[gmx-users] Re: a flat plane boundary condition

David spoel at xray.bmc.uu.se
Wed May 25 22:17:51 CEST 2005


On Wed, 2005-05-25 at 15:56 -0400, Beckett W Sterner wrote:
> Hi,
>   Thats looks great for fixing one end of the protein, but I also want to
> ensure that the rest of it is restricted to only half of space (the
> impenetrable plane boundary condition).  Or maybe I'm missing your
> meaning.  The constraint is important because as the protein exits the
> pore it should begin to fold but it shouldn't clump around the residue
> with fixed position.
> 
It's not clear to me what you want, or at least how you model the
protein coming out of the pore. Do you want to allow an ever increasing
(N-terminal) end to start folding in solution while you restrain the C-
terminal end?

> Thanks,
> Beckett
> 
> > You can freeze atoms in one, two or three dimensions. Check mdp options
> > on www.gromacs.org
> 
> 
> 
> 
> > On Wed, 2005-05-25 at 12:30 -0400, Beckett W Sterner wrote:
> > > Hi,
> > >   I'm interested in doing a simple simulation of how a protein folds as it
> > > slowly emerges from a pore through a cell membrane.  I unfortunately do
> > > not have a crystal structure for the pore, and would like to keep
> > > computational costs to a minimum, so I'm interested in running an MD
> > > simulation on the protein where one end is fixed to a flat plane with a 2d
> > > periodic boundary condition.  Is there a way to implement this in GROMACS,
> > > perhaps using a force field?
> 
> 
> 
> > You can freeze atoms in one, two or three dimensions. Check mdp options
> > on www.gromacs.org
> > >
> > > Thanks,
> > > Beckett
> > > _______________________________________________
> > > gmx-users mailing list
> > > gmx-users at gromacs.org
> > > http://www.gromacs.org/mailman/listinfo/gmx-users
> > > Please don't post (un)subscribe requests to the list. Use the
> > > www interface or send it to gmx-users-request at gromacs.org.
> > --
> > David.
> > ________________________________________________________________________
> > David van der Spoel, PhD, Assoc. Prof., Molecular Biophysics group,
> > Dept. of Cell and Molecular Biology, Uppsala University.
> > Husargatan 3, Box 596,          75124 Uppsala, Sweden
> > phone:  46 18 471 4205          fax: 46 18 511 755
> > spoel at xray.bmc.uu.se    spoel at gromacs.org   http://xray.bmc.uu.se/~spoel
> > ++++++++++++++++++++++++++++++++++++++++++++++++++++++++++++++++++++++++
> >
> >
> >
> > ------------------------------
> >
> > Message: 3
> > Date: Wed, 25 May 2005 13:55:46 -0400
> > From: Anthony Cruz <acb15885 at uprm.edu>
> > Subject: Re: [gmx-users] g_rms Fatal error: Error: Too many iterations
> > 	in	routine JACOBI
> > To: Discussion list for GROMACS users <gmx-users at gromacs.org>
> > Message-ID: <200505251355.46962.acb15885 at uprm.edu>
> > Content-Type: text/plain;  charset="iso-8859-1"
> >
> > I do the gmxcheck and this is the result:
> >
> > Checking file 1scn_bx_w_fullMD_mv.trr
> > trn version: GMX_trn_file (single precision)
> > Reading frame       0 time    0.000
> > # Atoms  110719
> > Last frame      10500 time 10500.001
> >
> >
> > Item        #frames Timestep (ps)
> > Step         10501    1
> > Time         10501    1
> > Lambda       10501    1
> > Coords       10501    1
> > Velocities   10501    1
> > Forces           0
> > Box          10501    1
> > Checking coordinate file 1scn_bx_w_CL_TPR4fullMD.tpr
> > Reading file 1scn_bx_w_CL_TPR4fullMD.tpr, VERSION 3.2.1 (single precision)
> > Reading file 1scn_bx_w_CL_TPR4fullMD.tpr, VERSION 3.2.1 (single precision)
> > 110719 atoms in file
> > coordinates found
> > box         found
> > velocities  found
> >
> > Kinetic energy: 411492 (kJ/mol)
> > Assuming the number of degrees of freedom to be Natoms * 3 or Natoms * 2,
> > the velocities correspond to a temperature of the system
> > of 297.996 K or 446.995 K respectively.
