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Solution structure of GppNHp-bound H-RasT35S mutant protein.
Authors
Araki, M.
Assembly
GppNHp-bound H-RasT35S mutant protein
Entity
1. GppNHp-bound H-RasT35S mutant protein (polymer), 172 monomers, 19365.50 Da Detail

GPLGSDMTEY KLVVVGAGGV GKSALTIQLI QNHFVDEYDP SIEDSYRKQV VIDGETCLLD ILDTAGQEEY SAMRDQYMRT GEGFLCVFAI NNTKSFEDIH QYREQIKRVK DSDDVPMVLV GNKCDLAART VESRQAQDLA RSYGIPYIET SAKTRQGVED AFYTLVREIR QH


2. PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER (non-polymer, Thiol state: not present), 522.196 Da
3. MG (non-polymer, Thiol state: not present), 24.305 Da
Total weight
19912.0 Da
Max. entity weight
19365.5 Da
Source organism
Homo sapiens
Exptl. method
solution NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts, heteronucl_NOEs, heteronucl_T1_relaxation, heteronucl_T2_relaxation
Chem. Shift Complete
Sequence coverage: 97.1 %, Completeness: 95.1 %, Completeness (bb): 96.2 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All95.1 % (1872 of 1968)95.4 % (973 of 1020)94.4 % (722 of 765)96.7 % (177 of 183)
Backbone96.2 % (985 of 1024)97.2 % (343 of 353)95.4 % (480 of 503)96.4 % (162 of 168)
Sidechain94.4 % (1041 of 1103)94.5 % (630 of 667)94.1 % (396 of 421)100.0 % (15 of 15)
Aromatic90.3 % (121 of 134)95.5 % (64 of 67)85.1 % (57 of 67)
Methyl97.9 % (190 of 194)97.9 % (95 of 97)97.9 % (95 of 97)

1. GppNHp-bound H-RasT35S mutant protein

GPLGSDMTEY KLVVVGAGGV GKSALTIQLI QNHFVDEYDP SIEDSYRKQV VIDGETCLLD ILDTAGQEEY SAMRDQYMRT GEGFLCVFAI NNTKSFEDIH QYREQIKRVK DSDDVPMVLV GNKCDLAART VESRQAQDLA RSYGIPYIET SAKTRQGVED AFYTLVREIR QH

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.8


#NameIsotope labelingTypeConcentration
1GppNHp-bound H-RasT35S mutant protein[U-98% 13C; U-98% 15N]1.0 ~ 2.0 mM
2PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTERnatural abundance1.0 ~ 2.0 mM
3magnesium ionsnatural abundance10 mM
4sodium chloridenatural abundance150 mM
5sodium phosphatenatural abundance25 mM
6H20natural abundance90 %
7D2Onatural abundance10 %
Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.8


#NameIsotope labelingTypeConcentration
8GppNHp-bound H-RasT35S mutant protein[U-98% 13C; U-98% 15N]1.0 ~ 2.0 mM
9PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTERnatural abundance1.0 ~ 2.0 mM
10magnesium ionsnatural abundance10 mM
11sodium chloridenatural abundance150 mM
12sodium phosphatenatural abundance25 mM
13H20natural abundance90 %
14D2Onatural abundance10 %

Protein Blocks Logo
Calculated from 20 models in PDB: 2LCF, Strand ID: A Detail


Heteronucl. T1
130 T1 values in 1 lists
Coherence Sz, Field strength (1H) 749.93 MHz, Pressure 1 atm, Temperature 298 K, pH 6.8 Detail
Heteronucl. T2
130 T2 values in 1 lists
Coherence S(+,-), Field strength (1H) 749.93 MHz, Pressure 1 atm, Temperature 298 K, pH 6.8 Detail
Heteronucl. NOE
130 NOE values in 1 lists
Value type peak height, Field strength (1H) 749.93 MHz, Pressure 1 atm, Temperature 298 K, pH 6.8 Detail
Heteronucl. T1/T2
130 T1/T2 values in 1 lists
Field strength (1H) 749.93 MHz, Pressure 1 atm, Temperature 298 K, pH 6.8 Detail
Release date
2011-05-09
Citation
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
Araki, M., Shima, F., Yoshikawa, Y., Muraoka, S., Ijiri, Y., Nagahara, Y., Shirono, T., Kataoka, T., Tamura, A.
J. Biol. Chem. (2011), 286, 39644-39653, PubMed 21930707 , DOI 10.1074/jbc.M111.227074 ,
Entries sharing articles BMRB: 1 entries Detail
  BMRB: 18461 released on 2012-06-25
    Title Chemical shift assignments and backbone dynamics of H-Ras-GppNHp bound to Ras-binding domain of cRaf1.
Related entities 1. GppNHp-bound H-RasT35S mutant protein, : 1 : 5 : 1 : 2 : 291 entities Detail
Interaction partners 1. GppNHp-bound H-RasT35S mutant protein, : 60 interactors Detail
Experiments performed 13 experiments Detail
nullKeywords Protein, Ras