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.
261 SMS ( 301-) A -
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
Coordinate problems, unexpected atoms, B-factor and occupancy checks
Warning: Missing atoms
The atoms listed in the table below are missing from the entry. If many atoms
are missing, the other checks can become less sensitive. Be aware that it
often happens that groups at the termini of DNA or RNA are really missing,
so that the absence of these atoms normally is neither an error nor the
result of poor electron density. Some of the atoms listed here might also be
listed by other checks, most noticeably by the options in the previous
section that list missing atoms in several categories. The plausible atoms
with zero occupancy are not listed here, as they already got assigned a
non-zero occupancy, and thus are no longer 'missing'.
1 HIS ( 3-) A CG 1 HIS ( 3-) A ND1 1 HIS ( 3-) A CD2 1 HIS ( 3-) A CE1 1 HIS ( 3-) A NE2
Atoms want to move. That is the direct result of the second law of thermodynamics, in a somewhat weird way of thinking. Any way, many atoms seem to have more than one position where they like to sit, and they jump between them. The population difference between those sites (which is related to their energy differences) is seen in the occupancy factors. As also for atoms it is 'to be or not to be', these occupancies should add up to 1.0. Obviously, it is possible that they add up to a number less than 1.0, in cases where there are yet more, but undetected' rotamers/positions in play, but also in those cases a warning is in place as the information shown in the PDB file is less certain than it could have been. The residues listed below contain atoms that have an occupancy greater than zero, but all their alternates do not add up to one.
WARNING. Presently WHAT CHECK only deals with a maximum of two alternate positions. A small number of atoms in the PDB has three alternates. In those cases the warning given here should obviously be neglected! In a next release we will try to fix this.
7 LYS ( 9-) A 0.50
Obviously, the temperature at which the X-ray data was collected has some importance too:
Crystal temperature (K) :103.000
Warning: More than 5 percent of buried atoms has low B-factor
For normal protein structures, no more than about 1 percent of the B factors
of buried atoms is below 5.0. The fact that this value is much higher in the
current structure could be a signal that the B-factors were restraints or
constraints to too-low values, misuse of B-factor field in the PDB file, or
a TLS/scaling problem. If the average B factor is low too, it is probably a
low temperature structure determination.
Percentage of buried atoms with B less than 5 : 5.15
Note: B-factor plot
The average atomic B-factor per residue is plotted as function of the residue
Chain identifier: A
Nomenclature related problems
Warning: Tyrosine convention problem
The tyrosine residues listed in the table below have their chi-2 not between
-90.0 and 90.0
112 TYR ( 114-) A
83 ASP ( 85-) A
12 GLU ( 14-) A 184 GLU ( 186-) A
12 GLU ( 14-) A 83 ASP ( 85-) A 184 GLU ( 186-) A
204 VAL ( 206-) A 5.48
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.
173 PHE ( 175-) A -2.8 81 PRO ( 83-) A -2.5 58 LEU ( 60-) A -2.2 90 GLN ( 92-) A -2.1 20 ILE ( 22-) A -2.1 160 VAL ( 162-) A -2.1 164 ILE ( 166-) A -2.1 53 THR ( 55-) A -2.1 200 LEU ( 202-) A -2.1 56 ARG ( 58-) A -2.1 28 PRO ( 30-) A -2.1 148 GLY ( 150-) A -2.0
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.
2 HIS ( 4-) A Poor phi/psi 27 SER ( 29-) A PRO omega poor 73 ASP ( 75-) A Poor phi/psi 108 ASP ( 110-) A Poor phi/psi 109 LYS ( 111-) A Poor phi/psi 175 ASN ( 177-) A Poor phi/psi 198 PRO ( 200-) A PRO omega poor 249 LYS ( 251-) A Poor phi/psi 250 ASN ( 252-) A Poor phi/psi chi-1/chi-2 correlation Z-score : -2.802
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 TRP ( 5-) A 0 5 TYR ( 7-) A 0 8 HIS ( 10-) A 0 17 ASP ( 19-) A 0 18 PHE ( 20-) A 0 22 LYS ( 24-) A 0 25 ARG ( 27-) A 0 26 GLN ( 28-) A 0 27 SER ( 29-) A 0 36 ALA ( 38-) A 0 48 SER ( 50-) A 0 56 ARG ( 58-) A 0 60 ASN ( 62-) A 0 62 HIS ( 64-) A 0 70 ASP ( 72-) A 0 71 SER ( 73-) A 0 73 ASP ( 75-) A 0 74 LYS ( 76-) A 0 78 LYS ( 80-) A 0 81 PRO ( 83-) A 0 83 ASP ( 85-) A 0 90 GLN ( 92-) A 0 94 HIS ( 96-) A 0 97 SER ( 99-) A 0 101 GLN ( 103-) A 0And so on for a total of 113 lines.
