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Biological Magnetic Resonance Data Bank


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BMRB Entry 17673

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17673
MolProbity Validation Chart

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Title: Not Available   PubMed: 22864287

Deposition date: 2011-05-30 Original release date: 2012-05-09

Authors: Cui, Gaofeng; Botuyan, Maria; Mer, Georges

Citation: Cui, Gaofeng; Park, Sungman; Badeaux, Aimee; Kim, Donghwa; Lee, Joseph; Thompson, James; Yan, Fei; Kaneko, Satoshi; Yuan, Zengqiang; Botuyan, Maria; Bedford, Mark; Cheng, Jin; Mer, Georges. "PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53"  Nat. Struct. Mol. Biol. 19, 916-924 (2012).

Assembly members:
entity, polymer, 81 residues, 8743.901 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity: GHMSSEFQINEQVLASWSDS RFYPAKVTAVNKDGTYTVKF YDGVVQTVKHIHVKAFSKDQ NIVGNARGSRAHSSHLXSKK G

Data sets:
Data typeCount
13C chemical shifts306
15N chemical shifts78
1H chemical shifts519

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1TDRD71

Entities:

Entity 1, TDRD7 81 residues - 8743.901 Da.

X=M2L

1   GLYHISMETSERSERGLUPHEGLNILEASN
2   GLUGLNVALLEUALASERTRPSERASPSER
3   ARGPHETYRPROALALYSVALTHRALAVAL
4   ASNLYSASPGLYTHRTYRTHRVALLYSPHE
5   TYRASPGLYVALVALGLNTHRVALLYSHIS
6   ILEHISVALLYSALAPHESERLYSASPGLN
7   ASNILEVALGLYASNALAARGGLYSERARG
8   ALAHISSERSERHISLEUM2LSERLYSLYS
9   GLY

Samples:

sample_1: entity, [U-100% 15N], 1 mM; sodium phosphate 25 mM; DSS 0.3 mM; H2O 90%; D2O 10%

sample_2: entity, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 25 mM; DSS 0.3 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.025 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_2isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - peak picking, processing

SANE, Duggan, Legge, Dyson & Wright - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v8, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

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