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 25068

Title: NMR Structure and 1H, 13C and 15N Chemical Shift Assignments for High mobility group protein from Plasmodium falciparum 3D7.

Deposition date: 2014-07-02 Original release date: 2014-07-21

Authors: Tang, Changyan; Barnwal, Ravi P; Varani, Gabriele

Citation: Tang, Changyan; Barnwal, Ravi P; Varani, Gabriele. "NMR Structure and 1H, 13C and 15N Chemical Shift Assignments for High mobility group protein from Plasmodium falciparum 3D7."  To be Published ., .-..

Assembly members:
entity, polymer, 92 residues, 10861.796 Da.

Natural source:   Common Name: apicomplexans   Taxonomy ID: 36329   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Plasmodium falciparum

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

Entity Sequences (FASTA):
entity: MAHHHHHHMKKKDPLAPKRA LSAYMFYVKDKRLEIIKEKP ELAKDVAQVGKLIGEAWGQL SPAQKAPYEKKAQLDKVRYS KEIEEYRKKNQE

Data sets:
Data typeCount
1H chemical shifts497
13C chemical shifts351
15N chemical shifts80

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 92 residues - 10861.796 Da.

1   METALAHISHISHISHISHISHISMETLYS
2   LYSLYSASPPROLEUALAPROLYSARGALA
3   LEUSERALATYRMETPHETYRVALLYSASP
4   LYSARGLEUGLUILEILELYSGLULYSPRO
5   GLULEUALALYSASPVALALAGLNVALGLY
6   LYSLEUILEGLYGLUALATRPGLYGLNLEU
7   SERPROALAGLNLYSALAPROTYRGLULYS
8   LYSALAGLNLEUASPLYSVALARGTYRSER
9   LYSGLUILEGLUGLUTYRARGLYSLYSASN
10   GLNGLU

Samples:

sample_1: High mobility group protein, [U-95% 13C; U-95% 15N], 0.9 mM; H2O 93%; D20 7%

sample_conditions_1: temperature: 298 K; pH: 7.0; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

TALOS, Cornilescu, Delaglio and Bax - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution, refinement

CCPNMR, CCPN - data analysis, chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AMX 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB

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