BMRB Entry 6236

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PDB ID: 1tkn
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6236
MolProbity Validation Chart

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

Deposition date:

2004-06-11

Original release date:

2004-09-01

Authors:

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

Citation:

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).
PubMed: 15274612

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- shift_set_1

Data type	Count
1H chemical shifts	897
13C chemical shifts	545
15N chemical shifts	129

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	APP fragment, CAPPD*	1

Entities:

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

1

ARG

VAL

GLU

ALA

MET

LEU

ASN

ASP

ARG

2

ARG

LEU

ALA

LEU

GLU

ASN

TYR

ILE

THR

ALA

3

LEU

GLN

ALA

VAL

PRO

ARG

PRO

ARG

HIS

4

VAL

PHE

ASN

MET

LEU

LYS

TYR

VAL

ARG

5

ALA

GLU

GLN

LYS

ASP

ARG

GLN

HIS

THR

LEU

6

LYS

HIS

PHE

GLU

HIS

VAL

ARG

MET

VAL

ASP

7

PRO

LYS

ALA

GLN

ILE

ARG

SER

GLN

8

VAL

MET

THR

HIS

LEU

ARG

VAL

ILE

TYR

GLU

9

ARG

MET

ASN

GLN

SER

LEU

SER

LEU

TYR

10

ASN

VAL

PRO

ALA

VAL

ALA

GLU

ILE

GLN

11

ASP

GLU

VAL

ASP

GLU

LEU

GLN

LYS

GLU

12

GLN

ASN

TYR

SER

ASP

VAL

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:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY-HSQC and TOCSY-HSQC	not available	not available	not available
HNCO, HNCACB	not available	not available	not available
H(C)(CO)NH-TOCSY	not available	not available	not available
(H)C(CO)NH-TOCSY	not available	not available	not available
HCCH-TOCSY	not available	not available	not available

Software:

VNMR v6.1 -

NMR spectrometers:

Varian INOVA 500 MHz

PDB	1TKN 3NYL 3UMH 3UMI 3UMK
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
AlphaFold	P05067 P08592 P12023 P53601 P79307