BMRB Entry 15899

Name: 1H, 13C and 15N backbone chemical shift assignments of the C-terminal CH domain of human alpha-parvin
Published: 2008-11-19

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15899

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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:

1H, 13C and 15N backbone chemical shift assignments of the C-terminal CH domain of human alpha-parvin

Deposition date:

2008-07-31

Original release date:

2008-11-19

Authors:

Lorenz, Sonja; Vakonakis, Ioannis; Campbell, Iain

Citation:

Citation: Lorenz, Sonja; Vakonakis, Ioannis; Lowe, Edward; Campbell, Iain; Noble, Martin; Hoellerer, Maria. "Structural Analysis of the Interactions between Paxillin LD motifs and alpha-Parvin" Structure 16, 1521-1531 (2008).
PubMed: 18940607

Assembly members:

Assembly members:
C-terminal_CH_domain_of_alpha-parvin, polymer, 135 residues, 15460.8 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-6P1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
C-terminal_CH_domain_of_alpha-parvin: GPLGSGRHERDAFDTLFDHA PDKLNVVKKTLITFVNKHLN KLNLEVTELETQFADGVYLV LLMGLLEGYFVPLHSFFLTP DSFEQKVLNVSFAFELMQDG GLEKPKPRPEDIVNCDLKST LRVLYNLFTKYRNVE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	231
15N chemical shifts	120
1H chemical shifts	120

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C-terminal CH domain of alpha-parvin	1

Entities:

Entity 1, C-terminal CH domain of alpha-parvin 135 residues - 15460.8 Da.

1

GLY

PRO

LEU

GLY

SER

GLY

ARG

HIS

GLU

ARG

2

ASP

ALA

PHE

ASP

THR

LEU

PHE

ASP

HIS

ALA

3

PRO

ASP

LYS

LEU

ASN

VAL

LYS

THR

4

LEU

ILE

THR

PHE

VAL

ASN

LYS

HIS

LEU

ASN

5

LYS

LEU

ASN

LEU

GLU

VAL

THR

GLU

LEU

GLU

6

THR

GLN

PHE

ALA

ASP

GLY

VAL

TYR

LEU

VAL

7

LEU

MET

GLY

LEU

GLU

GLY

TYR

PHE

8

VAL

PRO

LEU

HIS

SER

PHE

LEU

THR

PRO

9

ASP

SER

PHE

GLU

GLN

LYS

VAL

LEU

ASN

VAL

10

SER

PHE

ALA

PHE

GLU

LEU

MET

GLN

ASP

GLY

11

GLY

LEU

GLU

LYS

PRO

LYS

PRO

ARG

PRO

GLU

12

ASP

ILE

VAL

ASN

CYS

ASP

LEU

LYS

SER

THR

13

LEU

ARG

VAL

LEU

TYR

ASN

LEU

PHE

THR

LYS

14

TYR

ARG

ASN

VAL

GLU

Samples:

sample_1: sodium phosphate 50 mM; sodium chloride 100 mM; DSS 0.1 mM; D2O 5%; CHAPS 1.5 mM; C-terminal CH domain of alpha-parvin, [U-98% 13C; U-98% 15N], 240 uM; DTT 2 mM; H2O 95%

sample_conditions_1: ionic strength: 325 mM; pH: 6.9; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.2.2_01, Johnson, One Moon Scientific - data analysis

TOPSPIN v1.3, Bruker Biospin - collection

NMR spectrometers:

Bruker DMX 500 MHz
home-built n.a. 750 MHz

BMRB	15760
PDB	2K2R 2VZC 2VZD 2VZG 2VZI 3KMW 3REP
DBJ	BAA91815 BAA97981 BAC36771 BAE28686 BAG73514
GB	AAG09802 AAG09803 AAG27173 AAG27175 AAH14535
REF	NP_001092614 NP_060692 NP_065631 NP_065707 XP_001091788
SP	Q9EPC1 Q9HB97 Q9NVD7
TPG	DAA22326
AlphaFold	Q9EPC1 Q9HB97 Q9NVD7