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 17364

Title: The solution structure of the PTB Domain of TENC1 in complex with the peptide of DLC1   PubMed: 22645138

Deposition date: 2010-12-14 Original release date: 2012-06-04

Authors: Liu, Changdong; Chen, Lihong; Feng, Rui; Zhu, Guang

Citation: Chen, Lihong; Liu, Changdong; Ko, Frankie Chi Fat; Xu, Naining; Ng, Irene Oi-Lin; Yam, Judy Wai Ping; Zhu, Guang. "Solution structure of the phosphotyrosine binding (PTB) domain of human tensin2 protein in complex with deleted in liver cancer 1 (DLC1) peptide reveals a novel peptide binding mode."  J. Biol. Chem. 287, 26104-26114 (2012).

Assembly members:
PTB_domian, polymer, 147 residues, 15983.273 Da.
DLC1_peptide, polymer, 21 residues, 2243.518 Da.

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

Experimental source:   Production method: recombinant technology' 'Escherichia coli

Entity Sequences (FASTA):
PTB_domian: MSTAADLLRQGAACSVLYLT SVETESLTGPQAVARASSAA LSCSPRPTPAVVHFKVSAQG ITLTDNQRKLFFRRHYPVNS ITFSSTDPQDRRWTNPDGTT SKIFGFVAKKPGSPWENVCH LFAELDPDQPAGAIVTFITK VLLGQRK
DLC1_peptide: IPEDHKPGTFPKALTNGSFS P

Data sets:
Data typeCount
13C chemical shifts484
15N chemical shifts133
1H chemical shifts992

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PTB domian1
2DLC1 peptide2

Entities:

Entity 1, PTB domian 147 residues - 15983.273 Da.

1   METSERTHRALAALAASPLEULEUARGGLN
2   GLYALAALACYSSERVALLEUTYRLEUTHR
3   SERVALGLUTHRGLUSERLEUTHRGLYPRO
4   GLNALAVALALAARGALASERSERALAALA
5   LEUSERCYSSERPROARGPROTHRPROALA
6   VALVALHISPHELYSVALSERALAGLNGLY
7   ILETHRLEUTHRASPASNGLNARGLYSLEU
8   PHEPHEARGARGHISTYRPROVALASNSER
9   ILETHRPHESERSERTHRASPPROGLNASP
10   ARGARGTRPTHRASNPROASPGLYTHRTHR
11   SERLYSILEPHEGLYPHEVALALALYSLYS
12   PROGLYSERPROTRPGLUASNVALCYSHIS
13   LEUPHEALAGLULEUASPPROASPGLNPRO
14   ALAGLYALAILEVALTHRPHEILETHRLYS
15   VALLEULEUGLYGLNARGLYS

Entity 2, DLC1 peptide 21 residues - 2243.518 Da.

1   ILEPROGLUASPHISLYSPROGLYTHRPHE
2   PROLYSALALEUTHRASNGLYSERPHESER
3   PRO

Samples:

sample_1: PTB domian' '[U-100% 13C; U-100% 15N]; .; . mM; . mM; 2, $DLC1_peptide, ; .; .

sample_2: PTB domian' '[U-100% 13C; U-100% 15N]; .; . mM; .; .; .

sample_conditions_1: ionic strength: 0.2 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 13C/15N filtered-13C edited NOESYsample_2isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

HADDOCK v1.3, Alexandre Bonvin - structure solution

ProcheckNMR, Laskowski and MacArthur - geometry optimization

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 750 MHz
  • Varian INOVA 800 MHz

Related Database Links:

BMRB 10318
PDB
DBJ BAA83027 BAG09960 BAG54765 BAB21814 BAF82423 BAF84371 BAG10131 BAG61122
EMBL CAB70815 CAH56176
GB AAH54099 AAI10855 AAI29829 AAI29830 AAI31504 AAB81637 AAB87700 AAH54511 AAK97501 ACE86794
REF NP_056134 NP_736610 NP_938072 XP_001102202 XP_001790253 NP_001157743 NP_006085 NP_872584 XP_001092830 XP_003256738
SP Q63HR2 Q96QB1
TPG DAA29990
PIR G59435

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