BMRB Entry 11295

Name: Solution structure of the RWD domain of human protein C21orf6
Published: 2011-08-19

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PDB ID: 2dax
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11295
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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 RWD domain of human protein C21orf6

Deposition date:

2010-08-09

Original release date:

2011-08-19

Authors:

Yoneyama, M.; Kigawa, T.; Saito, K.; Tochio, N.; Koshiba, S.; Inoue, M.; Yokoyama, S.

Citation:

Citation: Yoneyama, M.; Kigawa, T.; Saito, K.; Tochio, N.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of the RWD domain of human protein C21orf6" .

Assembly members:

Assembly members:
RWD domain, polymer, 152 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: P050302-87

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RWD domain: GSSGSSGEQAEAQLAELDLL ASMFPGENELIVNDQLAVAE LKDCIEKKTMEGRSSKVYFT INMNLDVSDEKMAMFSLACI LPFKYPAVLPEITVRSVLLS RSQQTQLNTDLTAFLQKHCH GDVCILNATEWVREHASGYV SRDTSSSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	613
15N chemical shifts	147
1H chemical shifts	996

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RWD domain	1

Entities:

Entity 1, RWD domain 152 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

GLU

GLN

ALA

2

GLU

ALA

GLN

LEU

ALA

GLU

LEU

ASP

LEU

3

ALA

SER

MET

PHE

PRO

GLY

GLU

ASN

GLU

LEU

4

ILE

VAL

ASN

ASP

GLN

LEU

ALA

VAL

ALA

GLU

5

LEU

LYS

ASP

CYS

ILE

GLU

LYS

THR

MET

6

GLU

GLY

ARG

SER

LYS

VAL

TYR

PHE

THR

7

ILE

ASN

MET

ASN

LEU

ASP

VAL

SER

ASP

GLU

8

LYS

MET

ALA

MET

PHE

SER

LEU

ALA

CYS

ILE

9

LEU

PRO

PHE

LYS

TYR

PRO

ALA

VAL

LEU

PRO

10

GLU

ILE

THR

VAL

ARG

SER

VAL

LEU

SER

11

ARG

SER

GLN

THR

GLN

LEU

ASN

THR

ASP

12

LEU

THR

ALA

PHE

LEU

GLN

LYS

HIS

CYS

HIS

13

GLY

ASP

VAL

CYS

ILE

LEU

ASN

ALA

THR

GLU

14

TRP

VAL

ARG

GLU

HIS

ALA

SER

GLY

TYR

VAL

15

SER

ARG

ASP

THR

SER

GLY

PRO

SER

16

SER

GLY

Samples:

sample_1: RWD domain, [U-13C; U-15N], 1.26 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 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 v3.5, Bruker - collection

NMRPipe v20030801, Delaglio, F. - processing

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

Kujira v0.9318, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	2DAX
DBJ	BAA90913 BAD97077 BAK64033
EMBL	CAB88085 CAB90431
GB	AAH12546 AAH17912 AAK14918 ADQ32121 AIC50494
REF	NP_001267094 NP_058636 XP_003813235 XP_003927746 XP_004062697
SP	P57060
AlphaFold	P57060