WHAT IF Check report

This file was created 2012-07-04 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 pdb2len.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 MET   (   1-)  A    Zero
   2 GLN   (   2-)  A    Zero
   3 LEU   (   3-)  A    Zero
   4 LYS   (   4-)  A    Zero
   5 PRO   (   5-)  A    Zero
   6 MET   (   6-)  A    Zero
   7 GLU   (   7-)  A    Zero
   8 ILE   (   8-)  A    Zero
   9 ASN   (   9-)  A    Zero
  10 PRO   (  10-)  A    Zero
  11 GLU   (  11-)  A    Zero
  12 MET   (  12-)  A    Zero
  13 LEU   (  13-)  A    Zero
  14 ASN   (  14-)  A    Zero
  15 LYS   (  15-)  A    Zero
  16 VAL   (  16-)  A    Zero
  17 LEU   (  17-)  A    Zero
  18 TYR   (  18-)  A    Zero
  19 ARG   (  19-)  A    Zero
  20 LEU   (  20-)  A    Zero
  21 GLY   (  21-)  A    Zero
  22 VAL   (  22-)  A    Zero
  23 ALA   (  23-)  A    Zero
  24 GLY   (  24-)  A    Zero
  25 GLN   (  25-)  A    Zero
And so on for a total of 4620 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 : 0.669
Model 2 : 0.668
Model 3 : 0.669
Model 4 : 0.673
Model 5 : 0.673
Model 6 : 0.663
Model 7 : 0.670
Model 8 : 0.666
Model 9 : 0.673
Model 10 : 0.666
Model 11 : 0.663
Model 12 : 0.658
Model 13 : 0.664
Model 14 : 0.655
Model 15 : 0.665
Model 16 : 0.666
Model 17 : 0.666
Model 18 : 0.663
Model 19 : 0.666
Model 20 : 0.662

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.

Warning: Unusual bond angles

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

  72 GLY   (  72-)  A     -C    N    CA  127.70    4.2
  73 GLN   (  73-)  A      NE2  CD   OE1 117.81   -4.8
 184 ASN   ( 184-)  A      CA   CB   CG  116.77    4.2
 184 ASN   ( 184-)  A      ND2  CG   OD1 117.98   -4.6
 202 ARG   ( 202-)  A      CD   NE   CZ  129.10    4.1
 209 GLN   ( 209-)  A      NE2  CD   OE1 118.60   -4.0
 347 GLN   ( 116-)  A      NE2  CD   OE1 118.44   -4.2
 379 GLN   ( 148-)  A      NE2  CD   OE1 118.43   -4.2
 409 ARG   ( 178-)  A      CD   NE   CZ  129.21    4.2
 464 GLN   (   2-)  A      NE2  CD   OE1 118.50   -4.1
 528 GLN   (  66-)  A      NE2  CD   OE1 118.35   -4.2
 565 GLN   ( 103-)  A      NE2  CD   OE1 118.45   -4.1
 610 GLN   ( 148-)  A      NE2  CD   OE1 118.48   -4.1
 613 GLN   ( 151-)  A      NE2  CD   OE1 118.44   -4.2
 695 GLN   (   2-)  A      NE2  CD   OE1 118.57   -4.0
 796 GLN   ( 103-)  A      NE2  CD   OE1 118.45   -4.1
 801 PHE   ( 108-)  A      CA   CB   CG  117.99    4.2
 833 GLN   ( 140-)  A      NE2  CD   OE1 118.54   -4.1
 957 GLY   (  33-)  A     -C    N    CA  127.49    4.1
1008 GLN   (  84-)  A      NE2  CD   OE1 118.48   -4.1
1064 GLN   ( 140-)  A      NE2  CD   OE1 118.11   -4.5
1271 GLN   ( 116-)  A      NE2  CD   OE1 118.60   -4.0
1284 ARG   ( 129-)  A      CD   NE   CZ  129.78    4.5
1295 GLN   ( 140-)  A      NE2  CD   OE1 118.41   -4.2
1395 ASN   (   9-)  A      CA   CB   CG  117.25    4.6
And so on for a total of 76 lines.

Note: Per-model averages for bond-angle check

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

Model 1 : 1.112
Model 2 : 1.105
Model 3 : 1.122
Model 4 : 1.119
Model 5 : 1.126
Model 6 : 1.109
Model 7 : 1.123
Model 8 : 1.114
Model 9 : 1.133
Model 10 : 1.110
Model 11 : 1.094
Model 12 : 1.115
Model 13 : 1.113
Model 14 : 1.106
Model 15 : 1.103
Model 16 : 1.109
Model 17 : 1.107
Model 18 : 1.106
Model 19 : 1.118
Model 20 : 1.122

Note: Per-model averages for chirality check

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

Model 1 : 0.814
Model 2 : 0.816
Model 3 : 0.808
Model 4 : 0.825
Model 5 : 0.847
Model 6 : 0.821
Model 7 : 0.768
Model 8 : 0.807
Model 9 : 0.835
Model 10 : 0.853
Model 11 : 0.805
Model 12 : 0.813
Model 13 : 0.807
Model 14 : 0.811
Model 15 : 0.811
Model 16 : 0.843
Model 17 : 0.806
Model 18 : 0.824
Model 19 : 0.828
Model 20 : 0.821

Torsion-related checks

Note: Per-model averages for Ramachandran check

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

Model 1 : -2.490
Model 2 : -2.605
Model 3 : -3.124
Model 4 : -2.644
Model 5 : -2.508
Model 6 : -2.431
Model 7 : -2.694
Model 8 : -2.952
Model 9 : -2.914
Model 10 : -2.178
Model 11 : -2.444
Model 12 : -2.882
Model 13 : -2.458
Model 14 : -2.576
Model 15 : -2.644
Model 16 : -2.637
Model 17 : -2.458
Model 18 : -2.512
Model 19 : -3.372
Model 20 : -1.983

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.

1709 THR   (  92-)  A    -3.2
2864 THR   (  92-)  A 1   -3.0
 622 PHE   ( 160-)  A    -2.9
1934 ILE   (  86-)  A    -2.9
1782 PHE   ( 165-)  A    -2.7
1087 ILE   ( 163-)  A    -2.7
 394 ILE   ( 163-)  A    -2.6
 686 LEU   ( 224-)  A    -2.6
2957 HIS   ( 185-)  A 1   -2.6
1698 PHE   (  81-)  A    -2.6
4151 LEU   ( 224-)  A 1   -2.6
 455 LEU   ( 224-)  A    -2.6
4112 HIS   ( 185-)  A 1   -2.6
1384 HIS   ( 229-)  A    -2.6
4549 PHE   ( 160-)  A 2   -2.6
4247 SER   (  89-)  A 1   -2.6
 774 PHE   (  81-)  A    -2.5
3458 LEU   ( 224-)  A 1   -2.5
 856 ILE   ( 163-)  A    -2.5
 512 LEU   (  50-)  A    -2.5
2935 ILE   ( 163-)  A 1   -2.5
2493 VAL   ( 183-)  A 1   -2.5
2242 ILE   ( 163-)  A 1   -2.5
4469 TYR   (  80-)  A 2   -2.5
3881 HIS   ( 185-)  A 1   -2.5
And so on for a total of 222 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.

  24 GLY   (  24-)  A  Poor phi/psi
  72 GLY   (  72-)  A  Poor phi/psi
  82 MET   (  82-)  A  Poor phi/psi
  88 ASN   (  88-)  A  omega poor
  91 GLY   (  91-)  A  Poor phi/psi
 169 ASP   ( 169-)  A  Poor phi/psi
 171 HIS   ( 171-)  A  omega poor
 180 PRO   ( 180-)  A  Poor phi/psi
 223 ALA   ( 223-)  A  Poor phi/psi
 400 ASP   ( 169-)  A  Poor phi/psi
 404 TYR   ( 173-)  A  omega poor
 409 ARG   ( 178-)  A  omega poor
 443 VAL   ( 212-)  A  Poor phi/psi
 448 VAL   ( 217-)  A  omega poor
 544 MET   (  82-)  A  omega poor
 550 ASN   (  88-)  A  Poor phi/psi
 553 GLY   (  91-)  A  Poor phi/psi
 631 ASP   ( 169-)  A  Poor phi/psi
 636 GLU   ( 174-)  A  omega poor
 638 ASP   ( 176-)  A  Poor phi/psi
 642 PRO   ( 180-)  A  Poor phi/psi
 684 ALA   ( 222-)  A  Poor phi/psi
 686 LEU   ( 224-)  A  omega poor
 907 PHE   ( 214-)  A  omega poor
 910 VAL   ( 217-)  A  omega poor
And so on for a total of 124 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 : -4.226

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 : -3.658
Model 2 : -3.986
Model 3 : -4.028
Model 4 : -4.405
Model 5 : -4.230
Model 6 : -5.006
Model 7 : -4.294
Model 8 : -3.974
Model 9 : -3.316
Model 10 : -4.019
Model 11 : -4.119
Model 12 : -4.633
Model 13 : -4.014
Model 14 : -4.347
Model 15 : -4.492
Model 16 : -4.323
Model 17 : -4.892
Model 18 : -4.392
Model 19 : -4.558
Model 20 : -3.825

Warning: Unusual rotamers

The residues listed in the table below have a rotamer that is not seen very often in the database of solved protein structures. This option determines for every residue the position specific chi-1 rotamer distribution. Thereafter it verified whether the actual residue in the molecule has the most preferred rotamer or not. If the actual rotamer is the preferred one, the score is 1.0. If the actual rotamer is unique, the score is 0.0. If there are two preferred rotamers, with a population distribution of 3:2 and your rotamer sits in the lesser populated rotamer, the score will be 0.667. No value will be given if insufficient hits are found in the database.

It is not necessarily an error if a few residues have rotamer values below 0.3, but careful inspection of all residues with these low values could be worth it.

1397 GLU   (  11-)  A    0.33
2090 GLU   (  11-)  A 1   0.36
2429 SER   ( 119-)  A 1   0.36
1967 SER   ( 119-)  A    0.36
3353 SER   ( 119-)  A 1   0.37
4277 SER   ( 119-)  A 1   0.38
4508 SER   ( 119-)  A 2   0.39
 350 SER   ( 119-)  A    0.40
3122 SER   ( 119-)  A 1   0.40

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!

   9 ASN   (   9-)  A      0
  20 LEU   (  20-)  A      0
  25 GLN   (  25-)  A      0
  28 PHE   (  28-)  A      0
  29 VAL   (  29-)  A      0
  32 LEU   (  32-)  A      0
  41 SER   (  41-)  A      0
  43 PRO   (  43-)  A      0
  44 ALA   (  44-)  A      0
  45 PRO   (  45-)  A      0
  46 ALA   (  46-)  A      0
  47 CYS   (  47-)  A      0
  73 GLN   (  73-)  A      0
  83 LYS   (  83-)  A      0
  84 GLN   (  84-)  A      0
  86 ILE   (  86-)  A      0
  88 ASN   (  88-)  A      0
  89 SER   (  89-)  A      0
  90 CYS   (  90-)  A      0
 110 ASP   ( 110-)  A      0
 123 LYS   ( 123-)  A      0
 136 ASN   ( 136-)  A      0
 137 GLU   ( 137-)  A      0
 149 GLU   ( 149-)  A      0
 154 VAL   ( 154-)  A      0
And so on for a total of 1835 lines.

Note: Per-model averages for omega angle check

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

Model 1 : 4.895
Model 2 : 5.030
Model 3 : 5.847
Model 4 : 5.234
Model 5 : 5.909
Model 6 : 4.912
Model 7 : 5.504
Model 8 : 5.274
Model 9 : 4.941
Model 10 : 5.637
Model 11 : 5.235
Model 12 : 5.123
Model 13 : 5.520
Model 14 : 5.144
Model 15 : 5.228
Model 16 : 5.501
Model 17 : 4.991
Model 18 : 5.328
Model 19 : 5.539
Model 20 : 4.984

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!

 648 GLY   ( 186-)  A   2.18   13
1227 GLY   (  72-)  A   2.04   14
1974 PRO   ( 126-)  A   1.99   10
2156 PRO   (  77-)  A 1  1.98   11
2849 PRO   (  77-)  A 1  1.86   10
 534 GLY   (  72-)  A   1.81   18
 303 GLY   (  72-)  A   1.79   11
2667 PRO   ( 126-)  A 1  1.75   12
2205 PRO   ( 126-)  A 1  1.67   10
 186 GLY   ( 186-)  A   1.66   18
 126 PRO   ( 126-)  A   1.64   10
 588 PRO   ( 126-)  A   1.63   11
 819 PRO   ( 126-)  A   1.62   10
3822 PRO   ( 126-)  A 1  1.61   10
1281 PRO   ( 126-)  A   1.61   10
2436 PRO   ( 126-)  A 1  1.60   10
 996 GLY   (  72-)  A   1.57   18
4284 PRO   ( 126-)  A 1  1.54   11
2898 PRO   ( 126-)  A 1  1.53   11
 357 PRO   ( 126-)  A   1.53   11

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].

3475 PRO   (  10-)  A 1 -115.4 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.

2553 MET   (  12-)  A 1    SD  <-> 2687 VAL   ( 146-)  A 1    CG2    0.05    3.35
1021 HIS   (  97-)  A      NE2 <-> 1025 ASN   ( 101-)  A      ND2    0.04    2.96
3703 GLU   (   7-)  A 1    C   <-> 3786 CYS   (  90-)  A 1    SG     0.03    3.37
3986 HIS   (  59-)  A 1    NE2 <-> 3990 ARG   (  63-)  A 1    NE     0.03    2.97
2658 PHE   ( 117-)  A 1    CE2 <-> 2673 CYS   ( 132-)  A 1    SG     0.03    3.37
3484 ARG   (  19-)  A 1    NH2 <-> 3696 HIS   ( 231-)  A 1    NE2    0.02    2.98
2706 PHE   ( 165-)  A 1    CE2 <-> 2713 LEU   ( 172-)  A 1    CD1    0.02    3.18
3562 HIS   (  97-)  A 1    NE2 <-> 3566 ASN   ( 101-)  A 1    ND2    0.02    2.98
 156 ASP   ( 156-)  A      CG  <->  157 LYS   ( 157-)  A      N      0.02    2.98
1714 HIS   (  97-)  A      NE2 <-> 1783 ASN   ( 166-)  A      CG     0.01    3.09
2778 MET   (   6-)  A 1    CE  <-> 2862 CYS   (  90-)  A 1    SG     0.01    3.39
1773 ASP   ( 156-)  A      CG  <-> 1774 LYS   ( 157-)  A      N      0.01    2.99

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


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