BMRB Entry 4463

Name: Sequential NMR assignment of the Ras-binding domain of Byr2
Published: 2000-12-15

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4463

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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:

Sequential NMR assignment of the Ras-binding domain of Byr2

Deposition date:

1999-11-22

Original release date:

2000-12-15

Authors:

Huber, Fritz; Gronwald, Wolfram; Wohlgemuth, Sabine; Herrmann, Christian; Geyer, Matthias; Wittinghofer, Alfred; Kalbitzer, Hans

Citation:

Citation: Huber, Fritz; Gronwald, Wolfram; Wohlgemuth, Sabine; Herrmann, Christian; Geyer, Matthias; Wittinghofer, Alfred; Kalbitzer, Hans. "Letter to the Editor: Sequential NMR Assignment of the RAS-binding Domain of Byr2" J. Biomol. NMR 16, 355-356 (2000).

Assembly members:

Assembly members:
Byr2, polymer, 116 residues, 13193 Da.

Natural source:

Natural source: Common Name: fission yeast Taxonomy ID: 4896 Superkingdom: Eukaryota Kingdom: not available Genus/species: Schizosaccharomyces pombe

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX4T3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Byr2: REFPRPCILRFIACNGQTRA VQSRGDYQKTLAIALKKFSL EDASKFIVCVSQSSRIKLIT EEEFKQICFNSSSPERDRLI IVPKEKPCPSFEDLRRSWEI ELAQPAALSSQSSLSP

Data sets:

assigned_chemical_shifts
- Byrshift

Data type	Count
1H chemical shifts	584
13C chemical shifts	217
15N chemical shifts	110

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Byr2	1

Entities:

Entity 1, Byr2 116 residues - 13193 Da.

1

ARG

GLU

PHE

PRO

ARG

PRO

CYS

ILE

LEU

ARG

2

PHE

ILE

ALA

CYS

ASN

GLY

GLN

THR

ARG

ALA

3

VAL

GLN

SER

ARG

GLY

ASP

TYR

GLN

LYS

THR

4

LEU

ALA

ILE

ALA

LEU

LYS

PHE

SER

LEU

5

GLU

ASP

ALA

SER

LYS

PHE

ILE

VAL

CYS

VAL

6

SER

GLN

SER

ARG

ILE

LYS

LEU

ILE

THR

7

GLU

PHE

LYS

GLN

ILE

CYS

PHE

ASN

8

SER

PRO

GLU

ARG

ASP

ARG

LEU

ILE

9

ILE

VAL

PRO

LYS

GLU

LYS

PRO

CYS

PRO

SER

10

PHE

GLU

ASP

LEU

ARG

SER

TRP

GLU

ILE

11

GLU

LEU

ALA

GLN

PRO

ALA

LEU

SER

12

GLN

SER

LEU

SER

PRO

Samples:

sample_1: Byr2, [U-13C; U-15N], 0.7 mM; phosphate buffer 20 mM; DTE 25 mM; glycine, [U-2H], 0.200 M

sample_2: Byr2, [U-15N], 1.2 mM

sample_3: Byr2 1.2 mM

sample_1_conditions: pH: 6.9; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
CBCA(CO)NH	not available	not available	sample_1_conditions
CBCANH	not available	not available	sample_1_conditions
HBHA(CO)NH	not available	not available	sample_1_conditions
HNCA	not available	not available	sample_1_conditions
HN(CO)CA	not available	not available	sample_1_conditions
TOCSY-HSQC	not available	not available	sample_1_conditions
NOESY-HSQC	not available	not available	sample_1_conditions
HCCH-TOCSY	not available	not available	sample_1_conditions
HNHA	not available	not available	sample_1_conditions
2D NOESY and TOCSY spectra measured in H2O	not available	not available	sample_1_conditions
and D2O.	not available	not available	sample_1_conditions
2D 1H-15N and 1H-13C HSQC	not available	not available	sample_1_conditions

Software:

XWINNMR v2.5 - aquisition and processing of spectra

AURELIA v2.5 - sequence specific assignment

NMR spectrometers:

Bruker DRX 600 MHz
Bruker DRX 800 MHz

PDB	1I35 1K8R
EMBL	CAA48731 CAB10150
GB	AAA35289
REF	NP_595714
SP	P28829
AlphaFold	P28829