BMRB Entry 10089

Name: Solution structure of phosphotyrosine interaction domain of mouse Numb protein
Published: 2008-08-14

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PDB ID: 1wj1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10089
MolProbity Validation Chart

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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 phosphotyrosine interaction domain of mouse Numb protein

Deposition date:

2007-01-24

Original release date:

2008-08-14

Authors:

Sato, M.; Tomizawa, T.; Koshiba, S.; Tochio, N.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Sato, M.; Tomizawa, T.; Koshiba, S.; Tochio, N.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of phosphotyrosine interaction domain of mouse Numb protein" .

Assembly members:

Assembly members:
PID domain, polymer, 156 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: P031020-52

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PID domain: GSSGSSGASRPHQWQTDEEG VRTGKCSFPVKYLGHVEVDE SRGMHICEDAVKRLKATGKK AVKAVLWVSADGLRVVDEKT KDLIVDQTIEKVSFCAPDRN FDRAFSYICRDGTTRRWICH CFMAVKDTGERLSHAVGCAF AACLERKQKRSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	666
15N chemical shifts	162
1H chemical shifts	1038

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Numb protein	1

Entities:

Entity 1, Numb protein 156 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

ALA

SER

ARG

2

PRO

HIS

GLN

TRP

GLN

THR

ASP

GLU

GLY

3

VAL

ARG

THR

GLY

LYS

CYS

SER

PHE

PRO

VAL

4

LYS

TYR

LEU

GLY

HIS

VAL

GLU

VAL

ASP

GLU

5

SER

ARG

GLY

MET

HIS

ILE

CYS

GLU

ASP

ALA

6

VAL

LYS

ARG

LEU

LYS

ALA

THR

GLY

LYS

7

ALA

VAL

LYS

ALA

VAL

LEU

TRP

VAL

SER

ALA

8

ASP

GLY

LEU

ARG

VAL

ASP

GLU

LYS

THR

9

LYS

ASP

LEU

ILE

VAL

ASP

GLN

THR

ILE

GLU

10

LYS

VAL

SER

PHE

CYS

ALA

PRO

ASP

ARG

ASN

11

PHE

ASP

ARG

ALA

PHE

SER

TYR

ILE

CYS

ARG

12

ASP

GLY

THR

ARG

TRP

ILE

CYS

HIS

13

CYS

PHE

MET

ALA

VAL

LYS

ASP

THR

GLY

GLU

14

ARG

LEU

SER

HIS

ALA

VAL

GLY

CYS

ALA

PHE

15

ALA

CYS

LEU

GLU

ARG

LYS

GLN

LYS

ARG

16

SER

GLY

PRO

SER

GLY

Samples:

sample_1: PID domain, [U-13C; U-15N], 1.3 mM; phosphate 20 mM; NaCl 100 mM; d-DTT 5 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 6.0; 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 v0.8996, Kobayashi, N. - data analysis

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

NMR spectrometers:

Bruker AVANCE 800 MHz

PDB	1WJ1
DBJ	BAB23367 BAE45130 BAG37583
EMBL	CAD66588 CAH91534
GB	AAB09586 AAC97962 AAD47834 AAD49434 AAD54281
REF	NP_001005745 NP_001095421 NP_001125900 NP_001258984 NP_001258985
TPG	DAA25078