[gmx-users] Fix the residues

liming_52 liming_52 at 163.com
Fri Jan 6 20:57:27 CET 2017


Thank you for reppy. The full information is as follows:
$ gmx pdb2gmx -f lactoferrin.pdb -o lactoferrin.gro -water spce
                  :-) GROMACS - gmx pdb2gmx, VERSION 5.1.4 (-:
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  Gerrit Groenhof   Christoph Junghans   Anca Hamuraru    Vincent Hindriksen
 Dimitrios Karkoulis    Peter Kasson        Jiri Kraus      Carsten Kutzner
    Per Larsson      Justin A. Lemkul   Magnus Lundborg   Pieter Meulenhoff
   Erik Marklund      Teemu Murtola       Szilard Pall       Sander Pronk
   Roland Schulz     Alexey Shvetsov     Michael Shirts     Alfons Sijbers
   Peter Tieleman    Teemu Virolainen  Christian Wennberg    Maarten Wolf
                           and the project leaders:
        Mark Abraham, Berk Hess, Erik Lindahl, and David van der Spoel
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GROMACS:      gmx pdb2gmx, VERSION 5.1.4
Executable:   /usr/local/gromacs/bin//gmx.exe
Data prefix:  /usr/local/gromacs
Command line:
  gmx pdb2gmx -f lactoferrin.pdb -o lactoferrin.gro -water spce

Select the Force Field:
From '/usr/local/gromacs/share/gromacs/top':
 1: AMBER03 protein, nucleic AMBER94 (Duan et al., J. Comp. Chem. 24, 1999-2012, 2003)
 2: AMBER94 force field (Cornell et al., JACS 117, 5179-5197, 1995)
 3: AMBER96 protein, nucleic AMBER94 (Kollman et al., Acc. Chem. Res. 29, 461-469, 1996)
 4: AMBER99 protein, nucleic AMBER94 (Wang et al., J. Comp. Chem. 21, 1049-1074, 2000)
 5: AMBER99SB protein, nucleic AMBER94 (Hornak et al., Proteins 65, 712-725, 2006)
 6: AMBER99SB-ILDN protein, nucleic AMBER94 (Lindorff-Larsen et al., Proteins 78, 1950-58, 2010)
 7: AMBERGS force field (Garcia & Sanbonmatsu, PNAS 99, 2782-2787, 2002)
 8: CHARMM27 all-atom force field (CHARM22 plus CMAP for proteins)
 9: GROMOS96 43a1 force field
10: GROMOS96 43a2 force field (improved alkane dihedrals)
11: GROMOS96 45a3 force field (Schuler JCC 2001 22 1205)
12: GROMOS96 53a5 force field (JCC 2004 vol 25 pag 1656)
13: GROMOS96 53a6 force field (JCC 2004 vol 25 pag 1656)
14: GROMOS96 54a7 force field (Eur. Biophys. J. (2011), 40,, 843-856, DOI: 10.1007/s00249-011-0700-9)
15: OPLS-AA/L all-atom force field (2001 aminoacid dihedrals)
9
Using the Gromos43a1 force field in directory gromos43a1.ff
Opening force field file /usr/local/gromacs/share/gromacs/top/gromos43a1.ff/aminoacids.r2b
Reading lactoferrin.pdb...
WARNING: all CONECT records are ignored
Read 2560 atoms
Analyzing pdb file
Splitting chemical chains based on TER records or chain id changing.
There are 1 chains and 0 blocks of water and 335 residues with 2560 atoms
  chain  #res #atoms
  1 'A'   335   2560
All occupancies are one
Opening force field file /usr/local/gromacs/share/gromacs/top/gromos43a1.ff/atomtypes.atp
Atomtype 50
Reading residue database... (gromos43a1)
Opening force field file /usr/local/gromacs/share/gromacs/top/gromos43a1.ff/aminoacids.rtp
Residue 96
Sorting it all out...
Opening force field file /usr/local/gromacs/share/gromacs/top/gromos43a1.ff/aminoacids.hdb
Opening force field file /usr/local/gromacs/share/gromacs/top/gromos43a1.ff/aminoacids.n.tdb
Opening force field file /usr/local/gromacs/share/gromacs/top/gromos43a1.ff/aminoacids.c.tdb
Back Off! I just backed up topol.top to ./#topol.top.1#
Processing chain 1 'A' (2560 atoms, 335 residues)
Analysing hydrogen-bonding network for automated assignment of histidine
 protonation. 500 donors and 499 acceptors were found.
There are 743 hydrogen bonds
Will use HISE for residue 420
Will use HISH for residue 458
Will use HISD for residue 588
Will use HISE for residue 595
Will use HISE for residue 606
Will use HISE for residue 613
Identified residue TYR342 as a starting terminus.
Identified residue SER676 as a ending terminus.
8 out of 8 lines of specbond.dat converted successfully
Special Atom Distance matrix:
                  CYS348  CYS358  CYS371  CYS380  CYS405  HIS420  CYS425
                    SG64   SG138   SG241   SG300   SG481  NE2595   SG629
  CYS358   SG138   0.849
  CYS371   SG241   0.940   0.213
  CYS380   SG300   0.204   0.933   1.049
  CYS405   SG481   1.411   2.186   2.303   1.371
  HIS420  NE2595   3.406   3.321   3.509   3.348   3.338
  CYS425   SG629   2.460   2.150   2.323   2.429   2.901   1.313
  CYS457   SG875   2.702   2.932   3.096   2.502   2.930   3.532   3.094
  HIS458  NE2885   2.548   2.968   3.141   2.345   2.426   3.418   3.123
  MET471   SD983   2.682   3.182   3.361   2.487   2.293   3.347   3.207
  CYS481  SG1051   3.086   3.770   3.933   2.924   2.167   3.844   3.883
  CYS491  SG1133   2.184   2.509   2.651   1.985   2.495   3.728   3.130
  CYS502  SG1209   2.159   2.671   2.793   1.969   2.249   4.093   3.530
  CYS505  SG1228   2.166   2.539   2.672   1.970   2.452   3.880   3.273
  CYS515  SG1297   2.029   2.503   2.628   1.837   2.216   3.962   3.362
  CYS532  SG1436   2.629   2.850   3.005   2.431   2.930   3.653   3.146
  CYS573  SG1764   3.775   3.952   4.158   3.598   3.597   2.648   2.951
  CYS587  SG1867   3.594   3.755   3.960   3.419   3.463   2.533   2.771
  HIS588 NE21877   3.277   3.459   3.671   3.127   3.007   1.800   2.233
  HIS595 NE21927   1.637   1.836   2.046   1.488   1.825   2.179   1.605
  HIS606 NE22008   1.686   1.478   1.480   1.846   2.316   3.172   2.230
  HIS613 NE22066   2.250   1.623   1.635   2.359   3.154   2.929   1.780
  CYS625  SG2156   2.333   1.651   1.753   2.329   3.350   2.606   1.332
  CYS630  SG2197   2.270   1.572   1.667   2.261   3.342   2.763   1.491
  CYS647  SG2337   2.306   2.002   2.173   2.286   2.760   1.421   0.205
  CYS675  SG2554   2.907   3.577   3.743   2.742   2.024   3.670   3.679
                  CYS457  HIS458  MET471  CYS481  CYS491  CYS502  CYS505
                   SG875  NE2885   SD983  SG1051  SG1133  SG1209  SG1228
  HIS458  NE2885   0.746
  MET471   SD983   1.209   0.486
  CYS481  SG1051   2.332   1.591   1.152
  CYS491  SG1133   0.700   0.843   1.287   2.240
  CYS502  SG1209   1.263   1.036   1.308   1.939   0.670
  CYS505  SG1228   0.873   0.919   1.329   2.200   0.207   0.484
  CYS515  SG1297   1.171   1.014   1.329   2.039   0.523   0.202   0.343
  CYS532  SG1436   0.207   0.847   1.329   2.423   0.569   1.166   0.740
  CYS573  SG1764   1.883   1.857   1.818   2.626   2.461   2.877   2.626
  CYS587  SG1867   1.757   1.754   1.744   2.603   2.323   2.759   2.493
  HIS588 NE21877   2.175   1.985   1.862   2.508   2.559   2.918   2.715
  HIS595 NE21927   1.755   1.601   1.689   2.421   1.670   1.978   1.789
  HIS606 NE22008   4.076   3.936   3.996   4.306   3.707   3.784   3.737
  HIS613 NE22066   4.109   4.155   4.299   4.857   3.868   4.130   3.948
  CYS625  SG2156   3.130   3.389   3.640   4.482   3.059   3.515   3.190
  CYS630  SG2197   3.034   3.320   3.592   4.455   2.945   3.405   3.073
  CYS647  SG2337   3.121   3.125   3.204   3.846   3.112   3.483   3.246
  CYS675  SG2554   2.186   1.441   1.001   0.209   2.089   1.817   2.058
                  CYS515  CYS532  CYS573  CYS587  HIS588  HIS595  HIS606
                  SG1297  SG1436  SG1764  SG1867 NE21877 NE21927 NE22008
  CYS532  SG1436   1.063
  CYS573  SG1764   2.816   2.085
  CYS587  SG1867   2.687   1.956   0.205
  HIS588 NE21877   2.835   2.354   0.952   0.859
  HIS595 NE21927   1.831   1.805   2.198   2.012   1.663
  HIS606 NE22008   3.645   4.043   4.641   4.457   3.901   2.523
  HIS613 NE22066   3.956   4.078   4.559   4.364   3.878   2.644   1.163
  CYS625  SG2156   3.318   3.104   3.598   3.398   3.138   2.074   2.269
  CYS630  SG2197   3.206   2.996   3.606   3.404   3.187   2.069   2.325
  CYS647  SG2337   3.316   3.165   3.060   2.878   2.325   1.567   2.028
  CYS675  SG2554   1.902   2.278   2.507   2.470   2.354   2.213   4.124
                  HIS613  CYS625  CYS630  CYS647
                 NE22066  SG2156  SG2197  SG2337
  CYS625  SG2156   1.454
  CYS630  SG2197   1.554   0.210
  CYS647  SG2337   1.628   1.318   1.473
  CYS675  SG2554   4.656   4.273   4.247   3.642
Linking CYS-348 SG-64 and CYS-380 SG-300...
Linking CYS-358 SG-138 and CYS-371 SG-241...
Linking CYS-425 SG-629 and CYS-647 SG-2337...
Linking CYS-457 SG-875 and CYS-532 SG-1436...
Linking CYS-481 SG-1051 and CYS-675 SG-2554...
Linking CYS-491 SG-1133 and CYS-505 SG-1228...
Linking CYS-502 SG-1209 and CYS-515 SG-1297...
Linking CYS-573 SG-1764 and CYS-587 SG-1867...
Linking CYS-625 SG-2156 and CYS-630 SG-2197...
Start terminus TYR-342: NH3+
End terminus SER-676: COO-
Checking for duplicate atoms....
Generating any missing hydrogen atoms and/or adding termini.
Now there are 335 residues with 3278 atoms
Making bonds...
Number of bonds was 3340, now 3335
Generating angles, dihedrals and pairs...
WARNING: WARNING: Residue 1 named TYR of a molecule in the input file was mapped
to an entry in the topology database, but the atom H used in
an interaction of type angle in that entry is not found in the
input file. Perhaps your atom and/or residue naming needs to be
fixed.
 
