WHAT IF Check report

This file was created 2012-01-04 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 pdb1m3a.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 CYS   ( 135-)  A    Zero
   2 TYR   ( 136-)  A    Zero
   3 VAL   ( 137-)  A    Zero
   4 ARG   ( 138-)  A    Zero
   5 ALA   ( 139-)  A    Zero
   6 LEU   ( 140-)  A    Zero
   7 PHE   ( 141-)  A    Zero
   8 ASP   ( 142-)  A    Zero
   9 PHE   ( 143-)  A    Zero
  10 ASN   ( 144-)  A    Zero
  11 GLY   ( 145-)  A    Zero
  12 ASN   ( 146-)  A    Zero
  13 ASP   ( 147-)  A    Zero
  14 GLU   ( 148-)  A    Zero
  15 GLU   ( 149-)  A    Zero
  16 ASP   ( 150-)  A    Zero
  17 LEU   ( 151-)  A    Zero
  18 PRO   ( 152-)  A    Zero
  19 PHE   ( 153-)  A    Zero
  20 LYS   ( 154-)  A    Zero
  21 LYS   ( 155-)  A    Zero
  22 GLY   ( 156-)  A    Zero
  23 ASP   ( 157-)  A    Zero
  24 ILE   ( 158-)  A    Zero
  25 LEU   ( 159-)  A    Zero
And so on for a total of 1140 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 : 0.531
Model 2 : 0.533
Model 3 : 0.532
Model 4 : 0.535
Model 5 : 0.534
Model 6 : 0.535
Model 7 : 0.530
Model 8 : 0.535
Model 9 : 0.534
Model 10 : 0.534
Model 11 : 0.532
Model 12 : 0.534
Model 13 : 0.532
Model 14 : 0.533
Model 15 : 0.532
Model 16 : 0.535
Model 17 : 0.535
Model 18 : 0.534
Model 19 : 0.532
Model 20 : 0.533

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 : 0.898
Model 2 : 0.899
Model 3 : 0.901
Model 4 : 0.901
Model 5 : 0.900
Model 6 : 0.902
Model 7 : 0.900
Model 8 : 0.901
Model 9 : 0.900
Model 10 : 0.904
Model 11 : 0.902
Model 12 : 0.903
Model 13 : 0.898
Model 14 : 0.901
Model 15 : 0.900
Model 16 : 0.901
Model 17 : 0.900
Model 18 : 0.903
Model 19 : 0.900
Model 20 : 0.902

Note: Per-model averages for chirality check

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

Model 1 : 0.687
Model 2 : 0.689
Model 3 : 0.688
Model 4 : 0.686
Model 5 : 0.689
Model 6 : 0.691
Model 7 : 0.686
Model 8 : 0.690
Model 9 : 0.687
Model 10 : 0.690
Model 11 : 0.688
Model 12 : 0.688
Model 13 : 0.688
Model 14 : 0.693
Model 15 : 0.693
Model 16 : 0.687
Model 17 : 0.687
Model 18 : 0.689
Model 19 : 0.689
Model 20 : 0.689

Torsion-related checks

Error: Ramachandran Z-score very low

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

Ramachandran Z-score : -5.859

Note: Per-model averages for Ramachandran check

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

Model 1 : -5.371
Model 2 : -6.243
Model 3 : -6.109
Model 4 : -5.861
Model 5 : -6.134
Model 6 : -5.833
Model 7 : -6.097
Model 8 : -5.904
Model 9 : -5.951
Model 10 : -5.190
Model 11 : -5.513
Model 12 : -5.900
Model 13 : -5.773
Model 14 : -6.254
Model 15 : -5.999
Model 16 : -5.828
Model 17 : -5.124
Model 18 : -5.905
Model 19 : -5.824
Model 20 : -6.364

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.

1102 PHE   ( 153-)  A 2   -3.4
 287 TYR   ( 136-)  A    -3.3
 760 PHE   ( 153-)  A 1   -3.2
1045 PHE   ( 153-)  A 1   -3.1
 589 PHE   ( 153-)  A 1   -3.1
  19 PHE   ( 153-)  A    -3.0
 686 TYR   ( 136-)  A 1   -2.9
 180 PHE   ( 143-)  A    -2.8
 771 LYS   ( 164-)  A 1   -2.8
 864 PHE   ( 143-)  A 1   -2.7
 372 LYS   ( 164-)  A    -2.7
 714 LYS   ( 164-)  A 1   -2.7
 315 LYS   ( 164-)  A    -2.7
 874 PHE   ( 153-)  A 1   -2.7
 144 LYS   ( 164-)  A    -2.7
1092 PHE   ( 143-)  A 2   -2.6
 657 LYS   ( 164-)  A 1   -2.6
 696 ASN   ( 146-)  A 1   -2.6
 543 LYS   ( 164-)  A 1   -2.6
 294 PHE   ( 143-)  A    -2.6
 753 ASN   ( 146-)  A 1   -2.5
 807 PHE   ( 143-)  A 1   -2.5
  30 LYS   ( 164-)  A    -2.5
 981 ASN   ( 146-)  A 1   -2.5
 354 ASN   ( 146-)  A    -2.5
And so on for a total of 185 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.

   9 PHE   ( 143-)  A  Poor phi/psi
  12 ASN   ( 146-)  A  Poor phi/psi
  13 ASP   ( 147-)  A  Poor phi/psi
  15 GLU   ( 149-)  A  Poor phi/psi
  40 ASP   ( 174-)  A  Poor phi/psi
  66 PHE   ( 143-)  A  Poor phi/psi
  72 GLU   ( 149-)  A  Poor phi/psi
  85 ARG   ( 162-)  A  Poor phi/psi
 123 PHE   ( 143-)  A  Poor phi/psi
 126 ASN   ( 146-)  A  Poor phi/psi
 127 ASP   ( 147-)  A  Poor phi/psi
 130 ASP   ( 150-)  A  Poor phi/psi
 148 GLN   ( 168-)  A  Poor phi/psi
 154 ASP   ( 174-)  A  Poor phi/psi
 183 ASN   ( 146-)  A  Poor phi/psi
 186 GLU   ( 149-)  A  Poor phi/psi
 211 ASP   ( 174-)  A  Poor phi/psi
 241 ASP   ( 147-)  A  Poor phi/psi
 242 GLU   ( 148-)  A  Poor phi/psi
 250 GLY   ( 156-)  A  Poor phi/psi
 262 GLN   ( 168-)  A  Poor phi/psi
 268 ASP   ( 174-)  A  Poor phi/psi
 300 GLU   ( 149-)  A  Poor phi/psi
 325 ASP   ( 174-)  A  Poor phi/psi
 354 ASN   ( 146-)  A  Poor phi/psi
And so on for a total of 76 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 : -7.482

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 : -6.788
Model 2 : -7.342
Model 3 : -7.530
Model 4 : -7.408
Model 5 : -6.993
Model 6 : -7.626
Model 7 : -7.240
Model 8 : -7.764
Model 9 : -8.131
Model 10 : -7.176
Model 11 : -8.061
Model 12 : -7.530
Model 13 : -8.154
Model 14 : -8.163
Model 15 : -7.417
Model 16 : -7.601
Model 17 : -7.378
Model 18 : -6.643
Model 19 : -7.845
Model 20 : -6.846

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.

 972 VAL   ( 137-)  A 1   0.35
 744 VAL   ( 137-)  A 1   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!

   6 LEU   ( 140-)  A      0
   9 PHE   ( 143-)  A      0
  10 ASN   ( 144-)  A      0
  12 ASN   ( 146-)  A      0
  13 ASP   ( 147-)  A      0
  14 GLU   ( 148-)  A      0
  15 GLU   ( 149-)  A      0
  16 ASP   ( 150-)  A      0
  21 LYS   ( 155-)  A      0
  28 ARG   ( 162-)  A      0
  30 LYS   ( 164-)  A      0
  31 PRO   ( 165-)  A      0
  32 GLU   ( 166-)  A      0
  33 GLU   ( 167-)  A      0
  34 GLN   ( 168-)  A      0
  35 TRP   ( 169-)  A      0
  36 TRP   ( 170-)  A      0
  37 ASN   ( 171-)  A      0
  42 GLU   ( 176-)  A      0
  44 LYS   ( 178-)  A      0
  45 ARG   ( 179-)  A      0
  47 MET   ( 181-)  A      0
  49 PRO   ( 183-)  A      0
  52 TYR   ( 186-)  A      0
  55 LYS   ( 189-)  A      0
And so on for a total of 711 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 : 0.000
Model 2 : 0.107
Model 3 : 0.135
Model 4 : 0.101
Model 5 : 0.153
Model 6 : 0.000
Model 7 : 0.000
Model 8 : 0.084
Model 9 : 0.094
Model 10 : 0.081
Model 11 : 0.000
Model 12 : 0.000
Model 13 : 0.000
Model 14 : 0.049
Model 15 : 0.000
Model 16 : 0.000
Model 17 : 0.060
Model 18 : 0.000
Model 19 : 0.057
Model 20 : 0.000

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!

 638 GLY   ( 145-)  A 1  2.14   29
 980 GLY   ( 145-)  A 1  1.97   10
 353 GLY   ( 145-)  A   1.75   23
 410 GLY   ( 145-)  A   1.70   10
 592 GLY   ( 156-)  A 1  1.58   80
 877 GLY   ( 156-)  A 1  1.58   80
 193 GLY   ( 156-)  A   1.56   80
1105 GLY   ( 156-)  A 2  1.55   80
 136 GLY   ( 156-)  A   1.51   80

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]

  18 PRO   ( 152-)  A    0.18 LOW
  31 PRO   ( 165-)  A    0.18 LOW
  49 PRO   ( 183-)  A    0.18 LOW
  51 PRO   ( 185-)  A    0.18 LOW
  75 PRO   ( 152-)  A    0.18 LOW
  88 PRO   ( 165-)  A    0.18 LOW
 106 PRO   ( 183-)  A    0.18 LOW
 108 PRO   ( 185-)  A    0.18 LOW
 132 PRO   ( 152-)  A    0.18 LOW
 145 PRO   ( 165-)  A    0.18 LOW
 163 PRO   ( 183-)  A    0.18 LOW
 165 PRO   ( 185-)  A    0.18 LOW
 189 PRO   ( 152-)  A    0.18 LOW
 202 PRO   ( 165-)  A    0.18 LOW
 220 PRO   ( 183-)  A    0.18 LOW
 222 PRO   ( 185-)  A    0.18 LOW
 246 PRO   ( 152-)  A    0.18 LOW
 259 PRO   ( 165-)  A    0.18 LOW
 277 PRO   ( 183-)  A    0.18 LOW
 279 PRO   ( 185-)  A    0.18 LOW
 303 PRO   ( 152-)  A    0.18 LOW
 316 PRO   ( 165-)  A    0.18 LOW
 334 PRO   ( 183-)  A    0.18 LOW
 336 PRO   ( 185-)  A    0.18 LOW
 360 PRO   ( 152-)  A    0.18 LOW
And so on for a total of 80 lines.

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.

 343 CYS   ( 135-)  A      N   <->  399 GLY   ( 191-)  A      C      1.61    1.49
  58 CYS   ( 135-)  A      N   <->  114 GLY   ( 191-)  A      C      1.61    1.49
 457 CYS   ( 135-)  A      N   <->  513 GLY   ( 191-)  A      C      1.61    1.49
 742 CYS   ( 135-)  A 1    N   <->  798 GLY   ( 191-)  A 1    C      1.60    1.50
 229 CYS   ( 135-)  A      N   <->  285 GLY   ( 191-)  A      C      1.60    1.50
1027 CYS   ( 135-)  A 1    N   <-> 1083 GLY   ( 191-)  A 1    C      1.60    1.50
 913 CYS   ( 135-)  A 1    N   <->  969 GLY   ( 191-)  A 1    C      1.60    1.50
 799 CYS   ( 135-)  A 1    N   <->  855 GLY   ( 191-)  A 1    C      1.60    1.50
 685 CYS   ( 135-)  A 1    N   <->  741 GLY   ( 191-)  A 1    C      1.60    1.50
 286 CYS   ( 135-)  A      N   <->  342 GLY   ( 191-)  A      C      1.60    1.50
 571 CYS   ( 135-)  A 1    N   <->  627 GLY   ( 191-)  A 1    C      1.60    1.50
 856 CYS   ( 135-)  A 1    N   <->  912 GLY   ( 191-)  A 1    C      1.59    1.51
 628 CYS   ( 135-)  A 1    N   <->  684 GLY   ( 191-)  A 1    C      1.59    1.51
1084 CYS   ( 135-)  A 2    N   <-> 1140 GLY   ( 191-)  A 2    C      1.59    1.51
 400 CYS   ( 135-)  A      N   <->  456 GLY   ( 191-)  A      C      1.59    1.51
 115 CYS   ( 135-)  A      N   <->  171 GLY   ( 191-)  A      C      1.58    1.52
 970 CYS   ( 135-)  A 1    N   <-> 1026 GLY   ( 191-)  A 1    C      1.58    1.52
   1 CYS   ( 135-)  A      N   <->   57 GLY   ( 191-)  A      C      1.58    1.52
 514 CYS   ( 135-)  A 1    N   <->  570 GLY   ( 191-)  A 1    C      1.58    1.52
 172 CYS   ( 135-)  A      N   <->  228 GLY   ( 191-)  A      C      1.58    1.52
1019 VAL   ( 184-)  A 1    N   <-> 1020 PRO   ( 185-)  A 1    CD     0.62    2.38
1133 VAL   ( 184-)  A 2    N   <-> 1134 PRO   ( 185-)  A 2    CD     0.62    2.38
 905 VAL   ( 184-)  A 1    N   <->  906 PRO   ( 185-)  A 1    CD     0.61    2.39
1076 VAL   ( 184-)  A 1    N   <-> 1077 PRO   ( 185-)  A 1    CD     0.61    2.39
 115 CYS   ( 135-)  A      N   <->  171 GLY   ( 191-)  A      CA     0.61    2.49
And so on for a total of 1099 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


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