BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19684

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts270
15N chemical shifts66
1H chemical shifts437

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR9129A1

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   METGLYHISHISHISHISHISHISSERHIS
2   METILEARGSERARGLYSALAARGALAVAL
3   TYRPROCYSGLUALAGLUHISSERSERGLU
4   LEUSERPHEGLUILEGLYALAILEPHEGLU
5   ASPVALGLNTHRSERARGGLUPROGLYTRP
6   LEUGLUGLYTHRLEUASNGLYLYSARGGLY
7   LEUILEPROGLNASNTYRVALLYSLEULEU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C CT HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-13C CT HSQC aromaticsample_1isotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D(H)CCH-TOCSY alisample_1isotropicsample_conditions_1
3D (H)CCH-COSY alisample_1isotropicsample_conditions_1
GFT-43D (H)CCH-COSY aromaticsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
gNfHSQC_Hissample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C ct-HSQC methyl(28ms)sample_2isotropicsample_conditions_1
2D 1H-13C CT HSQC-methyl (42ms)sample_2isotropicsample_conditions_1
2D 1H-13C CT HSQC-methyl (56ms)sample_2isotropicsample_conditions_1
2D J-modulation 1H-15N HSQCsample_2Aligned in poly acrylamidesample_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

Related Database Links:

HUGO ARHGAP10
NCBI 79658
UNP A1A4S6
PDB
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

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts