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Biological Magnetic Resonance Data Bank


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BMRB Entry 17607

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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/BMR17607
MolProbity Validation Chart

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Title: Solution structure of RBBP1 tudor domain   PubMed: 22247551

Deposition date: 2011-04-28 Original release date: 2012-05-09

Authors: Gong, Weibin; Feng, Yingang

Citation: Gong, Weibin; Zhou, Tao; Mo, Jinjin; Perrett, Sarah; Wang, Jinfeng; Feng, Yingang. "Structural insight into recognition of methylated histone tails by retinoblastoma-binding protein 1."  J. Biol. Chem. 287, 8531-8540 (2012).

Assembly members:
entity, polymer, 118 residues, 13172.984 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: ADEPAYLTVGTDVSAKYRGA FCEAKIKTVKRLVKVKVLLK QDNTTQLVQDDQVKGPLRVG AIVETRTSDGSFQEAIISKL TDASWYTVVFDDGDERTLRR TSLCLKGERHFAESETLD

Data sets:
Data typeCount
13C chemical shifts488
15N chemical shifts116
1H chemical shifts719

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1RBBP11

Entities:

Entity 1, RBBP1 118 residues - 13172.984 Da.

1   ALAASPGLUPROALATYRLEUTHRVALGLY
2   THRASPVALSERALALYSTYRARGGLYALA
3   PHECYSGLUALALYSILELYSTHRVALLYS
4   ARGLEUVALLYSVALLYSVALLEULEULYS
5   GLNASPASNTHRTHRGLNLEUVALGLNASP
6   ASPGLNVALLYSGLYPROLEUARGVALGLY
7   ALAILEVALGLUTHRARGTHRSERASPGLY
8   SERPHEGLNGLUALAILEILESERLYSLEU
9   THRASPALASERTRPTYRTHRVALVALPHE
10   ASPASPGLYASPGLUARGTHRLEUARGARG
11   THRSERLEUCYSLEULYSGLYGLUARGHIS
12   PHEALAGLUSERGLUTHRLEUASP

Samples:

sample_1: RBBP1, [U-95% 15N], 0.6 mM; TRIS 50 mM; DTT 5 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_2: RBBP1, [U-95% 13C; U-95% 15N], 0.6 mM; TRIS 50 mM; DTT 5 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 7; 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 aromaticsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

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

NMRView, Johnson, One Moon Scientific - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
DBJ BAC31192
GB AAB28543 AAH25436 AAH26230 AAH58209 AAI57976
REF NP_001074664 NP_001231108 NP_001243510 NP_002883 NP_075376
SP P29374
TPG DAA25277

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SPARKY: Backbone or all simulated shifts