WHAT IF Check report

This file was created 2011-12-18 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 pdb2zjc.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 C

All-atom RMS fit for the two chains : 1.685
CA-only RMS fit for the two chains : 1.228

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 C

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.

 439 GOL   ( 158-)  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

Note: Ramachandran plot

Chain identifier: C

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. The header of the PDB file states that TLS groups were used. So, if WHAT IF complains about your B-factors, while 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:


Number of TLS groups mentione in PDB file header: 3

Crystal temperature (K) :100.000

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

Note: B-factor plot

Chain identifier: C

Nomenclature related problems

Warning: Tyrosine convention problem

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

  52 TYR   (  59-)  A
  80 TYR   (  87-)  A
 104 TYR   ( 119-)  A
 126 TYR   ( 141-)  A
 136 TYR   ( 151-)  A
 251 TYR   ( 115-)  B
 277 TYR   ( 141-)  B
 419 TYR   ( 141-)  C

Warning: Phenylalanine convention problem

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

 109 PHE   ( 124-)  A
 200 PHE   (  64-)  B
 260 PHE   ( 124-)  B
 402 PHE   ( 124-)  C
 422 PHE   ( 144-)  C

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.

  38 ASP   (  45-)  A
 128 ASP   ( 143-)  A
 279 ASP   ( 143-)  B
 296 ASP   (  10-)  C
 421 ASP   ( 143-)  C

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.

  35 GLU   (  42-)  A
  46 GLU   (  53-)  A
 240 GLU   ( 104-)  B
 243 GLU   ( 107-)  B
 263 GLU   ( 127-)  B
 405 GLU   ( 127-)  C
 413 GLU   ( 135-)  C

Geometric checks

Warning: Possible cell scaling problem

Comparison of bond distances with Engh and Huber [REF] standard values for protein residues and Parkinson et al [REF] values for DNA/RNA shows a significant systematic deviation. It could be that the unit cell used in refinement was not accurate enough. The deformation matrix given below gives the deviations found: the three numbers on the diagonal represent the relative corrections needed along the A, B and C cell axis. These values are 1.000 in a normal case, but have significant deviations here (significant at the 99.99 percent confidence level)

There are a number of different possible causes for the discrepancy. First the cell used in refinement can be different from the best cell calculated. Second, the value of the wavelength used for a synchrotron data set can be miscalibrated. Finally, the discrepancy can be caused by a dataset that has not been corrected for significant anisotropic thermal motion.

Please note that the proposed scale matrix has NOT been restrained to obey the space group symmetry. This is done on purpose. The distortions can give you an indication of the accuracy of the determination.

If you intend to use the result of this check to change the cell dimension of your crystal, please read the extensive literature on this topic first. This check depends on the wavelength, the cell dimensions, and on the standard bond lengths and bond angles used by your refinement software.

Unit Cell deformation matrix

 |  0.998729 -0.000079  0.000532|
 | -0.000079  0.997137 -0.000239|
 |  0.000532 -0.000239  0.997911|
Proposed new scale matrix

 |  0.007370  0.004262 -0.000003|
 |  0.000000  0.008522  0.000002|
 | -0.000009  0.000004  0.017271|
With corresponding cell

    A    = 135.692  B   = 135.546  C    =  57.900
    Alpha=  90.054  Beta=  89.939  Gamma= 120.041

The CRYST1 cell dimensions

    A    = 135.873  B   = 135.873  C    =  58.023
    Alpha=  90.000  Beta=  90.000  Gamma= 120.000

Variance: 62.172
(Under-)estimated Z-score: 5.811

Warning: Unusual bond angles

The bond angles listed in the table below were found to deviate more than 4 sigma from standard bond angles (both standard values and sigma for protein residues have been taken from Engh and Huber [REF], for DNA/RNA from Parkinson et al [REF]). In the table below for each strange angle the bond angle and the number of standard deviations it differs from the standard values is given. Please note that disulphide bridges are neglected. Atoms starting with "-" belong to the previous residue in the sequence.

 281 ALA   ( 145-)  B      N    CA   C    98.50   -4.5
 387 CYS   ( 101-)  C      N    CA   C   124.37    4.7

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.

  35 GLU   (  42-)  A
  38 ASP   (  45-)  A
  46 GLU   (  53-)  A
 128 ASP   ( 143-)  A
 240 GLU   ( 104-)  B
 243 GLU   ( 107-)  B
 263 GLU   ( 127-)  B
 279 ASP   ( 143-)  B
 296 ASP   (  10-)  C
 405 GLU   ( 127-)  C
 413 GLU   ( 135-)  C
 421 ASP   ( 143-)  C

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.

 281 ALA   ( 145-)  B    5.35
 387 CYS   ( 101-)  C    5.02

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.

  82 THR   (  89-)  A    -3.2
 283 THR   ( 147-)  B    -2.7
 432 ILE   ( 154-)  C    -2.6
 365 THR   (  79-)  C    -2.5
 280 PHE   ( 144-)  B    -2.4
 160 GLY   (  24-)  B    -2.4
 298 PRO   (  12-)  C    -2.4
 173 LEU   (  37-)  B    -2.4
 310 GLY   (  24-)  C    -2.4
  30 LEU   (  37-)  A    -2.3
 129 PHE   ( 144-)  A    -2.3
 199 LEU   (  63-)  B    -2.2
 156 PRO   (  20-)  B    -2.2
 349 LEU   (  63-)  C    -2.2
 267 ARG   ( 131-)  B    -2.1
 295 SER   (   9-)  C    -2.1
 371 VAL   (  85-)  C    -2.1
 111 LEU   ( 126-)  A    -2.1
 162 LEU   (  26-)  B    -2.1
   6 VAL   (  13-)  A    -2.1
 271 GLU   ( 135-)  B    -2.1
 272 ILE   ( 136-)  B    -2.1
  56 LEU   (  63-)  A    -2.0
 105 LEU   ( 120-)  A    -2.0
  75 ARG   (  82-)  A    -2.0
 140 ILE   ( 155-)  A    -2.0
 399 GLY   ( 121-)  C    -2.0
 398 LEU   ( 120-)  C    -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.

   2 SER   (   9-)  A  Poor phi/psi, omega poor
  39 ASN   (  46-)  A  Poor phi/psi
  49 TYR   (  56-)  A  omega poor
  72 THR   (  79-)  A  omega poor
  81 GLN   (  88-)  A  Poor phi/psi
  94 CYS   ( 101-)  A  omega poor
 159 GLU   (  23-)  B  Poor phi/psi
 160 GLY   (  24-)  B  Poor phi/psi, omega poor
 175 ASN   (  39-)  B  Poor phi/psi
 182 ASN   (  46-)  B  Poor phi/psi
 207 SER   (  71-)  B  Poor phi/psi
 236 PRO   ( 100-)  B  omega poor
 270 ALA   ( 134-)  B  omega poor
 279 ASP   ( 143-)  B  omega poor
 280 PHE   ( 144-)  B  Poor phi/psi, omega poor
 295 SER   (   9-)  C  Poor phi/psi
 310 GLY   (  24-)  C  Poor phi/psi
 319 ALA   (  33-)  C  omega poor
 320 ASN   (  34-)  C  Poor phi/psi
 323 LEU   (  37-)  C  Poor phi/psi
 325 ASN   (  39-)  C  Poor phi/psi
 332 ASN   (  46-)  C  Poor phi/psi
 342 TYR   (  56-)  C  omega poor
 387 CYS   ( 101-)  C  omega poor
 chi-1/chi-2 correlation Z-score : -3.853

Warning: chi-1/chi-2 angle correlation Z-score low

The score expressing how well the chi-1/chi-2 angles of all residues correspond to the populated areas in the database is a bit low.

chi-1/chi-2 correlation Z-score : -3.853

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!

   3 ASP   (  10-)  A      0
   5 PRO   (  12-)  A      0
  15 ALA   (  22-)  A      0
  16 GLU   (  23-)  A      0
  22 LYS   (  29-)  A      0
  24 ALA   (  31-)  A      0
  27 ASN   (  34-)  A      0
  30 LEU   (  37-)  A      0
  31 ALA   (  38-)  A      0
  32 ASN   (  39-)  A      0
  37 ARG   (  44-)  A      0
  39 ASN   (  46-)  A      0
  44 PRO   (  51-)  A      0
  46 GLU   (  53-)  A      0
  52 TYR   (  59-)  A      0
  58 SER   (  65-)  A      0
  60 GLN   (  67-)  A      0
  62 CYS   (  69-)  A      0
  63 PRO   (  70-)  A      0
  65 THR   (  72-)  A      0
  66 HIS   (  73-)  A      0
  81 GLN   (  88-)  A      0
  87 LEU   (  94-)  A      0
  94 CYS   ( 101-)  A      0
  95 GLN   ( 102-)  A      0
And so on for a total of 212 lines.

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!

 399 GLY   ( 121-)  C   1.53   16

Warning: Unusual PRO puckering phases

The proline residues listed in the table below have a puckering phase that is not expected to occur in protein structures. Puckering parameters were calculated by the method of Cremer and Pople [REF]. Normal PRO rings approximately show a so-called envelope conformation with the C-gamma atom above the plane of the ring (phi=+72 degrees), or a half-chair conformation with C-gamma below and C-beta above the plane of the ring (phi=-90 degrees). If phi deviates strongly from these values, this is indicative of a very strange conformation for a PRO residue, and definitely requires a manual check of the data. Be aware that this is a warning with a low confidence level. See: Who checks the checkers? Four validation tools applied to eight atomic resolution structures [REF].

   1 PRO   (   8-)  A   137.5 envelop C-alpha (144 degrees)
 144 PRO   (   8-)  B    47.3 half-chair C-delta/C-gamma (54 degrees)
 148 PRO   (  12-)  B   102.1 envelop C-beta (108 degrees)
 156 PRO   (  20-)  B    39.9 envelop C-delta (36 degrees)
 187 PRO   (  51-)  B   -52.7 half-chair C-beta/C-alpha (-54 degrees)
 253 PRO   ( 117-)  B   -42.4 envelop C-alpha (-36 degrees)
 298 PRO   (  12-)  C   108.8 envelop C-beta (108 degrees)
 337 PRO   (  51-)  C   -64.2 envelop C-beta (-72 degrees)
 356 PRO   (  70-)  C  -128.8 half-chair C-delta/C-gamma (-126 degrees)

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.

