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 17092

Title: NMR solution structure of the N-terminal domain of DNA-binding protein SATB1 from Homo sapiens: Northeast Structural Genomics Target HR4435B(179-250)

Authors: Swapna, G. V. T.; Montelione, Alexander; Shastry, Ritu; Ciccosanti, Colleen; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano

Citation: Swapna, G. V. T.; Montelione, Alexander; Shastry, Ritu; Ciccosanti, Colleen; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano. "NMR solution structure of the N-terminal domain of DNA-binding protein SATB1 from Homo sapiens: Northeast Structural Genomics Target HR4435B(179-250)"  Not known ., .-..

Assembly members:
entity, polymer, 83 residues, 9699.189 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):
entity: MGHHHHHHSHMLPPEQWSHT TVRNALKDLLKDMNQSSLAK ECPLSQSMISSIVNSTYYAN VSAAKCQEFGRWYKHFKKTK DMM

Data typeCount
13C chemical shifts326
15N chemical shifts79
1H chemical shifts519

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SATB11

Entities:

Entity 1, SATB1 83 residues - 9699.189 Da.

Consists of an N-terminal tag MGHHHHHHSH.

1   METGLYHISHISHISHISHISHISSERHIS
2   METLEUPROPROGLUGLNTRPSERHISTHR
3   THRVALARGASNALALEULYSASPLEULEU
4   LYSASPMETASNGLNSERSERLEUALALYS
5   GLUCYSPROLEUSERGLNSERMETILESER
6   SERILEVALASNSERTHRTYRTYRALAASN
7   VALSERALAALALYSCYSGLNGLUPHEGLY
8   ARGTRPTYRLYSHISPHELYSLYSTHRLYS
9   ASPMETMET

Samples:

HR4435B.009: HR4435B, [U-100% 13C; U-100% 15N], 1.08 ± 0.2 mM; DTT 10 mM; DSS 50 mM; NaN3 0.02%; NaCl 100 mM; CaCl2 5 mM; MES 20 mM; H2O 90%; D2O 10%

HR4435B.009_conditions: ionic strength: 105 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCHR4435B.009isotropicHR4435B.009_conditions
2D 1H-13C HSQCHR4435B.009isotropicHR4435B.009_conditions
3D CBCA(CO)NHHR4435B.009isotropicHR4435B.009_conditions
3D HNCACBHR4435B.009isotropicHR4435B.009_conditions
3D HBHA(CO)NHHR4435B.009isotropicHR4435B.009_conditions
3D HNCOHR4435B.009isotropicHR4435B.009_conditions
3D HCCH-TOCSYHR4435B.009isotropicHR4435B.009_conditions
3D 1H-15N NOESYHR4435B.009isotropicHR4435B.009_conditions
3D 1H-13C NOESYHR4435B.009isotropicHR4435B.009_conditions
2D 1H-15N HSQCHR4435B.009isotropicHR4435B.009_conditions
2D 1H-13C HSQCHR4435B.009isotropicHR4435B.009_conditions

Software:

AutoAssign v2.2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - chemical shift assignment, structure solution

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution

CNS v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAC40427 BAD92998 BAE34542 BAG10908 BAG54463
EMBL CAJ18578
GB AAA17372 AAA60304 AAH01744 AAH11132 AAH85814
REF NP_001012129 NP_001093671 NP_001095510 NP_001124482 NP_001157102
SP Q01826 Q60611
TPG DAA32913