data_4708 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; WT1-KTS/DNA complex ; _BMRB_accession_number 4708 _BMRB_flat_file_name bmr4708.str _Entry_type new _Submission_date 2000-03-30 _Accession_date 2000-03-30 _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 Laity John H . 2 Chung John . . 3 Dyson H Jane . 4 Wright Peter E . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 108 "13C chemical shifts" 227 "15N chemical shifts" 108 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-07-19 update BMRB 'update DNA residue label to two-letter code' 2000-05-01 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 4707 'WT1-KTS/DNA free' 4709 WT1+KTS/free 4710 'WT1+KTS/DNA complex' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Alternative Splicing of Wilms' Tumor Suppressor Protein Modulates DNA Binding Activity Through Isoform-Specific DNA-Induced Conformational Changes ; _Citation_status 'in press' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Laity John H. . 2 Chung John . . 3 Dyson H. Jane . 4 Wright Peter E. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2000 _Details ; amide 1H and 15N, and backbone 13Ca chemical shifts of free and DNA-bound WT1 of two alternative splice forms are compared" ; loop_ _Keyword 'transcription factors' 'alternative splicing' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_wt1_ref_1 _Saveframe_category citation _Citation_full . _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code 90304885 _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_wt1_ref_2 _Saveframe_category citation _Citation_full . _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code 90158822 _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_WT1-KTS_DNA_complex _Saveframe_category molecular_system _Mol_system_name 'WT1 zinc finger domain DNA complex' _Abbreviation_common WT1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label WT1-KTS $WT1-KTS 'DNA strand 1' $DNA_1 'DNA strand 2' $DNA_2 'Zn 1' $ZN 'Zn 2' $ZN 'Zn 3' $ZN 'Zn 4' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Biological_function ; transcription factor post-trancriptional regulator (putative) ; stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_WT1-KTS _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common WT1 _Name_variant WT1-KTS _Abbreviation_common WT1-KTS _Molecular_mass 14450 _Mol_thiol_state 'all other bound' _Details ; 4 Cys2-His2 zinc fingers complexed to a 14 base pair DNA duplex with a coding sequence of 5'-CGCGGGGGCGTCTG-3'. The molecular mass of the WT1-DNA complex is ~25,000 daltons ; ############################## # Polymer residue sequence # ############################## _Residue_count 119 _Mol_residue_sequence ; ASEKRPFMCAYPGCNKRYFK LSHLQMHSRKHTGEKPYQCD FKDCERRFSRSDQLKRHQRR HTGVKPFQCKTCQRKFSRSD HLKTHTRTHTGEKPFSCRWP SCQKKFARSDELVRHHNMH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 . ALA 2 318 SER 3 319 GLU 4 320 LYS 5 321 ARG 6 322 PRO 7 323 PHE 8 324 MET 9 325 CYS 10 326 ALA 11 327 TYR 12 328 PRO 13 329 GLY 14 330 CYS 15 331 ASN 16 332 LYS 17 333 ARG 18 334 TYR 19 335 PHE 20 336 LYS 21 337 LEU 22 338 SER 23 339 HIS 24 340 LEU 25 341 GLN 26 342 MET 27 343 HIS 28 344 SER 29 345 ARG 30 346 LYS 31 347 HIS 32 348 THR 33 349 GLY 34 350 GLU 35 351 LYS 36 352 PRO 37 353 TYR 38 354 GLN 39 355 CYS 40 356 ASP 41 357 PHE 42 358 LYS 43 359 ASP 44 360 CYS 45 361 GLU 46 362 ARG 47 363 ARG 48 364 PHE 49 365 SER 50 366 ARG 51 367 SER 52 368 ASP 53 369 GLN 54 370 LEU 55 371 LYS 56 372 ARG 57 373 HIS 58 374 GLN 59 375 ARG 60 376 ARG 61 377 HIS 62 378 THR 63 379 GLY 64 380 VAL 65 381 LYS 66 382 PRO 67 383 PHE 68 384 GLN 69 385 CYS 70 386 LYS 71 387 THR 72 388 CYS 73 389 GLN 74 390 ARG 75 391 LYS 76 392 PHE 77 393 SER 78 394 ARG 79 395 SER 80 396 ASP 81 397 HIS 82 398 LEU 83 399 LYS 84 400 THR 85 401 HIS 86 402 THR 87 403 ARG 88 404 THR 89 405 HIS 90 406 THR 91 407 GLY 92 408 GLU 93 409 LYS 94 410 PRO 95 411 PHE 96 412 SER 97 413 CYS 98 414 ARG 99 415 TRP 100 416 PRO 101 417 SER 102 418 CYS 103 419 GLN 104 420 LYS 105 421 LYS 106 422 PHE 107 423 ALA 108 424 ARG 109 425 SER 110 426 ASP 111 427 GLU 112 428 LEU 113 429 VAL 114 430 ARG 115 431 HIS 116 432 HIS 117 433 ASN 118 434 MET 119 435 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-06 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15532 wt1-17mer 100.00 119 100.00 100.00 3.09e-80 BMRB 15533 wt1-zf14 100.00 119 100.00 100.00 3.09e-80 BMRB 4707 WT1 100.00 119 100.00 100.00 3.09e-80 BMRB 4709 WT1 102.52 122 97.54 97.54 2.04e-78 BMRB 4710 WT1 102.52 122 97.54 97.54 2.04e-78 PDB 2JP9 "Structure Of The Wilms Tumor Suppressor Protein Zinc Finger Domain Bound To Dna" 100.00 119 100.00 100.00 3.09e-80 PDB 2JPA "Structure Of The Wilms Tumor Suppressor Protein Zinc Finger Domain Bound To Dna" 100.00 119 100.00 100.00 3.09e-80 PDB 2PRT "Structure Of The Wilms Tumor Suppressor Protein Zinc Finger Domain Bound To Dna" 100.00 119 100.00 100.00 3.09e-80 DBJ BAA11522 "WT1 [Xenopus laevis]" 100.00 407 99.16 100.00 9.69e-79 DBJ BAA28147 "unnamed protein product [Sus scrofa]" 101.68 449 97.52 97.52 8.62e-77 DBJ BAA94793 "WT1(-KTS) [Gallus gallus]" 99.16 414 99.15 100.00 4.36e-78 DBJ BAF84425 "unnamed protein product [Homo sapiens]" 99.16 446 100.00 100.00 8.28e-79 EMBL CAA35956 "Krueppel-like zinc-finger protein [Homo sapiens]" 101.68 575 97.52 97.52 4.35e-76 EMBL CAA43819 "unnamed protein product [Homo sapiens]" 99.16 446 99.15 99.15 3.28e-78 EMBL CDG23662 "Wt1 protein [Capreolus capreolus]" 101.68 450 97.52 97.52 1.03e-76 GB AAA36810 "Wilms' tumor protein, partial [Homo sapiens]" 100.00 345 98.32 98.32 8.88e-78 GB AAA61299 "Wilms' tumor assocated protein [Homo sapiens]" 101.68 449 97.52 97.52 1.00e-76 GB AAB33443 "WT1 [Homo