BMRB Entry 5850

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PDB ID: 1p8a
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR5850
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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:

Kinetic and Structural Studies of the Low Moleuclar Weight Protein Tyrosine Phosphatase from Tritrichomonas foetus

Deposition date:

2003-06-26

Original release date:

2005-10-21

Authors:

Thomas, C.; Hallenga, K.; Stauffacher, C.; Van Etten, R.

Citation:

Citation: Gustafson, Christin; Stauffacher, Cynthia; Hallenga, Klaas; Van Etten, Robert. "Solution structure of the low-molecular-weight protein tyrosine phosphatase from Tritrichomonas foetus reveals a flexible phosphate binding loop" Protein Sci. 14, 2515-2525 (2005).
PubMed: 16195543

Assembly members:

Assembly members:
protein tyrosine phosphatase (E.C.3.1.3.48), polymer, 146 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Tritrichomonas foetus Taxonomy ID: 5724 Superkingdom: Eukaryota Kingdom: not available Genus/species: Tritrichomonas foetus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PET23D

Entity Sequences (FASTA):

Entity Sequences (FASTA):
protein tyrosine phosphatase (E.C.3.1.3.48): AAEKKAVLFVCLGNICRSPA CEGICRDMVGDKLIIDSAAT SGFHVGQSPDTRSQKVCKSN GVDISKQRARQITKADFSKF DVIAALDQSILSDINSMKPS NCRAKVVLFNPPNGVDDPYY SSDGFPTMFASISKEMKPFL TEHGLI

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
1H chemical shifts	900
13C chemical shifts	439
15N chemical shifts	153

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	protein tyrosine phosphatase	1

Entities:

Entity 1, protein tyrosine phosphatase 146 residues - Formula weight is not available

1

ALA

GLU

LYS

ALA

VAL

LEU

PHE

VAL

2

CYS

LEU

GLY

ASN

ILE

CYS

ARG

SER

PRO

ALA

3

CYS

GLU

GLY

ILE

CYS

ARG

ASP

MET

VAL

GLY

4

ASP

LYS

LEU

ILE

ASP

SER

ALA

THR

5

SER

GLY

PHE

HIS

VAL

GLY

GLN

SER

PRO

ASP

6

THR

ARG

SER

GLN

LYS

VAL

CYS

LYS

SER

ASN

7

GLY

VAL

ASP

ILE

SER

LYS

GLN

ARG

ALA

ARG

8

GLN

ILE

THR

LYS

ALA

ASP

PHE

SER

LYS

PHE

9

ASP

VAL

ILE

ALA

LEU

ASP

GLN

SER

ILE

10

LEU

SER

ASP

ILE

ASN

SER

MET

LYS

PRO

SER

11

ASN

CYS

ARG

ALA

LYS

VAL

LEU

PHE

ASN

12

PRO

ASN

GLY

VAL

ASP

PRO

TYR

13

SER

ASP

GLY

PHE

PRO

THR

MET

PHE

ALA

14

SER

ILE

SER

LYS

GLU

MET

LYS

PRO

PHE

LEU

15

THR

GLU

HIS

GLY

LEU

ILE

Samples:

sample_1: protein tyrosine phosphatase (E.C.3.1.3.48), [U-15N; U-13C], 1 – 2 mM; NaCl 130 mM; NaH2PO4 20 mM; DSS 1 mM; H20 90%; D2O 10%

sample_2: protein tyrosine phosphatase (E.C.3.1.3.48), [U-15N], 1 – 2 mM; NaCl 130 mM; NaH2PO4 20 mM; DSS 1 mM; H20 90%; D2O 10%

sample_cond_1: pH: 5.2; temperature: 298 K; ionic strength: 130 mM; pressure: 1 atm

Experiments:

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

Software:

VNMR v6.1c - collection

NMRPipe vNA - processing

SPARKY v3 - data analysis

X-PLOR v3.851 - structure solution, refinement

NMR spectrometers:

Varian INOVA 600 MHz

PDB	1P8A
GB	AAB51113