WHAT IF Check report

This file was created 2012-01-19 from WHAT_CHECK output by a conversion script. If you are new to WHAT_CHECK, please study the pdbreport pages. There also exists a legend to the output.

Please note that you are looking at an abridged version of the output (all checks that gave normal results have been removed from this report). You can have a look at the Full report instead.

Verification log for pdb1yzx.ent

Checks that need to be done early-on in validation

Note: Non crystallographic symmetry RMS plot

The plot shows the RMS differences between two similar chains on a residue- by-residue basis. Individual "spikes" can be indicative of interesting or wrong residues. If all residues show a high RMS value, the structure could be incorrectly refined.

Chain identifiers of the two chains: A and B

All-atom RMS fit for the two chains : 0.563
CA-only RMS fit for the two chains : 0.230

Note: Non crystallographic symmetry backbone difference plot

The plot shows the differences in backbone torsion angles between two similar chains on a residue-by-residue basis. Individual "spikes" can be indicative of interesting or wrong residues. If all residues show high differences, the structure could be incorrectly refined.

Chain identifiers of the two chains: A and B

Warning: Ligands for which a topology was generated automatically

The topology for the ligands in the table below were determined automatically. WHAT IF uses a local copy of Daan van Aalten's Dundee PRODRG server to automatically generate topology information for ligands. For this PDB file that seems to have gone fine, but be aware that automatic topology generation is a complicated task. So, if you get messages that you fail to understand or that you believe are wrong, and one of these ligands is involved, then check the ligand topology first.

 437 GSF   ( 301-)  A  -
 438 GSF   (1301-)  B  -

Non-validating, descriptive output paragraph

Note: Ramachandran plot

In this Ramachandran plot x-signs represent glycines, squares represent prolines, and plus-signs represent the other residues. If too many plus- signs fall outside the contoured areas then the molecule is poorly refined (or worse). Proline can only occur in the narrow region around phi=-60 that also falls within the other contour islands.

In a colour picture, the residues that are part of a helix are shown in blue, strand residues in red. Preferred regions for helical residues are drawn in blue, for strand residues in red, and for all other residues in green. A full explanation of the Ramachandran plot together with a series of examples can be found at the WHAT_CHECK website.

Chain identifier: A

Note: Ramachandran plot

Chain identifier: B

Coordinate problems, unexpected atoms, B-factor and occupancy checks

Warning: What type of B-factor?

WHAT IF does not yet know well how to cope with B-factors in case TLS has been used. It simply assumes that the B-factor listed on the ATOM and HETATM cards are the total B-factors. When TLS refinement is used that assumption sometimes is not correct. TLS seems not mentioned in the header of the PDB file. But anyway, if WHAT IF complains about your B-factors, and you think that they are OK, then check for TLS related B-factor problems first.

Obviously, the temperature at which the X-ray data was collected has some importance too:

Crystal temperature (K) :293.000

Note: B-factor plot

The average atomic B-factor per residue is plotted as function of the residue number.

Chain identifier: A

Note: B-factor plot

Chain identifier: B

Nomenclature related problems

Warning: Arginine nomenclature problem

The arginine residues listed in the table below have their N-H-1 and N-H-2 swapped.

  37 ARG   (  40-)  A
  58 ARG   (  61-)  A
 276 ARG   (  61-)  B

Warning: Tyrosine convention problem

The tyrosine residues listed in the table below have their chi-2 not between -90.0 and 90.0

   9 TYR   (  12-)  A
 175 TYR   ( 178-)  A
 227 TYR   (  12-)  B
 393 TYR   ( 178-)  B

Warning: Phenylalanine convention problem

The phenylalanine residues listed in the table below have their chi-2 not between -90.0 and 90.0.

  80 PHE   (  83-)  A
 178 PHE   ( 181-)  A
 195 PHE   ( 198-)  A
 298 PHE   (  83-)  B
 396 PHE   ( 181-)  B
 413 PHE   ( 198-)  B

Warning: Aspartic acid convention problem

The aspartic acid residues listed in the table below have their chi-2 not between -90.0 and 90.0, or their proton on OD1 instead of OD2.

 128 ASP   ( 131-)  A

Warning: Glutamic acid convention problem

The glutamic acid residues listed in the table below have their chi-3 outside the -90.0 to 90.0 range, or their proton on OE1 instead of OE2.

 106 GLU   ( 109-)  A
 109 GLU   ( 112-)  A
 112 GLU   ( 115-)  A
 131 GLU   ( 134-)  A
 140 GLU   ( 143-)  A
 147 GLU   ( 150-)  A
 154 GLU   ( 157-)  A
 170 GLU   ( 173-)  A
 201 GLU   ( 204-)  A
 327 GLU   ( 112-)  B
 330 GLU   ( 115-)  B
 335 GLU   ( 120-)  B
 365 GLU   ( 150-)  B
 385 GLU   ( 170-)  B
 388 GLU   ( 173-)  B
 419 GLU   ( 204-)  B

Geometric checks

Warning: Low bond length variability

Bond lengths were found to deviate less than normal from the mean Engh and Huber [REF] and/or Parkinson et al [REF] standard bond lengths. The RMS Z-score given below is expected to be near 1.0 for a normally restrained data set. The fact that it is lower than 0.667 in this structure might indicate that too-strong restraints have been used in the refinement. This can only be a problem for high resolution X-ray structures.

RMS Z-score for bond lengths: 0.246
RMS-deviation in bond distances: 0.006

Warning: Low bond angle variability

Bond angles were found to deviate less than normal from the standard bond angles (normal values for protein residues were taken from Engh and Huber [REF], for DNA/RNA from Parkinson et al [REF]). The RMS Z-score given below is expected to be near 1.0 for a normally restrained data set. The fact that it is lower than 0.667 in this structure might indicate that too-strong restraints have been used in the refinement. This can only be a problem for high resolution X-ray structures.

RMS Z-score for bond angles: 0.554
RMS-deviation in bond angles: 1.165

Error: Nomenclature error(s)

Checking for a hand-check. WHAT IF has over the course of this session already corrected the handedness of atoms in several residues. These were administrative corrections. These residues are listed here.

  37 ARG   (  40-)  A
  58 ARG   (  61-)  A
 106 GLU   ( 109-)  A
 109 GLU   ( 112-)  A
 112 GLU   ( 115-)  A
 128 ASP   ( 131-)  A
 131 GLU   ( 134-)  A
 140 GLU   ( 143-)  A
 147 GLU   ( 150-)  A
 154 GLU   ( 157-)  A
 170 GLU   ( 173-)  A
 201 GLU   ( 204-)  A
 276 ARG   (  61-)  B
 327 GLU   ( 112-)  B
 330 GLU   ( 115-)  B
 335 GLU   ( 120-)  B
 365 GLU   ( 150-)  B
 385 GLU   ( 170-)  B
 388 GLU   ( 173-)  B
 419 GLU   ( 204-)  B

Error: Tau angle problems

The side chains of the residues listed in the table below contain a tau angle (N-Calpha-C) that was found to deviate from te expected value by more than 4.0 times the expected standard deviation. The number in the table is the number of standard deviations this RMS value deviates from the expected value.

 122 VAL   ( 125-)  A    4.46
 340 VAL   ( 125-)  B    4.15

Torsion-related checks

Warning: Torsion angle evaluation shows unusual residues

The residues listed in the table below contain bad or abnormal torsion angles.

These scores give an impression of how `normal' the torsion angles in protein residues are. All torsion angles except omega are used for calculating a `normality' score. Average values and standard deviations were obtained from the residues in the WHAT IF database. These are used to calculate Z-scores. A residue with a Z-score of below -2.0 is poor, and a score of less than -3.0 is worrying. For such residues more than one torsion angle is in a highly unlikely position.

  57 PRO   (  60-)  A    -2.7
 275 PRO   (  60-)  B    -2.5
 298 PHE   (  83-)  B    -2.3
 175 TYR   ( 178-)  A    -2.0

Warning: Backbone evaluation reveals unusual conformations

The residues listed in the table below have abnormal backbone torsion angles.

Residues with `forbidden' phi-psi combinations are listed, as well as residues with unusual omega angles (deviating by more than 3 sigma from the normal value). Please note that it is normal if about 5 percent of the residues is listed here as having unusual phi-psi combinations.

