BMRB Entry 16983

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16983
MolProbity Validation Chart

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Title:
The solution structure of the PHD3 finger of MLL
Deposition date:
2010-06-08
Original release date:
2010-08-12
Authors:
Park, Sangho; Bushweller, John
Citation:

Citation: Park, Sangho; Osmers, Ute; Raman, Gayathree; Schwantes, Rebecca; Diaz, Manuel; Bushweller, John. "The PHD3 Domain of MLL Acts as a CYP33-Regulated Switch between MLL-Mediated Activation and Repression ."  Biochemistry 49, 6576-6586 (2010).
PubMed: 20677832

Assembly members:

Assembly members:
PHD3, polymer, 67 residues, 7719.658 Da.
ZN, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: GE Healthcare

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PHD3: GSAKGNFCPLCDKCYDDDDY ESKMMQCGKCDRWVHSKCEN LSDEMYEILSNLPESVAYTC VNCTERH

Data sets:
Data typeCount
13C chemical shifts262
15N chemical shifts67
1H chemical shifts429

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1PHD31
2ZINC ION_12
3ZINC ION_22

Entities:

Entity 1, PHD3 67 residues - 7719.658 Da.

1   GLYSERALALYSGLYASNPHECYSPROLEU
2   CYSASPLYSCYSTYRASPASPASPASPTYR
3   GLUSERLYSMETMETGLNCYSGLYLYSCYS
4   ASPARGTRPVALHISSERLYSCYSGLUASN
5   LEUSERASPGLUMETTYRGLUILELEUSER
6   ASNLEUPROGLUSERVALALATYRTHRCYS
7   VALASNCYSTHRGLUARGHIS

Entity 2, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: PHD3, [U-98% 13C; U-98% 15N], 1 mM; ZINC ION 100 uM; potassium phosphate 25 mM; DTT 3 mM; sodium chloride 50 mM; sodium azide 1 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.9; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1anisotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Varian Avance 600 MHz

Related Database Links:

PDB
DBJ BAA03407 BAD92745
EMBL CAA58584
GB AAA58669 AAA92511 AAB34770 AAM33377 AAQ63624
REF NP_001074518 NP_005924 XP_003253537 XP_003910832 XP_004052287
SP Q03164
TPG DAA22311
AlphaFold Q03164

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks