WHAT IF Check report

This file was created 2012-01-30 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 pdb2l2s.ent

Checks that need to be done early-on in validation

Warning: Ligands for which topology could not be determined

The ligands in the table below are too complicated for the automatic topology determination. WHAT IF uses a local copy of Daan van Aalten's Dundee PRODRG server to automatically generate topology information for ligands. Some molecules are too complicated for this software. If that happens, WHAT IF / WHAT-CHECK continue with a simplified topology that lacks certain information. Ligands with a simplified topology can, for example, not form hydrogen bonds, and that reduces the accuracy of all hydrogen bond related checking facilities.

The reason for topology generation failure is indicated. 'Atom types' indicates that the ligand contains atom types not known to PRODRUG. 'Attached' means that the ligand is covalently attached to a macromolecule. 'Size' indicates that the ligand has either too many atoms, or too many bonds, angles, or torsion angles. 'Fragmented' is written when the ligand is not one fully covalently connected molecule but consists of multiple fragments. 'N/O only' is given when the ligand contains only N and/or O atoms. 'OK' indicates that the automatic topology generation succeeded.

2341 L2S   ( 130-)  A  2
2342 L2S   ( 130-)  A  3
2343 L2S   ( 130-)  A  4
2344 L2S   ( 130-)  A  5
2345 L2S   ( 130-)  A  6
2346 L2S   ( 130-)  A  7
2347 L2S   ( 130-)  A  8
2348 L2S   ( 130-)  A  9
2349 L2S   ( 130-)  A 10
2350 L2S   ( 130-)  A 11
2351 L2S   ( 130-)  A 12
2352 L2S   ( 130-)  A 13
2353 L2S   ( 130-)  A 14
2354 L2S   ( 130-)  A 15
2355 L2S   ( 130-)  A 16
2356 L2S   ( 130-)  A 17
2357 L2S   ( 130-)  A 18
2358 L2S   ( 130-)  A 19
2359 L2S   ( 130-)  A 20
2360 L2S   ( 130-)  A  1

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 GLY   (   3-)  A    Zero
   4 SER   (   4-)  A    Zero
   5 MET   (   5-)  A    Zero
   6 THR   (   6-)  A    Zero
   7 VAL   (   7-)  A    Zero
   8 VAL   (   8-)  A    Zero
   9 THR   (   9-)  A    Zero
  10 THR   (  10-)  A    Zero
  11 GLU   (  11-)  A    Zero
  12 SER   (  12-)  A    Zero
  13 GLY   (  13-)  A    Zero
  14 LEU   (  14-)  A    Zero
  15 LYS   (  15-)  A    Zero
  16 TYR   (  16-)  A    Zero
  17 GLU   (  17-)  A    Zero
  18 ASP   (  18-)  A    Zero
  19 LEU   (  19-)  A    Zero
  20 THR   (  20-)  A    Zero
  21 GLU   (  21-)  A    Zero
  22 GLY   (  22-)  A    Zero
  23 SER   (  23-)  A    Zero
  24 GLY   (  24-)  A    Zero
  25 ALA   (  25-)  A    Zero
And so on for a total of 2340 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 : 0.118
Model 2 : 0.117
Model 3 : 0.115
Model 4 : 0.117
Model 5 : 0.116
Model 6 : 0.116
Model 7 : 0.116
Model 8 : 0.116
Model 9 : 0.117
Model 10 : 0.118
Model 11 : 0.117
Model 12 : 0.116
Model 13 : 0.116
Model 14 : 0.116
Model 15 : 0.117
Model 16 : 0.117
Model 17 : 0.117
Model 18 : 0.117
Model 19 : 0.116
Model 20 : 0.117