 205 CYS   (  69-)  B      N   <->  241 THR   ( 105-)  B      CG2    0.23    2.87  INTRA
 234 ARG   (  98-)  B      NH2 <->  440 HOH   ( 209 )  A      O      0.21    2.49  INTRA
 158 ALA   (  22-)  B      O   <->  160 GLY   (  24-)  B      N      0.21    2.49  INTRA
 301 HIS   (  15-)  C      ND1 <->  345 TYR   (  59-)  C      OH     0.21    2.49  INTRA BL
   8 HIS   (  15-)  A      ND1 <->   52 TYR   (  59-)  A      OH     0.21    2.49  INTRA BL
 214 HIS   (  78-)  B      ND1 <->  256 LEU   ( 120-)  B      CD2    0.20    2.90  INTRA BL
 280 PHE   ( 144-)  B      CB  <->  281 ALA   ( 145-)  B      CA     0.19    2.81  INTRA
 354 GLY   (  68-)  C      O   <->  392 TRP   ( 114-)  C      NE1    0.18    2.52  INTRA
  68 LEU   (  75-)  A      O   <->  122 ASN   ( 137-)  A      ND2    0.18    2.52  INTRA
 336 VAL   (  50-)  C      O   <->  407 GLY   ( 129-)  C      N      0.15    2.55  INTRA BL
   1 PRO   (   8-)  A      O   <->    3 ASP   (  10-)  A      N      0.14    2.56  INTRA
  48 LEU   (  55-)  A      O   <->  142 LEU   ( 157-)  A      N      0.14    2.56  INTRA BL
  66 HIS   (  73-)  A      NE2 <->  249 PRO   ( 113-)  B      O      0.14    2.56  INTRA
  88 SER   (  95-)  A      N   <->  284 GLY   ( 148-)  B      O      0.12    2.58  INTRA BL
 332 ASN   (  46-)  C      N   <->  442 HOH   ( 213 )  C      O      0.11    2.59  INTRA
  75 ARG   (  82-)  A      NH1 <->  115 ASP   ( 130-)  A      OD2    0.11    2.59  INTRA
 305 ASN   (  19-)  C      N   <->  313 GLN   (  27-)  C      O      0.10    2.60  INTRA
 263 GLU   ( 127-)  B      N   <->  266 ASP   ( 130-)  B      OD2    0.09    2.61  INTRA BL
 312 LEU   (  26-)  C      N   <->  442 HOH   ( 180 )  C      O      0.09    2.61  INTRA
 331 ASP   (  45-)  C      N   <->  442 HOH   ( 204 )  C      O      0.07    2.63  INTRA
  43 VAL   (  50-)  A      O   <->  114 GLY   ( 129-)  A      N      0.07    2.63  INTRA BL
  93 PRO   ( 100-)  A      C   <->   94 CYS   ( 101-)  A      SG     0.07    3.23  INTRA
 362 LEU   (  76-)  C      O   <->  384 ARG   (  98-)  C      N      0.07    2.63  INTRA BL
  97 ASN   ( 112-)  A      CG  <->  359 HIS   (  73-)  C      CG     0.06    3.14  INTRA
 330 ARG   (  44-)  C      O   <->  333 GLN   (  47-)  C      N      0.06    2.64  INTRA BL
And so on for a total of 52 lines.

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

Note: Inside/Outside RMS Z-score plot

Chain identifier: C

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.

 157 GLN   (  21-)  B      -7.07
  81 GLN   (  88-)  A      -6.21
  60 GLN   (  67-)  A      -5.98
 373 TYR   (  87-)  C      -5.61
 238 GLN   ( 102-)  B      -5.56
 353 GLN   (  67-)  C      -5.42
 374 GLN   (  88-)  C      -5.27
 224 GLN   (  88-)  B      -5.22
 161 GLN   (  25-)  B      -5.16
 203 GLN   (  67-)  B      -5.08
 309 GLU   (  23-)  C      -5.01

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

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: C

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.

 280 PHE   ( 144-)  B   -2.55
  66 HIS   (  73-)  A   -2.52
 160 GLY   (  24-)  B   -2.51

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

Note: Second generation quality Z-score plot

Chain identifier: C

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.

 440 HOH   ( 158 )  A      O      6.30   -0.48    4.53

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   ( 158 )  A      O
 440 HOH   ( 198 )  A      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.

  27 ASN   (  34-)  A
 175 ASN   (  39-)  B
 214 HIS   (  78-)  B
 353 GLN   (  67-)  C

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.

   4 MET   (  11-)  A      N
  18 GLN   (  25-)  A      N
  24 ALA   (  31-)  A      N
  45 SER   (  52-)  A      N
  45 SER   (  52-)  A      OG
  48 LEU   (  55-)  A      N
  56 LEU   (  63-)  A      N
  67 VAL   (  74-)  A      N
  85 ASN   (  92-)  A      ND2
  90 ILE   (  97-)  A      N
  94 CYS   ( 101-)  A      N
 131 SER   ( 146-)  A      N
 145 SER   (   9-)  B      N
 162 LEU   (  26-)  B      N
 170 ASN   (  34-)  B      N
 188 SER   (  52-)  B      N
 199 LEU   (  63-)  B      N
 203 GLN   (  67-)  B      NE2
 205 CYS   (  69-)  B      N
 207 SER   (  71-)  B      N
 210 VAL   (  74-)  B      N
 223 TYR   (  87-)  B      N
 233 ILE   (  97-)  B      N
 237 CYS   ( 101-)  B      N
 255 TYR   ( 119-)  B      N
 270 ALA   ( 134-)  B      N
 278 LEU   ( 142-)  B      N
 280 PHE   ( 144-)  B      N
 295 SER   (   9-)  C      N
 297 MET   (  11-)  C      N
 317 ALA   (  31-)  C      N
 321 ALA   (  35-)  C      N
 325 ASN   (  39-)  C      ND2
 338 SER   (  52-)  C      N
 349 LEU   (  63-)  C      N
 358 THR   (  72-)  C      N
 359 HIS   (  73-)  C      N
 371 VAL   (  85-)  C      N
 373 TYR   (  87-)  C      N
 378 ASN   (  92-)  C      ND2
 383 ILE   (  97-)  C      N
 416 ARG   ( 138-)  C      NH1
 416 ARG   ( 138-)  C      NH2
 424 SER   ( 146-)  C      N
 426 GLY   ( 148-)  C      N

Warning: Buried unsatisfied hydrogen bond acceptors

The buried side-chain hydrogen bond acceptors listed in the table below are not involved in a hydrogen bond in the optimized hydrogen bond network.

Side-chain hydrogen bond acceptors buried inside the protein normally form hydrogen bonds within the protein. If there are any not hydrogen bonded in the optimized hydrogen bond network they will be listed here.

Waters are not listed by this option.

 252 GLU   ( 116-)  B      OE1
 261 GLN   ( 125-)  B      OE1
 364 HIS   (  78-)  C      ND1

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.

   3 ASP   (  10-)  A   H-bonding suggests Asn; but Alt-Rotamer
 252 GLU   ( 116-)  B   H-bonding suggests Gln
 279 ASP   ( 143-)  B   H-bonding suggests Asn
 413 GLU   ( 135-)  C   H-bonding suggests Gln

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 :  -0.435
  2nd generation packing quality :  -2.099
  Ramachandran plot appearance   :  -2.141
  chi-1/chi-2 rotamer normality  :  -3.853 (poor)
  Backbone conformation          :  -0.217

RMS Z-scores, should be close to 1.0:
  Bond lengths                   :   0.440 (tight)
  Bond angles                    :   0.627 (tight)
  Omega angle restraints         :   1.190
  Side chain planarity           :   0.340 (tight)
  Improper dihedral distribution :   0.618
  B-factor distribution          :   0.370
  Inside/Outside distribution    :   0.943

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 : 2.50


Structure Z-scores, positive is better than average:

  1st generation packing quality :   0.5
  2nd generation packing quality :  -0.7
  Ramachandran plot appearance   :  -0.1
  chi-1/chi-2 rotamer normality  :  -1.9
  Backbone conformation          :   0.1

RMS Z-scores, should be close to 1.0:
  Bond lengths                   :   0.440 (tight)
  Bond angles                    :   0.627 (tight)
  Omega angle restraints         :   1.190
  Side chain planarity           :   0.340 (tight)
  Improper dihedral distribution :   0.618
  B-factor distribution          :   0.370
  Inside/Outside distribution    :   0.943
==============

WHAT IF
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WHAT_CHECK (verification routines from WHAT IF)
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    (see also http://swift.cmbi.ru.nl/gv/whatcheck for a course and extra inform

Bond lengths and angles, protein residues
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Bond lengths and angles, DNA/RNA
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DSSP
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Hydrogen bond networks
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      protein structures
    PROTEINS, 26, 363--376 (1996).

Matthews' Coefficient
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      Solvent content of Protein Crystals
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Protein side chain planarity
    R.W.W. Hooft, C. Sander and G. Vriend,
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    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,
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      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.