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BMRB Entry 19399

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19399
MolProbity Validation Chart

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Title: NMR structure of EKLF(22-40)/Ubiquitin Complex   PubMed: 24139988

Deposition date: 2013-07-31 Original release date: 2013-10-08

Authors: Raiola, Luca; Omichinski, James

Citation: Raiola, Luca; Lussier-Price, Mathieu; Gagnon, David; Lafrance-Vanasse, Julien; Mascle, Xavier; Arseneault, Genevieve; Legault, Pascale; Archambault, Jacques; Omichinski, James. "Structural Characterization of a Noncovalent Complex between Ubiquitin and the Transactivation Domain of the Erythroid-Specific Factor EKLF."  Structure 21, 2014-2024 (2013).

Assembly members:
EKLF, polymer, 19 residues, 2359.502 Da.
Ubiquitin, polymer, 76 residues, 8576.914 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
EKLF: DTQDDFLKWWRSEEAQDMG
Ubiquitin: MQIFVKTLTGKTITLEVEPS DTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG

Data sets:
Data typeCount
13C chemical shifts339
15N chemical shifts101
1H chemical shifts693

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1EKLF1
2Ubiquitin2

Entities:

Entity 1, EKLF 19 residues - 2359.502 Da.

1   ASPTHRGLNASPASPPHELEULYSTRPTRP
2   ARGSERGLUGLUALAGLNASPMETGLY

Entity 2, Ubiquitin 76 residues - 8576.914 Da.

1   METGLNILEPHEVALLYSTHRLEUTHRGLY
2   LYSTHRILETHRLEUGLUVALGLUPROSER
3   ASPTHRILEGLUASNVALLYSALALYSILE
4   GLNASPLYSGLUGLYILEPROPROASPGLN
5   GLNARGLEUILEPHEALAGLYLYSGLNLEU
6   GLUASPGLYARGTHRLEUSERASPTYRASN
7   ILEGLNLYSGLUSERTHRLEUHISLEUVAL
8   LEUARGLEUARGGLYGLY

Samples:

sample_1: Ubi_unl 4 mM; EKLF, [U-100% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_2: EKLF_unl 4 mM; Ubiquitin, [U-100% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_3: EKLF_unl 4 mM; Ubiquitin, [U-100% 13C; U-100% 15N], 0.8 mM; D2O 100%

sample_4: Ubi_unl 4 mM; phosphate buffer 20 mM; EKLF, [U-100% 13C; U-100% 15N], 0.8 mM; D2O 100%

conditions_1: ionic strength: 20 mM; pH: 6.5; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicconditions_1
3D 1H-13C NOESYsample_4isotropicconditions_1
3D 1H-15N NOESYsample_2isotropicconditions_1
3D 1H-13C NOESYsample_3isotropicconditions_1

Software:

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

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAG73333 BAA03983 BAA09860 BAA11842 BAA11843 BAA23486
GB AAB51173 AAC50562 AAC51108 AAH33580 AFW90650 AAA02769 AAA28154 AAA28997 AAA28998 AAA28999
REF NP_001181384 NP_006554 XP_002761831 XP_002828790 XP_003275639 NP_001005123 NP_001006688 NP_001009117 NP_001009202 NP_001009286
SP Q13351 P0C273 P0C275 P0C276 P0CG47 P0CG48
BMRB 11505 11547 15047 15410 15689 15866 15907 16228 16582 16626 16763 16880 16885 16895 17059 17181 17239 17333 17439 17769 17919 18582 18583 18584 18610 18611 18737 19394 19406 19412 19447 25070 25230 4245 4375 4983 5101 5387 6457 6466 6470 6488 68 7111
EMBL CAA25706 CAA26488 CAA28495 CAA30183 CAA30815
PIR I50437 I51568 I65237 JN0790 S13928
PRF 0412265A 1101405A 1212243A 1212243B 1212243C
TPD FAA00319
TPG DAA18802 DAA20663 DAA20672 DAA24675 DAA28295

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