BMRB Entry 18526

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18526
MolProbity Validation Chart

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Title:
Solution NMR Structure of PH Domain of Tyrosine-protein kinase Tec from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR3504C
Deposition date:
2012-06-15
Original release date:
2012-08-13
Authors:
Liu, Gaohua; Xiao, Rong; Janjua, Haleema; Hamilton, Keith; Shastry, Ritu; Kohan, Eitan; Acton, Thomas; Everett, John; Lee, Hsiau-Wei; Pederson, Kari; Huang, Yuangpeng; Montelione, Gaetano
Citation:

Citation: Liu, Gaohua; Xiao, Rong; Janjua, Haleema; Hamilton, Keith; Shastry, Ritu; Kohan, Eitan; Acton, Thomas; Everett, John; Lee, Hsiau-Wei; Pederson, Kari; Huang, Yuangpeng; Montelione, Gaetano. "Solution NMR Structure of PH Domain of Tyrosine-protein kinase Tec from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR3504C"  To be published ., .-..

Assembly members:

Assembly members:
HR3504C, polymer, 165 residues, 19577.119 Da.
ZINC ION, non-polymer, 65.409 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):
HR3504C: MGHHHHHHSHMNFNTILEEI LIKRSQQKKKTSPLNYKERL FVLTKSMLTYYEGRAEKKYR KGFIDVSKIKCVEIVKNDDG VIPCQNKYPFQVVHDANTLY IFAPSPQSRDLWVKKLKEEI KNNNNIMIKYHPKFWTDGSY QCCRQTEKLAPGCEKYNLFE SSIRX

Data sets:
Data typeCount
13C chemical shifts700
15N chemical shifts152
1H chemical shifts1131
residual dipolar couplings67

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR3504C1
2Zinc ion2

Entities:

Entity 1, HR3504C 165 residues - 19577.119 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METASNPHEASNTHRILELEUGLUGLUILE
3   LEUILELYSARGSERGLNGLNLYSLYSLYS
4   THRSERPROLEUASNTYRLYSGLUARGLEU
5   PHEVALLEUTHRLYSSERMETLEUTHRTYR
6   TYRGLUGLYARGALAGLULYSLYSTYRARG
7   LYSGLYPHEILEASPVALSERLYSILELYS
8   CYSVALGLUILEVALLYSASNASPASPGLY
9   VALILEPROCYSGLNASNLYSTYRPROPHE
10   GLNVALVALHISASPALAASNTHRLEUTYR
11   ILEPHEALAPROSERPROGLNSERARGASP
12   LEUTRPVALLYSLYSLEULYSGLUGLUILE
13   LYSASNASNASNASNILEMETILELYSTYR
14   HISPROLYSPHETRPTHRASPGLYSERTYR
15   GLNCYSCYSARGGLNTHRGLULYSLEUALA
16   PROGLYCYSGLULYSTYRASNLEUPHEGLU
17   SERSERILEARGZN

Entity 2, Zinc ion - Zn - 65.409 Da.

1   ZN

Samples:

sample_NC: hr3504c.023, [U-100% 13C; U-100% 15N], 0.614 mM; DSS 50 uM; DTT 10 mM; ZnSO4 50 uM; NaN3 0.02%; NaCL 100 mM; MES pH 6.5 20 mM; Proteinase Inhibitors 1 X; D2O 10%; H2O 90%

sample_NC5: hr3504c.025, [U-5% 13C; U-100% 15N], 0.828 mM; DSS 50 uM; DTT 10 mM; ZnSO4 50 uM; NaN3 0.02%; NaCL 100 mM; MES pH 6.5 20 mM; Proteinase Inhibitors 1 X; D2O 10%; H2O 90%

sample_NC5_RDC: hr3504c.027, [U-5% 13C; U-100% 15N], 0.52 mM; DSS 50 uM; DTT 10 mM; ZnSO4 50 uM; NaN3 0.02%; NaCL 100 mM; MES pH 6.5 20 mM; Proteinase Inhibitors 1 X; D2O 10%; H2O 90%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NCisotropicsample_conditions_1
3D HNCOsample_NCisotropicsample_conditions_1
3D CBCA(CO)NHsample_NCisotropicsample_conditions_1
3D HNCACBsample_NCisotropicsample_conditions_1
3D 1H-13C arom NOESYsample_NCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_NCisotropicsample_conditions_1
3D HCCH-TOCSYsample_NCisotropicsample_conditions_1
3D C(CO)NHsample_NCisotropicsample_conditions_1
3D HBHA(CO)NHsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NC5isotropicsample_conditions_1
2D 1H-15N HSQCsample_NC5_RDCisotropicsample_conditions_1

Software:

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

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

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

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

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

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

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

SPARKY, Goddard - data analysis

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

REDCAT, Valafar, Prestegard - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAA06171
GB AAI01712 AAI01714 AAI43488 AAQ02597 EAW93055
REF NP_003206 XP_001103213 XP_001493391 XP_002688295 XP_002806710
SP P42680
TPG DAA28680
AlphaFold P42680

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