WHAT IF Check report

This file was created 2012-01-19 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 pdb1x6b.ent

Non-validating, descriptive output paragraph

Note: Ramachandran plot

In this Ramachandran plot x-signs represent glycines, squares represent prolines, and plus-signs represent the other residues. If too many plus- signs fall outside the contoured areas then the molecule is poorly refined (or worse). Proline can only occur in the narrow region around phi=-60 that also falls within the other contour islands.

In a colour picture, the residues that are part of a helix are shown in blue, strand residues in red. Preferred regions for helical residues are drawn in blue, for strand residues in red, and for all other residues in green. A full explanation of the Ramachandran plot together with a series of examples can be found at the WHAT_CHECK website.

Chain identifier: A; Model number 1

Note: Ramachandran plot

Chain identifier: A; Model number 2

Note: Ramachandran plot

Chain identifier: A; Model number 3

Note: Ramachandran plot

Chain identifier: A; Model number 4

Note: Ramachandran plot

Chain identifier: A; Model number 5

Note: Ramachandran plot

Chain identifier: A; Model number 6

Note: Ramachandran plot

Chain identifier: A; Model number 7

Note: Ramachandran plot

Chain identifier: A; Model number 8

Note: Ramachandran plot

Chain identifier: A; Model number 9

Note: Ramachandran plot

Chain identifier: A; Model number 10

Note: Ramachandran plot

Chain identifier: A; Model number 11

Note: Ramachandran plot

Chain identifier: A; Model number 12

Note: Ramachandran plot

Chain identifier: A; Model number 13

Note: Ramachandran plot

Chain identifier: A; Model number 14

Note: Ramachandran plot

Chain identifier: A; Model number 15

Note: Ramachandran plot

Chain identifier: A; Model number 16

Note: Ramachandran plot

Chain identifier: A; Model number 17

Note: Ramachandran plot

Chain identifier: A; Model number 18

Note: Ramachandran plot

Chain identifier: A; Model number 19

Note: Ramachandran plot

Chain identifier: A; Model number 20

Coordinate problems, unexpected atoms, B-factor and occupancy checks

Warning: B-factors outside the range 0.0 - 100.0

In principle, B-factors can have a very wide range of values, but in practice, B-factors should not be zero while B-factors above 100.0 are a good indicator that the location of that atom is meaningless. Be aware that the cutoff at 100.0 is arbitrary. 'High' indicates that atoms with a B-factor > 100.0 were observed; 'Zero' indicates that atoms with a B-factor of zero were observed.

   1 GLY   (   1-)  A    Zero
   2 SER   (   2-)  A    Zero
   3 SER   (   3-)  A    Zero
   4 GLY   (   4-)  A    Zero
   5 SER   (   5-)  A    Zero
   6 SER   (   6-)  A    Zero
   7 GLY   (   7-)  A    Zero
   8 TRP   (   8-)  A    Zero
   9 GLN   (   9-)  A    Zero
  10 GLY   (  10-)  A    Zero
  11 LEU   (  11-)  A    Zero
  12 SER   (  12-)  A    Zero
  13 SER   (  13-)  A    Zero
  14 LYS   (  14-)  A    Zero
  15 GLY   (  15-)  A    Zero
  16 ASP   (  16-)  A    Zero
  17 LEU   (  17-)  A    Zero
  18 PRO   (  18-)  A    Zero
  19 GLN   (  19-)  A    Zero
  20 VAL   (  20-)  A    Zero
  21 GLU   (  21-)  A    Zero
  22 ILE   (  22-)  A    Zero
  23 THR   (  23-)  A    Zero
  24 LYS   (  24-)  A    Zero
  25 ALA   (  25-)  A    Zero
And so on for a total of 1580 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 : 0.494
Model 2 : 0.495
Model 3 : 0.494
Model 4 : 0.494
Model 5 : 0.495
Model 6 : 0.494
Model 7 : 0.496
Model 8 : 0.494
Model 9 : 0.495
Model 10 : 0.496
Model 11 : 0.493
Model 12 : 0.494
Model 13 : 0.494
Model 14 : 0.493
Model 15 : 0.495
Model 16 : 0.495
Model 17 : 0.495
Model 18 : 0.496
Model 19 : 0.494
Model 20 : 0.494

