BMRB Entry 5554

Name: Structure of the N-WASP EVH1 Domain-WIP complex
Published: 2003-02-21

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PDB ID: 1mke
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5554
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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:

Structure of the N-WASP EVH1 Domain-WIP complex

Deposition date:

2002-10-10

Original release date:

2003-02-21

Authors:

Volkman, B.; Prehoda, K.; Scott, J.; Peterson, F.; Lim, W.

Citation:

Citation: Volkman, B.; Prehoda, K.; Scott, J.; Peterson, F.; Lim, W.. "Structure of the N-WASP EVH1 Domain-WIP Complex: Insight into the Molecular Basis of Wiskott-Aldrich Syndrome " Cell 111, 565-576 (2002).
PubMed: 12437929

Assembly members:

Assembly members:
WIP PEPTIDE AND N-WASP EVH1 DOMAIN, polymer, 144 residues, Formula weight is not available

Natural source:

Natural source: Common Name: black rat Taxonomy ID: 10117 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: rattus rattus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PBH4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
WIP PEPTIDE AND N-WASP EVH1 DOMAIN: DLPPPEPYVQTTKSYPSKLA RNESRGSGSGSLFSFLGKKC VTMSSAVVQLYAADRNCMWS KKCSGVACLVKDNPQRSYFL RIFDIKDGKLLWEQELYNNF VYNSPRGYFHTFAGDTCQVA LNFANEEEAKKFRKAVTDLL GRRQ

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
1H chemical shifts	848
13C chemical shifts	522
15N chemical shifts	122

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Wiskott-Aldrich syndrome protein interacting protein plus link plus WASP	1

Entities:

Entity 1, Wiskott-Aldrich syndrome protein interacting protein plus link plus WASP 144 residues - Formula weight is not available

1

ASP

LEU

PRO

GLU

PRO

TYR

VAL

GLN

2

THR

LYS

SER

TYR

PRO

SER

LYS

LEU

ALA

3

ARG

ASN

GLU

SER

ARG

GLY

SER

GLY

SER

GLY

4

SER

LEU

PHE

SER

PHE

LEU

GLY

LYS

CYS

5

VAL

THR

MET

SER

ALA

VAL

GLN

LEU

6

TYR

ALA

ASP

ARG

ASN

CYS

MET

TRP

SER

7

LYS

CYS

SER

GLY

VAL

ALA

CYS

LEU

VAL

8

LYS

ASP

ASN

PRO

GLN

ARG

SER

TYR

PHE

LEU

9

ARG

ILE

PHE

ASP

ILE

LYS

ASP

GLY

LYS

LEU

10

LEU

TRP

GLU

GLN

GLU

LEU

TYR

ASN

PHE

11

VAL

TYR

ASN

SER

PRO

ARG

GLY

TYR

PHE

HIS

12

THR

PHE

ALA

GLY

ASP

THR

CYS

GLN

VAL

ALA

13

LEU

ASN

PHE

ALA

ASN

GLU

ALA

LYS

14

LYS

PHE

ARG

LYS

ALA

VAL

THR

ASP

LEU

15

GLY

ARG

GLN

Samples:

sample_1: WIP PEPTIDE AND N-WASP EVH1 DOMAIN, [U-15N], 1 mM; phosphate buffer 20 mM; dithiothreitol 1 mM; H2O 90%; D2O 10%

sample_2: WIP PEPTIDE AND N-WASP EVH1 DOMAIN, [U-15N; U-13C], 1 mM; phosphate buffer 20 mM; dithiothreitol 1 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 7.0; temperature: 303 K; ionic strength: 20 mM; pressure: 1 atm

Experiments:

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

Software:

DYANA v1.5 - structure solution, refinement

XWINNMR v3.0 - collection

xeasy v1.3 - data analysis

NMRPipe - processing

NMR spectrometers:

Bruker DRX 600 MHz

PDB	1MKE
DBJ	BAA21534 BAB29159 BAE24270 BAE25143 BAE25639
EMBL	CAC69994
GB	AAH19951 AAH55045 AAH58642 EAL24333 EDL13819
REF	NP_001103835 NP_001161217 NP_082735 XP_002712136 XP_003134773
SP	O08816 Q91YD9
AlphaFold	O08816 Q91YD9