WHAT IF Check report

This file was created 2011-12-17 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 pdb2rqs.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 PRO   (   2-)  A    Zero
   3 MET   (   3-)  A    Zero
   4 GLY   (   4-)  A    Zero
   5 SER   (   5-)  A    Zero
   6 MET   (   6-)  A    Zero
   7 ALA   (   7-)  A    Zero
   8 ASP   (   8-)  A    Zero
   9 LYS   (   9-)  A    Zero
  10 ILE   (  10-)  A    Zero
  11 LYS   (  11-)  A    Zero
  12 CYS   (  12-)  A    Zero
  13 SER   (  13-)  A    Zero
  14 HIS   (  14-)  A    Zero
  15 ILE   (  15-)  A    Zero
  16 LEU   (  16-)  A    Zero
  17 VAL   (  17-)  A    Zero
  18 LYS   (  18-)  A    Zero
  19 LYS   (  19-)  A    Zero
  20 GLN   (  20-)  A    Zero
  21 GLY   (  21-)  A    Zero
  22 GLU   (  22-)  A    Zero
  23 ALA   (  23-)  A    Zero
  24 LEU   (  24-)  A    Zero
  25 ALA   (  25-)  A    Zero
And so on for a total of 1940 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 : 0.222
Model 2 : 0.222
Model 3 : 0.229
Model 4 : 0.230
Model 5 : 0.236
Model 6 : 0.231
Model 7 : 0.230
Model 8 : 0.228
Model 9 : 0.231
Model 10 : 0.232
Model 11 : 0.226
Model 12 : 0.229
Model 13 : 0.225
Model 14 : 0.223
Model 15 : 0.219
Model 16 : 0.221
Model 17 : 0.221
Model 18 : 0.221
Model 19 : 0.230
Model 20 : 0.221

Note: Per-model averages for bond-angle check

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

Model 1 : 0.403
Model 2 : 0.409
Model 3 : 0.406
Model 4 : 0.399
Model 5 : 0.401
Model 6 : 0.391
Model 7 : 0.392
Model 8 : 0.414
Model 9 : 0.393
Model 10 : 0.407
Model 11 : 0.407
Model 12 : 0.393
Model 13 : 0.395
Model 14 : 0.395
Model 15 : 0.401
Model 16 : 0.402
Model 17 : 0.398
Model 18 : 0.394
Model 19 : 0.401
Model 20 : 0.394

Note: Per-model averages for chirality check

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

Model 1 : 0.379
Model 2 : 0.406
Model 3 : 0.373
Model 4 : 0.376
Model 5 : 0.360
Model 6 : 0.367
Model 7 : 0.360
Model 8 : 0.396
Model 9 : 0.376
Model 10 : 0.429
Model 11 : 0.412
Model 12 : 0.382
Model 13 : 0.367
Model 14 : 0.375
Model 15 : 0.380
Model 16 : 0.405
Model 17 : 0.372
Model 18 : 0.365
Model 19 : 0.365
Model 20 : 0.383

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 : -5.705

Note: Per-model averages for Ramachandran check

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

Model 1 : -5.654
Model 2 : -5.841
Model 3 : -5.966
Model 4 : -5.594
Model 5 : -5.514
Model 6 : -5.620
Model 7 : -5.996
Model 8 : -6.246
Model 9 : -5.498
Model 10 : -5.760
Model 11 : -5.746
Model 12 : -5.562
Model 13 : -5.683
Model 14 : -6.074
Model 15 : -5.558
Model 16 : -5.921
Model 17 : -5.578
Model 18 : -5.705
Model 19 : -5.424
Model 20 : -5.155

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.

  90 TYR   (  90-)  A    -3.0
 787 LYS   (  11-)  A    -2.6
 546 ARG   (  61-)  A    -2.6
1313 ARG   (  52-)  A 1   -2.6
1078 LYS   (  11-)  A 1   -2.6
 593 LYS   (  11-)  A    -2.6
 491 MET   (   6-)  A    -2.5
  45 ILE   (  45-)  A    -2.5
1112 ILE   (  45-)  A 1   -2.5
1701 ARG   (  52-)  A 1   -2.5
 496 LYS   (  11-)  A    -2.5
1791 ILE   (  45-)  A 1   -2.5
1216 ARG   (  52-)  A 1   -2.5
1757 LYS   (  11-)  A 1   -2.5
 399 LYS   (  11-)  A    -2.5
1119 ARG   (  52-)  A 1   -2.5
   6 MET   (   6-)  A    -2.5
1798 ARG   (  52-)  A 1   -2.5
 537 ARG   (  52-)  A    -2.5
 108 LYS   (  11-)  A    -2.5
1306 ILE   (  45-)  A 1   -2.5
 884 LYS   (  11-)  A 1   -2.5
1854 LYS   (  11-)  A 2   -2.5
 302 LYS   (  11-)  A    -2.4
 273 GLU   (  79-)  A    -2.4
And so on for a total of 225 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.

   6 MET   (   6-)  A  Poor phi/psi
  33 GLY   (  33-)  A  Poor phi/psi
  48 GLY   (  48-)  A  Poor phi/psi
  53 ASP   (  53-)  A  Poor phi/psi
  62 GLY   (  62-)  A  Poor phi/psi
 129 ALA   (  32-)  A  Poor phi/psi
 150 ASP   (  53-)  A  Poor phi/psi
 159 GLY   (  62-)  A  Poor phi/psi
 242 GLY   (  48-)  A  Poor phi/psi
 247 ASP   (  53-)  A  Poor phi/psi
 256 GLY   (  62-)  A  Poor phi/psi
 339 GLY   (  48-)  A  Poor phi/psi
 344 ASP   (  53-)  A  Poor phi/psi
 353 GLY   (  62-)  A  Poor phi/psi
 421 GLY   (  33-)  A  Poor phi/psi
 436 GLY   (  48-)  A  Poor phi/psi
 441 ASP   (  53-)  A  Poor phi/psi
 445 GLY   (  57-)  A  Poor phi/psi
 450 GLY   (  62-)  A  Poor phi/psi
 491 MET   (   6-)  A  Poor phi/psi
 533 GLY   (  48-)  A  Poor phi/psi
 538 ASP   (  53-)  A  Poor phi/psi
 542 GLY   (  57-)  A  Poor phi/psi
 547 GLY   (  62-)  A  Poor phi/psi
 630 GLY   (  48-)  A  Poor phi/psi
And so on for a total of 73 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 : -8.166

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 : -8.579
Model 2 : -7.991
Model 3 : -8.102
Model 4 : -8.028
Model 5 : -8.372
Model 6 : -7.980
Model 7 : -7.882
Model 8 : -8.125
Model 9 : -8.190
Model 10 : -8.114
Model 11 : -8.054
Model 12 : -8.180
Model 13 : -8.052
Model 14 : -7.936
Model 15 : -8.561
Model 16 : -8.137
Model 17 : -8.227
Model 18 : -8.305
Model 19 : -8.451
Model 20 : -8.057

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 MET   (   3-)  A      0
   5 SER   (   5-)  A      0
   6 MET   (   6-)  A      0
   7 ALA   (   7-)  A      0
  12 CYS   (  12-)  A      0
  19 LYS   (  19-)  A      0
  20 GLN   (  20-)  A      0
  32 ALA   (  32-)  A      0
  43 LEU   (  43-)  A      0
  53 ASP   (  53-)  A      0
  55 SER   (  55-)  A      0
  56 LEU   (  56-)  A      0
  58 TYR   (  58-)  A      0
  61 ARG   (  61-)  A      0
  63 LYS   (  63-)  A      0
  64 MET   (  64-)  A      0
  75 LEU   (  75-)  A      0
  76 GLN   (  76-)  A      0
  77 VAL   (  77-)  A      0
  82 GLU   (  82-)  A      0
  88 PHE   (  88-)  A      0
  90 TYR   (  90-)  A      0
  95 ARG   (  95-)  A      0
  96 LEU   (  96-)  A      0
  97 GLY   (  97-)  A      0
And so on for a total of 887 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 : 0.814

Note: Per-model averages for omega angle check

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

Model 1 : 0.896
Model 2 : 0.915
Model 3 : 0.817
Model 4 : 0.867
Model 5 : 0.807
Model 6 : 0.855
Model 7 : 0.767
Model 8 : 0.856
Model 9 : 0.798
Model 10 : 0.997
Model 11 : 0.964
Model 12 : 0.831
Model 13 : 0.831
Model 14 : 0.880
Model 15 : 0.876
Model 16 : 0.931
Model 17 : 0.900
Model 18 : 0.870
Model 19 : 0.796
Model 20 : 0.858

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!

 392 GLY   (   4-)  A   1.54   12

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]

 746 PRO   (  67-)  A    0.15 LOW
1231 PRO   (  67-)  A 1   0.19 LOW
1425 PRO   (  67-)  A 1   0.20 LOW

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].

 471 PRO   (  83-)  A  -118.2 half-chair C-delta/C-gamma (-126 degrees)
 568 PRO   (  83-)  A  -113.6 envelop C-gamma (-108 degrees)
 665 PRO   (  83-)  A  -112.6 envelop C-gamma (-108 degrees)
 859 PRO   (  83-)  A  -112.2 envelop C-gamma (-108 degrees)
1053 PRO   (  83-)  A 1 -117.1 half-chair C-delta/C-gamma (-126 degrees)
1247 PRO   (  83-)  A 1 -115.1 envelop C-gamma (-108 degrees)
1732 PRO   (  83-)  A 1 -114.7 envelop C-gamma (-108 degrees)

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.

  12 CYS   (  12-)  A      SG  <->   94 LYS   (  94-)  A      C      0.49    2.91
1114 GLY   (  47-)  A 1    O   <-> 1116 SER   (  49-)  A 1    N      0.46    2.24
 532 GLY   (  47-)  A      O   <->  534 SER   (  49-)  A      N      0.45    2.25
 241 GLY   (  47-)  A      O   <->  243 SER   (  49-)  A      N      0.45    2.25
1696 GLY   (  47-)  A 1    O   <-> 1698 SER   (  49-)  A 1    N      0.44    2.26
 823 GLY   (  47-)  A      O   <->  825 SER   (  49-)  A      N      0.43    2.27
1405 GLY   (  47-)  A 1    O   <-> 1407 SER   (  49-)  A 1    N      0.43    2.27
1890 GLY   (  47-)  A 2    O   <-> 1892 SER   (  49-)  A 2    N      0.43    2.27
1308 GLY   (  47-)  A 1    O   <-> 1310 SER   (  49-)  A 1    N      0.43    2.27
1211 GLY   (  47-)  A 1    O   <-> 1213 SER   (  49-)  A 1    N      0.43    2.27
1273 CYS   (  12-)  A 1    SG  <-> 1355 LYS   (  94-)  A 1    C      0.42    2.98
 629 GLY   (  47-)  A      O   <->  631 SER   (  49-)  A      N      0.42    2.28
1599 GLY   (  47-)  A 1    O   <-> 1601 SER   (  49-)  A 1    N      0.42    2.28
1855 CYS   (  12-)  A 2    SG  <-> 1937 LYS   (  94-)  A 2    C      0.42    2.98
  47 GLY   (  47-)  A      O   <->   49 SER   (  49-)  A      N      0.41    2.29
 435 GLY   (  47-)  A      O   <->  437 SER   (  49-)  A      N      0.41    2.29
1176 CYS   (  12-)  A 1    SG  <-> 1258 LYS   (  94-)  A 1    C      0.41    2.99
 497 CYS   (  12-)  A      SG  <->  579 LYS   (  94-)  A      C      0.41    2.99
1467 CYS   (  12-)  A 1    SG  <-> 1549 LYS   (  94-)  A 1    C      0.40    3.00
 338 GLY   (  47-)  A      O   <->  340 SER   (  49-)  A      N      0.40    2.30
 109 CYS   (  12-)  A      SG  <->  191 LYS   (  94-)  A      C      0.40    3.00
1370 CYS   (  12-)  A 1    SG  <-> 1452 LYS   (  94-)  A 1    C      0.40    3.00
 885 CYS   (  12-)  A 1    SG  <->  967 LYS   (  94-)  A 1    C      0.39    3.01
1793 GLY   (  47-)  A 1    O   <-> 1795 SER   (  49-)  A 1    N      0.39    2.31
1661 CYS   (  12-)  A 1    SG  <-> 1743 LYS   (  94-)  A 1    C      0.38    3.02
And so on for a total of 1234 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

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

Error: HIS, ASN, GLN side chain flips


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