BMRB Entry 11143

Name: Solution structure of the CH domain from human MICAL-3 protein
Published: 2011-04-01

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PDB ID: 2d88
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11143
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of the CH domain from human MICAL-3 protein

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 MICAL-3 protein" .

Assembly members:

Assembly members:
CH domain, polymer, 121 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: P050627-23

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CH domain: GSSGSSGVARSSKLLGWCQR QTDGYAGVNVTDLTMSWKSG LALCAIIHRYRPDLIDFDSL DEQNVEKNNQLAFDIAEKEL GISPIMTGKEMASVGEPDKL SMVMYLTQFYEMFKDSGPSS G

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	509
15N chemical shifts	119
1H chemical shifts	806

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 121 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

VAL

ALA

ARG

2

SER

LYS

LEU

GLY

TRP

CYS

GLN

ARG

3

GLN

THR

ASP

GLY

TYR

ALA

GLY

VAL

ASN

VAL

4

THR

ASP

LEU

THR

MET

SER

TRP

LYS

SER

GLY

5

LEU

ALA

LEU

CYS

ALA

ILE

HIS

ARG

TYR

6

ARG

PRO

ASP

LEU

ILE

ASP

PHE

ASP

SER

LEU

7

ASP

GLU

GLN

ASN

VAL

GLU

LYS

ASN

GLN

8

LEU

ALA

PHE

ASP

ILE

ALA

GLU

LYS

GLU

LEU

9

GLY

ILE

SER

PRO

ILE

MET

THR

GLY

LYS

GLU

10

MET

ALA

SER

VAL

GLY

GLU

PRO

ASP

LYS

LEU

11

SER

MET

VAL

MET

TYR

LEU

THR

GLN

PHE

TYR

12

GLU

MET

PHE

LYS

ASP

SER

GLY

PRO

SER

13

GLY

Samples:

sample_1: CH domain, [U-13C; U-15N], 1.12 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	2D88
DBJ	BAA92602 BAG10388
GB	AAI57877 AAI71887 EFB16615 EGW04922 EHB13700
REF	NP_001129476 NP_056056 XP_002722588 XP_002926775 XP_003278377
SP	Q7RTP6
AlphaFold	Q7RTP6