Residue-by-residue listing for refined_9 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 - - - - - - - - - - - 181.4 - - -
2 HIS 2 b - 185.3 - - - - - - - - 174.6 - 32.1 -
3 HIS 3 b - - -69.4 - - - - - - - 177.0 -2.1 33.0 -
4 HIS 4 b - - -66.9 - - - - - - - 183.5 - 31.1 -
5 HIS 5 B 55.7 - - - - - - - - - 179.6 -.7 31.9 -
+* +*
6 HIS 6 a 65.6 - - - - - - - - - 179.4 -.7 33.5 -
+* +*
7 HIS 7 b - 178.5 - - - - - - - - 180.5 - 34.4 -
8 LEU 8 B 53.3 - - - - - - - - - 177.6 - 30.4 -
9 GLU 9 B - - -62.1 178.2 - - - - - - 179.4 - 34.5 -
10 CYS 10 B - - -54.3 - - - - - - - 181.1 - 35.1 -
11 SER 11 b 50.6 - - - - - - - - - 180.9 - 31.7 -
12 SER 12 A - - -52.6 - - - - - - - 182.3 -2.4 35.8 -
13 ASP 13 l - 179.8 - - - - - - - - 181.9 - 31.8 -
14 SER 14 b - - -57.6 - - - - - - - 173.2 - 34.8 -
* *
15 LEU 15 S A - 185.4 - - - - - - - - 175.9 - 34.6 -
16 GLN 16 S B 61.5 - - 179.7 - - - - - - 183.0 - 33.4 -
17 LEU 17 B - - -59.4 - - - - - - - 186.0 - 32.1 -
* *
18 HIS 18 E B - - -54.3 - - - - - - - 177.6 -3.2 36.3 -
+* +*
19 ASN 19 E B 52.0 - - - - - - - - - 183.7 - 30.4 -
20 VAL 20 E B - 182.1 - - - - - - - - 178.3 -2.2 35.0 -
21 PHE 21 E B - 178.4 - - - - - - - - 180.4 -3.2 35.1 -
+* +*
Residue-by-residue listing for refined_9 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
-----------------------------------------------------------------------------------------------------------------------------------
22 VAL 22 E B 65.3 - - - - - - - - - 177.3 -3.3 34.5 -
+* +*
23 TYR 23 S a 70.9 - - - - - - - - - 183.1 - 34.7 -
24 GLY 24 t - - - - - - - - - - - 185.5 - - -
25 SER 25 T A - - -50.8 - - - - - - - 184.8 - 35.8 -
* *
26 PHE 26 T a - - -62.1 - - - - - - - 177.9 - 33.7 -
27 GLN 27 t A - 175.8 - - - - - - - - 183.4 -1.5 36.8 -
28 ASP 28 h B - 182.6 - - - - - - - - 181.7 - 34.4 -
29 PRO 29 H - - - - - -65.2 -65.2 -24.7 - - - 178.9 - 38.4 -
* * *
30 ASP 30 H A - 171.3 - - - -70.5 -29.1 - - - 174.4 - 32.3 -
31 VAL 31 H A - 178.2 - - - -66.6 -39.4 - - - 177.8 -.8 35.0 -
+* +*
32 ILE 32 H A - - -68.0 - - -62.9 -45.0 - - - 177.1 -1.1 34.1 -
* *
33 ASN 33 H A - - -87.8 - - -53.2 -42.9 - - - 182.6 -2.3 34.2 -
* * *
34 VAL 34 H A 60.5 - - - - -81.6 -36.7 - - - 181.2 -1.5 31.1 -
* *
35 MET 35 H A - 191.4 - - - -65.2 -35.9 - - - 172.5 -2.6 31.6 -
* *
36 LEU 36 h a 53.8 - - 153.5 - - - - - - 185.5 -2.5 29.4 -
* * *
37 ASP 37 t ~b - 179.0 - - - - - - - - 182.5 -.6 35.8 -
** +* **
38 ARG 38 S B - - -63.1 - - - - - - - 174.8 - 36.2 -
39 THR 39 B - - -56.7 - - - - - - - 173.0 - 34.8 -
* *
40 PRO 40 - - - - - -67.9 - - - - - 177.8 - 39.0 -
* *
41 GLU 41 E B - 186.0 - 179.8 - - - - - - 186.2 -1.2 33.8 -
* * *
42 ILE 42 E B - - -54.1 178.5 - - - - - - 174.7 - 36.2 -
43 VAL 43 E B 60.3 - - - - - - - - - 176.5 -1.8 33.7 -
44 SER 44 E B - - -57.9 - - - - - - - 181.8 - 35.3 -
45 ALA 45 E B - - - - - - - - - - 177.8 -2.4 34.4 -
46 THR 46 E B - - -56.6 - - - - - - - 176.1 -3.2 36.0 -
* *
47 LEU 47 E b - 176.7 - - - - - - - - 180.0 -3.8 34.4 -
** **
48 PRO 48 E - - - - - -85.5 - - - - - 179.8 - 38.8 -
+* * +*
49 GLY 49 e - - - - - - - - - - - 179.3 -2.7 - -
50 PHE 50 t B - - -68.4 - - - - - - - 182.4 -.7 34.3 -
+* +*
51 GLN 51 E B - 190.4 - - - - - - - - 176.7 -2.6 35.2 -
52 ARG 52 E B 63.6 - - - - - - - - - 179.9 - 34.1 -
53 PHE 53 e B - - -70.6 - - - - - - - 190.0 -1.7 30.4 -
+* +*
54 ARG 54 B - 170.5 - - - - - - - - 169.3 -1.8 35.4 -
+* +*
55 LEU 55 t ~a - 207.8 - 186.0 - - - - - - 186.0 - 34.3 -
** * * **
56 LYS 56 B B - 188.8 - 174.2 - - - - - - 186.1 - 31.6 -
* *
Residue-by-residue listing for refined_9 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
-----------------------------------------------------------------------------------------------------------------------------------
57 GLY 57 T - - - - - - - - - - - 175.5 -.6 - -
+* +*
58 ARG 58 T a - 179.5 - - - - - - - - 180.1 -2.3 33.8 -
59 LEU 59 B B - 185.1 - - - - - - - - 187.3 -3.1 32.8 -
* * *
60 TYR 60 B - - -45.2 - - - - - - - 171.5 - 37.0 -
* * *
61 PRO 61 - - - - - -66.3 - - - - - 186.1 - 38.2 -
* * *
62 CYS 62 e B 51.3 - - - - - - - - - 180.4 -1.1 34.5 -
* *
63 ILE 63 E B - - -62.4 - - - - - - - 174.3 - 36.1 -
64 VAL 64 E B - - -61.5 - - - - - - - 178.3 -1.8 32.5 -
65 PRO 65 - - - - - -64.1 - - - - - 179.7 - 38.0 -
* *
66 SER 66 t B - 189.1 - - - - - - - - 188.6 -.6 35.1 -
* +* +*
67 GLU 67 T A - - -60.8 181.2 - - - - - - 182.6 - 33.4 -
68 LYS 68 T A - - -54.9 - - - - - - - 180.2 - 34.3 -
69 GLY 69 e - - - - - - - - - - - 176.8 -2.0 - -
70 GLU 70 E B 70.9 - - 183.3 - - - - - - 178.4 - 34.1 -
71 VAL 71 E B - 182.3 - - - - - - - - 177.4 -2.6 34.8 -
72 HIS 72 E B - - -63.9 - - - - - - - 181.8 - 33.5 -
73 GLY 73 E - - - - - - - - - - - 182.5 -3.0 - -
* *
74 LYS 74 E B - - -59.4 - - - - - - - 175.8 -3.2 35.1 -
+* +*
75 VAL 75 E B - 169.0 - - - - - - - - 178.2 -3.1 34.5 -
* *
76 LEU 76 E B - - -55.0 179.4 - - - - - - 178.8 -3.4 36.8 -
+* +*
77 MET 77 E B 52.9 - - 177.7 - - - - - - 186.8 -3.3 32.2 -
* +* +*
78 GLY 78 E - - - - - - - - - - - 179.4 -1.5 - -
79 VAL 79 E B 70.7 - - - - - - - - - 183.8 -1.8 33.8 -
80 THR 80 h B 68.4 - - - - - - - - - 176.5 - 34.1 -
81 SER 81 H A - - -56.0 - - -65.8 -26.8 - - - 180.8 - 34.5 -
* *
82 ASP 82 H A - 184.4 - - - -75.6 -41.8 - - - 173.2 - 32.0 -
* *
83 GLU 83 H A - - -63.4 - - -70.2 -28.1 - - - 177.8 - 32.9 -
84 LEU 84 H A - 183.1 - - - -58.9 -51.2 - - - 177.6 -1.7 34.2 -
* *
85 GLU 85 H A 59.4 - - 175.9 - -65.8 -30.9 - - - 177.6 -2.3 32.8 -
86 ASN 86 H A - 156.1 - - - -63.7 -49.8 - - - 181.2 -1.6 35.3 -
+* +*
87 LEU 87 H A - - -60.0 176.9 - -69.8 -34.2 - - - 177.5 -3.3 34.6 -
+* +*
88 ASP 88 H A - 181.9 - - - -63.3 -36.8 - - - 175.0 -2.3 34.6 -
89 ALA 89 H A - - - - - -77.0 -50.0 - - - 185.3 -1.8 35.6 -
90 VAL 90 H A - 170.8 - - - -63.2 -57.7 - - - 177.4 -3.8 31.8 -
+* ** **
91 GLU 91 h A - - -64.8 - - - - - - - 185.3 -2.5 33.3 -
92 GLY 92 T - - - - - - - - - - - 182.4 -1.0 - -
* *
93 ASN 93 T A - - -63.5 - - - - - - - 179.0 -.6 33.4 -
+* +*
Residue-by-residue listing for refined_9 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
-----------------------------------------------------------------------------------------------------------------------------------
94 GLU 94 e a - - -63.5 179.7 - - - - - - 179.8 -1.5 32.3 -
95 TYR 95 E B - - -69.6 - - - - - - - 177.4 -1.2 34.2 -
* *
96 GLU 96 E B - 180.8 - 173.7 - - - - - - 182.7 -2.8 34.2 -
* *
97 ARG 97 E B - 174.9 - 173.1 - - - - - - 182.6 - 33.8 -
98 VAL 98 E B - - -61.6 - - - - - - - 179.8 -2.8 33.4 -
* *
99 THR 99 E B - 180.7 - - - - - - - - 184.7 - 32.1 -
100 VAL 100 E B - - -63.5 - - - - - - - 177.9 -3.1 35.2 -
* *
101 GLY 101 E - - - - - - - - - - - 179.4 - - -
102 ILE 102 E B 56.3 - - - - - - - - - 180.9 -3.1 32.3 -
* *
103 VAL 103 E B - 176.9 - - - - - - - - 180.6 -3.2 34.9 -
+* +*
104 ARG 104 E B - - -62.9 183.9 - - - - - - 180.5 -1.8 32.8 -
105 GLU 105 e A - - -61.5 182.7 - - - - - - 177.0 -3.0 33.0 -
* *
106 ASP 106 S A - - -65.5 - - - - - - - 180.5 - 33.9 -
107 ASN 107 S b - - -61.8 - - - - - - - 181.1 - 36.6 -
108 SER 108 S a - - -59.2 - - - - - - - 185.1 - 36.3 -
109 GLU 109 e B 43.3 - - - - - - - - - 182.7 - 31.7 -
* *
110 LYS 110 E B 71.0 - - - - - - - - - 176.7 - 32.4 -
111 MET 111 E B - - -57.4 188.7 - - - - - - 181.2 -3.4 34.3 -
+* +*
112 ALA 112 E B - - - - - - - - - - 181.5 - 33.5 -
113 VAL 113 E B - - -59.5 - - - - - - - 175.2 -2.7 35.1 -
114 LYS 114 E B - - -70.3 - - - - - - - 176.5 -2.7 34.7 -
115 THR 115 E B - 192.4 - - - - - - - - 180.9 -2.6 33.4 -
116 TYR 116 E B - - -64.3 - - - - - - - 185.6 -.6 31.6 -
+* +*
117 MET 117 E B - 180.6 - 177.6 - - - - - - 179.4 -2.9 35.5 -
* *
118 TRP 118 E B - 188.7 - - - - - - - - 188.4 -3.2 35.0 -
* +* +*
119 ILE 119 e A - - -56.4 - - - - - - - 180.0 -.6 32.1 -
+* +*
120 ASN 120 t b - 179.2 - - - - - - - - 183.5 - 32.4 -
121 LYS 121 T A 57.9 - - 186.7 - - - - - - 178.1 -1.3 33.5 -
122 ALA 122 T a - - - - - - - - - - 178.4 - 35.1 -
123 ASP 123 t B - 181.5 - - - - - - - - 183.0 -1.3 33.7 -
124 PRO 124 S - - - - - -84.9 - - - - - 183.3 - 39.2 -
+* +* +*
125 ASP 125 S A - - -68.1 - - - - - - - 181.5 - 32.2 -
126 MET 126 S A 59.1 - - 180.8 - - - - - - 184.1 - 34.8 -
127 PHE 127 b - 183.8 - - - - - - - - 179.4 - 33.3 -
128 GLY 128 S - - - - - - - - - - - 180.2 -.7 - -
+* +*
129 GLU 129 B 58.3 - - 174.1 - - - - - - 179.6 - 31.7 -
130 TRP 130 t B - 197.7 - - - - - - - - 187.4 - 35.5 -
* *
131 ASN 131 h A - 179.9 - - - - - - - - 174.7 - 30.6 -
132 PHE 132 H A - - -74.8 - - -54.3 -30.0 - - - 182.1 - 31.1 -
133 GLU 133 H A 71.8 - - - - -61.6 -28.3 - - - 174.7 -2.8 30.1 -
* * *
Residue-by-residue listing for refined_9 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
