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Structural Characterization of the Mengovirus Leader Protein Bound to Ran GTPase by Nuclear Magnetic Resonance
Authors
Bacot-Davis, V.R., Palmenberg, A.C., Cornilescu, C.C., Markley, J.L.
Assembly
Mengovirus Leader Protein Bound to Ran GTPase
Entity
1. Mengovirus Leader Protein Bound to Ran GTPase (polymer, Thiol state: all free), 216 monomers, 24422.78 Da Detail

MAAQGEPQVQ FKLVLVGDGG TGKTTFVKRH LTGEFEKKYV ATLGVEVHPL VFHTNRGPIK FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN VPNWHRDLVR VCENIPIVLC GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS AKSNYNFEKP FLWLARKLIG DPNLEFVAMP ALAPPEVVMD PALAAQYEHD LEVAQTTALP DEDDDL


Formula weight
24422.78 Da
Source organism
Homo sapiens
Exptl. method
solution NMR
Refine. method
torsion angle dynamics
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 99.5 %, Completeness: 85.9 %, Completeness (bb): 85.6 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All85.9 % (2213 of 2575)82.6 % (1105 of 1337)87.3 % (883 of 1012)99.6 % (225 of 226)
Backbone85.6 % (1089 of 1272)62.2 % (270 of 434)97.2 % (616 of 634)99.5 % (203 of 204)
Sidechain87.7 % (1320 of 1505)92.5 % (835 of 903)79.8 % (463 of 580)100.0 % (22 of 22)
Aromatic100.0 % (234 of 234)100.0 % (117 of 117)100.0 % (114 of 114)100.0 % (3 of 3)
Methyl96.9 % (248 of 256)96.1 % (123 of 128)97.7 % (125 of 128)

1. entity

MAAQGEPQVQ FKLVLVGDGG TGKTTFVKRH LTGEFEKKYV ATLGVEVHPL VFHTNRGPIK FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN VPNWHRDLVR VCENIPIVLC GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS AKSNYNFEKP FLWLARKLIG DPNLEFVAMP ALAPPEVVMD PALAAQYEHD LEVAQTTALP DEDDDL

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7.4, Details RAN GTPASE TITRATED WITH UNLABELED L MENGO. BUFFER:20mM HEPES (pH 7.4), 100mM KCl (99.9% purity), 2mM MgCl2 (99.9% purity), 2mM DTT, and 0.04% NaN3.


#NameIsotope labelingTypeConcentration
1RAN GTPASE[U-100% 13C; U-100% 15N]0.5 mM
2L MENGOnatural abundance0.5 mM
3HEPESnatural abundance20 mM
4potassium chloridenatural abundance100 mM
5magnesium chloridenatural abundance2 mM
6DTTnatural abundance2 mM
7sodium azidenatural abundance0.04 %
8H2Onatural abundance90 %
9D2Onatural abundance10 %

Protein Blocks Logo
Calculated from 10 models in PDB: 2MMG, Strand ID: A Detail


Release date
2014-10-06
Citation
Solution structures of Mengovirus Leader protein, its phosphorylated derivatives, and in complex with nuclear transport regulatory protein, RanGTPase
Bacot-Davis, V.R., Ciomperlik, J.J., Basta, H.A., Cornilescu, C.C., Palmenberg, A.C.
Proc. Natl. Acad. Sci. U. S. A. (2014), 111, 15792-15797, PubMed 25331866 , DOI 10.1073/pnas.1411098111 ,
Entries sharing articles BMRB: 4 entries Detail
  BMRB: 19855 released on 2014-10-06
    Title Structural Characterization of the Mengovirus Leader Protein Bound to Ran GTPase by Nuclear Magnetic Resonance
  BMRB: 19857 released on 2014-10-06
    Title NMR Studies of the Phosphorylation of the Mengovirus Leader Protein Reveal Stabilization of Intermolecular Domain Interactions
  BMRB: 19858 released on 2014-10-06
    Title NMR Studies of the Phosphorylation of the Mengovirus Leader Protein Reveal Stabilization of Intermolecular Domain Interactions
  BMRB: 19084 released on 2013-04-16
    Title The Mengovirus Leader protein
Related entities 1. Mengovirus Leader Protein Bound to Ran GTPase, : 1 : 70 : 1 : 32 : 91 entities Detail
Interaction partners 1. Mengovirus Leader Protein Bound to Ran GTPase, : 1 interactors Detail
Experiments performed 10 experiments Detail
NMR combined restraints 3 contents Detail
Keywords CARDIOVIRUSES, CYTOPLASM, G-PROTEIN, GTPASE, GTP-BINDING, LEADER, NUCLEAR PORE COMPLEX, NUCLEOCYTOPLASMIC TRANSPORT, NUCLEOTIDE-BINDING, NUCLEUS, TRANSPORT, TRANSPORT PROTEIN, VIRUS-HOST INTERACTIONS