  75 GLN   (  78-)  A  Poor phi/psi
  77 PRO   (  80-)  A  Poor phi/psi
 180 LEU   ( 183-)  A  PRO omega poor
 293 GLN   (  78-)  B  Poor phi/psi
 295 PRO   (  80-)  B  Poor phi/psi
 308 GLU   (  93-)  B  Poor phi/psi
 344 ASN   ( 129-)  B  Poor phi/psi
 398 LEU   ( 183-)  B  PRO omega poor
 407 GLY   ( 192-)  B  Poor phi/psi
 chi-1/chi-2 correlation Z-score : 0.477

Warning: Unusual rotamers

The residues listed in the table below have a rotamer that is not seen very often in the database of solved protein structures. This option determines for every residue the position specific chi-1 rotamer distribution. Thereafter it verified whether the actual residue in the molecule has the most preferred rotamer or not. If the actual rotamer is the preferred one, the score is 1.0. If the actual rotamer is unique, the score is 0.0. If there are two preferred rotamers, with a population distribution of 3:2 and your rotamer sits in the lesser populated rotamer, the score will be 0.667. No value will be given if insufficient hits are found in the database.

It is not necessarily an error if a few residues have rotamer values below 0.3, but careful inspection of all residues with these low values could be worth it.

 313 SER   (  98-)  B    0.38

Warning: Unusual backbone conformations

For the residues listed in the table below, the backbone formed by itself and two neighbouring residues on either side is in a conformation that is not seen very often in the database of solved protein structures. The number given in the table is the number of similar backbone conformations in the database with the same amino acid in the centre.

For this check, backbone conformations are compared with database structures using C-alpha superpositions with some restraints on the backbone oxygen positions.

A residue mentioned in the table can be part of a strange loop, or there might be something wrong with it or its directly surrounding residues. There are a few of these in every protein, but in any case it is worth looking at!

  12 LEU   (  15-)  A      0
  26 TYR   (  29-)  A      0
  30 TRP   (  33-)  A      0
  32 ILE   (  35-)  A      0
  48 SER   (  51-)  A      0
  50 ASN   (  53-)  A      0
  55 LEU   (  58-)  A      0
  77 PRO   (  80-)  A      0
  83 ASP   (  86-)  A      0
  91 LYS   (  94-)  A      0
  93 SER   (  96-)  A      0
  94 LEU   (  97-)  A      0
 125 ARG   ( 128-)  A      0
 129 ILE   ( 132-)  A      0
 130 THR   ( 133-)  A      0
 144 MET   ( 147-)  A      0
 175 TYR   ( 178-)  A      0
 177 ALA   ( 180-)  A      0
 178 PHE   ( 181-)  A      0
 180 LEU   ( 183-)  A      0
 188 ASP   ( 191-)  A      0
 195 PHE   ( 198-)  A      0
 198 ASP   ( 201-)  A      0
 199 ARG   ( 202-)  A      0
 211 TRP   ( 214-)  A      0
And so on for a total of 116 lines.

Warning: Omega angles too tightly restrained

The omega angles for trans-peptide bonds in a structure are expected to give a gaussian distribution with the average around +178 degrees and a standard deviation around 5.5 degrees. These expected values were obtained from very accurately determined structures. Many protein structures are too tightly restrained. This seems to be the case with the current structure too, as the observed standard deviation is below 4.0 degrees.

Standard deviation of omega values : 1.050

Warning: Backbone oxygen evaluation

The residues listed in the table below have an unusual backbone oxygen position.

For each of the residues in the structure, a search was performed to find 5-residue stretches in the WHAT IF database with superposable C-alpha coordinates, and some restraining on the neighbouring backbone oxygens.

In the following table the RMS distance between the backbone oxygen positions of these matching structures in the database and the position of the backbone oxygen atom in the current residue is given. If this number is larger than 1.5 a significant number of structures in the database show an alternative position for the backbone oxygen. If the number is larger than 2.0 most matching backbone fragments in the database have the peptide plane flipped. A manual check needs to be performed to assess whether the experimental data can support that alternative as well. The number in the last column is the number of database hits (maximum 80) used in the calculation. It is "normal" that some glycine residues show up in this list, but they are still worth checking!

  92 GLY   (  95-)  A   1.67   12

Bump checks

Error: Abnormally short interatomic distances

The pairs of atoms listed in the table below have an unusually short interactomic distance; each bump is listed in only one direction.

The contact distances of all atom pairs have been checked. Two atoms are said to `bump' if they are closer than the sum of their Van der Waals radii minus 0.40 Angstrom. For hydrogen bonded pairs a tolerance of 0.55 Angstrom is used. The first number in the table tells you how much shorter that specific contact is than the acceptable limit. The second distance is the distance between the centres of the two atoms. Although we believe that two water atoms at 2.4 A distance are too close, we only report water pairs that are closer than this rather short distance.

The last text-item on each line represents the status of the atom pair. If the final column contains the text 'HB', the bump criterion was relaxed because there could be a hydrogen bond. Similarly relaxed criteria are used for 1-3 and 1-4 interactions (listed as 'B2' and 'B3', respectively). BL indicates that the B-factors of the clashing atoms have a low B-factor thereby making this clash even more worrisome. INTRA and INTER indicate whether the clashes are between atoms in the same asymmetric unit, or atoms in symmetry related asymmetric units, respectively.

 106 GLU   ( 109-)  A      OE2 <->  155 LYS   ( 158-)  A      NZ     0.23    2.47  INTRA BF
  58 ARG   (  61-)  A      NH2 <->  265 ASP   (  50-)  B      OD2    0.21    2.49  INTRA
  71 ARG   (  74-)  A      NE  <->  439 HOH   ( 577 )  A      O      0.18    2.52  INTRA BF
 350 PRO   ( 135-)  B      CG  <->  351 GLN   ( 136-)  B      NE2    0.15    2.95  INTRA BF
 277 LYS   (  62-)  B      NZ  <->  440 HOH   ( 494 )  B      O      0.15    2.55  INTRA BF
 126 ASN   ( 129-)  A      ND2 <->  439 HOH   ( 411 )  A      O      0.13    2.57  INTRA
 224 GLU   (   9-)  B      OE2 <->  404 HIS   ( 189-)  B      NE2    0.12    2.58  INTRA
   6 GLU   (   9-)  A      OE2 <->  186 HIS   ( 189-)  A      NE2    0.10    2.60  INTRA BF
 339 ARG   ( 124-)  B      O   <->  345 GLU   ( 130-)  B      N      0.10    2.60  INTRA
 396 PHE   ( 181-)  B      N   <->  397 GLY   ( 182-)  B      N      0.09    2.51  INTRA BL
 131 GLU   ( 134-)  A      CB  <->  133 GLN   ( 136-)  A      NE2    0.09    3.01  INTRA BF
 178 PHE   ( 181-)  A      N   <->  179 GLY   ( 182-)  A      N      0.08    2.52  INTRA BL
 121 ARG   ( 124-)  A      O   <->  127 GLU   ( 130-)  A      N      0.08    2.62  INTRA BL
 190 GLN   ( 193-)  A      NE2 <->  192 HIS   ( 195-)  A      CE1    0.07    3.03  INTRA BF
 350 PRO   ( 135-)  B      CD  <->  351 GLN   ( 136-)  B      NE2    0.07    3.03  INTRA BF
 415 SER   ( 200-)  B      N   <->  416 ASP   ( 201-)  B      N      0.04    2.56  INTRA BL
 321 VAL   ( 106-)  B      O   <->  325 HIS   ( 110-)  B      N      0.04    2.66  INTRA BF
 294 ILE   (  79-)  B      O   <->  296 ILE   (  81-)  B      N      0.04    2.66  INTRA
  75 GLN   (  78-)  A      CD  <->  215 ILE   ( 218-)  A      CD1    0.04    3.16  INTRA
 346 ASP   ( 131-)  B      CG  <->  347 ILE   ( 132-)  B      N      0.04    2.96  INTRA
  76 ILE   (  79-)  A      O   <->   78 ILE   (  81-)  A      N      0.03    2.67  INTRA BL
  59 LYS   (  62-)  A      NZ  <->  439 HOH   ( 522 )  A      O      0.03    2.67  INTRA BF
 325 HIS   ( 110-)  B      N   <->  326 PRO   ( 111-)  B      CD     0.03    2.97  INTRA BF
 197 SER   ( 200-)  A      N   <->  198 ASP   ( 201-)  A      N      0.03    2.57  INTRA BL
 174 ARG   ( 177-)  A      NH2 <->  439 HOH   ( 564 )  A      O      0.02    2.68  INTRA BF
 103 VAL   ( 106-)  A      O   <->  107 HIS   ( 110-)  A      N      0.02    2.68  INTRA
  31 ASN   (  34-)  A      N   <->  209 GLU   ( 212-)  A      OE2    0.01    2.69  INTRA BF
 175 TYR   ( 178-)  A      N   <->  176 GLY   ( 179-)  A      N      0.01    2.59  INTRA BL
 128 ASP   ( 131-)  A      CG  <->  129 ILE   ( 132-)  A      N      0.01    2.99  INTRA BL

Packing, accessibility and threading

Note: Inside/Outside RMS Z-score plot

The Inside/Outside distribution normality RMS Z-score over a 15 residue window is plotted as function of the residue number. High areas in the plot (above 1.5) indicate unusual inside/outside patterns.

