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Biological Magnetic Resonance Data Bank


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BMRB Entry 18352

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18352
MolProbity Validation Chart

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Title: Solution NMR Structure of CASP8-associated protein 2 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8150A

Deposition date: 2012-03-27 Original release date: 2012-04-30

Authors: Pulavarti, Surya V.S.R.K; Sathyamoorthy, Bharathwaj; Eletsky, Alex; Sukumaran, Dinesh; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Guy; Szyperski, Thomas

Citation: Pulavarti, Surya V.S.R.K; Sathyamoorthy, Bharathwaj; Eletsky, Alex; Sukumaran, Dinesh; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Guy; Szyperski, Thomas. "Solution NMR Structure of CASP8-associated protein 2 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8150A"  To be published ., .-..

Assembly members:
HR8150A, polymer, 70 residues, 8267.851 Da.

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

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

Entity Sequences (FASTA):
HR8150A: SHMKNVIKKKGEIIILWTRN DDRVILLECQKRGPSSKTFA YLAAKLDKNPNQVSERFQQL MKLFEKSKCR

Data sets:
Data typeCount
13C chemical shifts308
15N chemical shifts70
1H chemical shifts505

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HR8150A1

Entities:

Entity 1, HR8150A 70 residues - 8267.851 Da.

1   SERHISMETLYSASNVALILELYSLYSLYS
2   GLYGLUILEILEILELEUTRPTHRARGASN
3   ASPASPARGVALILELEULEUGLUCYSGLN
4   LYSARGGLYPROSERSERLYSTHRPHEALA
5   TYRLEUALAALALYSLEUASPLYSASNPRO
6   ASNGLNVALSERGLUARGPHEGLNGLNLEU
7   METLYSLEUPHEGLULYSSERLYSCYSARG

Samples:

sample_1: HR8150A.006, [U-100% 13C; U-100% 15N], 0.75 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; H2O 90%

sample_2: HR8150A.006, [U-5% 13C; U-100% 15N], 0.17 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; H2O 90%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
(4,3)D GFT-HNCACBCAsample_1isotropicsample_conditions_1
(4,3)D GFT-CBCACA(CO)NHNsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSY-alisample_1isotropicsample_conditions_1
3D HCCH-COSY-arosample_1isotropicsample_conditions_1
2D 1H-15N HSQC (Wide range)sample_1isotropicsample_conditions_1
1D Protonsample_1isotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-13C(CT-27ms) HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C(CT-16ms) HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C(CT-28ms) HSQC aliphaticsample_2isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement,structure solution,geometry optimization

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

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - refinement

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

PROSA, Guntert - processing

CSI, (CSI) Wishart and Sykes - Secondary structure information

VNMRJ, Varian - collection

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

PSVS, Bhattacharya, Montelione - structure validation

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
DBJ BAA92067 BAA92553 BAG10450
GB AAD45157 AAD45537 AAF03367 AAH42577 AAI32829
REF NP_001131139 NP_001131140 NP_036247 XP_001159871 XP_001159913
SP Q9UKL3

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