BMRB Entry 18461
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18461
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Title: Chemical shift assignments and backbone dynamics of H-Ras-GppNHp bound to Ras-binding domain of cRaf1. PubMed: 21930707
Deposition date: 2012-05-15 Original release date: 2012-06-26
Authors: Araki, Mitsugu; Tamura, Atsuo
Citation: Araki, Mitsugu; Shima, Fumi; Yoshikawa, Yoko; Muraoka, Shin; Ijiri, Yuichi; Nagahara, Yuka; Shirono, Tomoya; Kataoka, Tohru; Tamura, Atsuo. "Solution structure of the state 1 conformer of GTP-bound H-Ras protein and distinct dynamic properties between the state 1 and state 2 conformers" J. Biol. Chem. 286, 39644-39653 (2011).
Assembly members:
entity_1, polymer, 172 residues, 18861.303 Da.
entity_GNP, non-polymer, 522.196 Da.
entity_MG, non-polymer, 24.305 Da.
entity_HOH, water, 18.015 Da.
entry_2, polymer, . residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GPLGSDMTEYKLVVVGAGGV
GKSALTIQLIQNHFVDEYDP
TIEDSYRKQVVIDGETCLLD
ILDTAGQEEYSAMRDQYMRT
GEGFLCVFAINNTKSFEDIH
QYREQIKRVKDSDDVPMVLV
GNKCDLAARTVESRQAQDLA
RSYGIPYIETSAKTRQGVED
AFYTLVREIRQH
entry_2: XXXSNTIRVFLPNKQRTVVN
VRNGMSLHDCLMKALKVRGL
QPECCAVFRLLHEHKGKKAR
LDWNTDAASLIGEELQVDF
- assigned_chemical_shifts
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
- heteronucl_NOEs
Data type | Count |
1H chemical shifts | 162 |
13C chemical shifts | 163 |
15N chemical shifts | 162 |
heteronuclear NOE values | 134 |
T1 relaxation values | 134 |
T2 relaxation values | 135 |
Additional metadata:
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