data_19914 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Structure of KDM5B PHD1 finger in complex with H3K4me0(1-10aa) ; _BMRB_accession_number 19914 _BMRB_flat_file_name bmr19914.str _Entry_type original _Submission_date 2014-04-16 _Accession_date 2014-04-16 _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 Zhang Yan . . 2 Yang Huirong . . 3 Guo Xue . . 4 Rong Naiyan . . 5 Song Yujiao . . 6 Xu Youwei . . 7 Lan Wenxian . . 8 Xu Yanhui . . 9 Cao Chunyang . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 338 "13C chemical shifts" 165 "15N chemical shifts" 51 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-08-04 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 19913 'KDM5B PHD1 finger' stop_ _Original_release_date 2014-08-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The PHD1 finger of KDM5B recognizes unmodified H3K4 during the demethylation of histone H3K4me2/3 by KDM5B' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24952722 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhang Yan . . 2 Yang Huirong . . 3 Guo Xue . . 4 Rong Naiyan . . 5 Rong Yujiao . . 6 Xu Youwei . . 7 Lan Wenxian . . 8 Xu Yanhui . . 9 Cao Chunyang . . stop_ _Journal_abbreviation 'Protein Cell' _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 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'KDM5B PHD1 finger in complex with H3K4me0(1-10aa)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 'ZINC ION_1' $entity_ZN 'ZINC ION_2' $entity_ZN H3K4me0(1-10aa) $entity_3 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 7360.083 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 55 _Mol_residue_sequence ; AVDLYVCLLCGSGNDEDRLL LCDGCDDSYHTFCLIPPLHD VPKGDWRCPKCLAQE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 306 ALA 2 307 VAL 3 308 ASP 4 309 LEU 5 310 TYR 6 311 VAL 7 312 CYS 8 313 LEU 9 314 LEU 10 315 CYS 11 316 GLY 12 317 SER 13 318 GLY 14 319 ASN 15 320 ASP 16 321 GLU 17 322 ASP 18 323 ARG 19 324 LEU 20 325 LEU 21 326 LEU 22 327 CYS 23 328 ASP 24 329 GLY 25 330 CYS 26 331 ASP 27 332 ASP 28 333 SER 29 334 TYR 30 335 HIS 31 336 THR 32 337 PHE 33 338 CYS 34 339 LEU 35 340 ILE 36 341 PRO 37 342 PRO 38 343 LEU 39 344 HIS 40 345 ASP 41 346 VAL 42 347 PRO 43 348 LYS 44 349 GLY 45 350 ASP 46 351 TRP 47 352 ARG 48 353 CYS 49 354 PRO 50 355 LYS 51 356 CYS 52 357 LEU 53 358 ALA 54 359 GLN 55 360 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 19913 PHD1_finger_of_KDM5B 100.00 55 100.00 100.00 1.77e-30 PDB 2MNY "Nmr Structure Of Kdm5b Phd1 Finger" 100.00 55 100.00 100.00 1.77e-30 PDB 2MNZ "Nmr Structure Of Kdm5b Phd1 Finger In Complex With H3k4me0(1-10aa)" 100.00 55 100.00 100.00 1.77e-30 DBJ BAC30898 "unnamed protein product [Mus musculus]" 100.00 1433 98.18 100.00 2.78e-29 DBJ BAD90482 "mKIAA4034 protein [Mus musculus]" 100.00 1554 98.18 100.00 3.12e-29 DBJ BAE37363 "unnamed protein product [Mus musculus]" 100.00 600 98.18 100.00 4.27e-32 DBJ BAE89761 "unnamed protein product [Macaca fascicularis]" 100.00 194 100.00 100.00 