[gmx-users] Inconsistent behavior for bonds involving dummy atoms for alchemical perturbation

Justin Lemkul jalemkul at vt.edu
Fri Mar 18 12:57:41 CET 2016



On 3/17/16 6:04 PM, Ryan Muraglia wrote:
> Dear GROMACS users,
>
> I've been attempting to calculate delta G values for GXG tripeptide
> mutations as a test case to validate and benchmark my set up, but I have
> run into a host of issues and curiosities, one of which I describe below.
>
> Depending on the direction in which I carry out a mutation, a given bond
> may or may not throw a (fatal) warning as I execute the grompp call to set
> up the NVT equilibration (and subsequently mdruns).
>
> To clarify, here is an example: when running a GAG to GLG mutation, during
> the grompp call I receive the following warning:
>
> "WARNING 1 [file topol.top, line 388]:
>    The bond in molecule-type Protein between atoms 21 DCD1 and 22 DHD1 has
>    an estimated oscillational period of 8.3e-03 ps, which is less than 5
>    times the time step of 2.0e-03 ps.
>    Maybe you forgot to change the constraints mdp option."
>
> If I choose to ignore this warning by setting maxwarn to 1, the NVT
> equilibration blows up.
>
> In the other direction, when running a GLG to GAG mutation, for the same
> mdp file, the grompp step before the NVT throws no warning, and the NVT
> equilibration runs to completion without a hitch.
>
> I can reduce the time step for the GAG to GLG mutation to have it run to
> completion, but I do not understand why I only see this warning in one
> direction, when this bond exists in both topologies. I also do not
> understand why there is only one bond for which this warning comes up, when
> there are several other identical bonds (in terms of atom types, etc) that
> fly under the radar. Lastly, I have set "constraints = h-bonds" so it
> puzzles me that a bond involving a hydrogen is the culprit here.
>

If the atoms are named "D" then grompp won't detect them as hydrogen.  The 
checking is done with respect to the first character in the atom name.  So 
that's why you're blowing up; a bond that should be constrained isn't.

> I use the pmx package to generate topologies for amino acid substitutions,
> and my system uses the amber99sb forcefield with tip3p water. The [atoms]
> directive of my A2L topology is reproduced below:
>
>   [ atoms ]
> ;   nr       type  resnr residue  atom   cgnr     charge       mass  typeB
>     chargeB      massB
>       1          N3      1    GLY      N      1   0.294300    14.0100
>       2           H      1    GLY     H1      2   0.164200     1.0080
>       3           H      1    GLY     H2      3   0.164200     1.0080
>       4           H      1    GLY     H3      4   0.164200     1.0080
>       5          CT      1    GLY     CA      5  -0.010000    12.0100
>       6          HP      1    GLY    HA1      6   0.089500     1.0080
>       7          HP      1    GLY    HA2      7   0.089500     1.0080
>       8           C      1    GLY      C      8   0.616300    12.0100
>       9           O      1    GLY      O      9  -0.572200    16.0000
>      10           N      2    A2L      N     10  -0.415700    14.0100
>      11           H      2    A2L      H     11   0.271900     1.0080
>      12          CT      2    A2L     CA     12   0.033700    12.0100
>     CT  -0.051800    12.0100
>      13          H1      2    A2L     HA     13   0.082300     1.0080
>     H1   0.092200     1.0080
>      14          CT      2    A2L     CB     14  -0.182500    12.0100
>     CT  -0.110200    12.0100
>      15          HC      2    A2L    HB1     15   0.060300     1.0080
>     CT   0.353100    12.0100
>      16          HC      2    A2L    HB2     16   0.060300     1.0080
>     HC   0.045700     1.0080
>      17          HC      2    A2L    HB3     17   0.060300     1.0080
>     HC   0.045700     1.0080
>      18           C      2    A2L      C     18   0.597300    12.0100
>      19           O      2    A2L      O     19  -0.567900    16.0000
>      20      DUM_HC      2    A2L    DHG     20   0.000000     1.0000
>     HC  -0.036100     1.0080
>      21      DUM_CT      2    A2L   DCD1     21   0.000000     1.0000
>     CT  -0.412100    12.0100
>      22      DUM_HC      2    A2L   DHD1     22   0.000000     1.0000
>     HC   0.100000     1.0080
>      23      DUM_HC      2    A2L   DHD2     23   0.000000     1.0000
>     HC   0.100000     1.0080
>      24      DUM_HC      2    A2L   DHD3     24   0.000000     1.0000
>     HC   0.100000     1.0080
>      25      DUM_CT      2    A2L   DCD2     25   0.000000     1.0000
>     CT  -0.412100    12.0100
>      26      DUM_HC      2    A2L   DHD4     26   0.000000     1.0000
>     HC   0.100000     1.0080
>      27      DUM_HC      2    A2L   DHD5     27   0.000000     1.0000
>     HC   0.100000     1.0080
>      28      DUM_HC      2    A2L   DHD6     28   0.000000     1.0000
>     HC   0.100000     1.0080
>      29           N      3    GLY      N     29  -0.382100    14.0100
>      30           H      3    GLY      H     30   0.268100     1.0080
>      31          CT      3    GLY     CA     31  -0.249300    12.0100
>      32          H1      3    GLY    HA1     32   0.105600     1.0080
>      33          H1      3    GLY    HA2     33   0.105600     1.0080
>      34           C      3    GLY      C     34   0.723100    12.0100
>      35          O2      3    GLY    OC1     35  -0.785500    16.0000
>      36          O2      3    GLY    OC2     36  -0.785500    16.0000
>
> The L2A topology is similar. The second residue is as follows:
>
>      10           N      2    L2A      N     10  -0.415700    14.0100
>      11           H      2    L2A      H     11   0.271900     1.0080
>      12          CT      2    L2A     CA     12  -0.051800    12.0100
>     CT   0.033700    12.0100
>      13          H1      2    L2A     HA     13   0.092200     1.0080
>     H1   0.082300     1.0080
>      14          CT      2    L2A     CB     14  -0.110200    12.0100
>     CT  -0.182500    12.0100
>      15          HC      2    L2A    HB1     15   0.045700     1.0080
>     HC   0.060300     1.0080
>      16          HC      2    L2A    HB2     16   0.045700     1.0080
>     HC   0.060300     1.0080
>      17          CT      2    L2A     CG     17   0.353100    12.0100
>     HC   0.060300     1.0080
>      18          HC      2    L2A     HG     18  -0.036100     1.0080
>   DUM_HC   0.000000     1.0000
>      19          CT      2    L2A    CD1     19  -0.412100    12.0100
>   DUM_CT   0.000000     1.0000
>      20          HC      2    L2A   HD11     20   0.100000     1.0080
>   DUM_HC   0.000000     1.0000
>      21          HC      2    L2A   HD12     21   0.100000     1.0080
>   DUM_HC   0.000000     1.0000
>      22          HC      2    L2A   HD13     22   0.100000     1.0080
>   DUM_HC   0.000000     1.0000
>      23          CT      2    L2A    CD2     23  -0.412100    12.0100
>   DUM_CT   0.000000     1.0000
>      24          HC      2    L2A   HD21     24   0.100000     1.0080
>   DUM_HC   0.000000     1.0000
>      25          HC      2    L2A   HD22     25   0.100000     1.0080
>   DUM_HC   0.000000     1.0000
>      26          HC      2    L2A   HD23     26   0.100000     1.0080
>   DUM_HC   0.000000     1.0000
>      27           C      2    L2A      C     27   0.597300    12.0100
>      28           O      2    L2A      O     28  -0.567900    16.0000
>
> An additional quirk is that in the A2L direction (the one that is
> problematic), mdrun reports that I have 16 constraints in my system,
> whereas in the L2A direction, mdrun reports 19 constraints.
>

