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seq.B99990001.pdb
--
The packing quality control per amino acid:
Average for range 1 - 182 : -2.231
If a residue has a score of -5.0 or lower, something is really going on:
the residue makes symmetry contacts, is contacting a ligand or an ion, or something is wrong.

Bond lengths that deviate more than 4 sigma:
The bond lengths listed in the table below were found to deviate more than 4
sigma from standard bond lengths (both standard values and sigmas for amino
acid residues have been taken from Engh and Huber [REF], for DNA they were
taken from Parkinson et al [REF]). In the table below for each unusual bond
the bond length and the number of standard deviations it differs from the
normal value is given.
Atom names starting with "-" belong to the previous residue in the chain. If
the second atom name is "-SG*", the disulphide bridge has a deviating length.
157 GLN ( 157 ) A N CA 1.55 4.7
157 GLN ( 157 ) A CA C 1.81 13.8
157 GLN ( 157 ) A N -C 1.44 5.6
158 LEU ( 158 ) A N CA 1.64 9.8
158 LEU ( 158 ) A N -C 1.55 10.9
Bond lengths were found to deviate normally from the standard bond lengths
(values for Protein residues were taken from Engh and Huber [REF], for
DNA/RNA from Parkinson et al [REF]).
RMS Z-score for bond lengths: 1.023
RMS-deviation in bond distances: 0.021
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.
You have most probably seen symmetry problems earlier. Please correct these
and rerun this check to see the possible implications on the X-ray cell axes.

Planarity validation results:
The side chains of the residues listed in the table below contain a planar
group that was found to deviate from planarity by more than 4.0 times the
expected value. For an amino acid residue that has a side chain with a
planar group, the RMS deviation of the atoms to a least squares plane was
determined. The number in the table is the number of standard deviations
this RMS value deviates from the expected value. Not knowing better yet, we
assume that planarity of the groups analyzed should be perfect.
98 TRP ( 98 ) A 4.86
All of the atoms that are connected to planar aromatic rings in side chains
of amino-acid residues are in the plane within expected RMS deviations.
Since there is no DNA and no protein with hydrogens, no uncalibrated
planarity check was performed.

The packing quality control per amino acid:
----Residue------- State AllAll BB-BB BB-SC SC-BB SC-SC
---------------------------------------------------------------------------
1 MET ( 1 ) A 3 -0.791 -0.688 -0.478 -0.944 -0.642
2 ARG ( 2 ) A 3 -1.516 -0.994 -0.816 -0.952 -1.203
3 ILE ( 3 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
4 ALA ( 4 ) A 3 -0.971 -1.078 -0.794 0.000 0.000
5 PHE ( 5 ) A 3 -1.356 -0.801 -0.898 -1.026 -0.958
6 PHE ( 6 ) A 3 -1.353 -0.801 -0.898 -1.017 -0.958
7 LEU ( 7 ) A 3 -1.547 -1.068 -1.105 -1.015 -1.030
8 LEU ( 8 ) A 3 -2.110 -1.233 -1.533 -1.174 -1.419
9 ILE ( 9 ) A 3 -1.049 -0.719 -1.143 -1.207 -1.585
10 LEU ( 10 ) A 3 -0.826 -0.754 -0.770 -0.470 -1.030
11 SER ( 11 ) A 3 -0.753 -0.534 -0.763 -0.826 -0.580
12 ILE ( 12 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
13 ILE ( 13 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
14 VAL ( 14 ) A 3 -1.352 -0.821 -0.810 -0.825 -1.086
15 GLY ( 15 ) A 3 -1.413 -1.020 -0.877 0.000 0.000
16 LEU ( 16 ) A 3 -0.826 -0.754 -0.770 -0.470 -1.030
17 ALA ( 17 ) A 3 -0.971 -1.078 -0.794 0.000 0.000
18 TYR ( 18 ) A 3 -1.539 -0.859 -1.134 -1.153 -1.399
19 GLY ( 19 ) A 3 -1.413 -1.020 -0.877 0.000 0.000
20 TYR ( 20 ) A 3 -1.481 -0.798 -1.079 -1.153 -1.380
21 SER ( 21 ) A 3 -1.497 -0.891 -1.400 -0.581 -1.030
22 CYS ( 22 ) A 3 -1.678 -1.207 -1.754 -1.379 -2.034
23 PRO ( 23 ) A 3 -1.194 -0.710 -0.817 -0.752 -0.830
24 LYS ( 24 ) A 3 -1.581 -1.490 -1.227 -1.088 -0.210
25 PRO ( 25 ) A 3 -0.245 -0.710 0.586 -0.752 0.110
26 CYS ( 26 ) A 3 -1.601 -1.778 -0.229 -1.475 -1.646
27 TYR ( 27 ) A 3 0.111 0.813 -0.209 0.212 -1.052
28 GLY ( 28 ) A 3 -0.528 -0.177 -0.606 0.000 0.000
29 ASN ( 29 ) A 3 -0.879 -0.273 -0.306 -1.270 -0.936
30 MET ( 30 ) A 3 -0.052 1.564 -1.140 0.758 -0.798
31 CYS ( 31 ) A 3 -0.060 0.753 0.185 -0.652 -1.296
32 CYS ( 32 ) A 3 -1.193 -0.683 -1.177 -1.133 -1.920
33 SER ( 33 ) A 2 -0.859 -1.055 0.964 -1.628 -0.327
34 THR ( 34 ) A 2 -0.988 -1.073 0.223 -1.113 -1.221
35 SER ( 35 ) A 2 -0.113 0.180 -0.156 -0.915 -0.992
36 PRO ( 36 ) A 2 -0.627 0.529 -1.586 -0.213 -1.984
37 ASP ( 37 ) A 2 -0.225 0.436 -0.028 -0.531 -0.905
38 HIS ( 38 ) A 2 2.133 1.591 2.712 0.406 1.266
39 LYS ( 39 ) A 2 0.015 0.805 0.603 -0.821 -0.776
40 TYR ( 40 ) A 2 -0.259 0.326 -0.266 -0.223 -1.234
41 TYR ( 41 ) A 2 0.310 0.149 -0.216 0.499 0.911
42 LEU ( 42 ) A 2 -0.651 -0.311 -1.315 -0.352 -0.491
43 THR ( 43 ) A 3 -0.866 -0.830 -0.916 -0.788 0.063
44 ASP ( 44 ) A 3 -0.526 0.997 -1.088 -0.619 -0.866
45 PHE ( 45 ) A 2 -1.573 -1.159 -1.730 -1.157 -0.816
46 CYS ( 46 ) A 3 -1.616 -0.890 -1.777 -1.533 -1.584
47 GLY ( 47 ) A 3 -0.075 0.843 -1.555 0.000 0.000
48 SER ( 48 ) A 3 -0.869 -0.488 -1.329 -0.115 -0.169
49 THR ( 49 ) A 3 -1.075 -1.274 -0.823 -0.853 -0.299
50 SER ( 50 ) A 3 0.134 1.090 -0.757 -0.447 -0.580
51 ALA ( 51 ) A 3 -0.618 -0.253 -0.585 0.000 0.000
52 CYS ( 52 ) A 3 -0.946 -0.400 -0.850 -1.215 -1.433
53 GLY ( 53 ) A 2 -1.782 -1.797 -1.096 0.000 0.000
54 PRO ( 54 ) A 2 -1.200 -1.207 -0.557 -0.729 -0.815
55 LYS ( 55 ) A 2 -1.452 -1.276 -0.296 -1.578 -0.944
56 PRO ( 56 ) A 2 -1.347 -0.721 -1.758 -0.631 -1.415
57 SER ( 57 ) A 2 -0.291 -0.031 0.081 -1.173 -0.978
58 CYS ( 58 ) A 2 -0.089 0.254 -0.358 -0.556 0.719
59 SER ( 59 ) A 2 0.159 0.806 -1.087 -0.138 -0.523
60 GLY ( 60 ) A 2 -0.169 0.386 -1.279 0.000 0.000
61 LYS ( 61 ) A 2 -1.249 -0.701 -1.322 -0.666 -1.689
62 LEU ( 62 ) A 2 -1.286 -0.955 -1.290 -0.911 -1.304
63 TYR ( 63 ) A 2 -1.312 -0.960 -1.317 -0.137 -1.812
64 PHE ( 64 ) A 3 0.050 0.197 0.501 -0.162 -0.250
65 THR ( 65 ) A 3 -0.466 -0.194 -0.447 -0.664 -0.648
66 ALA ( 66 ) A 3 -0.895 -0.479 -0.721 0.000 0.000
67 ASP ( 67 ) A 3 0.689 1.767 -0.350 1.078 -0.792
68 SER ( 68 ) A 3 0.431 1.228 -1.094 1.872 -1.584
69 GLN ( 69 ) A 3 -0.781 -0.232 -0.764 0.009 -0.845
70 ARG ( 70 ) A 3 0.575 0.838 0.061 0.285 0.194
71 PHE ( 71 ) A 3 -0.158 0.464 -0.654 -1.206 0.321
72 GLY ( 72 ) A 1 -0.846 -0.627 -0.980 0.000 0.000
73 CYS ( 73 ) A 3 -1.028 -0.579 -0.668 -1.195 -1.773
74 GLY ( 74 ) A 3 -1.777 -0.734 -2.014 0.000 0.000
75 LYS ( 75 ) A 3 -1.227 -0.706 -0.605 -1.058 -1.346
76 HIS ( 76 ) A 3 -1.555 -1.823 -0.768 -1.533 -0.479
77 LEU ( 77 ) A 3 -0.641 -0.335 0.606 -0.453 -1.119
78 ASN ( 78 ) A 3 -1.254 -0.123 -0.913 -0.923 -1.165
79 LEU ( 79 ) A 3 0.110 0.556 0.453 -0.067 -0.512
80 CYS ( 80 ) A 1 -1.075 -0.209 -1.919 -1.085 -1.810
81 ARG ( 81 ) A 1 -1.040 -0.818 -1.077 -0.532 -0.734
82 GLY ( 82 ) A 3 0.898 1.615 -0.688 0.000 0.000
83 LYS ( 83 ) A 3 0.780 1.005 -0.113 0.830 0.170
84 LYS ( 84 ) A 3 -0.502 0.880 -0.128 -0.136 -1.517
85 CYS ( 85 ) A 3 0.482 0.426 -0.383 1.636 -0.782
86 VAL ( 86 ) A 3 -0.222 -0.433 0.268 -0.720 0.340
87 LYS ( 87 ) A 3 -0.659 -0.426 -1.136 1.172 -1.414
88 ALA ( 88 ) A 3 -0.148 0.167 -0.392 0.000 0.000
89 LYS ( 89 ) A 3 -1.141 -0.405 -0.999 0.531 -1.941
90 VAL ( 90 ) A 3 -0.604 0.650 -1.963 1.419 -2.088
91 TYR ( 91 ) A 3 -0.898 -0.838 -0.244 -0.806 -0.110
92 ASP ( 92 ) A 3 -0.756 -1.025 -0.656 -0.120 -0.167
93 ALA ( 93 ) A 1 -1.928 -1.858 -1.481 0.000 0.000
94 GLY ( 94 ) A 3 -0.107 0.464 -0.777 0.000 0.000
95 PRO ( 95 ) A 3 0.703 -0.130 0.845 1.513 -0.177
96 ALA ( 96 ) A 3 -0.482 -0.394 -0.242 0.000 0.000
97 GLU ( 97 ) A 3 -1.251 0.110 -0.660 0.268 -1.578
98 TRP ( 98 ) A 2 -2.190 -1.616 -1.700 -0.645 -2.545
99 VAL ( 99 ) A 3 0.376 0.484 1.026 -0.794 -0.030
100 GLU ( 100 ) A 3 -0.871 -0.110 0.090 -0.326 -1.070
101 LYS ( 101 ) A 3 -1.542 -1.096 -1.439 -0.825 -0.858
102 ASP ( 102 ) A 3 -1.558 -0.895 -1.268 -0.488 -1.066
103 ALA ( 103 ) A 3 -1.113 -1.403 -0.162 0.000 0.000
104 GLY ( 104 ) A 3 -1.208 -1.387 -0.101 0.000 0.000
105 LYS ( 105 ) A 3 -1.595 -1.401 -1.422 -0.857 -0.389
106 MET ( 106 ) A 3 -2.024 -0.686 -1.472 -1.119 -1.244
107 ILE ( 107 ) A 3 -1.660 -0.174 -1.691 -0.227 -1.895
108 ILE ( 108 ) A 3 -1.218 -0.278 -0.865 -0.933 -1.043
109 ASP ( 109 ) A 3 -1.471 -0.800 -1.278 -0.083 -1.369
110 ALA ( 110 ) A 3 -1.063 -0.889 -0.489 0.000 0.000
111 SER ( 111 ) A 3 -1.811 -1.452 -1.124 -1.112 -0.978
112 PRO ( 112 ) A 3 -0.272 -0.154 0.257 -0.400 -0.513
113 THR ( 113 ) A 3 -0.994 -0.533 -0.352 -1.402 -0.590
114 ILE ( 114 ) A 3 -1.301 -0.538 -0.023 -1.096 -1.247
115 CYS ( 115 ) A 3 -1.227 -1.034 -0.663 -1.031 -1.049
116 HIS ( 116 ) A 2 -1.341 -0.711 -1.011 -1.404 -1.117
117 GLU ( 117 ) A 2 -2.114 -1.971 -1.618 -1.250 -1.296
118 LEU ( 118 ) A 2 -2.372 -1.903 -2.275 -1.090 -1.774
119 THR ( 119 ) A 2 -1.839 -1.362 -2.124 -1.329 -1.894
120 GLY ( 120 ) A 3 -0.484 0.343 -1.306 0.000 0.000
121 GLY ( 121 ) A 3 0.235 -0.005 0.383 0.000 0.000
122 SER ( 122 ) A 3 -0.792 -0.969 -0.424 -1.011 0.402
123 SER ( 123 ) A 3 -0.424 -0.901 0.184 0.437 -0.182
124 CYS ( 124 ) A 3 -1.443 -1.768 0.067 -1.807 -0.364
125 GLY ( 125 ) A 3 -0.834 -1.122 0.388 0.000 0.000
126 TRP ( 126 ) A 3 -1.451 -0.620 -1.638 -1.101 -1.100
127 SER ( 127 ) A 3 -1.096 -1.060 -0.760 -1.057 -0.659
128 ASP ( 128 ) A 3 -0.790 -0.337 -0.865 -0.658 -0.325
129 LYS ( 129 ) A 3 -1.887 -0.917 -0.966 -1.180 -1.553
130 PHE ( 130 ) A 2 -1.163 -0.598 -0.627 -1.001 -1.867
131 GLU ( 131 ) A 2 -0.131 0.370 0.169 -0.399 -0.620
132 ILE ( 132 ) A 2 -0.410 -0.681 0.345 -0.764 0.442
133 THR ( 133 ) A 2 -0.582 -0.022 -0.386 -1.176 -1.541
134 ALA ( 134 ) A 2 -0.380 0.501 -1.725 0.000 0.000
135 THR ( 135 ) A 2 0.266 1.426 -0.437 -1.739 0.060
136 VAL ( 136 ) A 2 0.356 0.606 -0.166 0.152 0.401
137 THR ( 137 ) A 2 -0.252 0.334 0.046 -1.391 -1.517
138 SER ( 138 ) A 2 -0.527 -0.120 -1.042 0.114 -1.564
139 LEU ( 139 ) A 2 -1.571 -0.681 -1.582 -1.244 -1.441
140 THR ( 140 ) A 2 -1.177 -1.160 -0.673 -1.040 -0.272
141 ASP ( 141 ) A 3 -1.305 -0.797 -0.775 -0.966 -0.755
142 SER ( 142 ) A 3 -0.732 -0.528 -0.721 -0.826 -0.580
143 ARG ( 143 ) A 3 -0.701 -0.271 -0.274 -0.684 -0.488
144 PRO ( 144 ) A 3 -0.261 -0.202 0.083 0.067 -0.523
145 LEU ( 145 ) A 3 -1.110 -0.671 0.817 -1.141 -1.168
146 GLY ( 146 ) A 3 -1.764 -0.953 -1.555 0.000 0.000
147 PRO ( 147 ) A 3 -0.112 -0.216 0.275 -0.367 -0.016
148 PHE ( 148 ) A 3 -0.968 -1.116 -0.664 -0.609 -0.033
149 ASN ( 149 ) A 3 -1.092 -1.362 0.038 -1.363 0.024
150 VAL ( 150 ) A 3 -1.195 -0.821 -0.733 -0.825 -1.064
151 THR ( 151 ) A 3 -1.251 -1.078 -0.992 -1.082 -0.153
152 GLU ( 152 ) A 3 -2.160 -1.248 -1.465 -1.148 -1.240
153 GLU ( 153 ) A 3 -0.897 -0.612 -0.894 -1.148 -0.727
154 GLU ( 154 ) A 3 -2.097 -1.495 -1.080 -1.425 -1.237
155 MET ( 155 ) A 3 -1.388 -0.240 -0.874 -0.211 -1.363
156 ASP ( 156 ) A 3 -1.608 -1.046 -1.009 -1.028 -0.929
157 GLN ( 157 ) A 3 0.205 -0.288 -0.108 2.344 -1.004
158 LEU ( 158 ) A 3 -1.180 -0.242 -1.327 0.456 -1.541
159 PHE ( 159 ) A 3 -0.406 0.385 -0.802 -0.111 -0.516
160 ILE ( 160 ) A 2 -0.970 -0.350 0.239 -1.692 -0.774
161 ASP ( 161 ) A 2 -1.017 -0.469 -1.268 -0.656 -1.163
162 HIS ( 162 ) A 3 -0.623 0.471 -1.438 0.383 -1.046
163 GLU ( 163 ) A 2 -1.269 -0.346 -1.691 -0.177 -1.960
164 ILE ( 164 ) A 2 -1.217 -0.793 -1.098 -1.146 0.176
165 ALA ( 165 ) A 2 -1.190 -1.191 -0.745 0.000 0.000
166 MET ( 166 ) A 3 -1.073 -0.092 -0.751 -0.457 -1.221
167 ALA ( 167 ) A 3 -1.117 -0.673 -0.969 0.000 0.000
168 GLN ( 168 ) A 3 -0.632 -0.023 -0.734 -0.888 -1.186
169 CYS ( 169 ) A 3 -1.133 -1.099 -1.372 -1.010 0.399
170 GLU ( 170 ) A 3 -0.604 -0.057 -1.086 0.104 -0.810
171 ALA ( 171 ) A 2 -1.983 -2.095 -0.786 0.000 0.000
172 GLU ( 172 ) A 2 -1.612 -0.979 -0.964 -0.987 -0.940
173 LYS ( 173 ) A 2 -0.770 -0.625 0.072 -0.685 -0.754
174 THR ( 174 ) A 2 -1.839 -1.624 -1.493 -1.408 -1.826
175 CYS ( 175 ) A 3 -1.374 -0.943 -1.379 -1.451 -0.865
176 ASN ( 176 ) A 3 -0.564 -0.756 -0.926 0.253 0.160
177 GLY ( 177 ) A 3 -1.158 -0.985 -0.364 0.000 0.000
178 PHE ( 178 ) A 2 -2.820 -2.350 -1.813 -1.746 -2.357
179 ASP ( 179 ) A 3 -1.358 -0.853 -0.447 -0.883 -0.866
180 LEU ( 180 ) A 3 -1.598 -1.403 -0.756 -1.278 -0.436
181 GLU ( 181 ) A 3 0.411 -0.612 3.138 -1.148 -0.561
All contacts : Average = -0.907 Z-score = -5.87
BB-BB contacts : Average = -0.493 Z-score = -3.26
BB-SC contacts : Average = -0.701 Z-score = -5.37
SC-BB contacts : Average = -0.624 Z-score = -3.70
SC-SC contacts : Average = -0.912 Z-score = -5.22
If an individual residue has a quality control value of -2.5 or worse, you should take a look at it. It can mean that the residue:
is involved in symmetry contacts, or
is binding a co-factor, ligand or ion, or
is an active site residue, or
is wrong.
Average protein values ("Z-score for all contacts") can be read as follows:
-5.0 Guaranteed wrong structure. Bad structure or poor model
-3.0 Probably bad structure or unrefined model. Doubtful structure or model
-2.0 Structure OK or good model. Good structures
0.0 Good structures.
2.0 Good structures. Unusually Good structures
4.0 Probably a strange model of a perfect helix

-------------------------------------
seq.B99990002.pdb
--
The packing quality control per amino acid:
Average for range 1 - 182 : -2.249
If a residue has a score of -5.0 or lower, something is really going on:
the residue makes symmetry contacts, is contacting a ligand or an ion, or something is wrong.

Bond lengths that deviate more than 4 sigma:
The bond lengths listed in the table below were found to deviate more than 4
sigma from standard bond lengths (both standard values and sigmas for amino
acid residues have been taken from Engh and Huber [REF], for DNA they were
taken from Parkinson et al [REF]). In the table below for each unusual bond
the bond length and the number of standard deviations it differs from the
normal value is given.
Atom names starting with "-" belong to the previous residue in the chain. If
the second atom name is "-SG*", the disulphide bridge has a deviating length.
85 CYS ( 85 ) A CA C 1.42 -4.9
157 GLN ( 157 ) A CA C 1.83 14.6
157 GLN ( 157 ) A N -C 1.44 5.5
158 LEU ( 158 ) A N CA 1.64 9.7
158 LEU ( 158 ) A N -C 1.55 11.1
159 PHE ( 159 ) A N -C 1.41 4.3
Bond lengths were found to deviate normally from the standard bond lengths
(values for Protein residues were taken from Engh and Huber [REF], for
DNA/RNA from Parkinson et al [REF]).
RMS Z-score for bond lengths: 1.046
RMS-deviation in bond distances: 0.021
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.
You have most probably seen symmetry problems earlier. Please correct these
and rerun this check to see the possible implications on the X-ray cell axes.

Planarity validation results:
The side chains of the residues listed in the table below contain a planar
group that was found to deviate from planarity by more than 4.0 times the
expected value. For an amino acid residue that has a side chain with a
planar group, the RMS deviation of the atoms to a least squares plane was
determined. The number in the table is the number of standard deviations
this RMS value deviates from the expected value. Not knowing better yet, we
assume that planarity of the groups analyzed should be perfect.
157 GLN ( 157 ) A 4.90
All of the atoms that are connected to planar aromatic rings in side chains
of amino-acid residues are in the plane within expected RMS deviations.
Since there is no DNA and no protein with hydrogens, no uncalibrated
planarity check was performed.

The packing quality control per amino acid:
----Residue------- State AllAll BB-BB BB-SC SC-BB SC-SC
---------------------------------------------------------------------------
1 MET ( 1 ) A 3 -0.791 -0.688 -0.478 -0.944 -0.642
2 ARG ( 2 ) A 3 -1.516 -0.994 -0.572 -0.952 -1.203
3 ILE ( 3 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
4 ALA ( 4 ) A 3 -0.764 -1.078 -0.668 0.000 0.000
5 PHE ( 5 ) A 3 -1.356 -0.801 -0.898 -1.026 -0.958
6 PHE ( 6 ) A 3 -1.410 -0.948 -0.779 -1.083 -1.044
7 LEU ( 7 ) A 3 -2.110 -1.233 -1.533 -1.174 -1.419
8 LEU ( 8 ) A 3 -1.547 -1.068 -1.105 -1.015 -1.030
9 ILE ( 9 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
10 LEU ( 10 ) A 3 -0.826 -0.754 -0.770 -0.470 -1.030
11 SER ( 11 ) A 3 -1.635 -0.986 -1.431 -0.826 -1.098
12 ILE ( 12 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
13 ILE ( 13 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
14 VAL ( 14 ) A 3 -1.352 -0.821 -0.810 -0.825 -1.086
15 GLY ( 15 ) A 3 -1.413 -1.020 -0.590 0.000 0.000
16 LEU ( 16 ) A 3 -0.826 -0.754 -0.770 -0.470 -1.030
17 ALA ( 17 ) A 3 -0.971 -1.078 -0.794 0.000 0.000
18 TYR ( 18 ) A 3 -1.539 -0.859 -1.134 -1.153 -1.399
19 GLY ( 19 ) A 3 -1.692 -1.399 -0.891 0.000 0.000
20 TYR ( 20 ) A 3 -1.417 -0.784 -0.969 -1.153 -1.324
21 SER ( 21 ) A 3 -1.143 -0.729 -1.005 -0.826 -0.742
22 CYS ( 22 ) A 3 -1.654 -1.207 -1.754 -1.379 -1.835
23 PRO ( 23 ) A 3 -0.690 -0.102 -0.271 -0.752 -0.702
24 LYS ( 24 ) A 3 -2.526 -1.558 -1.230 -2.011 -1.358
25 PRO ( 25 ) A 3 -1.370 -1.183 -0.711 -1.416 -0.609
26 CYS ( 26 ) A 3 -1.369 -1.180 -0.606 -1.357 -1.801
27 TYR ( 27 ) A 3 -0.656 -0.174 0.161 -1.136 -0.933
28 GLY ( 28 ) A 3 -0.381 0.072 -0.762 0.000 0.000
29 ASN ( 29 ) A 3 -0.794 0.176 -0.684 -0.760 -1.204
30 MET ( 30 ) A 3 2.626 3.912 -0.412 2.876 -0.626
31 CYS ( 31 ) A 3 -0.528 -0.151 -0.676 -0.880 -0.032
32 CYS ( 32 ) A 3 -0.917 -0.446 -0.553 -1.166 -1.694
33 SER ( 33 ) A 3 0.182 -0.147 0.719 -0.553 0.715
34 THR ( 34 ) A 2 -0.559 -0.723 1.216 -1.283 -1.072
35 SER ( 35 ) A 2 -0.711 -0.685 -0.475 -0.432 -0.202
36 PRO ( 36 ) A 2 -1.462 -0.386 -1.509 -1.956 -1.314
37 ASP ( 37 ) A 2 -0.374 0.063 -0.390 -0.360 -0.663
38 HIS ( 38 ) A 2 1.094 1.015 1.241 -0.271 0.623
39 LYS ( 39 ) A 2 -0.843 0.924 -1.118 -1.602 -2.258
40 TYR ( 40 ) A 2 -0.645 0.266 -1.470 -0.352 -1.303
41 TYR ( 41 ) A 2 0.171 0.334 -0.431 0.206 0.112
42 LEU ( 42 ) A 2 -0.193 0.793 -1.158 -0.797 -0.897
43 THR ( 43 ) A 2 -1.539 -1.203 -1.469 -1.471 -1.134
44 ASP ( 44 ) A 3 -0.938 0.278 -1.272 -0.508 -1.059
45 PHE ( 45 ) A 2 -1.804 -1.045 -1.871 -1.402 -1.509
46 CYS ( 46 ) A 3 -1.010 -0.427 -1.293 -1.032 -1.494
47 GLY ( 47 ) A 3 0.462 1.195 -1.312 0.000 0.000
48 SER ( 48 ) A 3 -1.040 -0.500 -1.314 -0.649 -0.646
49 THR ( 49 ) A 3 -1.075 -1.278 -0.820 -0.891 -0.256
50 SER ( 50 ) A 3 -0.234 0.545 -0.793 -0.447 -0.742
51 ALA ( 51 ) A 3 -0.568 -0.082 -0.702 0.000 0.000
52 CYS ( 52 ) A 3 -1.254 -0.682 -1.406 -1.252 -1.676
53 GLY ( 53 ) A 3 -1.811 -0.621 -2.064 0.000 0.000
54 PRO ( 54 ) A 2 -1.404 -1.261 -1.031 -0.791 -0.975
55 LYS ( 55 ) A 2 -1.678 -1.033 -0.834 -1.895 -1.364
56 PRO ( 56 ) A 2 -1.294 -0.931 -1.385 -0.541 -1.340
57 SER ( 57 ) A 2 -0.575 0.067 -1.102 -0.882 -1.497
58 CYS ( 58 ) A 2 -0.773 0.109 -0.588 -1.698 -6.552
59 SER ( 59 ) A 2 0.273 0.722 0.059 -0.984 -0.768
60 GLY ( 60 ) A 2 -0.023 0.276 -0.647 0.000 0.000
61 LYS ( 61 ) A 2 -1.066 -0.610 -0.979 -1.057 -0.689
62 LEU ( 62 ) A 2 -2.174 -1.178 -1.281 -1.396 -1.957
63 TYR ( 63 ) A 2 -1.674 -1.269 -1.413 -0.178 -2.046
64 PHE ( 64 ) A 3 -0.261 0.114 0.413 -0.540 -0.670
65 THR ( 65 ) A 3 -0.670 -0.804 -0.199 -0.972 -0.542
66 ALA ( 66 ) A 3 -0.735 -0.640 -0.324 0.000 0.000
67 ASP ( 67 ) A 3 -0.074 1.482 -0.837 -0.245 -0.965
68 SER ( 68 ) A 3 0.122 0.917 -1.264 1.520 -1.405
69 GLN ( 69 ) A 3 -0.872 -0.228 -0.673 0.306 -1.464
70 ARG ( 70 ) A 3 -0.923 0.053 -0.045 -0.183 -1.198
71 PHE ( 71 ) A 3 0.457 0.166 1.097 -0.438 0.353
72 GLY ( 72 ) A 1 -0.394 -0.322 -0.388 0.000 0.000
73 CYS ( 73 ) A 3 -1.060 -0.391 -1.234 -1.107 -1.983
74 GLY ( 74 ) A 3 -1.325 -0.781 -1.187 0.000 0.000
75 LYS ( 75 ) A 3 -0.898 -0.677 0.475 -1.045 -1.282
76 HIS ( 76 ) A 3 -1.643 -1.823 -1.077 -1.411 -0.523
77 LEU ( 77 ) A 3 -0.562 0.185 -0.074 -0.280 -1.222
78 ASN ( 78 ) A 3 -1.837 -0.150 -1.079 -1.126 -2.300
79 LEU ( 79 ) A 3 -1.307 0.342 -0.334 -1.220 -1.747
80 CYS ( 80 ) A 1 -1.221 -0.431 -2.094 -1.102 -1.844
81 ARG ( 81 ) A 1 -1.409 -1.139 -1.172 -0.704 -1.063
82 GLY ( 82 ) A 3 1.543 1.784 0.116 0.000 0.000
83 LYS ( 83 ) A 3 0.283 0.623 -0.467 1.430 -0.869
84 LYS ( 84 ) A 3 -0.437 0.616 -1.133 0.525 -1.224
85 CYS ( 85 ) A 3 -0.150 0.684 -0.837 -0.118 -1.039
86 VAL ( 86 ) A 3 -0.843 -0.200 -0.628 -0.334 -1.354
87 LYS ( 87 ) A 3 -0.653 0.015 -1.293 0.631 -1.207
88 ALA ( 88 ) A 3 -0.233 -0.202 -0.107 0.000 0.000
89 LYS ( 89 ) A 3 -0.778 -0.620 -0.519 0.484 -1.244
90 VAL ( 90 ) A 3 -1.157 -0.506 -1.324 0.210 -1.555
91 TYR ( 91 ) A 3 -0.764 -0.983 0.390 -0.885 -0.055
92 ASP ( 92 ) A 3 -1.027 -0.629 -0.485 -0.988 -0.590
93 ALA ( 93 ) A 1 -1.601 -1.694 -0.783 0.000 0.000
94 GLY ( 94 ) A 3 -0.245 0.284 -0.761 0.000 0.000
95 PRO ( 95 ) A 3 0.817 0.158 0.223 1.924 -0.068
96 ALA ( 96 ) A 3 -0.556 -0.481 -0.249 0.000 0.000
97 GLU ( 97 ) A 3 -1.184 0.256 -0.924 0.537 -1.568
98 TRP ( 98 ) A 2 -2.234 -1.484 -2.118 -0.584 -2.653
99 VAL ( 99 ) A 3 0.099 0.603 0.190 -0.770 -0.260
100 GLU ( 100 ) A 3 -0.669 0.155 -0.331 -0.191 -0.860
101 LYS ( 101 ) A 3 -1.666 -1.416 -1.647 -1.015 -0.516
102 ASP ( 102 ) A 3 -1.413 -0.974 -0.835 -0.378 -1.098
103 ALA ( 103 ) A 3 -1.994 -1.614 -0.983 0.000 0.000
104 GLY ( 104 ) A 3 -1.202 -1.509 0.068 0.000 0.000
105 LYS ( 105 ) A 3 -1.887 -1.321 -1.404 -1.125 -0.951
106 MET ( 106 ) A 3 -1.449 -0.433 -0.904 -0.341 -1.239
107 ILE ( 107 ) A 3 -0.970 0.032 -1.892 0.702 -1.605
108 ILE ( 108 ) A 3 -1.626 -0.812 -0.657 -1.272 -1.054
109 ASP ( 109 ) A 3 -1.647 -0.972 -1.263 -0.314 -1.434
110 ALA ( 110 ) A 3 -1.120 -1.164 -0.241 0.000 0.000
111 SER ( 111 ) A 3 -1.631 -1.216 -1.467 -0.353 -0.956
112 PRO ( 112 ) A 3 -0.886 -0.730 -1.025 -0.433 -0.265
113 THR ( 113 ) A 3 -0.956 -0.014 -0.860 -0.979 -1.404
114 ILE ( 114 ) A 3 -1.241 -0.639 -0.651 -1.382 -0.765
115 CYS ( 115 ) A 3 -1.024 -1.096 0.104 -1.145 -0.714
116 HIS ( 116 ) A 2 -1.146 -0.989 0.002 -1.957 -1.108
117 GLU ( 117 ) A 3 -0.869 -0.363 -0.564 -0.366 -0.608
118 LEU ( 118 ) A 2 -2.392 -2.373 -1.440 -0.926 -1.975
119 THR ( 119 ) A 3 0.012 0.046 0.150 0.295 -0.705
120 GLY ( 120 ) A 3 -0.373 -0.097 -0.517 0.000 0.000
121 GLY ( 121 ) A 3 -0.102 -0.342 0.440 0.000 0.000
122 SER ( 122 ) A 3 -0.612 -1.111 0.412 -1.011 0.073
123 SER ( 123 ) A 3 -0.099 -1.093 0.959 0.003 1.208
124 CYS ( 124 ) A 3 -0.944 -0.584 -0.746 -1.079 -1.200
125 GLY ( 125 ) A 3 -1.172 -0.935 -0.781 0.000 0.000
126 TRP ( 126 ) A 3 -1.447 -0.561 -1.157 -1.103 -1.411
127 SER ( 127 ) A 3 -1.635 -0.986 -1.431 -0.826 -1.098
128 ASP ( 128 ) A 3 -1.195 -0.450 -1.021 -0.889 -0.754
129 LYS ( 129 ) A 3 -0.518 -0.229 -0.158 -0.092 -0.735
130 PHE ( 130 ) A 2 -1.317 -0.769 -0.981 -0.872 -2.074
131 GLU ( 131 ) A 2 -0.599 0.227 -1.016 -0.233 -1.159
132 ILE ( 132 ) A 2 -0.914 -0.096 0.104 -1.870 -0.944
133 THR ( 133 ) A 2 -0.689 0.284 -1.181 -1.394 -1.792
134 ALA ( 134 ) A 2 -0.347 0.433 -1.534 0.000 0.000
135 THR ( 135 ) A 2 0.414 1.453 -0.578 -1.095 -0.224
136 VAL ( 136 ) A 2 0.046 1.015 -0.102 -1.537 -1.377
137 THR ( 137 ) A 2 -0.308 0.472 -0.655 -1.400 -1.147
138 SER ( 138 ) A 2 -0.248 -0.087 -0.280 0.031 -1.104
139 LEU ( 139 ) A 2 -2.250 -1.161 -2.027 -1.717 -2.007
140 THR ( 140 ) A 2 -1.239 -1.029 -0.947 -1.282 -0.838
141 ASP ( 141 ) A 3 -1.171 -0.695 -0.776 -0.788 -0.701
142 SER ( 142 ) A 3 -0.297 -0.712 0.622 -0.826 -0.742
143 ARG ( 143 ) A 3 0.610 -0.154 1.467 -1.055 1.320
144 PRO ( 144 ) A 3 0.022 -0.108 0.605 0.209 -0.572
145 LEU ( 145 ) A 3 -0.494 -0.384 1.530 -0.810 -0.880
146 GLY ( 146 ) A 3 -0.788 -0.275 -0.891 0.000 0.000
147 PRO ( 147 ) A 3 -0.776 -0.336 -1.201 0.927 -1.371
148 PHE ( 148 ) A 3 -0.884 -0.901 -0.896 -0.154 -0.318
149 ASN ( 149 ) A 3 -1.051 -0.834 -0.949 -0.979 0.332
150 VAL ( 150 ) A 3 -0.907 -1.490 0.664 -1.120 0.048
151 THR ( 151 ) A 3 -0.293 -1.078 -0.146 -1.082 0.627
152 GLU ( 152 ) A 3 -1.958 -1.166 -0.914 -1.196 -1.390
153 GLU ( 153 ) A 3 -1.329 -1.163 -0.776 -0.809 -0.468
154 GLU ( 154 ) A 3 -1.821 -0.802 -1.158 -1.119 -1.209
155 MET ( 155 ) A 3 -1.249 -0.837 -0.772 -0.560 -1.059
156 ASP ( 156 ) A 3 -1.610 -1.223 -0.875 -0.827 -0.961
157 GLN ( 157 ) A 3 -0.317 -0.217 0.099 1.068 -1.527
158 LEU ( 158 ) A 3 -0.685 -0.530 -0.880 0.851 -1.017
159 PHE ( 159 ) A 3 1.559 1.103 0.666 2.276 -0.048
160 ILE ( 160 ) A 2 -1.335 -0.734 -1.134 -1.379 -1.094
161 ASP ( 161 ) A 2 -0.709 -0.414 -0.794 -0.440 -0.758
162 HIS ( 162 ) A 2 -0.078 -0.158 -0.350 0.137 0.350
163 GLU ( 163 ) A 2 -1.676 -0.897 -1.456 -0.969 -1.942
164 ILE ( 164 ) A 2 -1.417 -0.755 -1.046 -1.317 -0.939
165 ALA ( 165 ) A 2 -1.388 -1.666 -0.215 0.000 0.000
166 MET ( 166 ) A 2 -2.297 -1.600 -1.412 -1.819 -1.950
167 ALA ( 167 ) A 3 -1.850 -0.882 -1.483 0.000 0.000
168 GLN ( 168 ) A 3 -0.826 -0.636 -0.734 -0.790 -1.186
169 CYS ( 169 ) A 3 -1.424 -1.107 -1.505 -0.977 -1.865
170 GLU ( 170 ) A 3 -0.675 -0.071 -1.255 0.109 -0.810
171 ALA ( 171 ) A 2 -1.696 -1.892 -0.632 0.000 0.000
172 GLU ( 172 ) A 2 -1.759 -1.373 -0.898 -1.106 -1.143
173 LYS ( 173 ) A 2 -0.871 -0.668 -0.127 -0.716 -0.762
174 THR ( 174 ) A 2 -1.747 -1.634 -1.504 -1.121 -1.567
175 CYS ( 175 ) A 3 -1.361 -0.923 -1.415 -1.299 -1.130
176 ASN ( 176 ) A 3 -0.452 -0.715 -0.347 0.050 0.023
177 GLY ( 177 ) A 3 -1.706 -1.382 -0.953 0.000 0.000
178 PHE ( 178 ) A 2 -3.058 -2.358 -2.229 -1.879 -2.707
179 ASP ( 179 ) A 3 -1.457 -0.844 -0.718 -0.887 -0.866
180 LEU ( 180 ) A 3 -1.523 -1.334 -0.827 -0.920 -0.586
181 GLU ( 181 ) A 3 -0.289 -0.595 1.411 -1.148 -0.772
All contacts : Average = -0.947 Z-score = -6.13
BB-BB contacts : Average = -0.509 Z-score = -3.36
BB-SC contacts : Average = -0.708 Z-score = -5.42
SC-BB contacts : Average = -0.670 Z-score = -3.98
SC-SC contacts : Average = -1.033 Z-score = -5.94
If an individual residue has a quality control value of -2.5 or worse, you should take a look at it. It can mean that the residue:
is involved in symmetry contacts, or
is binding a co-factor, ligand or ion, or
is an active site residue, or
is wrong.
Average protein values ("Z-score for all contacts") can be read as follows:
-5.0 Guaranteed wrong structure. Bad structure or poor model
-3.0 Probably bad structure or unrefined model. Doubtful structure or model
-2.0 Structure OK or good model. Good structures
0.0 Good structures.
2.0 Good structures. Unusually Good structures
4.0 Probably a strange model of a perfect helix
-------------------------------------
seq.B99990003.pdb
--
The packing quality control per amino acid:
Average for range 1 - 182 : -2.281
If a residue has a score of -5.0 or lower, something is really going on:
the residue makes symmetry contacts, is contacting a ligand or an ion, or something is wrong.

Bond lengths that deviate more than 4 sigma:
All bond lengths are in agreement with standard bond lengths using a
tolerance of 4 sigma (both standard values and sigma for amino acids have
been taken from Engh and Huber [REF], for DNA/RNA from Parkinson et al [REF])
Bond lengths were found to deviate normally from the standard bond lengths
(values for Protein residues were taken from Engh and Huber [REF], for
DNA/RNA from Parkinson et al [REF]).
RMS Z-score for bond lengths: 0.968
RMS-deviation in bond distances: 0.020
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.
You have most probably seen symmetry problems earlier. Please correct these
and rerun this check to see the possible implications on the X-ray cell axes.

Planarity validation results:
All of the side chains of residues that have a planar group are planar
within expected RMS deviations.
All of the atoms that are connected to planar aromatic rings in side chains
of amino-acid residues are in the plane within expected RMS deviations.
Since there is no DNA and no protein with hydrogens, no uncalibrated
planarity check was performed.
If you have detected any error, or have any question or suggestion, please send an Email to Gert Vriend.
Roland Krause, Jens Erik Nielsen, Gert Vriend.

The packing quality control per amino acid:
----Residue------- State AllAll BB-BB BB-SC SC-BB SC-SC
---------------------------------------------------------------------------
1 MET ( 1 ) A 3 -0.791 -0.688 -0.478 -0.944 -0.642
2 ARG ( 2 ) A 3 -1.516 -0.994 -0.572 -0.952 -1.203
3 ILE ( 3 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
4 ALA ( 4 ) A 3 -0.971 -1.078 -0.794 0.000 0.000
5 PHE ( 5 ) A 3 -1.356 -0.801 -0.898 -1.027 -0.958
6 PHE ( 6 ) A 3 -1.409 -0.948 -0.779 -1.079 -1.044
7 LEU ( 7 ) A 3 -2.110 -1.233 -1.533 -1.174 -1.419
8 LEU ( 8 ) A 3 -1.547 -1.068 -1.105 -1.015 -1.030
9 ILE ( 9 ) A 3 -1.049 -0.719 -1.144 -1.207 -1.585
10 LEU ( 10 ) A 3 -0.826 -0.754 -0.770 -0.470 -1.030
11 SER ( 11 ) A 3 -1.143 -0.729 -1.005 -0.826 -0.742
12 ILE ( 12 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
13 ILE ( 13 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
14 VAL ( 14 ) A 3 -1.352 -0.821 -0.810 -0.825 -1.086
15 GLY ( 15 ) A 3 -1.413 -1.020 -0.877 0.000 0.000
16 LEU ( 16 ) A 3 -0.826 -0.754 -0.770 -0.470 -1.030
17 ALA ( 17 ) A 3 -0.971 -1.078 -0.794 0.000 0.000
18 TYR ( 18 ) A 3 -1.539 -0.859 -1.134 -1.153 -1.399
19 GLY ( 19 ) A 3 -1.945 -1.399 -1.423 0.000 0.000
20 TYR ( 20 ) A 3 -1.338 -0.772 -0.859 -1.153 -1.209
21 SER ( 21 ) A 3 -0.350 -0.239 -0.636 0.365 0.118
22 CYS ( 22 ) A 3 -1.613 -1.114 -1.706 -1.363 -2.016
23 PRO ( 23 ) A 3 -1.181 -0.710 -0.536 -0.752 -0.493
24 LYS ( 24 ) A 3 -2.484 -1.549 -1.565 -2.202 -0.868
25 PRO ( 25 ) A 3 -0.312 -0.470 0.384 -0.752 -0.071
26 CYS ( 26 ) A 3 -0.979 -1.139 0.061 -1.077 -0.704
27 TYR ( 27 ) A 3 0.270 0.229 0.462 0.588 -0.595
28 GLY ( 28 ) A 3 -1.264 -0.335 -1.570 0.000 0.000
29 ASN ( 29 ) A 3 -0.649 0.194 -1.447 0.941 -1.502
30 MET ( 30 ) A 3 0.853 3.271 -0.755 0.566 -0.726
31 CYS ( 31 ) A 3 -0.725 -0.322 -1.312 -0.276 -0.651
32 CYS ( 32 ) A 3 -1.162 -0.626 -1.164 -1.178 -1.802
33 SER ( 33 ) A 2 -0.698 -0.574 -0.023 -1.273 -1.104
34 THR ( 34 ) A 2 -1.278 -1.070 -0.642 -1.515 -1.070
35 SER ( 35 ) A 2 -0.790 -0.342 -0.939 -1.391 -1.000
36 PRO ( 36 ) A 2 -1.189 -0.013 -1.033 -1.694 -1.807
37 ASP ( 37 ) A 2 -0.397 0.317 -0.850 -0.720 -0.391
38 HIS ( 38 ) A 2 0.486 0.965 0.590 -1.265 -0.884
39 LYS ( 39 ) A 2 0.155 0.783 -0.339 -0.359 -0.127
40 TYR ( 40 ) A 2 -0.423 -0.295 -0.489 -0.213 -0.310
41 TYR ( 41 ) A 2 -0.086 0.209 -0.476 0.196 -0.562
42 LEU ( 42 ) A 2 -1.856 -0.922 -1.796 -1.841 -1.457
43 THR ( 43 ) A 3 -0.571 -0.686 -0.605 0.099 0.079
44 ASP ( 44 ) A 3 -0.628 0.648 -0.994 -0.809 -0.699
45 PHE ( 45 ) A 3 -0.786 0.301 -1.486 0.069 -0.831
46 CYS ( 46 ) A 3 -1.175 -1.078 -0.013 -1.561 -0.847
47 GLY ( 47 ) A 3 0.149 0.819 -1.252 0.000 0.000
48 SER ( 48 ) A 3 -0.784 -0.628 -1.235 0.106 -0.137
49 THR ( 49 ) A 3 -0.857 -0.877 -0.769 0.009 -0.430
50 SER ( 50 ) A 3 0.353 0.211 0.786 -0.701 -0.595
51 ALA ( 51 ) A 3 -0.481 -0.379 -0.258 0.000 0.000
52 CYS ( 52 ) A 3 -0.970 -0.298 -1.276 -0.982 -1.872
53 GLY ( 53 ) A 3 -1.211 -1.034 -0.569 0.000 0.000
54 PRO ( 54 ) A 2 -1.507 -1.149 -1.350 -0.810 -1.302
55 LYS ( 55 ) A 2 -1.223 -1.049 -0.758 -1.337 -0.446
56 PRO ( 56 ) A 2 -0.959 -0.591 -1.167 -0.528 -0.998
57 SER ( 57 ) A 2 -0.392 0.044 -1.015 -0.387 -0.596
58 CYS ( 58 ) A 2 -0.377 0.536 0.346 -1.856 -6.117
59 SER ( 59 ) A 2 0.970 1.125 0.710 -0.601 0.874
60 GLY ( 60 ) A 2 0.292 0.690 -0.656 0.000 0.000
61 LYS ( 61 ) A 2 -0.758 -0.302 -0.740 -0.820 -0.730
62 LEU ( 62 ) A 2 -1.495 -0.802 -1.549 -0.096 -2.046
63 TYR ( 63 ) A 2 -1.610 -1.019 -1.441 -0.322 -2.196
64 PHE ( 64 ) A 3 -0.028 0.510 -0.237 0.532 -0.876
65 THR ( 65 ) A 3 -0.740 -0.733 -0.379 -1.108 -0.639
66 ALA ( 66 ) A 3 -0.649 -0.031 -0.869 0.000 0.000
67 ASP ( 67 ) A 3 0.130 2.093 -0.544 -0.405 -1.274
68 SER ( 68 ) A 3 0.141 0.855 -0.947 1.130 -1.339
69 GLN ( 69 ) A 3 -0.337 0.085 0.014 0.013 -0.842
70 ARG ( 70 ) A 3 -0.721 0.737 -0.977 0.438 -1.415
71 PHE ( 71 ) A 3 0.371 0.076 0.492 -0.443 0.700
72 GLY ( 72 ) A 1 -0.648 -0.648 -0.465 0.000 0.000
73 CYS ( 73 ) A 3 -1.093 -0.433 -1.280 -1.143 -1.903
74 GLY ( 74 ) A 3 -1.725 -0.708 -1.963 0.000 0.000
75 LYS ( 75 ) A 3 -1.234 -0.719 -0.831 -1.058 -1.346
76 HIS ( 76 ) A 3 -1.450 -1.122 -1.559 -0.760 -0.900
77 LEU ( 77 ) A 3 -0.228 0.173 0.358 0.119 -1.083
78 ASN ( 78 ) A 3 -1.212 0.147 -0.878 -1.036 -1.345
79 LEU ( 79 ) A 3 -0.497 0.229 -0.006 -0.669 -0.673
80 CYS ( 80 ) A 1 -1.184 -0.534 -1.786 -1.036 -1.824
81 ARG ( 81 ) A 1 -1.430 -1.174 -1.136 -0.688 -0.737
82 GLY ( 82 ) A 3 1.685 1.687 0.468 0.000 0.000
83 LYS ( 83 ) A 3 0.702 1.250 -0.895 2.077 -0.825
84 LYS ( 84 ) A 3 -0.280 0.802 -1.537 0.586 -0.892
85 CYS ( 85 ) A 3 -1.118 -0.137 -1.814 -0.468 -2.078
86 VAL ( 86 ) A 3 -1.082 0.204 -1.490 -0.283 -1.930
87 LYS ( 87 ) A 3 0.188 0.150 -0.515 2.009 -1.158
88 ALA ( 88 ) A 3 -0.608 -0.554 -0.242 0.000 0.000
89 LYS ( 89 ) A 3 -1.204 -0.731 -0.892 -0.520 -0.989
90 VAL ( 90 ) A 3 -0.802 -0.444 -0.437 0.251 -1.488
91 TYR ( 91 ) A 3 -0.999 -0.765 0.310 -0.991 -0.994
92 ASP ( 92 ) A 3 -0.908 -0.753 0.032 -0.769 -0.707
93 ALA ( 93 ) A 1 -1.342 -1.655 -0.329 0.000 0.000
94 GLY ( 94 ) A 3 0.462 0.631 -0.104 0.000 0.000
95 PRO ( 95 ) A 3 0.420 -0.119 -0.141 1.441 -0.033
96 ALA ( 96 ) A 3 -0.834 -0.437 -0.625 0.000 0.000
97 GLU ( 97 ) A 3 -0.979 0.707 -0.900 -0.648 -1.186
98 TRP ( 98 ) A 2 -1.552 -1.000 -1.532 0.036 -2.349
99 VAL ( 99 ) A 3 0.658 0.578 0.811 0.089 0.184
100 GLU ( 100 ) A 1 -1.169 -1.226 -0.258 -0.609 -0.674
101 LYS ( 101 ) A 3 -1.567 -0.996 -1.393 -0.431 -1.342
102 ASP ( 102 ) A 3 -0.886 -0.759 -1.122 0.873 -0.589
103 ALA ( 103 ) A 3 -1.601 -1.213 -1.116 0.000 0.000
104 GLY ( 104 ) A 3 -1.162 -1.012 -0.520 0.000 0.000
