Residue-by-residue listing for refined_15 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 - - - - - - - - - - - 179.6 - - -
2 HIS 2 B - 194.1 - - - - - - - - 188.7 - 34.5 -
* *
3 HIS 3 b - - -77.2 - - - - - - - 170.6 -.6 30.5 -
+* +* +*
4 HIS 4 B - - -68.4 - - - - - - - 185.5 - 34.5 -
5 HIS 5 B - 190.2 - - - - - - - - 176.5 - 34.2 -
6 HIS 6 B - - -60.9 - - - - - - - 181.8 -.9 33.7 -
* *
7 HIS 7 B 67.1 - - - - - - - - - 176.9 - 35.0 -
8 LEU 8 B - - -56.8 181.1 - - - - - - 176.7 - 34.8 -
9 GLU 9 B - - -62.1 176.9 - - - - - - 182.9 - 34.5 -
10 CYS 10 S B - - -57.3 - - - - - - - 172.6 -.5 36.5 -
* +* +*
11 SER 11 B - 183.1 - - - - - - - - 188.2 - 34.3 -
* *
12 SER 12 A - 185.4 - - - - - - - - 186.7 -1.2 34.1 -
* * *
13 ASP 13 S XX - - -70.5 - - - - - - - 169.6 - 30.6 -
**** +* ****
14 SER 14 S B - - -54.3 - - - - - - - 189.2 -1.8 36.4 -
+* +*
15 LEU 15 b - - -67.1 - - - - - - - 170.2 - 31.0 -
+* +*
16 GLN 16 ~p - - -56.9 177.6 - - - - - - 167.6 -1.8 36.5 -
** ** **
17 LEU 17 B - - -60.3 - - - - - - - 184.3 - 33.4 -
Residue-by-residue listing for refined_15 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 - - -50.2 - - - - - - - 174.4 -2.3 35.7 -
* *
19 ASN 19 E B 34.6 - - - - - - - - - 186.1 - 27.8 -
+* * +* +*
20 VAL 20 E B - 179.2 - - - - - - - - 179.1 -1.7 35.5 -
21 PHE 21 E B - 181.1 - - - - - - - - 182.8 -3.0 35.2 -
* *
22 VAL 22 E B - - -65.8 - - - - - - - 184.9 -2.9 32.3 -
* *
23 TYR 23 A 56.1 - - - - - - - - - 180.2 - 31.8 -
24 GLY 24 t - - - - - - - - - - - 184.1 - - -
25 SER 25 T A - - -51.3 - - - - - - - 183.1 - 35.4 -
* *
26 PHE 26 T a - - -60.9 - - - - - - - 180.1 - 34.4 -
27 GLN 27 t A 60.7 - - - - - - - - - 177.8 -1.6 29.6 -
* *
28 ASP 28 h B - 176.7 - - - - - - - - 183.0 - 34.7 -
29 PRO 29 H - - - - - -62.8 -62.8 -31.6 - - - 180.3 - 37.8 -
* *
30 ASP 30 H A - 181.1 - - - -67.3 -40.3 - - - 174.9 - 33.0 -
31 VAL 31 H A - 173.4 - - - -59.7 -37.6 - - - 180.8 - 34.6 -
32 ILE 32 H A - - -62.9 - - -63.1 -44.3 - - - 176.1 -1.5 33.4 -
33 ASN 33 H A - - -70.3 - - -59.5 -35.8 - - - 183.4 -2.0 33.9 -
34 VAL 34 H A - 181.3 - - - -81.1 -35.7 - - - 182.3 -1.6 33.1 -
* *
35 MET 35 H A - 198.2 - - - -75.1 -37.1 - - - 179.4 -2.9 33.7 -
* *
36 LEU 36 h a 52.1 - - 165.1 - - - - - - 185.4 -2.4 28.5 -
+* +*
37 ASP 37 t ~b - 172.8 - - - - - - - - 182.2 -.9 34.2 -
** * **
38 ARG 38 S b - - -64.7 180.1 - - - - - - 179.8 - 33.8 -
39 THR 39 B - - -49.9 - - - - - - - 170.1 - 35.5 -
* +* +*
40 PRO 40 - - - - - -61.5 - - - - - 181.9 - 39.1 -
* *
41 GLU 41 E b - 179.3 - 176.5 - - - - - - 182.2 -.5 32.0 -
** **
42 ILE 42 E B - - -52.8 178.4 - - - - - - 176.2 - 36.6 -
43 VAL 43 E B 67.1 - - - - - - - - - 177.1 -2.4 33.7 -
44 SER 44 E B - - -58.6 - - - - - - - 179.2 - 35.2 -
45 ALA 45 E B - - - - - - - - - - 178.9 -3.0 34.1 -
* *
46 THR 46 E B - - -55.4 - - - - - - - 172.4 -2.8 36.9 -
* * *
47 LEU 47 E b - 178.1 - - - - - - - - 182.7 -3.4 33.9 -
+* +*
48 PRO 48 E - - - - - -83.6 - - - - - 180.4 - 38.5 -
+* * +*
49 GLY 49 e - - - - - - - - - - - 180.4 -1.8 - -
50 PHE 50 t B - - -66.5 - - - - - - - 181.3 -.7 34.9 -
+* +*
51 GLN 51 E B - 182.0 - - - - - - - - 176.0 -2.7 35.0 -
