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 15795

Title: NMR structure of the c-terminal domain of a multiprotein bridging factor 1 (MBF1) of Trichoderma reesei   PubMed: 19137618

Authors: Kopke Salinas, Roberto; Camilo, Cesar; Tomaselli, Simona; Valencia, Estela; Farah, Chuck; El-Dorry, Hamza; Felipe, Chambergo

Citation: Salinas, Roberto; Camilo, Cesar; Tomaselli, Simona; Valencia, Estela; Farah, Chuck; El-Dorry, Hamza; Chambergo, Felipe. "Solution structure of the C-terminal domain of multiprotein bridging factor 1 (MBF1) of Trichoderma reesei"  Proteins 75, 518-523 (2009).

Assembly members:
MBF1, polymer, 107 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
MBF1: GAMDPEFAGGTEGQRLTKVD RSDDIIKPKTVGKEVGKAIE QGRQKFEPTMTQAELGKEIG ETAATVASYERGTATPDQNI LSKMERVLNVKLRGANIGAP RLGPKKK

Data sets:
Data typeCount
13C chemical shifts424
15N chemical shifts107
1H chemical shifts580
heteronuclear NOE values82
H exchange protection factors34
T1 relaxation values71
T2 relaxation values71

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MBF11

Entities:

Entity 1, MBF1 107 residues - Formula weight is not available

The protein construction has a fusion of 7 extra amino acids (GAMDPEF) due to the expression vector. Therefore, Ala8 corresponds to Ala56 in the full length protein.

1   GLYALAMETASPPROGLUPHEALAGLYGLY
2   THRGLUGLYGLNARGLEUTHRLYSVALASP
3   ARGSERASPASPILEILELYSPROLYSTHR
4   VALGLYLYSGLUVALGLYLYSALAILEGLU
5   GLNGLYARGGLNLYSPHEGLUPROTHRMET
6   THRGLNALAGLULEUGLYLYSGLUILEGLY
7   GLUTHRALAALATHRVALALASERTYRGLU
8   ARGGLYTHRALATHRPROASPGLNASNILE
9   LEUSERLYSMETGLUARGVALLEUASNVAL
10   LYSLEUARGGLYALAASNILEGLYALAPRO
11   ARGLEUGLYPROLYSLYSLYS

Samples:

sample_1: MBF1, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 10 mM; sodium chloride 50 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.0; 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRView v5.2.2, CCPN, Johnson, One Moon Scientific - chemical shift assignment, chemical shift assignment, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker DRX 500 MHz

Related Database Links:

PDB
GB EGR47693 ETS01125
REF XP_006966326