BMRB Entry 25326

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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/BMR25326
MolProbity Validation Chart

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Title:
The structure of the carboxy-terminal domain of DNTTIP1
Deposition date:
2014-11-11
Original release date:
2015-02-16
Authors:
Schwabe, John; Muskett, Frederick; Itoh, Toshimasa
Citation:

Citation: Itoh, Toshimasa; Fairall, Louise; Muskett, Frederick; Milano, Charles; Watson, Peter; Arnaudo, Nadia; Martino, Fabrizio; Schwabe, John. "Structural and functional characterization of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting"  Nucleic Acids Res. 43, 2033-2044 (2015).
PubMed: 25653165

Assembly members:

Assembly members:
entity, polymer, 122 residues, 14060.309 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: pET30A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GAREGPKWDPARLNESTTFV LGSRANKALGMGGTRGRIYI KHPHLFKYAADPQDKHWLAE QHHMRATGGKMAYLLIEEDI RDLAASDDYRGCLDLKLEEL KSFVLPSWMVEKMRKYMETL RT

Data sets:
Data typeCount
13C chemical shifts382
15N chemical shifts108
1H chemical shifts734

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 122 residues - 14060.309 Da.

1   GLYALAARGGLUGLYPROLYSTRPASPPRO
2   ALAARGLEUASNGLUSERTHRTHRPHEVAL
3   LEUGLYSERARGALAASNLYSALALEUGLY
4   METGLYGLYTHRARGGLYARGILETYRILE
5   LYSHISPROHISLEUPHELYSTYRALAALA
6   ASPPROGLNASPLYSHISTRPLEUALAGLU
7   GLNHISHISMETARGALATHRGLYGLYLYS
8   METALATYRLEULEUILEGLUGLUASPILE
9   ARGASPLEUALAALASERASPASPTYRARG
10   GLYCYSLEUASPLEULYSLEUGLUGLULEU
11   LYSSERPHEVALLEUPROSERTRPMETVAL
12   GLULYSMETARGLYSTYRMETGLUTHRLEU
13   ARGTHR

Samples:

sample_1: potassium phosphate 40 mM; DTT 1 mM; sodium azide 1 mM; DNTTIP1(197-316), [U-100% 13C; U-100% 15N], 0.3 mM; H2O 90%; D2O 10%

sample_2: potassium phosphate 40 mM; DTT 1 mM; sodium azide 1 mM; DNTTIP1(197-316), [U-100% 13C; U-100% 15N], 0.3 mM; D2O 100%

sample_conditions_1: ionic strength: 80 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 80 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D CCH-TOCSYsample_2isotropicsample_conditions_2
2D 1H-13C HSQCsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_2

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement

SPARKY v3.1, Goddard - chemical shift assignment

TOPSPIN v2.1, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP Q9H147
PDB
DBJ BAB62888 BAB82521 BAE26320 BAE40293 BAG36715
EMBL CAH93071
GB AAH03486 AAH09535 AAH24290 AAI00641 AAI46176
REF NP_001092346 NP_001126819 NP_001181292 NP_443183 NP_598524
SP A6H7A8 Q5R595 Q91Y53 Q99LB0 Q9H147
TPG DAA23166
AlphaFold Q9H148 A6H7A8 Q5R595 Q91Y53 Q99LB0 Q9H147

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