data_18764 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Phf19 links methylated lysine 36 of histone H3 to regulation of Polycomb activity ; _BMRB_accession_number 18764 _BMRB_flat_file_name bmr18764.str _Entry_type original _Submission_date 2012-10-04 _Accession_date 2012-10-04 _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 Lapinaite Audrone . . 2 Simon B. . . 3 Carlomagno T. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 3 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 381 "13C chemical shifts" 198 "15N chemical shifts" 59 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-18 update BMRB 'update entry citation' 2012-10-29 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Phf19 links methylated Lys36 of histone H3 to regulation of Polycomb activity.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23104054 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ballare Cecilia . . 2 Lange Martin . . 3 Lapinaite Audrone . . 4 Martin 'Gloria Mas' . . 5 Morey Lluis . . 6 Pascual Gloria . . 7 Liefke Robert . . 8 Simon Bernd . . 9 Shi Yang . . 10 Gozani Or . . 11 Carlomagno Teresa . . 12 Benitah 'Salvador Aznar' . . 13 'Di Croce' Luciano . . stop_ _Journal_abbreviation 'Nat. Struct. Mol. Biol.' _Journal_name_full 'Nature structural & molecular biology' _Journal_volume 19 _Journal_issue 12 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1257 _Page_last 1265 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Phf19 links methylated lysine 36 of histone H3 to regulation of Polycomb activity' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PHD FINGER PROTEIN 19' $PHD_FINGER_PROTEIN_19 'HISTONE H3' $HISTONE_H3 stop_ _System_molecular_weight 7973.1621 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PHD_FINGER_PROTEIN_19 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PHD_FINGER_PROTEIN_19 _Molecular_mass 6714.6566 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 58 _Mol_residue_sequence ; SKLTEGQYVLCRWTDGLYYL GKIKRVSSSKQSCLVTFEDN SKYWVLWKDIQHAGVPGE ; loop_ _Residue_seq_code _Residue_label 1 SER 2 LYS 3 LEU 4 THR 5 GLU 6 GLY 7 GLN 8 TYR 9 VAL 10 LEU 11 CYS 12 ARG 13 TRP 14 THR 15 ASP 16 GLY 17 LEU 18 TYR 19 TYR 20 LEU 21 GLY 22 LYS 23 ILE 24 LYS 25 ARG 26 VAL 27 SER 28 SER 29 SER 30 LYS 31 GLN 32 SER 33 CYS 34 LEU 35 VAL 36 THR 37 PHE 38 GLU 39 ASP 40 ASN 41 SER 42 LYS 43 TYR 44 TRP 45 VAL 46 LEU 47 TRP 48 LYS 49 ASP 50 ILE 51 GLN 52 HIS 53 ALA 54 GLY 55 VAL 56 PRO 57 GLY 58 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 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 PDB 2E5Q "Solution Structure Of The Tudor Domain Of Phd Finger Protein 19, Isoform B [homo Sapiens]" 100.00 63 98.28 98.28 5.29e-33 PDB 4BD3 "Phf19 Links Methylated Lysine 36 Of Histone H3 To Regulation Of Polycomb Activity" 100.00 58 100.00 100.00 9.40e-34 DBJ BAG53700 "unnamed protein product [Homo sapiens]" 100.00 563 100.00 100.00 2.56e-31 DBJ BAI45704 "PHD finger protein 19 [synthetic construct]" 100.00 580 100.00 100.00 2.83e-31 EMBL CAE45832 "hypothetical protein [Homo sapiens]" 100.00 621 100.00 100.00 4.41e-31 GB AAH22374 "PHD finger protein 19 [Homo sapiens]" 100.00 207 100.00 100.00 2.78e-33 GB AAI08664 "PHF19 protein [Homo sapiens]" 100.00 130 100.00 100.00 1.19e-33 GB AAI25077 "PHD finger protein 19 [Homo sapiens]" 100.00 580 100.00 100.00 2.83e-31 GB AAI25078 "PHD finger protein 19 [Homo sapiens]" 100.00 580 100.00 100.00 2.83e-31 GB ADQ32204 "PHD finger protein 19 [synthetic construct]" 100.00 207 100.00 100.00 2.78e-33 REF NP_001009936 "PHD finger protein 19 isoform b [Homo sapiens]" 100.00 207 100.00 100.00 2.78e-33 REF NP_001179644 "PHD finger protein 19 [Bos taurus]" 100.00 580 100.00 100.00 2.19e-31 REF NP_001273769 "PHD finger protein 19 isoform c [Homo sapiens]" 100.00 599 100.00 100.00 3.53e-31 REF NP_001273772 "PHD finger protein 19 isoform e [Homo sapiens]" 100.00 130 100.00 100.00 1.19e-33 REF NP_056466 "PHD finger protein 19 isoform a [Homo sapiens]" 100.00 580 100.00 100.00 2.83e-31 SP Q5T6S3 "RecName: Full=PHD finger protein 19; AltName: Full=Polycomb-like protein 3; Short=hPCL3" 100.00 580 100.00 100.00 2.83e-31 TPG DAA26446 "TPA: PHD finger protein 19 [Bos taurus]" 100.00 692 100.00 100.00 3.77e-31 stop_ save_ save_HISTONE_H3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HISTONE_H3 _Molecular_mass 1258.5055 _Mol_thiol_state 'not present' _Details . _Residue_count 11 _Mol_residue_sequence ATGGVXKPHRY loop_ _Residue_seq_code _Residue_label 1 ALA 2 THR 3 GLY 4 GLY 5 VAL 6 M3L 7 LYS 8 PRO 9 HIS 10 ARG 11 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 UNP H31_HUMAN P68431 . . . . . stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_M3L _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common N-TRIMETHYLLYSINE _BMRB_code M3L _PDB_code M3L _Standard_residue_derivative . _Molecular_mass 189.275 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CD CD C . 0 . ? CE CE C . 0 . ? CG CG C . 0 . ? CM1 CM1 C . 0 . ? CM2 CM2 C . 0 . ? CM3 CM3 C . 0 . ? H H H . 0 . ? H2 H2 H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HD2 HD2 H . 0 . ? HD3 HD3 H . 0 . ? HE2 HE2 H . 0 . ? HE3 HE3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HM11 HM11 H . 0 . ? HM12 HM12 H . 0 . ? HM13 HM13 H . 0 . ? HM21 HM21 H . 0 . ? HM22 HM22 H . 0 . ? HM23 HM23 H . 0 . ? HM31 HM31 H . 0 . ? HM32 HM32 H . 0 . ? HM33 HM33 H . 0 . ? HXT HXT H . 0 . ? N N N . 0 . ? NZ NZ N . 1 . ? O O O . 0 . ? OXT OXT O . 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 CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD ? ? SING CG HG2 ? ? SING CG HG3 ? ? SING CD CE ? ? SING CD HD2 ? ? SING CD HD3 ? ? SING CE NZ ? ? SING CE HE2 ? ? SING CE HE3 ? ? SING NZ CM1 ? ? SING NZ CM2 ? ? SING NZ CM3 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? SING CM1 HM11 ? ? SING CM1 HM12 ? ? SING CM1 HM13 ? ? SING CM2 HM21 ? ? SING CM2 HM22 ? ? SING CM2 HM23 ? ? SING CM3 HM31 ? ? SING CM3 HM32 ? ? SING CM3 HM33 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PHD_FINGER_PROTEIN_19 Human 9606 Eukaryota Metazoa Homo sapiens $HISTONE_H3 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 _Variant _Vector_type _Vector_name _Details $PHD_FINGER_PROTEIN_19 'recombinant technology' 'ESCHERICHIA COLI BL21' . . BL21 'Rosetta 2' pET-MCN . . $HISTONE_H3 'chemical synthesis' . . . . . . . 'SYNTHETIC. THE SEQUENCE ATGGVKKPHRY. OCCURS NATURALLY IN HUMANS ON HISTONE 3' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '0.1-0.6 mmol/l' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $PHD_FINGER_PROTEIN_19 . mM 0.1 0.6 '[U-13C; U-15N]' $HISTONE_H3 . mM 0.1 0.6 '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_AutoDep _Saveframe_category software _Name AutoDep _Version 4.3 loop_ _Vendor _Address _Electronic_address PDBe . . stop_ loop_ _Task collection stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version 1.2 loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version any loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_Bruker_Avance-600 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_TRIPLE_RESONANCE_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'TRIPLE RESONANCE' _Sample_label $sample_1 save_ save_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ save_EDITED-FILTERED_3 _Saveframe_category NMR_applied_experiment _Experiment_name EDITED-FILTERED _Sample_label $sample_1 save_ save_EDITED_-FILTERED_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'EDITED -FILTERED' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'pH [7.0], temp [298], pressure [1.0], ionStrength [200.0]' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 200.000 . mM pH 7.000 . pH pressure 1.000 . atm temperature 298.000 . 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 HDO H 1 HDO ppm 4.773 internal indirect . . . 1 HDO C 13 HDO ppm 4.773 internal indirect . . . 0.25144953 HDO N 15 HDO ppm 4.773 internal 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 'Origin nmrStar file /ebi/msd/pdb_root/Processing/prepare/4bd3/ebi/submit_tud_pep_ppm3_chainA.str.csh' loop_ _Experiment_label 'TRIPLE RESONANCE' NOESY EDITED-FILTERED 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 'PHD FINGER PROTEIN 19' _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 . 1 SER HA H 4.109 . 1 2 . 1 SER CB C 63.490 . 1 3 . 1 SER HB2 H 3.533 . 1 4 . 1 SER CA C 58.568 . 1 5 . 2 LYS N N 122.730 . 1 6 . 2 LYS H H 8.100 . 1 7 . 2 LYS CA C 55.833 . 1 8 . 2 LYS HA H 4.135 . 1 9 . 2 LYS CB C 32.590 . 1 10 . 2 LYS HB3 H 1.712 . 2 11 . 2 LYS HB2 H 1.566 . 2 12 . 2 LYS CG C 24.660 . 1 13 . 2 LYS HG3 H 1.285 . 2 14 . 2 LYS HG2 H 1.234 . 2 15 . 2 LYS CD C 28.762 . 1 16 . 2 LYS HD2 H 1.539 . 1 17 . 2 LYS CE C 42.161 . 1 18 . 2 LYS HE2 H 2.861 . 1 19 . 3 LEU N N 123.170 . 1 20 . 3 LEU H H 7.658 . 1 21 . 3 LEU CA C 54.193 . 1 22 . 3 LEU HA H 4.478 . 1 23 . 3 LEU CB C 42.161 . 1 24 . 3 LEU HB3 H 0.825 . 2 25 . 3 LEU HB2 H 1.257 . 2 26 . 3 LEU CG C 26.301 . 1 27 . 3 LEU HG H 1.189 . 1 28 . 3 LEU CD1 C 23.020 . 2 29 . 3 LEU HD1 H 0.469 . 2 30 . 3 LEU CD2 C 25.481 . 2 31 . 3 LEU HD2 H 0.160 . 2 32 . 4 THR N N 114.152 . 1 33 . 4 THR H H 7.723 . 1 34 . 4 THR CA C 59.935 . 1 35 . 4 THR HA H 4.410 . 1 36 . 4 THR CB C 71.967 . 1 37 . 4 THR HB H 3.897 . 1 38 . 4 THR CG2 C 20.832 . 1 39 . 4 THR HG2 H 1.097 . 1 40 . 5 GLU N N 122.290 . 1 41 . 5 GLU H H 8.643 . 1 42 . 5 GLU CA C 58.568 . 1 43 . 5 GLU HA H 3.423 . 1 44 . 5 GLU CB C 29.036 . 1 45 . 5 GLU HB3 H 1.856 . 2 46 . 5 GLU HB2 H 1.819 . 2 47 . 5 GLU CG C 36.692 . 1 48 . 5 GLU HG3 H 2.288 . 2 49 . 5 GLU HG2 H 2.139 . 2 50 . 6 GLY N N 112.612 . 1 51 . 6 GLY H H 9.032 . 1 52 . 6 GLY CA C 44.759 . 1 53 . 6 GLY HA3 H 3.292 . 2 54 . 6 GLY HA2 H 4.279 . 2 55 . 7 GLN N N 119.431 . 1 56 . 7 GLN H H 7.341 . 1 57 . 7 GLN CA C 55.833 . 1 58 . 7 GLN HA H 4.221 . 1 59 . 7 GLN CB C 30.129 . 1 60 . 7 GLN HB3 H 2.119 . 2 61 . 7 GLN HB2 H 2.026 . 2 62 . 7 GLN CG C 33.958 . 1 63 . 7 GLN HG3 H 2.326 . 2 64 . 7 GLN HG2 H 2.384 . 2 65 . 7 GLN NE2 N 110.632 . 1 66 . 7 GLN HE21 H 7.437 . 1 67 . 7 GLN HE22 H 6.651 . 1 68 . 8 TYR N N 122.510 . 1 69 . 8 TYR H H 8.742 . 1 70 . 8 TYR CA C 58.021 . 1 71 . 8 TYR HA H 5.263 . 1 72 . 8 TYR CB C 39.153 . 1 73 . 