105 LYS ( 105 ) A 3 -0.476 -0.692 -0.838 -0.787 -0.304
106 MET ( 106 ) A 3 -0.696 -0.186 -0.478 -0.944 -0.642
107 ILE ( 107 ) A 3 -1.442 -0.524 -1.599 0.495 -1.724
108 ILE ( 108 ) A 3 -0.330 0.509 -1.101 -0.737 -1.501
109 ASP ( 109 ) A 3 -1.789 -0.720 -1.804 -0.257 -1.657
110 ALA ( 110 ) A 3 -1.107 -0.950 -0.480 0.000 0.000
111 SER ( 111 ) A 3 -1.319 -1.302 -0.738 -0.516 -0.446
112 PRO ( 112 ) A 3 -1.001 -0.746 -1.043 -0.418 -0.563
113 THR ( 113 ) A 1 -1.947 -2.053 -0.926 -1.613 -0.505
114 ILE ( 114 ) A 3 -0.070 0.397 0.484 -0.534 -0.565
115 CYS ( 115 ) A 2 -1.418 -1.338 -0.072 -1.560 -1.543
116 HIS ( 116 ) A 2 -1.090 -0.856 -0.038 -2.531 -0.868
117 GLU ( 117 ) A 2 -2.250 -1.922 -1.597 -1.383 -1.404
118 LEU ( 118 ) A 2 -2.080 -2.203 -1.131 -1.091 -1.228
119 THR ( 119 ) A 3 0.278 0.270 -0.396 1.767 -0.870
120 GLY ( 120 ) A 3 0.028 0.128 -0.148 0.000 0.000
121 GLY ( 121 ) A 3 0.026 -0.882 1.231 0.000 0.000
122 SER ( 122 ) A 3 -0.342 -0.356 -0.189 -0.422 -0.069
123 SER ( 123 ) A 3 -0.404 -0.806 0.541 -1.069 0.532
124 CYS ( 124 ) A 3 -1.215 -1.216 -0.364 -1.567 -0.230
125 GLY ( 125 ) A 3 -2.175 -1.633 -1.318 0.000 0.000
126 TRP ( 126 ) A 3 -1.547 -0.632 -1.449 -1.121 -1.411
127 SER ( 127 ) A 3 -1.309 -1.203 -1.354 -0.848 -0.266
128 ASP ( 128 ) A 3 -0.669 -0.759 -0.565 -0.201 -0.320
129 LYS ( 129 ) A 3 -0.518 -0.379 -0.498 0.694 -1.059
130 PHE ( 130 ) A 2 -2.318 -1.429 -1.798 -1.065 -2.978
131 GLU ( 131 ) A 2 -0.257 0.324 -1.055 0.217 -0.653
132 ILE ( 132 ) A 2 -0.836 -0.390 0.788 -1.816 -0.761
133 THR ( 133 ) A 2 -0.142 0.053 0.258 -0.614 -1.034
134 ALA ( 134 ) A 2 -0.364 0.494 -1.679 0.000 0.000
135 THR ( 135 ) A 2 0.237 1.502 -1.046 -1.621 0.108
136 VAL ( 136 ) A 2 1.079 0.983 0.254 0.556 2.010
137 THR ( 137 ) A 2 -0.583 0.022 -0.274 -1.470 -1.547
138 SER ( 138 ) A 2 -0.065 0.003 0.397 -0.864 -0.509
139 LEU ( 139 ) A 2 -1.627 -0.973 -1.001 -1.046 -1.869
140 THR ( 140 ) A 2 -1.029 -1.069 -0.567 -0.833 -0.039
141 ASP ( 141 ) A 3 -1.365 -0.895 -0.825 -0.671 -0.951
142 SER ( 142 ) A 3 -0.660 -0.607 -0.494 -0.826 0.028
143 ARG ( 143 ) A 3 -1.186 -0.463 -0.212 -0.494 -1.286
144 PRO ( 144 ) A 3 0.061 -0.341 0.715 0.564 -0.483
145 LEU ( 145 ) A 3 -1.262 -1.086 0.042 -1.060 -0.887
146 GLY ( 146 ) A 3 -0.859 -0.781 -0.340 0.000 0.000
147 PRO ( 147 ) A 3 -0.104 -0.386 0.454 -0.037 -0.284
148 PHE ( 148 ) A 3 -0.734 -0.299 -0.262 0.167 -1.044
149 ASN ( 149 ) A 3 -0.257 -0.570 1.178 -1.054 -0.237
150 VAL ( 150 ) A 3 -1.293 -0.888 -0.653 -0.934 -1.058
151 THR ( 151 ) A 3 -0.309 -1.078 -0.038 -1.082 0.155
152 GLU ( 152 ) A 3 -1.921 -1.103 -0.953 -1.027 -1.218
153 GLU ( 153 ) A 3 -0.961 -0.612 -0.609 -1.148 -0.810
154 GLU ( 154 ) A 3 -1.439 -0.930 -1.255 -1.148 -0.810
155 MET ( 155 ) A 3 -0.788 -0.477 -0.447 1.009 -1.275
156 ASP ( 156 ) A 3 -0.996 -0.503 -0.292 -1.205 -0.669
157 GLN ( 157 ) A 3 -0.997 -0.342 -0.688 -0.088 -1.509
158 LEU ( 158 ) A 3 -0.396 -0.681 -0.386 0.559 -0.359
159 PHE ( 159 ) A 2 -2.965 -2.376 -1.831 -2.032 -2.547
160 ILE ( 160 ) A 3 -0.971 -0.843 0.104 -0.448 -0.695
161 ASP ( 161 ) A 2 -0.726 -0.413 0.210 -1.113 -0.961
162 HIS ( 162 ) A 2 -0.562 -0.271 -0.753 -0.719 -0.284
163 GLU ( 163 ) A 3 -0.787 -0.117 -1.160 0.407 -0.740
164 ILE ( 164 ) A 3 0.973 0.818 -0.586 0.232 0.325
165 ALA ( 165 ) A 2 -1.417 -1.703 -0.215 0.000 0.000
166 MET ( 166 ) A 2 -2.196 -1.565 -1.270 -1.938 -1.721
167 ALA ( 167 ) A 3 -1.884 -0.878 -1.533 0.000 0.000
168 GLN ( 168 ) A 3 -0.923 -0.635 -0.733 -0.900 -1.186
169 CYS ( 169 ) A 3 -1.488 -1.097 -1.708 -1.016 -1.951
170 GLU ( 170 ) A 3 -0.331 -0.037 -1.255 0.598 -0.507
171 ALA ( 171 ) A 2 -2.011 -1.961 -1.265 0.000 0.000
172 GLU ( 172 ) A 2 -1.596 -1.002 -0.842 -0.997 -0.809
173 LYS ( 173 ) A 3 -0.477 -0.090 -0.505 -0.243 -0.683
174 THR ( 174 ) A 2 -1.924 -1.482 -1.966 -1.243 -2.071
175 CYS ( 175 ) A 2 -1.851 -0.997 -2.119 -1.732 0.000
176 ASN ( 176 ) A 3 -0.614 -0.567 -0.331 -0.127 -0.633
177 GLY ( 177 ) A 3 -0.740 -0.853 0.299 0.000 0.000
178 PHE ( 178 ) A 3 -1.382 -0.832 -0.691 -0.795 -0.986
179 ASP ( 179 ) A 3 -1.322 -0.821 -0.431 -0.889 -0.825
180 LEU ( 180 ) A 3 -1.797 -1.364 -0.952 -1.299 -0.738
181 GLU ( 181 ) A 3 0.063 -0.311 1.760 -1.148 -0.585
All contacts : Average = -0.877 Z-score = -5.68
BB-BB contacts : Average = -0.477 Z-score = -3.16
BB-SC contacts : Average = -0.675 Z-score = -5.17
SC-BB contacts : Average = -0.567 Z-score = -3.35
SC-SC contacts : Average = -0.990 Z-score = -5.69
If an individual residue has a quality control value of -2.5 or worse, you should take a look at it. It can mean that the residue:
is involved in symmetry contacts, or
is binding a co-factor, ligand or ion, or
is an active site residue, or
is wrong.
Average protein values ("Z-score for all contacts") can be read as follows:
-5.0 Guaranteed wrong structure. Bad structure or poor model
-3.0 Probably bad structure or unrefined model. Doubtful structure or model
-2.0 Structure OK or good model. Good structures
0.0 Good structures.
2.0 Good structures. Unusually Good structures
4.0 Probably a strange model of a perfect helix
-------------------------------------
seq.B99990004.pdb
--
The packing quality control per amino acid:
Average for range 1 - 182 : -2.347
If a residue has a score of -5.0 or lower, something is really going on:
the residue makes symmetry contacts, is contacting a ligand or an ion, or something is wrong.

Bond lengths that deviate more than 4 sigma:
All bond lengths are in agreement with standard bond lengths using a
tolerance of 4 sigma (both standard values and sigma for amino acids have
been taken from Engh and Huber [REF], for DNA/RNA from Parkinson et al [REF])
Bond lengths were found to deviate normally from the standard bond lengths
(values for Protein residues were taken from Engh and Huber [REF], for
DNA/RNA from Parkinson et al [REF]).
RMS Z-score for bond lengths: 0.968
RMS-deviation in bond distances: 0.020
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.
You have most probably seen symmetry problems earlier. Please correct these
and rerun this check to see the possible implications on the X-ray cell axes.

Planarity validation results:
The side chains of the residues listed in the table below contain a planar
group that was found to deviate from planarity by more than 4.0 times the
expected value. For an amino acid residue that has a side chain with a
planar group, the RMS deviation of the atoms to a least squares plane was
determined. The number in the table is the number of standard deviations
this RMS value deviates from the expected value. Not knowing better yet, we
assume that planarity of the groups analyzed should be perfect.
98 TRP ( 98 ) A 4.54
All of the atoms that are connected to planar aromatic rings in side chains
of amino-acid residues are in the plane within expected RMS deviations.
Since there is no DNA and no protein with hydrogens, no uncalibrated
planarity check was performed.

