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Found 1 Document (0.769 seconds)

BMRB: 15128

2JNU

Solution structure of the RGS domain of human RGS14

Authors

Dowler, E.F., Diehl, A., Bray, J., Elkins, J., Soundararajan, M., Doyle, D., Gileadi, C., Phillips, C., Schoch, G., Yang, X., Brockmann, C., Leidert, M., Rehbein, K., Schmieder, P., Kuhne, R., Higman, V.A., Sundstrom, M., Arrowsmith, C., Weigelt, J., Edwards, A., Oschkinat, H., Ball, L.J.

Assembly

RGS domain from human RGS14 protein

Entity

1. RGS domain from human RGS14 protein (polymer, Thiol state: all free), 154 monomers, 17701.76 Da Detail

SMTEEQPVAS WALSFERLLQ DPLGLAYFTE FLKKEFSAEN VTFWKACERF QQIPASDTQQ LAQEARNIYQ EFLSSQALSP VNIDRQAWLG EEVLAEPRPD MFRAQQLQIF NLMKFDSYAR FVKSPLYREC LLAEAEGRPL REPGSSRLGS PDAT

Formula weight

17701.76 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 99.4 %, Completeness: 85.8 %, Completeness (bb): 93.8 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	85.8 % (1589 of 1851)	88.6 % (860 of 971)	80.7 % (578 of 716)	92.1 % (151 of 164)
Backbone	93.8 % (848 of 904)	97.4 % (295 of 303)	89.9 % (411 of 457)	98.6 % (142 of 144)
Sidechain	79.2 % (868 of 1096)	84.6 % (565 of 668)	72.1 % (294 of 408)	45.0 % (9 of 20)
Aromatic	82.0 % (146 of 178)	93.3 % (83 of 89)	69.8 % (60 of 86)	100.0 % (3 of 3)
Methyl	88.0 % (132 of 150)	96.0 % (72 of 75)	80.0 % (60 of 75)

1. RGS14

SMTEEQPVAS WALSFERLLQ DPLGLAYFTE FLKKEFSAEN VTFWKACERF QQIPASDTQQ LAQEARNIYQ EFLSSQALSP VNIDRQAWLG EEVLAEPRPD MFRAQQLQIF NLMKFDSYAR FVKSPLYREC LLAEAEGRPL REPGSSRLGS PDAT

Show sample condition

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 297 (±0.2) K, pH 6 (±0.05), Details 15N labelled RGS14

#	Name	Isotope labeling	Concentration
1	RGS14	[U-95% 15N]	1 mM
2	sodium phosphate	natural abundance	20 mM
3	sodium chloride	natural abundance	50 mM
4	D2O	natural abundance	10 %
5	DTT	[U-99% 2H]	1 mM

Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 297 (±0.2) K, pH 6 (±0.05), Details 15N, 13C labelled RGS14

#	Name	Isotope labeling	Concentration
6	RGS14	[U-95% 13C; U-95% 15N]	1.7 mM
7	sodium phosphate	natural abundance	20 mM
8	sodium chloride	natural abundance	50 mM
9	DTT	[U-99% 2H]	1 mM
10	D2O	natural abundance	10 %

Sample #3

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 297 (±0.2) K, pH 6 (±0.05), Details 15N, 13C labelled RGS14

#	Name	Isotope labeling	Concentration
11	RGS14	[U-95% 13C; U-95% 15N]	1.4 mM
12	sodium phosphate	natural abundance	20 mM
13	sodium chloride	natural abundance	50 mM
14	DTT	[U-99% 2H]	1 mM
15	D2O	natural abundance	10 %

Sample #4

Solvent system 100% D2O, Pressure 1 atm, Temperature 297 (±0.2) K, pH 6 (±0.05), Details Freeze-dried 15N, 13C labelled RGS14 in 100% D2O

#	Name	Isotope labeling	Concentration
16	RGS14	[U-95% 13C; U-95% 15N]	1.1 mM
17	sodium phosphate	natural abundance	20 mM
18	sodium chloride	natural abundance	50 mM
19	DTT	[U-99% 2H]	1 mM
20	D2O	[U-100% 2H]	100 %
21	sodium azide	natural abundance	0.02 %

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	external	indirect	0.2514495
¹H	DSS	methyl protons	external	direct	1.0
¹⁵N	DSS	methyl protons	external	indirect	0.1013291

Referencing offset: -0.12 ppm, Outliers: 2 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	external	indirect	0.2514495
¹H	DSS	methyl protons	external	direct	1.0
¹⁵N	DSS	methyl protons	external	indirect	0.1013291

Referencing offset: -0.12 ppm, Outliers: 2 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	external	indirect	0.2514495
¹H	DSS	methyl protons	external	direct	1.0
¹⁵N	DSS	methyl protons	external	indirect	0.1013291

Referencing offset: 0.06 ppm, Outliers: 1 Detail

LACS Plot; CO

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹³C	DSS	methyl protons	external	indirect	0.2514495
¹H	DSS	methyl protons	external	direct	1.0
¹⁵N	DSS	methyl protons	external	indirect	0.1013291

Referencing offset: 5.1 ppm, Outliers: 1 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2JNU, Strand ID: A Detail

Release date

2007-08-22

Citation

Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits
Soundararajan, M., Willard, F.S., Kimple, A.J., Turnbull, A.P., Ball, L.J., Schoch, G.A., Gileadi, C., Fedorov, O.Y., Dowler, E.F., Higman, V.A., Hutsell, S.Q., Sundstrom, M., Doyle, D.A., Siderovski, D.P.
Proc. Natl. Acad. Sci. U. S. A. (2008), 105, 6457-6462, PubMed 18434541 , DOI 10.1073/pnas.0801508105 , Abstract

Related entities 1. RGS domain from human RGS14 protein, : 1 : 2 : 177 entities Detail

Interaction partners 1. RGS domain from human RGS14 protein, : 7 interactors Detail

More details for 7 interactors identified by 5 citations

Experiments performed 11 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker DMX - 750 MHz standard configuration with triple resonance cryogenic probe equipped with self-shielded single axis gradient coils

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 297 (±0.2) K, pH 6 (±0.05), Details 15N labelled RGS14

#	Name	Isotope labeling	Concentration
1	RGS14	[U-95% 15N]	1 mM
2	sodium phosphate	natural abundance	20 mM
3	sodium chloride	natural abundance	50 mM
4	D2O	natural abundance	10 %
5	DTT	[U-99% 2H]	1 mM

2 3D 1H-15N NOESY

Instrument

Bruker DMX - 750 MHz standard configuration with triple resonance cryogenic probe equipped with self-shielded single axis gradient coils

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 297 (±0.2) K, pH 6 (±0.05), Details 15N labelled RGS14

#	Name	Isotope labeling	Concentration
1	RGS14	[U-95% 15N]	1 mM
2	sodium phosphate	natural abundance	20 mM
3	sodium chloride	natural abundance	50 mM
4	D2O	natural abundance	10 %
5	DTT	[U-99% 2H]	1 mM

3 3D CBCANH

Instrument

Bruker DMX - 750 MHz standard configuration with triple resonance cryogenic probe equipped with self-shielded single axis gradient coils

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 297 (±0.2) K, pH 6 (±0.05), Details 15N, 13C labelled RGS14

#	Name	Isotope labeling	Concentration
6	RGS14	[U-95% 13C; U-95% 15N]	1.7 mM
7	sodium phosphate	natural abundance	20 mM
8	sodium chloride	natural abundance	50 mM
9	DTT	[U-99% 2H]	1 mM
10	D2O	natural abundance	10 %

4 3D CBCA(CO)NH

Instrument

Bruker DMX - 750 MHz standard configuration with triple resonance cryogenic probe equipped with self-shielded single axis gradient coils

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 297 (±0.2) K, pH 6 (±0.05), Details 15N, 13C labelled RGS14

#	Name	Isotope labeling	Concentration
6	RGS14	[U-95% 13C; U-95% 15N]	1.7 mM
7	sodium phosphate	natural abundance	20 mM
8	sodium chloride	natural abundance	50 mM
9	DTT	[U-99% 2H]	1 mM
10	D2O	natural abundance	10 %

5 3D HNCO

Instrument

Bruker DMX - 750 MHz standard configuration with triple resonance cryogenic probe equipped with self-shielded single axis gradient coils

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 297 (±0.2) K, pH 6.2 (±0.05), Details 15N, 13C labelled RGS14

#	Name	Isotope labeling	Concentration
11	RGS14	[U-95% 13C; U-95% 15N]	1.4 mM
12	sodium phosphate	natural abundance	20 mM
13	sodium chloride	natural abundance	50 mM
14	DTT	[U-99% 2H]	1 mM
15	D2O	natural abundance	10 %

6 3D HN(CA)CO

Instrument

Bruker DMX - 750 MHz standard configuration with triple resonance cryogenic probe equipped with self-shielded single axis gradient coils

Sample

State isotropic, Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 297 (±0.2) K, pH 6.2 (±0.05), Details 15N, 13C labelled RGS14

#	Name	Isotope labeling	Concentration
11	RGS14	[U-95% 13C; U-95% 15N]	1.4 mM
12	sodium phosphate	natural abundance	20 mM
13	sodium chloride	natural abundance	50 mM
14	DTT	[U-99% 2H]	1 mM
15	D2O	natural abundance	10 %

7 3D HCCH-COSY

Instrument

Bruker DRX - 600 MHz standard configuration with triple resonance cryogenic probe equipped with self-shielded single axis gradient coils

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 297 (±0.2) K, pH 6 (±0.05), Details Freeze-dried 15N, 13C labelled RGS14 in 100% D2O

#	Name	Isotope labeling	Concentration
16	RGS14	[U-95% 13C; U-95% 15N]	1.1 mM
17	sodium phosphate	natural abundance	20 mM
18	sodium chloride	natural abundance	50 mM
19	DTT	[U-99% 2H]	1 mM
20	D2O	[U-100% 2H]	100 %
21	sodium azide	natural abundance	0.02 %

8 3D 1H-13C HMQC NOESY

Instrument

Bruker DMX - 750 MHz standard configuration with triple resonance cryogenic probe equipped with self-shielded single axis gradient coils

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 297 (±0.2) K, pH 6 (±0.05), Details Freeze-dried 15N, 13C labelled RGS14 in 100% D2O

#	Name	Isotope labeling	Concentration
16	RGS14	[U-95% 13C; U-95% 15N]	1.1 mM
17	sodium phosphate	natural abundance	20 mM
18	sodium chloride	natural abundance	50 mM
19	DTT	[U-99% 2H]	1 mM
20	D2O	[U-100% 2H]	100 %
21	sodium azide	natural abundance	0.02 %

9 2D 1H-1H NOESY

Instrument

Bruker DMX - 750 MHz standard configuration with triple resonance cryogenic probe equipped with self-shielded single axis gradient coils

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 297 (±0.2) K, pH 6 (±0.05), Details Freeze-dried 15N, 13C labelled RGS14 in 100% D2O

#	Name	Isotope labeling	Concentration
16	RGS14	[U-95% 13C; U-95% 15N]	1.1 mM
17	sodium phosphate	natural abundance	20 mM
18	sodium chloride	natural abundance	50 mM
19	DTT	[U-99% 2H]	1 mM
20	D2O	[U-100% 2H]	100 %
21	sodium azide	natural abundance	0.02 %

10 2D DQF-COSY

Instrument

Bruker DMX - 750 MHz standard configuration with triple resonance cryogenic probe equipped with self-shielded single axis gradient coils

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 297 (±0.2) K, pH 6 (±0.05), Details Freeze-dried 15N, 13C labelled RGS14 in 100% D2O

#	Name	Isotope labeling	Concentration
16	RGS14	[U-95% 13C; U-95% 15N]	1.1 mM
17	sodium phosphate	natural abundance	20 mM
18	sodium chloride	natural abundance	50 mM
19	DTT	[U-99% 2H]	1 mM
20	D2O	[U-100% 2H]	100 %
21	sodium azide	natural abundance	0.02 %

11 3D HCCH-TOCSY

Instrument

Bruker DRX - 600 MHz standard configuration with triple resonance cryogenic probe equipped with self-shielded single axis gradient coils

Sample

State isotropic, Solvent system 100% D2O, Pressure 1 atm, Temperature 297 (±0.2) K, pH 6 (±0.05), Details Freeze-dried 15N, 13C labelled RGS14 in 100% D2O

#	Name	Isotope labeling	Concentration
16	RGS14	[U-95% 13C; U-95% 15N]	1.1 mM
17	sodium phosphate	natural abundance	20 mM
18	sodium chloride	natural abundance	50 mM
19	DTT	[U-99% 2H]	1 mM
20	D2O	[U-100% 2H]	100 %
21	sodium azide	natural abundance	0.02 %

NMR combined restraints 5 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints, Dihedral angle restraints	combined_15128_2jnu.nef
Input source #2: Coordindates	2jnu.cif
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

Sequence alignments

Entity_assembly_ID (NMR): A vs Auth_asym_ID (model): A

--------10--------20--------30--------40--------50--------60--------70--------80--------90-------100
SMTEEQPVASWALSFERLLQDPLGLAYFTEFLKKEFSAENVTFWKACERFQQIPASDTQQLAQEARNIYQEFLSSQALSPVNIDRQAWLGEEVLAEPRPD
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
SMTEEQPVASWALSFERLLQDPLGLAYFTEFLKKEFSAENVTFWKACERFQQIPASDTQQLAQEARNIYQEFLSSQALSPVNIDRQAWLGEEVLAEPRPD

-------110-------120-------130-------140-------150----
MFRAQQLQIFNLMKFDSYARFVKSPLYRECLLAEAEGRPLREPGSSRLGSPDAT
||||||||||||||||||||||||||||||||||||||||||||||||||||||
MFRAQQLQIFNLMKFDSYARFVKSPLYRECLLAEAEGRPLREPGSSRLGSPDAT

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	154	0	0	100.0

Content subtype: combined_15128_2jnu.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1581		99.4 (chain: A, length: 154)
1	Distance restraints	CNS/XPLOR_distance_constraints_2	OK	2258 (1)	noe	99.4 (chain: A, length: 154)
2	Distance restraints	CNS/XPLOR_distance_constraints_3	OK	67 (1)	hbond	37.7 (chain: A, length: 154)
1	Dihedral angle restraints	CNS/XPLOR_dihedral_4	Warning	14 (14)	.	7.1 (chain: A, length: 154)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 154, Sequence coverage: 99.4%
- Total number of assignments
  - ¹H chemical shifts: 863
  - ¹³C chemical shifts: 567
  - ¹⁵N chemical shifts: 151
- Completeness of assignments
  - Entity_assemble_ID: A
- Redox state of CYS
- Peptide bond of PRO
- Rotameric state of ILE , LEU, and VAL
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: A

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	971	863	88.9
¹³C chemical shifts	716	567	79.2
¹⁵N chemical shifts	175	151	86.3

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	303	299	98.7
¹³C chemical shifts	308	284	92.2
¹⁵N chemical shifts	144	142	98.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	668	564	84.4
¹³C chemical shifts	408	283	69.4
¹⁵N chemical shifts	31	9	29.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	78	74	94.9
¹³C chemical shifts	78	56	71.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	89	80	89.9
¹³C chemical shifts	86	56	65.1
¹⁵N chemical shifts	3	3	100.0

Distance restraints

Saveframe: CNS/XPLOR_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 154, Sequence coverage: 99.4%
- Total number of restraints: 2252
- Weight of restraints: 1.0 (2252)
- Potential type of restraints: square-well-parabolic (2252)
- Range of distance target values: 2.3, 4.4 (Å)
- Histogram of distance target values
- Histogram of discrepancy in distance target values
- Distance restraints per residue
  - Chain_ID: A
- Distance restraints on contact map
- Saveframe: CNS/XPLOR_distance_constraints_3
  - Status: OK
  - Experiment type: hbond
  - Sequence coverage of experimental data
    - Entity_assembly_ID: A, Chain length: 154, Sequence coverage: 37.7%
  - Total number of restraints: 67
  - Weight of restraints: 1.0 (67)
  - Potential type of restraints: square-well-parabolic (67)
  - Range of distance target values: 2.05, 3.0 (Å)
  - Histogram of distance target values
  - Distance restraints per residue
    - Chain_ID: A
  - Distance restraints on contact map

Dihedral angle restraints

Saveframe: CNS/XPLOR_dihedral_4
- Status: Warning
- Experiment type: .
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 154, Sequence coverage: 7.1%
- Total number of restraints: 14
- Total number of restraints per polymer type: 14
- Weight of restraints: 1.0 (14)
- Potential type of restraints: square-well-parabolic (14)
- Plot of Phi-Psi angle restraints
- Dihedral angle restraints per residue

Keywords signalling, Regulator of G-protein signalling domain

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Found 1 Document (0.769 seconds)

BMRB: 15128

Sample #1

Sample #2

Sample #3

Sample #4

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. RGS domain from human RGS14 protein, : 1 : 2 : 177 entities Detail

Interaction partners 1. RGS domain from human RGS14 protein, : 7 interactors Detail

Experiments performed 11 experiments Detail

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NMR combined restraints 5 contents Detail