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 17389

Title: Solution NMR Structure of the serine-rich domain of hEF1( Enhancer of filamentation 1) from homo sapiens, Northeast Structural Genomics Consortium Target HR5554A

Deposition date: 2010-12-31 Original release date: 2011-01-31

Authors: Liu, Gaohua; Xiao, Rong; Huang, Yuanpeng; Patel, Daya; Ciccosanti, Colleen; Acton, Thomas; Tong, Saichu; Everett, John; Montelione, Gaetano

Citation: Liu, Gaohua; Xiao, Rong; Huang, Yuanpeng; Patel, Daya; Ciccosanti, Colleen; Tong, Saichu; Acton, Thomas; Everett, John; Montelione, Gaetano. "Northeast Structural Genomics Consortium Target HR5554A"  To be published ., .-..

Assembly members:
HR5554A, polymer, 176 residues, 20238.305 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
HR5554A: MGHHHHHHSHMDKRLFLDPD TAIERLQRLQQALEMGVSSL MALVTTDWRCYGYMERHINE IRTAVDKVELFLKEYLHFVK GAVANAACLPELILHNKMKR ELQRVEDSHQILSQTSHDLN ECSWSLNILAINKPQNKCDD LDRFVMVAKTVPDDAKQLTT TINTNAEALFRPGPGS

Data sets:
Data typeCount
13C chemical shifts569
15N chemical shifts162
1H chemical shifts1181

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR5554A1

Entities:

Entity 1, HR5554A 176 residues - 20238.305 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METASPLYSARGLEUPHELEUASPPROASP
3   THRALAILEGLUARGLEUGLNARGLEUGLN
4   GLNALALEUGLUMETGLYVALSERSERLEU
5   METALALEUVALTHRTHRASPTRPARGCYS
6   TYRGLYTYRMETGLUARGHISILEASNGLU
7   ILEARGTHRALAVALASPLYSVALGLULEU
8   PHELEULYSGLUTYRLEUHISPHEVALLYS
9   GLYALAVALALAASNALAALACYSLEUPRO
10   GLULEUILELEUHISASNLYSMETLYSARG
11   GLULEUGLNARGVALGLUASPSERHISGLN
12   ILELEUSERGLNTHRSERHISASPLEUASN
13   GLUCYSSERTRPSERLEUASNILELEUALA
14   ILEASNLYSPROGLNASNLYSCYSASPASP
15   LEUASPARGPHEVALMETVALALALYSTHR
16   VALPROASPASPALALYSGLNLEUTHRTHR
17   THRILEASNTHRASNALAGLUALALEUPHE
18   ARGPROGLYPROGLYSER

Samples:

sample_NC: HR5554A, [U-100% 13C; U-100% 15N], 0.56 mM; H2O 95 mM; D2O 5 mM

sample_NC5: HR5554A, [U-5% 13C; U-100% 15N], 0.56 mM; H2O 95 mM; D2O 5 mM

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQC 28 ctsample_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
2D 1H-13C HSQC 28a ctsample_NCisotropicsample_conditions_1
2D 1H-13C HSQC 42 ctsample_NCisotropicsample_conditions_1
2D 1H-13C HSQC 42a ctsample_NCisotropicsample_conditions_1
3D CC(CO)NH TOCSYsample_NCisotropicsample_conditions_1
3D HBHA(CO)NHsample_NCisotropicsample_conditions_1
3D HNCAsample_NCisotropicsample_conditions_1
3D HN(CO)CAsample_NCisotropicsample_conditions_1
3D (H)CCH TOCSYsample_NCisotropicsample_conditions_1
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-15N HSQC T1sample_NCisotropicsample_conditions_1
2D 1H-15N HSQC T2sample_NCisotropicsample_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

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAF85371 BAI46717
GB AAA98770 AAB53696 AAH40207 ABM82651 ABM85828
REF NP_001135865 NP_001257962 NP_006394 XP_001088846 XP_001089291
SP Q14511

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