Chain identifier: A

Note: Inside/Outside RMS Z-score plot

Chain identifier: B

Warning: Abnormal packing environment for some residues

The residues listed in the table below have an unusual packing environment.

The packing environment of the residues is compared with the average packing environment for all residues of the same type in good PDB files. A low packing score can indicate one of several things: Poor packing, misthreading of the sequence through the density, crystal contacts, contacts with a co-factor, or the residue is part of the active site. It is not uncommon to see a few of these, but in any case this requires further inspection of the residue.

 430 MET   ( 215-)  B      -6.73
 212 MET   ( 215-)  A      -6.47
 269 LYS   (  54-)  B      -6.09
  51 LYS   (  54-)  A      -6.00
 174 ARG   ( 177-)  A      -5.75
 392 ARG   ( 177-)  B      -5.73
 433 ILE   ( 218-)  B      -5.45
 215 ILE   ( 218-)  A      -5.44

Note: Quality value plot

The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate unusual packing.

Chain identifier: A

Note: Quality value plot

The quality value smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -2.0) indicate unusual packing.

Chain identifier: B

Warning: Low packing Z-score for some residues

The residues listed in the table below have an unusual packing environment according to the 2nd generation packing check. The score listed in the table is a packing normality Z-score: positive means better than average, negative means worse than average. Only residues scoring less than -2.50 are listed here. These are the unusual residues in the structure, so it will be interesting to take a special look at them.

  55 LEU   (  58-)  A   -2.55

Note: Second generation quality Z-score plot

The second generation quality Z-score smoothed over a 10 residue window is plotted as function of the residue number. Low areas in the plot (below -1.3) indicate unusual packing.

Chain identifier: A

Note: Second generation quality Z-score plot

Chain identifier: B

Water, ion, and hydrogenbond related checks

Warning: Water molecules need moving

The water molecules listed in the table below were found to be significantly closer to a symmetry related non-water molecule than to the ones given in the coordinate file. For optimal viewing convenience revised coordinates for these water molecules should be given.

The number in brackets is the identifier of the water molecule in the input file. Suggested coordinates are also given in the table. Please note that alternative conformations for protein residues are not taken into account for this calculation. If you are using WHAT IF / WHAT-CHECK interactively, then the moved waters can be found in PDB format in the file: MOVEDH2O.pdb.

 439 HOH   ( 500 )  A      O      7.33   76.94   32.62

Error: Water molecules without hydrogen bonds

The water molecules listed in the table below do not form any hydrogen bonds, neither with the protein or DNA/RNA, nor with other water molecules. This is a strong indication of a refinement problem. The last number on each line is the identifier of the water molecule in the input file.

 440 HOH   ( 526 )  B      O

Error: HIS, ASN, GLN side chain flips

Listed here are Histidine, Asparagine or Glutamine residues for which the orientation determined from hydrogen bonding analysis are different from the assignment given in the input. Either they could form energetically more favourable hydrogen bonds if the terminal group was rotated by 180 degrees, or there is no assignment in the input file (atom type 'A') but an assignment could be made. Be aware, though, that if the topology could not be determined for one or more ligands, then this option will make errors.

 245 GLN   (  30-)  B
 344 ASN   ( 129-)  B
 368 GLN   ( 153-)  B

Warning: Buried unsatisfied hydrogen bond donors

The buried hydrogen bond donors listed in the table below have a hydrogen atom that is not involved in a hydrogen bond in the optimized hydrogen bond network.

Hydrogen bond donors that are buried inside the protein normally use all of their hydrogens to form hydrogen bonds within the protein. If there are any non hydrogen bonded buried hydrogen bond donors in the structure they will be listed here. In very good structures the number of listed atoms will tend to zero.

Waters are not listed by this option.

  10 ASP   (  13-)  A      N
  13 SER   (  16-)  A      OG
  15 TYR   (  18-)  A      N
  28 ASN   (  31-)  A      N
  50 ASN   (  53-)  A      ND2
 130 THR   ( 133-)  A      N
 147 GLU   ( 150-)  A      N
 180 LEU   ( 183-)  A      N
 199 ARG   ( 202-)  A      N
 211 TRP   ( 214-)  A      NE1
 228 ASP   (  13-)  B      N
 231 SER   (  16-)  B      OG
 233 TYR   (  18-)  B      N
 268 ASN   (  53-)  B      ND2
 348 THR   ( 133-)  B      N
 351 GLN   ( 136-)  B      N
 365 GLU   ( 150-)  B      N
 375 ALA   ( 160-)  B      N
 398 LEU   ( 183-)  B      N
 417 ARG   ( 202-)  B      N
 429 TRP   ( 214-)  B      NE1

Warning: Unusual water packing

We implemented the ion valence determination method of Brown and Wu [REF] similar to Nayal and Di Cera [REF] and Mueller, Koepke and Sheldrick [REF]. It must be stated that the validation of ions in PDB files is very difficult. Ideal ion-ligand distances often differ no more than 0.1 Angstrom, and in a 2.0 Angstrom resolution structure 0.1 Angstrom is not very much. Nayal and Di Cera showed that this method nevertheless has great potential for detecting water molecules that actually should be metal ions. The method has not been extensively validated, though. Part of our implementation (comparing waters with multiple ion types) is even fully new and despite that we see it work well in the few cases that are trivial, we must emphasize that this method is untested.

The score listed is the valency score. This number should be close to (preferably a bit above) 1.0 for the suggested ion to be a likely alternative for the water molecule. Ions listed in brackets are good alternate choices. *1 indicates that the suggested ion-type has been observed elsewhere in the PDB file too. *2 indicates that the suggested ion-type has been observed in the REMARK 280 cards of the PDB file. Ion-B and ION-B indicate that the B-factor of this water is high, or very high, respectively. H2O-B indicates that the B-factors of atoms that surround this water/ion are suspicious. See: swift.cmbi.ru.nl/teach/theory/ for a detailed explanation.

 440 HOH   ( 429 )  B      O  0.94  K  6

Warning: Possible wrong residue type

The residues listed in the table below have a weird environment that cannot be improved by rotamer flips. This can mean one of three things, non of which WHAT CHECK really can do much about. 1) The side chain has actually another rotamer than is present in the PDB file; 2) A counter ion is present in the structure but is not given in the PDB file; 3) The residue actually is another amino acid type. The annotation 'Alt-rotamer' indicates that WHAT CHECK thinks you might want to find an alternate rotamer for this residue. The annotation 'Sym-induced' indicates that WHAT CHECK believes that symmetry contacts might have something to do with the difficulties of this residue's side chain. Determination of these two annotations is difficult, so their absence is less meaningful than their presence. The annotation Ligand-bound indicates that a ligand seems involved with this residue. In nine of ten of these cases this indicates that the ligand is causing the weird situation rather than the residue.

 198 ASP   ( 201-)  A   H-bonding suggests Asn; but Alt-Rotamer; Ligand-contact
 372 GLU   ( 157-)  B   H-bonding suggests Gln
 416 ASP   ( 201-)  B   H-bonding suggests Asn; but Alt-Rotamer; Ligand-contact

Final summary

Note: Summary report for users of a structure

This is an overall summary of the quality of the structure as compared with current reliable structures. This summary is most useful for biologists seeking a good structure to use for modelling calculations.

The second part of the table mostly gives an impression of how well the model conforms to common refinement restraint values. The first part of the table shows a number of global quality indicators.


Structure Z-scores, positive is better than average:

  1st generation packing quality :  -0.075
  2nd generation packing quality :  -1.332
  Ramachandran plot appearance   :  -0.086
  chi-1/chi-2 rotamer normality  :   0.477
  Backbone conformation          :   0.190

RMS Z-scores, should be close to 1.0:
  Bond lengths                   :   0.246 (tight)
  Bond angles                    :   0.554 (tight)
  Omega angle restraints         :   0.191 (tight)
  Side chain planarity           :   0.203 (tight)
  Improper dihedral distribution :   0.507
  B-factor distribution          :   0.434
  Inside/Outside distribution    :   0.935

Note: Summary report for depositors of a structure

This is an overall summary of the quality of the X-ray structure as compared with structures solved at similar resolutions. This summary can be useful for a crystallographer to see if the structure makes the best possible use of the data. Warning. This table works well for structures solved in the resolution range of the structures in the WHAT IF database, which is presently (summer 2008) mainly 1.1 - 1.3 Angstrom. The further the resolution of your file deviates from this range the more meaningless this table becomes.

