO CA C 61.395 0.2 1 229 364 57 TPO CB C 72.715 0.2 1 230 364 57 TPO N N 125.605 0.03 1 231 365 58 PRO C C 176.535 0.03 1 232 365 58 PRO CA C 63.185 0.2 1 233 365 58 PRO CB C 32.335 0.2 1 234 366 59 VAL H H 8.415 0.003 1 235 366 59 VAL C C 176.035 0.03 1 236 366 59 VAL CA C 62.235 0.2 1 237 366 59 VAL CB C 32.885 0.2 1 238 366 59 VAL N N 122.485 0.03 1 239 367 60 LEU H H 8.555 0.003 1 240 367 60 LEU C C 176.735 0.03 1 241 367 60 LEU CA C 54.735 0.2 1 242 367 60 LEU CB C 42.335 0.2 1 243 367 60 LEU N N 127.935 0.03 1 244 368 61 LEU H H 8.385 0.003 1 245 368 61 LEU C C 176.925 0.03 1 246 368 61 LEU CA C 54.415 0.2 1 247 368 61 LEU CB C 42.675 0.2 1 248 368 61 LEU N N 124.935 0.03 1 249 369 62 TPO H H 8.725 0.003 1 250 369 62 TPO CA C 60.025 0.2 1 251 369 62 TPO CB C 71.305 0.2 1 252 369 62 TPO N N 118.785 0.03 1 253 370 63 PRO C C 177.955 0.03 1 254 370 63 PRO CA C 64.695 0.2 1 255 370 63 PRO CB C 32.485 0.2 1 256 371 64 SER H H 9.275 0.003 1 257 371 64 SER C C 175.235 0.03 1 258 371 64 SER CA C 59.805 0.2 1 259 371 64 SER CB C 63.215 0.2 1 260 371 64 SER N N 116.735 0.03 1 261 372 65 SER H H 8.285 0.003 1 262 372 65 SER C C 173.905 0.03 1 263 372 65 SER CA C 58.685 0.2 1 264 372 65 SER CB C 64.235 0.2 1 265 372 65 SER N N 117.985 0.03 1 266 373 66 LEU H H 7.975 0.003 1 267 373 66 LEU CA C 53.135 0.2 1 268 373 66 LEU CB C 41.635 0.2 1 269 373 66 LEU N N 124.725 0.03 1 270 375 68 PRO C C 176.925 0.03 1 271 375 68 PRO CA C 62.875 0.2 1 272 375 68 PRO CB C 32.145 0.2 1 273 376 69 SER H H 8.485 0.003 1 274 376 69 SER C C 174.625 0.03 1 275 376 69 SER CA C 58.125 0.2 1 276 376 69 SER CB C 63.855 0.2 1 277 376 69 SER N N 116.265 0.03 1 278 377 70 ILE H H 8.195 0.003 1 279 377 70 ILE C C 175.785 0.03 1 280 377 70 ILE CA C 61.155 0.2 1 281 377 70 ILE CB C 38.675 0.2 1 282 377 70 ILE N N 122.375 0.03 1 283 378 71 HIS H H 8.370 0.003 1 284 378 71 HIS CA C 55.385 0.2 1 285 378 71 HIS CB C 30.185 0.2 1 286 378 71 HIS N N 123.055 0.03 1 287 379 72 PHE C C 175.195 0.03 1 288 379 72 PHE CA C 58.035 0.2 1 289 379 72 PHE CB C 39.625 0.2 1 290 380 73 TRP H H 8.065 0.003 1 291 380 73 TRP C C 175.875 0.03 1 292 380 73 TRP CA C 57.155 0.2 1 293 380 73 TRP CB C 29.715 0.2 1 294 380 73 TRP N N 122.445 0.03 1 295 381 74 SER H H 8.135 0.003 1 296 381 74 SER C C 174.435 0.03 1 297 381 74 SER CA C 58.095 0.2 1 298 381 74 SER CB C 64.025 0.2 1 299 381 74 SER N N 117.435 0.03 1 300 382 75 THR H H 8.225 0.003 1 301 382 75 THR C C 174.345 0.03 1 302 382 75 THR CA C 61.845 0.2 1 303 382 75 THR CB C 69.685 0.2 1 304 382 75 THR N N 115.945 0.03 1 305 383 76 LEU H H 8.275 0.003 1 306 383 76 LEU C C 177.325 0.03 1 307 383 76 LEU CA C 54.755 0.2 1 308 383 76 LEU CB C 42.425 0.2 1 309 383 76 LEU N N 124.155 0.03 1 310 384 77 SEP H H 8.735 0.003 1 311 384 77 SEP CA C 56.325 0.2 1 312 384 77 SEP CB C 64.565 0.2 1 313 384 77 SEP N N 120.455 0.03 1 314 385 78 PRO C C 176.735 0.03 1 315 385 78 PRO CA C 63.205 0.2 1 316 385 78 PRO CB C 32.265 0.2 1 317 386 79 ILE H H 8.385 0.003 1 318 386 79 ILE C C 175.935 0.03 1 319 386 79 ILE CA C 60.825 0.2 1 320 386 79 ILE CB C 38.665 0.2 1 321 386 79 ILE N N 121.935 0.03 1 322 387 80 ALA H H 8.535 0.003 1 323 387 80 ALA CA C 50.435 0.2 1 324 387 80 ALA CB C 18.065 0.2 1 325 387 80 ALA N N 130.605 0.03 1 326 388 81 PRO C C 176.835 0.03 1 327 388 81 PRO CA C 62.685 0.2 1 328 388 81 PRO CB C 32.425 0.2 1 329 389 82 ARG H H 8.545 0.003 1 330 389 82 ARG C C 176.265 0.03 1 331 389 82 ARG CA C 55.635 0.2 1 332 389 82 ARG CB C 31.235 0.2 1 333 389 82 ARG N N 122.125 0.03 1 334 390 83 SEP H H 9.005 0.003 1 335 390 83 SEP CA C 55.835 0.2 1 336 390 83 SEP CB C 64.725 0.2 1 337 390 83 SEP N N 119.805 0.03 1 338 391 84 PRO C C 176.705 0.03 1 339 391 84 PRO CA C 63.175 0.2 1 340 391 84 PRO CB C 31.995 0.2 1 341 392 85 ALA H H 8.565 0.003 1 342 392 85 ALA C C 178.105 0.03 1 343 392 85 ALA CA C 52.695 0.2 1 344 392 85 ALA CB C 18.935 0.2 1 345 392 85 ALA N N 124.565 0.03 1 346 393 86 LYS H H 8.505 0.003 1 347 393 86 LYS C C 176.785 0.03 1 348 393 86 LYS CA C 55.995 0.2 1 349 393 86 LYS CB C 33.005 0.2 1 350 393 86 LYS N N 121.445 0.03 1 351 394 87 LEU H H 8.385 0.003 1 352 394 87 LEU C C 177.355 0.03 1 353 394 87 LEU CA C 55.075 0.2 1 354 394 87 LEU CB C 42.335 0.2 1 355 394 87 LEU N N 123.475 0.03 1 356 395 88 SER H H 8.335 0.003 1 357 395 88 SER C C 174.085 0.03 1 358 395 88 SER CA C 58.075 0.2 1 359 395 88 SER CB C 63.895 0.2 1 360 395 88 SER N N 116.565 0.03 1 361 396 89 PHE H H 8.305 0.003 1 362 396 89 PHE C C 175.185 0.03 1 363 396 89 PHE CA C 57.935 0.2 1 364 396 89 PHE CB C 39.685 0.2 1 365 396 89 PHE N N 122.335 0.03 1 366 397 90 GLN H H 8.125 0.003 1 367 397 90 GLN C C 174.835 0.03 1 368 397 90 GLN CA C 55.235 0.2 1 369 397 90 