-----------------------------------------------------------------------------------------------------------------------------------
134 GLU 134 H A - 182.3 - 180.1 - -61.0 -41.0 - - - 176.5 -1.5 33.5 -
135 TRP 135 H A - 179.0 - - - -73.5 -31.3 - - - 174.2 -.6 32.5 -
* +* +*
136 LYS 136 H A - 179.7 - - - -60.5 -37.2 - - - 176.8 -1.9 34.9 -
137 ARG 137 H A - 168.8 - 178.7 - -63.4 -51.0 - - - 178.9 -2.2 34.5 -
* *
138 LEU 138 H A - - -75.6 - - -72.0 -14.9 - - - 179.2 -1.9 31.4 -
** **
139 HIS 139 H A - 189.7 - - - -95.5 -28.9 - - - 180.6 -1.4 33.3 -
+** +**
140 LYS 140 H A 68.2 - - 183.1 - -62.1 -32.7 - - - 184.0 -2.3 32.8 -
141 LYS 141 H A - 191.6 - - - -48.9 -39.2 - - - 176.6 -1.0 33.4 -
* * *
142 LYS 142 H A - 175.9 - - - -57.5 -44.5 - - - 179.4 -1.0 34.5 -
* *
143 PHE 143 H A - - -57.5 - - -76.0 -35.5 - - - 180.3 -1.0 35.2 -
* *
144 ILE 144 H A - - -56.5 - - -61.0 -32.6 - - - 176.4 -3.0 31.4 -
* *
145 GLU 145 H A - - -63.9 185.9 - -55.1 -44.5 - - - 177.6 -2.0 32.5 -
146 THR 146 H A - 183.9 - - - -80.2 -36.7 - - - 178.5 -.7 30.6 -
* +* +*
147 PHE 147 H A - - -75.0 - - -66.9 -30.7 - - - 176.3 -2.8 29.3 -
* * *
148 LYS 148 H A - 182.2 - 180.3 - -62.1 -36.9 - - - 179.3 -3.4 35.7 -
+* +*
149 LYS 149 H A - 176.7 - 182.4 - -74.1 -37.9 - - - 177.5 -.8 35.9 -
+* +*
150 ILE 150 H A - - -60.7 174.8 - -67.0 -33.7 - - - 175.5 -2.0 32.8 -
151 MET 151 H A - - -64.5 - - -66.4 -30.5 - - - 175.7 -2.4 33.2 -
152 GLU 152 H A - - -60.1 - - -72.3 -30.5 - - - 175.9 -.9 33.6 -
* *
153 CYS 153 H A - - -57.8 - - -70.6 -31.6 - - - 175.8 -1.2 34.1 -
* *
154 LYS 154 H A - - -60.6 186.4 - -79.9 -19.8 - - - 182.4 -1.6 35.4 -
* +* +*
155 LYS 155 h l - 186.7 - 180.8 - - - - - - 180.5 -.8 31.2 -
+* +*
156 LYS 156 t B - - -63.4 177.2 - - - - - - 182.1 -2.1 34.1 -
157 PRO 157 - - - - - -79.6 - - - - - 176.4 - 39.3 -
* +* +*
158 GLN 158 b 53.0 - - 181.6 - - - - - - 184.6 - 31.5 -
159 GLY 159 - - - - - - - - - - - 173.4 -.7 - -
* +* +*
160 GLN 160 B - - -69.9 - - - - - - - 180.4 -1.2 33.9 -
* *
161 GLY 161 - - - - - - - - - - - 180.4 -.8 - -
+* +*
162 ASN 162 B 69.2 - - - - - - - - - 181.7 - 33.4 -
163 ASP 163 B - 179.5 - - - - - - - - 180.0 - 34.0 -
164 ASP 164 B 63.8 - - - - - - - - - 180.4 - 34.4 -
165 ILE 165 B 56.2 - - 176.9 - - - - - - 175.9 - 32.9 -
166 SER 166 B 46.9 - - - - - - - - - 186.1 - 32.8 -
* * *
167 HIS 167 B 63.9 - - - - - - - - - 177.4 - 35.1 -
168 VAL 168 B - - -58.9 - - - - - - - 177.1 - 34.1 -
169 LEU 169 B - 188.0 - - - - - - - - 181.9 - 34.5 -
Residue-by-residue listing for refined_9 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
-----------------------------------------------------------------------------------------------------------------------------------
170 ARG 170 B 62.7 - - 180.0 - - - - - - 183.1 -.5 31.9 -
** **
171 GLU 171 B - 181.6 - 181.6 - - - - - - 175.0 - 35.3 -
172 ASP 172 B - 177.2 - - - - - - - - 182.6 - 33.7 -
173 GLN 173 - - 204.7 - - - - - - - - - - 34.9 -
* *
-----------------------------------------------------------------------------------------------------------------------------------
Max deviations: ** * +* * * +* +** ** +* ** +* +**
-----------------------------------------------------------------------------------------------------------------------------------
Mean values: 60.3 182.0 -62.1 179.3 -73.4 -67.0 -36.0 - - - 179.8 -2.0 33.9
Standard deviations: 7.6 8.3 6.8 5.8 9.6 8.9 8.8 - - - 3.7 .9 1.9
Numbers of values: 33 56 61 37 7 40 40 0 0 0 172 99 161 0
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 refined_9 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 - 1.240 1.497 - 1.463 - 117.12 120.13 - 110.95 - 122.75
* *
2 HIS 2 1.322 1.232 1.519 1.542 1.443 120.62 114.78 121.31 111.25 110.90 112.56 123.69
* *
3 HIS 3 1.302 1.226 1.491 1.549 1.448 124.16 116.02 120.87 109.04 108.76 114.39 122.94
+* +* * ** **
4 HIS 4 1.288 1.228 1.485 1.533 1.428 121.31 114.52 121.98 112.80 109.57 112.98 123.44
+** +* +* * * +**
5 HIS 5 1.289 1.226 1.506 1.557 1.428 122.19 115.43 121.34 112.56 110.59 111.91 123.21
+** * +* * +**
6 HIS 6 1.303 1.217 1.512 1.563 1.444 121.62 115.27 120.50 111.28 109.10 111.39 124.22
+* +* +*
7 HIS 7 1.342 1.235 1.516 1.558 1.469 123.51 115.86 120.82 110.47 110.33 110.34 123.31
* * *
8 LEU 8 1.296 1.243 1.510 1.569 1.417 121.57 115.17 121.74 114.23 111.62 111.91 122.99
** +* ** ** **
9 GLU 9 1.289 1.240 1.482 1.530 1.426 122.20 116.19 120.10 110.20 107.85 111.42 123.67
+** ** +* * +**
10 CYS 10 1.297 1.239 1.520 1.527 1.428 121.67 116.74 120.18 110.88 108.47 109.34 123.03
** +* **
11 SER 11 1.321 1.234 1.522 1.534 1.434 121.51 114.60 121.93 113.06 111.37 111.03 123.35
* +* +*
Residue-by-residue listing for refined_9 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
-----------------------------------------------------------------------------------------------------------------------------------
12 SER 12 1.303 1.237 1.521 1.526 1.421 122.96 115.26 120.49 110.56 109.94 108.22 124.24
+* +* * +*
13 ASP 13 1.345 1.232 1.514 1.546 1.466 123.80 115.44 121.84 111.93 110.26 112.51 122.42
* * * *
14 SER 14 1.308 1.238 1.510 1.525 1.434 121.56 115.90 120.97 109.21 111.57 110.51 123.08
* * *
15 LEU 15 1.305 1.238 1.532 1.480 1.398 121.81 113.92 122.73 112.19 108.29 108.29 123.35
+* +** *** * * * * * ***
16 GLN 16 1.315 1.242 1.525 1.540 1.431 123.59 115.99 120.98 111.62 107.46 111.57 122.90
* * * * *
17 LEU 17 1.288 1.229 1.494 1.503 1.419 122.49 114.98 121.39 111.18 112.09 111.95 123.62
+** * * ** +**
18 HIS 18 1.290 1.246 1.507 1.532 1.437 122.86 115.96 120.47 108.64 109.21 109.65 123.53
+** * +**
19 ASN 19 1.303 1.238 1.526 1.538 1.438 121.97 115.67 121.36 112.89 112.09 112.57 122.94
+* * * * +*
20 VAL 20 1.320 1.218 1.538 1.568 1.456 122.58 116.62 120.35 108.92 110.36 111.04 123.02
* *
21 PHE 21 1.313 1.239 1.523 1.543 1.456 123.23 116.30 120.52 110.30 109.66 109.57 123.18
* *
22 VAL 22 1.314 1.233 1.536 1.567 1.443 122.31 116.84 120.63 109.62 109.42 111.47 122.51
* * *
23 TYR 23 1.315 1.232 1.536 1.540 1.451 121.25 116.53 120.89 109.90 110.13 110.34 122.58
24 GLY 24 1.324 1.219 1.504 - 1.437 119.80 115.92 120.50 - 113.29 - 123.54
25 SER 25 1.317 1.232 1.531 1.514 1.459 123.46 116.22 121.00 109.33 112.74 108.25 122.77
* *
26 PHE 26 1.314 1.224 1.516 1.524 1.451 121.67 114.91 121.24 111.98 111.60 109.18 123.79
* *
27 GLN 27 1.317 1.242 1.544 1.533 1.454 124.03 115.64 121.27 109.71 110.60 107.18 123.09
* +* +*
28 ASP 28 1.314 1.235 1.544 1.527 1.445 122.05 117.47 120.76 110.77 111.67 109.20 121.76
* *
29 PRO 29 1.356 1.232 1.538 1.532 1.482 123.48 117.67 120.63 110.13 113.92 103.55 121.70
* *
30 ASP 30 1.316 1.243 1.523 1.528 1.464 120.46 115.41 121.29 112.27 110.06 111.19 123.26
* *
31 VAL 31 1.322 1.230 1.526 1.545 1.456 122.35 115.23 121.60 109.25 108.86 111.03 123.15
32 ILE 32 1.308 1.240 1.541 1.540 1.439 122.76 116.22 120.65 111.28 110.53 109.76 123.09
* * *
33 ASN 33 1.327 1.227 1.514 1.533 1.476 122.38 116.78 120.70 108.30 112.48 111.80 122.52
34 VAL 34 1.306 1.238 1.530 1.551 1.447 120.38 116.87 120.26 111.89 112.50 112.56 122.86
+* * +*
35 MET 35 1.331 1.233 1.544 1.554 1.443 121.26 117.68 120.18 113.97 110.69 110.64 122.11
* ** **
36 LEU 36 1.338 1.233 1.525 1.558 1.452 119.96 116.47 119.99 111.00 112.44 115.66 123.49
* *** ***
37 ASP 37 1.332 1.228 1.510 1.541 1.473 123.59 114.62 121.60 107.97 109.20 110.91 123.77
* * *
38 ARG 38 1.314 1.224 1.513 1.541 1.456 123.11 116.78 120.15 107.55 109.09 110.75 123.06
* * *
39 THR 39 1.307 1.230 1.540 1.532 1.437 122.38 117.52 120.36 109.91 111.14 109.88 122.03
+* * +*
40 PRO 40 1.349 1.250 1.534 1.535 1.468 123.39 116.17 120.61 109.54 111.38 103.85 123.18
41 GLU 41 1.316 1.236 1.539 1.534 1.454 122.09 116.49 120.94 110.87 109.18 110.87 122.57
Residue-by-residue listing for refined_9 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
-----------------------------------------------------------------------------------------------------------------------------------
42 ILE 42 1.301 1.239 1.530 1.558 1.444 121.75 115.73 120.93 108.58 110.63 109.70 123.34
+* * +*
43 VAL 43 1.307 1.239 1.528 1.566 1.442 122.53 116.44 120.53 109.97 109.10 112.38 123.00
+* +*
44 SER 44 1.300 1.243 1.522 1.519 1.429 122.41 116.29 120.80 110.59 108.89 109.10 122.88
** +* **
45 ALA 45 1.303 1.237 1.507 1.506 1.432 121.54 114.36 121.94 109.81 112.05 110.09 123.70
+* * +*
46 THR 46 1.287 1.217 1.512 1.545 1.418 123.82 116.45 120.28 108.65 108.13 110.53 123.23
+** ** * * +**
47 LEU 47 1.285 1.232 1.520 1.535 1.422 122.71 117.40 120.56 111.27 108.69 110.11 121.92
*** +* ***
48 PRO 48 1.331 1.243 1.523 1.523 1.444 122.32 116.22 120.88 110.91 111.37 102.90 122.88
* *
49 GLY 49 1.308 1.235 1.500 - 1.437 120.45 115.65 121.04 - 111.23 - 123.30
* *
50 PHE 50 1.313 1.210 1.482 1.538 1.448 123.06 117.86 119.72 109.68 107.96 112.07 122.41
* * ** * **
51 GLN 51 1.290 1.235 1.509 1.542 1.429 119.78 115.21 120.71 110.35 109.17 109.80 124.03
+** +* * +**
52 ARG 52 1.313 1.241 1.513 1.573 1.442 122.52 116.58 120.32 109.30 107.88 113.03 123.08
* ** * * **
53 PHE 53 1.289 1.230 1.527 1.518 1.438 121.70 117.19 120.07 113.91 112.00 111.38 122.74
+** * ** +**
54 ARG 54 1.331 1.228 1.521 1.538 1.449 121.10 114.42 121.32 109.21 114.72 108.73 124.21
* * *
55 LEU 55 1.321 1.246 1.525 1.549 1.458 125.17 114.86 121.82 110.35 104.09 112.19 123.32
+* +** +**
56 LYS 56 1.336 1.238 1.510 1.539 1.443 121.73 114.60 121.53 113.00 110.11 111.75 123.86
+* +*
57 GLY 57 1.295 1.230 1.500 - 1.434 122.73 114.21 121.79 - 107.91 - 124.01
** * * * +* **
58 ARG 58 1.316 1.230 1.525 1.573 1.448 123.63 115.86 121.34 112.41 108.03 110.22 122.80
** * * * **
59 LEU 59 1.310 1.211 1.521 1.539 1.434 122.04 117.46 120.09 112.56 108.98 110.93 122.45
* * * * *
60 TYR 60 1.291 1.232 1.514 1.536 1.447 121.56 118.90 119.16 108.68 108.31 108.63 121.91
+** * * * +**
61 PRO 61 1.352 1.247 1.524 1.542 1.452 121.26 115.60 121.11 110.92 108.65 104.48 123.21
* * *
62 CYS 62 1.298 1.237 1.526 1.517 1.433 122.55 115.32 121.03 111.52 112.94 108.07 123.65
** * * **
63 ILE 63 1.330 1.233 1.512 1.561 1.457 123.55 116.54 120.46 107.54 110.28 110.93 123.00
* *
64 VAL 64 1.301 1.242 1.518 1.565 1.449 121.72 117.51 120.15 109.89 109.49 114.00 122.27
+* * +*
65 PRO 65 1.337 1.243 1.534 1.536 1.463 122.70 115.63 121.15 110.98 112.29 103.78 123.19
66 SER 66 1.307 1.231 1.525 1.534 1.434 123.06 116.80 119.98 111.10 106.99 109.48 123.22
+* * +* +*
67 GLU 67 1.323 1.239 1.530 1.515 1.471 122.52 117.44 120.10 109.40 114.55 110.79 122.45
* *
68 LYS 68 1.313 1.240 1.528 1.539 1.451 120.79 116.40 121.18 110.25 110.67 110.46 122.40
* *
69 GLY 69 1.311 1.241 1.508 - 1.431 120.09 116.27 120.53 - 112.71 - 123.19
* * *
Residue-by-residue listing for refined_9 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
-----------------------------------------------------------------------------------------------------------------------------------
70 GLU 70 1.324 1.248 1.530 1.531 1.443 121.74 116.84 120.58 110.21 108.73 111.28 122.55
71 VAL 71 1.301 1.204 1.516 1.555 1.443 121.94 117.17 120.48 109.10 109.42 111.54 122.34
** * **
72 HIS 72 1.299 1.237 1.490 1.538 1.450 120.85 116.12 120.23 110.42 107.95 112.46 123.62
** +* * * **
73 GLY 73 1.291 1.238 1.486 - 1.421 120.81 116.58 120.49 - 110.80 - 122.92
+** +* +* +**
74 LYS 74 1.283 1.230 1.512 1.532 1.426 121.38 116.17 120.73 109.66 110.24 110.10 123.09
*** +* ***
75 VAL 75 1.299 1.231 1.513 1.548 1.431 122.26 114.99 120.94 109.19 110.21 111.58 124.08
** * **
76 LEU 76 1.306 1.227 1.512 1.539 1.433 123.61 116.65 120.27 107.95 107.67 110.06 123.03
+* * * * * +*
77 MET 77 1.293 1.219 1.495 1.530 1.449 121.96 116.43 120.71 111.75 109.86 112.27 122.87
+** * * +**
78 GLY 78 1.298 1.230 1.509 - 1.428 119.48 115.61 121.18 - 110.15 - 123.21
** * **
79 VAL 79 1.332 1.249 1.536 1.581 1.449 121.92 118.04 119.99 111.21 108.13 111.37 121.95
+* * +*
80 THR 80 1.316 1.239 1.516 1.551 1.439 119.38 115.48 121.18 108.54 110.47 112.69 123.35
* *
81 SER 81 1.299 1.232 1.547 1.526 1.443 123.01 116.93 120.77 110.77 110.94 109.32 122.29
** * **
82 ASP 82 1.332 1.220 1.519 1.518 1.461 120.35 117.37 120.68 111.20 110.80 112.42 121.95
* *
83 GLU 83 1.328 1.203 1.523 1.528 1.457 119.02 116.65 120.65 108.08 108.86 114.89 122.70
* * * +** +**
84 LEU 84 1.331 1.223 1.530 1.532 1.458 121.91 116.91 120.13 110.06 109.70 110.83 122.94
85 GLU 85 1.345 1.222 1.527 1.546 1.471 121.13 115.38 121.18 110.49 110.19 112.39 123.42
* * *
86 ASN 86 1.317 1.201 1.504 1.521 1.449 123.52 116.35 120.62 110.28 111.33 108.71 122.99
* * * * *
87 LEU 87 1.298 1.235 1.504 1.531 1.447 122.43 114.66 121.18 110.42 109.26 110.27 124.16
** * **
88 ASP 88 1.321 1.214 1.518 1.540 1.451 123.48 115.77 121.19 111.58 109.07 109.16 123.04
89 ALA 89 1.312 1.230 1.548 1.513 1.447 122.85 115.87 120.94 109.63 111.47 108.55 123.15
* * * *
90 VAL 90 1.329 1.236 1.553 1.593 1.465 123.79 117.68 119.82 112.52 113.17 111.04 122.50
* +* * +* +*
91 GLU 91 1.322 1.245 1.530 1.531 1.480 122.00 114.66 121.49 110.72 111.55 110.76 123.83
* *