sapiens]" 100.00 168 98.32 98.32 8.97e-79 GB AAB53152 "WT1 [Xenopus laevis]" 100.00 409 98.32 100.00 1.27e-78 GB AAH32861 "WT1 protein [Homo sapiens]" 100.00 302 99.16 99.16 1.21e-79 PRF 1604420A "Zn finger protein" 101.68 575 97.52 97.52 4.35e-76 REF NP_000369 "Wilms tumor protein isoform A [Homo sapiens]" 99.16 497 100.00 100.00 1.71e-78 REF NP_001001264 "Wilms tumor protein homolog [Sus scrofa]" 101.68 449 97.52 97.52 8.62e-77 REF NP_001079057 "Wilms tumor protein homolog A [Xenopus laevis]" 100.00 409 98.32 100.00 1.27e-78 REF NP_001079336 "Wilms tumor protein homolog B [Xenopus laevis]" 100.00 407 99.16 100.00 9.69e-79 REF NP_001135625 "Wilms tumor protein homolog [Xenopus (Silurana) tropicalis]" 100.00 413 98.32 100.00 1.41e-78 SP B5DE03 "RecName: Full=Wilms tumor protein homolog" 100.00 413 98.32 100.00 1.41e-78 SP O62651 "RecName: Full=Wilms tumor protein homolog" 101.68 449 97.52 97.52 8.62e-77 SP P19544 "RecName: Full=Wilms tumor protein; AltName: Full=WT33" 101.68 449 97.52 97.52 1.00e-76 SP P79958 "RecName: Full=Wilms tumor protein homolog B; Short=XWT1b; Short=XeWT1" 100.00 407 99.16 100.00 9.69e-79 TPG DAA21902 "TPA: Wilms tumor 1-like [Bos taurus]" 99.16 877 100.00 100.00 3.65e-76 stop_ save_ save_DNA_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class DNA _Name_common 'DNA strand 1' _Molecular_mass . _Mol_thiol_state . _Details . _Residue_count 14 _Mol_residue_sequence CGCGGGGGCGTCTG loop_ _Residue_seq_code _Residue_label 1 DC 2 DG 3 DC 4 DG 5 DG 6 DG 7 DG 8 DG 9 DC 10 DG 11 DT 12 DC 13 DT 14 DG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_DNA_2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class DNA _Name_common 'DNA strand 2' _Molecular_mass . _Mol_thiol_state . _Details . _Residue_count 14 _Mol_residue_sequence CAGACGCCCCCGCG loop_ _Residue_seq_code _Residue_label 1 DC 2 DA 3 DG 4 DA 5 DC 6 DG 7 DC 8 DC 9 DC 10 DC 11 DC 12 DG 13 DC 14 DG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common Zn _Abbreviation_common Zn _Name_IUPAC 'ZINC ION' _BMRB_code . _PDB_code ZN _Molecular_mass . _Mol_charge 2+ _Mol_paramagnetic no _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction _Gene_mnemonic $WT1-KTS Human 9606 Eukaryota . Homo Sapiens cytoplasm wt1 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 _Details $WT1-KTS 'recombinant technology' 'E. coli' . . BL21 PET21 . $DNA_1 'chemical synthesis' . . . . . 'using the phosphoramidite method' $DNA_2 'chemical synthesis' . . . . . 'using the phosphoramidite method' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_WT1-DNA_complex _Saveframe_category sample _Sample_type solution _Details 'WT1 complexes with DNA' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $WT1-KTS . mM 0.15 0.3 '[U-95% 13C; U-95% 15N]' $DNA_1 . mM 0.15 0.3 . $DNA_2 . mM 0.15 0.3 . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version '95, 97' loop_ _Task 'processing, peakpicking, analysis' stop_ _Details 'In-house macros programmed in FELIX command language utilized' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details 'Nalorac 8mm Probe' save_ ############################# # NMR applied experiments # ############################# save_15N-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HCACO(CA)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCACO(CA)NH _Sample_label . save_ save_HNCACB_(deuterium_decoupling)_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'HNCACB (deuterium decoupling)' _Sample_label . save_ save_HN(CO)CACB_(deuterium_decoupling)_9 _Saveframe_category NMR_applied_experiment _Experiment_name 'HN(CO)CACB (deuterium decoupling)' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCACO(CA)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'HNCACB (deuterium decoupling)' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name 'HN(CO)CACB (deuterium decoupling)' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.70 0.05 n/a temperature 310 0.3 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 H 1 'methyl protons' ppm 0.00 internal direct . internal . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_chemical_shift_assignment_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $WT1-DNA_complex stop_ _Sample_conditions_label $Conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name WT1-KTS _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 . 2 SER CA C 58.0 0.1 1 2 . 2 SER CB C 63.3 0.1 1 3 . 3 GLU H H 8.55 0.03 1 4 . 3 GLU CA C 55.9 0.1 1 5 . 3 GLU CB C 29.4 0.1 1 6 . 3 GLU N N 123.3 0.1 1 7 . 4 LYS H H 8.37 0.03 1 8 . 4 LYS CA C 55.8 0.1 1 9 . 4 LYS CB C 31.8 0.1 1 10 . 4 LYS N N 123.1 0.1 1 11 . 5 ARG H H 8.25 0.03 1 12 . 5 ARG CA C 52.6 0.1 1 13 . 5 ARG CB C 29.8 0.1 1 14 . 5 ARG N N 121.5 0.1 1 15 . 6 PRO CA C 63.0 0.1 1 16 . 6 PRO CB C 31.3 0.1 1 17 . 7 PHE H H 7.88 0.03 1 18 . 7 PHE CA C 56.9 0.1 1 19 . 7 PHE CB C 38.3 0.1 1 20 . 7 PHE N N 117.3 0.1 1 21 . 8 MET H H 8.65 0.03 1 22 . 8 MET CA C 53.8 0.1 1 23 . 8 MET CB C 34.2 0.1 1 24 . 8 MET N N 124.3 0.1 1 25 . 9 CYS H H 8.72 0.03 1 26 . 9 CYS CA C 60.7 0.1 1 27 . 9 CYS CB C 29.4 0.1 1 28 . 9 CYS N N 127.4 0.1 1 29 . 10 ALA H H 8.79 0.03 1 30 . 10 ALA CA C 51.4 0.1 1 31 . 10 ALA CB C 18.5 0.1 1 32 . 10 ALA N N 131.7 0.1 1 33 . 11 TYR H H 9.10 0.03 1 34 . 11 TYR CA C 57.6 0.1 1 35 . 11 TYR CB C 37.9 0.1 1 36 . 11 TYR N N 127.9 0.1 1 37 . 12 PRO CA C 63.7 0.1 1 38 . 12 PRO CB C 30.1 0.1 1 39 . 13 GLY H H 8.77 0.03 1 40 . 13 GLY CA C 44.7 0.1 1 41 . 13 GLY N N 112.5 0.1 1 42 . 14 CYS H H 8.09 0.03 1 43 . 14 CYS CA C 60.5 0.1 1 44 . 14 CYS CB C 29.7 0.1 1 45 . 14 CYS N N 123.6 0.1 1 46 . 15 ASN H H 8.68 0.03 1 47 . 15 ASN CA C 53.0 0.1 1 48 . 15 ASN CB C 37.8 0.1 1 49 . 15 ASN N N 116.1 0.1 1 50 . 16 LYS H H 8.05 0.03 1 51 . 16 LYS CA C 56.6 0.1 1 52 . 16 LYS CB C 31.7 0.1 1 53 . 16 LYS N N 121.3 0.1 1 54 . 17 ARG H H 7.69 0.03 1 55 . 17 ARG CA C 53.7 0.1 1 56 . 17 ARG CB C 32.7 0.1 1 57 . 17 ARG N N 117.6 0.1 1 58 . 18 TYR H H 8.74 0.03 1 59 . 18 TYR CA C 57.6 0.1 1 60 . 18 TYR CB C 43.2 0.1 1 61 . 18 TYR N N 117.4 0.1 1 62 . 19 PHE H H 9.93 0.03 1 63 . 19 PHE CA C 59.6 0.1 1 64 . 19 PHE CB C 39.6 0.1 1 65 . 19 PHE N N 118.9 0.1 1 66 . 20 LYS H H 7.08 0.03 1 67 . 20 LYS CA C 53.6 0.1 1 68 . 20 LYS CB C 34.1 0.1 1 69 . 20 LYS N N 114.5 0.1 1 70 . 21 LEU H H 8.18 0.03 1 71 . 21 LEU CA C 56.8 0.1 1 72 . 21 LEU CB C 39.4 0.1 1 73 . 21 LEU N N 126.9 0.1 1 74 . 22 SER H H 8.33 0.03 1 75 . 22 SER CA C 60.2 0.1 1 76 . 22 SER N N 113.1 0.1 1 77 . 23 HIS H H 6.57 0.03 1 78 . 23 HIS CA C 56.2 0.1 1 79 . 23 HIS CB C 30.8 0.1 1 80 . 23 HIS N N 121.0 0.1 1 81 . 24 LEU H H 7.10 0.03 1 82 . 24 LEU CA C 57.0 0.1 1 83 . 24 LEU CB C 39.2 0.1 1 84 . 24 LEU N N 121.5 0.1 1 85 . 25 GLN H H 8.66 0.03 1 86 . 25 GLN CA C 58.5 0.1 1 87 . 25 GLN CB C 27.0 0.1 1 88 . 25 GLN N N 119.5 0.1 1 89 . 26 MET H H 7.78 0.03 1 90 . 26 MET CA C 58.0 0.1 1 91 . 26 MET CB C 31.4 0.1 1 92 . 26 MET N N 117.9 0.1 1 93 . 27 HIS H H 7.73 0.03 1 94 . 27 HIS CA C 58.5 0.1 1 95 . 27 HIS CB C 27.5 0.1 1 96 . 27 HIS N N 120.2 0.1 1 97 . 28 SER H H 8.71 0.03 1 98 . 28 SER CA C 61.7 0.1 1 99 . 28 SER CB C 62.8 0.1 1 100 . 28 SER N N 113.3 0.1 1 101 . 29 ARG H H 7.18 0.03 1 102 . 29 ARG CA C 57.8 0.1 1 103 . 29 ARG CB C 28.5 0.1 1 104 . 29 ARG N N 119.8 0.1 1 105 . 30 LYS H H 8.03 0.03 1 106 . 30 LYS CA C 57.6 0.1 1 107 . 30 LYS CB C 30.3 0.1 1 108 . 30 LYS N N 119.5 0.1 1 109 . 31 HIS H H 7.08 0.03 1 110 . 31 HIS CA C 55.1 0.1 1 111 . 31 HIS CB C 27.6 0.1 1 112 . 31 HIS N N 114.4 0.1 1 113 . 32 THR H H 7.92 0.03 1 114 . 32 THR CA C 61.9 0.1 1 115 . 32 THR CB C 69.5 0.1 1 116 . 32 THR N N 107.1 0.1 1 117 . 33 GLY H H 8.00 0.03 1 118 . 33 GLY CA C 44.9 0.1 1 119 . 33 GLY N N 109.7 0.1 1 120 . 34 GLU H H 7.77 0.03 1 121 . 34 GLU CA C 56.5 0.1 1 122 . 34 GLU CB C 29.7 0.1 1 123 . 34 GLU N N 120.4 0.1 1 124 . 35 LYS H H 8.52 0.03 1 125 . 35 LYS CA C 53.1 0.1 1 126 . 35 LYS CB C 32.7 0.1 1 127 . 35 LYS N N 123.0 0.1 1 128 . 36 PRO CA C 63.1 0.1 1 129 . 36 PRO CB C 31.3 0.1 1 130 . 37 TYR H H 7.71 0.03 1 131 . 37 TYR CA C 56.9 0.1 1 132 . 37 TYR CB C 37.5 0.1 1 133 . 37 TYR N N 117.2 0.1 1 134 . 38 GLN H H 8.79 0.03 1 135 . 38 GLN CA C 53.8 0.1 1 136 . 38 GLN CB C 30.4 0.1 1 137 . 38 GLN N N 124.9 0.1 1 138 . 39 CYS H H 8.91 0.03 1 139 . 39 CYS CA C 61.2 0.1 1 140 . 39 CYS CB C 29.9 0.1 1 141 . 39 CYS N N 128.5 0.1 1 142 . 40 ASP H H 8.51 0.03 1 143 . 40 ASP CA C 53.0 0.1 1 144 . 40 ASP CB C 39.7 0.1 1 145 . 40 ASP N N 127.1 0.1 1 146 . 41 PHE H H 8.94 0.03 1 147 . 41 PHE CA C 59.1 0.1 1 148 . 41 PHE CB C 38.8 0.1 1 149 . 41 PHE N N 126.0 0.1 1 150 . 42 LYS H H 7.83 0.03 1 151 . 