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Found 1 Document (0.731 seconds)

BMRB: 18461

7Z37

Chemical shift assignments and backbone dynamics of H-Ras-GppNHp bound to Ras-binding domain of cRaf1.

Authors

Araki, M., Tamura, A.

Assembly

H-Ras-GppNHp

Entity

1. H-Ras-GppNHp, entity 1 (polymer, Thiol state: all free), 172 monomers, 19379.53 Da Detail

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

2. H-Ras-GppNHp, entity GNP (non-polymer), 522.196 Da
3. H-Ras-GppNHp, entity MG (non-polymer), 24.305 Da
4. H-Ras-GppNHp, entity HOH (water), 18.015 Da
5. entry 2 (polymer, Thiol state: all free), 79 monomers, na Da Detail

XXXSNTIRVF LPNKQRTVVN VRNGMSLHDC LMKALKVRGL QPECCAVFRL LHEHKGKKAR LDWNTDAASL IGEELQVDF

Total weight

19926.03 Da

Max. entity weight

19379.53 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Data set

assigned_chemical_shifts, heteronucl_T1_relaxation, heteronucl_T2_relaxation, heteronucl_NOEs

Chem. Shift Complete

Sequence coverage: 67.3 %, Completeness: 19.9 %, Completeness (bb): 35.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	19.9 % (572 of 2873)	13.9 % (207 of 1493)	18.0 % (200 of 1114)	62.0 % (165 of 266)
Backbone	35.9 % (530 of 1476)	34.9 % (177 of 507)	25.9 % (188 of 727)	68.2 % (165 of 242)
Sidechain	3.4 % (56 of 1628)	3.0 % (30 of 986)	4.2 % (26 of 618)	0.0 % (0 of 24)
Aromatic	0.0 % (0 of 188)	0.0 % (0 of 94)	0.0 % (0 of 93)	0.0 % (0 of 1)
Methyl	7.3 % (21 of 288)	7.6 % (11 of 144)	6.9 % (10 of 144)

1. entity 1

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

5. entry 2

XXXSNTIRVF LPNKQRTVVN VRNGMSLHDC LMKALKVRGL QPECCAVFRL LHEHKGKKAR LDWNTDAASL IGEELQVDF

Show sample condition

Sample #1

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

#	Name	Isotope labeling	Concentration
1	H-Ras-GppNHp	[U-98% 13C; U-98% 15N]	1-2 mM
2	PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER	natural abundance	1-2 mM
3	MAGNESIUM ION	natural abundance	10 mM
4	sodium chloride	natural abundance	150 mM
5	sodium phosphate	natural abundance	25 mM
6	Ras-binding domain of cRaf1	natural abundance	1-2 mM

Sample #2

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

#	Name	Isotope labeling	Concentration
7	H-Ras-GppNHp	[U-98% 15N]	1-2 mM
8	PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER	natural abundance	1-2 mM
9	MAGNESIUM ION	natural abundance	10 mM
10	sodium chloride	natural abundance	150 mM
11	sodium phosphate	natural abundance	25 mM
12	Ras-binding domain of cRaf1	natural abundance	1-2 mM

Heteronucl. T₁

134 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

135 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

134 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

133 T₁/T₂ values in 1 lists
Field strength (¹H) 749.93 MHz, Pressure 1 atm, Temperature 298 K, pH 6.8 Detail

Release date

2012-06-25

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 , Abstract

Entries sharing articles BMRB: 1 entries Detail

BMRB: 17610 released on 2011-05-09
Title Solution structure of GppNHp-bound H-RasT35S mutant protein.

Related entities 1. H-Ras-GppNHp, entity 1, : 3 : 98 entities Detail

Related entities 5. entry 2, : 1 : 30 : 52 entities Detail

Interaction partners 5. entry 2, : 1 interactors Detail

More details for 1 interactors identified by 1 citations

Experiments performed 4 experiments Detail

Chemical shift validation 7 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts, Heteronucl NOE exptl data, Heteronucl T1 relaxation data, Heteronucl T2 relaxation data	bmr18461_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	None
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

Disulfide bonds

None

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr18461_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	OK	487		95.9 (chain: 1, length: 172)
1	Chemical shift references	chemical_shift_reference_1	OK	3		No information

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: OK
- Sequence coverage of experimental data
  - Entity_assembly_ID: 1, Chain length: 172, Sequence coverage: 95.9%
- Total number of assignments
  - ¹H chemical shifts: 162
  - ¹³C chemical shifts: 163
  - ¹⁵N chemical shifts: 162
- Completeness of assignments
  - Entity_assemble_ID: 1
- Redox state of CYS
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	1020	162	15.9
¹³C chemical shifts	766	163	21.3
¹⁵N chemical shifts	194	162	83.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	353	162	45.9
¹³C chemical shifts	344	163	47.4
¹⁵N chemical shifts	168	162	96.4

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	667	0	0.0
¹³C chemical shifts	422	0	0.0
¹⁵N chemical shifts	26	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	102	0	0.0
¹³C chemical shifts	102	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	67	0	0.0
¹³C chemical shifts	67	0	0.0

Keywords Ras, Signaling protein, GTP-bound form, Conformational states, Protein

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Found 1 Document (0.731 seconds)

BMRB: 18461

Sample #1

Sample #2

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. H-Ras-GppNHp, entity 1, : 3 : 98 entities Detail

Related entities 5. entry 2, : 1 : 30 : 52 entities Detail

Interaction partners 5. entry 2, : 1 interactors Detail

Experiments performed 4 experiments Detail

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Instrument

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Chemical shift validation 7 contents Detail