8 TYR HB3 H 2.837 . 2 74 . 8 TYR HB2 H 2.702 . 2 75 . 8 TYR CD1 C 133.219 . 3 76 . 8 TYR HD1 H 7.058 . 3 77 . 8 TYR CE1 C 118.179 . 3 78 . 8 TYR HE1 H 6.776 . 3 79 . 9 VAL N N 114.812 . 1 80 . 9 VAL H H 9.179 . 1 81 . 9 VAL CA C 58.841 . 1 82 . 9 VAL HA H 4.726 . 1 83 . 9 VAL CB C 36.419 . 1 84 . 9 VAL HB H 2.118 . 1 85 . 9 VAL CG1 C 18.098 . 2 86 . 9 VAL HG1 H 0.484 . 2 87 . 9 VAL CG2 C 23.567 . 2 88 . 9 VAL HG2 H 0.693 . 2 89 . 10 LEU N N 121.630 . 1 90 . 10 LEU H H 8.767 . 1 91 . 10 LEU CA C 53.646 . 1 92 . 10 LEU HA H 4.930 . 1 93 . 10 LEU CB C 44.075 . 1 94 . 10 LEU HB3 H 1.245 . 2 95 . 10 LEU HB2 H 1.557 . 2 96 . 10 LEU CG C 26.898 . 1 97 . 10 LEU HG H 1.357 . 1 98 . 10 LEU CD1 C 24.660 . 2 99 . 10 LEU HD1 H 0.493 . 2 100 . 10 LEU CD2 C 23.020 . 2 101 . 10 LEU HD2 H 0.419 . 2 102 . 11 CYS N N 120.970 . 1 103 . 11 CYS H H 9.296 . 1 104 . 11 CYS CA C 57.201 . 1 105 . 11 CYS HA H 5.452 . 1 106 . 11 CYS CB C 30.676 . 1 107 . 11 CYS HB3 H 2.931 . 2 108 . 11 CYS HB2 H 3.296 . 2 109 . 12 ARG N N 128.669 . 1 110 . 12 ARG H H 9.444 . 1 111 . 12 ARG CA C 56.380 . 1 112 . 12 ARG HA H 3.844 . 1 113 . 12 ARG CB C 30.129 . 1 114 . 12 ARG HB3 H 1.290 . 2 115 . 12 ARG HB2 H 1.699 . 2 116 . 12 ARG CG C 27.121 . 1 117 . 12 ARG HG3 H 1.446 . 2 118 . 12 ARG HG2 H 0.698 . 2 119 . 12 ARG CD C 43.255 . 1 120 . 12 ARG HD3 H 3.049 . 2 121 . 12 ARG HD2 H 3.017 . 2 122 . 13 TRP N N 129.989 . 1 123 . 13 TRP H H 9.057 . 1 124 . 13 TRP CA C 54.193 . 1 125 . 13 TRP HA H 5.100 . 1 126 . 13 TRP CB C 31.770 . 1 127 . 13 TRP HB3 H 3.983 . 2 128 . 13 TRP HB2 H 3.041 . 2 129 . 13 TRP HD1 H 6.769 . 1 130 . 13 TRP CE3 C 120.094 . 1 131 . 13 TRP HE3 H 7.324 . 1 132 . 13 TRP CZ2 C 114.625 . 1 133 . 13 TRP HZ2 H 6.885 . 1 134 . 13 TRP CZ3 C 122.555 . 1 135 . 13 TRP HZ3 H 6.652 . 1 136 . 14 THR N N 114.592 . 1 137 . 14 THR H H 6.112 . 1 138 . 14 THR CA C 63.490 . 1 139 . 14 THR HA H 3.710 . 1 140 . 14 THR CB C 67.592 . 1 141 . 14 THR HB H 3.880 . 1 142 . 14 THR CG2 C 21.652 . 1 143 . 14 THR HG2 H 0.641 . 1 144 . 15 ASP N N 118.991 . 1 145 . 15 ASP H H 7.618 . 1 146 . 15 ASP CA C 53.099 . 1 147 . 15 ASP HA H 4.441 . 1 148 . 15 ASP CB C 39.973 . 1 149 . 15 ASP HB3 H 3.067 . 2 150 . 15 ASP HB2 H 2.658 . 2 151 . 16 GLY N N 108.433 . 1 152 . 16 GLY H H 8.179 . 1 153 . 16 GLY CA C 45.169 . 1 154 . 16 GLY HA3 H 3.467 . 2 155 . 16 GLY HA2 H 4.135 . 2 156 . 17 LEU N N 122.510 . 1 157 . 17 LEU H H 8.177 . 1 158 . 17 LEU CA C 53.099 . 1 159 . 17 LEU HA H 4.543 . 1 160 . 17 LEU CB C 41.614 . 1 161 . 17 LEU HB3 H 1.120 . 2 162 . 17 LEU HB2 H 1.959 . 2 163 . 17 LEU CG C 27.121 . 1 164 . 17 LEU HG H 1.350 . 1 165 . 17 LEU CD1 C 25.207 . 2 166 . 17 LEU HD1 H 0.780 . 2 167 . 17 LEU CD2 C 22.473 . 2 168 . 17 LEU HD2 H 0.796 . 2 169 . 18 TYR N N 116.571 . 1 170 . 18 TYR H H 8.393 . 1 171 . 18 TYR CA C 56.927 . 1 172 . 18 TYR HA H 5.283 . 1 173 . 18 TYR CB C 40.794 . 1 174 . 18 TYR HB3 H 2.482 . 2 175 . 18 TYR HB2 H 2.888 . 2 176 . 18 TYR CD1 C 132.946 . 3 177 . 18 TYR HD1 H 6.936 . 3 178 . 18 TYR CE1 C 118.179 . 3 179 . 18 TYR HE1 H 6.734 . 3 180 . 19 TYR N N 118.111 . 1 181 . 19 TYR H H 8.920 . 1 182 . 19 TYR CA C 57.471 . 1 183 . 19 TYR HA H 5.062 . 1 184 . 19 TYR CB C 42.620 . 1 185 . 19 TYR HB3 H 2.948 . 2 186 . 19 TYR HB2 H 2.953 . 2 187 . 19 TYR CD1 C 133.492 . 3 188 . 19 TYR HD1 H 6.780 . 3 189 . 19 TYR CE1 C 119.820 . 3 190 . 19 TYR HE1 H 6.973 . 3 191 . 20 LEU N N 126.909 . 1 192 . 