Standard deviation of omega values : 1.723
Warning: Backbone oxygen evaluation
The residues listed in the table below have an unusual backbone oxygen
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!
4 GLY ( 6-) A 1.55 20
19 PRO ( 21-) A 0.19 LOW 40 PRO ( 42-) A 0.17 LOW
81 PRO ( 83-) A -54.6 half-chair C-beta/C-alpha (-54 degrees) 135 PRO ( 137-) A -113.0 envelop C-gamma (-108 degrees) 192 PRO ( 194-) A -53.1 half-chair C-beta/C-alpha (-54 degrees)
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). BL indicates that the B-factors of the clashing atoms have a low B-factor thereby making this clash even more worrisome. INTRA and INTER indicate whether the clashes are between atoms in the same asymmetric unit, or atoms in symmetry related asymmetric units, respectively.
222 LYS ( 224-) A NZ <-> 262 HOH ( 547 ) A O 0.26 2.44 INTRA 153 GLY ( 155-) A N <-> 262 HOH ( 430 ) A O 0.25 2.45 INTRA BL 13 HIS ( 15-) A ND1 <-> 16 LYS ( 18-) A NZ 0.24 2.76 INTRA BL 110 LYS ( 112-) A NZ <-> 262 HOH ( 518 ) A O 0.22 2.48 INTRA BL 73 ASP ( 75-) A OD1 <-> 87 ARG ( 89-) A NE 0.22 2.48 INTRA BL 105 HIS ( 107-) A NE2 <-> 191 TYR ( 193-) A OH 0.22 2.48 INTRA BL 196 THR ( 198-) A OG1 <-> 261 SMS ( 301-) A N1 0.19 2.51 INTRA 177 ASP ( 179-) A OD2 <-> 179 ARG ( 181-) A NH2 0.16 2.54 INTRA BL 15 HIS ( 17-) A ND1 <-> 262 HOH ( 436 ) A O 0.16 2.54 INTRA BL 43 LYS ( 45-) A NZ <-> 82 LEU ( 84-) A O 0.15 2.55 INTRA 115 GLU ( 117-) A OE2 <-> 117 HIS ( 119-) A NE2 0.11 2.59 INTRA BL 101 GLN ( 103-) A NE2 <-> 240 ASP ( 242-) A OD1 0.09 2.61 INTRA BL 167 LYS ( 169-) A NZ <-> 230 GLY ( 232-) A N 0.09 2.76 INTRA BL 49 TYR ( 51-) A OH <-> 120 HIS ( 122-) A NE2 0.07 2.63 INTRA BL 2 HIS ( 4-) A CB <-> 3 TRP ( 5-) A N 0.06 2.64 INTRA B3 70 ASP ( 72-) A OD2 <-> 121 TRP ( 123-) A NE1 0.06 2.64 INTRA BL 165 LYS ( 167-) A O <-> 227 ASN ( 229-) A N 0.05 2.65 INTRA BL 97 SER ( 99-) A N <-> 98 LEU ( 100-) A N 0.05 2.55 INTRA BL 204 VAL ( 206-) A CG1 <-> 205 THR ( 207-) A N 0.05 2.95 INTRA BL 58 LEU ( 60-) A O <-> 65 ASN ( 67-) A N 0.04 2.66 INTRA BL 226 LEU ( 228-) A O <-> 238 MET ( 240-) A N 0.04 2.66 INTRA BL 62 HIS ( 64-) A NE2 <-> 262 HOH ( 570 ) A O 0.04 2.66 INTRA 229 ASN ( 231-) A OD1 <-> 236 GLU ( 238-) A N 0.03 2.67 INTRA BL 30 ASP ( 32-) A N <-> 262 HOH ( 576 ) A O 0.03 2.67 INTRA BL 197 THR ( 199-) A C <-> 198 PRO ( 200-) A C 0.03 2.77 INTRA BL 148 GLY ( 150-) A N <-> 215 VAL ( 217-) A O 0.03 2.67 INTRA BL 20 ILE ( 22-) A O <-> 23 GLY ( 25-) A N 0.02 2.68 INTRA BL 59 ASN ( 61-) A ND2 <-> 166 THR ( 168-) A C 0.02 3.08 INTRA BL 30 ASP ( 32-) A OD1 <-> 109 LYS ( 111-) A N 0.02 2.68 INTRA BL 83 ASP ( 85-) A OD1 <-> 262 HOH ( 498 ) A O 0.02 2.38 INTRA 94 HIS ( 96-) A ND1 <-> 262 HOH ( 479 ) A O 0.01 2.69 INTRA 116 LEU ( 118-) A N <-> 143 ILE ( 145-) A O 0.01 2.69 INTRA BL 50 ASP ( 52-) A OD1 <-> 262 HOH ( 502 ) A O 0.01 2.39 INTRA 17 ASP ( 19-) A OD1 <-> 262 HOH ( 575 ) A O 0.01 2.39 INTRA 70 ASP ( 72-) A C <-> 72 GLN ( 74-) A N 0.01 2.89 INTRA BL
