BMRB Entry 19955

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19955
MolProbity Validation Chart

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Title:
solution structure of tandem SH3 domain of Sorbin and SH3 domain-containing protein 1
Deposition date:
2014-05-07
Original release date:
2014-05-27
Authors:
Zhao, Debiao; Wang, Chongyuan; Zhang, Jiahai; Wu, Jihui; Shi, Yunyu; Zhang, Zhiyong; Gong, Qingguo
Citation:

Citation: Zhao, Debiao; Wang, Xuejuan; Peng, Junhui; Wang, Chongyuan; Li, Fudong; Sun, Qianqian; Zhang, Yibo; Zhang, Jiahai; Cai, Gang; Zuo, Xiaobing; Wu, Jihui; Shi, Yunyu; Zhang, Zhiyong; Gong, Qingguo. "Structural Investigation of the Interaction between the Tandem SH3 Domains of c-Cbl-Associated Protein and Vinculin"  .

Assembly members:

Assembly members:
entity, polymer, 143 residues, 16663.225 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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: QHMSGSEMRPARAKFDFKAQ TLKELPLQKGDIVYIYKQID QNWYEGEHHGRVGIFPRTYI ELLPPAEKAQPKKLTPVQVL EYGEAIAKFNFNGDTQVEMS FRKGERITLLRQVDENWYEG RIPGTSRQGIFPITYVDVIK RPL

Data sets:
Data typeCount
13C chemical shifts551
15N chemical shifts132
1H chemical shifts970

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1tandem SH3 domain of CAP1

Entities:

Entity 1, tandem SH3 domain of CAP 143 residues - 16663.225 Da.

1   GLNHISMETSERGLYSERGLUMETARGPRO
2   ALAARGALALYSPHEASPPHELYSALAGLN
3   THRLEULYSGLULEUPROLEUGLNLYSGLY
4   ASPILEVALTYRILETYRLYSGLNILEASP
5   GLNASNTRPTYRGLUGLYGLUHISHISGLY
6   ARGVALGLYILEPHEPROARGTHRTYRILE
7   GLULEULEUPROPROALAGLULYSALAGLN
8   PROLYSLYSLEUTHRPROVALGLNVALLEU
9   GLUTYRGLYGLUALAILEALALYSPHEASN
10   PHEASNGLYASPTHRGLNVALGLUMETSER
11   PHEARGLYSGLYGLUARGILETHRLEULEU
12   ARGGLNVALASPGLUASNTRPTYRGLUGLY
13   ARGILEPROGLYTHRSERARGGLNGLYILE
14   PHEPROILETHRTYRVALASPVALILELYS
15   ARGPROLEU

Samples:

sample_1: sodium phosphate 50 mM; protein, [U-100% 15N], 0.5 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_2: sodium phosphate 50 mM; EDTA 1 mM; protein, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%

sample_3: sodium phosphate 50 mM; EDTA 1 mM; protein, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%

sample_4: sodium phosphate, [U-100% 15N], 50 mM; EDTA 1 mM; C12E5 4.5%; protein, [U-100% 15N], 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
IPAP schemesample_4anisotropicsample_conditions_1

Software:

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

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Bruker DMX 500 MHz
  • Bruker DMX 600 MHz

Related Database Links:

PDB
EMBL CAE45892 CAJ97431
GB AAI60134 AAK37563 AAK37564 AAK37565 EHB15262
REF NP_001030126 NP_001030127 NP_001030128 NP_001277223 XP_001501975
SP Q9BX66
AlphaFold Q9BX66

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks