BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 15437

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15437
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Title: Assignment, structure, and dynamics of de novo designed protein S836   PubMed: 19636868

Deposition date: 2007-08-16 Original release date: 2008-01-28

Authors: Go, Abigail; Kim, Seho; Baum, Jean; Hecht, Michael

Citation: Go, Abigail; Kim, Seho; Hecht, Michael; Baum, Jean. "NMR assignment of S836: a de novo protein from a designed superfamily"  Biomol. NMR Assignments 1, 213-215 (2007).

Assembly members:
S836, polymer, 102 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

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

Entity Sequences (FASTA):
S836: MYGKLNDLLEDLQEVLKHVN QHWQGGQKNMNKVDHHLQNV IEDIHDFMQGGGSGGKLQEM MKEFQQVLDEIKQQLQGGDN SLHNVHENIKEIFHHLEELV HR

Data sets:
Data typeCount
13C chemical shifts414
15N chemical shifts121
1H chemical shifts719
heteronuclear NOE values198
T1 relaxation values198
T2 relaxation values198

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1S836 monomer1

Entities:

Entity 1, S836 monomer 102 residues - Formula weight is not available

1   METTYRGLYLYSLEUASNASPLEULEUGLU
2   ASPLEUGLNGLUVALLEULYSHISVALASN
3   GLNHISTRPGLNGLYGLYGLNLYSASNMET
4   ASNLYSVALASPHISHISLEUGLNASNVAL
5   ILEGLUASPILEHISASPPHEMETGLNGLY
6   GLYGLYSERGLYGLYLYSLEUGLNGLUMET
7   METLYSGLUPHEGLNGLNVALLEUASPGLU
8   ILELYSGLNGLNLEUGLNGLYGLYASPASN
9   SERLEUHISASNVALHISGLUASNILELYS
10   GLUILEPHEHISHISLEUGLUGLULEUVAL
11   HISARG

Samples:

sample_1: S836, [U-15N], 1 – 2 mM; D2O, [U-2H], 10%; acetic acid - sodium acetate 50 mM

sample_2: S836, [U-13C; U-15N], 2 mM; D2O, [U-2H], 10%; acetic acid - sodium acetate, [U-13C], 50 mM

sample_conditions_1: pH: 4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D (HCA)CO(CA)NHsample_2isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

AQUA, Rullmann, Doreleijers and Kaptein - validation

ProcheckNMR, Laskowski and MacArthur - validation

Molmol, Koradi, Billeter and Wuthrich - structural visualization

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB

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