BMRB Entry 10068

Name: Solution Structure of the CH domain from Mouse Trangelin
Published: 2008-08-14

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PDB ID: 1ujo
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10068
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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 Mouse Trangelin

Deposition date:

2006-12-25

Original release date:

2008-08-14

Authors:

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

Citation:

Citation: Tomizawa, T.; Koshiba, S.; Kigawa, T.; Yokoyama, S.. "Solution Structure of the CH domain from Mouse Trangelin" .

Assembly members:

Assembly members:
Calponin homology (CH) domain, polymer, 144 residues, Formula weight is not available

Natural source:

Natural source: Common Name: mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: cell free synthesis Vector: P020520-56

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Calponin homology (CH) domain: GSSGSSGEELEERLVEWIVV QCGPDVGRPDRGRLGFQVWL KNGVILSKLVNSLYPEGSKP VKVPENPPSMVFKQMEQVAQ FLKAAEDYGVIKTDMFQTVD LYEGKDMAAVQRTLMALGSL AVTKNDGNYRGDPNWFMKSG PSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	609
15N chemical shifts	146
1H chemical shifts	989

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Transgelin	1

Entities:

Entity 1, Transgelin 144 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

GLU

LEU

2

GLU

ARG

LEU

VAL

GLU

TRP

ILE

VAL

3

GLN

CYS

GLY

PRO

ASP

VAL

GLY

ARG

PRO

ASP

4

ARG

GLY

ARG

LEU

GLY

PHE

GLN

VAL

TRP

LEU

5

LYS

ASN

GLY

VAL

ILE

LEU

SER

LYS

LEU

VAL

6

ASN

SER

LEU

TYR

PRO

GLU

GLY

SER

LYS

PRO

7

VAL

LYS

VAL

PRO

GLU

ASN

PRO

SER

MET

8

VAL

PHE

LYS

GLN

MET

GLU

GLN

VAL

ALA

GLN

9

PHE

LEU

LYS

ALA

GLU

ASP

TYR

GLY

VAL

10

ILE

LYS

THR

ASP

MET

PHE

GLN

THR

VAL

ASP

11

LEU

TYR

GLU

GLY

LYS

ASP

MET

ALA

VAL

12

GLN

ARG

THR

LEU

MET

ALA

LEU

GLY

SER

LEU

13

ALA

VAL

THR

LYS

ASN

ASP

GLY

ASN

TYR

ARG

14

GLY

ASP

PRO

ASN

TRP

PHE

MET

LYS

SER

GLY

15

PRO

SER

GLY

Samples:

sample_1: CH domain, [U-13C; U-15N], 1.0 mM; Tris-HCl(pH 7.0) 20 mM; NaCl 200 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 220 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	sample_1	not available	condition_1
3D 15N-separated NOESY	sample_1	not available	condition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

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

Kujira v0.820, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	1UJO
DBJ	BAA21811 BAA21839 BAB22427 BAC36700 BAG36752
EMBL	CAA92941 CAG46482 CAH18406
GB	AAA58375 AAA79165 AAA79166 AAC08010 AAC21582
REF	NP_001001522 NP_003177 NP_035656 XP_003253239 XP_003253241
SP	P37804 Q01995
AlphaFold	P37804 Q01995