BMRB Entry 11265

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PDB ID: 1wxm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11265
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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:

Solution Structure of the N-terminal Ras-binding Domain (RBD) in Human a-Raf Kinase

Deposition date:

2010-08-09

Original release date:

2011-08-18

Authors:

Zhao, C.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Zhao, C.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the N-terminal Ras-binding Domain (RBD) in Human a-Raf Kinase" .

Assembly members:

Assembly members:
Ras-binding domain, polymer, 86 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: cell free synthesis Host organism: E. coli - cell free Vector: P040712-12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ras-binding domain: GSSGSSGGTVKVYLPNKQRT VVTVRDGMSVYDSLDKALKV RGLNQDCCVVYRLIKGRKTV TAWDTAIAPLDGEELIVEVL SGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	338
15N chemical shifts	75
1H chemical shifts	556

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Ras-binding domain	1

Entities:

Entity 1, Ras-binding domain 86 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

THR

VAL

2

LYS

VAL

TYR

LEU

PRO

ASN

LYS

GLN

ARG

THR

3

VAL

THR

VAL

ARG

ASP

GLY

MET

SER

VAL

4

TYR

ASP

SER

LEU

ASP

LYS

ALA

LEU

LYS

VAL

5

ARG

GLY

LEU

ASN

GLN

ASP

CYS

VAL

6

TYR

ARG

LEU

ILE

LYS

GLY

ARG

LYS

THR

VAL

7

THR

ALA

TRP

ASP

THR

ALA

ILE

ALA

PRO

LEU

8

ASP

GLY

GLU

LEU

ILE

VAL

GLU

VAL

LEU

9

SER

GLY

PRO

SER

GLY

Samples:

sample_1: Ras-binding domain, [U-13C; U-15N], 0.86 mM; d-Tris-HCl 20 mM; NaCl 200 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 200 mM; pH: 7.0; pressure: 1 atm; temperature: 296.0 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	sample_1	isotropic	condition_1
3D 13C-separated NOESY	sample_1	isotropic	condition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B. A. - data analysis

Kujira v0.921, Kobayashi, N. - data analysis

CYANA v1.0.8, Guntert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	1WXM 2MSE
DBJ	BAA22379 BAB23522 BAB26674 BAB32131 BAC30217
EMBL	CAA28476 CAA30023
GB	AAA65219 AAB03517 AAB27592 AAH02466 AAH04757
REF	NP_001014964 NP_001028835 NP_001153117 NP_001159362 NP_001243125
SP	O19004 P04627 P10398 P14056
TPG	DAA12857
AlphaFold	O19004 P04627 P10398 P14056