WARNING: WARNING: Residue 335 named SER of a molecule in the input file was mapped
to an entry in the topology database, but the atom O used in
an interaction of type angle in that entry is not found in the
input file. Perhaps your atom and/or residue naming needs to be
fixed.

Before cleaning: 5477 pairs
Before cleaning: 6310 dihedrals
Making cmap torsions...
There are 1781 dihedrals, 1618 impropers, 4878 angles
          5477 pairs,     3335 bonds and     0 virtual sites
Total mass 36559.344 a.m.u.
Total charge 0.000 e
Writing topology
Back Off! I just backed up posre.itp to ./#posre.itp.1#
Writing coordinate file...
Back Off! I just backed up lactoferrin.gro to ./#lactoferrin.gro.1#
                --------- PLEASE NOTE ------------
You have successfully generated a topology from: lactoferrin.pdb.
The Gromos43a1 force field and the spce water model are used.
                --------- ETON ESAELP ------------
gcq#395: "It was something to at least have a choice of nightmares" (Joseph Conrad)






--

With my best wishes,
Ming Li, PhD
Chinese Academy of Agricultural Sciences, Beijing, China



At 2017-01-07 03:22:36, "Justin Lemkul" <jalemkul at vt.edu> wrote:
>
>
>On 1/6/17 1:58 PM, liming_52 wrote:
>> Dear Gromacs users,
>>
>> I am trying to run a md using 4n6p.cif, which was obtained from PDB. I converted the file into pdb format using DS4.1, and got the file named lactoferrin.pdb. When I directly run
>> the command "gmx pdb2gmx -f lactoferrin.pdb -o lactoferrin.gro -water spce", the program runs and produces the information as follows:
>> ...
>
>You snipped out the most important information.  Please provide the full screen 
>output from pdb2gmx.
>
>-Justin
>
>> WARNING: WARNING: Residue 1 named TYR of a molecule in the input file was mapped
>> to an entry in the topology database, but the atom H used in
>> an interaction of type angle in that entry is not found in the
>> input file. Perhaps your atom and/or residue naming needs to be
>> fixed.
>>
>> WARNING: WARNING: Residue 335 named SER of a molecule in the input file was mapped
>> to an entry in the topology database, but the atom O used in
>> an interaction of type angle in that entry is not found in the
>> input file. Perhaps your atom and/or residue naming needs to be
>> fixed.
>>
>> ...
>> How should I fix the residues? And which tools should I use? Is there any examples or tutorials?
>>
>> If anyone can suggest a solution to this issue, it would be really helpful.
>>
>>
>>
>>
>>
>>
>>
>> --
>>
>> With my best wishes,
>> Ming Li, PhD
>> Chinese Academy of Agricultural Sciences, Beijing, China
>>
>
>-- 
>==================================================
>
>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
>
>==================================================
>-- 
>Gromacs Users mailing list
>
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