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 : 0.902
Model 2 : 0.903
Model 3 : 0.903
Model 4 : 0.902
Model 5 : 0.903
Model 6 : 0.904
Model 7 : 0.903
Model 8 : 0.902
Model 9 : 0.901
Model 10 : 0.902
Model 11 : 0.902
Model 12 : 0.905
Model 13 : 0.903
Model 14 : 0.903
Model 15 : 0.902
Model 16 : 0.903
Model 17 : 0.902
Model 18 : 0.904
Model 19 : 0.904
Model 20 : 0.903

Note: Per-model averages for chirality check

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

Model 1 : 0.627
Model 2 : 0.626
Model 3 : 0.629
Model 4 : 0.626
Model 5 : 0.628
Model 6 : 0.628
Model 7 : 0.626
Model 8 : 0.626
Model 9 : 0.625
Model 10 : 0.627
Model 11 : 0.626
Model 12 : 0.628
Model 13 : 0.626
Model 14 : 0.627
Model 15 : 0.628
Model 16 : 0.626
Model 17 : 0.627
Model 18 : 0.626
Model 19 : 0.628
Model 20 : 0.627

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 : -4.571

Note: Per-model averages for Ramachandran check

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

Model 1 : -4.702
Model 2 : -4.299
Model 3 : -4.658
Model 4 : -5.177
Model 5 : -4.591
Model 6 : -4.528
Model 7 : -4.300
Model 8 : -4.507
Model 9 : -4.519
Model 10 : -4.780
Model 11 : -4.191
Model 12 : -4.545
Model 13 : -4.894
Model 14 : -4.272
Model 15 : -5.112
Model 16 : -4.397
Model 17 : -4.174
Model 18 : -5.224
Model 19 : -4.728
Model 20 : -3.824

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.

 895 PHE   (  26-)  A 1   -2.8
 342 PHE   (  26-)  A    -2.8
1278 LYS   (  14-)  A 1   -2.8
 959 LEU   (  11-)  A 1   -2.7
 170 SER   (  12-)  A    -2.7
 864 SER   (  74-)  A 1   -2.7
1356 SER   (  13-)  A 1   -2.6
1026 SER   (  78-)  A 1   -2.6
 171 SER   (  13-)  A    -2.6
 551 SER   (  77-)  A    -2.6
1180 SER   (  74-)  A 1   -2.6
 714 SER   (   3-)  A 1   -2.6
1369 PHE   (  26-)  A 1   -2.6
1514 SER   (  13-)  A 2   -2.6
1559 ARG   (  58-)  A 2   -2.6
 243 SER   (   6-)  A    -2.6
1211 PHE   (  26-)  A 1   -2.6
1275 LEU   (  11-)  A 1   -2.6
  14 LYS   (  14-)  A    -2.5
 407 SER   (  12-)  A    -2.5
 466 ARG   (  71-)  A    -2.5
1040 SER   (  13-)  A 1   -2.5
1199 LYS   (  14-)  A 1   -2.5
 248 LEU   (  11-)  A    -2.5
 485 LEU   (  11-)  A    -2.5
And so on for a total of 262 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.

   3 SER   (   3-)  A  Poor phi/psi
   5 SER   (   5-)  A  Poor phi/psi
  11 LEU   (  11-)  A  Poor phi/psi
  39 ALA   (  39-)  A  Poor phi/psi
  76 PRO   (  76-)  A  Poor phi/psi
  85 SER   (   6-)  A  Poor phi/psi
 118 ALA   (  39-)  A  Poor phi/psi
 171 SER   (  13-)  A  Poor phi/psi
 197 ALA   (  39-)  A  Poor phi/psi
 239 SER   (   2-)  A  Poor phi/psi
 242 SER   (   5-)  A  Poor phi/psi
 243 SER   (   6-)  A  Poor phi/psi
 245 TRP   (   8-)  A  Poor phi/psi
 250 SER   (  13-)  A  Poor phi/psi
 276 ALA   (  39-)  A  Poor phi/psi
 328 SER   (  12-)  A  Poor phi/psi
 330 LYS   (  14-)  A  Poor phi/psi
 355 ALA   (  39-)  A  Poor phi/psi
 386 ALA   (  70-)  A  Poor phi/psi
 409 LYS   (  14-)  A  Poor phi/psi
 434 ALA   (  39-)  A  Poor phi/psi
 477 SER   (   3-)  A  Poor phi/psi
 486 SER   (  12-)  A  Poor phi/psi
 513 ALA   (  39-)  A  Poor phi/psi
 555 SER   (   2-)  A  Poor phi/psi
And so on for a total of 84 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 : -6.320

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 : -6.541
Model 2 : -6.422
Model 3 : -6.216
Model 4 : -5.840
Model 5 : -5.985
Model 6 : -6.406
Model 7 : -6.986
Model 8 : -7.100
Model 9 : -6.509
Model 10 : -6.562
Model 11 : -6.981
Model 12 : -5.716
Model 13 : -5.677
Model 14 : -5.636
Model 15 : -6.796
Model 16 : -6.660
Model 17 : -5.875
Model 18 : -5.928
Model 19 : -6.402
Model 20 : -6.154

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 SER   (   3-)  A      0
   5 SER   (   5-)  A      0
   6 SER   (   6-)  A      0
   8 TRP   (   8-)  A      0
   9 GLN   (   9-)  A      0
  11 LEU   (  11-)  A      0
  14 LYS   (  14-)  A      0
  16 ASP   (  16-)  A      0
  17 LEU   (  17-)  A      0
  29 LYS   (  29-)  A      0
  30 GLN   (  30-)  A      0
  38 GLN   (  38-)  A      0
  39 ALA   (  39-)  A      0
  49 ASP   (  49-)  A      0
  51 TRP   (  51-)  A      0
  57 LEU   (  57-)  A      0
  58 ARG   (  58-)  A      0
  69 PHE   (  69-)  A      0
  72 PHE   (  72-)  A      0
  74 SER   (  74-)  A      0
  76 PRO   (  76-)  A      0
  78 SER   (  78-)  A      0
  79 GLY   (  79-)  A      0
  80 GLY   (   1-)  A      0
  81 SER   (   2-)  A      0
And so on for a total of 874 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 : 0.250

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 : 0.000
Model 3 : 0.144
Model 4 : 0.057
Model 5 : 0.099
Model 6 : 0.067
Model 7 : 0.000
Model 8 : 0.036
Model 9 : 0.051
Model 10 : 0.000
Model 11 : 0.000
Model 12 : 0.000
Model 13 : 0.036
Model 14 : 0.066
Model 15 : 0.106
Model 16 : 0.104
Model 17 : 0.000
Model 18 : 0.127
Model 19 : 0.000
Model 20 : 0.106

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!

 478 GLY   (   4-)  A   2.82   31
 557 GLY   (   4-)  A   2.22   11
 320 GLY   (   4-)  A   2.17   12
1339 GLY   (  75-)  A 1  2.12   25
 563 GLY   (  10-)  A   2.10   14
1271 GLY   (   7-)  A 1  2.04   10
 247 GLY   (  10-)  A   1.88   20
1511 GLY   (  10-)  A 2  1.87   26
 241 GLY   (   4-)  A   1.81   14
 489 GLY   (  15-)  A   1.69   10
1508 GLY   (   7-)  A 2  1.68   23
 876 GLY   (   7-)  A 1  1.64   12
 639 GLY   (   7-)  A   1.64   10