92 GLY 92 1.321 1.229 1.512 - 1.462 123.96 117.51 119.74 - 115.91 - 122.74
+* * +*
93 ASN 93 1.325 1.226 1.522 1.540 1.471 121.45 117.38 120.41 109.76 111.83 111.70 122.20
94 GLU 94 1.326 1.228 1.527 1.525 1.461 120.19 116.61 120.62 111.47 112.74 111.08 122.76
95 TYR 95 1.313 1.230 1.510 1.535 1.458 122.32 116.64 120.38 109.42 110.27 111.42 122.98
* *
96 GLU 96 1.310 1.235 1.516 1.535 1.436 121.31 115.77 120.85 111.15 109.51 110.20 123.38
* * *
97 ARG 97 1.312 1.230 1.517 1.543 1.439 122.37 115.35 121.26 111.89 110.13 109.91 123.38
* * *
98 VAL 98 1.308 1.235 1.513 1.545 1.451 123.18 116.45 120.38 109.38 110.86 112.58 123.15
* *
99 THR 99 1.306 1.238 1.524 1.568 1.448 121.16 116.22 120.87 111.87 109.20 112.79 122.89
+* * * +*
Residue-by-residue listing for refined_9 Page 11
----------------------------------------
...................................................................................................................................
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
-----------------------------------------------------------------------------------------------------------------------------------
100 VAL 100 1.308 1.237 1.517 1.552 1.447 122.25 115.65 120.78 108.37 111.03 111.12 123.56
* *
101 GLY 101 1.314 1.236 1.510 - 1.429 121.34 116.19 120.78 - 110.99 - 123.02
* * *
102 ILE 102 1.298 1.204 1.502 1.579 1.439 122.28 117.13 120.09 111.94 109.50 112.58 122.78
** * * * * **
103 VAL 103 1.276 1.233 1.497 1.559 1.434 121.91 117.54 119.63 110.40 107.91 110.70 122.80
+*** * * * +***
104 ARG 104 1.318 1.240 1.490 1.519 1.442 119.47 115.29 121.43 109.26 110.17 113.69 123.27
+* * +* +*
105 GLU 105 1.288 1.233 1.521 1.513 1.427 121.92 115.59 121.35 112.15 111.04 110.07 123.05
+** +* * +**
106 ASP 106 1.320 1.238 1.507 1.529 1.453 121.65 116.20 121.01 109.15 109.94 112.33 122.79
* *
107 ASN 107 1.317 1.236 1.529 1.538 1.419 121.97 114.46 121.66 107.44 108.43 110.59 123.84
** * **
108 SER 108 1.315 1.225 1.531 1.539 1.449 126.54 115.63 121.32 108.46 107.29 110.13 123.04
* +** * +**
109 GLU 109 1.321 1.232 1.514 1.554 1.439 122.44 116.41 120.78 113.20 111.74 110.91 122.81
* * +* +*
110 LYS 110 1.302 1.240 1.518 1.565 1.431 120.46 115.04 121.22 110.63 110.70 113.07 123.72
+* +* * +* +*
111 MET 111 1.294 1.224 1.469 1.513 1.436 124.00 114.85 121.27 106.73 108.46 114.59 123.87
+** +** * * +* ** +**
112 ALA 112 1.249 1.235 1.496 1.515 1.431 121.66 116.27 120.48 110.86 108.89 111.58 123.24
*5.7* * * *5.7*
113 VAL 113 1.298 1.236 1.512 1.564 1.443 121.76 116.14 120.67 108.05 109.62 112.21 123.19
** **
114 LYS 114 1.302 1.215 1.502 1.545 1.434 121.82 117.34 120.23 109.11 108.25 112.01 122.42
+* * * * +*
115 THR 115 1.281 1.248 1.510 1.561 1.423 120.79 116.20 120.37 110.56 108.21 112.68 123.43
*** +* * ***
116 TYR 116 1.291 1.229 1.492 1.527 1.416 121.98 114.24 121.72 114.11 110.13 110.83 124.03
+** +* ** ** +**
117 MET 117 1.293 1.244 1.500 1.546 1.424 122.90 115.39 120.84 110.79 108.96 109.06 123.75
+** * +* +**
118 TRP 118 1.298 1.239 1.514 1.522 1.420 122.54 116.76 120.15 112.36 107.07 108.32 123.08
** +* * * * **
119 ILE 119 1.314 1.243 1.525 1.581 1.456 120.46 116.29 121.04 109.55 111.17 114.30 122.66
* +* +* +*
120 ASN 120 1.304 1.219 1.512 1.528 1.437 120.46 115.54 121.65 111.46 110.72 111.94 122.80
+* * +*
121 LYS 121 1.302 1.234 1.537 1.543 1.453 122.83 115.72 121.23 112.10 111.30 109.43 123.05
+* * +*
122 ALA 122 1.317 1.234 1.524 1.508 1.439 122.99 116.42 120.78 110.07 110.04 109.37 122.80
123 ASP 123 1.328 1.237 1.535 1.539 1.466 121.56 117.84 120.60 110.33 109.92 111.29 121.55
124 PRO 124 1.335 1.237 1.538 1.525 1.457 122.61 117.42 120.37 110.20 113.79 102.46 122.20
125 ASP 125 1.314 1.228 1.495 1.533 1.448 120.69 116.52 120.33 110.58 112.08 112.57 123.14
* * * *
126 MET 126 1.313 1.223 1.543 1.526 1.462 121.92 116.76 120.65 109.68 112.22 109.55 122.59
* *
127 PHE 127 1.323 1.232 1.539 1.536 1.457 122.24 115.83 121.17 111.22 112.02 110.31 122.99
128 GLY 128 1.315 1.242 1.505 - 1.438 122.05 117.39 119.68 - 110.41 - 122.93
129 GLU 129 1.319 1.234 1.528 1.534 1.450 120.88 115.53 121.36 110.97 112.40 112.55 123.11
* *
Residue-by-residue listing for refined_9 Page 12
----------------------------------------
...................................................................................................................................