The packing quality control per amino acid:
----Residue------- State AllAll BB-BB BB-SC SC-BB SC-SC
---------------------------------------------------------------------------
1 MET ( 1 ) A 3 -0.791 -0.688 -0.478 -0.944 -0.642
2 ARG ( 2 ) A 3 -1.516 -0.994 -0.572 -0.952 -1.203
3 ILE ( 3 ) A 3 -1.834 -1.013 -1.146 -1.207 -1.585
4 ALA ( 4 ) A 3 -1.669 -1.078 -1.201 0.000 0.000
5 PHE ( 5 ) A 3 -1.356 -0.801 -0.898 -1.027 -0.958
6 PHE ( 6 ) A 3 -1.356 -0.801 -0.898 -1.027 -0.958
7 LEU ( 7 ) A 3 -2.110 -1.233 -1.533 -1.174 -1.419
8 LEU ( 8 ) A 3 -2.110 -1.233 -1.533 -1.174 -1.419
9 ILE ( 9 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
10 LEU ( 10 ) A 3 -0.826 -0.754 -0.770 -0.470 -1.030
11 SER ( 11 ) A 3 -1.143 -0.729 -1.005 -0.826 -0.742
12 ILE ( 12 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
13 ILE ( 13 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
14 VAL ( 14 ) A 3 -1.352 -0.821 -0.810 -0.825 -1.086
15 GLY ( 15 ) A 3 -1.413 -1.020 -0.877 0.000 0.000
16 LEU ( 16 ) A 3 -0.786 -0.754 -0.737 -0.470 -1.030
17 ALA ( 17 ) A 3 -0.764 -1.078 -0.668 0.000 0.000
18 TYR ( 18 ) A 3 -1.539 -0.859 -1.134 -1.153 -1.399
19 GLY ( 19 ) A 3 -1.413 -1.020 -0.877 0.000 0.000
20 TYR ( 20 ) A 3 -1.512 -0.859 -1.074 -1.153 -1.382
21 SER ( 21 ) A 3 -1.183 -0.903 -1.060 -0.248 -0.477
22 CYS ( 22 ) A 3 -1.678 -1.207 -1.754 -1.379 -2.034
23 PRO ( 23 ) A 3 -1.194 -0.710 -0.817 -0.752 -0.831
24 LYS ( 24 ) A 3 -2.062 -1.532 -1.511 -1.344 -0.862
25 PRO ( 25 ) A 3 -0.591 -0.710 0.386 -0.752 -0.618
26 CYS ( 26 ) A 3 -1.147 -1.154 -0.305 -1.166 -1.124
27 TYR ( 27 ) A 3 -0.485 0.043 -0.212 -0.464 -0.920
28 GLY ( 28 ) A 3 -1.101 -0.763 -0.749 0.000 0.000
29 ASN ( 29 ) A 3 -0.509 0.362 -0.092 -0.926 -1.191
30 MET ( 30 ) A 3 1.663 3.846 0.228 1.012 -0.562
31 CYS ( 31 ) A 3 -0.607 0.124 -1.077 -0.646 -0.805
32 CYS ( 32 ) A 3 -0.926 -0.374 -0.801 -1.168 -1.594
33 SER ( 33 ) A 3 -0.332 -0.669 0.380 -0.774 0.164
34 THR ( 34 ) A 2 -0.855 -0.958 0.511 -1.402 -0.868
35 SER ( 35 ) A 2 -0.612 -0.580 -0.558 -0.256 -0.020
36 PRO ( 36 ) A 2 -1.283 -0.064 -1.175 -1.801 -1.810
37 ASP ( 37 ) A 2 -0.708 -0.149 -0.250 -0.825 -1.030
38 HIS ( 38 ) A 2 0.969 0.981 1.545 -0.982 0.239
39 LYS ( 39 ) A 2 -0.418 0.662 -0.672 -0.381 -1.691
40 TYR ( 40 ) A 2 -0.775 -0.010 -1.423 0.070 -1.585
41 TYR ( 41 ) A 2 0.202 -0.040 0.037 0.062 1.047
42 LEU ( 42 ) A 2 -0.268 0.602 -0.907 -0.931 -0.498
43 THR ( 43 ) A 3 -0.998 -0.662 -1.027 -0.886 -0.728
44 ASP ( 44 ) A 3 -0.993 0.154 -1.197 -0.725 -0.972
45 PHE ( 45 ) A 2 -1.717 -1.027 -1.942 -1.224 -1.336
46 CYS ( 46 ) A 3 -1.107 -0.602 -1.429 -1.052 -1.263
47 GLY ( 47 ) A 3 -0.564 0.396 -1.794 0.000 0.000
48 SER ( 48 ) A 2 -1.226 -1.395 -0.641 -0.403 0.430
49 THR ( 49 ) A 3 -0.955 -1.341 -0.718 -0.436 0.377
50 SER ( 50 ) A 3 -0.278 -0.018 -0.305 -0.684 -0.346
51 ALA ( 51 ) A 3 -0.471 -0.412 -0.208 0.000 0.000
52 CYS ( 52 ) A 3 -1.293 -0.702 -1.506 -1.196 -1.885
53 GLY ( 53 ) A 3 -1.392 -0.513 -1.540 0.000 0.000
54 PRO ( 54 ) A 2 -1.675 -1.571 -1.022 -1.337 -1.197
55 LYS ( 55 ) A 2 -1.438 -1.255 -0.578 -1.379 -0.950
56 PRO ( 56 ) A 2 -1.028 -0.410 -1.196 -0.728 -1.399
57 SER ( 57 ) A 2 -0.348 0.060 -0.582 -0.493 -1.353
58 CYS ( 58 ) A 2 0.057 0.365 0.071 -0.840 4.039
59 SER ( 59 ) A 2 1.208 1.037 0.442 1.125 1.769
60 GLY ( 60 ) A 2 0.166 0.465 -0.527 0.000 0.000
61 LYS ( 61 ) A 2 -1.254 -0.646 -0.563 -1.434 -1.393
62 LEU ( 62 ) A 2 -1.538 -0.938 -1.439 -0.814 -1.733
63 TYR ( 63 ) A 2 -1.224 -0.823 -1.579 0.167 -1.735
64 PHE ( 64 ) A 3 0.102 0.308 0.150 0.330 -0.354
65 THR ( 65 ) A 3 -0.500 -0.727 0.183 -0.889 -0.255
66 ALA ( 66 ) A 3 -0.358 -0.602 0.156 0.000 0.000
67 ASP ( 67 ) A 3 0.896 2.126 0.269 0.791 -0.980
68 SER ( 68 ) A 3 -0.028 0.840 -1.258 1.150 -1.521
69 GLN ( 69 ) A 3 -0.520 -0.121 -0.397 0.218 -0.909
70 ARG ( 70 ) A 3 0.126 0.902 -0.200 -0.063 -0.265
71 PHE ( 71 ) A 3 -0.472 0.574 -1.282 -0.967 -0.186
72 GLY ( 72 ) A 1 -1.473 -1.441 -1.107 0.000 0.000
73 CYS ( 73 ) A 3 -0.250 -0.809 0.182 -0.341 1.342
74 GLY ( 74 ) A 3 -1.292 -0.971 -0.964 0.000 0.000
75 LYS ( 75 ) A 3 -1.260 -0.770 -0.831 -1.059 -1.346
76 HIS ( 76 ) A 3 -0.770 -1.241 -0.452 -1.305 0.768
77 LEU ( 77 ) A 3 -1.847 -0.475 -1.402 -0.847 -1.631
78 ASN ( 78 ) A 3 -1.493 -0.120 -1.558 -1.061 -0.986
79 LEU ( 79 ) A 3 -1.668 -0.239 -1.092 -0.953 -1.736
80 CYS ( 80 ) A 1 -0.522 0.429 -1.810 -0.769 -0.845
81 ARG ( 81 ) A 1 -1.943 -1.320 -1.359 -1.487 -1.217
82 GLY ( 82 ) A 3 1.163 1.870 -0.600 0.000 0.000
83 LYS ( 83 ) A 3 0.043 1.160 -1.397 1.743 -1.556
84 LYS ( 84 ) A 3 -0.388 0.490 -1.084 0.822 -1.302
85 CYS ( 85 ) A 3 -0.267 0.277 -1.444 0.483 -1.562
86 VAL ( 86 ) A 3 -0.970 0.177 -1.742 0.150 -1.637
87 LYS ( 87 ) A 3 0.010 0.583 -1.248 1.199 -0.799
88 ALA ( 88 ) A 3 0.292 0.036 0.361 0.000 0.000
89 LYS ( 89 ) A 3 -1.094 -0.590 -0.862 0.320 -1.596
90 VAL ( 90 ) A 3 -1.126 -0.168 -1.455 -0.037 -1.685
91 TYR ( 91 ) A 3 -0.847 -0.672 -0.481 -0.676 -0.125
92 ASP ( 92 ) A 3 -1.029 -1.115 -1.297 0.025 -0.332
93 ALA ( 93 ) A 1 -1.575 -1.844 -0.524 0.000 0.000
94 GLY ( 94 ) A 3 -0.205 0.122 -0.485 0.000 0.000
95 PRO ( 95 ) A 3 -0.551 0.001 -0.182 -0.092 -0.958
96 ALA ( 96 ) A 3 -0.812 -0.489 -0.596 0.000 0.000
97 GLU ( 97 ) A 3 -1.808 0.123 -1.474 -0.274 -1.831
98 TRP ( 98 ) A 2 -2.306 -1.583 -2.146 -0.580 -2.679
99 VAL ( 99 ) A 3 0.184 0.566 -0.385 0.038 -0.012
100 GLU ( 100 ) A 1 -1.021 -1.006 -0.620 -0.314 -0.654
101 LYS ( 101 ) A 3 -1.023 -0.905 -0.275 -0.629 -0.753
102 ASP ( 102 ) A 3 -0.936 -0.840 -0.779 0.016 -0.789
103 ALA ( 103 ) A 3 -1.608 -1.669 -0.347 0.000 0.000
104 GLY ( 104 ) A 3 -1.106 -1.164 -0.231 0.000 0.000
105 LYS ( 105 ) A 3 -1.269 -1.066 -1.215 -0.932 -0.181
106 MET ( 106 ) A 3 -0.707 -0.243 -0.477 -0.944 -0.642
107 ILE ( 107 ) A 3 -1.590 -0.073 -1.711 -0.389 -1.743
108 ILE ( 108 ) A 3 -0.331 0.436 -0.818 0.389 -1.129
109 ASP ( 109 ) A 3 -1.414 -0.821 -0.952 -0.129 -1.427
110 ALA ( 110 ) A 3 -0.991 -0.788 -0.505 0.000 0.000
111 SER ( 111 ) A 3 -1.696 -1.594 -0.934 -0.402 -1.123
112 PRO ( 112 ) A 3 0.349 -0.122 0.543 0.282 0.250
113 THR ( 113 ) A 1 -1.324 -1.398 -0.263 -1.425 -0.591
114 ILE ( 114 ) A 3 -0.824 0.155 -0.312 -0.912 -1.086
115 CYS ( 115 ) A 2 -1.568 -1.493 -0.504 -1.389 -1.441
116 HIS ( 116 ) A 2 -1.456 -1.068 -0.577 -1.579 -0.808
117 GLU ( 117 ) A 2 -2.279 -1.879 -1.737 -1.232 -1.597
118 LEU ( 118 ) A 2 -2.410 -2.355 -1.248 -1.119 -1.988
119 THR ( 119 ) A 2 -1.764 -1.575 -1.552 -1.239 -1.652
120 GLY ( 120 ) A 3 -0.268 -0.650 0.416 0.000 0.000
121 GLY ( 121 ) A 3 -0.537 -1.077 0.547 0.000 0.000
122 SER ( 122 ) A 3 -0.837 -0.698 -0.737 -0.572 -0.771
123 SER ( 123 ) A 3 -0.865 -1.237 -0.190 -0.844 0.849
124 CYS ( 124 ) A 3 -1.050 -0.732 -0.424 -1.331 -1.415
125 GLY ( 125 ) A 3 -2.042 -1.599 -1.151 0.000 0.000
126 TRP ( 126 ) A 3 -1.648 -0.795 -1.573 -1.121 -1.406
127 SER ( 127 ) A 3 -1.212 -1.037 -1.290 -0.828 -0.578
128 ASP ( 128 ) A 3 -1.180 -0.775 -0.193 -0.875 -0.758
129 LYS ( 129 ) A 3 -1.414 -1.190 -0.553 -0.903 -0.844
130 PHE ( 130 ) A 2 -2.296 -1.237 -1.941 -1.221 -2.998
131 GLU ( 131 ) A 2 -0.305 0.510 -0.584 0.044 -1.185
132 ILE ( 132 ) A 2 -0.728 -0.279 0.819 -1.772 -0.575
133 THR ( 133 ) A 2 -0.593 -0.119 -0.867 -0.666 -1.621
134 ALA ( 134 ) A 2 -0.332 0.366 -1.384 0.000 0.000
135 THR ( 135 ) A 2 1.076 1.474 -0.800 1.128 1.203
136 VAL ( 136 ) A 2 -0.029 0.848 0.147 -1.551 -0.521
137 THR ( 137 ) A 2 -0.439 0.250 -0.563 -1.165 -1.606
138 SER ( 138 ) A 2 -0.615 -0.334 -0.826 0.041 -1.482
139 LEU ( 139 ) A 2 -1.134 -0.468 -1.525 -0.601 -1.139
140 THR ( 140 ) A 2 -1.379 -1.178 -1.048 -1.284 -1.179
141 ASP ( 141 ) A 3 -1.490 -0.861 -0.996 -0.931 -0.966
142 SER ( 142 ) A 3 -1.124 -0.721 -0.977 -0.826 -0.742
143 ARG ( 143 ) A 3 -0.226 -0.073 0.223 -0.936 0.105
144 PRO ( 144 ) A 3 -0.408 -0.245 0.224 -0.202 -0.707
145 LEU ( 145 ) A 3 -1.015 -0.750 -0.315 -0.693 -0.718
146 GLY ( 146 ) A 3 -1.966 -1.249 -1.487 0.000 0.000
147 PRO ( 147 ) A 3 -1.347 -0.483 -1.414 0.588 -1.820
148 PHE ( 148 ) A 3 -1.761 -1.051 -0.915 -1.485 -1.086
149 ASN ( 149 ) A 3 -1.205 -1.224 -0.179 -0.979 -0.713
150 VAL ( 150 ) A 3 -1.275 -1.356 -0.854 -0.640 0.418
151 THR ( 151 ) A 3 -1.051 -1.078 -0.973 -1.082 -0.813
152 GLU ( 152 ) A 3 -1.748 -1.176 -1.021 -1.134 -1.030
153 GLU ( 153 ) A 3 -0.961 -0.612 -0.894 -1.148 -0.810
154 GLU ( 154 ) A 3 -2.188 -1.239 -1.546 -1.148 -1.240
155 MET ( 155 ) A 3 -1.266 -0.583 -1.533 0.559 -1.561
156 ASP ( 156 ) A 3 -1.968 -1.271 -1.459 -0.699 -1.434
157 GLN ( 157 ) A 3 0.356 -0.378 -0.203 2.886 -0.887
158 LEU ( 158 ) A 3 -1.357 -0.384 -1.435 0.065 -1.558
159 PHE ( 159 ) A 3 -0.374 0.250 -0.958 0.299 -0.494
160 ILE ( 160 ) A 2 -0.794 -0.633 0.422 -1.324 -0.065
161 ASP ( 161 ) A 2 -0.865 -0.135 0.055 -1.109 -1.525
162 HIS ( 162 ) A 3 0.579 0.862 -0.872 1.154 0.164
163 GLU ( 163 ) A 2 -1.057 -0.307 -1.383 -0.328 -1.417
164 ILE ( 164 ) A 2 -0.783 -1.064 -0.756 -0.395 0.865
165 ALA ( 165 ) A 2 -1.640 -1.674 -0.874 0.000 0.000
166 MET ( 166 ) A 2 -2.716 -1.646 -1.176 -1.903 -1.612
167 ALA ( 167 ) A 3 -1.036 -0.446 -0.985 0.000 0.000
168 GLN ( 168 ) A 3 -0.921 -0.628 -0.734 -0.900 -1.186
169 CYS ( 169 ) A 3 -2.094 -1.843 -2.027 -1.638 -1.367
170 GLU ( 170 ) A 3 1.488 -0.237 0.415 -0.316 2.383
171 ALA ( 171 ) A 2 -1.681 -1.914 -0.539 0.000 0.000
172 GLU ( 172 ) A 2 -1.529 -1.370 -0.337 -1.171 -0.782
173 LYS ( 173 ) A 2 -0.383 -0.631 -0.426 0.092 0.113
174 THR ( 174 ) A 2 -1.704 -1.577 -1.371 -1.119 -1.305
175 CYS ( 175 ) A 3 -1.692 -1.491 -1.151 -1.616 -0.995
176 ASN ( 176 ) A 3 -1.737 -1.206 -1.423 -0.790 -0.675
177 GLY ( 177 ) A 3 -1.344 -0.984 -0.484 0.000 0.000
178 PHE ( 178 ) A 2 -2.948 -2.345 -2.176 -1.810 -2.447
179 ASP ( 179 ) A 3 -1.470 -0.860 -0.734 -0.888 -0.866
180 LEU ( 180 ) A 3 -1.663 -1.311 -0.996 -1.211 -0.569
181 GLU ( 181 ) A 3 0.052 -0.605 2.203 -1.148 -0.647
All contacts : Average = -0.980 Z-score = -6.34
BB-BB contacts : Average = -0.561 Z-score = -3.69
BB-SC contacts : Average = -0.770 Z-score = -5.89
SC-BB contacts : Average = -0.634 Z-score = -3.76
SC-SC contacts : Average = -0.946 Z-score = -5.42
If an individual residue has a quality control value of -2.5 or worse, you should take a look at it. It can mean that the residue:
is involved in symmetry contacts, or
is binding a co-factor, ligand or ion, or
is an active site residue, or
is wrong.
Average protein values ("Z-score for all contacts") can be read as follows:
-5.0 Guaranteed wrong structure. Bad structure or poor model
-3.0 Probably bad structure or unrefined model. Doubtful structure or model
-2.0 Structure OK or good model. Good structures
0.0 Good structures.
2.0 Good structures. Unusually Good structures
4.0 Probably a strange model of a perfect helix
-------------------------------------
seq.B99990005.pdb
--
The packing quality control per amino acid:
Average for range 1 - 182 : -2.203
If a residue has a score of -5.0 or lower, something is really going on:
the residue makes symmetry contacts, is contacting a ligand or an ion, or something is wrong.