2.11e-32 DBJ BAG53706 "unnamed protein product [Homo sapiens]" 100.00 1275 100.00 100.00 1.48e-29 EMBL CAB43532 "PLU-1 protein [Homo sapiens]" 100.00 1544 100.00 100.00 2.61e-29 EMBL CAB61368 "hypothetical protein [Homo sapiens]" 100.00 1350 100.00 100.00 1.57e-29 EMBL CAB63108 "RB-binding protein [Homo sapiens]" 100.00 1681 100.00 100.00 2.58e-29 EMBL CAH65222 "hypothetical protein RCJMB04_9d3 [Gallus gallus]" 100.00 1522 98.18 100.00 6.55e-29 GB AAD16061 "retinoblastoma binding protein 2 homolog 1 [Homo sapiens]" 100.00 1580 100.00 100.00 2.31e-29 GB AAH48180 "Jumonji, AT rich interactive domain 1B (Rbp2 like) [Mus musculus]" 100.00 1544 98.18 100.00 3.63e-29 GB AAH57318 "Jumonji, AT rich interactive domain 1B (Rbp2 like) [Mus musculus]" 100.00 1544 98.18 100.00 3.63e-29 GB AAI56050 "Jumonji, AT rich interactive domain 1B, partial [synthetic construct]" 100.00 1544 100.00 100.00 2.61e-29 GB AAI57032 "Jumonji, AT rich interactive domain 1B [synthetic construct]" 100.00 1544 100.00 100.00 2.61e-29 REF NP_001026200 "lysine-specific demethylase 5B [Gallus gallus]" 100.00 1522 98.18 100.00 6.55e-29 REF NP_001100647 "lysine-specific demethylase 5B [Rattus norvegicus]" 100.00 1544 98.18 100.00 4.76e-29 REF NP_001300971 "lysine-specific demethylase 5B isoform 1 [Homo sapiens]" 100.00 1580 100.00 100.00 2.43e-29 REF NP_006609 "lysine-specific demethylase 5B isoform 2 [Homo sapiens]" 100.00 1544 100.00 100.00 2.61e-29 REF NP_690855 "lysine-specific demethylase 5B [Mus musculus]" 100.00 1544 98.18 100.00 3.63e-29 SP Q5F3R2 "RecName: Full=Lysine-specific demethylase 5B; AltName: Full=Histone demethylase JARID1B; AltName: Full=Jumonji/ARID domain-cont" 100.00 1522 98.18 100.00 6.55e-29 SP Q80Y84 "RecName: Full=Lysine-specific demethylase 5B; AltName: Full=Histone demethylase JARID1B; AltName: Full=Jumonji/ARID domain-cont" 100.00 1544 98.18 100.00 3.63e-29 SP Q9UGL1 "RecName: Full=Lysine-specific demethylase 5B; AltName: Full=Cancer/testis antigen 31; Short=CT31; AltName: Full=Histone demethy" 100.00 1544 100.00 100.00 2.61e-29 TPG DAA21261 "TPA: RB-binding protein-like [Bos taurus]" 100.00 1489 98.18 100.00 1.42e-28 stop_ save_ save_entity_3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_3 _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 10 _Mol_residue_sequence ARTKQTARKS loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 363 ALA 2 364 ARG 3 365 THR 4 366 LYS 5 367 GLN 6 368 THR 7 369 ALA 8 370 ARG 9 371 LYS 10 372 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'ZINC ION' _BMRB_code ZN _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _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 $entity_1 Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $entity_1 'recombinant technology' . Escherichia coli . pGEX-6p-1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $entity_1 . mM 0.8 2 '[U-99% 13C; U-99% 15N]' H2O 90 % . . 'natural abundance' D2O 10 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CNS _Saveframe_category software _Name CNS _Version . loop_ _Vendor _Address _Electronic_address 'Brunger A. T. et.al.' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aliphatic_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aromatic_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aromatic' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_aliphatic_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aliphatic' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_aromatic_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aromatic' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 . M pH 7.4 . pH pressure 1 . atm temperature 293 . 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 water H 1 protons ppm 4.76 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $CNS stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '2D 1H-13C HSQC aliphatic' '2D 1H-13C HSQC aromatic' 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 entity_1 _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 1 306 1 ALA H H 8.362 . . 2 306 1 ALA HA H 4.806 . . 3 306 1 ALA HB H 1.355 . . 4 306 1 ALA N N 126.125 . . 5 307 2 VAL H H 7.927 . . 6 307 2 VAL HA H 3.931 . . 7 307 2 VAL HB H 1.962 . . 8 307 2 VAL HG2 H 0.861 . . 9 307 2 VAL CB C 32.181 . . 10 307 2 VAL CG1 C 21.407 . . 11 307 2 VAL CG2 C 21.407 . . 12 307 2 VAL N N 118.426 . . 13 308 3 ASP H H 7.897 . . 14 308 3 ASP HB2 H 2.466 . . 15 308 3 ASP CB C 41.13 . . 16 309 4 LEU H H 7.493 . . 17 309 4 LEU HA H 4.113 . . 18 309 4 LEU HB2 H 1.482 . . 19 309 4 LEU HB3 H 1.433 . . 20 309 4 LEU HG H 1.398 . . 21 309 4 LEU HD1 H 0.71 . . 22 309 4 LEU HD2 H 0.763 . . 23 309 4 LEU CA C 55.279 . . 24 309 4 LEU CG C 26.8 . . 25 309 4 LEU CD1 C 22.943 . . 26 309 4 LEU N N 117.182 . . 27 310 5 TYR H H 7.458 . . 28 310 5 TYR HA H 4.538 . . 29 310 5 TYR HB2 H 2.697 . . 30 310 5 TYR HB3 H 2.795 . . 31 310 5 TYR HD2 H 7.089 . . 32 310 5 TYR HE2 H 6.738 . . 33 310 5 TYR CA C 57.874 . . 34 310 5 TYR CB C 37.551 . . 35 310 5 TYR CD1 C 132.47 . . 36 310 5 TYR CD2 C 132.47 . . 37 310 5 TYR CE1 C 118.255 . . 38 310 5 TYR CE2 C 118.255 . . 39 310 5 TYR N N 118.773 . . 40 311 6 VAL H H 7.785 . . 41 311 6 VAL HA H 3.976 . . 42 311 6 VAL HB H 1.479 . . 43 311 6 VAL HG1 H 0.589 . . 44 311 6 VAL HG2 H 0.607 . . 45 311 6 VAL CA C 59.373 . . 46 311 6 VAL CB C 35.587 . . 47 311 6 VAL CG1 C 19.193 . . 48 311 6 VAL CG2 C 21.22 . . 49 311 6 VAL N N 118.252 . . 50 312 7 CYS H H 7.531 . . 51 312 7 CYS HA H 3.839 . . 52 312 7 CYS HB2 H 1.93 . . 53 312 7 CYS HB3 H 3.374 . . 54 312 7 CYS CA C 58.415 . . 55 312 7 CYS CB C 31.585 . . 56 312 7 CYS N N 125.429 . . 57 313 8 LEU H H 8.453 . . 58 313 8 LEU HA H 3.891 . . 59 313 8 LEU HB2 H 1.216 . . 60 313 8 LEU HB3 H 1.164 . . 61 313 8 LEU HD1 H 0.843 . . 62 313 8 LEU CA C 57.173 . . 63 313 8 LEU CB C 42.47 . . 64 313 8 LEU CD1 C 24.701 . . 65 313 8 LEU N N 130.689 . . 66 314 9 LEU H H 8.521 . . 67 314 9 LEU HA H 4.504 . . 68 314 9 LEU HB2 H 1.814 . . 69 314 9 LEU HB3 H 1.648 . . 70 314 9 LEU HG H 1.795 . . 71 314 9 LEU HD1 H 1.087 . . 