GLN CB C 29.785 0.2 1 370 397 90 GLN N N 122.285 0.03 1 371 398 91 PHE H H 8.335 0.003 1 372 398 91 PHE CA C 55.935 0.2 1 373 398 91 PHE CB C 38.885 0.2 1 374 398 91 PHE N N 122.435 0.03 1 375 399 92 PRO C C 177.055 0.03 1 376 399 92 PRO CA C 62.965 0.2 1 377 399 92 PRO CB C 32.055 0.2 1 378 400 93 SER H H 8.645 0.003 1 379 400 93 SER C C 174.975 0.03 1 380 400 93 SER CA C 58.505 0.2 1 381 400 93 SER CB C 63.895 0.2 1 382 400 93 SER N N 116.815 0.03 1 383 401 94 SER H H 8.565 0.003 1 384 401 94 SER C C 175.205 0.03 1 385 401 94 SER CA C 58.775 0.2 1 386 401 94 SER CB C 63.885 0.2 1 387 401 94 SER N N 117.965 0.03 1 388 402 95 GLY H H 8.575 0.003 1 389 402 95 GLY C C 174.305 0.03 1 390 402 95 GLY CA C 45.395 0.2 1 391 402 95 GLY N N 111.095 0.03 1 392 403 96 SER H H 8.315 0.003 1 393 403 96 SER C C 174.385 0.03 1 394 403 96 SER CA C 58.345 0.2 1 395 403 96 SER CB C 63.985 0.2 1 396 403 96 SER N N 115.925 0.03 1 397 404 97 ALA H H 8.475 0.003 1 398 404 97 ALA C C 177.645 0.03 1 399 404 97 ALA CA C 52.585 0.2 1 400 404 97 ALA CB C 19.135 0.2 1 401 404 97 ALA N N 125.995 0.03 1 402 405 98 GLN H H 8.415 0.003 1 403 405 98 GLN C C 175.835 0.03 1 404 405 98 GLN CA C 55.685 0.2 1 405 405 98 GLN CB C 29.625 0.2 1 406 405 98 GLN N N 120.035 0.03 1 407 406 99 VAL H H 8.275 0.003 1 408 406 99 VAL C C 175.685 0.03 1 409 406 99 VAL CA C 62.215 0.2 1 410 406 99 VAL CB C 32.975 0.2 1 411 406 99 VAL N N 122.305 0.03 1 412 407 100 HIS H H 8.685 0.003 1 413 407 100 HIS C C 174.475 0.03 1 414 407 100 HIS CA C 55.675 0.2 1 415 407 100 HIS CB C 30.375 0.2 1 416 407 100 HIS N N 124.575 0.03 1 417 408 101 ILE H H 8.415 0.003 1 418 408 101 ILE CA C 58.365 0.2 1 419 408 101 ILE CB C 38.555 0.2 1 420 408 101 ILE N N 126.755 0.03 1 421 409 102 PRO C C 176.785 0.03 1 422 409 102 PRO CA C 62.905 0.2 1 423 409 102 PRO CB C 32.315 0.2 1 424 410 103 SER H H 8.635 0.003 1 425 410 103 SER C C 174.565 0.03 1 426 410 103 SER CA C 58.255 0.2 1 427 410 103 SER CB C 63.775 0.2 1 428 410 103 SER N N 117.175 0.03 1 429 411 104 ILE H H 8.345 0.003 1 430 411 104 ILE C C 176.225 0.03 1 431 411 104 ILE CA C 61.145 0.2 1 432 411 104 ILE CB C 39.095 0.2 1 433 411 104 ILE N N 122.755 0.03 1 434 412 105 SER H H 8.545 0.003 1 435 412 105 SER C C 174.865 0.03 1 436 412 105 SER CA C 58.025 0.2 1 437 412 105 SER CB C 63.905 0.2 1 438 412 105 SER N N 120.575 0.03 1 439 413 106 VAL H H 8.495 0.003 1 440 413 106 VAL C C 176.125 0.03 1 441 413 106 VAL CA C 62.445 0.2 1 442 413 106 VAL CB C 32.695 0.2 1 443 413 106 VAL N N 122.435 0.03 1 444 414 107 ASP H H 8.435 0.003 1 445 414 107 ASP C C 176.735 0.03 1 446 414 107 ASP CA C 54.515 0.2 1 447 414 107 ASP CB C 41.215 0.2 1 448 414 107 ASP N N 123.085 0.03 1 449 415 108 GLY H H 8.385 0.003 1 450 415 108 GLY C C 174.125 0.03 1 451 415 108 GLY CA C 45.425 0.2 1 452 415 108 GLY N N 109.405 0.03 1 453 416 109 LEU H H 8.185 0.003 1 454 416 109 LEU C C 177.455 0.03 1 455 416 109 LEU CA C 54.935 0.2 1 456 416 109 LEU CB C 42.525 0.2 1 457 416 109 LEU N N 121.525 0.03 1 458 417 110 SER H H 8.365 0.003 1 459 417 110 SER C C 174.015 0.03 1 460 417 110 SER CA C 58.435 0.2 1 461 417 110 SER CB C 64.075 0.2 1 462 417 110 SER N N 117.355 0.03 1 463 418 111 TPO H H 9.325 0.003 1 464 418 111 TPO CA C 60.965 0.2 1 465 418 111 TPO CB C 72.905 0.2 1 466 418 111 TPO N N 123.045 0.03 1 467 419 112 PRO C C 176.585 0.03 1 468 419 112 PRO CA C 63.235 0.2 1 469 419 112 PRO CB C 32.285 0.2 1 470 420 113 VAL H H 8.470 0.003 1 471 420 113 VAL C C 176.115 0.03 1 472 420 113 VAL CA C 62.585 0.2 1 473 420 113 VAL CB C 32.835 0.2 1 474 420 113 VAL N N 122.635 0.03 1 475 421 114 VAL H H 8.555 0.003 1 476 421 114 VAL C C 175.875 0.03 1 477 421 114 VAL CA C 62.115 0.2 1 478 421 114 VAL CB C 32.835 0.2 1 479 421 114 VAL N N 127.165 0.03 1 480 422 115 LEU H H 8.585 0.003 1 481 422 115 LEU C C 177.025 0.03 1 482 422 115 LEU CA C 54.485 0.2 1 483 422 115 LEU CB C 42.585 0.2 1 484 422 115 LEU N N 128.265 0.03 1 485 423 116 SEP H H 8.815 0.003 1 486 423 116 SEP CA C 55.755 0.2 1 487 423 116 SEP CB C 65.065 0.2 1 488 423 116 SEP N N 119.675 0.03 1 489 424 117 PRO C C 177.395 0.03 1 490 424 117 PRO CA C 63.635 0.2 1 491 424 117 PRO CB C 32.365 0.2 1 492 425 118 GLY H H 8.345 0.003 1 493 425 118 GLY CA C 44.565 0.2 1 494 425 118 GLY N N 109.095 0.03 1 495 426 119 PRO C C 177.215 0.03 1 496 426 119 PRO CA C 63.015 0.2 1 497 426 119 PRO CB C 32.265 0.2 1 498 427 120 GLN H H 8.685 0.003 1 499 427 120 GLN C C 175.875 0.03 1 500 427 120 GLN CA C 55.715 0.2 1 501 427 120 GLN CB C 29.565 0.2 1 502 427 120 GLN N N 121.415 0.03 1 503 428 121 LYS H H 8.575 0.003 1 504 428 121 LYS CA C 54.205 0.2 1 505 428 121 LYS CB C 32.415 0.2 1 506 428 121 LYS N N 125.525 0.03 1 stop_ save_