: / Protein of unknown function DUF903 / Bacterial protein of unknown function (DUF903) / SH3 type barrels. - #100 / LSM domain superfamily / SH3 type barrels. / Prokaryotic membrane lipoprotein lipid attachment site profile. / Roll / Mainly Beta Similarity search - Domain/homology
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelength
Relative weight: 1
NMR spectrometer
Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz
-
Processing
NMR software
Name
Version
Developer
Classification
CNSSOLVE
1.1
BRUNGER, et. al.
refinement
X-PLOR
2.11.2
CLOREet. al.
refinement
PROCHECK NMR
3.51
LASKOWSKI, MACARTHUR
refinement
MolProbity
3.01
LOVELL, RICHARDSONET. AL.
refinement
QUEEN
1.1
NABUURS, VUISTER
refinement
PSVS
1.3
BHATTACHARYA, MONTELIONE
refinement
AutoStructure
2.1.1
structuresolution
NMRPipe
structuresolution
Sparky
structuresolution
MOLMOL
structuresolution
CNS
structuresolution
PROCHECK
structuresolution
XPLOR-NIH
structuresolution
DIANA
structuresolution
QUEEN
1.1
structuresolution
Refinement
Method: simulated annealing / Software ordinal: 1 Details: NOESY ASSIGNMENT MADE WITH ITERATIVE METHOD USING CNS, HYPER (DIHEDRAL) AND DYANA FOLLOWED BY NIH- XPLOR FOR SIMMULATED ANNEALING MD. CONVERGED STRUCTURES WERE FURTHER MINIMIZED USING CNS IN ...Details: NOESY ASSIGNMENT MADE WITH ITERATIVE METHOD USING CNS, HYPER (DIHEDRAL) AND DYANA FOLLOWED BY NIH- XPLOR FOR SIMMULATED ANNEALING MD. CONVERGED STRUCTURES WERE FURTHER MINIMIZED USING CNS IN EXPLICIT H2O SHELL (NILGES PROTOCOL). FULL LENGTH SEQUENCE WAS CARRIED THROUGH THE REFINEMENT PROTOCOL. COORDINATES FROM DISORDERED REGIONS, INCLUDING HEXHIS TAG, WERE NOT REPORTED. STRUCTURE IS BASED ON 439 CONSTRAINTS (216 LONG RANGE), 43 DIHEDRAL AND 20 H-BOND.
NMR representative
Selection criteria: lowest energy
NMR ensemble
Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20
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