> >
> > Checking for atoms closer than 0.8 and not between 0.4 and 0.7,
> > relative to sum of Van der Waals distance:
> > WARNING: masses will be determined based on residue and atom names,
> >          this can deviate from the real mass of the atom type
> > In case you use free energy of solvation predictions:
> >
> > ++++++++ PLEASE CITE THE FOLLOWING REFERENCE ++++++++
> > D. Eisenberg and A. D. McLachlan
> > Solvation energy in protein folding and binding
> > Nature 319 (1986) pp. 199-203
> > -------- -------- --- Thank You --- -------- --------
> >
> > Opening library file /usr/local/gromacs/share/top/aminoacids.dat
> > Opening library file /usr/local/gromacs/share/top/atommass.dat
> > Opening library file /usr/local/gromacs/share/top/vdwradii.dat
> > Opening library file /usr/local/gromacs/share/top/dgsolv.dat
> > #Entries in atommass.dat: 82 vdwradii.dat: 26 dgsolv.dat: 7
> > atom# name  residue r_vdw  atom# name  residue r_vdw  distance
> >    40   CB  PRO   5 0.15      42   CD  PRO   5 0.15   0.2332
> >    50  CD1  TYR   6 0.15      58   CZ  TYR   6 0.15   0.2369
> >    52  CD2  TYR   6 0.15      58   CZ  TYR   6 0.15   0.2358
> >    78   CA  PRO   9 0.15      80   CG  PRO   9 0.15   0.2383
> >    87   CB  LEU  10 0.15      91    C  LEU  10 0.15   0.2399
> >   149    C  VAL  16 0.15     153   CA  GLN  17 0.15   0.2398
> >   190   CG  PHE  21 0.15     195  CE1  PHE  21 0.15   0.2395
> >   191  CD1  PHE  21 0.15     193  CD2  PHE  21 0.15   0.2393
> >   193  CD2  PHE  21 0.15     199   CZ  PHE  21 0.15   0.2369
> >   244    C  VAL  26 0.15     248   CA LYSH  27 0.15   0.2371
> >   277  CG1  VAL  30 0.15     278  CG2  VAL  30 0.15   0.2398
> >   302   CB  THR  33 0.15     306    C  THR  33 0.15   0.2383
> >   352   CG HISB  39 0.15     355  CE1 HISB  39 0.15   0.2174
> >   354  CD2 HISB  39 0.15     355  CE1 HISB  39 0.15   0.2169
> >   361   CA  PRO  40 0.15     364   CD  PRO  40 0.15   0.2395
> >   362   CB  PRO  40 0.15     364   CD  PRO  40 0.15   0.2387
> >   383    C  LEU  42 0.15     387   CA  ASN  43 0.15   0.2391
> >   440   CG  PHE  50 0.15     447  CE2  PHE  50 0.15   0.2371
> >   441  CD1  PHE  50 0.15     449   CZ  PHE  50 0.15   0.2331
> >   443  CD2  PHE  50 0.15     449   CZ  PHE  50 0.15   0.2371
> >   459    C  VAL  51 0.15     463   CA  ALA  52 0.15   0.2376
> >   492   CG  TYR  56 0.15     497  CE1  TYR  56 0.15   0.2334
> >   492   CG  TYR  56 0.15     499  CE2  TYR  56 0.15   0.2398
> >   497  CE1  TYR  56 0.15     499  CE2  TYR  56 0.15   0.2375
> >   558   CA HISA  63 0.15     560   CG HISA  63 0.15   0.2398
> >   560   CG HISA  63 0.15     564  CE1 HISA  63 0.15   0.212
> >   563  CD2 HISA  63 0.15     564  CE1 HISA  63 0.15   0.2126
> >   586   CG HISB  66 0.15     589  CE1 HISB  66 0.15   0.2163
