WHAT IF Check report

This file was created 2011-12-29 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 pdb1kn6.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 PHE   (   4-)  A    Zero
   2 VAL   (   5-)  A    Zero
   3 ASN   (   6-)  A    Zero
   4 GLU   (   7-)  A    Zero
   5 TRP   (   8-)  A    Zero
   6 ALA   (   9-)  A    Zero
   7 ALA   (  10-)  A    Zero
   8 GLU   (  11-)  A    Zero
   9 ILE   (  12-)  A    Zero
  10 PRO   (  13-)  A    Zero
  11 GLY   (  14-)  A    Zero
  12 GLY   (  15-)  A    Zero
  13 GLN   (  16-)  A    Zero
  14 GLU   (  17-)  A    Zero
  15 ALA   (  18-)  A    Zero
  16 ALA   (  19-)  A    Zero
  17 SER   (  20-)  A    Zero
  18 ALA   (  21-)  A    Zero
  19 ILE   (  22-)  A    Zero
  20 ALA   (  23-)  A    Zero
  21 GLU   (  24-)  A    Zero
  22 GLU   (  25-)  A    Zero
  23 LEU   (  26-)  A    Zero
  24 GLY   (  27-)  A    Zero
  25 TYR   (  28-)  A    Zero
And so on for a total of 1460 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 : 0.240
Model 2 : 0.254
Model 3 : 0.236
Model 4 : 0.246
Model 5 : 0.254
Model 6 : 0.238
Model 7 : 0.240
Model 8 : 0.241
Model 9 : 0.241
Model 10 : 0.238
Model 11 : 0.243
Model 12 : 0.244
Model 13 : 0.244
Model 14 : 0.242
Model 15 : 0.229
Model 16 : 0.234
Model 17 : 0.231
Model 18 : 0.244
Model 19 : 0.238
Model 20 : 0.264

Note: Per-model averages for bond-angle check

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

Model 1 : 0.500
Model 2 : 0.515
Model 3 : 0.496
Model 4 : 0.518
Model 5 : 0.511
Model 6 : 0.502
Model 7 : 0.510
Model 8 : 0.498
Model 9 : 0.505
Model 10 : 0.497
Model 11 : 0.507
Model 12 : 0.513
Model 13 : 0.488
Model 14 : 0.500
Model 15 : 0.510
Model 16 : 0.482
Model 17 : 0.491
Model 18 : 0.494
Model 19 : 0.503
Model 20 : 0.526

Note: Per-model averages for chirality check

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

Model 1 : 0.334
Model 2 : 0.343
Model 3 : 0.353
Model 4 : 0.332
Model 5 : 0.342
Model 6 : 0.310
Model 7 : 0.337
Model 8 : 0.318
Model 9 : 0.338
Model 10 : 0.317
Model 11 : 0.343
Model 12 : 0.357
Model 13 : 0.310
Model 14 : 0.352
Model 15 : 0.329
Model 16 : 0.303
Model 17 : 0.306
Model 18 : 0.313
Model 19 : 0.318
Model 20 : 0.337

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 : -6.900

Note: Per-model averages for Ramachandran check

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

Model 1 : -6.243
Model 2 : -6.375
Model 3 : -6.852
Model 4 : -7.002
Model 5 : -7.744
Model 6 : -6.235
Model 7 : -7.403
Model 8 : -6.824
Model 9 : -6.786
Model 10 : -6.982
Model 11 : -6.908
Model 12 : -7.267
Model 13 : -6.778
Model 14 : -6.425
Model 15 : -7.387
Model 16 : -6.748
Model 17 : -6.280
Model 18 : -6.727
Model 19 : -7.094
Model 20 : -7.941

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.

1356 HIS   (  45-)  A 1   -3.3
 410 HIS   (  48-)  A    -3.3
 334 HIS   (  45-)  A    -3.2
 261 HIS   (  45-)  A    -3.1
1286 HIS   (  48-)  A 1   -3.1
 724 THR   (  70-)  A 1   -2.9
1368 LEU   (  57-)  A 1   -2.9
1222 LEU   (  57-)  A 1   -2.9
 346 LEU   (  57-)  A    -2.9
 930 LEU   (  57-)  A 1   -2.9
  48 ARG   (  51-)  A    -2.9
1441 LEU   (  57-)  A 2   -2.8
 492 LEU   (  57-)  A    -2.8
 200 LEU   (  57-)  A    -2.8
 472 LEU   (  37-)  A    -2.8
 273 LEU   (  57-)  A    -2.8
 711 LEU   (  57-)  A 1   -2.8
1295 LEU   (  57-)  A 1   -2.8
 194 ARG   (  51-)  A    -2.8
 997 ARG   (  51-)  A 1   -2.8
 629 HIS   (  48-)  A    -2.8
 699 HIS   (  45-)  A 1   -2.8
 851 ARG   (  51-)  A 1   -2.8
 857 LEU   (  57-)  A 1   -2.8
 642 LYS   (  61-)  A    -2.8
And so on for a total of 423 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 VAL   (   5-)  A  Poor phi/psi
   3 ASN   (   6-)  A  Poor phi/psi
  12 GLY   (  15-)  A  Poor phi/psi
  29 GLY   (  32-)  A  Poor phi/psi
  35 GLU   (  38-)  A  Poor phi/psi
  36 ASN   (  39-)  A  Poor phi/psi
  43 LYS   (  46-)  A  Poor phi/psi
  44 SER   (  47-)  A  Poor phi/psi
  46 PRO   (  49-)  A  Poor phi/psi
  49 SER   (  52-)  A  Poor phi/psi
  52 SER   (  55-)  A  Poor phi/psi
  53 ALA   (  56-)  A  Poor phi/psi
  58 LYS   (  61-)  A  Poor phi/psi
  75 VAL   (   5-)  A  Poor phi/psi
  76 ASN   (   6-)  A  Poor phi/psi
  85 GLY   (  15-)  A  Poor phi/psi
 108 GLU   (  38-)  A  Poor phi/psi
 109 ASN   (  39-)  A  Poor phi/psi
 121 ARG   (  51-)  A  Poor phi/psi
 122 SER   (  52-)  A  Poor phi/psi
 127 LEU   (  57-)  A  Poor phi/psi
 140 THR   (  70-)  A  Poor phi/psi
 149 ASN   (   6-)  A  Poor phi/psi
 158 GLY   (  15-)  A  Poor phi/psi
 168 GLU   (  25-)  A  Poor phi/psi
And so on for a total of 218 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 : -7.588

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 : -7.708
Model 2 : -7.761
Model 3 : -7.880
Model 4 : -6.965
Model 5 : -8.018
Model 6 : -7.273
Model 7 : -7.871
Model 8 : -7.826
Model 9 : -7.318
Model 10 : -7.454
Model 11 : -7.906
Model 12 : -7.779
Model 13 : -7.653
Model 14 : -7.293
Model 15 : -8.167
Model 16 : -7.387
Model 17 : -7.277
Model 18 : -7.179
Model 19 : -7.497
Model 20 : -7.552

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 ASN   (   6-)  A      0
  10 PRO   (  13-)  A      0
  23 LEU   (  26-)  A      0
  25 TYR   (  28-)  A      0
  28 LEU   (  31-)  A      0
  30 GLN   (  33-)  A      0
  31 ILE   (  34-)  A      0
  34 LEU   (  37-)  A      0
  35 GLU   (  38-)  A      0
  36 ASN   (  39-)  A      0
  37 HIS   (  40-)  A      0
  41 LYS   (  44-)  A      0
  42 HIS   (  45-)  A      0
  43 LYS   (  46-)  A      0
  44 SER   (  47-)  A      0
  45 HIS   (  48-)  A      0
  46 PRO   (  49-)  A      0
  47 ARG   (  50-)  A      0
  48 ARG   (  51-)  A      0
  49 SER   (  52-)  A      0
  51 ARG   (  54-)  A      0
  52 SER   (  55-)  A      0
  53 ALA   (  56-)  A      0
  54 LEU   (  57-)  A      0
  57 THR   (  60-)  A      0
And so on for a total of 865 lines.

Warning: Backbone conformation Z-score low

A comparison of the backbone conformation with database proteins shows that the backbone fold in this structure is unusual.

Backbone conformation Z-score : -3.212

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 : 0.749

Note: Per-model averages for omega angle check

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

Model 1 : 0.910
Model 2 : 0.748
Model 3 : 0.918
Model 4 : 0.766
Model 5 : 0.830
Model 6 : 0.727
Model 7 : 0.712
Model 8 : 0.727
Model 9 : 0.974
Model 10 : 0.722
Model 11 : 0.854
Model 12 : 0.864
Model 13 : 0.654
Model 14 : 0.775
Model 15 : 0.791
Model 16 : 0.638
Model 17 : 0.743
Model 18 : 0.764
Model 19 : 0.792
Model 20 : 0.757

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!

