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.

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

Chain identifier: A; Model number 2

Chain identifier: A; Model number 3

Chain identifier: A; Model number 4

Chain identifier: A; Model number 5

Chain identifier: A; Model number 6

Chain identifier: A; Model number 7

Chain identifier: A; Model number 8

Chain identifier: A; Model number 9

Chain identifier: A; Model number 10

1 MET ( 1-) A Zero 2 ASP ( 2-) A Zero 3 VAL ( 3-) A Zero 4 PHE ( 4-) A Zero 5 MET ( 5-) A Zero 6 LYS ( 6-) A Zero 7 GLY ( 7-) A Zero 8 LEU ( 8-) A Zero 9 SER ( 9-) A Zero 10 LYS ( 10-) A Zero 11 ALA ( 11-) A Zero 12 LYS ( 12-) A Zero 13 MET ( 1-) A Zero 14 ASP ( 2-) A Zero 15 VAL ( 3-) A Zero 16 PHE ( 4-) A Zero 17 MET ( 5-) A Zero 18 LYS ( 6-) A Zero 19 GLY ( 7-) A Zero 20 LEU ( 8-) A Zero 21 SER ( 9-) A Zero 22 LYS ( 10-) A Zero 23 ALA ( 11-) A Zero 24 LYS ( 12-) A Zero 25 MET ( 1-) A ZeroAnd so on for a total of 120 lines.

Model 1 : 0.213

Model 2 : 0.210

Model 3 : 0.212

Model 4 : 0.210

Model 5 : 0.213

Model 6 : 0.218

Model 7 : 0.200

Model 8 : 0.209

Model 9 : 0.211

Model 10 : 0.216

Model 1 : 0.220

Model 2 : 0.208

Model 3 : 0.215

Model 4 : 0.208

Model 5 : 0.205

Model 6 : 0.222

Model 7 : 0.202

Model 8 : 0.216

Model 9 : 0.227

Model 10 : 0.229

Model 1 : 0.220

Model 2 : 0.218

Model 3 : 0.250

Model 4 : 0.225

Model 5 : 0.228

Model 6 : 0.219

Model 7 : 0.221

Model 8 : 0.219

Model 9 : 0.210

Model 10 : 0.227

Model 1 : -7.306

Model 2 : -5.409

Model 3 : -5.379

Model 4 : -5.099

Model 5 : -6.714

Model 6 : -6.326

Model 7 : -5.370

Model 8 : -6.262

Model 9 : -5.067

Model 10 : -5.889

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.

94 LYS ( 10-) A -2.5 46 LYS ( 10-) A -2.5 27 VAL ( 3-) A -2.5 39 VAL ( 3-) A -2.5 75 VAL ( 3-) A -2.5 3 VAL ( 3-) A -2.5 51 VAL ( 3-) A -2.5 15 VAL ( 3-) A -2.4 111 VAL ( 3-) A 1 -2.4 99 VAL ( 3-) A -2.4 87 VAL ( 3-) A -2.4 91 GLY ( 7-) A -2.2 55 GLY ( 7-) A -2.2 67 GLY ( 7-) A -2.2 19 GLY ( 7-) A -2.2 103 GLY ( 7-) A -2.2 31 GLY ( 7-) A -2.2 63 VAL ( 3-) A -2.1 43 GLY ( 7-) A -2.1 115 GLY ( 7-) A 1 -2.1 79 GLY ( 7-) A -2.1 70 LYS ( 10-) A -2.1 7 GLY ( 7-) A -2.1 58 LYS ( 10-) A -2.1 106 LYS ( 10-) A -2.1 118 LYS ( 10-) A 1 -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.

3 VAL ( 3-) A Poor phi/psi 15 VAL ( 3-) A Poor phi/psi 20 LEU ( 8-) A Poor phi/psi 27 VAL ( 3-) A Poor phi/psi 39 VAL ( 3-) A Poor phi/psi 51 VAL ( 3-) A Poor phi/psi 63 VAL ( 3-) A Poor phi/psi 75 VAL ( 3-) A Poor phi/psi 87 VAL ( 3-) A Poor phi/psi 93 SER ( 9-) A Poor phi/psi 99 VAL ( 3-) A Poor phi/psi 110 ASP ( 2-) A 1 Poor phi/psi 111 VAL ( 3-) A 1 Poor phi/psi chi-1/chi-2 correlation Z-score : -6.221

chi-1/chi-2 correlation Z-score : -6.221

Model 1 : -4.415

Model 2 : -6.759

Model 3 : -6.013

Model 4 : -7.230

Model 5 : -6.049

Model 6 : -5.914

Model 7 : -7.323

Model 8 : -6.607

Model 9 : -5.735

Model 10 : -6.169

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 VAL ( 3-) A 0 4 PHE ( 4-) A 0 5 MET ( 5-) A 0 6 LYS ( 6-) A 0 8 LEU ( 8-) A 0 9 SER ( 9-) A 0 10 LYS ( 10-) A 0 11 ALA ( 11-) A 0 12 LYS ( 12-) A 0 13 MET ( 1-) A 0 14 ASP ( 2-) A 0 15 VAL ( 3-) A 0 17 MET ( 5-) A 0 18 LYS ( 6-) A 0 20 LEU ( 8-) A 0 21 SER ( 9-) A 0 22 LYS ( 10-) A 0 23 ALA ( 11-) A 0 24 LYS ( 12-) A 0 25 MET ( 1-) A 0 26 ASP ( 2-) A 0 27 VAL ( 3-) A 0 28 PHE ( 4-) A 0 29 MET ( 5-) A 0 30 LYS ( 6-) A 0And so on for a total of 106 lines.

Backbone conformation Z-score : -3.178

Standard deviation of omega values : 0.257

Model 1 : 0.339

Model 2 : 0.181

Model 3 : 0.296

Model 4 : 0.225

Model 5 : 0.256

Model 6 : 0.222

Model 7 : 0.202

Model 8 : 0.222

Model 9 : 0.413

Model 10 : 0.248

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.

2 ASP ( 2-) A N <-> 12 LYS ( 12-) A NZ 0.07 2.78 6 LYS ( 6-) A C <-> 10 LYS ( 10-) A NZ 0.06 3.04 109 MET ( 1-) A 1 O <-> 120 LYS ( 12-) A 1 NZ 0.05 2.65 104 LEU ( 8-) A CG <-> 105 SER ( 9-) A N 0.04 2.96 68 LEU ( 8-) A CG <-> 69 SER ( 9-) A N 0.04 2.96 56 LEU ( 8-) A CG <-> 57 SER ( 9-) A N 0.03 2.97 80 LEU ( 8-) A CG <-> 81 SER ( 9-) A N 0.03 2.97 61 MET ( 1-) A C <-> 62 ASP ( 2-) A CG 0.02 3.08 26 ASP ( 2-) A CG <-> 36 LYS ( 12-) A NZ 0.01 3.09 62 ASP ( 2-) A N <-> 72 LYS ( 12-) A NZ 0.01 2.84

inside/outside RMS Z-score : 1.476