BMRB Entry 19684

Name: Solution NMR Structure of SH3 Domain 1 of Rho GTPase-activating Protein 10 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target: HR9129A
Published: 2013-12-20

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PDB ID: 2mio
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19684
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of SH3 Domain 1 of Rho GTPase-activating Protein 10 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target: HR9129A

Deposition date:

2013-12-13

Original release date:

2013-12-20

Authors:

Xu, Xianzhong; Eletsky, Alexander; Pulavarti, Surya; Wang, Huang; O'Connell, Patrick; Janjua, Haleema; Xiao, Rong; Everett, John; Sukumaran, Dinesh; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: Xu, Xianzhong; Eletsky, Alexander; Pulavarti, Surya; Wang, Huang; O'Connell, Patrick; Janjua, Haleema; Xiao, Rong; Everett, John; Sukumaran, Dinesh; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of SH3 Domain 1 of Rho GTPase-activating Protein 10 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target: HR9129A" To be published ., .-..

Assembly members:

Assembly members:
HR9129A, polymer, 70 residues, 8044.164 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HR9129A: MGHHHHHHSHMIRSRKARAV YPCEAEHSSELSFEIGAIFE DVQTSREPGWLEGTLNGKRG LIPQNYVKLL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- cali
- caro
- n

Data type	Count
13C chemical shifts	270
15N chemical shifts	66
1H chemical shifts	437

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HR9129A	1

Entities:

Entity 1, HR9129A 70 residues - 8044.164 Da.

Residues 12-70 correspond to the residues 728-786 of the native protein. Residues 1-11 are the un-cleaved his-tag.

1	MET	GLY	HIS	HIS	HIS	HIS	HIS	HIS	SER	HIS
2	MET	ILE	ARG	SER	ARG	LYS	ALA	ARG	ALA	VAL
3	TYR	PRO	CYS	GLU	ALA	GLU	HIS	SER	SER	GLU
4	LEU	SER	PHE	GLU	ILE	GLY	ALA	ILE	PHE	GLU
5	ASP	VAL	GLN	THR	SER	ARG	GLU	PRO	GLY	TRP
6	LEU	GLU	GLY	THR	LEU	ASN	GLY	LYS	ARG	GLY
7	LEU	ILE	PRO	GLN	ASN	TYR	VAL	LYS	LEU	LEU

Samples:

sample_1: HR9129A, [U-99% 13C; U-98% 15N], 0.72 mM

sample_2: HR9129A, [U-99% 13C; U-98% 15N], 0.72 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C CT HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D 1H-13C CT HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D(H)CCH-TOCSY ali	sample_1	isotropic	sample_conditions_1
3D (H)CCH-COSY ali	sample_1	isotropic	sample_conditions_1
GFT-43D (H)CCH-COSY aromatic	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
gNfHSQC_His	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C ct-HSQC methyl(28ms)	sample_2	isotropic	sample_conditions_1
2D 1H-13C CT HSQC-methyl (42ms)	sample_2	isotropic	sample_conditions_1
2D 1H-13C CT HSQC-methyl (56ms)	sample_2	isotropic	sample_conditions_1
2D J-modulation 1H-15N HSQC	sample_2	Aligned in poly acrylamide	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinemen, structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinemen, structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

VNMRJ, Varian - collection

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PSVS, Bhattacharya, Montelione, Guntert - processing, structure validation

CSI, David Wishart,Leigh Willard,Tim Jellard,Brian Sykes - data analysis

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

Varian INOVA 600 MHz

HUGO	ARHGAP10
NCBI	79658
UNP	A1A4S6
PDB	2MIO
DBJ	BAB14924 BAB61771 BAG65274
EMBL	CAD39024 CAG33609
GB	AAH11920 AAH47914 AAI06019 AAI09030 AAI09031
REF	NP_001070298 NP_001102971 NP_078881 XP_002815242 XP_003258064
SP	A1A4S6 Q08DP6
TPG	DAA20889
AlphaFold	Q96S75 A1A4S6 Q08DP6

1	MET	GLY	HIS	HIS	HIS	HIS	HIS	HIS	SER	HIS
2	MET	ILE	ARG	SER	ARG	LYS	ALA	ARG	ALA	VAL
3	TYR	PRO	CYS	GLU	ALA	GLU	HIS	SER	SER	GLU
4	LEU	SER	PHE	GLU	ILE	GLY	ALA	ILE	PHE	GLU
5	ASP	VAL	GLN	THR	SER	ARG	GLU	PRO	GLY	TRP
6	LEU	GLU	GLY	THR	LEU	ASN	GLY	LYS	ARG	GLY
7	LEU	ILE	PRO	GLN	ASN	TYR	VAL	LYS	LEU	LEU

1	MET	GLY	HIS	HIS	HIS	HIS	HIS	HIS	SER	HIS
2	MET	ILE	ARG	SER	ARG	LYS	ALA	ARG	ALA	VAL
3	TYR	PRO	CYS	GLU	ALA	GLU	HIS	SER	SER	GLU
4	LEU	SER	PHE	GLU	ILE	GLY	ALA	ILE	PHE	GLU
5	ASP	VAL	GLN	THR	SER	ARG	GLU	PRO	GLY	TRP
6	LEU	GLU	GLY	THR	LEU	ASN	GLY	LYS	ARG	GLY
7	LEU	ILE	PRO	GLN	ASN	TYR	VAL	LYS	LEU	LEU