Note: Per-model averages for bond-angle check

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

Model 1 : 0.250
Model 2 : 0.251
Model 3 : 0.250
Model 4 : 0.250
Model 5 : 0.251
Model 6 : 0.250
Model 7 : 0.251
Model 8 : 0.250
Model 9 : 0.250
Model 10 : 0.249
Model 11 : 0.250
Model 12 : 0.250
Model 13 : 0.250
Model 14 : 0.251
Model 15 : 0.249
Model 16 : 0.249
Model 17 : 0.249
Model 18 : 0.250
Model 19 : 0.249
Model 20 : 0.250

Note: Per-model averages for chirality check

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

Model 1 : 0.296
Model 2 : 0.297
Model 3 : 0.296
Model 4 : 0.296
Model 5 : 0.296
Model 6 : 0.296
Model 7 : 0.296
Model 8 : 0.298
Model 9 : 0.297
Model 10 : 0.297
Model 11 : 0.297
Model 12 : 0.296
Model 13 : 0.297
Model 14 : 0.297
Model 15 : 0.296
Model 16 : 0.297
Model 17 : 0.297
Model 18 : 0.295
Model 19 : 0.295
Model 20 : 0.297

Torsion-related checks

Warning: Ramachandran Z-score low

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

Ramachandran Z-score : -3.291

Note: Per-model averages for Ramachandran check

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

Model 1 : -2.845
Model 2 : -2.993
Model 3 : -3.287
Model 4 : -2.942
Model 5 : -3.635
Model 6 : -2.938
Model 7 : -3.249
Model 8 : -3.472
Model 9 : -3.645
Model 10 : -2.962
Model 11 : -3.216
Model 12 : -3.610
Model 13 : -3.165
Model 14 : -3.553
Model 15 : -3.491
Model 16 : -3.152
Model 17 : -2.622
Model 18 : -3.807
Model 19 : -3.586
Model 20 : -3.646

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.

 825 THR   (   6-)  A    -3.5
1073 THR   (  20-)  A 1   -2.9
1775 THR   (  20-)  A 1   -2.8
 137 THR   (  20-)  A    -2.7
1307 THR   (  20-)  A 1   -2.7
 956 THR   (  20-)  A    -2.7
  20 THR   (  20-)  A    -2.7
 371 THR   (  20-)  A    -2.6
1995 THR   (   6-)  A 1   -2.6
2012 SER   (  23-)  A 1   -2.6
1057 SER   (   4-)  A 1   -2.5
 842 SER   (  23-)  A    -2.5
 257 SER   (  23-)  A    -2.5
 903 ARG   (  84-)  A    -2.5
1910 THR   (  38-)  A 1   -2.4
 605 THR   (  20-)  A    -2.4
 254 THR   (  20-)  A    -2.4
 942 THR   (   6-)  A    -2.4
1937 MET   (  65-)  A 1   -2.4
1892 THR   (  20-)  A 1   -2.4
 722 THR   (  20-)  A    -2.4
1559 THR   (  38-)  A 1   -2.4
1642 SER   (   4-)  A 1   -2.4
1820 MET   (  65-)  A 1   -2.4
1994 MET   (   5-)  A 1   -2.4
And so on for a total of 177 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.

  25 ALA   (  25-)  A  Poor phi/psi
  48 ASP   (  48-)  A  Poor phi/psi
  54 ASN   (  54-)  A  Poor phi/psi
  64 GLY   (  64-)  A  Poor phi/psi
  76 GLY   (  76-)  A  Poor phi/psi
 100 GLY   ( 100-)  A  Poor phi/psi
 106 ALA   ( 106-)  A  Poor phi/psi
 142 ALA   (  25-)  A  Poor phi/psi
 165 ASP   (  48-)  A  Poor phi/psi
 171 ASN   (  54-)  A  Poor phi/psi
 219 ILE   ( 102-)  A  Poor phi/psi
 257 SER   (  23-)  A  Poor phi/psi
 259 ALA   (  25-)  A  Poor phi/psi
 282 ASP   (  48-)  A  Poor phi/psi
 288 ASN   (  54-)  A  Poor phi/psi
 310 GLY   (  76-)  A  Poor phi/psi
 399 ASP   (  48-)  A  Poor phi/psi
 405 ASN   (  54-)  A  Poor phi/psi
 427 GLY   (  76-)  A  Poor phi/psi
 453 ILE   ( 102-)  A  Poor phi/psi
 456 ASN   ( 105-)  A  Poor phi/psi
 516 ASP   (  48-)  A  Poor phi/psi
 522 ASN   (  54-)  A  Poor phi/psi
 531 GLY   (  63-)  A  Poor phi/psi
 544 GLY   (  76-)  A  Poor phi/psi
And so on for a total of 101 lines.

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

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

chi-1/chi-2 correlation Z-score : -6.574

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 : -7.217
Model 2 : -6.549
Model 3 : -6.883
Model 4 : -6.565
Model 5 : -6.658
Model 6 : -7.058
Model 7 : -6.134
Model 8 : -6.561
Model 9 : -6.331
Model 10 : -6.499
Model 11 : -6.867
Model 12 : -6.128
Model 13 : -6.033
Model 14 : -6.453
Model 15 : -6.883
Model 16 : -6.575
Model 17 : -6.281
Model 18 : -6.218
Model 19 : -6.771
Model 20 : -6.810

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.

 168 LYS   (  51-)  A    0.36

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 MET   (   5-)  A      0
  12 SER   (  12-)  A      0
  15 LYS   (  15-)  A      0
  23 SER   (  23-)  A      0
  29 ALA   (  29-)  A      0
  41 LEU   (  41-)  A      0
  46 LYS   (  46-)  A      0
  47 PHE   (  47-)  A      0
  48 ASP   (  48-)  A      0
  53 ARG   (  53-)  A      0
  54 ASN   (  54-)  A      0
  61 LEU   (  61-)  A      0
  65 MET   (  65-)  A      0
  67 ILE   (  67-)  A      0
  77 MET   (  77-)  A      0
  79 VAL   (  79-)  A      0
  91 LEU   (  91-)  A      0
  93 TYR   (  93-)  A      0
  96 ARG   (  96-)  A      0
 101 VAL   ( 101-)  A      0
 102 ILE   ( 102-)  A      0
 104 PRO   ( 104-)  A      0
 105 ASN   ( 105-)  A      0
 106 ALA   ( 106-)  A      0
 116 ASP   ( 116-)  A      0
And so on for a total of 935 lines.

Warning: Omega angles too tightly restrained

The omega angles for trans-peptide bonds in a structure are expected to give a gaussian distribution with the average around +178 degrees and a standard deviation around 5.5 degrees. These expected values were obtained from very accurately determined structures. Many protein structures are too tightly restrained. This seems to be the case with the current structure too, as the observed standard deviation is below 4.0 degrees.

Standard deviation of omega values : 0.000

Note: Per-model averages for omega angle check

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

Model 1 : 0.088
Model 2 : 0.141
Model 3 : 0.169
Model 4 : 0.115
Model 5 : 0.077
Model 6 : 0.099
Model 7 : 0.140
Model 8 : 0.143
Model 9 : 0.106
Model 10 : 0.056
Model 11 : 0.076
Model 12 : 0.000
Model 13 : 0.000
Model 14 : 0.000
Model 15 : 0.063
Model 16 : 0.094
Model 17 : 0.119
Model 18 : 0.114
Model 19 : 0.144
Model 20 : 0.076

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!

2286 GLY   (  63-)  A 2  2.17   18
 297 GLY   (  63-)  A   2.08   18
 237 GLY   (   3-)  A   1.97   17
1017 GLY   (  81-)  A   1.81   19
 315 GLY   (  81-)  A   1.76   21
1368 GLY   (  81-)  A 1  1.75   21
 432 GLY   (  81-)  A   1.75   18
1134 GLY   (  81-)  A 1  1.74   20
2070 GLY   (  81-)  A 1  1.72   21
1466 GLY   (  62-)  A 1  1.71   80
2304 GLY   (  81-)  A 2  1.68   13
2323 GLY   ( 100-)  A 2  1.68   13
1836 GLY   (  81-)  A 1  1.66   21
 198 GLY   (  81-)  A   1.64   22
2187 GLY   (  81-)  A 1  1.61   23
 549 GLY   (  81-)  A   1.59   19
 331 GLY   (  97-)  A   1.58   14
2119 GLY   (  13-)  A 1  1.57   80
1719 GLY   (  81-)  A 1  1.57   22
1953 GLY   (  81-)  A 1  1.56   18
 949 GLY   (  13-)  A   1.52   80
 179 GLY   (  62-)  A   1.51   29
1300 GLY   (  13-)  A 1  1.51   80
 481 GLY   (  13-)  A   1.50   80

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.

1241 ASP   (  71-)  A 1    CG  <-> 1245 GLN   (  75-)  A 1    NE2    0.15    2.95
1358 ASP   (  71-)  A 1    CG  <-> 1359 GLU   (  72-)  A 1    N      0.13    2.87
1716 LYS   (  78-)  A 1    C   <-> 1752 LEU   ( 114-)  A 1    CD1    0.12    3.08
  78 LYS   (  78-)  A      C   <->  114 LEU   ( 114-)  A      CD1    0.12    3.08
2296 GLY   (  73-)  A 2    C   <-> 2300 MET   (  77-)  A 2    SD     0.11    3.29
1247 MET   (  77-)  A 1    SD  <-> 1251 GLY   (  81-)  A 1    C      0.10    3.30
2296 GLY   (  73-)  A 2    C   <-> 2300 MET   (  77-)  A 2    CE     0.09    3.11
1548 ALA   (  27-)  A 1    CB  <-> 1595 VAL   (  74-)  A 1    CG2    0.08    3.12
  82 VAL   (  82-)  A      CG2 <->  113 GLU   ( 113-)  A      CD     0.08    3.12
1040 PRO   ( 104-)  A      C   <-> 1041 ASN   ( 105-)  A      CG     0.07    3.03
 787 LEU   (  85-)  A      N   <->  812 PHE   ( 110-)  A      O      0.07    2.63
 319 LEU   (  85-)  A      N   <->  344 PHE   ( 110-)  A      O      0.07    2.63
1720 VAL   (  82-)  A 1    CG1 <-> 1751 GLU   ( 113-)  A 1    CD     0.07    3.13
 897 LYS   (  78-)  A      C   <->  933 LEU   ( 114-)  A      CD2    0.07    3.13
1840 LEU   (  85-)  A 1    N   <-> 1865 PHE   ( 110-)  A 1    O      0.06    2.64
1138 LEU   (  85-)  A 1    N   <-> 1163 PHE   ( 110-)  A 1    O      0.06    2.64
1255 LEU   (  85-)  A 1    N   <-> 1280 PHE   ( 110-)  A 1    O      0.06    2.64
1957 LEU   (  85-)  A 1    N   <-> 1982 PHE   ( 110-)  A 1    O      0.05    2.65
1723 LEU   (  85-)  A 1    N   <-> 1748 PHE   ( 110-)  A 1    O      0.05    2.65
  77 MET   (  77-)  A      CE  <->   83 ARG   (  83-)  A      N      0.05    3.05
1021 LEU   (  85-)  A      N   <-> 1046 PHE   ( 110-)  A      O      0.05    2.65
 202 LEU   (  85-)  A      N   <->  227 PHE   ( 110-)  A      O      0.05    2.65
1606 LEU   (  85-)  A 1    N   <-> 1631 PHE   ( 110-)  A 1    O      0.05    2.65
 670 LEU   (  85-)  A      N   <->  695 PHE   ( 110-)  A      O      0.05    2.65
1556 VAL   (  35-)  A 1    CG1 <-> 1635 LEU   ( 114-)  A 1    CD1    0.05    3.15
And so on for a total of 136 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: 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