42 LYS CA C 57.7 0.1 1 152 . 42 LYS CB C 30.7 0.1 1 153 . 42 LYS N N 127.0 0.1 1 154 . 43 ASP H H 8.73 0.03 1 155 . 43 ASP CA C 55.3 0.1 1 156 . 43 ASP CB C 38.7 0.1 1 157 . 43 ASP N N 119.7 0.1 1 158 . 44 CYS H H 8.27 0.03 1 159 . 44 CYS CA C 60.8 0.1 1 160 . 44 CYS CB C 29.6 0.1 1 161 . 44 CYS N N 122.9 0.1 1 162 . 45 GLU H H 8.52 0.03 1 163 . 45 GLU CA C 55.6 0.1 1 164 . 45 GLU CB C 28.0 0.1 1 165 . 45 GLU N N 117.3 0.1 1 166 . 46 ARG H H 8.26 0.03 1 167 . 46 ARG CA C 57.0 0.1 1 168 . 46 ARG CB C 29.6 0.1 1 169 . 46 ARG N N 122.3 0.1 1 170 . 47 ARG H H 7.80 0.03 1 171 . 47 ARG CA C 53.7 0.1 1 172 . 47 ARG CB C 32.4 0.1 1 173 . 47 ARG N N 118.5 0.1 1 174 . 48 PHE H H 8.84 0.03 1 175 . 48 PHE CA C 56.4 0.1 1 176 . 48 PHE CB C 43.6 0.1 1 177 . 48 PHE N N 115.9 0.1 1 178 . 49 SER H H 9.33 0.03 1 179 . 49 SER CA C 59.9 0.1 1 180 . 49 SER CB C 63.8 0.1 1 181 . 49 SER N N 116.3 0.1 1 182 . 50 ARG H H 7.30 0.03 1 183 . 50 ARG CA C 53.9 0.1 1 184 . 50 ARG CB C 34.6 0.1 1 185 . 50 ARG N N 117.3 0.1 1 186 . 51 SER H H 8.67 0.03 1 187 . 51 SER CA C 60.1 0.1 1 188 . 51 SER CB C 61.5 0.1 1 189 . 51 SER N N 120.0 0.1 1 190 . 52 ASP H H 8.82 0.03 1 191 . 52 ASP CA C 56.0 0.1 1 192 . 52 ASP CB C 38.3 0.1 1 193 . 52 ASP N N 120.8 0.1 1 194 . 53 GLN H H 6.98 0.03 1 195 . 53 GLN CA C 57.0 0.1 1 196 . 53 GLN CB C 28.5 0.1 1 197 . 53 GLN N N 121.5 0.1 1 198 . 54 LEU H H 6.90 0.03 1 199 . 54 LEU CA C 57.2 0.1 1 200 . 54 LEU CB C 38.9 0.1 1 201 . 54 LEU N N 121.0 0.1 1 202 . 55 LYS H H 8.09 0.03 1 203 . 55 LYS CA C 59.0 0.1 1 204 . 55 LYS CB C 30.9 0.1 1 205 . 55 LYS N N 118.7 0.1 1 206 . 56 ARG H H 7.84 0.03 1 207 . 56 ARG CA C 59.3 0.1 1 208 . 56 ARG CB C 30.1 0.1 1 209 . 56 ARG N N 119.5 0.1 1 210 . 57 HIS H H 7.70 0.03 1 211 . 57 HIS CA C 58.6 0.1 1 212 . 57 HIS CB C 27.7 0.1 1 213 . 57 HIS N N 119.7 0.1 1 214 . 58 GLN H H 8.56 0.03 1 215 . 58 GLN CA C 59.0 0.1 1 216 . 58 GLN CB C 27.5 0.1 1 217 . 58 GLN N N 115.9 0.1 1 218 . 59 ARG H H 7.35 0.03 1 219 . 59 ARG CA C 58.5 0.1 1 220 . 59 ARG CB C 28.0 0.1 1 221 . 59 ARG N N 117.2 0.1 1 222 . 60 ARG H H 8.02 0.03 1 223 . 60 ARG CA C 57.7 0.1 1 224 . 60 ARG CB C 28.5 0.1 1 225 . 60 ARG N N 120.1 0.1 1 226 . 61 HIS H H 7.08 0.03 1 227 . 61 HIS CA C 55.1 0.1 1 228 . 61 HIS CB C 27.6 0.1 1 229 . 61 HIS N N 114.4 0.1 1 230 . 62 THR H H 7.92 0.03 1 231 . 62 THR CA C 61.8 0.1 1 232 . 62 THR CB C 69.4 0.1 1 233 . 62 THR N N 107.1 0.1 1 234 . 63 GLY H H 7.93 0.03 1 235 . 63 GLY CA C 45.2 0.1 1 236 . 63 GLY N N 109.9 0.1 1 237 . 64 VAL H H 7.31 0.03 1 238 . 64 VAL CA C 63.3 0.1 1 239 . 64 VAL CB C 31.2 0.1 1 240 . 64 VAL N N 119.9 0.1 1 241 . 65 LYS H H 8.26 0.03 1 242 . 65 LYS CA C 52.9 0.1 1 243 . 65 LYS CB C 34.1 0.1 1 244 . 65 LYS N N 126.9 0.1 1 245 . 66 PRO CA C 62.4 0.1 1 246 . 66 PRO CB C 31.3 0.1 1 247 . 67 PHE H H 7.71 0.03 1 248 . 67 PHE CA C 56.3 0.1 1 249 . 67 PHE CB C 39.3 0.1 1 250 . 