WHAT IF Check report

This file was created 2012-01-25 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 pdb2kfv.ent

Administrative problems that can generate validation failures

Error: Overlapping residues removed

The pairs of residues listed in the table overlapped too much.

The left-hand residue has been removed, and the right hand residue has been kept for validation. Be aware that WHAT IF calls everything a residue. Two residues are defined as overlapping if the two smallest ellipsoids encompassing the two residues interpenetrate by 33% of the longest axis. Many artefacts can actually cause this problem. The most often observed reason is alternative residue conformations expressed by two residues that accidentally both got 1.0 occupancy for all atoms.

1024 ALA   (  22-)  A 15             1022 LYS   (  92-)  A 14           2.0

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   (  20-)  A    Zero
   2 ALA   (  21-)  A    Zero
   3 ALA   (  22-)  A    Zero
   4 ALA   (  23-)  A    Zero
   5 VAL   (  24-)  A    Zero
   6 PRO   (  25-)  A    Zero
   7 GLN   (  26-)  A    Zero
   8 ARG   (  27-)  A    Zero
   9 ALA   (  28-)  A    Zero
  10 TRP   (  29-)  A    Zero
  11 THR   (  30-)  A    Zero
  12 VAL   (  31-)  A    Zero
  13 GLU   (  32-)  A    Zero
  14 GLN   (  33-)  A    Zero
  15 LEU   (  34-)  A    Zero
  16 ARG   (  35-)  A    Zero
  17 SER   (  36-)  A    Zero
  18 GLU   (  37-)  A    Zero
  19 GLN   (  38-)  A    Zero
  20 LEU   (  39-)  A    Zero
  21 PRO   (  40-)  A    Zero
  22 LYS   (  41-)  A    Zero
  23 LYS   (  42-)  A    Zero
  24 ASP   (  43-)  A    Zero
  25 ILE   (  44-)  A    Zero
And so on for a total of 1459 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 : 0.871
Model 2 : 0.877
Model 3 : 0.850
Model 4 : 0.869
Model 5 : 0.891
Model 6 : 0.880
Model 7 : 0.867
Model 8 : 0.864
Model 9 : 0.884
Model 10 : 0.863
Model 11 : 0.864
Model 12 : 0.880
Model 13 : 0.859
Model 14 : 0.840
Model 15 : 0.872
Model 16 : 0.857
Model 17 : 0.871
Model 18 : 0.881
Model 19 : 0.875
Model 20 : 0.885

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.

  32 HIS   (  51-)  A      CG   ND1  CE1 109.99    4.4
  65 HIS   (  84-)  A      CG   ND1  CE1 109.82    4.2
 251 HIS   (  51-)  A      CG   ND1  CE1 109.66    4.1
 357 HIS   (  84-)  A      CG   ND1  CE1 109.82    4.2
 423 HIS   (  77-)  A      CG   ND1  CE1 109.62    4.0
 430 HIS   (  84-)  A      CG   ND1  CE1 109.65    4.0
 470 HIS   (  51-)  A      CA   CB   CG  117.90    4.1
 470 HIS   (  51-)  A      CG   ND1  CE1 109.72    4.1
 552 HIS   (  60-)  A      CG   ND1  CE1 109.64    4.0
 625 HIS   (  60-)  A      CG   ND1  CE1 109.69    4.1
 649 HIS   (  84-)  A      CG   ND1  CE1 109.75    4.1
 722 HIS   (  84-)  A 1    CG   ND1  CE1 109.63    4.0
 835 HIS   (  51-)  A 1    CG   ND1  CE1 109.85    4.3
 844 HIS   (  60-)  A 1    CG   ND1  CE1 109.64    4.0
 861 HIS   (  77-)  A 1    CG   ND1  CE1 109.66    4.1
 868 HIS   (  84-)  A 1    CG   ND1  CE1 109.65    4.1
 917 HIS   (  60-)  A 1    CG   ND1  CE1 109.66    4.1
 941 HIS   (  84-)  A 1    CG   ND1  CE1 109.73    4.1
 990 HIS   (  60-)  A 1    CG   ND1  CE1 109.73    4.1
1014 HIS   (  84-)  A 1    CG   ND1  CE1 109.70    4.1
1053 HIS   (  51-)  A 1    CG   ND1  CE1 109.69    4.1
1086 HIS   (  84-)  A 1    CG   ND1  CE1 109.66    4.1
1159 HIS   (  84-)  A 1    CG   ND1  CE1 109.60    4.0
1166 PHE   (  91-)  A 1    CA   CB   CG  118.11    4.3
1199 HIS   (  51-)  A 1    CG   ND1  CE1 109.60    4.0
1232 HIS   (  84-)  A 1    CG   ND1  CE1 109.63    4.0
1341 PHE   (  47-)  A 1    CA   CB   CG  118.04    4.2
1371 HIS   (  77-)  A 1    CG   ND1  CE1 109.62    4.0
1427 HIS   (  60-)  A 2    CG   ND1  CE1 109.63    4.0

Note: Per-model averages for bond-angle check

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

Model 1 : 0.739
Model 2 : 0.715
Model 3 : 0.733
Model 4 : 0.726
Model 5 : 0.745
Model 6 : 0.725
Model 7 : 0.740
Model 8 : 0.737
Model 9 : 0.718
Model 10 : 0.744
Model 11 : 0.712
Model 12 : 0.752
Model 13 : 0.720
Model 14 : 0.719
Model 15 : 0.733
Model 16 : 0.723
Model 17 : 0.702
Model 18 : 0.713
Model 19 : 0.753
Model 20 : 0.736

Note: Per-model averages for chirality check

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

Model 1 : 0.566
Model 2 : 0.637
Model 3 : 0.585
Model 4 : 0.647
Model 5 : 0.613
Model 6 : 0.650
Model 7 : 0.598
Model 8 : 0.646
Model 9 : 0.569
Model 10 : 0.640
Model 11 : 0.552
Model 12 : 0.638
Model 13 : 0.580
Model 14 : 0.582
Model 15 : 0.636
Model 16 : 0.591
Model 17 : 0.599
Model 18 : 0.618
Model 19 : 0.651
Model 20 : 0.642

Torsion-related checks

Note: Per-model averages for Ramachandran check

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

Model 1 : -1.495
Model 2 : -1.674
Model 3 : -1.645
Model 4 : -1.670
Model 5 : -1.528
Model 6 : -1.412
Model 7 : -0.839
Model 8 : -1.406
Model 9 : -0.735
Model 10 : -1.860
Model 11 : -1.966
Model 12 : -1.003
Model 13 : -1.622
Model 14 : -0.472
Model 15 : -1.522
Model 16 : -1.563
Model 17 : -1.538
Model 18 : -1.988
Model 19 : -0.768
Model 20 : -1.845

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.

 470 HIS   (  51-)  A    -2.2
 510 PHE   (  91-)  A    -2.1
1126 HIS   (  51-)  A 1   -2.1
 143 LYS   (  89-)  A    -2.0

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 ALA   (  22-)  A  Poor phi/psi
  32 HIS   (  51-)  A  Poor phi/psi
  42 LYS   (  61-)  A  Poor phi/psi
  70 LYS   (  89-)  A  Poor phi/psi
 143 LYS   (  89-)  A  Poor phi/psi
 149 ALA   (  22-)  A  Poor phi/psi
 188 LYS   (  61-)  A  Poor phi/psi
 251 HIS   (  51-)  A  Poor phi/psi
 261 LYS   (  61-)  A  Poor phi/psi
 289 LYS   (  89-)  A  Poor phi/psi
 295 ALA   (  22-)  A  Poor phi/psi
 334 LYS   (  61-)  A  Poor phi/psi
 369 ALA   (  23-)  A  Poor phi/psi
 397 HIS   (  51-)  A  Poor phi/psi
 407 LYS   (  61-)  A  Poor phi/psi
 435 LYS   (  89-)  A  Poor phi/psi
 470 HIS   (  51-)  A  omega poor
 480 LYS   (  61-)  A  Poor phi/psi
 543 HIS   (  51-)  A  Poor phi/psi
 553 LYS   (  61-)  A  Poor phi/psi
 581 LYS   (  89-)  A  Poor phi/psi
 626 LYS   (  61-)  A  Poor phi/psi
 654 LYS   (  89-)  A  Poor phi/psi
 664 GLN   (  26-)  A 1 omega poor
 727 LYS   (  89-)  A 1 Poor phi/psi
And so on for a total of 53 lines.