> >   588  CD2 HISB  66 0.15     589  CE1 HISB  66 0.15   0.2109
> >   692    C  GLY  79 0.15     696   CA  VAL  80 0.15   0.2391
> >   698  CG1  VAL  80 0.15     699  CG2  VAL  80 0.15   0.2384
> >   732   CB  PRO  85 0.15     734   CD  PRO  85 0.15   0.2341
> >   751    C  VAL  87 0.15     755   CA  SER  88 0.15   0.2397
> >   775  CD1  TYR  90 0.15     783   CZ  TYR  90 0.15   0.2391
> >   777  CD2  TYR  90 0.15     783   CZ  TYR  90 0.15   0.2398
> >   817   CA  VAL  94 0.15     819  CG1  VAL  94 0.15   0.2397
> >   890  CD1  TYR 103 0.15     892  CD2  TYR 103 0.15   0.2384
> >   894  CE1  TYR 103 0.15     896  CE2  TYR 103 0.15   0.2346
> >   929  CG1  VAL 107 0.15     930  CG2  VAL 107 0.15   0.2398
> >   969   CG  TRP 112 0.15     975  CE2  TRP 112 0.15   0.2231
> >   970  CD1  TRP 112 0.15     972  CD2  TRP 112 0.15   0.2171
> >   970  CD1  TRP 112 0.15     975  CE2  TRP 112 0.15   0.2157
> >   975  CE2  TRP 112 0.15     976  CE3  TRP 112 0.15   0.2367
> >   978  CZ2  TRP 112 0.15     980  CZ3  TRP 112 0.15   0.2378
> >  1079    C  MET 123 0.15    1083   CA  SER 124 0.15   0.2396
> >  1094  CD1  LEU 125 0.15    1095  CD2  LEU 125 0.15   0.239
> >  1216    C  ASN 140 0.15    1220   CA  ALA 141 0.15   0.2389
> >  1228   CG  TYR 142 0.15    1233  CE1  TYR 142 0.15   0.2379
> >  1229  CD1  TYR 142 0.15    1231  CD2  TYR 142 0.15   0.2377
> >  1233  CE1  TYR 142 0.15    1235  CE2  TYR 142 0.15   0.2356
> >  1251   CB  ARG 144 0.15    1263    C  ARG 144 0.15   0.2347
> >  1347    C  GLY 156 0.15    1351   CA  ASN 157 0.15   0.2398
> >  1428   CG  TYR 166 0.15    1433  CE1  TYR 166 0.15   0.238
> >  1428   CG  TYR 166 0.15    1435  CE2  TYR 166 0.15   0.2363
> >  1443   CA  PRO 167 0.15    1446   CD  PRO 167 0.15   0.2391
> >  1473  CD1  TYR 170 0.15    1475  CD2  TYR 170 0.15   0.237
> >  1473  CD1  TYR 170 0.15    1481   CZ  TYR 170 0.15   0.2383
> >  1477  CE1  TYR 170 0.15    1479  CE2  TYR 170 0.15   0.2392
> >  1530  CG1  VAL 176 0.15    1531  CG2  VAL 176 0.15   0.2373
> >  1635   CG  PHE 188 0.15    1640  CE1  PHE 188 0.15   0.2336
> >  1635   CG  PHE 188 0.15    1642  CE2  PHE 188 0.15   0.2393
> >  1640  CE1  PHE 188 0.15    1642  CE2  PHE 188 0.15   0.2399
> >  1686   CB  GLU 194 0.15    1691    C  GLU 194 0.15   0.2396
> >  1698  CD1  LEU 195 0.15    1699  CD2  LEU 195 0.15   0.2293
> >  1736   CA  PRO 200 0.15    1738   CG  PRO 200 0.15   0.2346
> >  1762  CG1  VAL 204 0.15    1763  CG2  VAL 204 0.15   0.2344
> >  1771  CD1  TYR 205 0.15    1773  CD2  TYR 205 0.15   0.2366
> >  1775  CE1  TYR 205 0.15    1777  CE2  TYR 205 0.15   0.2391
> >  1806  CD1  TYR 208 0.15    1808  CD2  TYR 208 0.15   0.2383
> >  1810  CE1  TYR 208 0.15    1812  CE2  TYR 208 0.15   0.2356
> >  1859   CG  TYR 213 0.15    1864  CE1  TYR 213 0.15   0.2375
> >  1860  CD1  TYR 213 0.15    1862  CD2  TYR 213 0.15   0.24
> >  1862  CD2  TYR 213 0.15    1868   CZ  TYR 213 0.15   0.2396
> >  1864  CE1  TYR 213 0.15    1866  CE2  TYR 213 0.15   0.2366
> >  1954   CA  PRO 224 0.15    1957   CD  PRO 224 0.15   0.2351
> >  1964   CG HISA 225 0.15    1968  CE1 HISA 225 0.15   0.2137
> >  1967  CD2 HISA 225 0.15    1968  CE1 HISA 225 0.15   0.2127
> >  2012   CB  LEU 232 0.15    2014  CD1  LEU 232 0.15   0.2396
> >  2032  CD1  LEU 234 0.15    2033  CD2  LEU 234 0.15   0.2395
> >  2063  CD2 HISB 237 0.15    2064  CE1 HISB 237 0.15   0.2173
> >  2070   CA  PRO 238 0.15    2072   CG  PRO 238 0.15   0.2387
> >  2236   CG  TYR 255 0.15    2243  CE2  TYR 255 0.15   0.2388
> >  2241  CE1  TYR 255 0.15    2243  CE2  TYR 255 0.15   0.237
> >  2284   CG  PHE 260 0.15    2289  CE1  PHE 260 0.15   0.2363
> >  2285  CD1  PHE 260 0.15    2287  CD2  PHE 260 0.15   0.2389
> >  2287  CD2  PHE 260 0.15    2293   CZ  PHE 260 0.15   0.2339
> >  2301   CG  TYR 261 0.15    2308  CE2  TYR 261 0.15   0.2389
> >  2302  CD1  TYR 261 0.15    2310   CZ  TYR 261 0.15   0.2358
> >  2304  CD2  TYR 261 0.15    2310   CZ  TYR 261 0.15   0.2395
> >  2319   CG  TYR 262 0.15    2326  CE2  TYR 262 0.15   0.2376
> >  2324  CE1  TYR 262 0.15    2326  CE2  TYR 262 0.15   0.238
> >
> > Atoms outside box ( 10.4513 10.4513 10.4513 ):
> > (These may occur often and are normally not a problem)
> > atom# name  residue r_vdw  coordinate
> >  2488   OW  SOL 293 0.105 -0.034   2.79   4.15
> >  2491   OW  SOL 294 0.105 -0.031   5.54   9.37
> >  2494   OW  SOL 295 0.105 -0.024   3.92   10.1
> >  2497   OW  SOL 296 0.105  -0.02   5.24   10.3
> >  2500   OW  SOL 297 0.105 -0.018   4.16   8.09
> >  2501  HW1  SOL 297 0.04  -0.027   4.18   8.19
> >  2503   OW  SOL 298 0.105 -0.018   6.61   5.17
> >  2506   OW  SOL 299 0.105 -0.016   1.37    7.5
> >  2509   OW  SOL 300 0.105 -0.015   2.23   9.93
> >  2511  HW2  SOL 300 0.04  -0.048   2.29     10
> > (maybe more)-bash-2.05b$ g_rms -f 1scn_bx_w_fullMD_mv.trr -s
> > 1scn_bx_w_CL_TPR4fullMD.tpr -o
> >                          :-)  G  R  O  M  A  C  S  (-:
> >
> >                                Grunge ROck MAChoS
> >
> >                             :-)  VERSION 3.2.1  (-:
> >
> >
> >       Written by David van der Spoel, Erik Lindahl, Berk Hess, and others.
> >        Copyright (c) 1991-2000, University of Groningen, The Netherlands.
> >              Copyright (c) 2001-2004, The GROMACS development team,
> >             check out http://www.gromacs.org for more information.
> >
> >          This program is free software; you can redistribute it and/or
> >           modify it under the terms of the GNU General Public License
> >          as published by the Free Software Foundation; either version 2
> >              of the License, or (at your option) any later version.
