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 15047

Title: Ubiquitin in 8 M Urea   PubMed: 17243799

Deposition date: 2006-11-21 Original release date: 2006-12-11

Authors: Meier, Sebastian; Strohmeier, Mark; Blackledge, Martin; Grzesiek, Stephan

Citation: Meier, Sebastian; Strohmeier, Mark; Blackledge, Martin; Grzesiek, Stephan. "Direct Observation of Dipolar Couplings and Hydrogen Bonds across a beta-hairpin in 8 M Urea"  J. Am. Chem. Soc. 129, 754-755 (2007).

Assembly members:
denatured_ubiquitin, polymer, 76 residues, Formula weight is not available

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   Vector: pET21b+

Entity Sequences (FASTA):
denatured_ubiquitin: MQIFVKTLTGKTITLEVEPS DTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG

Data sets:
Data typeCount
13C chemical shifts71
15N chemical shifts72
1H chemical shifts72

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ubiquitin1

Entities:

Entity 1, ubiquitin 76 residues - Formula weight is not available

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

Samples:

sample_1: denatured ubiquitin, [U-13C; U-15N; U-2H], 2.5 mM; H2O 55.5 M; D2O, [U-2H], 5%; urea 8 M

sample_conditions_1: ionic strength: 20 mM; pH: 2.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N ROESYsample_1isotropicsample_conditions_1
3D 15N HNHN-COSYsample_1anisotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

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

PIPP, Garrett - data analysis

xwinnmr, Bruker Biospin - collection

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

BMRB 11505 11547 15410 15689 15907 16228 16582 16626 16895 17181 17439 17769 17919 18582 18583 18584 18610 18611 18737 19406 19412 25070 25123 25601 26604 4245 4375
PDB
DBJ BAA03983 BAA09860 BAA11842 BAA11843 BAA23486
EMBL CAA25706 CAA26488 CAA28495 CAA30183 CAA30815
GB AAA02769 AAA28154 AAA28997 AAA28998 AAA28999
PIR I50437 I51568 I65237 JN0790 S13928
PRF 0412265A 1101405A 1212243A 1212243B 1212243C
REF NP_001005123 NP_001006688 NP_001009117 NP_001009202 NP_001009286
SP P0C273 P0C275 P0C276 P0CG47 P0CG48
TPD FAA00319
TPE CEL68433 CEL70397 CEL75964 CEL78064
TPG DAA18802 DAA20663 DAA20672 DAA24675 DAA28295
AlphaFold P0CG48 P0CG47 P0C275 P0C276 P0C273

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