BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 5552

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments of the Catalytic Domain of Pac1   PubMed: 12575935

Authors: Farooq, A.; Zhou, M.-M.

Citation: Farooq, A.; Plotnikova, O.; Chaturvedi, G.; Yan, S.; Zeng, L.; Zhang, Q.; Zhou, M.-M.. "Solution Structure of the MAPK Phosphotase PAC-1: Catalytic Domain. Insights into Substrate-induced Enzymatic Activation of MKP"  Structure 11, 155-164 (2003).

Assembly members:
dual specificity protein phosphatase 2, polymer, 145 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
dual specificity protein phosphatase 2: QGGPVEILPYLFLGSCSHSS DLQGLQACGITAVLNVSASC PNHFEGLFRYKSIPVEDNQM VEISAWFQEAIGFIDWVKNS GGRVLVHSQAGISRSATICL AYLMQSRRVRLDEAFDFVKQ RRGVISPNFSFMGQLLQFET QVLCH

Data sets:
Data typeCount
1H chemical shifts666
13C chemical shifts334
15N chemical shifts124

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1dual specificity protein phosphatase 21

Entities:

Entity 1, dual specificity protein phosphatase 2 145 residues - Formula weight is not available

1   GLNGLYGLYPROVALGLUILELEUPROTYR
2   LEUPHELEUGLYSERCYSSERHISSERSER
3   ASPLEUGLNGLYLEUGLNALACYSGLYILE
4   THRALAVALLEUASNVALSERALASERCYS
5   PROASNHISPHEGLUGLYLEUPHEARGTYR
6   LYSSERILEPROVALGLUASPASNGLNMET
7   VALGLUILESERALATRPPHEGLNGLUALA
8   ILEGLYPHEILEASPTRPVALLYSASNSER
9   GLYGLYARGVALLEUVALHISSERGLNALA
10   GLYILESERARGSERALATHRILECYSLEU
11   ALATYRLEUMETGLNSERARGARGVALARG
12   LEUASPGLUALAPHEASPPHEVALLYSGLN
13   ARGARGGLYVALILESERPROASNPHESER
14   PHEMETGLYGLNLEULEUGLNPHEGLUTHR
15   GLNVALLEUCYSHIS

Samples:

sample_1: dual specificity protein phosphatase 2, [U-13C; U-15N], 0.5 mM; phosphate buffer 5 mM

sample_cond_1: pH: 6.5; temperature: 298 K; ionic strength: 10 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYnot availablenot availablenot available
3D 15N-separated NOESYnot availablenot availablenot available
HNHAnot availablenot availablenot available

Software:

XPLOR - structure solution, refinement

ARIA - structure solution, refinement

XWINNMR - collection

NMRPIPE - processing

NMRVIEW - data analysis

NMR spectrometers:

  • BRUKER DRX 600 MHz

Related Database Links:

BMRB 5000
PDB
GB AAA50779 AAA86112 AAH07771 AAL57044 AAY24222
REF NP_004409 XP_001111118 XP_002757414 XP_002811694 XP_003281084
SP Q05923