Bond lengths that deviate more than 4 sigma:
The bond lengths listed in the table below were found to deviate more than 4
sigma from standard bond lengths (both standard values and sigmas for amino
acid residues have been taken from Engh and Huber [REF], for DNA they were
taken from Parkinson et al [REF]). In the table below for each unusual bond
the bond length and the number of standard deviations it differs from the
normal value is given.
Atom names starting with "-" belong to the previous residue in the chain. If
the second atom name is "-SG*", the disulphide bridge has a deviating length.
157 GLN ( 157 ) A N CA 1.55 4.7
157 GLN ( 157 ) A CA C 1.83 14.5
157 GLN ( 157 ) A N -C 1.46 6.7
158 LEU ( 158 ) A N CA 1.64 9.6
158 LEU ( 158 ) A N -C 1.55 10.9
Bond lengths were found to deviate normally from the standard bond lengths
(values for Protein residues were taken from Engh and Huber [REF], for
DNA/RNA from Parkinson et al [REF]).
RMS Z-score for bond lengths: 1.031
RMS-deviation in bond distances: 0.021
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.
You have most probably seen symmetry problems earlier. Please correct these
and rerun this check to see the possible implications on the X-ray cell axes.

Planarity validation results:
All of the side chains of residues that have a planar group are planar
within expected RMS deviations.
All of the atoms that are connected to planar aromatic rings in side chains
of amino-acid residues are in the plane within expected RMS deviations.
Since there is no DNA and no protein with hydrogens, no uncalibrated
planarity check was performed.