67 PHE N N 115.7 0.1 1 251 . 68 GLN H H 9.02 0.03 1 252 . 68 GLN CA C 54.1 0.1 1 253 . 68 GLN CB C 31.0 0.1 1 254 . 68 GLN N N 124.1 0.1 1 255 . 69 CYS H H 9.22 0.03 1 256 . 69 CYS CA C 59.0 0.1 1 257 . 69 CYS CB C 29.3 0.1 1 258 . 69 CYS N N 128.4 0.1 1 259 . 70 LYS H H 9.18 0.03 1 260 . 70 LYS CA C 57.6 0.1 1 261 . 70 LYS CB C 31.1 0.1 1 262 . 70 LYS N N 131.1 0.1 1 263 . 71 THR H H 8.87 0.03 1 264 . 71 THR CA C 65.3 0.1 1 265 . 71 THR CB C 68.4 0.1 1 266 . 71 THR N N 118.5 0.1 1 267 . 72 CYS H H 8.27 0.03 1 268 . 72 CYS CA C 58.0 0.1 1 269 . 72 CYS CB C 31.4 0.1 1 270 . 72 CYS N N 119.1 0.1 1 271 . 73 GLN H H 7.83 0.03 1 272 . 73 GLN CA C 58.0 0.1 1 273 . 73 GLN CB C 25.2 0.1 1 274 . 73 GLN N N 115.4 0.1 1 275 . 74 ARG H H 8.37 0.03 1 276 . 74 ARG CA C 57.8 0.1 1 277 . 74 ARG CB C 30.5 0.1 1 278 . 74 ARG N N 124.5 0.1 1 279 . 75 LYS H H 8.10 0.03 1 280 . 75 LYS CA C 54.7 0.1 1 281 . 75 LYS CB C 33.5 0.1 1 282 . 75 LYS N N 122.9 0.1 1 283 . 76 PHE H H 9.11 0.03 1 284 . 76 PHE CA C 56.8 0.1 1 285 . 76 PHE CB C 42.7 0.1 1 286 . 76 PHE N N 118.0 0.1 1 287 . 77 SER H H 9.71 0.03 1 288 . 77 SER CA C 59.6 0.1 1 289 . 77 SER CB C 64.1 0.1 1 290 . 77 SER N N 117.0 0.1 1 291 . 78 ARG H H 7.97 0.03 1 292 . 78 ARG CA C 54.4 0.1 1 293 . 78 ARG CB C 34.3 0.1 1 294 . 78 ARG N N 119.5 0.1 1 295 . 79 SER H H 8.21 0.03 1 296 . 79 SER CA C 59.5 0.1 1 297 . 79 SER CB C 61.2 0.1 1 298 . 79 SER N N 119.9 0.1 1 299 . 80 ASP H H 8.65 0.03 1 300 . 80 ASP CA C 55.4 0.1 1 301 . 80 ASP CB C 37.4 0.1 1 302 . 80 ASP N N 122.8 0.1 1 303 . 81 HIS H H 6.94 0.03 1 304 . 81 HIS CA C 54.5 0.1 1 305 . 81 HIS CB C 26.1 0.1 1 306 . 81 HIS N N 119.6 0.1 1 307 . 82 LEU H H 7.46 0.03 1 308 . 82 LEU CA C 57.4 0.1 1 309 . 82 LEU CB C 38.8 0.1 1 310 . 82 LEU N N 120.8 0.1 1 311 . 83 LYS H H 7.86 0.03 1 312 . 83 LYS CA C 59.7 0.1 1 313 . 83 LYS CB C 30.8 0.1 1 314 . 83 LYS N N 120.3 0.1 1 315 . 85 HIS H H 8.53 0.03 1 316 . 85 HIS CA C 59.6 0.1 1 317 . 85 HIS CB C 26.8 0.1 1 318 . 85 HIS N N 125.4 0.1 1 319 . 86 THR H H 8.69 0.03 1 320 . 86 THR CA C 66.8 0.1 1 321 . 86 THR CB C 68.5 0.1 1 322 . 86 THR N N 116.4 0.1 1 323 . 87 ARG H H 7.41 0.03 1 324 . 87 ARG CA C 58.5 0.1 1 325 . 87 ARG CB C 27.7 0.1 1 326 . 87 ARG N N 119.6 0.1 1 327 . 88 THR H H 8.16 0.03 1 328 . 88 THR CA C 64.2 0.1 1 329 . 88 THR CB C 68.0 0.1 1 330 . 88 THR N N 113.3 0.1 1 331 . 89 HIS H H 7.32 0.03 1 332 . 89 HIS CA C 55.2 0.1 1 333 . 89 HIS CB C 28.4 0.1 1 334 . 89 HIS N N 117.4 0.1 1 335 . 90 THR H H 7.94 0.03 1 336 . 90 THR CA C 61.9 0.1 1 337 . 90 THR CB C 69.5 0.1 1 338 . 90 THR N N 107.8 0.1 1 339 . 91 GLY H H 8.00 0.03 1 340 . 91 GLY CA C 44.9 0.1 1 341 . 91 GLY N N 109.7 0.1 1 342 . 92 GLU H H 7.60 0.03 1 343 . 92 GLU CA C 56.7 0.1 1 344 . 92 GLU CB C 29.4 0.1 1 345 . 92 GLU N N 121.4 0.1 1 346 . 93 LYS H H 8.32 0.03 1 347 . 93 LYS CA C 53.0 0.1 1 348 . 