BMRB Entry 11145

Name: Solution structure of the CH domain from human EH domain binding protein 1
Published: 2011-04-01

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PDB ID: 2d89
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11145
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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 CH domain from human EH domain binding protein 1

Deposition date:

2010-03-31

Original release date:

2011-04-01

Authors:

Tomizawa, T.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.

Citation:

Citation: Tomizawa, T.; Kigawa, T.; Koshiba, S.; Inoue, M.; Yokoyama, S.. "Solution structure of the CH domain from human EH domain binding protein 1" .

Assembly members:

Assembly members:
CH domain, polymer, 119 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: P050725-07

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CH domain: GSSGSSGPNASQSLLVWCKE VTKNYRGVKITNFTTSWRNG LSFCAILHHFRPDLIDYKSL NPQDIKENNKKAYDGFASIG ISRLLEPSDMVLLAIPDKLT VMTYLYQIRAHFSSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	520
15N chemical shifts	114
1H chemical shifts	809

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CH domain	1

Entities:

Entity 1, CH domain 119 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

PRO

ASN

ALA

2

SER

GLN

SER

LEU

VAL

TRP

CYS

LYS

GLU

3

VAL

THR

LYS

ASN

TYR

ARG

GLY

VAL

LYS

ILE

4

THR

ASN

PHE

THR

SER

TRP

ARG

ASN

GLY

5

LEU

SER

PHE

CYS

ALA

ILE

LEU

HIS

PHE

6

ARG

PRO

ASP

LEU

ILE

ASP

TYR

LYS

SER

LEU

7

ASN

PRO

GLN

ASP

ILE

LYS

GLU

ASN

LYS

8

LYS

ALA

TYR

ASP

GLY

PHE

ALA

SER

ILE

GLY

9

ILE

SER

ARG

LEU

GLU

PRO

SER

ASP

MET

10

VAL

LEU

ALA

ILE

PRO

ASP

LYS

LEU

THR

11

VAL

MET

THR

TYR

LEU

TYR

GLN

ILE

ARG

ALA

12

HIS

PHE

SER

GLY

PRO

SER

GLY

Samples:

sample_1: CH domain, [U-13C; U-15N], 0.85 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: 296 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 v0.932, Kobayashi, N. - data analysis

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

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	2D89
DBJ	BAA74926 BAD32333 BAF85234
EMBL	CAD38814
GB	AAH67215 AAI68392 AAL24806 AAQ97141 AAS48537
REF	NP_001136086 NP_001136087 NP_001136088 NP_001239444 NP_001248495
SP	Q69ZW3 Q8NDI1
TPG	DAA24644 DAA24645 DAA24646
AlphaFold	Q69ZW3 Q8NDI1