BMRB Entry 10235

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PDB ID: 1wgu
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10235
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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 the C-terminal Phosphotyrosine Interaction Domain of APBB2 from Mouse

Deposition date:

2008-08-22

Original release date:

2009-03-19

Authors:

Li, H.; Hayashi, F.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation:

Citation: Li, H.; Koshiba, S.; Hayashi, F.; Tochio, N.; Tomozawa, T.; Kasai, T.; Yabuki, T.; Motoda, Y.; Harada, T.; Watanabe, S.; Inoue, M.; Hayashizaki, Y.; Tanaka, A.; Kigawa, T.; Yokoyama, S.. "Structure of the C-terminal PID Domain of Fe65L1 Complexed with the Cytoplasmic Tail of APP Reveals a Novel Peptide Binding Mode" J. Biol. Chem. 283, 27165-27178 (2008).
PubMed: 18650440

Assembly members:

Assembly members:
Phosphotyrosine-Interaction Domain, polymer, 136 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: P031020-58

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Phosphotyrosine-Interaction Domain: GSSGSSGPTPKTELVQKFRV QYLGMLPVDRPVGMDTLNSA IENLMTSSSKEDWPSVNMNV ADATVTVISEKNEEEVLVEC RVRFLSFMGVGKDVHTFAFI MDTGNQRFECHVFWCEPNAA NVSEAVQAACSGPSSG

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	567
15N chemical shifts	136
1H chemical shifts	891

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Phosphotyrosine-Interaction Domain	1

Entities:

Entity 1, Phosphotyrosine-Interaction Domain 136 residues - Formula weight is not available

1

GLY

SER

GLY

SER

GLY

PRO

THR

PRO

2

LYS

THR

GLU

LEU

VAL

GLN

LYS

PHE

ARG

VAL

3

GLN

TYR

LEU

GLY

MET

LEU

PRO

VAL

ASP

ARG

4

PRO

VAL

GLY

MET

ASP

THR

LEU

ASN

SER

ALA

5

ILE

GLU

ASN

LEU

MET

THR

SER

LYS

6

GLU

ASP

TRP

PRO

SER

VAL

ASN

MET

ASN

VAL

7

ALA

ASP

ALA

THR

VAL

THR

VAL

ILE

SER

GLU

8

LYS

ASN

GLU

VAL

LEU

VAL

GLU

CYS

9

ARG

VAL

ARG

PHE

LEU

SER

PHE

MET

GLY

VAL

10

GLY

LYS

ASP

VAL

HIS

THR

PHE

ALA

PHE

ILE

11

MET

ASP

THR

GLY

ASN

GLN

ARG

PHE

GLU

CYS

12

HIS

VAL

PHE

TRP

CYS

GLU

PRO

ASN

ALA

13

ASN

VAL

SER

GLU

ALA

VAL

GLN

ALA

CYS

14

SER

GLY

PRO

SER

GLY

Samples:

sample_1: Phosphotyrosine-Interaction Domain, [U-13C; U-15N], 0.84 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 2 mM; NaN3 0.02%; D2O 10%; H2O 90%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C-separated NOESY	sample_1	isotropic	condition_1
3D 15N-separated NOESY	sample_1	isotropic	condition_1

Software:

VNMR v6.1c, Varian - collection

NMRPipe v20020425, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B. A. - data analysis

Kujira v0.897, Kobayashi, N. - data analysis

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

NMR spectrometers:

Varian INOVA 900 MHz

BMRB	10237 10238 10239
PDB	1WGU 2ROZ 2YSZ 2YT0 2YT1
DBJ	BAB23568 BAE31851 BAE39700 BAE41482 BAE42990
GB	AAD55360 AAH76587 EDL37768 EDL90042 EGW02447
REF	NP_001188342 NP_001188343 NP_001188344 NP_001188345 NP_001297555
SP	Q9DBR4
AlphaFold	Q9DBR4