WHAT IF Check report

This file was created 2012-01-25 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 pdb2jte.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 ALA   (   2-)  A    Zero
   3 MET   (   3-)  A    Zero
   4 GLY   (   4-)  A    Zero
   5 ALA   (   5-)  A    Zero
   6 LYS   (   6-)  A    Zero
   7 GLU   (   7-)  A    Zero
   8 TYR   (   8-)  A    Zero
   9 CYS   (   9-)  A    Zero
  10 ARG   (  10-)  A    Zero
  11 THR   (  11-)  A    Zero
  12 LEU   (  12-)  A    Zero
  13 PHE   (  13-)  A    Zero
  14 PRO   (  14-)  A    Zero
  15 TYR   (  15-)  A    Zero
  16 THR   (  16-)  A    Zero
  17 GLY   (  17-)  A    Zero
  18 THR   (  18-)  A    Zero
  19 ASN   (  19-)  A    Zero
  20 GLU   (  20-)  A    Zero
  21 ASP   (  21-)  A    Zero
  22 GLU   (  22-)  A    Zero
  23 LEU   (  23-)  A    Zero
  24 THR   (  24-)  A    Zero
  25 PHE   (  25-)  A    Zero
And so on for a total of 1280 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 : 0.817
Model 2 : 0.848
Model 3 : 0.787
Model 4 : 0.847
Model 5 : 0.835
Model 6 : 0.828
Model 7 : 0.830
Model 8 : 0.850
Model 9 : 0.800
Model 10 : 0.775
Model 11 : 0.777
Model 12 : 0.822
Model 13 : 0.789
Model 14 : 0.796
Model 15 : 0.845
Model 16 : 0.828
Model 17 : 0.851
Model 18 : 0.826
Model 19 : 0.825
Model 20 : 0.760

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 : 0.643
Model 2 : 0.609
Model 3 : 0.637
Model 4 : 0.671
Model 5 : 0.623
Model 6 : 0.661
Model 7 : 0.662
Model 8 : 0.667
Model 9 : 0.660
Model 10 : 0.682
Model 11 : 0.656
Model 12 : 0.652
Model 13 : 0.656
Model 14 : 0.621
Model 15 : 0.691
Model 16 : 0.650
Model 17 : 0.692
Model 18 : 0.655
Model 19 : 0.641
Model 20 : 0.667

Note: Per-model averages for chirality check

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

Model 1 : 0.782
Model 2 : 0.798
Model 3 : 0.748
Model 4 : 0.805
Model 5 : 0.709
Model 6 : 0.748
Model 7 : 0.868
Model 8 : 0.816
Model 9 : 0.804
Model 10 : 0.839
Model 11 : 0.765
Model 12 : 0.758
Model 13 : 0.791
Model 14 : 0.746
Model 15 : 0.796
Model 16 : 0.736
Model 17 : 0.817
Model 18 : 0.837
Model 19 : 0.785
Model 20 : 0.753

Torsion-related checks

Note: Per-model averages for Ramachandran check

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

Model 1 : -2.846
Model 2 : -1.668
Model 3 : -1.795
Model 4 : -1.534
Model 5 : -1.861
Model 6 : -2.408
Model 7 : -2.066
Model 8 : -2.084
Model 9 : -1.951
Model 10 : -2.276
Model 11 : -2.846
Model 12 : -1.825
Model 13 : -2.873
Model 14 : -2.278
Model 15 : -1.689
Model 16 : -2.428
Model 17 : -1.359
Model 18 : -3.126
Model 19 : -2.418
Model 20 : -1.440

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.

 436 GLU   (  52-)  A    -2.3
 324 GLY   (   4-)  A    -2.2
1038 PRO   (  14-)  A 1   -2.2
 388 GLY   (   4-)  A    -2.2
 646 LYS   (   6-)  A 1   -2.1
 727 LEU   (  23-)  A 1   -2.1
 132 GLY   (   4-)  A    -2.1
1203 LYS   (  51-)  A 1   -2.1
 948 GLU   (  52-)  A 1   -2.0
 421 GLU   (  37-)  A    -2.0
 402 THR   (  18-)  A    -2.0
 564 GLU   (  52-)  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.