The packing quality control per amino acid:
----Residue------- State AllAll BB-BB BB-SC SC-BB SC-SC
---------------------------------------------------------------------------
1 MET ( 1 ) A 3 -0.790 -0.688 -0.478 -0.940 -0.642
2 ARG ( 2 ) A 3 -1.516 -0.994 -0.816 -0.952 -1.203
3 ILE ( 3 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
4 ALA ( 4 ) A 3 -1.669 -1.078 -1.201 0.000 0.000
5 PHE ( 5 ) A 3 -1.356 -0.801 -0.898 -1.027 -0.958
6 PHE ( 6 ) A 3 -1.356 -0.801 -0.898 -1.027 -0.958
7 LEU ( 7 ) A 3 -2.110 -1.233 -1.533 -1.174 -1.419
8 LEU ( 8 ) A 3 -1.547 -1.068 -1.105 -1.015 -1.030
9 ILE ( 9 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
10 LEU ( 10 ) A 3 -0.826 -0.754 -0.770 -0.470 -1.030
11 SER ( 11 ) A 3 -1.143 -0.729 -1.005 -0.826 -0.742
12 ILE ( 12 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
13 ILE ( 13 ) A 3 -1.049 -0.719 -1.145 -1.207 -1.585
14 VAL ( 14 ) A 3 -1.352 -0.821 -0.810 -0.825 -1.086
15 GLY ( 15 ) A 3 -1.413 -1.020 -0.877 0.000 0.000
16 LEU ( 16 ) A 3 -0.826 -0.754 -0.770 -0.470 -1.030
17 ALA ( 17 ) A 3 -0.971 -1.078 -0.794 0.000 0.000
18 TYR ( 18 ) A 3 -1.539 -0.859 -1.134 -1.153 -1.399
19 GLY ( 19 ) A 3 -1.413 -1.020 -0.877 0.000 0.000
20 TYR ( 20 ) A 3 -1.502 -0.859 -1.127 -1.153 -1.276
21 SER ( 21 ) A 3 -1.632 -0.986 -1.429 -0.826 -1.085
22 CYS ( 22 ) A 3 -1.678 -1.207 -1.754 -1.379 -2.034
23 PRO ( 23 ) A 3 -1.137 -0.710 -0.817 -0.752 -0.668
24 LYS ( 24 ) A 3 -1.857 -1.526 -1.285 -1.350 -0.552
25 PRO ( 25 ) A 3 -0.376 -0.710 0.438 -0.752 -0.077
26 CYS ( 26 ) A 3 -1.253 -1.207 -0.676 -1.310 -0.699
27 TYR ( 27 ) A 3 -0.116 0.547 -0.481 0.544 -1.119
28 GLY ( 28 ) A 3 -0.989 -0.419 -1.117 0.000 0.000
29 ASN ( 29 ) A 3 -1.374 0.265 -1.529 -0.776 -1.989
30 MET ( 30 ) A 3 -0.839 1.469 -1.312 -0.350 -1.123
31 CYS ( 31 ) A 3 -0.410 0.249 -1.195 -0.270 -1.088
32 CYS ( 32 ) A 3 -0.870 -0.259 -0.896 -1.144 -1.483
33 SER ( 33 ) A 2 -0.731 -1.103 0.878 -1.565 0.668
34 THR ( 34 ) A 2 -0.563 -0.811 1.453 -1.326 -0.972
35 SER ( 35 ) A 2 -0.101 0.091 -0.288 -0.888 0.452
36 PRO ( 36 ) A 2 -0.604 0.634 -1.154 -0.712 -1.869
37 ASP ( 37 ) A 2 -0.387 0.449 -0.246 -0.630 -1.192
38 HIS ( 38 ) A 2 1.347 1.041 2.755 -0.912 0.634
39 LYS ( 39 ) A 2 -0.164 1.131 -0.534 -0.235 -1.865
40 TYR ( 40 ) A 2 -0.716 0.473 -1.794 -0.538 -1.554
41 TYR ( 41 ) A 2 -0.040 0.178 -0.542 0.256 -0.208
42 LEU ( 42 ) A 2 -0.136 0.127 -0.990 0.200 -0.840
43 THR ( 43 ) A 2 -0.979 -0.918 -0.707 -1.350 0.092
44 ASP ( 44 ) A 3 -0.948 0.142 -0.987 -0.741 -1.038
45 PHE ( 45 ) A 2 -1.437 -1.198 -1.323 -1.027 -0.727
46 CYS ( 46 ) A 3 -0.812 -0.612 0.116 -1.407 -0.510
47 GLY ( 47 ) A 3 -0.114 0.775 -1.519 0.000 0.000
48 SER ( 48 ) A 3 -0.445 -0.414 -0.478 -0.891 0.959
49 THR ( 49 ) A 3 -0.955 -0.973 -0.721 -0.402 -0.293
50 SER ( 50 ) A 3 0.226 0.530 0.013 -0.447 -0.473
51 ALA ( 51 ) A 3 -0.588 -0.200 -0.601 0.000 0.000
52 CYS ( 52 ) A 3 -0.917 -0.315 -1.203 -0.929 -1.630
53 GLY ( 53 ) A 3 -1.951 -1.309 -1.385 0.000 0.000
54 PRO ( 54 ) A 2 -1.022 -1.065 -0.158 -0.840 -0.670
55 LYS ( 55 ) A 2 -1.127 -1.110 0.275 -1.337 -0.884
56 PRO ( 56 ) A 2 -0.939 -0.873 -0.392 -0.740 -0.828
57 SER ( 57 ) A 2 -0.507 0.001 -0.549 -1.104 -1.616
58 CYS ( 58 ) A 2 -0.052 0.320 -0.700 -0.040 -0.786
59 SER ( 59 ) A 2 0.527 0.672 -0.371 0.742 0.499
60 GLY ( 60 ) A 2 -0.041 0.319 -0.785 0.000 0.000
61 LYS ( 61 ) A 2 -1.517 -0.568 -1.237 -1.632 -1.519
62 LEU ( 62 ) A 2 -1.603 -0.906 -1.524 -0.816 -2.016
63 TYR ( 63 ) A 2 -1.503 -1.159 -1.213 -0.209 -1.807
64 PHE ( 64 ) A 3 -0.588 0.200 -0.230 -0.224 -0.948
65 THR ( 65 ) A 3 -0.823 -0.611 -0.585 -1.144 -1.020
66 ALA ( 66 ) A 3 -0.629 -0.350 -0.494 0.000 0.000
67 ASP ( 67 ) A 3 0.106 1.952 -0.836 -0.155 -1.127
68 SER ( 68 ) A 3 0.132 0.664 -1.104 1.813 -1.211
69 GLN ( 69 ) A 3 -1.186 -0.023 -1.049 -0.291 -1.576
70 ARG ( 70 ) A 3 -0.330 0.553 -0.966 0.352 -0.740
71 PHE ( 71 ) A 3 -0.624 -0.298 -0.219 -1.034 -0.189
72 GLY ( 72 ) A 1 -0.451 -0.331 -0.499 0.000 0.000
73 CYS ( 73 ) A 3 -1.176 -0.564 -1.336 -1.169 -1.871
74 GLY ( 74 ) A 3 -1.769 -0.702 -2.046 0.000 0.000
75 LYS ( 75 ) A 3 -1.235 -0.721 -0.605 -1.058 -1.346
76 HIS ( 76 ) A 3 -1.375 -1.704 -0.115 -1.671 -0.428
77 LEU ( 77 ) A 3 -0.478 -0.392 0.513 0.062 -1.085
78 ASN ( 78 ) A 3 -1.115 -0.006 -0.774 -0.866 -1.168
79 LEU ( 79 ) A 3 -1.499 -0.022 -0.457 -1.418 -1.630
80 CYS ( 80 ) A 1 -1.330 -0.809 -1.950 -0.985 -1.843
81 ARG ( 81 ) A 3 -0.533 0.362 -0.081 -0.578 -0.675
82 GLY ( 82 ) A 3 0.698 1.576 -0.955 0.000 0.000
83 LYS ( 83 ) A 3 0.834 1.173 -1.060 2.046 -0.387
84 LYS ( 84 ) A 3 -0.088 0.898 -0.878 0.618 -0.941
85 CYS ( 85 ) A 3 -1.326 -0.684 -1.440 -0.851 -1.658
86 VAL ( 86 ) A 3 -0.883 -0.173 -1.048 0.027 -1.283
87 LYS ( 87 ) A 3 -0.494 -0.199 -0.658 0.342 -0.801
88 ALA ( 88 ) A 3 0.199 -0.441 0.752 0.000 0.000
89 LYS ( 89 ) A 3 -1.162 -0.721 -0.343 0.191 -1.790
90 VAL ( 90 ) A 3 -1.089 -0.493 -1.106 0.147 -1.535
91 TYR ( 91 ) A 3 -0.912 -0.890 0.388 -0.939 -0.396
92 ASP ( 92 ) A 3 -0.932 -1.008 0.495 -1.226 -0.512
93 ALA ( 93 ) A 3 -0.729 -0.638 -0.318 0.000 0.000
94 GLY ( 94 ) A 3 -0.304 0.400 -1.007 0.000 0.000
95 PRO ( 95 ) A 3 0.747 0.172 -0.057 1.413 0.347
96 ALA ( 96 ) A 3 -0.193 -0.432 0.200 0.000 0.000
97 GLU ( 97 ) A 3 -1.158 0.159 -0.582 0.352 -1.537
98 TRP ( 98 ) A 2 -2.170 -1.563 -1.816 -0.651 -2.473
99 VAL ( 99 ) A 3 0.800 0.541 0.927 -0.058 0.683
100 GLU ( 100 ) A 1 -1.173 -1.245 -0.574 -0.523 -0.532
101 LYS ( 101 ) A 3 -0.995 -1.314 -0.573 -0.594 -0.092
102 ASP ( 102 ) A 3 -1.392 -0.862 -1.017 -0.857 -0.861
103 ALA ( 103 ) A 3 -1.450 -1.455 -0.619 0.000 0.000
104 GLY ( 104 ) A 3 -0.787 -1.457 0.659 0.000 0.000
105 LYS ( 105 ) A 3 -1.826 -1.458 -1.182 -1.146 -1.023
106 MET ( 106 ) A 3 -1.109 -0.306 -1.089 -0.553 -0.744
107 ILE ( 107 ) A 3 -1.488 -0.125 -1.729 0.116 -1.793
108 ILE ( 108 ) A 3 -1.145 -0.507 -0.887 -0.650 -1.015
109 ASP ( 109 ) A 3 -1.614 -0.900 -1.049 -0.486 -1.482
110 ALA ( 110 ) A 3 -1.051 -1.000 -0.337 0.000 0.000
111 SER ( 111 ) A 3 -1.745 -1.607 -1.218 -0.475 -0.669
112 PRO ( 112 ) A 3 -0.678 -0.218 -1.001 0.192 -0.764
113 THR ( 113 ) A 1 -1.316 -1.636 -0.089 -1.419 0.413
114 ILE ( 114 ) A 3 -0.339 0.378 0.730 -0.705 -1.158
115 CYS ( 115 ) A 2 -1.343 -1.226 -0.315 -1.363 -1.367
116 HIS ( 116 ) A 2 -1.524 -0.920 -1.043 -1.499 -1.126
117 GLU ( 117 ) A 2 -1.509 -1.307 -0.449 -1.171 -1.246
118 LEU ( 118 ) A 2 -1.864 -2.017 -0.089 -1.323 -1.380
119 THR ( 119 ) A 3 -0.494 0.327 -1.305 0.415 -1.210
120 GLY ( 120 ) A 3 -0.507 0.139 -1.067 0.000 0.000
121 GLY ( 121 ) A 3 -0.253 -0.449 0.326 0.000 0.000
122 SER ( 122 ) A 3 -1.040 -1.070 -0.770 -1.242 0.116
123 SER ( 123 ) A 3 -0.708 -1.006 0.070 -0.200 -0.338
124 CYS ( 124 ) A 3 -1.100 -0.651 -1.065 -1.240 -1.191
125 GLY ( 125 ) A 3 -0.620 -0.649 -0.145 0.000 0.000
126 TRP ( 126 ) A 2 -2.679 -1.705 -2.216 -2.166 -2.574
127 SER ( 127 ) A 3 -1.635 -0.986 -1.431 -0.826 -1.098
128 ASP ( 128 ) A 3 -1.300 -0.474 -0.734 -0.889 -0.866
129 LYS ( 129 ) A 3 -0.498 -0.460 -0.926 0.320 -0.224
130 PHE ( 130 ) A 2 -2.109 -1.272 -2.107 -1.258 -2.090
131 GLU ( 131 ) A 2 -0.765 0.298 -1.150 -1.338 -0.704
132 ILE ( 132 ) A 2 -1.512 -0.406 -1.313 -1.701 -1.503
133 THR ( 133 ) A 2 -0.151 0.415 -0.943 -0.178 -1.336
134 ALA ( 134 ) A 2 -0.231 0.570 -1.509 0.000 0.000
135 THR ( 135 ) A 2 0.492 1.378 -0.272 -1.036 0.019
136 VAL ( 136 ) A 2 0.250 0.879 0.926 -1.575 0.019
137 THR ( 137 ) A 2 -0.706 -0.047 -0.607 -1.492 -1.549
138 SER ( 138 ) A 2 -0.367 0.131 -1.188 -0.131 -0.856
139 LEU ( 139 ) A 2 -1.695 -0.617 -1.407 -1.885 -1.287
140 THR ( 140 ) A 3 -0.737 -0.526 -0.652 -0.426 -0.776
141 ASP ( 141 ) A 3 -0.554 -0.572 -0.451 -0.445 0.082
142 SER ( 142 ) A 3 -0.999 -0.718 -0.792 -0.826 -0.602
143 ARG ( 143 ) A 3 0.525 -0.305 0.452 -0.135 1.258
144 PRO ( 144 ) A 3 -0.125 0.048 0.069 0.240 -0.662
145 LEU ( 145 ) A 3 -1.630 -0.585 -0.699 -1.066 -1.463
146 GLY ( 146 ) A 3 -1.743 -0.934 -1.546 0.000 0.000
147 PRO ( 147 ) A 3 -0.148 -0.408 1.061 -0.856 -0.203
148 PHE ( 148 ) A 3 -0.696 -0.563 -0.093 -0.039 -0.707
149 ASN ( 149 ) A 3 -0.154 -0.394 0.158 -0.919 -0.181
150 VAL ( 150 ) A 3 -1.311 -0.821 -1.327 -0.825 -0.906
151 THR ( 151 ) A 3 -0.921 -1.050 -0.415 -0.903 -0.008
152 GLU ( 152 ) A 3 -1.594 -1.098 -0.779 -0.868 -1.069
153 GLU ( 153 ) A 3 0.476 -0.599 0.663 -1.094 1.067
154 GLU ( 154 ) A 3 -0.877 -0.240 -0.599 -1.133 -0.753
155 MET ( 155 ) A 3 -1.852 -1.039 -1.555 -0.589 -1.676
156 ASP ( 156 ) A 3 -1.528 -1.251 -0.849 -0.796 -0.780
157 GLN ( 157 ) A 3 -0.301 -0.368 0.001 1.535 -1.617
158 LEU ( 158 ) A 3 -0.404 -0.268 -0.119 0.201 -0.641
159 PHE ( 159 ) A 3 0.690 0.599 1.289 0.358 -0.294
160 ILE ( 160 ) A 2 -1.162 -0.542 -0.848 -1.437 -1.160
161 ASP ( 161 ) A 2 -0.809 -0.362 -1.089 -0.399 -1.030
162 HIS ( 162 ) A 2 -0.539 -0.125 -1.224 0.173 -0.808
163 GLU ( 163 ) A 2 -1.792 -0.975 -1.927 -0.939 -1.574
164 ILE ( 164 ) A 2 -1.303 -0.697 -1.016 -1.314 -0.353
165 ALA ( 165 ) A 2 -1.360 -1.603 -0.313 0.000 0.000
166 MET ( 166 ) A 2 -2.404 -1.604 -1.511 -1.737 -2.226
167 ALA ( 167 ) A 3 -1.958 -0.932 -1.572 0.000 0.000
168 GLN ( 168 ) A 3 -0.925 -0.636 -0.734 -0.900 -1.186
169 CYS ( 169 ) A 3 -1.219 -1.115 -1.101 -0.959 -0.923
170 GLU ( 170 ) A 3 0.974 -0.711 1.348 -0.211 1.537
171 ALA ( 171 ) A 2 -1.940 -2.104 -0.656 0.000 0.000
172 GLU ( 172 ) A 2 -1.820 -1.073 -1.074 -1.168 -1.060
173 LYS ( 173 ) A 2 -0.521 -0.619 -0.606 -0.131 0.014
174 THR ( 174 ) A 3 -0.822 -0.623 -0.562 -0.581 -1.076
175 CYS ( 175 ) A 2 -1.563 -1.047 -0.782 -1.737 -9.554
176 ASN ( 176 ) A 3 -0.260 -0.066 -0.819 0.044 -0.646
177 GLY ( 177 ) A 3 -1.364 -0.998 -0.814 0.000 0.000
178 PHE ( 178 ) A 2 -2.931 -2.368 -2.059 -1.847 -2.410
179 ASP ( 179 ) A 3 -1.430 -0.859 -1.071 -0.887 -0.866
180 LEU ( 180 ) A 3 -1.883 -1.438 -0.927 -1.576 -0.638
181 GLU ( 181 ) A 3 -0.734 -0.612 -0.464 -1.148 -0.790
All contacts : Average = -0.925 Z-score = -5.98
BB-BB contacts : Average = -0.504 Z-score = -3.33
BB-SC contacts : Average = -0.692 Z-score = -5.30
SC-BB contacts : Average = -0.680 Z-score = -4.04
SC-SC contacts : Average = -0.981 Z-score = -5.63
If an individual residue has a quality control value of -2.5 or worse, you should take a look at it. It can mean that the residue:
is involved in symmetry contacts, or
is binding a co-factor, ligand or ion, or
is an active site residue, or
is wrong.
Average protein values ("Z-score for all contacts") can be read as follows:
-5.0 Guaranteed wrong structure. Bad structure or poor model
-3.0 Probably bad structure or unrefined model. Doubtful structure or model
-2.0 Structure OK or good model. Good structures
0.0 Good structures.
2.0 Good structures. Unusually Good structures
4.0 Probably a strange model of a perfect helix