The second part of the table mostly gives an impression of how well the model conforms to common refinement restraint values. The first part of the table shows a number of global quality indicators, which have been calibrated against structures of similar resolution.

Resolution found in PDB file : 1.93


Structure Z-scores, positive is better than average:

  1st generation packing quality :   0.4
  2nd generation packing quality :  -1.1
  Ramachandran plot appearance   :   0.3
  chi-1/chi-2 rotamer normality  :   0.9
  Backbone conformation          :  -0.1

RMS Z-scores, should be close to 1.0:
  Bond lengths                   :   0.246 (tight)
  Bond angles                    :   0.554 (tight)
  Omega angle restraints         :   0.191 (tight)
  Side chain planarity           :   0.203 (tight)
  Improper dihedral distribution :   0.507
  B-factor distribution          :   0.434
  Inside/Outside distribution    :   0.935
==============

WHAT IF
    G.Vriend,
      WHAT IF: a molecular modelling and drug design program,
    J. Mol. Graph. 8, 52--56 (1990).

WHAT_CHECK (verification routines from WHAT IF)
    R.W.W.Hooft, G.Vriend, C.Sander and E.E.Abola,
      Errors in protein structures
    Nature 381, 272 (1996).
    (see also http://swift.cmbi.ru.nl/gv/whatcheck for a course and extra inform

Bond lengths and angles, protein residues
    R.Engh and R.Huber,
      Accurate bond and angle parameters for X-ray protein structure
      refinement,
    Acta Crystallogr. A47, 392--400 (1991).

Bond lengths and angles, DNA/RNA
    G.Parkinson, J.Voitechovsky, L.Clowney, A.T.Bruenger and H.Berman,
      New parameters for the refinement of nucleic acid-containing structures
    Acta Crystallogr. D52, 57--64 (1996).

DSSP
    W.Kabsch and C.Sander,
      Dictionary of protein secondary structure: pattern
      recognition of hydrogen bond and geometrical features
    Biopolymers 22, 2577--2637 (1983).

Hydrogen bond networks
    R.W.W.Hooft, C.Sander and G.Vriend,
      Positioning hydrogen atoms by optimizing hydrogen bond networks in
      protein structures
    PROTEINS, 26, 363--376 (1996).

Matthews' Coefficient
    B.W.Matthews
      Solvent content of Protein Crystals
    J. Mol. Biol. 33, 491--497 (1968).

Protein side chain planarity
    R.W.W. Hooft, C. Sander and G. Vriend,
      Verification of protein structures: side-chain planarity
    J. Appl. Cryst. 29, 714--716 (1996).

Puckering parameters
    D.Cremer and J.A.Pople,
      A general definition of ring puckering coordinates
    J. Am. Chem. Soc. 97, 1354--1358 (1975).

Quality Control
    G.Vriend and C.Sander,
      Quality control of protein models: directional atomic
      contact analysis,
    J. Appl. Cryst. 26, 47--60 (1993).

Ramachandran plot
    G.N.Ramachandran, C.Ramakrishnan and V.Sasisekharan,
      Stereochemistry of Polypeptide Chain Conformations
    J. Mol. Biol. 7, 95--99 (1963).

Symmetry Checks
    R.W.W.Hooft, C.Sander and G.Vriend,
      Reconstruction of symmetry related molecules from protein
      data bank (PDB) files
    J. Appl. Cryst. 27, 1006--1009 (1994).

Ion Checks
    I.D.Brown and K.K.Wu,
      Empirical Parameters for Calculating Cation-Oxygen Bond Valences
    Acta Cryst. B32, 1957--1959 (1975).

    M.Nayal and E.Di Cera,
      Valence Screening of Water in Protein Crystals Reveals Potential Na+
      Binding Sites
    J.Mol.Biol. 256 228--234 (1996).

    P.Mueller, S.Koepke and G.M.Sheldrick,
      Is the bond-valence method able to identify metal atoms in protein
      structures?
    Acta Cryst. D 59 32--37 (2003).

Checking checks
    K.Wilson, C.Sander, R.W.W.Hooft, G.Vriend, et al.
      Who checks the checkers
    J.Mol.Biol. (1998) 276,417-436.