> >
> >                                 :-)  g_rms  (-:
> >
> > Option     Filename  Type         Description
> > ------------------------------------------------------------
> >   -s 1scn_bx_w_CL_TPR4fullMD.tpr  Input        Structure+mass(db): tpr tpb
> >                                    tpa gro g96 pdb xml
> >   -f 1scn_bx_w_fullMD_mv.trr  Input        Generic trajectory: xtc trr trj
> >                                    gro g96 pdb
> >  -f2       traj.xtc  Input, Opt.  Generic trajectory: xtc trr trj gro g96 pdb
> >   -n      index.ndx  Input, Opt.  Index file
> >   -o       rmsd.xvg  Output       xvgr/xmgr file
> > -mir    rmsdmir.xvg  Output, Opt. xvgr/xmgr file
> >   -a      avgrp.xvg  Output, Opt. xvgr/xmgr file
> > -dist rmsd-dist.xvg  Output, Opt. xvgr/xmgr file
> >   -m       rmsd.xpm  Output, Opt. X PixMap compatible matrix file
> > -bin       rmsd.dat  Output, Opt. Generic data file
> >  -bm       bond.xpm  Output, Opt. X PixMap compatible matrix file
> >
> >       Option   Type  Value  Description
> > ------------------------------------------------------
> >       -[no]h   bool     no  Print help info and quit
> >       -[no]X   bool     no  Use dialog box GUI to edit command line options
> >        -nice    int     19  Set the nicelevel
> >           -b   time     -1  First frame (ps) to read from trajectory
> >           -e   time     -1  Last frame (ps) to read from trajectory
> >          -dt   time     -1  Only use frame when t MOD dt = first time (ps)
> >          -tu   enum     ps  Time unit: ps, fs, ns, us, ms, s, m or h
> >       -[no]w   bool     no  View output xvg, xpm, eps and pdb files
> >        -what   enum   rmsd  Structural difference measure: rmsd, rho or rhosc
> >     -[no]pbc   bool    yes  PBC check
> >         -fit   enum rot+trans  Fit to reference structure: rot+trans,
> >                             translation or none
> >        -prev    int      0  Compare with previous frame
> >   -[no]split   bool     no  Split graph where time is zero
> >        -skip    int      1  Only write every nr-th frame to matrix
> >       -skip2    int      1  Only write every nr-th frame to matrix
> >         -max   real     -1  Maximum level in comparison matrix
> >         -min   real     -1  Minimum level in comparison matrix
> >        -bmax   real     -1  Maximum level in bond angle matrix
> >        -bmin   real     -1  Minimum level in bond angle matrix
> >     -nlevels    int     80  Number of levels in the matrices
> >
> > Reading file 1scn_bx_w_CL_TPR4fullMD.tpr, VERSION 3.2.1 (single precision)
> > Reading file 1scn_bx_w_CL_TPR4fullMD.tpr, VERSION 3.2.1 (single precision)
> > Select group for least squares fit
> > Opening library file /usr/local/gromacs/share/top/aminoacids.dat
> > Group     0 (      System) has 110719 elements
> > Group     1 (     Protein) has  2433 elements
> > Group     2 (   Protein-H) has  1920 elements
> > Group     3 (     C-alpha) has   274 elements
> > Group     4 (    Backbone) has   822 elements
> > Group     5 (   MainChain) has  1097 elements
> > Group     6 (MainChain+Cb) has  1336 elements
> > Group     7 ( MainChain+H) has  1364 elements
> > Group     8 (   SideChain) has  1069 elements
> > Group     9 ( SideChain-H) has   823 elements
> > Group    10 ( Prot-Masses) has  2433 elements
> > Group    11 ( Non-Protein) has 108286 elements
> > Group    12 (          CL) has     4 elements
> > Group    13 (         HOH) has   423 elements
> > Group    14 (         SOL) has 107856 elements
> > Group    15 (          CA) has     2 elements
> > Group    16 (          NA) has     1 elements
> > Group    17 (       Other) has 108286 elements
> > Select a group: 1
> > Selected 1: 'Protein'
> > How many groups do you want to compare ? 1
> > OK. I will compare 1 group
> > Select group for RMSD calculation
> > Opening library file /usr/local/gromacs/share/top/aminoacids.dat
> > Group     0 (      System) has 110719 elements
> > Group     1 (     Protein) has  2433 elements
> > Group     2 (   Protein-H) has  1920 elements
> > Group     3 (     C-alpha) has   274 elements
> > Group     4 (    Backbone) has   822 elements
> > Group     5 (   MainChain) has  1097 elements
> > Group     6 (MainChain+Cb) has  1336 elements
> > Group     7 ( MainChain+H) has  1364 elements
> > Group     8 (   SideChain) has  1069 elements
> > Group     9 ( SideChain-H) has   823 elements
> > Group    10 ( Prot-Masses) has  2433 elements
> > Group    11 ( Non-Protein) has 108286 elements
> > Group    12 (          CL) has     4 elements
> > Group    13 (         HOH) has   423 elements
> > Group    14 (         SOL) has 107856 elements
> > Group    15 (          CA) has     2 elements
> > Group    16 (          NA) has     1 elements
> > Group    17 (       Other) has 108286 elements
> > Select a group: 1
> > Selected 1: 'Protein'
> > trn version: GMX_trn_file (single precision)
> > Reading frame       0 time    0.000   Fatal error: Error: Too many iterations
> > in routine JACOBI
> >
> > How I could resolve the problem???
