BMRB Entry 18166

Title:
Solution NMR Structure of Stress-induced-phosphoprotein 1 STI1 from Homo sapiens, Northeast Structural Genomics Consortium Target HR4403E
Deposition date:
2011-12-28
Original release date:
2012-02-17
Authors:
Tang, Yuefeng; Liu, Gaohua; Hamilton, Keith; Ciccosanti, Colleen; Shastry, Ritu; Rost, Burkhard; Acton, Tom; Xiao, Rong; Everett, John; Montelione, Gaetano
Citation:

Citation: Tang, Yuefeng; Liu, Gaohua; Hamilton, Keith; Ciccosanti, Colleen; Shastry, Ritu; Rost, Burkhard; Acton, Tom; Xiao, Rong; Everett, John; Montelione, Gaetano. "Northeast Structural Genomics Consortium Target HR4403E"  To be published ., .-..

Assembly members:

Assembly members:
HR4403E, polymer, 133 residues, 15365.743 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: HR4403E-356-477-14.2

Data sets:
Data typeCount
13C chemical shifts434
15N chemical shifts141
1H chemical shifts909

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR4403E1

Entities:

Entity 1, HR4403E 133 residues - 15365.743 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METASNPROASPLEUALALEUMETVALLYS
3   ASNLYSGLYASNGLUCYSPHEGLNLYSGLY
4   ASPTYRPROGLNALAMETLYSHISTYRTHR
5   GLUALAILELYSARGASNPROLYSASPALA
6   LYSLEUTYRSERASNARGALAALACYSTYR
7   THRLYSLEULEUGLUPHEGLNLEUALALEU
8   LYSASPCYSGLUGLUCYSILEGLNLEUGLU
9   PROTHRPHEILELYSGLYTYRTHRARGLYS
10   ALAALAALALEUGLUALAMETLYSASPTYR
11   THRLYSALAMETASPVALTYRGLNLYSALA
12   LEUASPLEUASPSERSERCYSLYSGLUALA
13   ALAASPGLYTYRGLNARGCYSMETMETALA
14   GLNTYRASN

Samples:

sample_1: HR4403E, [U-100% 13C; U-100% 15N], 0.807 mM; H2O 95%; D2O 5%

sample_2: HR4403E, [U-5% 13C; U-100% 15N], 0.763 mM; H2O 95%; D2O 5%

sample_3: HR4403E, [U-100% 13C; U-100% 15N], 0.4 mM; D2O 100%

sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C arom NOESYsample_1isotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_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

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

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

PALES, PALES (Zweckstetter, Bax) - geometry optimization

REDCAT, Valafar, Prestegard - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB

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