Use gmx dump or gmx check on the .tpr files to see what the differences are.

-Justin

> Other mutations are a mixed bag. A2V and V2A, despite having the same type
> of bond that causes the error in A2L, both go through with no warnings
> (although their constraints number do differ, but they follow the pattern
> described in the pmx paper). Q2A goes through with no warning, but A2Q
> prints a similar warning as above, except this one is between atoms 22 DCD
> and 23 DOE1 with an estimated oscillational period of 6.4e-03 ps,
> indicating that the problem can arise for bonds that do not involve
> hydrogen as well.
>
> Pertinent portions of my mdp file are reproduced below:
>
> integrator = sd ; Langevin dynamics
> dt = 0.002 ; 2 fs
> constraints = h-bonds
> constraint-algorithm = LINCS
> continuation = no
> lincs-order = 6
> lincs-iter = 1
>
> ; Free energy calculations
> free_energy = yes
> delta_lambda = 0 ; no Jarzynski non-eq
> calc_lambda_neighbors = 1 ; only calculate energy to immediate neighbors
> (suitable for BAR, but MBAR needs all)
> sc-alpha                 = 0.5
> sc-coul                  = no
> sc-power                 = 1.0
> sc-sigma                 = 0.3
> couple-moltype           = Protein  ; name of moleculetype to decouple
> couple-lambda0           = vdw-q      ; all interactions
> couple-lambda1           = vdw     ; remove electrostatics, only vdW
> couple-intramol          = no
> nstdhdl                  = 100
>
> ; lambda vectors ; decharging only. Keep as A. Next file deals with
> uncharged A to uncharged L to charged L
> ; init_lambda_state   0   1   2   3   4   5   6   7   8   9   10
> init_lambda_state = 05
> coul_lambdas =        0.0 0.1 0.2 0.3 0.4 0.5 0.6 0.7 0.8 0.9 1.0
> vdw_lambdas =         0.0 0.0 0.0 0.0 0.0 0.0 0.0 0.0 0.0 0.0 0.0
> bonded_lambdas =      0.0 0.0 0.0 0.0 0.0 0.0 0.0 0.0 0.0 0.0 0.0 ; match
> vdw
> mass_lambdas =        0.0 0.0 0.0 0.0 0.0 0.0 0.0 0.0 0.0 0.0 0.0 ; match
> vdw
> temperature_lambdas = 0.0 0.0 0.0 0.0 0.0 0.0 0.0 0.0 0.0 0.0 0.0 ; not
> doing simulated tempering
>
> I considered that perhaps the issue was due to which atoms had "appeared"
> or "disappeared," so I also ran a test using an mdp file where the vdw,
> bonded and mass lambdas were set to 1 for the L2A mutation, which I believe
> means I should be simulating the same state as the A2L which causes an
> error, but I got no warning from grompp.
>
> Any information or advice as to why I am seeing unexpectedly different
> behaviors depending on the direction of my mutation would be appreciated.
>
> Thank you!
>

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

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

jalemkul at outerbanks.umaryland.edu | (410) 706-7441
http://mackerell.umaryland.edu/~jalemkul

==================================================


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