BMRB Entry 7102

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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/BMR7102
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein design
Deposition date:
2006-05-05
Original release date:
2007-04-16
Authors:
Reichow, S.
Citation:

Citation: Dantas, G.; Corrent, C.; Reichow, S.; Havranek, J.; Eletr, Z.; Isern, N.; Kuhlman, B.; Varani, G.; Merritt, E.; Baker, D.. "High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein design"  J. Mol. Biol. 366, 1209-1221 (2007).
PubMed: 17196978

Assembly members:

Assembly members:
Designed Protein AYE, polymer, 78 residues, Formula weight is not available

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Designed Protein AYE: HHHHHHGSKTIFVIVPTNEE QVAFLEALAKQDELNFDWQN PPTEPGQPVVILIPSDMVEW FLEMLKAKGIPFTVYVEE

Data sets:
Data typeCount
13C chemical shifts234
15N chemical shifts73
1H chemical shifts542

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1DESIGNED PROTEIN AYE, chain 11
2DESIGNED PROTEIN AYE, chain 21

Entities:

Entity 1, DESIGNED PROTEIN AYE, chain 1 78 residues - Formula weight is not available

1   HISHISHISHISHISHISGLYSERLYSTHR
2   ILEPHEVALILEVALPROTHRASNGLUGLU
3   GLNVALALAPHELEUGLUALALEUALALYS
4   GLNASPGLULEUASNPHEASPTRPGLNASN
5   PROPROTHRGLUPROGLYGLNPROVALVAL
6   ILELEUILEPROSERASPMETVALGLUTRP
7   PHELEUGLUMETLEULYSALALYSGLYILE
8   PROPHETHRVALTYRVALGLUGLU

Samples:

sample_1: Designed Protein AYE 1 mM; phosphate buffer 50 mM; KCl 100 mM; H2O 90%; D2O 10%

sample_2: Designed Protein AYE 1 mM; phosphate buffer 50 mM; KCl 100 mM; D2O 100%

sample_3: Designed Protein AYE, [U-15N], 1 mM; phosphate buffer 50 mM; KCl 100 mM; H2O 90%; D2O 10%

sample_4: Designed Protein AYE, [U-13C; U-15N], 1 mM; phosphate buffer 50 mM; KCl 100 mM; H2O 90%; D2O 10%

sample_cond_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D NOESYnot availablenot availablesample_cond_1
3D 13C-separated NOESYnot availablenot availablesample_cond_1
3D 15N-separated NOESYnot availablenot availablesample_cond_1
3D 13C-filtered NOESYnot availablenot availablesample_cond_1

Software:

CYANA v2.1 - refinement, structure solution

TALOS - data analysis

NMRPipe v2.3 - processing

SPARKY v3.112 - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB

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CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks