Residue-by-residue listing for analyzed_20 Page 1
----------------------------------------
This listing highlights the residues in the structure which may need investigation.
The ideal values and standard deviations against which the structure has been compared are shown in the following table:
<------------------------------- I D E A L V A L U E S ------------------------------->
Chi-1 dihedral Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality
g(-) trans g(+) Chi-2 phi helix psi rt-hand lf-hand bond dihedral en. C-alpha
------------------------------------------------------------------------------------------
Ideal value 64.1 183.6 -66.7 177.4 -65.4 -65.3 -39.4 96.8 -85.8 2.0 180.0 -2.0 33.9
Standard deviation 15.7 16.8 15.0 18.5 11.2 11.9 11.3 14.8 10.7 .1 5.8 .8 3.5
------------------------------------------------------------------------------------------
In the listing below, properties that deviate from these values are highlighted by asterisks and plus-signs. Each asterisk
represents one standard deviation, and each plus-sign represents half a standard deviation. So, a highlight such as +***, indicates
that the value of the parameter is between 3.5 and 4.0 standard deviations from the ideal value shown above.
Where the deviation is greater than 4.5 standard deviations its numerical value is shown; for example, *5.5*.
The final column gives the maximum deviation in each row, while the maximum column deviations are shown at the end of the listing.
Also at the end are the keys to the codes used for the secondary structure and Ramachandran plot assignments.
Full print-out.
...................................................................................................................................
Residue Kabsch Region
--------- Sander of
No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max
Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev
-----------------------------------------------------------------------------------------------------------------------------------
1 GLY 1 - - - - - - - - - - - 180.1 - - 1
* *
2 HIS 2 XX - 238.5 - - - - - - - - 180.0 - 34.4 -
**** *** ****
3 HIS 3 b 54.5 - - - - - - - - - 180.0 - 34.5 -
4 HIS 4 b - - -111.7 - - - - - - - 180.0 - 34.4 1
*** * ***
5 HIS 5 B 59.2 - - - - - - - - - 180.0 - 34.5 -
6 HIS 6 b - 237.0 - - - - - - - - 180.0 - 34.5 -
*** ***
7 HIS 7 B 58.9 - - - - - - - - - 180.0 - 34.4 -
8 LEU 8 b 41.4 - - - - - - - - - 179.9 - 34.5 -
* *
9 GLU 9 b 45.2 - - 131.9 - - - - - - 180.1 - 34.5 -
* ** **
10 CYS 10 S b - 227.9 - - - - - - - - 180.2 - 34.4 -
+** +**
11 SER 11 b - - -105.9 - - - - - - - 180.2 - 34.4 -
+** +**
12 SER 12 A - - -72.4 - - - - - - - 180.0 - 34.5 -
13 ASP 13 ~p - - -46.1 - - - - - - - 180.2 - 34.4 -
** * **
14 SER 14 S A - 184.1 - - - - - - - - 180.0 - 34.5 -
15 LEU 15 S B - - -100.8 - - - - - - - 180.0 - 34.5 -
** **
16 GLN 16 S ~p - - -58.1 - - - - - - - 180.0 - 34.4 -
** **
17 LEU 17 B - - -61.1 - - - - - - - 179.9 - 34.5 -
Residue-by-residue listing for analyzed_20 Page 2
----------------------------------------
...................................................................................................................................
Residue Kabsch Region
--------- Sander of
No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max
Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev
-----------------------------------------------------------------------------------------------------------------------------------
18 HIS 18 E B - - -51.0 - - - - - - - 180.1 -1.7 34.4 -
* *
19 ASN 19 E B - - -28.5 - - - - - - - 179.9 - 34.5 -
+** +**
20 VAL 20 E B - 185.9 - - - - - - - - 180.0 -1.7 34.3 -
21 PHE 21 E B - 176.4 - - - - - - - - 179.9 -2.8 34.5 -
22 VAL 22 E B - - -62.3 - - - - - - - 180.1 -2.7 34.4 -
23 TYR 23 S ~a 51.0 - - - - - - - - - 180.0 - 34.5 -
** **
24 GLY 24 t - - - - - - - - - - - 180.3 - - -
25 SER 25 T A 53.7 - - - - - - - - - 180.1 - 34.5 -
26 PHE 26 T a - - -51.6 - - - - - - - 180.0 - 34.5 -
* *
27 GLN 27 t A 52.9 - - 161.6 - - - - - - 180.0 -.6 34.4 -
+* +*
28 ASP 28 h B - 199.5 - - - - - - - - 180.0 - 34.4 -
29 PRO 29 H - - - - - -69.8 -69.8 -23.1 - - - 179.9 - 38.6 -
* * *
30 ASP 30 H A - 180.0 - - - -54.8 -48.7 - - - 180.0 - 34.4 -
31 VAL 31 H A 73.7 - - - - -69.0 -28.7 - - - 179.9 - 34.3 -
32 ILE 32 H A - - -71.9 - - -65.8 -44.1 - - - 179.9 -.8 34.3 -
+* +*
33 ASN 33 H A - - -97.4 - - -53.9 -40.3 - - - 179.9 -2.3 34.5 -
** **
34 VAL 34 H A - 181.5 - - - -81.6 -31.4 - - - 179.9 -1.0 34.3 -
* * *
35 MET 35 H A - 230.6 - - - -58.0 -35.6 - - - 180.0 -2.1 34.5 -
+** +**
36 LEU 36 h a 29.7 - - 138.1 - - - - - - 179.8 -1.9 34.5 -
** ** **
37 ASP 37 t ~b - 238.1 - - - - - - - - 180.1 -.6 34.4 -
** *** +* ***
38 ARG 38 B - - -114.6 207.1 - - - - - - 180.1 - 34.5 -
*** +* ***
39 THR 39 B - - -54.7 - - - - - - - 180.0 - 34.4 -
40 PRO 40 - - - - - -69.8 - - - - - 180.0 - 38.6 -
* *
41 GLU 41 e B - - -116.5 177.6 - - - - - - 180.0 - 34.5 -
*** ***
42 ILE 42 E B - - -47.9 - - - - - - - 179.8 - 34.3 -
* *
43 VAL 43 E B 68.1 - - - - - - - - - 180.1 -2.9 34.4 -
* *
44 SER 44 e B - - -70.3 - - - - - - - 179.9 - 34.5 -
45 ALA 45 E B - - - - - - - - - - 180.1 - 34.1 -
46 THR 46 E B - - -61.3 - - - - - - - 180.0 -1.6 34.3 -
47 LEU 47 E b - 166.1 - - - - - - - - 179.9 -3.4 34.5 -
* +* +*
48 PRO 48 E - - - - - -69.8 - - - - - 180.0 - 38.7 -
* *
49 GLY 49 E - - - - - - - - - - - 180.1 -2.4 - -
50 PHE 50 E B - - -73.8 - - - - - - - 180.1 -.9 34.5 -
+* +*
51 GLN 51 E B - 197.3 - 129.7 - - - - - - 180.1 -2.9 34.4 -
+** * +**
52 ARG 52 E B - 163.4 - - - - - - - - 180.1 - 34.5 -
* *
Residue-by-residue listing for analyzed_20 Page 3
----------------------------------------
...................................................................................................................................
Residue Kabsch Region
--------- Sander of
No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max
Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev
-----------------------------------------------------------------------------------------------------------------------------------
53 PHE 53 e B - - -80.6 - - - - - - - 180.1 -.9 34.4 -
* *
54 ARG 54 B 62.0 - - - - - - - - - 180.0 - 34.4 -
55 LEU 55 b - 224.0 - 186.3 - - - - - - 179.8 - 34.5 -
** **
56 LYS 56 S a - - -68.2 - - - - - - - 179.9 - 34.5 -
57 GLY 57 S - - - - - - - - - - - 180.2 - - -
58 ARG 58 S a 64.9 - - - - - - - - - 180.1 - 34.4 -
59 LEU 59 S B - 171.7 - - - - - - - - 180.0 - 34.5 -
60 TYR 60 B - - -39.5 - - - - - - - 180.0 - 34.5 -
+* +*
61 PRO 61 - - - - - -69.7 - - - - - 180.0 - 38.6 -
* *
62 CYS 62 e B 45.6 - - - - - - - - - 180.1 - 34.4 -
* *
63 ILE 63 E B - - -53.5 - - - - - - - 179.9 - 34.3 -
64 VAL 64 E B - - -55.5 - - - - - - - 180.0 -1.7 34.4 -
65 PRO 65 E - - - - - -69.7 - - - - - 180.1 - 38.6 -
* *
66 SER 66 E B - 182.3 - - - - - - - - 180.0 -1.8 34.5 -
67 GLU 67 E A - 218.2 - 165.8 - - - - - - 180.0 - 34.4 -
** **
68 LYS 68 E a - - -77.8 - - - - - - - 180.0 - 34.5 -
69 GLY 69 E - - - - - - - - - - - 180.1 - - -
70 GLU 70 E B 56.8 - - - - - - - - - 180.0 - 34.5 -
71 VAL 71 E B - 175.8 - - - - - - - - 180.0 -2.2 34.4 -
72 HIS 72 E B - - -64.7 - - - - - - - 180.1 -.5 34.5 -
+* +*
73 GLY 73 e - - - - - - - - - - - 180.0 -1.4 - -
74 LYS 74 E B - - -115.3 - - - - - - - 179.9 -.9 34.5 -
*** +* ***
75 VAL 75 E B - 157.0 - - - - - - - - 180.0 -3.3 34.3 -
+* +* +*
76 LEU 76 E B - - -78.0 137.8 - - - - - - 179.9 -3.4 34.5 -
** +* **
77 MET 77 E B 45.2 - - 173.9 - - - - - - 180.1 -2.0 34.5 -
* *
78 GLY 78 E - - - - - - - - - - - 180.1 - - -
79 VAL 79 E B 75.0 - - - - - - - - - 180.0 -1.4 34.3 -
80 THR 80 h B 64.7 - - - - - - - - - 180.1 - 34.4 -
81 SER 81 H A 89.9 - - - - -62.2 -27.2 - - - 180.0 - 34.4 -
+* * +*
82 ASP 82 H A - - -58.4 - - -72.4 -48.6 - - - 180.1 - 34.4 -
83 GLU 83 H A - - -89.5 - - -57.8 -36.3 - - - 180.0 - 34.4 1
+* * +*
84 LEU 84 H A - 179.4 - - - -52.6 -41.8 - - - 179.9 -1.7 34.5 -
* *
85 GLU 85 H A - - -98.8 209.0 - -73.8 -29.7 - - - 180.1 -.9 34.5 -
** +* +* **
86 ASN 86 H A 115.0 - - - - -75.2 -32.1 - - - 180.0 -1.3 34.5 -
*** * ***
87 LEU 87 H A - - -70.3 167.3 - -72.0 -46.5 - - - 179.8 -2.7 34.5 -
88 ASP 88 H A - 171.8 - - - -71.9 -27.8 - - - 180.0 -1.8 34.4 -
* *
89 ALA 89 H A - - - - - -76.4 -48.2 - - - 180.0 -1.4 34.0 -
90 VAL 90 H A - 165.1 - - - -57.0 -56.2 - - - 180.0 -2.4 34.3 -
* * *
Residue-by-residue listing for analyzed_20 Page 4
----------------------------------------
...................................................................................................................................
Residue Kabsch Region
--------- Sander of
No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max
Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev
-----------------------------------------------------------------------------------------------------------------------------------
91 GLU 91 H A - - -117.4 - - -77.1 -22.7 - - - 180.0 -1.8 34.5 -
*** * ***
92 GLY 92 H - - - - - - -58.4 -15.6 - - - 180.1 -.7 - -
** +* **
93 ASN 93 h A - 204.2 - - - - - - - - 180.0 -.9 34.4 -
* +* +*
94 GLU 94 T a - - -75.0 205.3 - - - - - - 180.1 -2.2 34.5 -
+* +*
95 TYR 95 t B - - -67.4 - - - - - - - 180.1 -.7 34.5 -
+* +*
96 GLU 96 E B 76.0 - - 177.7 - - - - - - 180.1 -.9 34.4 -
+* +*
97 ARG 97 E B - 197.9 - 203.8 - - - - - - 180.0 - 34.5 -
* *
98 VAL 98 E B - - -78.2 - - - - - - - 180.0 -1.8 34.4 -
99 THR 99 E B 33.3 - - - - - - - - - 179.9 - 34.4 -
+* +*
100 VAL 100 E B - - -66.5 - - - - - - - 180.0 -2.2 34.4 1
* *
101 GLY 101 E - - - - - - - - - - - 180.0 - - -
102 ILE 102 E B 56.9 - - - - - - - - - 179.8 -3.0 34.3 1
* * *
103 VAL 103 E B - 176.5 - - - - - - - - 180.0 -1.7 34.3 -
104 ARG 104 E B - - -106.3 176.6 - - - - - - 180.1 -1.9 34.5 -
+** +**
105 GLU 105 e A - - -71.0 172.2 - - - - - - 180.0 -3.1 34.4 -
* *
106 ASP 106 S A - 175.0 - - - - - - - - 180.1 - 34.5 -
107 ASN 107 S a - 157.3 - - - - - - - - 180.2 - 34.5 -
+* +*
108 SER 108 S ~b - - -100.3 - - - - - - - 180.1 - 34.5 -
** ** **
109 GLU 109 e B 48.8 - - 179.7 - - - - - - 180.0 - 34.5 -
110 LYS 110 E B 61.4 - - 209.1 - - - - - - 179.9 - 34.5 -
+* +*
111 MET 111 E B - 171.4 - 147.0 - - - - - - 180.0 -3.5 34.5 -
+* +* +*
112 ALA 112 E B - - - - - - - - - - 180.0 - 34.1 -
113 VAL 113 E B - - -48.2 - - - - - - - 179.9 -1.6 34.3 -
* *
114 LYS 114 E B - - -43.9 200.6 - - - - - - 180.0 -1.9 34.5 -
+* * +*
115 THR 115 E B - 192.2 - - - - - - - - 180.1 -1.7 34.4 -
116 TYR 116 E B - - -58.4 - - - - - - - 179.9 -.6 34.5 -
+* +*
117 MET 117 E B 95.3 - - 196.8 - - - - - - 180.0 -1.1 34.4 -
+* * * +*
118 TRP 118 B - 208.5 - - - - - - - - 179.9 -2.9 34.4 -
* * *
119 ILE 119 S A - - -37.4 - - - - - - - 179.9 - 34.4 -
+* +*
120 ASN 120 S A - 162.8 - - - - - - - - 179.9 - 34.5 1
* * *
121 LYS 121 l 62.4 - - 176.1 - - - - - - 179.9 - 34.5 -
122 ALA 122 ~a - - - - - - - - - - 180.0 - 34.0 -
** **
Residue-by-residue listing for analyzed_20 Page 5
----------------------------------------
...................................................................................................................................
Residue Kabsch Region
--------- Sander of
No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max
Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev
-----------------------------------------------------------------------------------------------------------------------------------
123 ASP 123 t B - 217.4 - - - - - - - - 180.0 - 34.4 -
** **
124 PRO 124 T - - - - - -69.8 - - - - - 179.9 - 38.6 -
* *
125 ASP 125 T A - - -92.2 - - - - - - - 180.0 - 34.5 -
+* +*
126 MET 126 t B 54.4 - - - - - - - - - 180.0 -1.4 34.4 -
127 PHE 127 b 60.8 - - - - - - - - - 180.1 - 34.5 -
128 GLY 128 - - - - - - - - - - - 180.1 - - -
129 GLU 129 B 65.3 - - 188.6 - - - - - - 180.1 - 34.4 -
130 TRP 130 g B - 235.2 - - - - - - - - 180.1 - 34.5 -
*** ***
131 ASN 131 G A - - -79.0 - - - - - - - 180.0 - 34.5 -
132 PHE 132 G A - 238.6 - - - - - - - - 180.1 - 34.4 -
*** ***
133 GLU 133 G A - - -74.6 - - - - - - - 180.1 -1.7 34.4 -
134 GLU 134 h A - 190.1 - 187.0 - - - - - - 180.1 -1.9 34.4 -
135 TRP 135 H A - 172.4 - - - -53.5 -29.5 - - - 179.9 -1.9 34.4 -
136 LYS 136 H A - 192.7 - - - -52.2 -52.1 - - - 180.0 -1.5 34.5 -
* * *
137 ARG 137 H A 90.3 - - 184.8 - -69.4 -30.8 - - - 180.1 -1.0 34.4 -
+* * +*
138 LEU 138 H A - - -88.5 - - -68.9 -32.8 - - - 179.9 -1.5 34.5 -
* *
139 HIS 139 h A - 197.6 - - - - - - - - 180.0 -2.5 34.5 -
140 LYS 140 h A - 167.1 - 164.1 - - - - - - 179.9 -.9 34.5 -
* *
141 LYS 141 H A - - -119.9 217.2 - -48.3 -31.8 - - - 179.9 -1.5 34.5 -
+*** ** * +***
142 LYS 142 H A - 171.4 - - - -54.5 -49.1 - - - 180.0 -2.3 34.5 -
143 PHE 143 H A - - -46.1 - - -76.8 -38.6 - - - 180.0 -1.3 34.4 -
* *
144 ILE 144 H A - - -60.8 - - -52.9 -33.2 - - - 180.0 -2.4 34.3 -
* *
145 GLU 145 H A - - -91.9 198.3 - -51.6 -30.8 - - - 180.1 -1.9 34.5 1
+* * * * +*
146 THR 146 H A - - -61.3 - - -80.2 -47.2 - - - 180.0 -2.3 34.4 -
* *
147 PHE 147 H A - - -106.4 - - -64.8 -30.1 - - - 180.0 -1.2 34.5 -
+** * +**
148 LYS 148 H A - 225.0 - - - -53.3 -38.1 - - - 179.9 -3.2 34.5 -
** * +* **
149 LYS 149 H A - - -81.7 174.6 - -74.1 -29.0 - - - 179.9 -.9 34.5 -
* +* +*
150 ILE 150 H A - - -58.4 167.7 - -70.2 -44.6 - - - 179.8 -.8 34.4 -
+* +*
151 MET 151 H A 57.0 - - 174.5 - -67.0 -28.0 - - - 180.1 -2.5 34.4 -
* *
152 GLU 152 H A - - -110.0 - - -56.0 -31.5 - - - 180.0 -1.1 34.5 -
+** * +**
153 CYS 153 H A - - -68.5 - - -67.8 -32.8 - - - 180.1 -1.0 34.4 -
* *
154 LYS 154 H A - - -45.7 232.2 - -81.9 -25.5 - - - 179.9 -1.1 34.5 -
* +** * * * +**
155 LYS 155 h l - 217.3 - 198.1 - - - - - - 179.9 -1.7 34.5 -
** * **
156 LYS 156 B - 180.4 - - - - - - - - 179.9 - 34.5 -
Residue-by-residue listing for analyzed_20 Page 6
----------------------------------------
...................................................................................................................................
Residue Kabsch Region
--------- Sander of
No. Type Seq sec Ramch. Chi-1 dihedral Chi-2 Proline Phi Helix Chi-3 Chi-3 Disulph Omega H-bond Chirality Bad Max
Chain no. struc plot g(-) trans g(+) trans phi helix psi rt-hand lf-hand bond dihedral en. C-alpha contacts dev
-----------------------------------------------------------------------------------------------------------------------------------
157 PRO 157 - - - - - -69.7 - - - - - 180.0 - 38.6 -
* *
158 GLN 158 b 65.2 - - - - - - - - - 180.1 - 34.5 -
159 GLY 159 - - - - - - - - - - - 180.1 - - -
160 GLN 160 B - 172.2 - 161.5 - - - - - - 180.1 - 34.4 -
161 GLY 161 - - - - - - - - - - - 180.1 - - -
162 ASN 162 b - 213.2 - - - - - - - - 179.9 - 34.5 -
+* +*
163 ASP 163 b - 218.0 - - - - - - - - 180.0 - 34.4 -
** **
164 ASP 164 b - 205.3 - - - - - - - - 180.0 - 34.4 -
* *
165 ILE 165 b - 180.1 - 135.9 - - - - - - 180.1 - 34.3 -
** **
166 SER 166 B - 183.5 - - - - - - - - 179.9 - 34.4 -
167 HIS 167 B - - -83.5 - - - - - - - 180.0 -.5 34.4 -
* ** **
168 VAL 168 B - - -66.0 - - - - - - - 180.0 - 34.3 -
169 LEU 169 B - - -112.1 - - - - - - - 180.0 - 34.5 -
*** ***
170 ARG 170 b - 205.3 - 196.0 - - - - - - 180.1 - 34.4 -
* * *
171 GLU 171 b - 234.3 - 239.5 - - - - - - 180.0 - 34.4 -
*** *** ***
172 ASP 172 b - 219.8 - - - - - - - - 180.1 - 34.4 -
** **
173 GLN 173 - - 211.2 - - - - - - - - - - 34.4 -
+* +*
-----------------------------------------------------------------------------------------------------------------------------------
Max deviations: **** *** *** +*** *** * ** ** * * ****
-----------------------------------------------------------------------------------------------------------------------------------
Mean values: 61.7 195.3 -75.0 180.3 -69.8 -64.9 -35.7 - - - 180.0 -1.7 34.6
Standard deviations: 17.5 24.6 23.4 26.6 .0 10.0 9.4 - - - .1 .8 .9
Numbers of values: 33 54 63 38 7 37 37 0 0 0 172 79 161 7
KEY TO CODES:
------------
Regions of the Ramachandran plot Secondary structure (extended Kabsch/Sander)
-------------------------------- --------------------------------------------
A - Core alpha B - residue in isolated beta-bridge
a - Allowed alpha E - extended strand, participates in beta-ladder
~a - Generous alpha ** Generous G - 3-helix (3/10 helix)
B - Core beta H - 4-helix (alpha-helix)
b - Allowed beta I - 5-helix (pi-helix)
~b - Generous beta ** Generous S - bend
L - Core left-handed alpha T - hydrogen-bonded turn
l - Allowed left-handed alpha
~l - Generous left-handed alpha ** Generous e - extension of beta-strand
p - Allowed epsilon g - extension of 3/10 helix
~p - Generous epsilon ** Generous h - extension of alpha-helix
XX - Outside major areas **** Disallowed
Residue-by-residue listing for analyzed_20 Page 7
----------------------------------------
M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S
..................................... Small molecule data .........................................
<---------- Bond lengths ----------> <---------------------- Bond angles ---------------------->
C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N
---------------------------------------------------------------------------------------------------
Any - 1.231 - - - - - - - - - -
( .020)
Pro 1.341 - - - 1.466 122.60 116.90 - - 111.80 103.00 122.00
( .016) ( .015) ( 5.00) ( 1.50) ( 2.50) ( 1.10) ( 1.40)
Except Pro 1.329 - - - - - - - - - - 123.00
( .014) ( 1.60)
Gly - - 1.516 - 1.451 120.60 116.40 120.80 - 112.50 - -
( .018) ( .016) ( 1.70) ( 2.10) ( 2.10) ( 2.90)
Except Gly - - 1.525 - - - - 120.80 - - - -
( .021) ( 1.70)
Ala - - - 1.521 - - - - 110.50 - 110.40 -
( .033) ( 1.50) ( 1.50)
Ile,Thr,Val - - - 1.540 - - - - 109.10 - 111.50 -
( .027) ( 2.20) ( 1.70)
Except Gly,Pro - - - - 1.458 121.70 116.20 - - 111.20 - -
( .019) ( 1.80) ( 2.00) ( 2.80)
The rest - - - 1.530 - - - - 110.10 - 110.50 -
( .020) ( 1.90) ( 1.70)
Note. The table above shows the mean values obtained from small molecule data by Engh & Huber (1991). The values shown in brackets
are standard deviations
...................................................................................................................................
Residue
------------- <---------- Bond lengths ----------> <---------------------- Bond angles ---------------------->
No. Type Seq Max
Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev
-----------------------------------------------------------------------------------------------------------------------------------
1 GLY 1 - 1.231 1.516 - 1.451 - 116.39 120.65 - 112.51 - 122.95
2 HIS 2 1.329 1.232 1.525 1.529 1.458 121.63 116.26 120.81 109.96 110.91 110.32 122.93
3 HIS 3 1.329 1.232 1.525 1.529 1.458 121.63 116.24 120.88 109.92 110.85 110.32 122.88
4 HIS 4 1.330 1.231 1.526 1.529 1.459 121.64 116.21 120.81 109.98 110.87 110.31 122.98
5 HIS 5 1.329 1.231 1.526 1.530 1.459 121.57 116.19 120.85 109.95 110.82 110.30 122.96
6 HIS 6 1.329 1.232 1.526 1.529 1.459 121.60 116.21 120.88 109.92 110.84 110.29 122.90
7 HIS 7 1.329 1.232 1.525 1.529 1.459 121.67 116.26 120.83 109.96 110.90 110.33 122.92
8 LEU 8 1.328 1.230 1.525 1.530 1.458 121.67 116.22 120.76 109.90 110.95 110.29 123.01
9 GLU 9 1.330 1.231 1.526 1.530 1.459 121.56 116.18 120.86 109.89 110.87 110.34 122.96
10 CYS 10 1.329 1.231 1.525 1.529 1.458 121.64 116.22 120.82 109.97 110.87 110.32 122.96
11 SER 11 1.329 1.231 1.526 1.530 1.458 121.68 116.13 120.89 109.94 110.81 110.34 122.98
12 SER 12 1.329 1.230 1.526 1.530 1.459 121.61 116.14 120.85 109.93 110.83 110.29 123.00
13 ASP 13 1.328 1.230 1.525 1.529 1.458 121.62 116.19 120.84 110.00 110.86 110.35 122.98
14 SER 14 1.329 1.232 1.526 1.530 1.457 121.63 116.11 120.91 109.89 110.86 110.36 122.97
15 LEU 15 1.329 1.231 1.526 1.530 1.459 121.59 116.21 120.74 109.87 110.92 110.23 123.04
16 GLN 16 1.328 1.232 1.524 1.529 1.459 121.56 116.25 120.85 109.97 110.93 110.31 122.91
17 LEU 17 1.329 1.231 1.526 1.530 1.458 121.66 116.21 120.82 109.87 110.94 110.26 122.98
18 HIS 18 1.329 1.230 1.526 1.529 1.459 121.60 116.20 120.80 109.96 110.85 110.32 123.00
19 ASN 19 1.329 1.231 1.526 1.530 1.459 121.60 116.23 120.88 109.91 110.91 110.30 122.89
20 VAL 20 1.329 1.232 1.524 1.541 1.457 121.68 116.23 120.83 109.03 111.17 111.38 122.95
21 PHE 21 1.328 1.231 1.526 1.531 1.457 121.66 116.15 120.90 109.90 110.88 110.33 122.95
22 VAL 22 1.329 1.231 1.524 1.541 1.458 121.65 116.18 120.84 109.03 111.18 111.37 122.98
Residue-by-residue listing for analyzed_20 Page 8
----------------------------------------
...................................................................................................................................
Residue
------------- <---------- Bond lengths ----------> <---------------------- Bond angles ---------------------->
No. Type Seq Max
Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev
-----------------------------------------------------------------------------------------------------------------------------------
23 TYR 23 1.329 1.230 1.526 1.530 1.458 121.62 116.10 120.93 109.91 110.94 110.31 122.96
24 GLY 24 1.330 1.231 1.515 - 1.451 120.76 116.40 120.65 - 112.50 - 122.95
25 SER 25 1.329 1.231 1.526 1.530 1.457 121.64 116.11 120.90 109.91 110.86 110.32 122.99
26 PHE 26 1.329 1.231 1.526 1.531 1.458 121.60 116.15 120.85 109.90 110.88 110.32 123.00
27 GLN 27 1.329 1.231 1.525 1.530 1.458 121.60 116.18 120.81 109.99 110.92 110.31 123.02
28 ASP 28 1.328 1.231 1.526 1.529 1.459 121.60 116.21 121.57 110.00 110.85 110.33 122.22
29 PRO 29 1.341 1.231 1.525 1.531 1.466 122.69 116.24 120.78 110.43 112.36 103.39 122.98
30 ASP 30 1.328 1.232 1.525 1.529 1.459 121.67 116.22 120.86 109.99 110.81 110.37 122.92
31 VAL 31 1.329 1.231 1.525 1.541 1.458 121.62 116.14 120.85 109.04 111.15 111.37 123.01
32 ILE 32 1.329 1.230 1.525 1.541 1.457 121.56 116.18 120.87 109.03 111.15 111.42 122.95
33 ASN 33 1.329 1.231 1.526 1.530 1.459 121.64 116.22 120.80 109.91 110.85 110.30 122.98
34 VAL 34 1.329 1.230 1.524 1.540 1.458 121.65 116.19 120.83 109.05 111.12 111.39 122.99
35 MET 35 1.329 1.232 1.526 1.530 1.458 121.60 116.22 120.79 109.91 110.85 110.29 122.98
36 LEU 36 1.328 1.231 1.525 1.530 1.459 121.61 116.24 120.76 109.89 110.94 110.22 123.00
37 ASP 37 1.328 1.231 1.525 1.530 1.458 121.63 116.18 120.83 109.97 110.89 110.33 122.99
38 ARG 38 1.329 1.232 1.525 1.529 1.459 121.61 116.15 120.93 109.92 110.84 110.31 122.91
39 THR 39 1.331 1.231 1.525 1.539 1.457 121.60 116.21 121.60 109.01 111.10 111.40 122.19
40 PRO 40 1.341 1.231 1.525 1.531 1.466 122.69 116.24 120.70 110.42 112.35 103.40 123.06
41 GLU 41 1.329 1.232 1.525 1.531 1.458 121.57 116.18 120.85 109.86 110.92 110.35 122.96
42 ILE 42 1.329 1.231 1.525 1.540 1.457 121.62 116.19 120.89 109.05 111.10 111.44 122.92
43 VAL 43 1.329 1.231 1.524 1.541 1.457 121.65 116.20 120.82 109.02 111.17 111.36 122.98
44 SER 44 1.330 1.231 1.526 1.530 1.458 121.60 116.13 120.87 109.92 110.91 110.27 123.00
45 ALA 45 1.329 1.231 1.525 1.522 1.458 121.59 116.20 120.89 110.36 111.10 110.28 122.91
46 THR 46 1.330 1.232 1.524 1.541 1.457 121.63 116.23 120.76 109.03 111.18 111.38 123.01
47 LEU 47 1.328 1.231 1.525 1.529 1.459 121.60 116.19 121.62 109.94 110.90 110.22 122.19
48 PRO 48 1.341 1.230 1.524 1.531 1.466 122.70 116.23 120.85 110.42 112.36 103.38 122.92
49 GLY 49 1.329 1.231 1.516 - 1.451 120.79 116.35 120.70 - 112.50 - 122.95
50 PHE 50 1.329 1.231 1.526 1.531 1.458 121.61 116.15 120.82 109.89 110.88 110.30 123.03
51 GLN 51 1.329 1.231 1.524 1.530 1.458 121.61 116.20 120.80 109.94 110.94 110.30 122.99
52 ARG 52 1.329 1.231 1.526 1.529 1.458 121.62 116.22 120.82 109.88 110.91 110.34 122.96
53 PHE 53 1.329 1.231 1.526 1.530 1.459 121.64 116.14 120.86 109.94 110.88 110.32 123.00
54 ARG 54 1.330 1.231 1.525 1.529 1.458 121.60 116.21 120.85 109.96 110.84 110.33 122.94
55 LEU 55 1.329 1.231 1.525 1.530 1.458 121.67 116.21 120.89 109.94 110.94 110.23 122.90
56 LYS 56 1.329 1.231 1.525 1.531 1.458 121.68 116.24 120.80 109.88 110.89 110.28 122.96
57 GLY 57 1.330 1.230 1.515 - 1.451 120.73 116.35 120.61 - 112.50 - 123.04
58 ARG 58 1.329 1.231 1.526 1.530 1.459 121.61 116.15 120.86 109.93 110.89 110.30 122.99
59 LEU 59 1.329 1.232 1.525 1.530 1.459 121.58 116.22 120.81 109.92 110.89 110.26 122.97
60 TYR 60 1.328 1.231 1.526 1.530 1.458 121.62 116.15 121.65 109.92 110.96 110.30 122.20
61 PRO 61 1.341 1.232 1.525 1.531 1.465 122.69 116.28 120.76 110.45 112.35 103.40 122.96
62 CYS 62 1.328 1.232 1.525 1.530 1.459 121.67 116.17 120.77 109.96 110.90 110.30 123.06
63 ILE 63 1.328 1.231 1.525 1.540 1.457 121.57 116.21 120.82 109.01 111.14 111.49 122.97
64 VAL 64 1.329 1.231 1.524 1.541 1.458 121.65 116.16 121.61 109.05 111.16 111.35 122.23
65 PRO 65 1.341 1.231 1.525 1.531 1.466 122.69 116.21 120.77 110.44 112.33 103.43 123.02
66 SER 66 1.329 1.231 1.526 1.530 1.459 121.60 116.10 120.83 109.93 110.84 110.31 123.07
67 GLU 67 1.329 1.231 1.526 1.531 1.459 121.51 116.11 120.95 109.89 110.95 110.34 122.94
68 LYS 68 1.329 1.231 1.526 1.531 1.458 121.64 116.22 120.82 109.88 110.88 110.30 122.96
69 GLY 69 1.329 1.231 1.516 - 1.452 120.76 116.42 120.57 - 112.50 - 123.01
70 GLU 70 1.329 1.232 1.526 1.531 1.458 121.58 116.12 120.90 109.89 110.88 110.32 122.98
71 VAL 71 1.329 1.232 1.524 1.540 1.458 121.60 116.17 120.90 109.01 111.13 111.39 122.93
72 HIS 72 1.330 1.231 1.526 1.530 1.459 121.57 116.23 120.85 109.92 110.85 110.31 122.91
73 GLY 73 1.329 1.230 1.515 - 1.451 120.81 116.35 120.74 - 112.54 - 122.92
74 LYS 74 1.329 1.231 1.526 1.531 1.458 121.67 116.21 120.85 109.86 110.89 110.28 122.93
75 VAL 75 1.329 1.232 1.525 1.540 1.458 121.64 116.18 120.83 109.01 111.15 111.39 122.99
76 LEU 76 1.328 1.231 1.526 1.530 1.459 121.61 116.19 120.78 109.94 110.90 110.24 123.02
77 MET 77 1.329 1.230 1.526 1.530 1.458 121.57 116.20 120.84 109.90 110.86 110.35 122.95
Residue-by-residue listing for analyzed_20 Page 9
----------------------------------------
...................................................................................................................................
Residue
------------- <---------- Bond lengths ----------> <---------------------- Bond angles ---------------------->
No. Type Seq Max
Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev
-----------------------------------------------------------------------------------------------------------------------------------
78 GLY 78 1.330 1.230 1.516 - 1.451 120.71 116.32 120.72 - 112.53 - 122.96
79 VAL 79 1.330 1.232 1.525 1.540 1.458 121.60 116.19 120.88 109.06 111.10 111.38 122.92
80 THR 80 1.329 1.231 1.525 1.540 1.458 121.63 116.17 120.79 108.98 111.14 111.37 123.04
81 SER 81 1.329 1.232 1.526 1.530 1.459 121.61 116.17 120.87 109.94 110.87 110.34 122.97
82 ASP 82 1.328 1.231 1.526 1.529 1.459 121.69 116.22 120.76 110.02 110.82 110.35 123.02
83 GLU 83 1.329 1.232 1.526 1.530 1.458 121.58 116.13 120.90 109.94 110.92 110.35 122.97
84 LEU 84 1.329 1.231 1.525 1.530 1.459 121.59 116.22 120.75 109.95 110.93 110.23 123.03
85 GLU 85 1.329 1.230 1.525 1.530 1.458 121.55 116.15 120.86 109.90 110.90 110.34 122.99
86 ASN 86 1.329 1.232 1.526 1.530 1.458 121.59 116.18 120.85 109.89 110.87 110.30 122.97
87 LEU 87 1.328 1.231 1.526 1.530 1.459 121.63 116.22 120.80 109.91 110.91 110.25 122.99
88 ASP 88 1.328 1.231 1.525 1.530 1.458 121.65 116.25 120.83 109.97 110.85 110.33 122.93
89 ALA 89 1.329 1.231 1.525 1.521 1.458 121.66 116.22 120.84 110.39 111.08 110.30 122.94
90 VAL 90 1.329 1.230 1.524 1.540 1.458 121.63 116.16 120.83 109.05 111.13 111.37 123.01
91 GLU 91 1.330 1.230 1.526 1.531 1.458 121.51 116.16 120.95 109.90 110.92 110.32 122.90
92 GLY 92 1.330 1.230 1.516 - 1.452 120.75 116.37 120.60 - 112.48 - 123.02
93 ASN 93 1.328 1.230 1.526 1.529 1.458 121.63 116.15 120.81 109.93 110.87 110.34 123.04
94 GLU 94 1.330 1.231 1.526 1.530 1.458 121.55 116.13 120.87 109.88 110.90 110.33 123.01
95 TYR 95 1.329 1.230 1.526 1.530 1.458 121.57 116.09 120.83 109.89 110.91 110.32 123.08
96 GLU 96 1.330 1.231 1.526 1.530 1.458 121.52 116.16 120.87 109.88 110.86 110.38 122.98
97 ARG 97 1.329 1.231 1.526 1.530 1.458 121.62 116.15 120.90 109.87 110.87 110.32 122.94
98 VAL 98 1.330 1.232 1.524 1.541 1.458 121.60 116.21 120.90 109.03 111.13 111.35 122.89
99 THR 99 1.330 1.232 1.524 1.541 1.457 121.66 116.25 120.84 108.99 111.19 111.40 122.91
100 VAL 100 1.329 1.231 1.525 1.540 1.458 121.66 116.17 120.85 109.01 111.15 111.36 122.98
101 GLY 101 1.329 1.232 1.516 - 1.451 120.75 116.38 120.58 - 112.52 - 123.04
102 ILE 102 1.328 1.231 1.525 1.540 1.458 121.58 116.14 120.92 109.05 111.10 111.46 122.94
103 VAL 103 1.329 1.230 1.525 1.540 1.458 121.62 116.19 120.83 109.05 111.13 111.38 122.97
104 ARG 104 1.329 1.230 1.526 1.530 1.457 121.63 116.17 120.80 109.83 110.86 110.34 123.04
105 GLU 105 1.329 1.232 1.526 1.530 1.458 121.55 116.18 120.81 109.90 110.85 110.37 123.01
106 ASP 106 1.328 1.230 1.526 1.529 1.459 121.62 116.23 120.80 109.94 110.87 110.29 122.96
107 ASN 107 1.329 1.231 1.526 1.530 1.458 121.63 116.14 120.84 109.94 110.87 110.28 123.02
108 SER 108 1.329 1.230 1.526 1.530 1.459 121.61 116.10 120.85 109.90 110.88 110.31 123.04
109 GLU 109 1.330 1.231 1.526 1.530 1.458 121.53 116.13 120.96 109.92 110.85 110.32 122.91
110 LYS 110 1.329 1.231 1.525 1.530 1.458 121.68 116.27 120.78 109.87 110.91 110.28 122.95
111 MET 111 1.329 1.230 1.525 1.530 1.458 121.64 116.21 120.79 109.88 110.90 110.33 123.01
112 ALA 112 1.330 1.231 1.525 1.522 1.458 121.56 116.20 120.87 110.37 111.05 110.28 122.93
113 VAL 113 1.329 1.231 1.525 1.540 1.458 121.63 116.18 120.91 109.05 111.11 111.38 122.91
114 LYS 114 1.329 1.232 1.525 1.530 1.458 121.68 116.24 120.89 109.85 110.90 110.30 122.87
115 THR 115 1.330 1.231 1.524 1.540 1.457 121.63 116.20 120.84 108.99 111.11 111.42 122.96
116 TYR 116 1.328 1.231 1.525 1.530 1.458 121.62 116.14 120.87 109.91 110.97 110.29 122.99
117 MET 117 1.329 1.231 1.526 1.530 1.459 121.61 116.22 120.76 109.96 110.89 110.29 123.02
118 TRP 118 1.328 1.231 1.525 1.530 1.458 121.61 116.26 120.73 109.96 110.91 110.35 123.01
119 ILE 119 1.329 1.230 1.524 1.541 1.457 121.56 116.20 120.84 109.00 111.15 111.40 122.96
120 ASN 120 1.329 1.231 1.526 1.530 1.459 121.61 116.21 120.87 109.93 110.85 110.28 122.92
121 LYS 121 1.328 1.230 1.525 1.530 1.458 121.68 116.21 120.76 109.92 110.89 110.32 123.03
122 ALA 122 1.329 1.231 1.526 1.522 1.458 121.58 116.19 120.77 110.36 111.11 110.32 123.04
123 ASP 123 1.328 1.231 1.525 1.529 1.458 121.59 116.20 121.63 109.97 110.84 110.36 122.16
124 PRO 124 1.342 1.231 1.525 1.531 1.465 122.66 116.20 120.74 110.42 112.34 103.38 123.05
125 ASP 125 1.328 1.231 1.525 1.530 1.459 121.56 116.20 120.84 109.97 110.90 110.27 122.96
126 MET 126 1.329 1.232 1.525 1.530 1.458 121.60 116.23 120.84 109.94 110.86 110.31 122.93
127 PHE 127 1.329 1.230 1.526 1.531 1.458 121.64 116.14 120.93 109.89 110.87 110.31 122.94
128 GLY 128 1.330 1.231 1.515 - 1.451 120.76 116.42 120.60 - 112.52 - 122.97
129 GLU 129 1.329 1.230 1.526 1.530 1.457 121.60 116.17 120.86 109.88 110.88 110.37 122.97
130 TRP 130 1.328 1.230 1.524 1.530 1.458 121.61 116.24 120.78 109.92 110.93 110.31 122.98
131 ASN 131 1.329 1.231 1.526 1.530 1.459 121.58 116.16 120.89 109.92 110.90 110.26 122.96
132 PHE 132 1.329 1.229 1.526 1.530 1.458 121.62 116.10 120.86 109.92 110.89 110.34 123.04
Residue-by-residue listing for analyzed_20 Page 10
----------------------------------------
...................................................................................................................................
Residue
------------- <---------- Bond lengths ----------> <---------------------- Bond angles ---------------------->
No. Type Seq Max
Chain no. C-N C-O CA-C CA-CB N-CA C-N-CA CA-C-N CA-C-O CB-CA-C N-CA-C N-CA-CB O-C-N dev
-----------------------------------------------------------------------------------------------------------------------------------
133 GLU 133 1.329 1.231 1.526 1.529 1.459 121.53 116.16 120.79 109.90 110.87 110.33 123.05
134 GLU 134 1.330 1.231 1.526 1.530 1.459 121.53 116.16 120.87 109.91 110.89 110.33 122.97
135 TRP 135 1.328 1.231 1.525 1.530 1.459 121.60 116.22 120.86 109.96 110.91 110.29 122.91
136 LYS 136 1.329 1.231 1.525 1.531 1.458 121.63 116.24 120.75 109.91 110.91 110.24 123.01
137 ARG 137 1.329 1.232 1.526 1.529 1.457 121.64 116.18 120.86 109.93 110.85 110.35 122.96
138 LEU 138 1.328 1.232 1.526 1.530 1.459 121.63 116.19 120.80 109.91 110.86 110.26 123.01
139 HIS 139 1.329 1.230 1.526 1.530 1.459 121.57 116.19 120.83 109.93 110.87 110.30 122.98
140 LYS 140 1.328 1.231 1.526 1.531 1.458 121.69 116.22 120.88 109.87 110.87 110.34 122.90
141 LYS 141 1.329 1.231 1.526 1.530 1.458 121.71 116.21 120.82 109.87 110.90 110.30 122.97
142 LYS 142 1.329 1.232 1.525 1.530 1.458 121.63 116.27 120.79 109.88 110.90 110.23 122.94
143 PHE 143 1.329 1.232 1.526 1.530 1.459 121.64 116.15 120.80 109.93 110.87 110.32 123.05
144 ILE 144 1.328 1.231 1.525 1.539 1.458 121.59 116.16 120.79 109.03 111.13 111.47 123.05
145 GLU 145 1.330 1.232 1.525 1.530 1.458 121.52 116.18 120.94 109.94 110.90 110.30 122.88
146 THR 146 1.330 1.231 1.525 1.540 1.457 121.66 116.17 120.79 109.02 111.16 111.36 123.04
147 PHE 147 1.329 1.232 1.526 1.531 1.459 121.55 116.16 120.92 109.91 110.88 110.27 122.92
148 LYS 148 1.329 1.232 1.525 1.530 1.458 121.68 116.26 120.84 109.88 110.88 110.30 122.90
149 LYS 149 1.328 1.231 1.525 1.531 1.458 121.68 116.23 120.78 109.88 110.93 110.24 122.99
150 ILE 150 1.329 1.231 1.525 1.541 1.457 121.57 116.17 120.84 108.97 111.16 111.43 122.99
151 MET 151 1.329 1.230 1.526 1.530 1.458 121.59 116.20 120.78 109.91 110.89 110.37 123.02
152 GLU 152 1.329 1.232 1.526 1.530 1.458 121.55 116.16 120.82 109.87 110.91 110.35 123.02
153 CYS 153 1.328 1.232 1.526 1.529 1.458 121.63 116.17 120.86 109.96 110.88 110.32 122.97
154 LYS 154 1.328 1.232 1.525 1.530 1.459 121.67 116.25 120.83 109.91 110.86 110.31 122.92
155 LYS 155 1.329 1.232 1.525 1.530 1.458 121.66 116.28 120.82 109.90 110.91 110.30 122.90
156 LYS 156 1.329 1.232 1.525 1.531 1.458 121.73 116.21 121.54 109.93 110.91 110.24 122.24
157 PRO 157 1.341 1.231 1.524 1.530 1.467 122.67 116.23 120.76 110.46 112.36 103.38 123.02
158 GLN 158 1.330 1.231 1.525 1.530 1.458 121.57 116.21 120.84 109.93 110.92 110.29 122.96
159 GLY 159 1.330 1.231 1.517 - 1.452 120.70 116.35 120.56 - 112.46 - 123.09
160 GLN 160 1.329 1.231 1.525 1.530 1.458 121.55 116.21 120.82 109.94 110.91 110.32 122.97
161 GLY 161 1.330 1.230 1.516 - 1.451 120.71 116.37 120.61 - 112.46 - 123.02
162 ASN 162 1.329 1.231 1.526 1.530 1.458 121.57 116.17 120.84 109.91 110.86 110.30 122.99
163 ASP 163 1.329 1.232 1.526 1.529 1.458 121.61 116.17 120.77 109.99 110.84 110.33 123.06
164 ASP 164 1.328 1.231 1.526 1.529 1.459 121.58 116.18 120.77 109.96 110.83 110.34 123.06
165 ILE 165 1.328 1.231 1.525 1.539 1.458 121.57 116.20 120.83 109.03 111.14 111.46 122.97
166 SER 166 1.330 1.232 1.525 1.530 1.458 121.64 116.16 120.88 109.97 110.84 110.32 122.96
167 HIS 167 1.329 1.231 1.526 1.529 1.459 121.61 116.17 120.83 109.96 110.84 110.31 123.00
168 VAL 168 1.330 1.232 1.524 1.540 1.458 121.60 116.15 120.90 109.08 111.09 111.36 122.94
169 LEU 169 1.328 1.231 1.526 1.529 1.459 121.64 116.19 120.82 109.91 110.92 110.26 122.99
170 ARG 170 1.329 1.230 1.526 1.530 1.457 121.60 116.22 120.77 109.91 110.88 110.34 123.02
171 GLU 171 1.329 1.232 1.526 1.530 1.458 121.61 116.20 120.84 109.90 110.92 110.39 122.96
172 ASP 172 1.328 1.231 1.525 1.529 1.458 121.66 116.20 120.80 110.01 110.86 110.34 123.01
173 GLN 173 1.329 - 1.526 1.529 1.458 121.60 - - 109.95 110.91 110.36 -
-----------------------------------------------------------------------------------------------------------------------------------
Max deviations:
-----------------------------------------------------------------------------------------------------------------------------------
Residue-by-residue listing for analyzed_20 Page 11
----------------------------------------
A N A L Y S I S O F M A I N C H A I N B O N D L E N G T H S A N D B O N D A N G L E S
+------------------+
| BOND LENGTHS |
+------------------+
-------------------------------------------------------------------------------------------------------------
(Small molecule data) Number of Min Max Mean Standard
Bond X-PLOR labelling Mean St. dev values value value value deviation
-------------------------------------------------------------------------------------------------------------
C-N C-NH1 (except Pro) 1.329 .014 165 1.328 1.331 1.329 .001
C-N (Pro) 1.341 .016 7 1.341 1.342 1.341 .000
C-O C-O 1.231 .020 172 1.229 1.232 1.231 .001
CA-C CH1E-C (except Gly) 1.525 .021 161 1.524 1.526 1.525 .001
CH2G*-C (Gly) 1.516 .018 12 1.515 1.517 1.516 .000
CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.521 1.522 1.522 .000
CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.539 1.541 1.540 .000
CH1E-CH2E (the rest) 1.530 .020 128 1.529 1.531 1.530 .001
N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.457 1.459 1.458 .001
NH1-CH2G* (Gly) 1.451 .016 12 1.451 1.452 1.451 .000
N-CH1E (Pro) 1.466 .015 7 1.465 1.467 1.466 .000
-------------------------------------------------------------------------------------------------------------
+-----------------+
| BOND ANGLES |
+-----------------+
-------------------------------------------------------------------------------------------------------------
(Small molecule data) Number of Min Max Mean Standard
Angle X-PLOR labelling Mean St. dev values value value value deviation
-------------------------------------------------------------------------------------------------------------
CA-C-N CH1E-C-NH1 (except Gly,Pro)116.2 2.0 153 116.09 116.28 116.19 .04
CH2G*-C-NH1 (Gly) 116.4 2.1 12 116.32 116.42 116.37 .03
CH1E-C-N (Pro) 116.9 1.5 7 116.20 116.28 116.23 .02
O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 122.16 123.09 122.94 .16
O-C-N (Pro) 122.0 1.4 7 122.92 123.06 123.00 .05
C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 121.51 121.73 121.61 .04
C-NH1-CH2G* (Gly) 120.6 1.7 11 120.70 120.81 120.75 .03
C-N-CH1E (Pro) 122.6 5.0 7 122.66 122.70 122.68 .01
CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 120.70 121.65 120.87 .16
CH2G*-C-O (Gly) 120.8 2.1 12 120.56 120.74 120.63 .06
CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 110.36 110.39 110.37 .01
CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 108.97 109.08 109.03 .02
CH2E-CH1E-C (the rest) 110.1 1.9 128 109.83 110.46 109.95 .12
N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 110.81 111.19 110.94 .11
NH1-CH2G*-C (Gly) 112.5 2.9 12 112.46 112.54 112.50 .02
N-CH1E-C (Pro) 111.8 2.5 7 112.33 112.36 112.35 .01
N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 110.28 110.32 110.29 .02
NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 111.35 111.49 111.40 .04
N-CH1E-CH2E (Pro) 103.0 1.1 7 103.38 103.43 103.39 .02
NH1-CH1E-CH2E (the rest) 110.5 1.7 121 110.22 110.39 110.31 .04
-------------------------------------------------------------------------------------------------------------
The small molecule data used in the above analysis is from Engh & Huber (1991). The atom labelling follows that used in the
X-PLOR dictionary, with some additional atoms (marked with an asterisk) as defined by Engh & Huber.
Residue-by-residue listing for analyzed_20 Page 12
----------------------------------------
B A D C O N T A C T S L I S T I N G
.......................................................................
Residue Residue
----------- -----------
No. Type No. Type Contact Distance
Chain Atom Chain Atom type (Angstroms)
-----------------------------------------------------------------------
1. 1 GLY O --> 2 HIS O Main-Main 2.6
2. 4 HIS O --> 106 ASP OD2 Main-Side 2.6
3. 83 GLU O --> 86 ASN OD1 Main-Side 2.6
4. 100 VAL O --> 113 VAL O Main-Main 2.6
5. 102 ILE O --> 111 MET O Main-Main 2.6
6. 120 ASN O --> 121 LYS C Main-Main 2.6
7. 145 GLU OE2 --> 163 ASP O Side-Main 2.6
Residue-by-residue listing for analyzed_20 Page 13
----------------------------------------
R A M A C H A N D R A N P L O T S T A T I S T I C S
Residues in most favoured regions [A,B,L] 119 77.8%
Residues in additional allowed regions [a,b,l,p] 27 17.6%
Residues in generously allowed regions [~a,~b,~l,~p] 6 3.9%
Residues in disallowed regions [XX] 1 .7%
---- ------
Number of non-glycine and non-proline residues 153 100.0%
Number of end-residues (excl. Gly and Pro) 1
Number of glycine residues 12
Number of proline residues 7
----
Total number of residues 173
Based on the analysis of 118 structures of resolution of at least 2.0 Angstroms and R-factor no greater than 20%, a good
quality model would be expected to have over 90% in the most favoured regions [E,H,L].
S T E R E O C H E M I S T R Y O F M A I N - C H A I N
Comparison values No. of
No. of Parameter Typical Band band widths
Stereochemical parameter data pts value value width from mean
------------------------ -------- ----- ----- ----- ---------
a. %-tage residues in A, B, L 153 77.8 83.8 10.0 -.6 Inside
b. Omega angle st dev 172 .1 6.0 3.0 -2.0 BETTER
c. Bad contacts / 100 residues 7 4.0 4.2 10.0 .0 Inside
d. Zeta angle st dev 161 .9 3.1 1.6 -1.4 BETTER
e. H-bond energy st dev 79 .8 .8 .2 -.1 Inside
f. Overall G-factor 173 .1 -.4 .3 1.7 BETTER
S T E R E O C H E M I S T R Y O F S I D E - C H A I N
Comparison values No. of
No. of Parameter Typical Band band widths
Stereochemical parameter data pts value value width from mean
------------------------ -------- ----- ----- ----- ---------
a. Chi-1 gauche minus st dev 33 17.5 18.1 6.5 -.1 Inside
b. Chi-1 trans st dev 54 24.6 19.0 5.3 1.1 WORSE
c. Chi-1 gauche plus st dev 63 23.4 17.5 4.9 1.2 WORSE
d. Chi-1 pooled st dev 150 24.2 18.2 4.8 1.2 WORSE
e. Chi-2 trans st dev 38 26.6 20.4 5.0 1.2 WORSE
M O R R I S E T A L . C L A S S I F I C A T I O N
Mean St.dev Classification
Parameter m s 1 2 3 4 Value Class
--------- ---- --- ------------------------------------ ----- -----
Phi-psi distribution - - >75.0% >65.0% >55.0% <55.0% 77.8 1
Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 24.8 4
H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .84 2
Residue-by-residue listing for analyzed_20 Page 14
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G - F A C T O R S
Average
Parameter Score Score
--------- ----- -----
Dihedral angles:-
Phi-psi distribution -.75
Chi1-chi2 distribution -1.28
Chi1 only -.18
Chi3 & chi4 .16
Omega .74
------ -.26
=====
Main-chain covalent forces:-
Main-chain bond lengths .71
Main-chain bond angles .70
------ .70
=====
OVERALL AVERAGE .11
=====
Ideally, scores should be above -0.5. Values below -1.0 may need investigation.