BMRB Entry 17683

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17683
MolProbity Validation Chart

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Title:
Solution NMR Structure of Heat shock factor protein 1 DNA binding domain from homo sapiens, Northeast Structural Genomics Consortium Target HR3023C
Deposition date:
2011-06-01
Original release date:
2011-07-05
Authors:
Liu, G.; Xiao, R.; Ciccosanti, C.; Janjua, H.; Acton, T.; Lee, Hsiau-wei; Wang, H.; Huang, Yuanpeng; Everett, J.; Montelione, G.
Citation:

Citation: Liu, G.; Xiao, R.; Ciccosanti, C.; Janjua, H.; Acton, T.; Wang, H.; Lee, Hsiau-wei; Huang, Yuanpeng; Everett, J.; Montelione, G.. "Northeast Structural Genomics Consortium Target HR3023C"  To be published ., .-..

Assembly members:

Assembly members:
HR3023C, polymer, 125 residues, 14401.479 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 14-15C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HR3023C: MGHHHHHHSHMAGPSNVPAF LTKLWTLVSDPDTDALICWS PSGNSFHVFDQGQFAKEVLP KYFKHNNMASFVRQLNMYGF RKVVHIEQGGLVKPERDDTE FQHPCFLRGQEQLLENIKRK VTSVS

Data sets:
Data typeCount
13C chemical shifts528
15N chemical shifts120
1H chemical shifts830

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR3023C1

Entities:

Entity 1, HR3023C 125 residues - 14401.479 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METALAGLYPROSERASNVALPROALAPHE
3   LEUTHRLYSLEUTRPTHRLEUVALSERASP
4   PROASPTHRASPALALEUILECYSTRPSER
5   PROSERGLYASNSERPHEHISVALPHEASP
6   GLNGLYGLNPHEALALYSGLUVALLEUPRO
7   LYSTYRPHELYSHISASNASNMETALASER
8   PHEVALARGGLNLEUASNMETTYRGLYPHE
9   ARGLYSVALVALHISILEGLUGLNGLYGLY
10   LEUVALLYSPROGLUARGASPASPTHRGLU
11   PHEGLNHISPROCYSPHELEUARGGLYGLN
12   GLUGLNLEULEUGLUASNILELYSARGLYS
13   VALTHRSERVALSER

Samples:

sample_NC: HR3023C, [U-100% 13C; U-100% 15N], 0.51 mM; H2O 90%; D2O 10%

sample_NC5: HR3023C, [U-100% 13C; U-100% 15N], 0.43 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES 20 mM; DSS 50 uM; D2O 10%; H2O 90%

sample_NC5_pol: HR3023C, [U-100% 13C; U-100% 15N], 0.43 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES 20 mM; DSS 50 uM; D2O 10%; H2O 90%

sample_NC5_peg: HR3023C, [U-100% 13C; U-100% 15N], 0.43 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES 20 mM; DSS 50 uM; 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_NC5isotropicsample_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
2D 1H-13C HSQC aromaticsample_NCisotropicsample_conditions_1
2D 1H-15N HSQCsample_NC5_polisotropicsample_conditions_1
2D 1H-15N HSQCsample_NC5_pegisotropicsample_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

NMR spectrometers:

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

Related Database Links:

PDB
DBJ BAD96217 BAF83664 BAG73234 BAK63583
EMBL CAA43892 CAD58796
GB AAA52695 AAC80425 AAH13716 AAH14638 AAH94064
PRF 2102256A
REF NP_001070277 NP_001230748 NP_001266850 NP_001301273 NP_005517
SP P38532 Q00613 Q08DJ8
TPG DAA22852
AlphaFold P38532 Q00613 Q08DJ8

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