BMRB Entry 15949

Name: 1H, 15N, 13C Resonance Assignments of the Reduced and Active Form of Human Protein Tyrosine Phosphatase, PRL-1
Published: 2009-01-15

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15949

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 15N, 13C Resonance Assignments of the Reduced and Active Form of Human Protein Tyrosine Phosphatase, PRL-1

Deposition date:

2008-09-10

Original release date:

2009-01-15

Authors:

Skinner, Andria; Laurence, Jennifer

Citation:

Citation: Skinner, Andria; Laurence, Jennifer. "1H, 15N, 13C resonance assignments of the reduced and active form of human Protein Tyrosine Phosphatase, PRL-1." Biomol. NMR Assignments 3, 61-65 (2009).
PubMed: 19636948

Assembly members:

Assembly members:
PRL-1-C170-171S, polymer, 173 residues, 19815 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET32XaLIC

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PRL-1-C170-171S: MARMNRPAPVEVTYKNMRFL ITHNPTNATLNKFIEELKKY GVTTIVRVCEATYDTTLVEK EGIHVLDWPFDDGAPPSNQI VDDWLSLVKIKFREEPGCCI AVHCVAGLGRAPVLVALALI EGGMKYEDAVQFIRQKRRGA FNSKQLLYLEKYRPKMRLRF KDSNGHRNNSSIQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	632
15N chemical shifts	148
1H chemical shifts	148

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PRL-1-C170-171S	1

Entities:

Entity 1, PRL-1-C170-171S 173 residues - 19815 Da.

1

MET

ALA

ARG

MET

ASN

ARG

PRO

ALA

PRO

VAL

2

GLU

VAL

THR

TYR

LYS

ASN

MET

ARG

PHE

LEU

3

ILE

THR

HIS

ASN

PRO

THR

ASN

ALA

THR

LEU

4

ASN

LYS

PHE

ILE

GLU

LEU

LYS

TYR

5

GLY

VAL

THR

ILE

VAL

ARG

VAL

CYS

GLU

6

ALA

THR

TYR

ASP

THR

LEU

VAL

GLU

LYS

7

GLU

GLY

ILE

HIS

VAL

LEU

ASP

TRP

PRO

PHE

8

ASP

GLY

ALA

PRO

SER

ASN

GLN

ILE

9

VAL

ASP

TRP

LEU

SER

LEU

VAL

LYS

ILE

10

LYS

PHE

ARG

GLU

PRO

GLY

CYS

ILE

11

ALA

VAL

HIS

CYS

VAL

ALA

GLY

LEU

GLY

ARG

12

ALA

PRO

VAL

LEU

VAL

ALA

LEU

ALA

LEU

ILE

13

GLU

GLY

MET

LYS

TYR

GLU

ASP

ALA

VAL

14

GLN

PHE

ILE

ARG

GLN

LYS

ARG

GLY

ALA

15

PHE

ASN

SER

LYS

GLN

LEU

TYR

LEU

GLU

16

LYS

TYR

ARG

PRO

LYS

MET

ARG

LEU

ARG

PHE

17

LYS

ASP

SER

ASN

GLY

HIS

ARG

ASN

SER

18

SER

ILE

GLN

Samples:

sample_1: PRL-1-C170-171S mM; sodium phosphate 50 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.169 M; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment, peak picking

PISTACHIO vPINE, Eghbalnia, Bahrami, Wang, Assadi and Markley - chemical shift assignment, refinement

NMR spectrometers:

Bruker Avance 800 MHz

PDB	1RXD 1X24 1ZCK 1ZCL 3RZ2
DBJ	BAC38233 BAE28460 BAE29619 BAE30480 BAE90330
EMBL	CAH18292 CAH92262
GB	AAA41935 AAB40597 AAB58913 AAC39836 AAF05715
PIR	A56059
REF	NP_001126324 NP_001193053 NP_001233568 NP_003454 NP_035330
SP	Q5R7J8 Q63739 Q78EG7 Q93096 Q9TSM6
TPG	DAA26421 DAA26422
AlphaFold	Q5R7J8 Q63739 Q78EG7 Q93096 Q9TSM6