BMRB Entry 7172

Name: Backbone and side-chain 1H, 13C and 15N resonance assignments of C-terminal domain of an actin monomer binding protein twinfilin
Published: 2007-01-10

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7172

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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:

Backbone and side-chain 1H, 13C and 15N resonance assignments of C-terminal domain of an actin monomer binding protein twinfilin

Deposition date:

2006-06-16

Original release date:

2007-01-10

Authors:

Hellman, Maarit; Paavilainen, Ville; Annila, Arto; Lappalainen, Pekka; Permi, Perttu

Citation:

Citation: Hellman, Maarit; Paavilainen, Ville; Annila, Arto; Lappalainen, Pekka; Permi, Perttu. "NMR assignment of the C-terminal ADF-H domain of an actin monomer binding protein, twinfilin" J. Biomol. NMR 36, 66-66 (2006).
PubMed: 16924408

Assembly members:

Assembly members:
Twf-C, polymer, 142 residues, 16617 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Vector: pRat4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Twf-C: AQGVAFPISRDAFQALEKLS KKQLNYVQLEIDIKNETIIL ANTENTELRDLPKRIPKDSA RYHFFLYKHSHEGDYLESVV FIYSMPGYTCSIRERMLYSS CKSPLLEIVERQLQMDVIRK IEIDNGDELTADFLYDEVHP KQ

Data sets:

assigned_chemical_shifts
- chem_shift_list_1

Data type	Count
13C chemical shifts	667
15N chemical shifts	153
1H chemical shifts	1057

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C-terminal domain of twinfilin	1

Entities:

Entity 1, C-terminal domain of twinfilin 142 residues - 16617 Da.

1

ALA

GLN

GLY

VAL

ALA

PHE

PRO

ILE

SER

ARG

2

ASP

ALA

PHE

GLN

ALA

LEU

GLU

LYS

LEU

SER

3

LYS

GLN

LEU

ASN

TYR

VAL

GLN

LEU

GLU

4

ILE

ASP

ILE

LYS

ASN

GLU

THR

ILE

LEU

5

ALA

ASN

THR

GLU

ASN

THR

GLU

LEU

ARG

ASP

6

LEU

PRO

LYS

ARG

ILE

PRO

LYS

ASP

SER

ALA

7

ARG

TYR

HIS

PHE

LEU

TYR

LYS

HIS

SER

8

HIS

GLU

GLY

ASP

TYR

LEU

GLU

SER

VAL

9

PHE

ILE

TYR

SER

MET

PRO

GLY

TYR

THR

CYS

10

SER

ILE

ARG

GLU

ARG

MET

LEU

TYR

SER

11

CYS

LYS

SER

PRO

LEU

GLU

ILE

VAL

GLU

12

ARG

GLN

LEU

GLN

MET

ASP

VAL

ILE

ARG

LYS

13

ILE

GLU

ILE

ASP

ASN

GLY

ASP

GLU

LEU

THR

14

ALA

ASP

PHE

LEU

TYR

ASP

GLU

VAL

HIS

PRO

15

LYS

GLN

Samples:

sample_1: C-terminal domain of twinfilin, [U-13C; U-15N], 1 mM; Bis-Tris 10 mM; Sodium Chloride 50 mM; Dithiothreitol 1 mM

conditions_1: ionic strength: 60 mM; pH: 6.8; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
15N-HSQC	sample_1	not available	conditions_1
13C-HSQC	sample_1	not available	conditions_1
13C-(CT)-HSQC	sample_1	not available	conditions_1
3D HNCA	sample_1	not available	conditions_1
3D HN(CO)CA	sample_1	not available	conditions_1
HNCACB	sample_1	not available	conditions_1
CBCA(CO)NH	sample_1	not available	conditions_1
HNCO	sample_1	not available	conditions_1
HN(CA)CO	sample_1	not available	conditions_1
HC(C)H-COSY	sample_1	not available	conditions_1
H(C)CH-TOCSY	sample_1	not available	conditions_1
(H)C(CO)NH	sample_1	not available	conditions_1
H(C)(CO)NH	sample_1	not available	conditions_1
(HB)CB(CGCDCE)HE	sample_1	not available	conditions_1
(HB)CB(CGCD)HD	sample_1	not available	conditions_1
DE-MQ-(H)CCmHm-TOCSY	sample_1	not available	conditions_1

Software:

VNMR v6.1 C - processing

NMR spectrometers:

Varian Inova 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks