BMRB Entry 16472

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16472
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
NMR Solution Structure of SH2 Domain of the Human Tensin Like C1 Domain Containing Phosphatase (TENC1)
Deposition date:
2009-08-27
Original release date:
2010-08-26
Authors:
Chen, Lihong; Feng, Rui; Liu, Changdong; Zhu, Guang
Citation:

Citation: Chen, Lihong; Liu, Changdong; Rui, Feng; Zhu, Guang. "1H, 15N and 13C chemical shift assignments of the SH2 domain of human tensin2 (TENC1)."  Biomol. NMR Assignments 5, 211-214 (2011).
PubMed: 21461930

Assembly members:

Assembly members:
SH2 Domain, polymer, 131 residues, 14402.661 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: pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SH2 Domain: MHHHHHHSSGLVPRGSDTSK FWYKPHLSRDQAIALLKDKD PGAFLIRDSHSFQGAYGLAL KVATPPPSAQPWKGDPVEQL VRHFLIETGPKGVKIKGCPS EPYFGSLSALVSQHSISPIS LPCCLRIPSKD

Data sets:
Data typeCount
13C chemical shifts337
15N chemical shifts103
1H chemical shifts774

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH2 Domain1

Entities:

Entity 1, SH2 Domain 131 residues - 14402.661 Da.

Residues 1-16 represent a non-native affinity tag. This tag comes from the expression vector. Residues 17-131 represent the SH2 domain of TENC1.

1   METHISHISHISHISHISHISSERSERGLY
2   LEUVALPROARGGLYSERASPTHRSERLYS
3   PHETRPTYRLYSPROHISLEUSERARGASP
4   GLNALAILEALALEULEULYSASPLYSASP
5   PROGLYALAPHELEUILEARGASPSERHIS
6   SERPHEGLNGLYALATYRGLYLEUALALEU
7   LYSVALALATHRPROPROPROSERALAGLN
8   PROTRPLYSGLYASPPROVALGLUGLNLEU
9   VALARGHISPHELEUILEGLUTHRGLYPRO
10   LYSGLYVALLYSILELYSGLYCYSPROSER
11   GLUPROTYRPHEGLYSERLEUSERALALEU
12   VALSERGLNHISSERILESERPROILESER
13   LEUPROCYSCYSLEUARGILEPROSERLYS
14   ASP

Samples:

sample_1: SH2, [U-100% 13C], 1 mM; sodium acetate 100 mM; sodium chloride 100 mM; D2O 100%

sample_2: SH2, [U-100% 15N], 1 mM; sodium acetate 100 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_3: SH2, [U-100% 13C; U-100% 15N], 1 mM; sodium acetate 100 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_4: SH2 1 mM; sodium acetate 100 mM; sodium chloride 100 mM; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement, structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 500 MHz

Related Database Links:

BMRB 17314
PDB
DBJ BAA83027 BAG09960
EMBL CAB70815 CAH56176
GB AAH25818 AAH42190 AAH54099 AAI10855 AAI29829
REF NP_056134 NP_705761 NP_736610 NP_938072 XP_001102202
SP Q63HR2 Q8CGB6
AlphaFold Q63HR2 Q8CGB6

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