WHAT IF Check report

This file was created 2012-01-13 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 pdb1uhf.ent

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; Model number 1

Note: Ramachandran plot

Chain identifier: A; Model number 2

Note: Ramachandran plot

Chain identifier: A; Model number 3

Note: Ramachandran plot

Chain identifier: A; Model number 4

Note: Ramachandran plot

Chain identifier: A; Model number 5

Note: Ramachandran plot

Chain identifier: A; Model number 6

Note: Ramachandran plot

Chain identifier: A; Model number 7

Note: Ramachandran plot

Chain identifier: A; Model number 8

Note: Ramachandran plot

Chain identifier: A; Model number 9

Note: Ramachandran plot

Chain identifier: A; Model number 10

Note: Ramachandran plot

Chain identifier: A; Model number 11

Note: Ramachandran plot

Chain identifier: A; Model number 12

Note: Ramachandran plot

Chain identifier: A; Model number 13

Note: Ramachandran plot

Chain identifier: A; Model number 14

Note: Ramachandran plot

Chain identifier: A; Model number 15

Note: Ramachandran plot

Chain identifier: A; Model number 16

Note: Ramachandran plot

Chain identifier: A; Model number 17

Note: Ramachandran plot

Chain identifier: A; Model number 18

Note: Ramachandran plot

Chain identifier: A; Model number 19

Note: Ramachandran plot

Chain identifier: A; Model number 20

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

Warning: B-factors outside the range 0.0 - 100.0

In principle, B-factors can have a very wide range of values, but in practice, B-factors should not be zero while B-factors above 100.0 are a good indicator that the location of that atom is meaningless. Be aware that the cutoff at 100.0 is arbitrary. 'High' indicates that atoms with a B-factor > 100.0 were observed; 'Zero' indicates that atoms with a B-factor of zero were observed.

   1 GLY   (   1-)  A    Zero
   2 SER   (   2-)  A    Zero
   3 SER   (   3-)  A    Zero
   4 GLY   (   4-)  A    Zero
   5 SER   (   5-)  A    Zero
   6 SER   (   6-)  A    Zero
   7 GLY   (   7-)  A    Zero
   8 GLY   (   8-)  A    Zero
   9 GLU   (   9-)  A    Zero
  10 GLU   (  10-)  A    Zero
  11 TYR   (  11-)  A    Zero
  12 ILE   (  12-)  A    Zero
  13 ALA   (  13-)  A    Zero
  14 LEU   (  14-)  A    Zero
  15 TYR   (  15-)  A    Zero
  16 PRO   (  16-)  A    Zero
  17 TYR   (  17-)  A    Zero
  18 SER   (  18-)  A    Zero
  19 SER   (  19-)  A    Zero
  20 VAL   (  20-)  A    Zero
  21 GLU   (  21-)  A    Zero
  22 PRO   (  22-)  A    Zero
  23 GLY   (  23-)  A    Zero
  24 ASP   (  24-)  A    Zero
  25 LEU   (  25-)  A    Zero
And so on for a total of 1380 lines.

Geometric checks

Note: Per-model averages for bond-length check

The table below gives the per-model bond-length RMS Z-scores.

Model 1 : 0.521
Model 2 : 0.522
Model 3 : 0.523
Model 4 : 0.521
Model 5 : 0.522
Model 6 : 0.523
Model 7 : 0.521
Model 8 : 0.523
Model 9 : 0.521
Model 10 : 0.522
Model 11 : 0.522
Model 12 : 0.521
Model 13 : 0.524
Model 14 : 0.522
Model 15 : 0.521
Model 16 : 0.522
Model 17 : 0.522
Model 18 : 0.522
Model 19 : 0.521
Model 20 : 0.522

Warning: Directionality in bond lengths

Comparison of bond distances with Engh and Huber [REF] standard values for protein residues and Parkinson et al [REF] standard values for DNA/RNA shows a significant systematic deviation.

Since this is not an XRAY structure this effect is hard to explain.

Note: Per-model averages for bond-angle check

The table below gives the per-model bond-angle RMS Z-scores.

Model 1 : 0.923
Model 2 : 0.923
Model 3 : 0.923
Model 4 : 0.922
Model 5 : 0.923
Model 6 : 0.923
Model 7 : 0.923
Model 8 : 0.923
Model 9 : 0.923
Model 10 : 0.922
Model 11 : 0.924
Model 12 : 0.922
Model 13 : 0.923
Model 14 : 0.923
Model 15 : 0.923
Model 16 : 0.923
Model 17 : 0.923
Model 18 : 0.922
Model 19 : 0.923
Model 20 : 0.923

Note: Per-model averages for chirality check

The table below gives the per-model improper dihedral RMS Z-scores.

Model 1 : 0.701
Model 2 : 0.702
Model 3 : 0.702
Model 4 : 0.701
Model 5 : 0.699
Model 6 : 0.701
Model 7 : 0.702
Model 8 : 0.702
Model 9 : 0.700
Model 10 : 0.701
Model 11 : 0.700
Model 12 : 0.700
Model 13 : 0.698
Model 14 : 0.700
Model 15 : 0.701
Model 16 : 0.702
Model 17 : 0.700
Model 18 : 0.702
Model 19 : 0.701
Model 20 : 0.700

Torsion-related checks

Error: Ramachandran Z-score very low

The score expressing how well the backbone conformations of all residues correspond to the known allowed areas in the Ramachandran plot is very low.

Ramachandran Z-score : -4.628

Note: Per-model averages for Ramachandran check

The table below gives the per-model Ramachandran Z-scores.

Model 1 : -4.497
Model 2 : -4.012
Model 3 : -4.871
Model 4 : -4.251
Model 5 : -5.172
Model 6 : -4.164
Model 7 : -5.316
Model 8 : -4.976
Model 9 : -5.016
Model 10 : -4.825
Model 11 : -4.720
Model 12 : -4.544
Model 13 : -4.426
Model 14 : -4.596
Model 15 : -4.613
Model 16 : -4.854
Model 17 : -4.730
Model 18 : -3.615
Model 19 : -5.024
Model 20 : -4.341

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.

  71 SER   (   2-)  A    -2.7
 555 SER   (   3-)  A    -2.7
 758 SER   (  68-)  A 1   -2.6
 137 SER   (  68-)  A    -2.6
 485 SER   (   2-)  A    -2.6
 420 SER   (   6-)  A    -2.6
 619 SER   (  67-)  A    -2.6
  74 SER   (   5-)  A    -2.6
 964 SER   (  67-)  A 1   -2.6
 830 SER   (   2-)  A 1   -2.6
1123 SER   (  19-)  A 1   -2.5
1099 SER   (  64-)  A 1   -2.5
 279 SER   (   3-)  A    -2.5
 133 SER   (  64-)  A    -2.5
1261 SER   (  19-)  A 1   -2.4
 551 SER   (  68-)  A    -2.4
 764 SER   (   5-)  A 1   -2.4
1192 SER   (  19-)  A 1   -2.4
 350 SER   (   5-)  A    -2.4
1054 SER   (  19-)  A 1   -2.3
1179 SER   (   6-)  A 1   -2.3
1309 SER   (  67-)  A 1   -2.3
1033 SER   (  67-)  A 1   -2.3
 132 ASP   (  63-)  A    -2.3
 709 SER   (  19-)  A 1   -2.3
And so on for a total of 101 lines.

