[gmx-users] Re:mdrun_problem

Erik Marklund erikm at xray.bmc.uu.se
Tue Aug 7 08:58:02 CEST 2007


As has been suggested already, this is probably related to PBC, and  
is in fact not a problem at all. Have you checked whether applying  
the PBC puts the protein and peptide back together? Try out trjconv - 
ur compact on your system and have a look at the output structure, or  
run g_mindist to see whether they really drift apart.

/Erik

6 aug 2007 kl. 23.18 skrev pkmukher:

> Hi users,
>
> I am having a problem during the running of the mdrun
> program on my prepared system.I have a system containing a
> protein/peptide complex. i have prepared the protein using
> the pdb2gmx utility and the peptide using the PRODRG
> utility. I have then included the ligand .itp file into the
> protein top file. when i run grommpp followed by mdrun I see
> a translation of the peptide/protein complex  in the output
> structure file(also confirmed by looking at the actual pdb
> file coordinates). Tranlation of a system to a new point
> (e.g. center of solvent box) is a normal procedure and would
> not effect calculations because the position of the peptide
> and the protein within the complex would remain the same
> relative to each other. However in this case i find that a
> translation of the X coordinates has been performed for the
> protein atoms while a translation of the Y and Z coordinates
> has been performed for the peptide. This results in the
> peptide moving outside of the binding site of the protein
> i.e. the protein and the peptide are not placed at the same
> place "relative to each other" as present in the input
> structure file.I have included portions of the input and the
> output structure files.
>
>
>
>
> In these files (given below)
>
> input file
>  atoms 1890-1895 - last five atoms of protein in the input
> file
>  atoms    1-10 - first ten atoms of the peptide in the input
> file
>
> output file
>
> atoms 1890-1895 - last five atoms of protein in the output
> file
> atoms 1896-1905 - first ten atoms of the peptide in the
> output file
>
> as an example
>
> this particular protein atom from the input file
> ATOM   1890  CD2 HIS A 181      17.104 -17.966  35.020  1.00
>
> gets translated to
>
> ATOM   1890  CD2 HIS A 181      57.476 -17.958  35.022  1.00
>
> NOTE: translation in X coordinates only
>
>
> while
>
> the first ligand atom from the input file
> HETATM    1  NAA DRG   182       3.259 -11.741 -15.248  1.00
>
>
> gets translated to
>
> ATOM   1896  NAA DRG B 182       3.259  41.631  44.612  1.00
>
>
> NOTE: translated in Y and Z coodinates only.
>
> thus the protein has been translated as [X,0,0]
> while the peptide has been translated by [0,Y,Z]
>
> The desired translation for protein is [X,Y,Z]
> and the desired translation for the ligand is [X,Y,Z].
>
> Could you kindly help me with your suggestions. Thanks in
> advance
>
> ####
> input structure
> ####
>
> ATOM   1890  CD2 HIS A 181      17.104 -17.966  35.020  1.00
>  0.00
> ATOM   1891  CE1 HIS A 181      15.979 -16.114  34.942  1.00
>  0.00
> ATOM   1892  NE2 HIS A 181      17.022 -16.732  34.381  1.00
>  0.00
> ATOM   1893  C   HIS A 181      15.328 -21.621  37.119  1.00
>  0.00
> ATOM   1894  O1  HIS A 181      14.341 -22.372  36.561  1.00
>  0.00
> ATOM   1895  O2  HIS A 181      15.818 -21.755  38.381  1.00
>  0.00
> TER
> HETATM    1  NAA DRG   182       3.259 -11.741 -15.248  1.00
> 20.00
> HETATM    2  HAA DRG   182       2.868 -11.170 -15.970  1.00
> 20.00
> HETATM    3  HAB DRG   182       4.140 -12.104 -15.551  1.00
> 20.00
> HETATM    4  HAC DRG   182       2.637 -12.498 -15.050  1.00
> 20.00
> HETATM    5  CAB DRG   182       3.456 -10.923 -14.017  1.00
> 20.00
> HETATM    6  CAC DRG   182       4.054 -11.797 -12.913  1.00
> 20.00
> HETATM    7  OAD DRG   182       3.478 -12.789 -12.512  1.00
> 20.00
> HETATM    8  N   DRG   182       5.208 -11.438 -12.418  1.00
> 20.00
> HETATM    9  HAD DRG   182       5.666 -10.619 -12.763  1.00
> 20.00
> HETATM   10  CA  DRG   182       5.843 -12.248 -11.340  1.00
> 20.00
>
> ####
> output structure
> ####
>
> ATOM   1890  CD2 HIS A 181      57.476 -17.958  35.022  1.00
>  0.00
> ATOM   1891  CE1 HIS A 181      56.353 -16.113  34.945  1.00
>  0.00
> ATOM   1892  NE2 HIS A 181      57.395 -16.742  34.389  1.00
>  0.00
> ATOM   1893  C   HIS A 181      55.696 -21.634  37.130  1.00
>  0.00
> ATOM   1894  O1  HIS A 181      54.730 -22.362  36.575  1.00
>  0.00
> ATOM   1895  O2  HIS A 181      56.185 -21.754  38.363  1.00
>  0.00
> ATOM   1896  NAA DRG B 182       3.259  41.631  44.612  1.00
>  0.00
> ATOM   1897  HAA DRG B 182       2.868  42.201  43.887  1.00
>  0.00
> ATOM   1898  HAB DRG B 182       4.140  41.267  44.306  1.00
>  0.00
> ATOM   1899  HAC DRG B 182       2.637  40.873  44.807  1.00
>  0.00
> ATOM   1900  CAB DRG B 182       3.456  42.447  45.837  1.00
>  0.00
> ATOM   1901  CAC DRG B 182       4.052  41.573  46.943  1.00
>  0.00
> ATOM   1902  OAD DRG B 182       3.475  40.579  47.344  1.00
>  0.00
> ATOM   1903  N   DRG B 182       5.210  41.933  47.440  1.00
>  0.00
> ATOM   1904  HAD DRG B 182       5.668  42.752  47.095  1.00
>  0.00
> ATOM   1905  CA  DRG B 182       5.844  41.127  48.515  1.00
>  0.00
>
>
> ####
> .mdp file
> ####
>
> cpp             = /usr/bin/cpp
> constraints     = none
> integrator      = cg
> nsteps          = 1
> emtol           = 100.0
> emstep          = 0.01
> nstcomm         =1
> ns_type         = grid
> morse           = no ; was given as yes in tutorial
> coulombtype     = shift
> vdw_type        = shift
> rlist           = 1.4
> rcoulomb        = 1.2
> rvdw            = 1.2
> rcoulomb_switch = 1.0
> rvdw_switch     = 1.0
> epsilon_r       = 6.0
>
>
>
>
>
>
> Prasenjit Kumar Mukherjee
> Graduate Student
> Department of Medicinal Chemistry
> School of Pharmacy
> University of Mississippi
> USA
>
> Cell   - 662 380 0146
> Office - 662 915 1286
>
>
>
>
>
>
>
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_______________________________________________
Erik Marklund, PhD student
Laboratory of Molecular Biophysics,
Dept. of Cell and Molecular Biology, Uppsala University.
Husargatan 3, Box 596,	75124 Uppsala, Sweden
phone:	+46 18 471 4537		fax: +46 18 511 755
erikm at xray.bmc.uu.se	http://xray.bmc.uu.se/molbiophys





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