BMRB Entry 16989

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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/BMR16989
MolProbity Validation Chart

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Title:
Solution structure of the RRM domain of CYP33
Deposition date:
2010-06-09
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:
CYP33, polymer, 83 residues, 9211.386 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: pGEX 4T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CYP33: GSTTKRVLYVGGLAEEVDDK VLHAAFIPFGDITDIQIPLD YETEKHRGFAFVEFELAEDA AAAIDNMNESELFGRTIRVN LAK

Data sets:
Data typeCount
13C chemical shifts330
15N chemical shifts77
1H chemical shifts538

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1CYP331

Entities:

Entity 1, CYP33 83 residues - 9211.386 Da.

1   GLYSERTHRTHRLYSARGVALLEUTYRVAL
2   GLYGLYLEUALAGLUGLUVALASPASPLYS
3   VALLEUHISALAALAPHEILEPROPHEGLY
4   ASPILETHRASPILEGLNILEPROLEUASP
5   TYRGLUTHRGLULYSHISARGGLYPHEALA
6   PHEVALGLUPHEGLULEUALAGLUASPALA
7   ALAALAALAILEASPASNMETASNGLUSER
8   GLULEUPHEGLYARGTHRILEARGVALASN
9   LEUALALYS

Samples:

sample_1: potassium phosphate 25 mM; sodium chloride 50 mM; DTT 1 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCABsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_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 INOVA 600 MHz

Related Database Links:

PDB
DBJ BAB25512 BAE01400 BAF85783 BAG36418 BAG73521
EMBL CAH92437
GB AAC00006 AAC00007 AAD19906 AAD19907 AAF01030
REF NP_001041333 NP_001091630 NP_001126436 NP_001156520 NP_001181936
SP A4FV72 Q5R723 Q9QZH3 Q9UNP9
TPG DAA31059
AlphaFold A4FV72 Q5R723 Q9QZH3 Q9UNP9

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