Chain identifier: A
Warning: Abnormal packing environment for some residues
The residues listed in the table below have an unusual packing environment.
The packing environment of the residues is compared with the average packing environment for all residues of the same type in good PDB files. A low packing score can indicate one of several things: Poor packing, misthreading of the sequence through the density, crystal contacts, contacts with a co-factor, or the residue is part of the active site. It is not uncommon to see a few of these, but in any case this requires further inspection of the residue.
2 HIS ( 4-) A -6.74 8 HIS ( 10-) A -6.03 98 LEU ( 100-) A -5.25
Chain identifier: A
Note: Second generation quality Z-score plot
The second generation quality Z-score smoothed over a 10 residue window
is plotted as function of the residue number. Low areas in the plot (below
-1.3) indicate unusual packing.
Chain identifier: A
Water, ion, and hydrogenbond related checks
Error: Water molecules without hydrogen bonds
The water molecules listed in the table below do not form any hydrogen bonds,
neither with the protein or DNA/RNA, nor with other water molecules. This is
a strong indication of a refinement problem. The last number on each line is
the identifier of the water molecule in the input file.
262 HOH ( 510 ) A O Metal-coordinating Histidine residue 92 fixed to 1 Metal-coordinating Histidine residue 94 fixed to 1 Metal-coordinating Histidine residue 117 fixed to 1
51 GLN ( 53-) A
Hydrogen bond donors that are buried inside the protein normally use all of their hydrogens to form hydrogen bonds within the protein. If there are any non hydrogen bonded buried hydrogen bond donors in the structure they will be listed here. In very good structures the number of listed atoms will tend to zero.
Waters are not listed by this option.
29 VAL ( 31-) A N 51 GLN ( 53-) A N 65 ASN ( 67-) A ND2 72 GLN ( 74-) A N 98 LEU ( 100-) A N 197 THR ( 199-) A N 201 LEU ( 203-) A N 227 ASN ( 229-) A ND2 241 ASN ( 243-) A ND2 242 TRP ( 244-) A N 257 PHE ( 259-) A N Only metal coordination for 92 HIS ( 94-) A NE2 Only metal coordination for 94 HIS ( 96-) A NE2 Only metal coordination for 117 HIS ( 119-) A ND1
30 ASP ( 32-) A H-bonding suggests Asn
The second part of the table mostly gives an impression of how well the model conforms to common refinement restraint values. The first part of the table shows a number of global quality indicators.