72 314 9 LEU HD2 H 1.008 . . 73 314 9 LEU CA C 56.415 . . 74 314 9 LEU CB C 42.668 . . 75 314 9 LEU CG C 26.967 . . 76 314 9 LEU CD1 C 26.476 . . 77 314 9 LEU CD2 C 22.119 . . 78 314 9 LEU N N 118.705 . . 79 315 10 CYS H H 8.143 . . 80 315 10 CYS HA H 5.045 . . 81 315 10 CYS HB2 H 3.151 . . 82 315 10 CYS HB3 H 3.308 . . 83 315 10 CYS CA C 58.541 . . 84 315 10 CYS CB C 31.635 . . 85 315 10 CYS N N 117.143 . . 86 316 11 GLY H H 7.936 . . 87 316 11 GLY HA2 H 3.759 . . 88 316 11 GLY HA3 H 4.112 . . 89 316 11 GLY CA C 46.276 . . 90 316 11 GLY N N 112.839 . . 91 317 12 SER H H 8.546 . . 92 317 12 SER HA H 4.839 . . 93 317 12 SER HB2 H 3.992 . . 94 317 12 SER HB3 H 4.26 . . 95 317 12 SER CB C 64.609 . . 96 317 12 SER N N 115.704 . . 97 318 13 GLY H H 9.167 . . 98 318 13 GLY HA2 H 3.694 . . 99 318 13 GLY HA3 H 3.694 . . 100 318 13 GLY CA C 44.994 . . 101 318 13 GLY N N 115.91 . . 102 319 14 ASN H H 8.113 . . 103 319 14 ASN HA H 4.599 . . 104 319 14 ASN HB2 H 3.021 . . 105 319 14 ASN HB3 H 2.666 . . 106 319 14 ASN HD21 H 7.038 . . 107 319 14 ASN HD22 H 7.695 . . 108 319 14 ASN CB C 38.457 . . 109 319 14 ASN N N 117.682 . . 110 319 14 ASN ND2 N 113.362 . . 111 320 15 ASP H H 9.087 . . 112 320 15 ASP HA H 4.32 . . 113 320 15 ASP HB2 H 2.594 . . 114 320 15 ASP HB3 H 2.823 . . 115 320 15 ASP CA C 56.114 . . 116 320 15 ASP CB C 40.355 . . 117 320 15 ASP N N 117.82 . . 118 321 16 GLU H H 8.859 . . 119 321 16 GLU HA H 3.72 . . 120 321 16 GLU HB2 H 1.903 . . 121 321 16 GLU HB3 H 1.981 . . 122 321 16 GLU HG2 H 2.527 . . 123 321 16 GLU HG3 H 2.392 . . 124 321 16 GLU CA C 60.46 . . 125 321 16 GLU CG C 35.952 . . 126 321 16 GLU N N 115.267 . . 127 322 17 ASP H H 9.182 . . 128 322 17 ASP HA H 4.298 . . 129 322 17 ASP HB2 H 2.669 . . 130 322 17 ASP CA C 54.579 . . 131 322 17 ASP CB C 39.136 . . 132 322 17 ASP N N 115.313 . . 133 323 18 ARG H H 7.902 . . 134 323 18 ARG HA H 4.314 . . 135 323 18 ARG HB2 H 1.598 . . 136 323 18 ARG HG2 H 1.624 . . 137 323 18 ARG HD2 H 3.158 . . 138 323 18 ARG HD3 H 3.245 . . 139 323 18 ARG CA C 54.783 . . 140 323 18 ARG CB C 31.199 . . 141 323 18 ARG CG C 27.2 . . 142 323 18 ARG CD C 43.557 . . 143 323 18 ARG N N 118.426 . . 144 324 19 LEU H H 7.132 . . 145 324 19 LEU HA H 4.096 . . 146 324 19 LEU HB2 H 1.935 . . 147 324 19 LEU HB3 H 1.056 . . 148 324 19 LEU HG H 1.042 . . 149 324 19 LEU HD1 H -0.044 . . 150 324 19 LEU HD2 H 0.511 . . 151 324 19 LEU CA C 53.95 . . 152 324 19 LEU CB C 41.658 . . 153 324 19 LEU CG C 26.486 . . 154 324 19 LEU CD1 C 23.099 . . 155 324 19 LEU CD2 C 26.224 . . 156 324 19 LEU N N 124.096 . . 157 325 20 LEU H H 8.134 . . 158 325 20 LEU HA H 4.129 . . 159 325 20 LEU HB2 H 1.141 . . 160 325 20 LEU HB3 H 0.435 . . 161 325 20 LEU HG H 1.181 . . 162 325 20 LEU HD1 H -0.685 . . 163 325 20 LEU HD2 H 0.258 . . 164 325 20 LEU CA C 54.405 . . 165 325 20 LEU CB C 43.036 . . 166 325 20 LEU CG C 25.574 . . 167 325 20 LEU CD1 C 24.594 . . 168 325 20 LEU CD2 C 24.161 . . 169 325 20 LEU N N 125.564 . . 170 326 21 LEU H H 7.684 . . 171 326 21 LEU HA H 4.13 . . 172 326 21 LEU HB2 H 1.278 . . 173 326 21 LEU HB3 H 1.082 . . 174 326 21 LEU HG H 1.418 . . 175 326 21 LEU HD1 H 0.849 . . 176 326 21 LEU HD2 H 0.326 . . 177 326 21 LEU CA C 54.58 . . 178 326 21 LEU CG C 26.757 . . 179 326 21 LEU CD2 C 25.213 . . 180 326 21 LEU N N 118.623 . . 181 327 22 CYS H H 8.913 . . 182 327 22 CYS HA H 4.595 . . 183 327 22 CYS HB2 H 3.442 . . 184 327 22 CYS HB3 H 2.916 . . 185 327 22 CYS CA C 60.667 . . 186 327 22 CYS CB C 30.903 . . 187 327 22 CYS N N 125.449 . . 188 328 23 ASP H H 9.432 . . 189 328 23 ASP HB2 H 2.758 . . 190 328 23 ASP CB C 41.512 . . 191 328 23 ASP N N 129.303 . . 192 329 24 GLY H H 10.289 . . 193 329 24 GLY HA2 H 4.085 . . 194 329 24 GLY HA3 H 4.173 . . 195 329 24 GLY CA C 46.054 . . 196 329 24 GLY N N 114.897 . . 197 330 25 CYS H H 8.128 . . 198 330 25 CYS HA H 4.85 . . 199 330 25 CYS HB2 H 3.102 . . 200 330 25 CYS HB3 H 2.411 . . 201 330 25 CYS CB C 33.094 . . 202 330 25 CYS N N 121.696 . . 203 331 26 ASP HA H 4.818 . . 204 331 26 ASP HB2 H 2.491 . . 205 331 26 ASP HB3 H 2.597 . . 206 331 26 ASP CB C 41.377 . . 207 332 27 ASP H H 8.271 . . 208 332 27 ASP HA H 4.793 . . 209 332 27 ASP HB2 H 2.644 . . 210 332 27 ASP HB3 H 3.061 . . 211 332 27 ASP CB C 42.346 . . 212 332 27 ASP N N 121.279 . . 213 333 28 SER H H 7.819 . . 214 333 28 SER HA H 5.88 . . 215 333 28 SER HB2 H 3.351 . . 216 333 28 SER CA C 56.39 . . 217 333 28 SER CB C 66.089 . . 218 333 28 SER N N 112.885 . . 219 334 29 TYR H H 8.592 . . 220 334 29 TYR HA H 5.372 . . 221 334 29 TYR HB2 H 2.613 . . 222 334 29 TYR HD2 H 7.065 . . 223 334 29 TYR HE2 H 6.804 . . 224 334 29 TYR CA C 56.183 . . 225 334 29 TYR CB C 44.513 . . 226 334 29 TYR CD1 C 133.385 . . 227 334 29 TYR CD2 C 133.385 . . 228 334 29 TYR CE1 C 117.297 . . 229 334 29 TYR CE2 C 117.297 . . 230 334 29 TYR N N 119.816 . . 231 335 30 HIS H H 8.975 . . 232 335 30 HIS HA H 5.193 . . 233 335 30 HIS HB2 H 2.966 . . 234 335 30 HIS HB3 H 1.246 . . 235 335 30 HIS HD2 H 6.555 . . 236 335 30 HIS HE1 H 7.499 . . 237 335 30 HIS HE2 H 12.036 . . 238 335 30 HIS CA C 58.016 . . 239 335 30 HIS CB C 30.573 . . 240 335 30 HIS CD2 C 117.75 . . 241 335 30 HIS CE1 C 138.964 . . 242 335 30 HIS N N 122.34 . . 243 336 31 THR H H 8.721 . . 244 336 31 THR HA H 3.569 . . 245 336 31 THR HB H 4.342 . . 246 336 31 THR HG2 H 1.036 . . 247 336 31 THR CA C 64.792 . . 248 336 31 THR CB C 65.853 . . 249 336 31 THR CG2 C 23.001 . . 250 336 31 THR N N 112.321 . . 251 337 32 PHE H H 6.503 . . 252 337 32 PHE HA H 4.623 . . 253 337 32 PHE HB2 H 3.482 . . 254 337 32 PHE HB3 H 2.928 . . 255 337 32 PHE HD2 H 7.104 . . 256 337 32 PHE HE2 H 6.924 . . 257 337 32 PHE HZ H 6.273 . . 258 337 32 PHE CB C 37.698 . . 259 337 32 PHE CD1 C 132.759 . . 260 337 32 PHE CD2 C 132.759 . . 261 337 32 PHE CE1 C 131.75 . . 262 337 32 PHE CE2 C 131.75 . . 263 337 32 PHE CZ C 130.733 . . 264 337 32 PHE N N 110.965 . . 265 338 33 CYS H H 7.299 . . 266 338 33 CYS HA H 4.368 . . 267 338 33 CYS HB2 H 3.241 . . 268 338 33 CYS HB3 H 2.692 . . 