BMRB Entry 4084

Title:
Determination of the Secondary Structure and Folding Topology of an RNA Binding Domain of Mammalian hnRNP A1 Protein Using Three-Dimensional Heteronuclear Magnetic Resonance Spectroscopy
Deposition date:
1997-12-23
Original release date:
2001-02-17
Authors:
Garrett, Daniel; Lodi, Patricia; Shamoo, Yousif; Williams, Kenneth; Clore, G.; Gronenborn, Angela
Citation:

Citation: Garrett, Daniel; Lodi, Patricia; Shamoo, Yousif; Williams, Kenneth; Clore, G.; Gronenborn, Angela. "Determination of the Secondary Structure and Folding Topology of an RNA Binding Domain of Mammalian nhRNP A1 Protein Using Three-Dimensional Heteronuclear Magnetic Resonance Spectroscopy"  Biochemistry 33, 2852-2858 (1994).

Assembly members:

Assembly members:
human hnRNP A1, polymer, 93 residues, Formula weight is not available

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: pYS45

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts274
15N chemical shifts92
1H chemical shifts577

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hnRNP(A1)1

Entities:

Entity 1, hnRNP(A1) 93 residues - Formula weight is not available

1   METSERLYSSERGLUSERPROLYSGLUPRO
2   GLUGLNLEUARGLYSLEUPHEILEGLYGLY
3   LEUSERPHEGLUTHRTHRASPGLUSERLEU
4   ARGSERHISPHEGLUGLNTRPGLYTHRLEU
5   THRASPCYSVALVALMETARGASPPROASN
6   THRLYSARGSERARGGLYPHEGLYPHEVAL
7   THRTYRALATHRVALGLUGLUVALASPALA
8   ALAMETASNALAARGPROHISLYSVALASP
9   GLYARGVALVALGLUPROLYSARGALAVAL
10   SERARGGLU

Samples:

sample_one: human hnRNP A1, [U-15N], 2 mM; D2O 10%; H2O 90%

sample_two: human hnRNP A1, [U-13C; U-15N], 2 mM; D2O 10%; H2O 90%

sample_three: human hnRNP A1, [U-15N], 2 mM; D2O 99.996%

sample_four: human hnRNP A1, [U-13C; U-15N], 2 mM; D2O 99.996%

sample_conditions: pH: 5.7; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions

Software:

No software information available

NMR spectrometers:

  • Bruker AM 600 MHz

Related Database Links:

DBJ BAG60447 BAG64377
GB AAP78702 ELK35268
REF XP_004274506 XP_007659907 XP_012323839

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