BMRB Entry 15775

Name: Backbone chemical shift assignment for the transmembrane and C-terminal domains of amyloid precursor protein (APP C99)
Published: 2008-08-19

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PDB ID: 2lp1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15775
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
APP_C99: MDAEFRHDSGYEVHHQKLVF FAEDVGSNKGAIIGLMVGGV VIATVIVITLVMLKKKQYTS IHHGVVEVDAAVTPEERHLS KMQQNGYENPTYKFFEQMQN QGRILQISITLAAALEHHHH HH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	284
15N chemical shifts	99
1H chemical shifts	99

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	APP C99	1

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

MET

ASP

ALA

GLU

PHE

ARG

HIS

ASP

SER

GLY

2

TYR

GLU

VAL

HIS

GLN

LYS

LEU

VAL

PHE

3

PHE

ALA

GLU

ASP

VAL

GLY

SER

ASN

LYS

GLY

4

ALA

ILE

GLY

LEU

MET

VAL

GLY

VAL

5

VAL

ILE

ALA

THR

VAL

ILE

VAL

ILE

THR

LEU

6

VAL

MET

LEU

LYS

GLN

TYR

THR

SER

7

ILE

HIS

GLY

VAL

GLU

VAL

ASP

ALA

8

ALA

VAL

THR

PRO

GLU

ARG

HIS

LEU

SER

9

LYS

MET

GLN

ASN

GLY

TYR

GLU

ASN

PRO

10

THR

TYR

LYS

PHE

GLU

GLN

MET

GLN

ASN

11

GLN

GLY

ARG

ILE

LEU

GLN

ILE

SER

ILE

THR

12

LEU

ALA

LEU

GLU

HIS

13

HIS

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1

Software:

FELIX v2000, Accelrys Software Inc. - chemical shift assignment

NMR spectrometers:

Varian INOVA 900 MHz

PDB	2LP1
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 P08592 P12023 P53601 P79307