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
-----------------------------------------------------------------------------------------------------------------------------------
130 TRP 130 1.308 1.214 1.529 1.540 1.450 122.73 119.19 118.40 111.90 105.91 108.29 122.41
* * * +* * +*
131 ASN 131 1.335 1.238 1.541 1.544 1.500 121.79 117.02 120.41 111.95 113.51 112.35 122.55
** * **
132 PHE 132 1.327 1.228 1.535 1.528 1.473 122.13 117.49 120.03 110.08 113.61 113.56 122.45
+* +*
133 GLU 133 1.336 1.226 1.511 1.538 1.475 121.29 115.48 121.02 112.58 112.10 113.20 123.49
* +* +*
134 GLU 134 1.298 1.224 1.537 1.533 1.456 121.92 116.44 121.17 111.22 109.31 110.87 122.33
** **
135 TRP 135 1.321 1.219 1.529 1.539 1.447 120.96 116.36 121.04 111.92 109.71 111.67 122.60
136 LYS 136 1.336 1.209 1.529 1.543 1.469 122.04 115.24 121.27 109.70 108.36 110.71 123.48
* * *
137 ARG 137 1.315 1.222 1.533 1.519 1.449 123.88 117.11 120.91 111.02 111.56 108.76 121.98
* * *
138 LEU 138 1.304 1.231 1.533 1.536 1.456 120.43 116.60 120.89 111.54 112.48 112.34 122.51
+* * +*
139 HIS 139 1.313 1.229 1.532 1.538 1.462 121.01 116.62 120.47 110.07 111.21 111.69 122.91
* *
140 LYS 140 1.334 1.202 1.506 1.562 1.466 122.16 115.78 120.26 109.99 110.06 113.20 123.97
* +* +* +*
141 LYS 141 1.340 1.229 1.548 1.562 1.469 124.40 116.89 120.05 112.95 111.10 108.93 123.05
* +* * +* +*
142 LYS 142 1.335 1.232 1.536 1.542 1.469 122.55 116.00 121.11 110.40 110.65 109.84 122.87
143 PHE 143 1.313 1.222 1.515 1.533 1.454 122.17 115.59 121.41 108.76 109.13 110.93 123.00
* *
144 ILE 144 1.317 1.197 1.514 1.564 1.445 122.48 117.59 119.79 111.63 110.86 113.39 122.61
+* * * +*
145 GLU 145 1.328 1.231 1.536 1.529 1.462 120.93 117.30 120.54 110.60 111.42 112.15 122.14
146 THR 146 1.324 1.219 1.546 1.578 1.439 119.82 117.65 120.35 112.60 110.36 113.61 121.93
* * * +* * +*
147 PHE 147 1.340 1.213 1.517 1.529 1.467 120.98 117.03 120.04 112.07 113.89 113.78 122.92
* +* +*
148 LYS 148 1.312 1.218 1.525 1.541 1.460 122.97 114.41 121.70 110.14 108.18 109.12 123.81
* * *
149 LYS 149 1.314 1.230 1.532 1.522 1.444 123.99 115.77 121.19 111.10 109.45 107.45 123.03
* * +* +*
150 ILE 150 1.326 1.232 1.534 1.564 1.456 122.51 116.45 120.96 111.66 110.22 111.47 122.57
* *
151 MET 151 1.327 1.228 1.519 1.536 1.464 121.66 116.00 120.81 110.24 109.98 112.17 123.17
152 GLU 152 1.327 1.224 1.534 1.531 1.450 122.04 116.37 121.11 110.74 109.70 111.09 122.52
153 CYS 153 1.329 1.231 1.530 1.531 1.463 122.22 115.69 121.48 110.35 109.63 110.72 122.82
154 LYS 154 1.325 1.229 1.513 1.517 1.455 122.32 114.20 121.18 108.44 109.56 110.69 124.62
* * *
155 LYS 155 1.320 1.240 1.525 1.547 1.454 125.63 114.68 122.07 112.42 109.76 113.02 123.08
** * * **
156 LYS 156 1.313 1.239 1.520 1.542 1.442 123.13 117.15 120.61 110.96 109.41 110.52 122.22
* *
157 PRO 157 1.335 1.237 1.520 1.528 1.452 122.68 115.48 121.41 109.64 112.77 103.26 123.11
158 GLN 158 1.304 1.242 1.528 1.546 1.432 122.43 115.00 122.13 113.61 109.28 111.64 122.79
+* * +* +*
159 GLY 159 1.305 1.237 1.500 - 1.424 120.98 116.19 120.56 - 113.37 - 123.23
+* +* +*
160 GLN 160 1.306 1.242 1.523 1.552 1.445 121.58 116.55 120.37 109.60 108.24 112.53 123.03
+* * * * +*
Residue-by-residue listing for refined_9 Page 13
----------------------------------------
...................................................................................................................................
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
-----------------------------------------------------------------------------------------------------------------------------------
161 GLY 161 1.321 1.245 1.516 - 1.450 121.08 116.68 120.21 - 112.07 - 123.11
162 ASN 162 1.325 1.233 1.524 1.553 1.473 121.83 116.52 120.78 109.51 110.45 112.57 122.69
* * *
163 ASP 163 1.294 1.235 1.519 1.531 1.452 121.68 116.29 120.74 111.31 110.42 109.76 122.95
** **
164 ASP 164 1.307 1.236 1.515 1.535 1.448 122.26 116.61 120.79 110.14 109.45 110.78 122.59
+* +*
165 ILE 165 1.303 1.242 1.512 1.559 1.441 120.92 116.01 121.01 109.55 111.09 113.30 122.97
+* * +*
166 SER 166 1.302 1.238 1.520 1.528 1.425 121.28 116.34 120.84 113.17 109.00 110.26 122.77
+* +* +* +*
167 HIS 167 1.305 1.235 1.507 1.556 1.435 121.52 116.35 120.32 110.38 109.94 109.81 123.32
+* * * +*
168 VAL 168 1.297 1.242 1.513 1.561 1.440 121.47 116.55 120.39 109.27 108.85 112.60 123.06
** **
169 LEU 169 1.294 1.228 1.512 1.566 1.431 121.56 116.90 120.38 112.60 106.56 109.52 122.65
** +* * * +* **
170 ARG 170 1.314 1.235 1.514 1.542 1.448 120.21 115.86 121.02 111.77 110.18 112.58 123.11
* * *
171 GLU 171 1.291 1.241 1.519 1.528 1.430 122.01 115.63 120.81 110.15 110.65 109.09 123.54
+** * +**
172 ASP 172 1.298 1.227 1.498 1.530 1.438 123.32 116.60 120.31 110.51 108.01 112.01 123.06
** * * * **
173 GLN 173 1.300 - 1.530 1.538 1.436 121.06 - - 110.73 107.91 109.96 -
** * * **
-----------------------------------------------------------------------------------------------------------------------------------
Max deviations: *5.7* +* +** +** *** +** * * ** +** *** * *5.7*
-----------------------------------------------------------------------------------------------------------------------------------
Residue-by-residue listing for refined_9 Page 14
----------------------------------------
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 1.249 1.345 1.311 .015
*5.7* * *
C-N (Pro) 1.341 .016 7 1.331 1.356 1.342 .009
C-O C-O 1.231 .020 172 1.197 1.250 1.232 .010
+*
CA-C CH1E-C (except Gly) 1.525 .021 161 1.469 1.553 1.520 .014
+** *
CH2G*-C (Gly) 1.516 .018 12 1.486 1.516 1.504 .008
+*
CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.506 1.515 1.510 .004
CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.532 1.593 1.561 .013
+*
CH1E-CH2E (the rest) 1.530 .020 128 1.480 1.573 1.536 .014
+** **
N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.398 1.500 1.446 .015
*** **
NH1-CH2G* (Gly) 1.451 .016 12 1.421 1.463 1.438 .013
+*
N-CH1E (Pro) 1.466 .015 7 1.444 1.482 1.460 .012
* *
-------------------------------------------------------------------------------------------------------------
Residue-by-residue listing for refined_9 Page 15
----------------------------------------
+-----------------+
| 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 2.0 153 113.92 119.19 116.17 .96
* *
CH2G*-C-NH1 (Gly) 116.4 2.1 12 114.21 117.51 116.28 .87
*
CH1E-C-N (Pro) 116.9 1.5 7 115.48 117.67 116.31 .82
O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 121.55 124.62 123.02 .55
*
O-C-N (Pro) 122.0 1.4 7 121.70 123.21 122.78 .55
C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 119.02 126.54 122.08 1.16
* +**
C-NH1-CH2G* (Gly) 120.6 1.7 11 119.48 123.96 121.16 1.27
+*
C-N-CH1E (Pro) 122.6 5.0 7 121.26 123.48 122.63 .68
CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 118.40 122.73 120.80 .59
* *
CH2G*-C-O (Gly) 120.8 2.1 12 119.68 121.79 120.55 .57
CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 109.63 110.86 110.09 .47
CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 107.54 112.60 110.03 1.39
+*
CH2E-CH1E-C (the rest) 110.1 1.9 128 106.73 114.23 110.75 1.45
+* **
N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 104.09 114.72 110.06 1.67
+** *
NH1-CH2G*-C (Gly) 112.5 2.9 12 107.91 115.91 111.65 1.93
+* *
N-CH1E-C (Pro) 111.8 2.5 7 108.65 113.92 112.03 1.67
*
N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 108.55 111.58 109.90 1.11
*
NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 109.70 114.30 111.89 1.22
* +*
N-CH1E-CH2E (Pro) 103.0 1.1 7 102.46 104.48 103.47 .62
*
NH1-CH1E-CH2E (the rest) 110.5 1.7 121 107.18 115.66 110.95 1.61
+* ***
-------------------------------------------------------------------------------------------------------------
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 refined_9 Page 16
----------------------------------------
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] 130 85.0%
Residues in additional allowed regions [a,b,l,p] 21 13.7%
Residues in generously allowed regions [~a,~b,~l,~p] 2 1.3%
Residues in disallowed regions [XX] 0 .0%
---- ------
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 85.0 83.8 10.0 .1 Inside
b. Omega angle st dev 172 3.7 6.0 3.0 -.8 Inside
c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside
d. Zeta angle st dev 161 1.9 3.1 1.6 -.8 Inside
e. H-bond energy st dev 99 .9 .8 .2 .6 Inside
f. Overall G-factor 173 .0 -.4 .3 1.2 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 7.6 18.1 6.5 -1.6 BETTER
b. Chi-1 trans st dev 56 8.3 19.0 5.3 -2.0 BETTER
c. Chi-1 gauche plus st dev 61 6.8 17.5 4.9 -2.2 BETTER
d. Chi-1 pooled st dev 150 8.4 18.2 4.8 -2.0 BETTER
e. Chi-2 trans st dev 37 5.8 20.4 5.0 -2.9 BETTER
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% 85.0 1
Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 8.2 1
H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .94 3
Residue-by-residue listing for refined_9 Page 17
----------------------------------------
G - F A C T O R S
Average
Parameter Score Score
--------- ----- -----
Dihedral angles:-
Phi-psi distribution -.50
Chi1-chi2 distribution -.32
Chi1 only -.16
Chi3 & chi4 .37
Omega -.04
------ -.19
=====
Main-chain covalent forces:-
Main-chain bond lengths -.01
Main-chain bond angles .41
------ .23
=====
OVERALL AVERAGE -.04
=====
Ideally, scores should be above -0.5. Values below -1.0 may need investigation.