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   (  18-)  A    0.18 LOW
  66 PRO   (  66-)  A    0.18 LOW
  76 PRO   (  76-)  A    0.18 LOW
  97 PRO   (  18-)  A    0.18 LOW
 145 PRO   (  66-)  A    0.18 LOW
 155 PRO   (  76-)  A    0.18 LOW
 176 PRO   (  18-)  A    0.18 LOW
 224 PRO   (  66-)  A    0.18 LOW
 234 PRO   (  76-)  A    0.18 LOW
 255 PRO   (  18-)  A    0.18 LOW
 303 PRO   (  66-)  A    0.18 LOW
 313 PRO   (  76-)  A    0.18 LOW
 334 PRO   (  18-)  A    0.18 LOW
 382 PRO   (  66-)  A    0.18 LOW
 392 PRO   (  76-)  A    0.18 LOW
 413 PRO   (  18-)  A    0.18 LOW
 461 PRO   (  66-)  A    0.18 LOW
 471 PRO   (  76-)  A    0.18 LOW
 492 PRO   (  18-)  A    0.18 LOW
 540 PRO   (  66-)  A    0.18 LOW
 550 PRO   (  76-)  A    0.18 LOW
 571 PRO   (  18-)  A    0.18 LOW
 619 PRO   (  66-)  A    0.18 LOW
 629 PRO   (  76-)  A    0.18 LOW
 650 PRO   (  18-)  A    0.18 LOW
And so on for a total of 60 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.

1467 LEU   (  45-)  A 1    CD1 <-> 1484 THR   (  62-)  A 1    CG2    0.43    2.77
1309 LEU   (  45-)  A 1    CD1 <-> 1326 THR   (  62-)  A 1    CG2    0.41    2.79
 124 LEU   (  45-)  A      CD1 <->  141 THR   (  62-)  A      CG2    0.41    2.79
 203 LEU   (  45-)  A      CD1 <->  220 THR   (  62-)  A      CG2    0.40    2.80
 914 LEU   (  45-)  A 1    CD1 <->  931 THR   (  62-)  A 1    CG2    0.39    2.81
 993 LEU   (  45-)  A 1    CD1 <-> 1010 THR   (  62-)  A 1    CG2    0.38    2.82
 282 LEU   (  45-)  A      CD1 <->  299 THR   (  62-)  A      CG2    0.38    2.82
 756 LEU   (  45-)  A 1    CD1 <->  773 THR   (  62-)  A 1    CG2    0.38    2.82
1072 LEU   (  45-)  A 1    CD1 <-> 1089 THR   (  62-)  A 1    CG2    0.36    2.84
  45 LEU   (  45-)  A      CD1 <->   62 THR   (  62-)  A      CG2    0.36    2.84
 440 LEU   (  45-)  A      CD1 <->  457 THR   (  62-)  A      CG2    0.35    2.85
1151 LEU   (  45-)  A 1    CD1 <-> 1168 THR   (  62-)  A 1    CG2    0.33    2.87
 361 LEU   (  45-)  A      CD1 <->  378 THR   (  62-)  A      CG2    0.33    2.87
 598 LEU   (  45-)  A      CD1 <->  615 THR   (  62-)  A      CG2    0.33    2.87
 519 LEU   (  45-)  A      CD1 <->  536 THR   (  62-)  A      CG2    0.30    2.90
 483 GLN   (   9-)  A      C   <->  485 LEU   (  11-)  A      CD2    0.30    2.90
 970 ILE   (  22-)  A 1    O   <->  987 ALA   (  39-)  A 1    N      0.28    2.42
1320 ARG   (  56-)  A 1    O   <-> 1324 GLY   (  60-)  A 1    N      0.27    2.43
 767 ARG   (  56-)  A 1    O   <->  771 GLY   (  60-)  A 1    N      0.27    2.43
 417 ILE   (  22-)  A      O   <->  434 ALA   (  39-)  A      N      0.26    2.44
1365 ILE   (  22-)  A 1    O   <-> 1382 ALA   (  39-)  A 1    N      0.26    2.44
1000 LEU   (  52-)  A 1    O   <-> 1013 PHE   (  65-)  A 1    CD2    0.26    2.54
 981 GLU   (  33-)  A 1    OE2 <->  999 TRP   (  51-)  A 1    CH2    0.26    2.54
 891 ILE   (  22-)  A 1    O   <->  908 ALA   (  39-)  A 1    N      0.26    2.44
 101 ILE   (  22-)  A      O   <->  118 ALA   (  39-)  A      N      0.26    2.44
And so on for a total of 621 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


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


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