BMRBj - BMREntryMaster

Found 1 Document (3.423 seconds)

BMRB: 18905

2M2B

NMR structure of the RRM2 domain of the protein RBM10 from homo sapiens

Authors

Serrano, P., Geralt, M., Dutta, S.K., Wuthrich, K., Wrobel, R.L., Makino, S., Misenhiemer, T.M., Markley, J.L., Fox, B.G.

Assembly

RRM2 domain of the protein RBM10 from homo sapiens

Entity

1. RRM2 domain of the protein RBM10 from homo sapiens (polymer, Thiol state: not present), 131 monomers, 13772.39 Da Detail

QAQGVLASQA LSQGSEPSSE NANDTIILRN LNPHSTMDSI LGALAPYAVL SSSNVRVIKD KQTQLNRGFA FIQLSTIEAA QLLQILQALH PPLTIDGKTI NVEFAKGSKR DMASNEGSRI SAASVASTAI A

Formula weight

13772.39 Da

Source organism

Exptl. method

Refine. method

molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 93.9 %, Completeness: 84.0 %, Completeness (bb): 86.6 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	84.0 % (1214 of 1446)	82.6 % (615 of 745)	84.7 % (472 of 557)	88.2 % (127 of 144)
Backbone	86.6 % (672 of 776)	88.6 % (234 of 264)	83.9 % (324 of 386)	90.5 % (114 of 126)
Sidechain	81.5 % (647 of 794)	78.4 % (377 of 481)	87.5 % (258 of 295)	66.7 % (12 of 18)
Aromatic	84.8 % (39 of 46)	87.0 % (20 of 23)	82.6 % (19 of 23)
Methyl	92.0 % (160 of 174)	92.0 % (80 of 87)	92.0 % (80 of 87)

1. entity

QAQGVLASQA LSQGSEPSSE NANDTIILRN LNPHSTMDSI LGALAPYAVL SSSNVRVIKD KQTQLNRGFA FIQLSTIEAA QLLQILQALH PPLTIDGKTI NVEFAKGSKR DMASNEGSRI SAASVASTAI A

Show sample condition

Sample

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-98% 13C; U-98% 15N]		0.6 mM
2	sodium chloride	natural abundance		100 mM
3	sodium acetate	[U-99% 2H]		10 mM
4	sodium azide	natural abundance		5 mM
5	DTT	natural abundance		2 mM
6	H2O	natural abundance		95 %
7	D20	natural abundance		5 %

LACS Plot; CA

Referencing offset: 2.58 ppm, Outliers: 1 Detail

LACS Plot; CB

Referencing offset: 2.58 ppm, Outliers: 1 Detail

LACS Plot; HA

Referencing offset: 0.06 ppm, Outliers: 3 Detail

LACS Plot; CO

Referencing offset: 2.84 ppm, Outliers: 4 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 2M2B, Strand ID: A Detail

Release date

2013-01-31

Citation

NMR structure of the RRM2 domain of the protein RBM10 from homo sapiens
Serrano, P., Wuthrich, K.
Not known

Related entities 1. RRM2 domain of the protein RBM10 from homo sapiens, : 1 : 25 entities Detail

Interaction partners 1. RRM2 domain of the protein RBM10 from homo sapiens, : 90 interactors Detail

More details for 90 interactors identified by 24 citations

Experiments performed 7 experiments Detail

1 2D 1H-15N HSQC

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-98% 13C; U-98% 15N]		0.6 mM
2	sodium chloride	natural abundance		100 mM
3	sodium acetate	[U-99% 2H]		10 mM
4	sodium azide	natural abundance		5 mM
5	DTT	natural abundance		2 mM
6	H2O	natural abundance		95 %
7	D20	natural abundance		5 %

2 3D 1H-13C NOESY aliphatic

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-98% 13C; U-98% 15N]		0.6 mM
2	sodium chloride	natural abundance		100 mM
3	sodium acetate	[U-99% 2H]		10 mM
4	sodium azide	natural abundance		5 mM
5	DTT	natural abundance		2 mM
6	H2O	natural abundance		95 %
7	D20	natural abundance		5 %

3 3D 1H-13C NOESY aromatic

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-98% 13C; U-98% 15N]		0.6 mM
2	sodium chloride	natural abundance		100 mM
3	sodium acetate	[U-99% 2H]		10 mM
4	sodium azide	natural abundance		5 mM
5	DTT	natural abundance		2 mM
6	H2O	natural abundance		95 %
7	D20	natural abundance		5 %

4 3D 1H-15N NOESY

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-98% 13C; U-98% 15N]		0.6 mM
2	sodium chloride	natural abundance		100 mM
3	sodium acetate	[U-99% 2H]		10 mM
4	sodium azide	natural abundance		5 mM
5	DTT	natural abundance		2 mM
6	H2O	natural abundance		95 %
7	D20	natural abundance		5 %

5 4D APSY HACANH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-98% 13C; U-98% 15N]		0.6 mM
2	sodium chloride	natural abundance		100 mM
3	sodium acetate	[U-99% 2H]		10 mM
4	sodium azide	natural abundance		5 mM
5	DTT	natural abundance		2 mM
6	H2O	natural abundance		95 %
7	D20	natural abundance		5 %

6 5D APSY CBCACONH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-98% 13C; U-98% 15N]		0.6 mM
2	sodium chloride	natural abundance		100 mM
3	sodium acetate	[U-99% 2H]		10 mM
4	sodium azide	natural abundance		5 mM
5	DTT	natural abundance		2 mM
6	H2O	natural abundance		95 %
7	D20	natural abundance		5 %

7 5D APSY HACACONH

Instrument

Bruker Avance - 600 MHz

Sample

State isotropic, Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 298 K, pH 5

#	Name	Isotope labeling	Type	Concentration
1	entity	[U-98% 13C; U-98% 15N]		0.6 mM
2	sodium chloride	natural abundance		100 mM
3	sodium acetate	[U-99% 2H]		10 mM
4	sodium azide	natural abundance		5 mM
5	DTT	natural abundance		2 mM
6	H2O	natural abundance		95 %
7	D20	natural abundance		5 %

NMR combined restraints 3 contents Detail

Properties

Input source #1: NMR data (NEF) - Assigned chemical shifts, Distance restraints	combined_18905_2m2b.nef
Input source #2: Coordindates	2m2b.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
QAQGVLASQALSQGSEPSSENANDTIILRNLNPHSTMDSILGALAPYAVLSSSNVRVIKDKQTQLNRGFAFIQLSTIEAAQLLQILQALHPPLTIDGKTI
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
QAQGVLASQALSQGSEPSSENANDTIILRNLNPHSTMDSILGALAPYAVLSSSNVRVIKDKQTQLNRGFAFIQLSTIEAAQLLQILQALHPPLTIDGKTI

-------110-------120-------130-
NVEFAKGSKRDMASNEGSRISAASVASTAIA
|||||||||||||||||||||||||||||||
NVEFAKGSKRDMASNEGSRISAASVASTAIA

Chain assignments

Entity_assembly_ID (NMR)	Auth_asym_ID (model)	Length	Unmapped	Conflict	Sequence coverage (%)
A	A	131	0	0	100.0

Content subtype: combined_18905_2m2b.nef

#	Content subtype	Saveframe	Status	# of rows (sets)	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	assigned_chem_shift_list_1	Warning	1176		90.1 (chain: A, length: 131)
1	Distance restraints	DYANA/DIANA_distance_constraints_2	OK	1804 (1)	noe	85.5 (chain: A, length: 131)

Assigned chemical shifts

Saveframe: assigned_chem_shift_list_1
- Status: Warning
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 131, Sequence coverage: 90.1%
- Total number of assignments
  - ¹H chemical shifts: 606
  - ¹³C chemical shifts: 446
  - ¹⁵N chemical shifts: 124
- Completeness of assignments
  - Entity_assemble_ID: A
- Peptide bond of PRO
- Tautomeric state of HIS
- 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

Distance restraints

Saveframe: DYANA/DIANA_distance_constraints_2
- Status: OK
- Experiment type: noe
- Sequence coverage of experimental data
  - Entity_assembly_ID: A, Chain length: 131, Sequence coverage: 85.5%
- Total number of restraints: 1804
- Weight of restraints: 1.0 (1804)
- Potential type of restraints: upper-bound-parabolic (1804)
- Range of distance target values: 2.4, 5.5 (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

Keywords PSI:Biology, RBM10, RNA binding protein, RRM, T-Cell