269 338 33 CYS CA C 61.854 . . 270 338 33 CYS CB C 31.13 . . 271 338 33 CYS N N 123.523 . . 272 339 34 LEU H H 6.423 . . 273 339 34 LEU HA H 3.946 . . 274 339 34 LEU HB2 H 1.681 . . 275 339 34 LEU HB3 H 1.393 . . 276 339 34 LEU HG H 1.785 . . 277 339 34 LEU HD1 H 0.741 . . 278 339 34 LEU HD2 H 0.823 . . 279 339 34 LEU CA C 55.368 . . 280 339 34 LEU CB C 44.141 . . 281 339 34 LEU CG C 27.097 . . 282 339 34 LEU CD1 C 23.211 . . 283 339 34 LEU CD2 C 27.047 . . 284 339 34 LEU N N 119.082 . . 285 340 35 ILE H H 8.037 . . 286 340 35 ILE HA H 4.221 . . 287 340 35 ILE HB H 1.723 . . 288 340 35 ILE HG12 H 0.972 . . 289 340 35 ILE HG13 H 1.565 . . 290 340 35 ILE HG2 H 0.811 . . 291 340 35 ILE HD1 H 0.872 . . 292 340 35 ILE CA C 57.694 . . 293 340 35 ILE CB C 40.082 . . 294 340 35 ILE CG1 C 26.974 . . 295 340 35 ILE CG2 C 17.226 . . 296 340 35 ILE CD1 C 13.424 . . 297 340 35 ILE N N 117.875 . . 298 341 36 PRO HA H 5.003 . . 299 341 36 PRO HB2 H 2.407 . . 300 341 36 PRO HB3 H 2.048 . . 301 341 36 PRO HG2 H 1.877 . . 302 341 36 PRO HG3 H 1.92 . . 303 341 36 PRO HD2 H 3.518 . . 304 341 36 PRO HD3 H 3.609 . . 305 341 36 PRO CA C 62.027 . . 306 341 36 PRO CB C 33.032 . . 307 341 36 PRO CG C 24.833 . . 308 341 36 PRO CD C 49.939 . . 309 342 37 PRO HA H 4.386 . . 310 342 37 PRO HB2 H 2.216 . . 311 342 37 PRO HB3 H 1.733 . . 312 342 37 PRO HG2 H 2.133 . . 313 342 37 PRO HD2 H 3.662 . . 314 342 37 PRO CA C 62.874 . . 315 342 37 PRO CB C 32.103 . . 316 342 37 PRO CG C 27.286 . . 317 342 37 PRO CD C 49.882 . . 318 343 38 LEU H H 7.666 . . 319 343 38 LEU HA H 4.486 . . 320 343 38 LEU HB2 H 1.541 . . 321 343 38 LEU HB3 H 1.275 . . 322 343 38 LEU HG H 1.717 . . 323 343 38 LEU HD1 H 0.732 . . 324 343 38 LEU HD2 H 0.852 . . 325 343 38 LEU CA C 53.31 . . 326 343 38 LEU CB C 43.415 . . 327 343 38 LEU CG C 27.014 . . 328 343 38 LEU CD1 C 25.945 . . 329 343 38 LEU CD2 C 22.822 . . 330 343 38 LEU N N 119.708 . . 331 344 39 HIS HA H 4.356 . . 332 344 39 HIS HB2 H 3.116 . . 333 344 39 HIS HB3 H 3.039 . . 334 344 39 HIS HD2 H 7.023 . . 335 344 39 HIS HE1 H 7.916 . . 336 344 39 HIS CA C 57.617 . . 337 344 39 HIS CB C 30.462 . . 338 344 39 HIS CD2 C 119.565 . . 339 344 39 HIS CE1 C 138.019 . . 340 345 40 ASP H H 7.517 . . 341 345 40 ASP HA H 4.794 . . 342 345 40 ASP HB2 H 2.347 . . 343 345 40 ASP HB3 H 2.448 . . 344 345 40 ASP CB C 43.637 . . 345 345 40 ASP N N 115.261 . . 346 346 41 VAL H H 8.773 . . 347 346 41 VAL HA H 3.707 . . 348 346 41 VAL HB H 1.902 . . 349 346 41 VAL HG1 H 0.779 . . 350 346 41 VAL HG2 H 0.947 . . 351 346 41 VAL CA C 61.05 . . 352 346 41 VAL CB C 32.389 . . 353 346 41 VAL CG1 C 20.522 . . 354 346 41 VAL CG2 C 22.093 . . 355 346 41 VAL N N 123.315 . . 356 347 42 PRO HA H 4.351 . . 357 347 42 PRO HB2 H 1.839 . . 358 347 42 PRO HG2 H 1.91 . . 359 347 42 PRO HD2 H 3.168 . . 360 347 42 PRO HD3 H 3.809 . . 361 347 42 PRO CA C 62.858 . . 362 347 42 PRO CB C 31.746 . . 363 347 42 PRO CG C 27.52 . . 364 347 42 PRO CD C 51.086 . . 365 348 43 LYS H H 8.581 . . 366 348 43 LYS HA H 4.191 . . 367 348 43 LYS HB2 H 1.753 . . 368 348 43 LYS HB3 H 1.807 . . 369 348 43 LYS HG2 H 1.47 . . 370 348 43 LYS HD2 H 1.662 . . 371 348 43 LYS HE2 H 2.975 . . 372 348 43 LYS CA C 56.833 . . 373 348 43 LYS CB C 32.537 . . 374 348 43 LYS CG C 25.046 . . 375 348 43 LYS CD C 28.857 . . 376 348 43 LYS N N 121.135 . . 377 349 44 GLY H H 8.286 . . 378 349 44 GLY HA2 H 4.179 . . 379 349 44 GLY HA3 H 3.803 . . 380 349 44 GLY CA C 43.97 . . 381 349 44 GLY N N 108.616 . . 382 350 45 ASP H H 8.235 . . 383 350 45 ASP HA H 4.638 . . 384 350 45 ASP HB2 H 2.607 . . 385 350 45 ASP CB C 41.863 . . 386 350 45 ASP N N 120.253 . . 387 351 46 TRP H H 9.548 . . 388 351 46 TRP HA H 4.494 . . 389 351 46 TRP HB2 H 2.828 . . 390 351 46 TRP HB3 H 3.342 . . 391 351 46 TRP HD1 H 7.245 . . 392 351 46 TRP HE1 H 9.839 . . 393 351 46 TRP HE3 H 7.227 . . 394 351 46 TRP HZ2 H 7.079 . . 395 351 46 TRP HZ3 H 6.7 . . 396 351 46 TRP HH2 H 6.592 . . 397 351 46 TRP CA C 59.903 . . 398 351 46 TRP CB C 31.221 . . 399 351 46 TRP CD1 C 126.256 . . 400 351 46 TRP CE3 C 121.434 . . 401 351 46 TRP CZ2 C 114.689 . . 402 351 46 TRP CZ3 C 119.477 . . 403 351 46 TRP CH2 C 122.038 . . 404 351 46 TRP N N 124.443 . . 405 351 46 TRP NE1 N 129.348 . . 406 352 47 ARG H H 6.761 . . 407 352 47 ARG HA H 4.966 . . 408 352 47 ARG HB2 H 1.151 . . 409 352 47 ARG HG2 H 1.26 . . 410 352 47 ARG HG3 H 1.463 . . 411 352 47 ARG HD2 H 2.845 . . 412 352 47 ARG HD3 H 2.907 . . 413 352 47 ARG CA C 52.486 . . 414 352 47 ARG CB C 33.767 . . 415 352 47 ARG CG C 27.922 . . 416 352 47 ARG CD C 43.118 . . 417 352 47 ARG CZ C 145.032 . . 418 352 47 ARG N N 124.482 . . 419 353 48 CYS H H 8.955 . . 420 353 48 CYS HA H 3.709 . . 421 353 48 CYS HB2 H 3.121 . . 422 353 48 CYS HB3 H 2.392 . . 423 353 48 CYS CA C 56.662 . . 424 353 48 CYS CB C 29.954 . . 425 353 48 CYS N N 124.884 . . 426 354 49 PRO HA H 3.961 . . 427 354 49 PRO HB3 H 3.045 . . 428 354 49 PRO HG2 H 1.872 . . 429 354 49 PRO HD2 H 3.277 . . 430 354 49 PRO HD3 H 3.007 . . 431 354 49 PRO CA C 65.401 . . 432 354 49 PRO CG C 27.618 . . 433 354 49 PRO CD C 49.623 . . 434 355 50 LYS H H 7.769 . . 435 355 50 LYS HA H 4.053 . . 436 355 50 LYS HB2 H 2.333 . . 437 355 50 LYS HB3 H 1.882 . . 438 355 50 LYS HG2 H 1.512 . . 439 355 50 LYS HG3 H 1.303 . . 440 355 50 LYS HD2 H 1.768 . . 441 355 50 LYS HE2 H 2.975 . . 442 355 50 LYS CA C 59.467 . . 443 355 50 LYS CB C 32.404 . . 444 355 50 LYS CG C 25.155 . . 445 355 50 LYS CD C 29.14 . . 446 355 50 LYS CE C 42.06 . . 447 355 50 LYS N N 118.518 . . 448 356 51 CYS H H 8.367 . . 449 356 51 CYS HA H 3.823 . . 450 356 51 CYS HB2 H 2.714 . . 451 356 51 CYS CA C 65.005 . . 452 356 51 CYS CB C 28.457 . . 453 356 51 CYS N N 124.003 . . 454 357 52 LEU H H 7.987 . . 455 357 52 LEU HA H 3.935 . . 456 357 52 LEU HB2 H 1.429 . . 457 357 52 LEU HB3 H 1.351 . . 458 357 52 LEU HG H 1.339 . . 459 357 52 LEU HD1 H 0.62 . . 460 357 52 LEU HD2 H 0.629 . . 461 357 52 LEU CA C 55.872 . . 462 357 52 LEU CB C 41.937 . . 463 357 52 LEU CG C 25.888 . . 464 357 52 LEU CD1 C 25.581 . . 465 357 52 LEU CD2 C 22.973 . . 466 357 52 LEU N N 119.215 . . 467 358 53 ALA H H 7.336 . . 468 358 53 ALA HA H 4.19 . . 469 358 53 ALA HB H 1.382 . . 470 358 53 ALA CA C 52.818 . . 471 358 53 ALA CB C 18.606 . . 472 358 53 ALA N N 120.997 . . 473 359 54 GLN H H 7.637 . . 474 359 54 GLN HA H 4.238 . . 475 359 54 GLN HB2 H 2.119 . . 476 359 54 GLN HB3 H 1.942 . . 477 359 54 GLN HG2 H 2.343 . . 478 359 54 GLN HE21 H 7.482 . . 479 359 54 GLN HE22 H 6.849 . . 480 359 54 GLN CA C 55.666 . . 481 359 54 GLN CB C 29.482 . . 482 359 54 GLN CG C 33.823 . . 483 359 54 GLN N N 117.963 . . 484 359 54 GLN NE2 N 112.784 . . 485 360 55 GLU H H 7.776 . . 486 360 55 GLU HA H 4.009 . . 487 360 55 GLU HB2 H 1.982 . . 488 360 55 GLU HB3 H 1.842 . . 489 360 55 GLU HG2 H 2.168 . . 490 360 55 GLU CA C 58.187 . . 491 360 55 GLU CB C 31.003 . . 492 360 55 GLU CG C 36.721 . . 493 360 55 GLU N N 126.928 . . stop_ save_ save_assigned_chem_shift_list_1_4 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $CNS stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '2D 1H-13C HSQC aliphatic' '2D 1H-13C HSQC aromatic' 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 H3K4me0(1-10aa) _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 1 363 1 ALA HA H 4.352 . . 2 363 1 ALA HB H 1.171 . . 3 363 1 ALA HB H 1.372 . . 4 363 1 ALA HB H 1.171 . . 5 364 2 ARG H H 8.11 . . 6 364 2 ARG HA H 4.284 . . 7 364 2 ARG HB2 H 1.931 . . 8 364 2 ARG HB3 H 1.711 . . 9 364 2 ARG HG2 H 1.163 . . 10 364 2 ARG HG3 H 1.653 . . 11 364 2 ARG HD2 H 2.434 . . 12 364 2 ARG HD3 H 2.287 . . 13 364 2 ARG HE H 6.395 . . 14 365 3 THR H H 8.028 . . 15 365 3 THR HA H 4.225 . . 16 365 3 THR HB H 3.768 . . 17 365 3 THR HG2 H 1.066 . . 18 366 4 LYS H H 8.04 . . 19 366 4 LYS HA H 4.117 . . 20 366 4 LYS HB2 H 1.317 . . 21 366 4 LYS HB3 H 2.274 . . 22 366 4 LYS HG2 H 2.073 . . 23 366 4 LYS HG3 H 1.84 . . 24 366 4 LYS HD2 H 1.673 . . 25 366 4 LYS HD3 H 1.582 . . 26 366 4 LYS HE2 H 3.172 . . 27 367 5 GLN HA H 4.44 . . 28 367 5 GLN HB2 H 1.819 . . 29 367 5 GLN HB3 H 1.641 . . 30 367 5 GLN HG2 H 3.188 . . 31 367 5 GLN HE21 H 6.445 . . 32 367 5 GLN HE22 H 7.548 . . 33 368 6 THR H H 8.25 . . 34 368 6 THR HA H 4.037 . . 35 368 6 THR HB H 3.567 . . 36 368 6 THR HG1 H 5.098 . . 37 368 6 THR HG2 H 1.249 . . 38 368 6 THR HG2 H 1.756 . . 39 368 6 THR HG2 H 1.249 . . 40 369 7 ALA HA H 4.056 . . 41 369 7 ALA HB H 1.489 . . 42 370 8 ARG H H 8.043 . . 43 370 8 ARG HA H 4.257 . . 44 370 8 ARG HB2 H 1.458 . . 45 370 8 ARG HB3 H 1.887 . . 46 370 8 ARG HG2 H 1.683 . . 47 370 8 ARG HD2 H 3.961 . . 48 370 8 ARG HD3 H 2.982 . . 49 370 8 ARG HE H 6.371 . . 50 371 9 LYS H H 7.995 . . 51 371 9 LYS HA H 3.742 . . 52 371 9 LYS HB2 H 1.438 . . 53 371 9 LYS HB3 H 1.872 . . 54 371 9 LYS HD2 H 1.597 . . 55 371 9 LYS HD3 H 1.679 . . 56 371 9 LYS HE2 H 3.019 . . 57 371 9 LYS HE3 H 3.208 . . 58 372 10 SER H H 8.035 . . 59 372 10 SER HA H 4.294 . . 60 372 10 SER HB2 H 3.812 . . 61 372 10 SER HB3 H 3.873 . . stop_ save_