On 9/1/15 8:14 AM, Smith, Micholas D. wrote:
Hi Sana Saeed,

What force field are you using? Also are you sure the structure you are 
starting with is stable to begin with? It is possible that the model you are 
starting with is actually fairly far away from the minimum energy structure in 
which case energy minimization may alter the structure (though i've never seen 
a beta sheet changing into a coil-like form).


Worth noting that visualization software sometimes fails to render secondary structure correctly. Analyzing the hydrogen bonding and backbone dihedrals is definitive; whatever VMD/PyMOL/etc come up with is not.

-Justin

-Micholas

===================
Micholas Dean Smith, PhD.
Post-doctoral Research Associate
University of Tennessee/Oak Ridge National Laboratory
Center for Molecular Biophysics

________________________________________
From: [email protected] 
<[email protected]> on behalf of Sana Saeed 
<[email protected]>
Sent: Monday, August 31, 2015 10:30 PM
To: [email protected]
Subject: [gmx-users] structure changed after energy minimization

hi gmx users,i want to simulate prion protein(beta-sheets structure; model in 
modeller), but after minimization the structure totally changes into elongated 
form.what am i missing? i am doing implicit solvent simulation. this is the mdp 
file for minimization:  title               =cpp                 =  /lib/cpp    
                                             ; prepocessor of the current 
machinedefine              =  -DFLEXIBLE                                        
       ; -DPOSRES, -DPOSRES_IONS ;DFLEX_SPC; FLEXible SPC and POSition 
REStraints
integrator          =  steep                                                    
; steepest descent algorithmdt                  =  0.005                        
                            ; time step in psnsteps              =  5000        
                                             ; number of steps
emtol               =  100                                                      
; convergence criterionemstep              =  0.05                              
                       ; intial step sizeconstraints           = 
noneconstraint-algorithm  = lincsunconstrained-start   = no                     
                                 ; Do not constrain the start 
configuration;shake_tol           = 0.0001nstlist             =  1              
                                          ; step frequency for updating 
neighbour listns_type             =  simple                                     
              ; grid ; method for nighbour searching (?)nstxout             =  
100                                                      ; frequency for 
writing coords to outputnstvout             =  100                              
                        ; frequency for writing velocities to outputnstfout     
        =  0    ; frequency for writing forces to outputnstlog              =
  100    ; frequency for writing energies to log filenstenergy           =  100 
 ; frequency for writing energies to energy filenstxtcout           =  0    ; 
frequency for writing coords to xtc trajxtc_grps            =  system ; 
group(s) whose coords are to be written in xtc trajenergygrps          =  
system ; group(s) whose energy is to be written in energy filepbc               
  =  xyz    ; use pbcrlist               =  1.0    ; cutoff (nm)coulombtype     
    =  cutoff ; truncation for minimisation, with large cutoffrcoulomb          
  =  1.0vdwtype             =  cut-off  ; truncation for minimisation, with 
large cutoffrvdw                =  1.0nstcomm             =  0  ; number of 
steps for centre of mass motion removal (in vacuo only!)Tcoupl              =  
noPcoupl              =  nogen_vel             =  no Free energy control 
stufffree_energy              = yesinit_lambda              = 0.0delta_lambda   
          = 0sc_alpha                 =0.5sc-power
      =1.0sc-sigma                 = 0.3

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--
==================================================

Justin A. Lemkul, Ph.D.
Ruth L. Kirschstein NRSA Postdoctoral Fellow

Department of Pharmaceutical Sciences
School of Pharmacy
Health Sciences Facility II, Room 629
University of Maryland, Baltimore
20 Penn St.
Baltimore, MD 21201

[email protected] | (410) 706-7441
http://mackerell.umaryland.edu/~jalemkul

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