Structure Z-scores, positive is better than average:
1st generation packing quality : -0.262 2nd generation packing quality : 0.630 Ramachandran plot appearance : -2.026 chi-1/chi-2 rotamer normality : -2.802 Backbone conformation : -0.537
Bond lengths : 0.368 (tight) Bond angles : 0.699 Omega angle restraints : 0.313 (tight) Side chain planarity : 0.222 (tight) Improper dihedral distribution : 0.654 Inside/Outside distribution : 0.963
The second part of the table mostly gives an impression of how well the model conforms to common refinement restraint values. The first part of the table shows a number of global quality indicators, which have been calibrated against structures of similar resolution.
Resolution found in PDB file : 2.10
Structure Z-scores, positive is better than average:
1st generation packing quality : 0.2 2nd generation packing quality : 0.6 Ramachandran plot appearance : -1.0 chi-1/chi-2 rotamer normality : -1.5 Backbone conformation : -0.5
Bond lengths : 0.368 (tight) Bond angles : 0.699 Omega angle restraints : 0.313 (tight) Side chain planarity : 0.222 (tight) Improper dihedral distribution : 0.654 Inside/Outside distribution : 0.963 ==============
WHAT IF G.Vriend, WHAT IF: a molecular modelling and drug design program, J. Mol. Graph. 8, 52--56 (1990). WHAT_CHECK (verification routines from WHAT IF) R.W.W.Hooft, G.Vriend, C.Sander and E.E.Abola, Errors in protein structures Nature 381, 272 (1996). (see also http://swift.cmbi.ru.nl/gv/whatcheck for a course and extra inform Bond lengths and angles, protein residues R.Engh and R.Huber, Accurate bond and angle parameters for X-ray protein structure refinement, Acta Crystallogr. A47, 392--400 (1991). Bond lengths and angles, DNA/RNA G.Parkinson, J.Voitechovsky, L.Clowney, A.T.Bruenger and H.Berman, New parameters for the refinement of nucleic acid-containing structures Acta Crystallogr. D52, 57--64 (1996). DSSP W.Kabsch and C.Sander, Dictionary of protein secondary structure: pattern recognition of hydrogen bond and geometrical features Biopolymers 22, 2577--2637 (1983). Hydrogen bond networks R.W.W.Hooft, C.Sander and G.Vriend, Positioning hydrogen atoms by optimizing hydrogen bond networks in protein structures PROTEINS, 26, 363--376 (1996). Matthews' Coefficient B.W.Matthews Solvent content of Protein Crystals J. Mol. Biol. 33, 491--497 (1968). Protein side chain planarity R.W.W. Hooft, C. Sander and G. Vriend, Verification of protein structures: side-chain planarity J. Appl. Cryst. 29, 714--716 (1996). Puckering parameters D.Cremer and J.A.Pople, A general definition of ring puckering coordinates J. Am. Chem. Soc. 97, 1354--1358 (1975). Quality Control G.Vriend and C.Sander, Quality control of protein models: directional atomic contact analysis, J. Appl. Cryst. 26, 47--60 (1993). Ramachandran plot G.N.Ramachandran, C.Ramakrishnan and V.Sasisekharan, Stereochemistry of Polypeptide Chain Conformations J. Mol. Biol. 7, 95--99 (1963). Symmetry Checks R.W.W.Hooft, C.Sander and G.Vriend, Reconstruction of symmetry related molecules from protein data bank (PDB) files J. Appl. Cryst. 27, 1006--1009 (1994). Ion Checks I.D.Brown and K.K.Wu, Empirical Parameters for Calculating Cation-Oxygen Bond Valences Acta Cryst. B32, 1957--1959 (1975). M.Nayal and E.Di Cera, Valence Screening of Water in Protein Crystals Reveals Potential Na+ Binding Sites J.Mol.Biol. 256 228--234 (1996). P.Mueller, S.Koepke and G.M.Sheldrick, Is the bond-valence method able to identify metal atoms in protein structures? Acta Cryst. D 59 32--37 (2003). Checking checks K.Wilson, C.Sander, R.W.W.Hooft, G.Vriend, et al. Who checks the checkers J.Mol.Biol. (1998) 276,417-436.