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 16348

Title: SOLUTION STRUCTURE OF DEAD RINGER-LIKE PROTEIN 1 (AT-RICH INTERACTIVE DOMAIN-CONTAINING PROTEIN 3A) FROM HOMO SAPIENS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET HR4394C

Authors: Liu, Gaohua; Wang, Dongyan; NWOSU, CHIOMA; OWENS, LEAH; Xiao, Rong; Liu, Jinfeng; Baran, Micheal; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation: Liu, Gaohua; Xiao, Rong; Montelione, Gaetano. "SOLUTION STRUCTURE OF DEAD RINGER-LIKE PROTEIN 1 (AT-RICH INTERACTIVE DOMAIN-CONTAINING PROTEIN 3A) FROM HOMO SAPIENS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET HR4394C"  Not known ., .-..

Assembly members:
HR4394C, polymer, 145 residues, 17162.803 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):
HR4394C: MGHHHHHHSHMPDHGDWTYE EQFKQLYELDGDPKRKEFLD DLFSFMQKRGTPVNRIPIMA KQVLDLFMLYVLVTEKGGLV EVINKKLWREITKGLNLPTS ITSAAFTLRTQYMKYLYPYE CEKRGLSNPNELQAAIDSNR REGRR

Data sets:
Data typeCount
13C chemical shifts587
15N chemical shifts134
1H chemical shifts990

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR4394C1

Entities:

Entity 1, HR4394C 145 residues - 17162.803 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METPROASPHISGLYASPTRPTHRTYRGLU
3   GLUGLNPHELYSGLNLEUTYRGLULEUASP
4   GLYASPPROLYSARGLYSGLUPHELEUASP
5   ASPLEUPHESERPHEMETGLNLYSARGGLY
6   THRPROVALASNARGILEPROILEMETALA
7   LYSGLNVALLEUASPLEUPHEMETLEUTYR
8   VALLEUVALTHRGLULYSGLYGLYLEUVAL
9   GLUVALILEASNLYSLYSLEUTRPARGGLU
10   ILETHRLYSGLYLEUASNLEUPROTHRSER
11   ILETHRSERALAALAPHETHRLEUARGTHR
12   GLNTYRMETLYSTYRLEUTYRPROTYRGLU
13   CYSGLULYSARGGLYLEUSERASNPROASN
14   GLULEUGLNALAALAILEASPSERASNARG
15   ARGGLUGLYARGARG

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.92 mM; NACL 200 mM

sample_2: entity, [U-100% 13C; U-100% 15N], 0.92 mM; NACL 200 mM

sample_3: entity, [U-10% 13C; U-100% 15N], 0.95 mM; NACL 200 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-13C-15N simutaneous NOESYsample_1isotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoStruct v1.2, Huang, Tejero, Powers and Montelione - data analysis, refinement

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

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

XEASY v1.3, Bartels et al. - chemical shift assignment, data analysis, peak picking

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

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB AAC28918 AAC32888 AAC69994 AAH33163 AAH60828
REF NP_001192624 NP_005215 XP_001374625 XP_002828411 XP_003460928
SP Q99856
TPG DAA27511