BMRB Entry 15760

Name: Solution structure of a cytoskeletal protein complex
Published: 2008-11-12

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15760

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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 a cytoskeletal protein complex

Deposition date:

2008-05-06

Original release date:

2008-11-12

Authors:

Wang, Xiaoxia; Fukuda, Koichi; Byeon, In-Ja; Velyvis, Algirdas; Wu, Chuanyue; Gronenborn, Angela; Qin, Jun

Citation:

Citation: Wang, Xiaoxia; Fukuda, Koichi; Byeon, In-Ja; Velyvis, Algirdas; Wu, Chuanyue; Gronenborn, Angela; Qin, Jun. "The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly" J. Biol. Chem. 283, 21113-21119 (2008).
PubMed: 18508764

Assembly members:

Assembly members:
alpha-parvin, polymer, 129 residues, 15011.396 Da.
LD1, polymer, 10 residues, 1087.189 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: pET3a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
alpha-parvin: RHERDAFDTLFDHAPDKLNV VKKTLITFVNKHLNKLNLEV TELETQFADGVYLVLLMGLL EGYFVPLHSFFLTPDSFEQK VLNVSFAFELMQDGGLEKPK PRPEDIVNCDLKSTLRVLYN LFTKYRNVE
LD1: DLDALLADLE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	500
15N chemical shifts	139
1H chemical shifts	1046

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	alpha-parvin	1
2	LD1	2

Entities:

Entity 1, alpha-parvin 129 residues - 15011.396 Da.

1

ARG

HIS

GLU

ARG

ASP

ALA

PHE

ASP

THR

LEU

2

PHE

ASP

HIS

ALA

PRO

ASP

LYS

LEU

ASN

VAL

3

VAL

LYS

THR

LEU

ILE

THR

PHE

VAL

ASN

4

LYS

HIS

LEU

ASN

LYS

LEU

ASN

LEU

GLU

VAL

5

THR

GLU

LEU

GLU

THR

GLN

PHE

ALA

ASP

GLY

6

VAL

TYR

LEU

VAL

LEU

MET

GLY

LEU

7

GLU

GLY

TYR

PHE

VAL

PRO

LEU

HIS

SER

PHE

8

PHE

LEU

THR

PRO

ASP

SER

PHE

GLU

GLN

LYS

9

VAL

LEU

ASN

VAL

SER

PHE

ALA

PHE

GLU

LEU

10

MET

GLN

ASP

GLY

LEU

GLU

LYS

PRO

LYS

11

PRO

ARG

PRO

GLU

ASP

ILE

VAL

ASN

CYS

ASP

12

LEU

LYS

SER

THR

LEU

ARG

VAL

LEU

TYR

ASN

13

LEU

PHE

THR

LYS

TYR

ARG

ASN

VAL

GLU

Entity 2, LD1 10 residues - 1087.189 Da.

1

ASP

LEU

ASP

ALA

LEU

ALA

ASP

LEU

GLU

Samples:

sample_1: entity_1, [U-13C; U-15N], 0.25 mM; entity_2, [U-13C; U-15N], 0.25 mM

sample_conditions_1: ionic strength: 130 mM; pH: 7.2; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH, Brunger - refinement, structure solution

NMR spectrometers:

Bruker N/A 600 MHz

BMRB	15899
PDB	2K2R 2VZC 2VZD 2VZG 2VZI 3KMU 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