   6 LYS   (   6-)  A  Poor phi/psi
  49 ASN   (  49-)  A  Poor phi/psi
  92 GLY   (  28-)  A  Poor phi/psi
 113 ASN   (  49-)  A  Poor phi/psi
 130 ALA   (   2-)  A  Poor phi/psi
 133 ALA   (   5-)  A  Poor phi/psi
 177 ASN   (  49-)  A  Poor phi/psi
 241 ASN   (  49-)  A  Poor phi/psi
 261 ALA   (   5-)  A  Poor phi/psi
 305 ASN   (  49-)  A  Poor phi/psi
 348 GLY   (  28-)  A  Poor phi/psi
 369 ASN   (  49-)  A  Poor phi/psi
 387 MET   (   3-)  A  Poor phi/psi
 433 ASN   (  49-)  A  Poor phi/psi
 453 ALA   (   5-)  A  Poor phi/psi
 497 ASN   (  49-)  A  Poor phi/psi
 517 ALA   (   5-)  A  Poor phi/psi
 561 ASN   (  49-)  A  Poor phi/psi
 578 ALA   (   2-)  A 1 Poor phi/psi
 625 ASN   (  49-)  A 1 Poor phi/psi
 689 ASN   (  49-)  A 1 Poor phi/psi
 709 ALA   (   5-)  A 1 Poor phi/psi
 753 ASN   (  49-)  A 1 Poor phi/psi
 817 ASN   (  49-)  A 1 Poor phi/psi
 881 ASN   (  49-)  A 1 Poor phi/psi
 900 GLY   (   4-)  A 1 Poor phi/psi
 902 LYS   (   6-)  A 1 Poor phi/psi
 945 ASN   (  49-)  A 1 Poor phi/psi
1009 ASN   (  49-)  A 1 Poor phi/psi
1073 ASN   (  49-)  A 1 Poor phi/psi
1137 ASN   (  49-)  A 1 Poor phi/psi
1201 ASN   (  49-)  A 1 Poor phi/psi
1222 LYS   (   6-)  A 2 Poor phi/psi
1265 ASN   (  49-)  A 2 Poor phi/psi
 chi-1/chi-2 correlation Z-score : -0.419

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 : -0.172
Model 2 : -0.280
Model 3 : -1.046
Model 4 : -0.307
Model 5 : -0.732
Model 6 : -1.474
Model 7 : 1.168
Model 8 : -0.575
Model 9 : 0.938
Model 10 : 0.485
Model 11 : -1.161
Model 12 : -0.338
Model 13 : -1.167
Model 14 : 0.188
Model 15 : -1.996
Model 16 : -0.090
Model 17 : -1.391
Model 18 : -0.512
Model 19 : -0.128
Model 20 : 0.218

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 ALA   (   5-)  A      0
   6 LYS   (   6-)  A      0
  12 LEU   (  12-)  A      0
  19 ASN   (  19-)  A      0
  27 GLU   (  27-)  A      0
  35 SER   (  35-)  A      0
  36 LYS   (  36-)  A      0
  38 THR   (  38-)  A      0
  41 ALA   (  41-)  A      0
  48 LEU   (  48-)  A      0
  49 ASN   (  49-)  A      0
  57 ASP   (  57-)  A      0
  59 PHE   (  59-)  A      0
  63 ILE   (  63-)  A      0
  64 SER   (  64-)  A      0
  65 GLY   (   1-)  A      0
  66 ALA   (   2-)  A      0
  67 MET   (   3-)  A      0
  69 ALA   (   5-)  A      0
  70 LYS   (   6-)  A      0
  71 GLU   (   7-)  A      0
  83 ASN   (  19-)  A      0
  91 GLU   (  27-)  A      0
  99 SER   (  35-)  A      0
 100 LYS   (  36-)  A      0
And so on for a total of 610 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 : 3.586

Note: Per-model averages for omega angle check

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

Model 1 : 3.484
Model 2 : 3.203
Model 3 : 3.995
Model 4 : 3.842
Model 5 : 3.593
Model 6 : 3.155
Model 7 : 3.681
Model 8 : 3.586
Model 9 : 3.087
Model 10 : 4.412
Model 11 : 3.502
Model 12 : 3.668
Model 13 : 3.685
Model 14 : 3.198
Model 15 : 3.583
Model 16 : 3.470
Model 17 : 3.518
Model 18 : 3.673
Model 19 : 3.820
Model 20 : 3.531

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!

 785 GLY   (  17-)  A 1  1.66   11
 516 GLY   (   4-)  A   1.61   18

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]

1166 PRO   (  14-)  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].

  78 PRO   (  14-)  A   -65.2 envelop C-beta (-72 degrees)
 184 PRO   (  56-)  A    51.5 half-chair C-delta/C-gamma (54 degrees)
 312 PRO   (  56-)  A    49.6 half-chair C-delta/C-gamma (54 degrees)
 632 PRO   (  56-)  A 1   50.4 half-chair C-delta/C-gamma (54 degrees)
 760 PRO   (  56-)  A 1   51.1 half-chair C-delta/C-gamma (54 degrees)
 888 PRO   (  56-)  A 1   48.9 half-chair C-delta/C-gamma (54 degrees)
 910 PRO   (  14-)  A 1  -64.3 envelop C-beta (-72 degrees)
1038 PRO   (  14-)  A 1  -53.1 half-chair C-beta/C-alpha (-54 degrees)
1144 PRO   (  56-)  A 1   44.8 envelop C-delta (36 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.

1261 LYS   (  45-)  A 2    NZ  <-> 1268 GLU   (  52-)  A 2    OE1    0.14    2.56
 131 MET   (   3-)  A      SD  <->  164 LYS   (  36-)  A      NZ     0.14    3.16
 390 LYS   (   6-)  A      N   <->  391 GLU   (   7-)  A      N      0.12    2.48        B3
1026 ALA   (   2-)  A 1    N   <-> 1031 GLU   (   7-)  A 1    OE1    0.12    2.58
 804 LYS   (  36-)  A 1    N   <->  805 GLU   (  37-)  A 1    N      0.10    2.50        B3
1170 THR   (  18-)  A 1    N   <-> 1171 ASN   (  19-)  A 1    N      0.10    2.50        B3
 685 LYS   (  45-)  A 1    NZ  <->  692 GLU   (  52-)  A 1    OE1    0.09    2.61
 422 THR   (  38-)  A      N   <->  423 GLY   (  39-)  A      N      0.09    2.51        B3
 338 THR   (  18-)  A      N   <->  339 ASN   (  19-)  A      N      0.09    2.51        B3
 231 GLY   (  39-)  A      N   <->  232 GLU   (  40-)  A      N      0.09    2.51        B3
 321 GLY   (   1-)  A      N   <->  357 GLU   (  37-)  A      OE1    0.09    2.61
 466 THR   (  18-)  A      N   <->  467 ASN   (  19-)  A      N      0.09    2.51        B3
 981 ASP   (  21-)  A 1    OD1 <-> 1005 LYS   (  45-)  A 1    NZ     0.09    2.61
  82 THR   (  18-)  A      N   <->   83 ASN   (  19-)  A      N      0.09    2.51        B3
 257 GLY   (   1-)  A      N   <->  293 GLU   (  37-)  A      OE1    0.09    2.61
 725 ASP   (  21-)  A 1    N   <->  726 GLU   (  22-)  A 1    N      0.09    2.51        B3
 210 THR   (  18-)  A      N   <->  211 ASN   (  19-)  A      N      0.08    2.52        B3
1217 GLY   (   1-)  A 2    N   <-> 1253 GLU   (  37-)  A 2    OE1    0.08    2.62
1161 CYS   (   9-)  A 1    SG  <-> 1183 ILE   (  31-)  A 1    CB     0.08    3.32
 579 MET   (   3-)  A 1    N   <->  580 GLY   (   4-)  A 1    N      0.08    2.52        B3
 530 THR   (  18-)  A      N   <->  531 ASN   (  19-)  A      N      0.08    2.52        B3
 914 THR   (  18-)  A 1    N   <->  915 ASN   (  19-)  A 1    N      0.08    2.52        B3
 402 THR   (  18-)  A      N   <->  406 GLU   (  22-)  A      OE1    0.08    2.62
 646 LYS   (   6-)  A 1    NZ  <->  647 GLU   (   7-)  A 1    OE2    0.07    2.63
 466 THR   (  18-)  A      N   <->  470 GLU   (  22-)  A      OE1    0.07    2.63
And so on for a total of 160 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


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

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