> >
> > then I try g_rms:
> >
> >
> > On Friday 20 May 2005 10:42 am, Anthony Cruz wrote:
> > > How I could do that???  a new tpr??
> > >
> > > On Friday 20 May 2005 7:53 am, Xavier Periole wrote:
> > > > Anthony Cruz wrote:
> > > > >Hi:
> > > > >I run a MD of a protein in water. when I try to analyse the trajectory
> > > > > with g_rms the program stop by the following error :
> > > > >Fatal error: Error: Too many iterations in routine JACOBI
> > > > >What could be the cause? How I can resolve the problem???
> > > >
> > > > That is certainly due to a mismatch between your reference topology and
> > > > the content of
> > > > the trajectory ... make an topology that fits the trajectory.
> > >
> > > _______________________________________________
> > > gmx-users mailing list
> > > gmx-users at gromacs.org
> > > http://www.gromacs.org/mailman/listinfo/gmx-users
> > > Please don't post (un)subscribe requests to the list. Use the
> > > www interface or send it to gmx-users-request at gromacs.org.
> >
> >
> > ------------------------------
> >
> > Message: 4
> > Date: Wed, 25 May 2005 13:48:43 -0500
> > From: "Francesco Mercuri" <mercuri at email.com>
> > Subject: [gmx-users] Time reversibility and settle
> > To: gmx-users at gromacs.org
> > Message-ID: <20050525184843.B8250101D9 at ws1-3.us4.outblaze.com>
> > Content-Type: text/plain; charset="iso-8859-1"
> >
> > > > Hello and thank you for your reply.
> > > > However, my question about the time reversibility of a leap-frog integrator
> > > > with settle (e.g. for TIP3P water molecules) was concerned with the
> > > > actual implementation in Gromacs, rather than the analytical point
> > > > of view. In other words, is this implementation of leap-frog +
> > > > settle still time-reversible in the limit of infinite numerical
> > > > accuracy?
> > > > This question arises since I tried different numerical
> > > > accuracies (single, double and quadruple precision numbers and
> > > > operations; for the latter I had to rewrite large parts of the
> > > > code...) with, in all cases, similar (and pretty large)
> > > > deviations from the "forward" trajectory when reversing the time.
> > > > On the other hand, just bypassing the "settle" subroutine
> > > > (e.g. by commenting all the code related to the original
> > > > implementation of settle by Miyamoto and Kollman), it works as
> > > > expected: the algorithm is almost perfectly time-reversible
> > > > and the only "noise" is due to numerical inaccuracies, with
> > > > deviations comparable, in the three different cases (single,
> > > > double, long double) to the accuracy of numbers.
> > > > Thus, I'm trying to understand whether just resetting the position
> > > > of atoms, as done in the current implementation of "settle",
> > > > still leads to a time-reversible MD (in the limit of infinite
> > > > machine accuracy).
> > > > Any suggestion about that?
> > >
> > > In the limit is should be time-reversible, unless there is a bug in
> > > the settle algorithm, which I consider very unlikely.
> > > Have you tried to use shake or lincs (with high precision settings)?
> > >
> > > There could be some other issues, but when the unconstrained
> > > dynamics is reversible you have probably taken care of these:
> > > You should not use temperature and pressure coupling (the new
> > > version will have reversible Nose-Hoover coupling).
> > > When reversing you should take care to use the proper velocities,
> > > as x(t), v(t-t/2dt) is stored you need to take the velocities from
> > > the next step when reversing.
> > >
> > > Berk.
> >
> > Hi again and thanks for your suggestions.
> > Still in the search of better time-reversibility properties, I'd like
> > to ask a few more questions.