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 : -1.580
Model 2 : -2.074
Model 3 : -2.070
Model 4 : -1.703
Model 5 : -3.434
Model 6 : -2.373
Model 7 : -1.886
Model 8 : -2.417
Model 9 : -2.677
Model 10 : -2.691
Model 11 : -1.936
Model 12 : -3.184
Model 13 : -3.609
Model 14 : -2.733
Model 15 : -1.830
Model 16 : -2.739
Model 17 : -2.734
Model 18 : -2.594
Model 19 : -1.635
Model 20 : -2.811

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 ALA   (  22-)  A      0
   7 GLN   (  26-)  A      0
   8 ARG   (  27-)  A      0
  10 TRP   (  29-)  A      0
  20 LEU   (  39-)  A      0
  32 HIS   (  51-)  A      0
  43 LEU   (  62-)  A      0
  44 LEU   (  63-)  A      0
  46 ASN   (  65-)  A      0
  53 THR   (  72-)  A      0
  54 ALA   (  73-)  A      0
  71 ARG   (  90-)  A      0
  72 PHE   (  91-)  A      0
  73 LYS   (  92-)  A      0
  74 MET   (  20-)  A      0
  75 ALA   (  21-)  A      0
  81 ARG   (  27-)  A      0
  82 ALA   (  28-)  A      0
  83 TRP   (  29-)  A      0
  93 LEU   (  39-)  A      0
 105 HIS   (  51-)  A      0
 116 LEU   (  62-)  A      0
 117 LEU   (  63-)  A      0
 119 ASN   (  65-)  A      0
 126 THR   (  72-)  A      0
And so on for a total of 510 lines.

Note: Per-model averages for omega angle check

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

Model 1 : 4.990
Model 2 : 4.409
Model 3 : 4.847
Model 4 : 4.766
Model 5 : 5.031
Model 6 : 4.239
Model 7 : 5.304
Model 8 : 4.247
Model 9 : 4.390
Model 10 : 5.258
Model 11 : 4.750
Model 12 : 5.525
Model 13 : 4.781
Model 14 : 4.812
Model 15 : 5.399
Model 16 : 5.512
Model 17 : 5.436
Model 18 : 5.198
Model 19 : 5.454
Model 20 : 4.596

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!

 471 GLY   (  52-)  A   1.70   10

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].

   6 PRO   (  25-)  A    42.6 envelop C-delta (36 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.

 768 LEU   (  57-)  A 1    O   <->  772 LYS   (  61-)  A 1    N      0.08    2.62
 672 LEU   (  34-)  A 1    O   <->  713 LYS   (  75-)  A 1    NZ     0.08    2.62
1351 LEU   (  57-)  A 1    O   <-> 1355 LYS   (  61-)  A 1    N      0.06    2.64
 239 LEU   (  39-)  A      O   <->  275 LYS   (  75-)  A      NZ     0.06    2.64
 750 LEU   (  39-)  A 1    O   <->  786 LYS   (  75-)  A 1    NZ     0.06    2.64
1424 LEU   (  57-)  A 2    O   <-> 1428 LYS   (  61-)  A 2    N      0.06    2.64
1189 LYS   (  41-)  A 1    NZ  <-> 1218 ALA   (  70-)  A 1    O      0.05    2.65
1205 LEU   (  57-)  A 1    O   <-> 1209 LYS   (  61-)  A 1    N      0.05    2.65
 674 SER   (  36-)  A 1    O   <->  713 LYS   (  75-)  A 1    NZ     0.05    2.65
 893 SER   (  36-)  A 1    O   <->  932 LYS   (  75-)  A 1    NZ     0.05    2.65
1330 SER   (  36-)  A 1    O   <-> 1369 LYS   (  75-)  A 1    NZ     0.03    2.67
1184 SER   (  36-)  A 1    O   <-> 1223 LYS   (  75-)  A 1    NZ     0.03    2.67
1041 LEU   (  39-)  A 1    O   <-> 1077 LYS   (  75-)  A 1    NZ     0.02    2.68
1333 LEU   (  39-)  A 1    O   <-> 1369 LYS   (  75-)  A 1    NZ     0.02    2.68
 908 HIS   (  51-)  A 1    NE2 <->  948 PHE   (  91-)  A 1    CD2    0.02    3.08
 695 LEU   (  57-)  A 1    O   <->  699 LYS   (  61-)  A 1    N      0.02    2.68
 431 LEU   (  85-)  A      O   <->  435 LYS   (  89-)  A      N      0.01    2.69

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


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

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