20 LEU H H 9.523 . 1 193 . 20 LEU CA C 55.286 . 1 194 . 20 LEU HA H 4.904 . 1 195 . 20 LEU CB C 43.528 . 1 196 . 20 LEU HB3 H 1.351 . 2 197 . 20 LEU HB2 H 1.878 . 2 198 . 20 LEU CG C 27.121 . 1 199 . 20 LEU HG H 1.546 . 1 200 . 20 LEU CD1 C 25.754 . 2 201 . 20 LEU HD1 H 0.753 . 2 202 . 20 LEU CD2 C 24.114 . 2 203 . 20 LEU HD2 H 0.783 . 2 204 . 21 GLY N N 115.471 . 1 205 . 21 GLY H H 9.487 . 1 206 . 21 GLY CA C 44.622 . 1 207 . 21 GLY HA3 H 2.902 . 2 208 . 21 GLY HA2 H 4.611 . 2 209 . 22 LYS N N 120.531 . 1 210 . 22 LYS H H 8.311 . 1 211 . 22 LYS CA C 53.646 . 1 212 . 22 LYS HA H 4.652 . 1 213 . 22 LYS CB C 35.572 . 1 214 . 22 LYS HB3 H 1.039 . 2 215 . 22 LYS HB2 H 1.271 . 2 216 . 22 LYS CG C 24.387 . 1 217 . 22 LYS HG3 H 0.381 . 2 218 . 22 LYS HG2 H 0.600 . 2 219 . 22 LYS CD C 29.309 . 1 220 . 22 LYS HD3 H 1.282 . 2 221 . 22 LYS HD2 H 1.271 . 2 222 . 22 LYS CE C 41.341 . 1 223 . 22 LYS HE3 H 2.612 . 2 224 . 22 LYS HE2 H 2.606 . 2 225 . 23 ILE N N 125.810 . 1 226 . 23 ILE H H 8.748 . 1 227 . 23 ILE CA C 64.037 . 1 228 . 23 ILE HA H 3.576 . 1 229 . 23 ILE CB C 37.512 . 1 230 . 23 ILE HB H 1.956 . 1 231 . 23 ILE CG1 C 28.489 . 1 232 . 23 ILE HG13 H 0.672 . 2 233 . 23 ILE HG12 H 1.728 . 2 234 . 23 ILE CG2 C 18.371 . 1 235 . 23 ILE HG2 H 0.562 . 1 236 . 23 ILE CD1 C 14.816 . 1 237 . 23 ILE HD1 H 0.829 . 1 238 . 24 LYS N N 131.969 . 1 239 . 24 LYS H H 9.729 . 1 240 . 24 LYS CA C 56.107 . 1 241 . 24 LYS HA H 4.387 . 1 242 . 24 LYS CB C 33.137 . 1 243 . 24 LYS HB3 H 1.487 . 2 244 . 24 LYS HB2 H 1.488 . 2 245 . 24 LYS CG C 24.660 . 1 246 . 24 LYS HG2 H 1.262 . 1 247 . 24 LYS CD C 27.668 . 1 248 . 24 LYS HD3 H 1.488 . 2 249 . 24 LYS HD2 H 1.402 . 2 250 . 24 LYS CE C 41.614 . 1 251 . 24 LYS HE3 H 2.905 . 1 252 . 24 LYS HE2 H 2.905 . 1 253 . 25 ARG N N 115.252 . 1 254 . 25 ARG H H 7.382 . 1 255 . 25 ARG CA C 55.013 . 1 256 . 25 ARG HA H 4.652 . 1 257 . 25 ARG CB C 34.778 . 1 258 . 25 ARG HB3 H 1.699 . 2 259 . 25 ARG HB2 H 1.615 . 2 260 . 25 ARG CG C 27.121 . 1 261 . 25 ARG HG3 H 1.615 . 2 262 . 25 ARG HG2 H 1.574 . 2 263 . 25 ARG CD C 43.255 . 1 264 . 25 ARG HD3 H 3.335 . 2 265 . 25 ARG HD2 H 3.252 . 2 266 . 26 VAL N N 126.250 . 1 267 . 26 VAL H H 9.550 . 1 268 . 26 VAL CA C 62.396 . 1 269 . 26 VAL HA H 4.485 . 1 270 . 26 VAL CB C 33.958 . 1 271 . 26 VAL HB H 2.204 . 1 272 . 26 VAL CG1 C 21.106 . 2 273 . 26 VAL HG1 H 0.851 . 2 274 . 26 VAL CG2 C 22.199 . 2 275 . 26 VAL HG2 H 1.197 . 2 276 . 27 SER N N 120.751 . 1 277 . 27 SER H H 8.987 . 1 278 . 27 SER CA C 55.560 . 1 279 . 27 SER HA H 5.110 . 1 280 . 27 SER CB C 63.490 . 1 281 . 27 SER HB3 H 3.697 . 2 282 . 27 SER HB2 H 3.781 . 2 283 . 28 SER CA C 61.302 . 1 284 . 28 SER HA H 4.547 . 1 285 . 28 SER CB C 62.123 . 1 286 . 28 SER HB2 H 4.099 . 1 287 . 29 SER CA C 60.755 . 1 288 . 29 SER HA H 4.117 . 1 289 . 29 SER CB C 62.123 . 1 290 . 29 SER HB2 H 3.765 . 1 291 . 30 LYS N N 117.891 . 1 292 . 30 LYS H H 7.306 . 1 293 . 30 LYS CA C 55.560 . 1 294 . 30 LYS HA H 4.586 . 1 295 . 30 LYS CB C 32.317 . 1 296 . 30 LYS HB3 H 1.523 . 2 297 . 30 LYS HB2 H 1.139 . 2 298 . 30 LYS CG C 24.660 . 1 299 . 30 LYS HG3 H 1.003 . 2 300 . 30 LYS HG2 H 1.064 . 2 301 . 30 LYS CD C 28.215 . 1 302 . 30 LYS HD2 H 0.875 . 1 303 . 30 LYS CE C 41.341 . 1 304 . 30 LYS HE2 H 2.253 . 1 305 . 31 GLN N N 119.431 . 1 306 . 31 GLN H H 7.335 . 1 307 . 31 GLN HA H 3.778 . 1 308 . 31 GLN HB3 H 1.394 . 2 309 . 31 GLN HB2 H 1.791 . 2 310 . 31 GLN CG C 33.958 . 1 311 . 31 GLN HG3 H 1.869 . 2 312 . 31 GLN HG2 H 1.791 . 2 313 . 31 GLN NE2 N 112.612 . 1 314 . 31 GLN HE21 H 7.469 . 1 315 . 31 GLN HE22 H 6.736 . 1 316 . 32 SER N N 109.533 . 1 317 . 32 SER H H 7.417 . 1 318 . 32 SER CA C 57.474 . 1 319 . 32 SER HA H 5.314 . 1 320 . 32 SER CB C 68.683 . 1 321 . 32 SER HB3 H 3.462 . 2 322 . 32 SER HB2 H 3.740 . 2 323 . 33 CYS N N 119.431 . 1 324 . 33 CYS H H 9.810 . 1 325 . 33 CYS CA C 56.927 . 1 326 . 33 CYS HA H 5.378 . 1 327 . 33 CYS CB C 32.043 . 1 328 . 33 CYS HB3 H 2.494 . 2 329 . 33 CYS HB2 H 2.896 . 2 330 . 34 LEU N N 129.769 . 1 331 . 34 LEU H H 8.583 . 1 332 . 34 LEU CA C 53.646 . 1 333 . 34 LEU HA H 3.766 . 1 334 . 34 LEU CB C 41.067 . 1 335 . 34 LEU HB3 H -1.136 . 2 336 . 34 LEU HB2 H 0.925 . 2 337 . 34 LEU CG C 26.301 . 1 338 . 34 LEU HG H 0.591 . 1 339 . 34 LEU CD1 C 20.559 . 2 340 . 34 LEU HD1 H -0.321 . 2 341 . 34 LEU CD2 C 25.481 . 2 342 . 34 LEU HD2 H 0.390 . 2 343 . 35 VAL N N 130.209 . 1 344 . 35 VAL H H 8.852 . 1 345 . 35 VAL CA C 60.755 . 1 346 . 35 VAL HA H 4.335 . 1 347 . 35 VAL CB C 34.778 . 1 348 . 35 VAL HB H 1.632 . 1 349 . 35 VAL CG1 C 21.379 . 2 350 . 35 VAL HG1 H 0.003 . 2 351 . 35 VAL CG2 C 21.106 . 2 352 . 35 VAL HG2 H 0.596 . 2 353 . 36 THR N N 118.771 . 1 354 . 36 THR H H 8.391 . 1 355 . 36 THR CA C 59.662 . 1 356 . 36 THR HA H 5.086 . 1 357 . 36 THR CB C 69.779 . 1 358 . 36 THR HB H 3.800 . 1 359 . 36 THR CG2 C 21.652 . 1 360 . 36 THR HG2 H 1.157 . 1 361 . 37 PHE N N 126.470 . 1 362 . 37 PHE H H 9.014 . 1 363 . 37 PHE CA C 58.294 . 1 364 . 37 PHE HA H 4.940 . 1 365 . 37 PHE CB C 39.700 . 1 366 . 37 PHE HB3 H 2.960 . 2 367 . 37 PHE HB2 H 3.427 . 2 368 . 37 PHE CD1 C 132.399 . 3 369 . 37 PHE HD1 H 7.295 . 3 370 . 37 PHE CE1 C 130.758 . 3 371 . 37 PHE HE1 H 7.060 . 3 372 . 37 PHE CZ C 129.117 . 1 373 . 37 PHE HZ H 6.986 . 1 374 . 38 GLU N N 120.531 . 1 375 . 38 GLU H H 9.805 . 1 376 . 38 GLU CA C 59.935 . 1 377 . 38 GLU HA H 4.096 . 1 378 . 38 GLU CB C 30.676 . 1 379 . 38 GLU HB3 H 2.216 . 2 380 . 38 GLU HB2 H 2.103 . 2 381 . 38 GLU CG C 37.512 . 1 382 . 38 GLU HG3 H 2.544 . 2 383 . 38 GLU HG2 H 2.341 . 2 384 . 39 ASP N N 115.471 . 1 385 . 39 ASP H H 7.961 . 1 386 . 39 ASP CA C 52.825 . 1 387 . 39 ASP HA H 4.452 . 1 388 . 39 ASP CB C 39.700 . 1 389 . 39 ASP HB3 H 2.342 . 2 390 . 39 ASP HB2 H 3.021 . 2 391 . 40 ASN N N 113.712 . 1 392 . 40 ASN H H 8.415 . 1 393 . 40 ASN CA C 55.013 . 1 394 . 40 ASN HA H 4.259 . 1 395 . 40 ASN CB C 37.512 . 1 396 . 40 ASN HB2 H 3.019 . 1 397 . 40 ASN ND2 N 113.272 . 1 398 . 40 ASN HD21 H 7.551 . 1 399 . 40 ASN HD22 H 6.850 . 1 400 . 41 SER N N 117.451 . 1 401 . 41 SER H H 8.016 . 1 402 . 41 SER CA C 59.662 . 1 403 . 41 SER HA H 5.088 . 1 404 . 41 SER CB C 63.832 . 1 405 . 41 SER HB2 H 3.800 . 1 406 . 42 LYS N N 118.771 . 1 407 . 42 LYS H H 7.851 . 1 408 . 42 LYS CA C 54.740 . 1 409 . 42 LYS HA H 5.664 . 1 410 . 42 LYS CB C 35.051 . 1 411 . 42 LYS HB2 H 1.309 . 1 412 . 42 LYS CG C 23.931 . 1 413 . 42 LYS HG3 H 1.322 . 2 414 . 42 LYS HG2 H 1.235 . 2 415 . 42 LYS CD C 29.582 . 1 416 . 42 LYS HD3 H 1.319 . 2 417 . 42 LYS HD2 H 1.444 . 2 418 . 42 LYS CE C 41.614 . 1 419 . 42 LYS HE2 H 2.832 . 1 420 . 43 TYR N N 119.211 . 1 421 . 43 TYR H H 8.510 . 1 422 . 43 TYR CB C 43.802 . 1 423 . 43 TYR HB3 H 2.658 . 2 424 . 43 TYR HB2 H 3.427 . 2 425 . 43 TYR CD1 C 133.492 . 3 426 . 43 TYR HD1 H 7.155 . 3 427 . 43 TYR CE1 C 118.179 . 3 428 . 43 TYR HE1 H 6.804 . 3 429 . 44 TRP N N 123.830 . 1 430 . 44 TRP H H 9.125 . 1 431 . 44 TRP CA C 57.474 . 1 432 . 44 TRP HA H 5.068 . 1 433 . 44 TRP CB C 28.762 . 1 434 . 44 TRP HB3 H 3.122 . 2 435 . 44 TRP HB2 H 3.009 . 2 436 . 44 TRP CD1 C 127.750 . 1 437 . 44 TRP HD1 H 7.335 . 1 438 . 44 TRP NE1 N 130.426 . 1 439 . 44 TRP HE1 H 10.288 . 1 440 . 44 TRP CE3 C 120.640 . 1 441 . 44 TRP HE3 H 7.217 . 1 442 . 44 TRP CZ2 C 114.898 . 1 443 . 44 TRP HZ2 H 7.456 . 1 444 . 44 TRP CZ3 C 121.734 . 1 445 . 44 TRP HZ3 H 6.578 . 1 446 . 44 TRP CH2 C 123.375 . 1 447 . 44 TRP HH2 H 6.927 . 1 448 . 45 VAL N N 127.129 . 1 449 . 45 VAL H H 9.780 . 1 450 . 45 VAL CA C 61.029 . 1 451 . 45 VAL HA H 4.427 . 1 452 . 45 VAL CB C 35.598 . 1 453 . 45 VAL HB H 2.020 . 1 454 . 45 VAL CG1 C 21.106 . 2 455 . 45 VAL HG1 H 1.208 . 2 456 . 45 VAL CG2 C 21.598 . 2 457 . 45 VAL HG2 H 1.264 . 2 458 . 46 LEU N N 128.669 . 1 459 . 46 LEU H H 9.358 . 1 460 . 46 LEU CA C 55.560 . 1 461 . 46 LEU HA H 4.585 . 1 462 . 46 LEU CB C 42.434 . 1 463 . 46 LEU HB2 H 1.803 . 1 464 . 46 LEU CG C 27.121 . 1 465 . 46 LEU HG H 1.874 . 1 466 . 46 LEU CD1 C 22.473 . 2 467 . 46 LEU HD1 H 0.879 . 2 468 . 46 LEU CD2 C 26.028 . 2 469 . 46 LEU HD2 H 0.949 . 2 470 . 47 TRP N N 122.290 . 1 471 . 47 TRP H H 9.012 . 1 472 . 47 TRP CA C 58.294 . 1 473 . 47 TRP HA H 4.477 . 1 474 . 47 TRP CB C 28.489 . 1 475 . 47 TRP HB3 H 3.268 . 2 476 . 47 TRP HB2 H 3.187 . 2 477 . 47 TRP CD1 C 122.555 . 1 478 . 47 TRP HD1 H 6.885 . 1 479 . 47 TRP CE3 C 121.734 . 1 480 . 47 TRP HE3 H 7.581 . 1 481 . 47 TRP CZ2 C 114.078 . 1 482 . 47 TRP HZ2 H 7.101 . 1 483 . 47 TRP CZ3 C 122.828 . 1 484 . 47 TRP HZ3 H 7.206 . 1 485 . 47 TRP CH2 C 125.836 . 1 486 . 47 TRP HH2 H 7.277 . 1 487 . 48 LYS N N 114.592 . 1 488 . 48 LYS H H 8.083 . 1 489 . 48 LYS CA C 58.021 . 1 490 . 48 LYS HA H 4.342 . 1 491 . 48 LYS CB C 31.497 . 1 492 . 48 LYS HB3 H 1.929 . 2 493 . 48 LYS HB2 H 1.856 . 2 494 . 48 LYS CG C 23.840 . 1 495 . 48 LYS HG3 H 1.442 . 2 496 . 48 LYS HG2 H 1.354 . 2 497 . 48 LYS CD C 29.039 . 1 498 . 48 LYS HD3 H 1.727 . 2 499 . 48 LYS HD2 H 1.632 . 2 500 . 48 LYS CE C 41.614 . 1 501 . 48 LYS HE3 H 2.988 . 1 502 . 48 LYS HE2 H 2.988 . 1 503 . 49 ASP N N 120.531 . 1 504 . 49 ASP H H 8.105 . 1 505 . 49 ASP CA C 54.466 . 1 506 . 49 ASP HA H 5.047 . 1 507 . 49 ASP CB C 42.434 . 1 508 . 49 ASP HB3 H 2.854 . 2 509 . 49 ASP HB2 H 3.370 . 2 510 . 50 ILE N N 120.970 . 1 511 . 50 ILE H H 7.673 . 1 512 . 50 ILE CA C 61.302 . 1 513 . 50 ILE HA H 4.905 . 1 514 . 50 ILE CB C 39.973 . 1 515 . 50 ILE HB H 1.889 . 1 516 . 50 ILE CG1 C 28.215 . 1 517 . 50 ILE HG13 H 1.053 . 2 518 . 50 ILE HG12 H 2.070 . 2 519 . 50 ILE CG2 C 17.824 . 1 520 . 50 ILE HG2 H 0.722 . 1 521 . 50 ILE CD1 C 14.543 . 1 522 . 50 ILE HD1 H 0.823 . 1 523 . 51 GLN N N 126.030 . 1 524 . 51 GLN H H 9.097 . 1 525 . 51 GLN CA C 53.919 . 1 526 . 51 GLN HA H 4.633 . 1 527 . 51 GLN CB C 31.770 . 1 528 . 51 GLN HB3 H 2.012 . 2 529 . 51 GLN HB2 H 1.810 . 2 530 . 51 GLN CG C 33.411 . 1 531 . 51 GLN HG3 H 2.196 . 2 532 . 51 GLN HG2 H 2.152 . 2 533 . 51 GLN NE2 N 111.292 . 1 534 . 51 GLN HE21 H 7.037 . 1 535 . 51 GLN HE22 H 6.518 . 1 536 . 52 HIS N N 122.070 . 1 537 . 52 HIS H H 8.637 . 1 538 . 52 HIS CA C 57.201 . 1 539 . 52 HIS HA H 4.452 . 1 540 . 52 HIS CB C 30.676 . 1 541 . 52 HIS HB3 H 3.027 . 2 542 . 52 HIS HB2 H 2.966 . 2 543 . 52 HIS HD2 H 6.931 . 1 544 . 52 HIS HE2 H 7.595 . 1 545 . 53 ALA N N 125.370 . 1 546 . 53 ALA H H 8.198 . 1 547 . 53 ALA CA C 52.005 . 1 548 . 53 ALA HA H 4.290 . 1 549 . 53 ALA CB C 19.465 . 1 550 . 53 ALA HB H 1.160 . 1 551 . 54 GLY N N 108.653 . 1 552 . 54 GLY H H 8.297 . 1 553 . 54 GLY CA C 45.282 . 1 554 . 54 GLY HA3 H 3.888 . 1 555 . 54 GLY HA2 H 3.888 . 1 556 . 55 VAL N N 120.476 . 1 557 . 55 VAL H H 7.898 . 1 558 . 55 VAL CA C 59.662 . 1 559 . 55 VAL HA H 4.239 . 1 560 . 55 VAL CB C 32.590 . 1 561 . 55 VAL HB H 1.952 . 1 562 . 55 VAL HG1 H 0.812 . 2 563 . 55 VAL CG2 C 20.285 . 1 564 . 55 VAL HG2 H 0.851 . 2 565 . 56 PRO CA C 63.490 . 1 566 . 56 PRO HA H 4.239 . 1 567 . 56 PRO CB C 31.770 . 1 568 . 56 PRO HB2 H 2.169 . 1 569 . 56 PRO CG C 27.395 . 1 570 . 56 PRO HG2 H 1.845 . 1 571 . 56 PRO CD C 50.911 . 1 572 . 56 PRO HD3 H 3.477 . 2 573 . 56 PRO HD2 H 3.674 . 2 574 . 57 GLY N N 110.412 . 1 575 . 57 GLY H H 8.377 . 1 576 . 57 GLY CA C 44.896 . 1 577 . 57 GLY HA3 H 4.001 . 2 578 . 57 GLY HA2 H 3.903 . 2 579 . 58 GLU N N 125.810 . 1 580 . 58 GLU H H 7.782 . 1 581 . 58 GLU HA H 4.089 . 1 582 . 58 GLU CB C 31.223 . 1 583 . 58 GLU HB2 H 2.010 . 1 584 . 58 GLU CG C 36.692 . 1 585 . 58 GLU HG2 H 2.150 . 1 586 . 58 GLU CA C 57.748 . 1 stop_ save_ save_assigned_chem_shift_list_1_2_1 _Saveframe_category assigned_chemical_shifts _Details 'Origin nmrStar file /ebi/msd/pdb_root/Processing/prepare/4bd3/ebi/submit_tud_pep_ppm3_chainB.str.csh' loop_ _Experiment_label 'TRIPLE RESONANCE' NOESY EDITED-FILTERED 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 'PHD FINGER PROTEIN 19' _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 . 1 SER HA H 4.127 . 1 2 . 2 LYS HA H 4.183 . 1 3 . 5 GLU H H 7.909 . 1 4 . 5 GLU HA H 4.168 . 1 5 . 7 GLN H H 8.826 . 1 6 . 7 GLN HA H 4.846 . 1 7 . 7 GLN HB3 H 1.793 . 2 8 . 7 GLN HB2 H 1.645 . 2 9 . 7 GLN HG3 H 1.384 . 1 10 . 7 GLN HG2 H 1.384 . 1 11 . 8 TYR HB3 H 1.651 . 1 12 . 9 VAL H H 8.900 . 1 13 . 9 VAL HA H 4.390 . 1 14 . 10 LEU H H 7.864 . 1 15 . 10 LEU HA H 3.062 . 1 16 . 10 LEU HB3 H 1.525 . 2 17 . 10 LEU HB2 H 1.669 . 2 18 . 11 CYS H H 7.635 . 1 19 . 11 CYS HA H 4.170 . 1 20 . 11 CYS HB3 H 2.608 . 2 21 . 11 CYS HB2 H 2.867 . 2 stop_ save_ save_assigned_chem_shift_list_1_2_2 _Saveframe_category assigned_chemical_shifts _Details 'Origin nmrStar file /ebi/msd/pdb_root/Processing/prepare/4bd3/ebi/submit_tud_pep_ppm3_chainB.str.csh' loop_ _Experiment_label 'TRIPLE RESONANCE' NOESY EDITED-FILTERED 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 'HISTONE H3' _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 . 1 ALA HB H 1.482 . 1 2 . 2 THR HB H 4.336 . 1 3 . 2 THR HG2 H 1.199 . 1 4 . 4 GLY HA3 H 4.016 . 2 5 . 4 GLY HA2 H 3.916 . 2 6 . 5 VAL HB H 1.925 . 1 7 . 5 VAL HG2 H 0.853 . 1 8 . 6 M3L HA H 4.408 . 1 9 . 6 M3L HB2 H 1.630 . 1 10 . 6 M3L HB3 H 1.630 . 1 11 . 6 M3L HG2 H 1.500 . 2 12 . 6 M3L HG3 H 1.360 . 2 13 . 6 M3L HD2 H 1.165 . 1 14 . 6 M3L HD3 H 1.165 . 1 15 . 7 LYS HD3 H 1.655 . 1 16 . 7 LYS HD2 H 1.655 . 1 17 . 7 LYS HE3 H 2.941 . 1 18 . 7 LYS HE2 H 2.941 . 1 19 . 8 PRO HG3 H 1.918 . 2 20 . 8 PRO HG2 H 1.639 . 2 21 . 8 PRO HD3 H 3.631 . 2 22 . 8 PRO HD2 H 3.845 . 2 23 . 9 HIS HB3 H 2.729 . 2 24 . 9 HIS HB2 H 2.794 . 2 25 . 9 HIS HD2 H 6.550 . 1 26 . 9 HIS HE1 H 7.526 . 1 27 . 10 ARG HG3 H 1.440 . 1 28 . 10 ARG HG2 H 1.440 . 1 29 . 10 ARG HD3 H 4.290 . 1 30 . 10 ARG HD2 H 4.290 . 1 31 . 11 TYR HD1 H 6.934 . 3 stop_ save_