93 LYS CB C 33.7 0.1 1 349 . 93 LYS N N 126.0 0.1 1 350 . 94 PRO CA C 62.5 0.1 1 351 . 94 PRO CB C 31.3 0.1 1 352 . 95 PHE H H 7.78 0.03 1 353 . 95 PHE CA C 56.9 0.1 1 354 . 95 PHE CB C 38.8 0.1 1 355 . 95 PHE N N 116.7 0.1 1 356 . 96 SER H H 8.66 0.03 1 357 . 96 SER CA C 57.0 0.1 1 358 . 96 SER CB C 64.8 0.1 1 359 . 96 SER N N 119.3 0.1 1 360 . 97 CYS H H 8.54 0.03 1 361 . 97 CYS CA C 60.2 0.1 1 362 . 97 CYS CB C 29.8 0.1 1 363 . 97 CYS N N 125.9 0.1 1 364 . 98 ARG CA C 55.9 0.1 1 365 . 99 TRP H H 9.75 0.03 1 366 . 99 TRP CA C 56.4 0.1 1 367 . 99 TRP CB C 28.1 0.1 1 368 . 99 TRP N N 130.0 0.1 1 369 . 100 PRO CA C 64.1 0.1 1 370 . 101 SER H H 8.43 0.03 1 371 . 101 SER CA C 59.2 0.1 1 372 . 101 SER CB C 62.4 0.1 1 373 . 101 SER N N 112.8 0.1 1 374 . 102 CYS H H 8.23 0.03 1 375 . 102 CYS CA C 60.0 0.1 1 376 . 102 CYS CB C 30.9 0.1 1 377 . 102 CYS N N 125.7 0.1 1 378 . 103 GLN CA C 55.5 0.1 1 379 . 103 GLN CB C 27.5 0.1 1 380 . 104 LYS H H 8.27 0.03 1 381 . 104 LYS CA C 56.9 0.1 1 382 . 104 LYS CB C 31.4 0.1 1 383 . 104 LYS N N 122.3 0.1 1 384 . 105 LYS H H 7.39 0.03 1 385 . 105 LYS CA C 53.8 0.1 1 386 . 105 LYS CB C 34.7 0.1 1 387 . 105 LYS N N 119.0 0.1 1 388 . 106 PHE H H 8.81 0.03 1 389 . 106 PHE CA C 56.6 0.1 1 390 . 106 PHE CB C 43.6 0.1 1 391 . 106 PHE N N 115.7 0.1 1 392 . 107 ALA H H 9.31 0.03 1 393 . 107 ALA CA C 54.0 0.1 1 394 . 107 ALA CB C 19.1 0.1 1 395 . 107 ALA N N 123.6 0.1 1 396 . 108 ARG H H 7.98 0.03 1 397 . 108 ARG CA C 53.6 0.1 1 398 . 108 ARG CB C 34.6 0.1 1 399 . 108 ARG N N 113.7 0.1 1 400 . 109 SER H H 8.37 0.03 1 401 . 109 SER CA C 59.9 0.1 1 402 . 109 SER CB C 61.0 0.1 1 403 . 109 SER N N 120.3 0.1 1 404 . 110 ASP H H 8.56 0.03 1 405 . 110 ASP CA C 55.3 0.1 1 406 . 110 ASP CB C 38.8 0.1 1 407 . 110 ASP N N 118.5 0.1 1 408 . 111 GLU H H 6.96 0.03 1 409 . 111 GLU CA C 57.7 0.1 1 410 . 111 GLU CB C 29.8 0.1 1 411 . 111 GLU N N 120.8 0.1 1 412 . 112 LEU H H 6.71 0.03 1 413 . 112 LEU CA C 56.6 0.1 1 414 . 112 LEU CB C 39.3 0.1 1 415 . 112 LEU N N 120.9 0.1 1 416 . 113 VAL H H 7.57 0.03 1 417 . 113 VAL CA C 66.1 0.1 1 418 . 113 VAL CB C 30.9 0.1 1 419 . 113 VAL N N 119.2 0.1 1 420 . 114 ARG H H 7.22 0.03 1 421 . 114 ARG CA C 58.7 0.1 1 422 . 114 ARG CB C 29.4 0.1 1 423 . 114 ARG N N 117.4 0.1 1 424 . 115 HIS H H 7.46 0.03 1 425 . 115 HIS CA C 58.7 0.1 1 426 . 115 HIS CB C 28.2 0.1 1 427 . 115 HIS N N 117.4 0.1 1 428 . 116 HIS H H 9.04 0.03 1 429 . 116 HIS CA C 58.1 0.1 1 430 . 116 HIS CB C 28.5 0.1 1 431 . 116 HIS N N 119.1 0.1 1 432 . 117 ASN H H 7.65 0.03 1 433 . 117 ASN CA C 54.1 0.1 1 434 . 117 ASN CB C 37.5 0.1 1 435 . 117 ASN N N 115.5 0.1 1 436 . 118 MET H H 7.72 0.03 1 437 . 118 MET CA C 54.9 0.1 1 438 . 118 MET CB C 31.4 0.1 1 439 . 118 MET N N 117.6 0.1 1 440 . 119 HIS H H 6.88 0.03 1 441 . 119 HIS CA C 57.7 0.1 1 442 . 119 HIS CB C 27.7 0.1 1 443 . 119 HIS N N 124.5 0.1 1 stop_ save_