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Biological Magnetic Resonance Data Bank


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BMRB Entry 19225

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19225
MolProbity Validation Chart

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Title: Solution structure of the carbohydrate binding module of the muscle glycogen-targeting subunit of Protein Phosphatase-1

Deposition date: 2013-05-03 Original release date: 2014-05-12

Authors: Koveal, Dorothy; Page, Rebecca; Peti, Wolfgang

Citation: Koveal, Dorothy; Choy, Meng; Page, Rebecca; Peti, Wolfgang. "Molecular basis for Protein Phosphatase-1 regulation by the muscle glycogen-targeting subunit GM"  Not known ., .-..

Assembly members:
GM_CBM21, polymer, 139 residues, 15998.133 Da.

Natural source:   Common Name: Rabbit   Taxonomy ID: 9986   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Oryctolagus cuniculus

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

Entity Sequences (FASTA):
GM_CBM21: GHMQTEEYVLSPLFDLPASK EDLMQQLQVQKAMLESTEYV PGSTSMKGIIRVLNISFEKL VYVRMSLDDWQTHYDILAEY VPNSCDGETDQFSFKISLVP PYQKDGSKVEFCIRYETSVG TFWSNNNGTNYTLVCQKKE

Data sets:
Data typeCount
13C chemical shifts422
15N chemical shifts144
1H chemical shifts958

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1GM_CBM211

Entities:

Entity 1, GM_CBM21 139 residues - 15998.133 Da.

The first three residues (GHM) represent non-native residues that remain after cleavage of the N-terminal affinity tag

1   GLYHISMETGLNTHRGLUGLUTYRVALLEU
2   SERPROLEUPHEASPLEUPROALASERLYS
3   GLUASPLEUMETGLNGLNLEUGLNVALGLN
4   LYSALAMETLEUGLUSERTHRGLUTYRVAL
5   PROGLYSERTHRSERMETLYSGLYILEILE
6   ARGVALLEUASNILESERPHEGLULYSLEU
7   VALTYRVALARGMETSERLEUASPASPTRP
8   GLNTHRHISTYRASPILELEUALAGLUTYR
9   VALPROASNSERCYSASPGLYGLUTHRASP
10   GLNPHESERPHELYSILESERLEUVALPRO
11   PROTYRGLNLYSASPGLYSERLYSVALGLU
12   PHECYSILEARGTYRGLUTHRSERVALGLY
13   THRPHETRPSERASNASNASNGLYTHRASN
14   TYRTHRLEUVALCYSGLNLYSLYSGLU

Samples:

sample_1: GM_CBM21, [U-99% 15N], 0.8 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 10 mM; H2O 90%; D2O 10%

sample_2: GM_CBM21, [U-99% 13C; U-99% 15N], 0.8 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 10 mM; H2O 90%; D2O 10%

sample_3: GM_CBM21 0.8 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 10 mM; D2O 100%

sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D (H)CC(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-1H COSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection, processing

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB AAA31462
REF NP_001075772
SP Q00756

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts