BMRB Entry 16818

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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/BMR16818
MolProbity Validation Chart

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Title:
Solution structure of a novel Ubiquitin-binding domain from Human PLAA (PUBD, Gly76-Pro77 trans isomer)
Deposition date:
2010-04-01
Original release date:
2010-05-11
Authors:
Fu, Qing-Shan; Zhou, Chen-Jie; Gao, Hong-Chang; Lin, Dong-Hai; Hu, Hong-Yu
Citation:

Citation: Fu, Qing-Shan; Zhou, Chen-Jie; Gao, Hong-Chang; Jiang, Ya-Jun; Zhou, Zi-Ren; Hong, Jing; Yao, Wen-Ming; Song, Ai-Xin; Lin, Dong-Hai; Hu, Hong-Yu. "Structural basis for ubiquitin recognition by a novel domain from human phospholipase A2-activating protein"  J. Biol. Chem. 284, 19043-19052 (2009).
PubMed: 19423704

Assembly members:

Assembly members:
PFUC_trans, polymer, 80 residues, 89.094 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: pET-32M

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PFUC_trans: ANQQTSGKVLYEGKEFDYVF SIDVNEGGPSYKLPYNTSDD PWLTAYNFLQKNDLNPMFLD QVAKFIIDNTKGQMLGLGNP

Data sets:
Data typeCount
13C chemical shifts221
15N chemical shifts87
1H chemical shifts462

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1PFUC_trans1

Entities:

Entity 1, PFUC_trans 80 residues - 89.094 Da.

1   ALAASNGLNGLNTHRSERGLYLYSVALLEU
2   TYRGLUGLYLYSGLUPHEASPTYRVALPHE
3   SERILEASPVALASNGLUGLYGLYPROSER
4   TYRLYSLEUPROTYRASNTHRSERASPASP
5   PROTRPLEUTHRALATYRASNPHELEUGLN
6   LYSASNASPLEUASNPROMETPHELEUASP
7   GLNVALALALYSPHEILEILEASPASNTHR
8   LYSGLYGLNMETLEUGLYLEUGLYASNPRO

Samples:

sample_1: PUBD_trans, [U-100% 13C; U-100% 15N], 1 ± 0.02 mM; NaCl 50 mM; phosphate 20 mM; H2O 90%; D2O 100%

sample_2: PUBD_trans, [U-100% 13C; U-100% 15N], 1 ± 0.02 mM; NaCl 50 mM; phosphate 20 mM; D2O 100%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; 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 C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian Unity 600 MHz

Related Database Links:

BMRB 16848
PDB
DBJ BAA91803 BAA92105 BAD97264 BAE87781 BAG10899
EMBL CAB42881 CAB63739
GB AAD03030 AAD42075 AAH32551 ABW03596 ABW03904
REF NP_001026859 NP_001247477 NP_001270166 XP_002708092 XP_002743032
SP Q9Y263
AlphaFold Q9Y263

Download HSQC peak lists in one of the following formats:
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