> > If I understood correctly, the leap-frog + settle algorithm is implemented
> > in Gromacs according to the following steps:
> >
> > v'(t+dt/2) = v(t-dt/2) + dt*f(t)/m   ("uncorrected" velocities)
> > r'(t+dt) = r(t) + dt*v'(t+dt/2)      (unconstrained move)
> > r(t+dt) = settle[r'(t+dt)]           (reset of atomic position calling "csettle")
> > v(t+dt/2) = [r(t+dt)-r(t)]/dt        (corrected velocities)
> >
> > is that correct?
> > In this case, is not very clear to me how is it possible to "reverse" it,
> > e.g. restarting from a [r(t),v(t+dt/2)] configuration and inverting the
> > sign of dt, since the settle procedure modifies the atomic position in a
> > way that is, apparently, not "reversible".
> > Is any modification of the velocities needed?
> >
> > Another question concerns the preparation of restart files containing
> > configurations like the one cited above for time-reversing purposes,
> > i.e. [r(t),v(t+dt/2)] (instead of the default [r(t),v(t-dt/2)] ).
> > I tried the quick and dirty way by just running one more MD step,
> > converting the .trr file in ascii format, manually editing the
> > ascii file in order to get the [r(t),v(t+dt/2)] configuration,
> > pasting into a .gro file and converting back the .gro file into
> > a .trr file for restarting. However, even if I modified the routine
> > pr_rvecs in txtdump.c in order to have more decimal digits in the
> > ascii files, the accuracy seems to be limited to the order of
> > 1.e-8, whereas I expected a better accuracy for double precision
> > numbers. Is there any better way to do that? Which is the accuracy
> > with which numbers are stored in the .trr file (with double
> > precision compilation)?
> > Thank you again and best regards,
> >
> >              Francesco
> >
> > --
> > ___________________________________________________________
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> >
> >
> >
> > ------------------------------
> >
> > Message: 5
> > Date: Wed, 25 May 2005 20:54:30 +0200
> > From: "Jordi Camps" <jcamps at lsi.upc.edu>
> > Subject: [gmx-users] Adding ions
> > To: "'Discussion list for GROMACS users'" <gmx-users at gromacs.org>
> > Message-ID: <200505251854.j4PIsNFw028595 at dagon.lsi.upc.edu>
> > Content-Type: text/plain;	charset="US-ASCII"
> >
> > Here I come with more problems :-(
> >
> > I have a protein file with 126 residues. I generated the topology from the
> > .gro file with pdb2gmx. Then I configured the box with editconf. Then I
> > added the solvent with genbox. At least I wanted to neutralize the system
> > with genion, but it gave me this error:
> > 	Fatal error: pbc_dx called before init_pbc
> > This time I think that I followed all the standard steps. Do you know which
> > could be the cause of this error?
> >
> > The command was:
> > 	$ genion -s 1agi.water.top -o 1agi.ion.gro -nn 6
> > And the last lines before the error are:
> > 	Selected 12: 'SOL'
> > 	Number of (3-atomic) solvent molecules: 7092
> > 	Doing single force calculation...
> > 	Replacing solvent molecule 1626 (atom 6216) with Cl
> > 	Fatal error: pbc_dx called before init_pbc
> >
> > Thank you in advance,
> >
> > --
> >
> > Jordi Camps Puchades
> >
> > Instituto Nacional de Bioinformatica (INB) Nodo Computacional GNHC-2
> > UPC-CIRI
> > c/. Jordi Girona 1-3
> > Modul C6-E201                     Tel. : 934 011 650
> > E-08034 Barcelona                 Fax  : 934 017 014
> > Catalunya (Spain)                 e-mail: jcamps at lsi.upc.edu
> >
> >
> >
> > ------------------------------
> >
> > _______________________________________________
> > gmx-users mailing list
> > gmx-users at gromacs.org
> > http://www.gromacs.org/mailman/listinfo/gmx-users
> >
> >
> > End of gmx-users Digest, Vol 13, Issue 66
> > *****************************************
> >
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-- 
David.
________________________________________________________________________
David van der Spoel, PhD, Assoc. Prof., Molecular Biophysics group,
Dept. of Cell and Molecular Biology, Uppsala University.
Husargatan 3, Box 596,          75124 Uppsala, Sweden
phone:  46 18 471 4205          fax: 46 18 511 755
spoel at xray.bmc.uu.se    spoel at gromacs.org   http://xray.bmc.uu.se/~spoel
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