BMRB Entry 4641

Name: Human Prion Protein Mutant E200K Fragment 90-231
Published: 2001-05-17

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PDB ID: 1fo7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4641
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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:

Human Prion Protein Mutant E200K Fragment 90-231

Deposition date:

2000-08-25

Original release date:

2001-05-17

Authors:

Zhang, Y.; Swietnicki, W.; Zagorski, M.; Surewicz, W.; Soennichsen, F.

Citation:

Citation: Zhang, Y.; Swietnicki, W.; Zagorski, M.; Surewicz, W.; Soennichsen, F.. "Solution structure of Human Prion Protein Mutant E200K Fragment 90-231" J. Biol. Chem. 275, 33650-33654 (2000).

Assembly members:

Assembly members:
PRION PROTEIN, polymer, 146 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: PRSETB

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PRION PROTEIN: GSDPGQGGGTHSQWNKPSKP KTNMKHMAGAAAAGAVVGGL GGYMLGSAMSRPIIHFGSDY EDRYYRENMHRYPNQVYYRP MDEYSNQNNFVHDCVNITIK QHTVTTTTKGENFTKTDVKM MERVVEQMCITQYERESQAY YQRGSS

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1
coupling_constants
- J_values

Data type	Count
13C chemical shifts	593
1H chemical shifts	929
15N chemical shifts	162
coupling constants	44

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PRION PROTEIN	1

Entities:

Entity 1, PRION PROTEIN 146 residues - Formula weight is not available

1

GLY

SER

ASP

PRO

GLY

GLN

GLY

THR

2

HIS

SER

GLN

TRP

ASN

LYS

PRO

SER

LYS

PRO

3

LYS

THR

ASN

MET

LYS

HIS

MET

ALA

GLY

ALA

4

ALA

GLY

ALA

VAL

GLY

LEU

5

GLY

TYR

MET

LEU

GLY

SER

ALA

MET

SER

6

ARG

PRO

ILE

HIS

PHE

GLY

SER

ASP

TYR

7

GLU

ASP

ARG

TYR

ARG

GLU

ASN

MET

HIS

8

ARG

TYR

PRO

ASN

GLN

VAL

TYR

ARG

PRO

9

MET

ASP

GLU

TYR

SER

ASN

GLN

ASN

PHE

10

VAL

HIS

ASP

CYS

VAL

ASN

ILE

THR

ILE

LYS

11

GLN

HIS

THR

VAL

THR

LYS

GLY

12

GLU

ASN

PHE

THR

LYS

THR

ASP

VAL

LYS

MET

13

MET

GLU

ARG

VAL

GLU

GLN

MET

CYS

ILE

14

THR

GLN

TYR

GLU

ARG

GLU

SER

GLN

ALA

TYR

15

TYR

GLN

ARG

GLY

SER

Samples:

sample_1: PRION PROTEIN, [U-15N; U-13C], 0.8 mM; acetate buffer 10 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 4.6; temperature: 299 K; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	sample_1	not available	sample_cond_1
3D 15N-separated NOESY	sample_1	not available	sample_cond_1
2D NOESY	sample_1	not available	sample_cond_1
HNHA	sample_1	not available	sample_cond_1

Software:

NMRPipe vsgi6x.m4 - processing

FELIX v98 - processing

PIPP v4.24 - data analysis

ARIA v0.9 - structure solution

CNS v0.9 - structure solution, refinement

NMR spectrometers:

Bruker DRX 800 MHz

BMRB	15676 16743 16757 17714 17756 17757 17780 18426 18550 19268 4379 4402 4434 4620 4736
PDB	1E1G 1E1J 1E1P 1E1S 1E1U 1E1W 1FKC 1FO7 1HJM 1HJN 1I4M 1QLX 1QLZ 1QM0 1QM1 1QM2 1QM3 2K1D 2KUN 2LEJ 2LFT 2LSB 2LV1 2M8T 2W9E 3HAF 3HAK 3HEQ 3HER 3HES 3HJ5 3HJX 4DGI 4KML 4N9O
DBJ	BAF62360 BAG32276 BAG32278 BAG52189 BAG56832
EMBL	CAA58442 CAG46836
GB	AAA60182 AAA68632 AAB59442 AAB59443 AAC05365
REF	NP_000302 NP_001009093 NP_001073590 NP_001073591 NP_001073592
SP	P04156 P61766 P61767 P61768
AlphaFold	P04156 P61766 P61767 P61768