1265 GLY   (  27-)  A 1  1.64   37
 535 GLY   (  27-)  A   1.62   49

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].

  83 PRO   (  13-)  A    51.6 half-chair C-delta/C-gamma (54 degrees)
 119 PRO   (  49-)  A   -17.2 half-chair C-alpha/N (-18 degrees)
 156 PRO   (  13-)  A    48.0 half-chair C-delta/C-gamma (54 degrees)
 265 PRO   (  49-)  A     6.9 envelop N (0 degrees)
 302 PRO   (  13-)  A    50.7 half-chair C-delta/C-gamma (54 degrees)
 338 PRO   (  49-)  A    13.8 half-chair N/C-delta (18 degrees)
 484 PRO   (  49-)  A  -137.4 envelop C-delta (-144 degrees)
 776 PRO   (  49-)  A 1   48.7 half-chair C-delta/C-gamma (54 degrees)
 813 PRO   (  13-)  A 1  106.3 envelop C-beta (108 degrees)
 922 PRO   (  49-)  A 1   25.0 half-chair N/C-delta (18 degrees)
1032 PRO   (  13-)  A 1  119.1 half-chair C-beta/C-alpha (126 degrees)
1397 PRO   (  13-)  A 2   99.0 envelop C-beta (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.

 441 ASN   (   6-)  A      ND2 <->  511 TYR   (  76-)  A      O      0.56    2.14
1025 ASN   (   6-)  A 1    OD1 <-> 1095 TYR   (  76-)  A 1    O      0.46    1.79
1025 ASN   (   6-)  A 1    CG  <-> 1095 TYR   (  76-)  A 1    O      0.38    2.42
1392 TRP   (   8-)  A 2    CZ2 <-> 1394 ALA   (  10-)  A 2    CB     0.35    2.85
 954 TRP   (   8-)  A 1    CZ2 <->  956 ALA   (  10-)  A 1    CB     0.33    2.87
 951 VAL   (   5-)  A 1    CG2 <->  997 ARG   (  51-)  A 1    N      0.33    2.77
1403 ALA   (  19-)  A 2    O   <-> 1414 LEU   (  30-)  A 2    CD2    0.33    2.47
  16 ALA   (  19-)  A      C   <->   27 LEU   (  30-)  A      CD1    0.32    2.88
 370 TRP   (   8-)  A      CZ2 <->  372 ALA   (  10-)  A      CB     0.32    2.88
1432 HIS   (  48-)  A 2    N   <-> 1433 PRO   (  49-)  A 2    CD     0.31    2.69
  78 TRP   (   8-)  A      CZ2 <->   80 ALA   (  10-)  A      CB     0.31    2.89
 848 HIS   (  48-)  A 1    N   <->  849 PRO   (  49-)  A 1    CD     0.31    2.69
 662 TRP   (   8-)  A 1    CZ2 <->  664 ALA   (  10-)  A 1    CB     0.31    2.89
 147 PHE   (   4-)  A      CD1 <->  219 TYR   (  76-)  A      CD2    0.31    2.89
1301 LEU   (  63-)  A 1    O   <-> 1305 ASP   (  67-)  A 1    N      0.30    2.40
 956 ALA   (  10-)  A 1    C   <->  986 HIS   (  40-)  A 1    ND1    0.30    2.80
1173 TRP   (   8-)  A 1    CZ2 <-> 1175 ALA   (  10-)  A 1    CB     0.30    2.90
   5 TRP   (   8-)  A      CZ2 <->    7 ALA   (  10-)  A      CB     0.30    2.90
 881 TRP   (   8-)  A 1    CZ2 <->  883 ALA   (  10-)  A 1    CB     0.29    2.91
 575 ASP   (  67-)  A      CG  <->  580 ALA   (  72-)  A      CB     0.29    2.91
1024 VAL   (   5-)  A 1    CG2 <-> 1070 ARG   (  51-)  A 1    N      0.29    2.81
 735 TRP   (   8-)  A 1    CZ2 <->  737 ALA   (  10-)  A 1    CB     0.29    2.91
  64 ASP   (  67-)  A      CG  <->   69 ALA   (  72-)  A      CB     0.29    2.91
 615 ILE   (  34-)  A      CD1 <->  617 SER   (  36-)  A      N      0.29    2.81
 173 LEU   (  30-)  A      CD2 <->  186 PHE   (  43-)  A      CE1    0.29    2.91
And so on for a total of 1476 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


Error: Abnormal average packing environment

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


Warning: Abnormal packing Z-score for sequential 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