BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 6236

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for CAPPD*, an Independently Folded Extracellular Domain of Human Amyloid-beta Precursor Protein   PubMed: 15274612

Deposition date: 2004-06-11 Original release date: 2004-09-01

Authors: Dulubova, Irina; Ho, Angela; Huryeva, Iryna; Sudhof, Thomas; Rizo, Josep

Citation: Dulubova, Irina; Ho, Angela; Huryeva, Iryna; Sudhof, Thomas; Rizo, Josep. "Three-Dimensional Structure of an Independently Folded Extracellular Domain of Human Amyloid-beta Precursor Protein"  Biochemistry 43, 9583-9588 (2004).

Assembly members:
Amyloid-beta Precursor Protein, polymer, 117 residues, Formula weight is not available

Natural source:   Common Name: 9606   Taxonomy ID: Human   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo Sapiens

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

Entity Sequences (FASTA):
Amyloid-beta Precursor Protein: RVEAMLNDRRRLALENYITA LQAVPPRPRHVFNMLKKYVR AEQKDRQHTLKHFEHVRMVD PKKAAQIRSQVMTHLRVIYE RMNQSLSLLYNVPAVAEEIQ DEVDELLQKEQNYSDDV

Data sets:
Data typeCount
1H chemical shifts897
13C chemical shifts545
15N chemical shifts129

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1APP fragment, CAPPD*1

Entities:

Entity 1, APP fragment, CAPPD* 117 residues - Formula weight is not available

1   ARGVALGLUALAMETLEUASNASPARGARG
2   ARGLEUALALEUGLUASNTYRILETHRALA
3   LEUGLNALAVALPROPROARGPROARGHIS
4   VALPHEASNMETLEULYSLYSTYRVALARG
5   ALAGLUGLNLYSASPARGGLNHISTHRLEU
6   LYSHISPHEGLUHISVALARGMETVALASP
7   PROLYSLYSALAALAGLNILEARGSERGLN
8   VALMETTHRHISLEUARGVALILETYRGLU
9   ARGMETASNGLNSERLEUSERLEULEUTYR
10   ASNVALPROALAVALALAGLUGLUILEGLN
11   ASPGLUVALASPGLULEULEUGLNLYSGLU
12   GLNASNTYRSERASPASPVAL

Samples:

sample_1: Amyloid-beta Precursor Protein, [U-99% 15N], 0.85 mM; sodium phosphate 50 mM; NaCl 250 mM; Guanidinium Chloride 300 mM; D2O 5%

sample_2: Amyloid-beta Precursor Protein, [U-99% 15N; U-13C], 0.85 mM; sodium phosphate 50 mM; NaCl 250 mM; Guanidinium Chloride 300 mM; D2O 5%

Ex-cond_1: pH: 6.4; temperature: 300 K; ionic strength: 0.6 M

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESY-HSQC and TOCSY-HSQCnot availablenot availablenot available
HNCO, HNCACBnot availablenot availablenot available
H(C)(CO)NH-TOCSYnot availablenot availablenot available
(H)C(CO)NH-TOCSYnot availablenot availablenot available
HCCH-TOCSYnot availablenot availablenot available

Software:

VNMR v6.1 -

NMR spectrometers:

  • Varian INOVA 500 MHz

Related Database Links:

PDB
DBJ BAA22264 BAA84580 BAC36369 BAD51938 BAE01907
EMBL CAA30050 CAA30488 CAA31830 CAA53090 CAA66230
GB AAA36829 AAA51722 AAA51726 AAA58727 AAB41502
PRF 1303338A 1403400A 1507304A 1507304B
REF NP_000475 NP_001006601 NP_001013036 NP_001070264 NP_001127014
SP P05067 P08592 P12023 P53601 P79307
TPG DAA33655

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