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:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | H-Ras-GppNHp | 1 |
| 2 | PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER | 2 |
| 3 | MAGNESIUM ION | 3 |
| 4 | water | 4 |
| 5 | Ras-binding domain of cRaf1 | 5 |
Entities:
Entity 1, H-Ras-GppNHp 172 residues - 18861.303 Da.
| 1 | GLY | PRO | LEU | GLY | SER | ASP | MET | THR | GLU | TYR | ||||
| 2 | LYS | LEU | VAL | VAL | VAL | GLY | ALA | GLY | GLY | VAL | ||||
| 3 | GLY | LYS | SER | ALA | LEU | THR | ILE | GLN | LEU | ILE | ||||
| 4 | GLN | ASN | HIS | PHE | VAL | ASP | GLU | TYR | ASP | PRO | ||||
| 5 | THR | ILE | GLU | ASP | SER | TYR | ARG | LYS | GLN | VAL | ||||
| 6 | VAL | ILE | ASP | GLY | GLU | THR | CYS | LEU | LEU | ASP | ||||
| 7 | ILE | LEU | ASP | THR | ALA | GLY | GLN | GLU | GLU | TYR | ||||
| 8 | SER | ALA | MET | ARG | ASP | GLN | TYR | MET | ARG | THR | ||||
| 9 | GLY | GLU | GLY | PHE | LEU | CYS | VAL | PHE | ALA | ILE | ||||
| 10 | ASN | ASN | THR | LYS | SER | PHE | GLU | ASP | ILE | HIS | ||||
| 11 | GLN | TYR | ARG | GLU | GLN | ILE | LYS | ARG | VAL | LYS | ||||
| 12 | ASP | SER | ASP | ASP | VAL | PRO | MET | VAL | LEU | VAL | ||||
| 13 | GLY | ASN | LYS | CYS | ASP | LEU | ALA | ALA | ARG | THR | ||||
| 14 | VAL | GLU | SER | ARG | GLN | ALA | GLN | ASP | LEU | ALA | ||||
| 15 | ARG | SER | TYR | GLY | ILE | PRO | TYR | ILE | GLU | THR | ||||
| 16 | SER | ALA | LYS | THR | ARG | GLN | GLY | VAL | GLU | ASP | ||||
| 17 | ALA | PHE | TYR | THR | LEU | VAL | ARG | GLU | ILE | ARG | ||||
| 18 | GLN | HIS |
Entity 2, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER - C10 H17 N6 O13 P3 - 522.196 Da.
| 1 | GNP |
Entity 3, MAGNESIUM ION - Mg - 24.305 Da.
| 1 | MG |
Entity 4, water - 18.015 Da.
| 1 | HOH |
Entity 5, Ras-binding domain of cRaf1 - Formula weight is not available
| 1 | X | X | X | SER | ASN | THR | ILE | ARG | VAL | PHE | ||||
| 2 | LEU | PRO | ASN | LYS | GLN | ARG | THR | VAL | VAL | ASN | ||||
| 3 | VAL | ARG | ASN | GLY | MET | SER | LEU | HIS | ASP | CYS | ||||
| 4 | LEU | MET | LYS | ALA | LEU | LYS | VAL | ARG | GLY | LEU | ||||
| 5 | GLN | PRO | GLU | CYS | CYS | ALA | VAL | PHE | ARG | LEU | ||||
| 6 | LEU | HIS | GLU | HIS | LYS | GLY | LYS | LYS | ALA | ARG | ||||
| 7 | LEU | ASP | TRP | ASN | THR | ASP | ALA | ALA | SER | LEU | ||||
| 8 | ILE | GLY | GLU | GLU | LEU | GLN | VAL | ASP | PHE |
Samples:
sample_1: H-Ras-GppNHp, [U-98% 13C; U-98% 15N], 1-2 mM; PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER 1-2 mM; MAGNESIUM ION 10 mM; sodium chloride 150 mM; sodium phosphate 25 mM; Ras-binding domain of cRaf1 1-2 mM
sample_2: H-Ras-GppNHp, [U-98% 15N], 1-2 mM; PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER 1-2 mM; MAGNESIUM ION 10 mM; sodium chloride 150 mM; sodium phosphate 25 mM; Ras-binding domain of cRaf1 1-2 mM
sample_conditions_1: temperature: 298 K; pH: 6.8; pressure: 1 atm; ionic strength: 0.24 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - peak picking
NMR spectrometers:
- Bruker DMX 750 MHz
Related Database Links:
| BMRB | 10051 17183 17610 17678 18479 18629 25730 |
| PDB | |
| DBJ | BAB61869 BAB61870 BAB88314 BAB88315 BAB88316 BAB39743 BAB39748 BAB83675 BAE24820 BAG10817 |
| EMBL | CAA25322 CAA25624 CAA27258 CAA35240 CAA90306 CAA27204 CAH92939 |
| GB | AAA36554 AAA42009 AAA46568 AAA46569 AAA46570 AAA42001 AAB27591 AAH15273 AAH18119 AAH62071 |
| PIR | A43816 TVMVNS |
| PRF | 0904302A 1604384A |
| REF | NP_001017003 NP_001018465 NP_001084278 NP_001091711 NP_001123913 NP_001095975 NP_001126730 NP_001253231 NP_002871 NP_036771 |
| SP | P01112 P01113 P01114 P01115 P08642 A7E3S4 P04049 P11345 Q5R5M7 Q99N57 |
| TPG | DAA13500 DAA16778 DAA16781 DAA16798 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts