BMRB Entry 18650

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18650
MolProbity Validation Chart

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Title:
NMR structure of RelA-TAD/CBP-TAZ1 complex
Deposition date:
2012-08-07
Original release date:
2013-09-10
Authors:
Wright, Peter; Mukherjee, Sulakshana
Citation:

Citation: Mukherjee, Sulakshana; Behar, Marcelo; Birnbaum, Harry; Hoffmann, Alexander; Wright, Peter; Ghosh, Gourisankar. "Analysis of the RelA:CBP/p300 interaction reveals its involvement in NF-B-driven transcription."  PLoS Biol. 11, .-. (2013).
PubMed: 24019758

Assembly members:

Assembly members:
TAZ1, polymer, 100 residues, 11281.236 Da.
RelA-TA2, polymer, 70 residues, 7322.905 Da.
ZINC ION, non-polymer, 65.409 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TAZ1: ATGPTADPEKRKLIQQQLVL LLHAHKCQRREQANGEVRAC SLPHCRTMKNVLNHMTHCQA GKACQVAHCASSRQIISHWK NCTRHDCPVCLPLKNASDKR
RelA-TA2: GSHMKSTQAGEGTLSEALLH LQFDADEDLGALLGNSTDPG VFTDLASVDNSEFQQLLNQG VSMSHSTAEP

Data sets:
Data typeCount
13C chemical shifts531
15N chemical shifts175
1H chemical shifts1116

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TAZ11
2RelA-TA22
3ZINC ION_13
4ZINC ION_23
5ZINC ION_33

Entities:

Entity 1, TAZ1 100 residues - 11281.236 Da.

1   ALATHRGLYPROTHRALAASPPROGLULYS
2   ARGLYSLEUILEGLNGLNGLNLEUVALLEU
3   LEULEUHISALAHISLYSCYSGLNARGARG
4   GLUGLNALAASNGLYGLUVALARGALACYS
5   SERLEUPROHISCYSARGTHRMETLYSASN
6   VALLEUASNHISMETTHRHISCYSGLNALA
7   GLYLYSALACYSGLNVALALAHISCYSALA
8   SERSERARGGLNILEILESERHISTRPLYS
9   ASNCYSTHRARGHISASPCYSPROVALCYS
10   LEUPROLEULYSASNALASERASPLYSARG

Entity 2, RelA-TA2 70 residues - 7322.905 Da.

RelA sequence starts from Lys-425. The first four N-terminal residues are due to thrombin cleavage site.

1   GLYSERHISMETLYSSERTHRGLNALAGLY
2   GLUGLYTHRLEUSERGLUALALEULEUHIS
3   LEUGLNPHEASPALAASPGLUASPLEUGLY
4   ALALEULEUGLYASNSERTHRASPPROGLY
5   VALPHETHRASPLEUALASERVALASPASN
6   SERGLUPHEGLNGLNLEULEUASNGLNGLY
7   VALSERMETSERHISSERTHRALAGLUPRO

Entity 3, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: TAZ1, [U-13C; U-15N], 0.8 – 1.1 mM; RelA-TA21.2 – 1.5 mM; DTT 2 mM; TRIS 20 mM; sodium chloride 40 mM; D2O, [U-2H], 5%

sample_2: TAZ1, [U-13C], 0.8 – 1.1 mM; RelA-TA21.2 – 1.5 mM; DTT, [U-2H], 2 mM; TRIS, [U-2H], 20 mM; sodium chloride 40 mM; D2O, [U-2H], 99.8%

sample_3: RelA-TA2, [U-13C], 0.7 – 0.9 mM; TAZ11.5 – 1.8 mM; DTT, [U-2H], 2 mM; TRIS, [U-2H], 20 mM; sodium chloride 40 mM; D2O, [U-2H], 99.8%

sample_4: RelA-TA2, [U-13C; U-15N], 0.7 – 0.9 mM; TAZ11.5 – 1.8 mM; DTT 2 mM; TRIS 20 mM; sodium chloride 40 mM; D2O, [U-2H], 5%; H2O 95%

sample_5: TAZ1, [U-15N], 0.8 – 1.1 mM; RelA-TA21.2 – 1.5 mM; DTT 2 mM; TRIS 20 mM; sodium chloride 40 mM; D2O, [U-2H], 5%; H2O 95%

sample_6: RelA-TA2, [U-15N], 0.7 – 0.9 mM; TAZ11.5 – 1.8 mM; DTT 2 mM; TRIS 20 mM; sodium chloride 40 mM; D2O, [U-2H], 5%; H2O 95%

sample_conditions_1: ionic strength: 40 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_5isotropicsample_conditions_1
3D 1H-15N TOCSYsample_5isotropicsample_conditions_1
3D 1H-15N NOESYsample_5isotropicsample_conditions_1
12C-filtered-13C-edited NOESY-HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_4isotropicsample_conditions_1
3D HCCH-COSYsample_4isotropicsample_conditions_1
3D 1H-15N NOESYsample_6isotropicsample_conditions_1
3D 1H-15N TOCSYsample_6isotropicsample_conditions_1
12C-filtered-13C-edited NOESY-HSQCsample_4isotropicsample_conditions_1
2D 1H-15N HSQCsample_5isotropicsample_conditions_1
2D 1H-15N HSQCsample_6isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_4isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v10, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

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

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 16014
PDB
DBJ BAE06125 BAG65526 BAI45616 BAC40904 BAE32727 BAE33485 BAE33954 BAE34348
EMBL CDQ85159
GB AAB28651 AAC08447 AAC51331 AAC51770 AAH44677 AAA39811 AAF82405 AAH03818 AAH79457 AAH94053
PRF 1923401A
REF NP_001020603 NP_001073315 NP_001088637 NP_001157494 NP_001247644 NP_033071 NP_954888 XP_005351804 XP_006531757 XP_006531758
SP P45481 Q6JHU9 Q92793 Q04207
TPG DAA15549
AlphaFold P45481 Q6JHU9 Q92793 Q04207

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