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   (   2-)  A  Poor phi/psi
   8 GLY   (   8-)  A  Poor phi/psi
 117 GLY   (  48-)  A  Poor phi/psi
 132 ASP   (  63-)  A  Poor phi/psi
 133 SER   (  64-)  A  Poor phi/psi
 137 SER   (  68-)  A  Poor phi/psi
 186 GLY   (  48-)  A  Poor phi/psi
 201 ASP   (  63-)  A  Poor phi/psi
 271 SER   (  64-)  A  Poor phi/psi
 275 SER   (  68-)  A  Poor phi/psi
 332 SER   (  56-)  A  Poor phi/psi
 339 ASP   (  63-)  A  Poor phi/psi
 340 SER   (  64-)  A  Poor phi/psi
 420 SER   (   6-)  A  Poor phi/psi
 463 ASP   (  49-)  A  Poor phi/psi
 480 PRO   (  66-)  A  Poor phi/psi
 485 SER   (   2-)  A  Poor phi/psi
 531 GLY   (  48-)  A  Poor phi/psi
 539 SER   (  56-)  A  Poor phi/psi
 572 VAL   (  20-)  A  Poor phi/psi
 574 PRO   (  22-)  A  Poor phi/psi
 575 GLY   (  23-)  A  Poor phi/psi
 619 SER   (  67-)  A  Poor phi/psi
 640 SER   (  19-)  A 1 Poor phi/psi
 641 VAL   (  20-)  A 1 Poor phi/psi
And so on for a total of 78 lines.

Error: chi-1/chi-2 angle correlation Z-score very low

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

chi-1/chi-2 correlation Z-score : -6.106

Note: Per-model averages for chi-1/chi-2 angle check

The table below gives the per-model chi-1/chi-2 correlation Z-scores.

Model 1 : -6.106
Model 2 : -5.770
Model 3 : -7.006
Model 4 : -6.121
Model 5 : -6.301
Model 6 : -6.053
Model 7 : -5.800
Model 8 : -5.652
Model 9 : -6.905
Model 10 : -6.322
Model 11 : -6.316
Model 12 : -5.783
Model 13 : -5.171
Model 14 : -6.129
Model 15 : -6.655
Model 16 : -5.308
Model 17 : -6.455
Model 18 : -6.080
Model 19 : -5.914
Model 20 : -6.270

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!

   5 SER   (   5-)  A      0
   6 SER   (   6-)  A      0
   9 GLU   (   9-)  A      0
  14 LEU   (  14-)  A      0
  15 TYR   (  15-)  A      0
  20 VAL   (  20-)  A      0
  21 GLU   (  21-)  A      0
  29 GLU   (  29-)  A      0
  37 GLN   (  37-)  A      0
  39 ASP   (  39-)  A      0
  41 GLU   (  41-)  A      0
  42 TRP   (  42-)  A      0
  49 ASP   (  49-)  A      0
  51 SER   (  51-)  A      0
  53 ILE   (  53-)  A      0
  58 TYR   (  58-)  A      0
  67 SER   (  67-)  A      0
  68 SER   (  68-)  A      0
  69 GLY   (  69-)  A      0
  70 GLY   (   1-)  A      0
  71 SER   (   2-)  A      0
  72 SER   (   3-)  A      0
  74 SER   (   5-)  A      0
  75 SER   (   6-)  A      0
  84 TYR   (  15-)  A      0
And so on for a total of 638 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 : 0.000

Note: Per-model averages for omega angle check

The table below gives the per-model omega angle standard deviations.

Model 1 : 0.106
Model 2 : 0.000
Model 3 : 0.000
Model 4 : 0.000
Model 5 : 0.037
Model 6 : 0.000
Model 7 : 0.109
Model 8 : 0.039
Model 9 : 0.179
Model 10 : 0.089
Model 11 : 0.072
Model 12 : 0.073
Model 13 : 0.057
Model 14 : 0.000
Model 15 : 0.080
Model 16 : 0.000
Model 17 : 0.000
Model 18 : 0.073
Model 19 : 0.000
Model 20 : 0.000

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!

 490 GLY   (   7-)  A   3.45   19
  73 GLY   (   4-)  A   3.13   12
 341 GLY   (  65-)  A   2.14   16
1039 GLY   (   4-)  A 1  1.94   11
 766 GLY   (   7-)  A 1  1.79   23
1042 GLY   (   7-)  A 1  1.77   15
1376 GLY   (  65-)  A 2  1.68   20
 832 GLY   (   4-)  A 1  1.65   13
 146 GLY   (   8-)  A   1.60   16
 211 GLY   (   4-)  A   1.55   14
 835 GLY   (   7-)  A 1  1.55   19
 697 GLY   (   7-)  A 1  1.52   65

Warning: Unusual PRO puckering amplitudes

The proline residues listed in the table below have a puckering amplitude that is outside of normal ranges. Puckering parameters were calculated by the method of Cremer and Pople [REF]. Normal PRO rings have a puckering amplitude Q between 0.20 and 0.45 Angstrom. If Q is lower than 0.20 Angstrom for a PRO residue, this could indicate disorder between the two different normal ring forms (with C-gamma below and above the ring, respectively). If Q is higher than 0.45 Angstrom something could have gone wrong during the refinement. 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]

  16 PRO   (  16-)  A    0.18 LOW
  22 PRO   (  22-)  A    0.18 LOW
  55 PRO   (  55-)  A    0.18 LOW
  61 PRO   (  61-)  A    0.18 LOW
  66 PRO   (  66-)  A    0.18 LOW
  85 PRO   (  16-)  A    0.18 LOW
  91 PRO   (  22-)  A    0.18 LOW
 124 PRO   (  55-)  A    0.18 LOW
 130 PRO   (  61-)  A    0.18 LOW
 135 PRO   (  66-)  A    0.18 LOW
 154 PRO   (  16-)  A    0.18 LOW
 160 PRO   (  22-)  A    0.18 LOW
 193 PRO   (  55-)  A    0.18 LOW
 199 PRO   (  61-)  A    0.18 LOW
 204 PRO   (  66-)  A    0.18 LOW
 223 PRO   (  16-)  A    0.18 LOW
 229 PRO   (  22-)  A    0.18 LOW
 262 PRO   (  55-)  A    0.18 LOW
 268 PRO   (  61-)  A    0.18 LOW
 273 PRO   (  66-)  A    0.18 LOW
 292 PRO   (  16-)  A    0.18 LOW
 298 PRO   (  22-)  A    0.18 LOW
 331 PRO   (  55-)  A    0.18 LOW
 337 PRO   (  61-)  A    0.18 LOW
 342 PRO   (  66-)  A    0.18 LOW
And so on for a total of 100 lines.

Bump checks

Error: Abnormally short interatomic distances

The pairs of atoms listed in the table below have an unusually short distance.

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).

Bumps between atoms for which the sum of their occupancies is lower than one are not reported. In any case, each bump is listed in only one direction. However, as this seems to be an NMR structure, this is unlikely to happen in this report.

 801 TRP   (  42-)  A 1    CE3 <->  813 PHE   (  54-)  A 1    C      0.32    2.88
1067 GLU   (  32-)  A 1    CD  <-> 1097 LYS   (  62-)  A 1    NZ     0.31    2.79
 675 PHE   (  54-)  A 1    CE1 <->  680 VAL   (  59-)  A 1    CG1    0.30    2.90
 908 TYR   (  11-)  A 1    CD2 <->  957 LYS   (  60-)  A 1    C      0.30    2.90
 701 TYR   (  11-)  A 1    CD2 <->  750 LYS   (  60-)  A 1    C      0.29    2.91
 929 GLU   (  32-)  A 1    CD  <->  959 LYS   (  62-)  A 1    NZ     0.29    2.81
1184 TYR   (  11-)  A 1    CD2 <-> 1233 LYS   (  60-)  A 1    C      0.29    2.91
  80 TYR   (  11-)  A      CD2 <->  129 LYS   (  60-)  A      C      0.28    2.92
 977 TYR   (  11-)  A 1    CD2 <-> 1026 LYS   (  60-)  A 1    C      0.27    2.93
 563 TYR   (  11-)  A      CD2 <->  612 LYS   (  60-)  A      C      0.26    2.94
 813 PHE   (  54-)  A 1    CE1 <->  818 VAL   (  59-)  A 1    CG1    0.26    2.94
 356 TYR   (  11-)  A      CD2 <->  405 LYS   (  60-)  A      C      0.26    2.94
1115 TYR   (  11-)  A 1    CD2 <-> 1164 LYS   (  60-)  A 1    C      0.26    2.94
  11 TYR   (  11-)  A      CD2 <->   60 LYS   (  60-)  A      C      0.26    2.94
1046 TYR   (  11-)  A 1    CD2 <-> 1095 LYS   (  60-)  A 1    C      0.25    2.95
 456 TRP   (  42-)  A      CE3 <->  468 PHE   (  54-)  A      C      0.24    2.96
 468 PHE   (  54-)  A      CE1 <->  473 VAL   (  59-)  A      CG1    0.23    2.97
1151 ILE   (  47-)  A 1    O   <-> 1153 ASP   (  49-)  A 1    N      0.23    2.47
 806 ILE   (  47-)  A 1    O   <->  808 ASP   (  49-)  A 1    N      0.22    2.48
 875 ILE   (  47-)  A 1    O   <->  877 ASP   (  49-)  A 1    N      0.22    2.48
 865 GLN   (  37-)  A 1    O   <->  872 THR   (  44-)  A 1    N      0.22    2.48
 944 ILE   (  47-)  A 1    O   <->  946 ASP   (  49-)  A 1    N      0.22    2.48
  47 ILE   (  47-)  A      O   <->   49 ASP   (  49-)  A      N      0.21    2.49
1082 ILE   (  47-)  A 1    O   <-> 1084 ASP   (  49-)  A 1    N      0.21    2.49
 116 ILE   (  47-)  A      O   <->  118 ASP   (  49-)  A      N      0.21    2.49
And so on for a total of 366 lines.

Packing, accessibility and threading

Note: Per-model averages for inside/outside residue distributi ...heck




















Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 1

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 2

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 3

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 4

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 5

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 6

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 7

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 8

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 9

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 10

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 11

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 12

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 13

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 14

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 15

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 16

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 17

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 18

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 19

Note: Inside/Outside RMS Z-score plot

Chain identifier: A; Model number 20

Warning: Abnormal packing environment for some residues


Warning: Abnormal packing environment for sequential residues


Warning: Structural average packing environment a bit worrysome

Note: Quality value plot

Chain identifier: A; Model number 1

Note: Quality value plot

Chain identifier: A; Model number 2

Note: Quality value plot

Chain identifier: A; Model number 3

Note: Quality value plot

Chain identifier: A; Model number 4

Note: Quality value plot

Chain identifier: A; Model number 5

Note: Quality value plot

Chain identifier: A; Model number 6

Note: Quality value plot

Chain identifier: A; Model number 7

Note: Quality value plot

Chain identifier: A; Model number 8

Note: Quality value plot

Chain identifier: A; Model number 9

Note: Quality value plot

Chain identifier: A; Model number 10

Note: Quality value plot

Chain identifier: A; Model number 11

Note: Quality value plot

Chain identifier: A; Model number 12

Note: Quality value plot

Chain identifier: A; Model number 13

Note: Quality value plot

Chain identifier: A; Model number 14

Note: Quality value plot

Chain identifier: A; Model number 15

Note: Quality value plot

Chain identifier: A; Model number 16

Note: Quality value plot

Chain identifier: A; Model number 17

Note: Quality value plot

Chain identifier: A; Model number 18

Note: Quality value plot

Chain identifier: A; Model number 19

Note: Quality value plot

Chain identifier: A; Model number 20

Warning: Low packing Z-score for some residues


Note: Per-model averages for NQA




















Note: Second generation quality Z-score plot

Chain identifier: A; Model number 1

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 2

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 3

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 4

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 5

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 6

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 7

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 8

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 9

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 10

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 11

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 12

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 13

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 14

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 15

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 16

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 17

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 18

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 19

Note: Second generation quality Z-score plot

Chain identifier: A; Model number 20

Water, ion, and hydrogenbond related checks

Warning: Buried unsatisfied hydrogen bond donors


Warning: Buried unsatisfied hydrogen bond acceptors


Warning: No crystallisation information

Warning: Possible wrong residue type


Final summary

Note: Summary report for users of a structure