BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25411

Title: MPMV MA T41I T78I

Deposition date: 2015-01-05 Original release date: 2016-01-04

Authors: Kroupa, Tomas; Hrabal, Richard

Citation: Kroupa, Tomas; Dolezal, Michal; Prchal, Jan; Ruml, Tomas; Hrabal, Richard. "Mason-Pfizer monkey virus matrix protein mutants - structural view of impaired membrane interaction"  J. Mol. Biol. ., .-..

Assembly members:
MPMV_MA_T41I_T78I, polymer, 125 residues, 14737.889 Da.

Natural source:   Common Name: Simian retrovirus   Taxonomy ID: 11855   Superkingdom: Viruses   Kingdom: not available   Genus/species: Betaretrovirus Mason-Pfizer monkey virus

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

Entity Sequences (FASTA):
MPMV_MA_T41I_T78I: XGQELSQHERYVEQLKQALK TRGVKVKYADLLKFFDFVKD ICPWFPQEGTIDIKRWRRVG DCFQDYYNTFGPEKVPVIAF SYWNLIKELIDKKEVNPQVM AAVAQTEEILKSNSQTDLEH HHHHH

Data sets:
Data typeCount
13C chemical shifts374
15N chemical shifts100
1H chemical shifts687

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MPMV MA T41I T78I1

Entities:

Entity 1, MPMV MA T41I T78I 125 residues - 14737.889 Da.

1   MYRGLYGLNGLULEUSERGLNHISGLUARG
2   TYRVALGLUGLNLEULYSGLNALALEULYS
3   THRARGGLYVALLYSVALLYSTYRALAASP
4   LEULEULYSPHEPHEASPPHEVALLYSASP
5   ILECYSPROTRPPHEPROGLNGLUGLYTHR
6   ILEASPILELYSARGTRPARGARGVALGLY
7   ASPCYSPHEGLNASPTYRTYRASNTHRPHE
8   GLYPROGLULYSVALPROVALILEALAPHE
9   SERTYRTRPASNLEUILELYSGLULEUILE
10   ASPLYSLYSGLUVALASNPROGLNVALMET
11   ALAALAVALALAGLNTHRGLUGLUILELEU
12   LYSSERASNSERGLNTHRASPLEUGLUHIS
13   HISHISHISHISHIS

Samples:

sample_1: MPMV_MA_T41I_T78I, [U-99% 13C; U-99% 15N, NA-MYR], 0.4 – 0.7 mM; sodium chloride 300 mM; sodium phosphate 100 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 1 M; pH: 6; pressure: 1 atm; temperature: 298 K

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 HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CcpNmr_Analysis v2.3, CCPN - chemical shift assignment

TOPSPIN v3.2, Bruker Biospin - collection, processing

X-PLOR_NIH, Brunger - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz

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