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Biological Magnetic Resonance Data Bank


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BMRB Entry 17271

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17271
MolProbity Validation Chart

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Title: Co-ordinates and 1H, 13C and 15N chemical shift assignments for the complex of GPS2 53-90 and SMRT 167-207   PubMed: 21240272

Deposition date: 2010-11-01 Original release date: 2011-01-18

Authors: Oberoi, Jasmeen; Yang, Ji-Chun; Neuhaus, David; Schwabe, John

Citation: Oberoi, Jasmeen; Fairall, Louise; Watson, Peter; Yang, Ji-Chun; Czimmerer, Zsolt; Kampmann, Thorsten; Goult, Benjamin; Greenwood, Jacquie; Gooch, John; Kallenberger, Bettina; Nagy, Laszlo; Neuhaus, David; Schwabe, John. "Structural basis for the assembly of the SMRT/NCoR core transcriptional repression machinery."  Nat. Struct. Mol. Biol. 18, 177-184 (2011).

Assembly members:
GPS2_53-90, polymer, 38 residues, 4692.534 Da.
SMRT_167-207, polymer, 42 residues, 4948.712 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):
GPS2_53-90: KKEMEERMSLEETKEQILKL EEKLLALQEEKHQLFLQL
SMRT_167-207: GLSKEELIQNMDRVDREITM VEQQISKLKKKQQQLEEEAA KP

Data sets:
Data typeCount
13C chemical shifts232
15N chemical shifts90
1H chemical shifts578

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1GPS2_53-901
2SMRT_167-2072

Entities:

Entity 1, GPS2_53-90 38 residues - 4692.534 Da.

1   LYSLYSGLUMETGLUGLUARGMETSERLEU
2   GLUGLUTHRLYSGLUGLNILELEULYSLEU
3   GLUGLULYSLEULEUALALEUGLNGLUGLU
4   LYSHISGLNLEUPHELEUGLNLEU

Entity 2, SMRT_167-207 42 residues - 4948.712 Da.

1   GLYLEUSERLYSGLUGLULEUILEGLNASN
2   METASPARGVALASPARGGLUILETHRMET
3   VALGLUGLNGLNILESERLYSLEULYSLYS
4   LYSGLNGLNGLNLEUGLUGLUGLUALAALA
5   LYSPRO

Samples:

sample_1: GPS2_53-90, [U-98% 13C; U-98% 15N], 0.4 mM; SMRT_167-207, [U-98% 13C; U-98% 15N], 0.4 mM; Tris 20 mM; H2O 90%; D2O 10%

sample_2: SMRT_167-207, [U-98% 13C; U-98% 15N], 0.4 mM; GPS2_53-90 0.4 mM; Tris 20 mM; H2O 90%; D2O 10%

sample_3: GPS2_53-90, [U-98% 13C; U-98% 15N], 0.4 mM; SMRT_167-207 0.4 mM; Tris 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC CT aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC CT aromaticsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESY (filtered to remove 15N-coupled signals in F1 and F2)sample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-1H NOESY filtered to retain only interchain cross-peakssample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-1H NOESY filtered to retain only interchain cross-peakssample_3isotropicsample_conditions_1
3D HNHAHBsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.19, Schwieters, Kuszewski, Tjandra and Clore - structure solution

xwinnmr v3.6, Bruker Biospin - processing

Analysis v1.0.15, CCPN - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker DMX 600 MHz
  • Bruker DRX 500 MHz

Related Database Links:

PDB
DBJ BAG63313 BAD92326 BAG72661
EMBL CAB59255 CAG46524 CAG46550 CAJ82276
GB AAB60432 AAH13652 AAI03902 AAI03903 AAI03904 AAD20944 AAD20946 AAD22973 AAI29557 AAI56550
REF NP_001069242 NP_004480 XP_001365129 XP_002718857 XP_002748019 NP_001007033 NP_001038041 NP_001070729 NP_001084492 NP_001101804
SP Q13227 Q9WU42 Q9Y618
TPG DAA18863 DAA20733

Download simulated HSQC data in one of the following formats:
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