BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 19801

Click here to enlarge.

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/BMR19801
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: solution structure of a protein C-terminal domain   PubMed: 24752541

Deposition date: 2014-02-17 Original release date: 2015-01-05

Authors: Feng, Yingang; Jiao, Lianying

Citation: Jiao, Lianying; Ouyang, Songying; Shaw, Neil; Song, Gaojie; Feng, Yingang; Niu, Fengfeng; Qiu, Weicheng; Zhu, Hongtao; Hung, Li-Wei; Zuo, Xiaobing; Shtykova, V. Eleonora; Zhu, Ping; Dong, Yu-Hui; Xu, Ruxiang; Liu, Zhi-Jie. "Mechanism of the Rpn13-induced activation of Uch37"  Protein Cell 5, 616-630 (2014).

Assembly members:
entity, polymer, 141 residues, 14822.638 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):
entity: SNAILATMNVPAGPAGGQQV DLASVLTPEIMAPILANADV QERLLPYLPSGESLPQTADE IQNTLTSPQFQQALGMFSAA LASGQLGPLMCQFGLPAEAV EAANKGDVEAFAKAMQNNAK PEQKEGDTKDKKDEEEDMSL D

Data sets:
Data typeCount
13C chemical shifts577
15N chemical shifts146
1H chemical shifts942

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein C-terminal domain1

Entities:

Entity 1, protein C-terminal domain 141 residues - 14822.638 Da.

1   SERASNALAILELEUALATHRMETASNVAL
2   PROALAGLYPROALAGLYGLYGLNGLNVAL
3   ASPLEUALASERVALLEUTHRPROGLUILE
4   METALAPROILELEUALAASNALAASPVAL
5   GLNGLUARGLEULEUPROTYRLEUPROSER
6   GLYGLUSERLEUPROGLNTHRALAASPGLU
7   ILEGLNASNTHRLEUTHRSERPROGLNPHE
8   GLNGLNALALEUGLYMETPHESERALAALA
9   LEUALASERGLYGLNLEUGLYPROLEUMET
10   CYSGLNPHEGLYLEUPROALAGLUALAVAL
11   GLUALAALAASNLYSGLYASPVALGLUALA
12   PHEALALYSALAMETGLNASNASNALALYS
13   PROGLUGLNLYSGLUGLYASPTHRLYSASP
14   LYSLYSASPGLUGLUGLUASPMETSERLEU
15   ASP

Samples:

sample_1: entity, [U-13C; U-15N], 0.5 – 1.0 mM; sodium phosphate 40 mM; potassium chloride 20 mM; DSS 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 80 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_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

Software:

xwinnmr, Bruker Biospin - collection

Felix, Accelrys Software Inc. - chemical shift assignment, processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

SANE, Duggan, Legge, Dyson & Wright - refinement

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

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

BMRB 17286
PDB
DBJ BAA11023 BAJ20420
GB AAH10733 AAH17245 AAX42432 ABM84246 ABM87634
REF NP_001247458 NP_001268366 NP_001268367 NP_008933 NP_783163
SP Q16186
TPD FAA00246

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts