BMRB Entry 15775

Title:
Backbone chemical shift assignment for the transmembrane and C-terminal domains of amyloid precursor protein (APP C99)
Deposition date:
2008-05-15
Original release date:
2008-08-19
Authors:
Sanders, Charles
Citation:

Citation: Beel, Andrew; Mobley, Charles; Kim, Hak; Tian, Fang; Hadziselimovic, Arina; Jap, Bing; Prestegard, James; Sanders, Charles. "Structural Studies of the Transmembrane C-Terminal Domain of the Amyloid Precursor Protein (APP): Does APP Function as a Cholesterol Sensor?"  Biochemistry 47, 9428-9446 (2008).
PubMed: 18702528

Assembly members:

Assembly members:
APP_C99, polymer, 122 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: pET-21a

Data sets:
Data typeCount
13C chemical shifts284
15N chemical shifts99
1H chemical shifts99

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1APP C991

Entities:

Entity 1, APP C99 122 residues - Formula weight is not available

Residues 101 to 122 represent a non-native tag; The N-terminal Met residues corresponds to site 671 in the amyloid precursor protein (APP); Asn100 represents the C-terminal residues 770 of the full length APP

1   METASPALAGLUPHEARGHISASPSERGLY
2   TYRGLUVALHISHISGLNLYSLEUVALPHE
3   PHEALAGLUASPVALGLYSERASNLYSGLY
4   ALAILEILEGLYLEUMETVALGLYGLYVAL
5   VALILEALATHRVALILEVALILETHRLEU
6   VALMETLEULYSLYSLYSGLNTYRTHRSER
7   ILEHISHISGLYVALVALGLUVALASPALA
8   ALAVALTHRPROGLUGLUARGHISLEUSER
9   LYSMETGLNGLNASNGLYTYRGLUASNPRO
10   THRTYRLYSPHEPHEGLUGLNMETGLNASN
11   GLNGLYARGILELEUGLNILESERILETHR
12   LEUALAALAALALEUGLUHISHISHISHIS
13   HISHIS

Samples:

sample_1: APP C99, [U-100% 13C; U-100% 15N; 80% 2H], 2.5 mM; LMPG micelle 9%; imidazole-acetate 250 mM; EDTA 1 mM

sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1

Software:

FELIX v2000, Accelrys Software Inc. - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 900 MHz

Related Database Links:

PDB
DBJ BAA22264 BAA84580 BAC34997 BAC36369 BAE01907
EMBL CAA30050 CAA30488 CAA31830 CAA66230 CAA68374
GB AAA35540 AAA36829 AAA37139 AAA51722 AAA51726
PIR PQ0438
PRF 1303338A 1403400A 1507304A 1507304B 1507304C
REF NP_000475 NP_001006601 NP_001013036 NP_001070264 NP_001127014
SP P05067 P08592 P12023 P53601 P79307
TPG DAA33655
AlphaFold P05067 P79307 P53601 P12023 P08592

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