52 ARG 52 E B 56.7 - - 175.2 - - - - - - 182.5 - 32.0 -
53 PHE 53 e B - - -60.9 - - - - - - - 177.4 -2.1 35.6 -
54 ARG 54 B - - -95.1 - - - - - - - 177.8 - 30.1 -
+* * +*
Residue-by-residue listing for refined_15 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
-----------------------------------------------------------------------------------------------------------------------------------
55 LEU 55 B - 199.6 - - - - - - - - 187.3 -.5 35.3 -
* ** **
56 LYS 56 A - - -61.2 175.5 - - - - - - 183.8 - 33.5 -
57 GLY 57 S - - - - - - - - - - - 175.9 - - -
58 ARG 58 S ~l - 178.5 - - - - - - - - 174.9 -.5 29.5 -
** ** * **
59 LEU 59 S B - 185.5 - - - - - - - - 191.0 - 31.6 -
+* +*
60 TYR 60 B - - -44.5 - - - - - - - 174.9 - 37.3 -
* *
61 PRO 61 S - - - - - -68.2 - - - - - 185.8 - 40.1 -
+* +*
62 CYS 62 e B 58.2 - - - - - - - - - 178.7 -2.3 34.6 -
63 ILE 63 E B - - -58.3 - - - - - - - 171.0 -.5 37.9 -
+* +* * +*
64 VAL 64 E B - - -63.6 - - - - - - - 175.8 -1.4 34.1 -
65 PRO 65 - - - - - -66.1 - - - - - 179.4 - 37.9 -
* *
66 SER 66 t B - 181.5 - - - - - - - - 183.1 -.6 34.0 -
+* +*
67 GLU 67 T A - - -49.5 - - - - - - - 186.1 - 35.3 -
* * *
68 LYS 68 T A - - -62.9 - - - - - - - 185.2 - 34.5 -
69 GLY 69 e - - - - - - - - - - - 178.3 -.9 - -
* *
70 GLU 70 E B 65.6 - - 185.7 - - - - - - 183.1 - 34.7 -
71 VAL 71 E B - 183.2 - - - - - - - - 173.4 -3.0 35.5 -
* * *
72 HIS 72 E B - - -64.9 - - - - - - - 182.9 -.6 32.7 -
+* +*
73 GLY 73 E - - - - - - - - - - - 181.4 -2.8 - -
* *
74 LYS 74 E B - - -87.9 - - - - - - - 178.4 -1.0 31.0 -
* * *
75 VAL 75 E B - 170.0 - - - - - - - - 177.3 -3.5 35.3 -
+* +*
76 LEU 76 E B - - -55.5 180.9 - - - - - - 178.5 -3.1 36.5 -
* *
77 MET 77 E B - - -55.9 179.4 - - - - - - 180.5 -3.4 36.5 -
+* +*
78 GLY 78 E - - - - - - - - - - - 178.0 - - -
79 VAL 79 E B - 177.6 - - - - - - - - 176.1 -2.1 35.7 -
80 THR 80 h B 55.5 - - - - - - - - - 180.8 - 33.9 -
81 SER 81 H A 49.9 - - - - -55.2 -36.9 - - - 179.9 - 33.9 -
82 ASP 82 H A - - -61.2 - - -59.9 -51.4 - - - 180.6 - 35.7 -
* *
83 GLU 83 H A - - -55.0 169.0 - -68.0 -35.4 - - - 175.2 - 36.5 -
84 LEU 84 H A - 181.5 - - - -57.8 -49.6 - - - 177.8 -2.5 33.6 -
85 GLU 85 H A - - -61.0 180.0 - -67.7 -33.5 - - - 179.5 -2.6 34.2 -
86 ASN 86 H A - 184.0 - - - -60.4 -49.0 - - - 180.3 -2.2 36.0 -
87 LEU 87 H A - - -60.5 176.2 - -66.9 -42.8 - - - 179.2 -3.0 34.5 -
* *
88 ASP 88 H A - 176.8 - - - -63.2 -32.0 - - - 177.5 -2.2 34.4 -
89 ALA 89 H A - - - - - -73.8 -45.4 - - - 181.2 -2.0 34.8 -
90 VAL 90 H A - 176.5 - - - -65.3 -56.9 - - - 183.0 -2.4 33.4 -
+* +*
Residue-by-residue listing for refined_15 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 - - -61.4 - - -78.0 -22.5 - - - 182.4 -2.8 32.2 -
* * *
92 GLY 92 h - - - - - - - - - - - 179.8 -.9 - -
+* +*
93 ASN 93 T A - - -66.7 - - - - - - - 181.4 -.8 32.5 -
+* +*
94 GLU 94 T a - 184.8 - 165.1 - - - - - - 177.7 -1.9 33.4 -
95 TYR 95 t B - - -69.5 - - - - - - - 178.0 -2.1 34.1 -
96 GLU 96 E B - 181.9 - 178.0 - - - - - - 184.0 -1.1 34.9 -
* *
97 ARG 97 E B - 186.1 - 186.8 - - - - - - 178.8 - 35.4 -
98 VAL 98 E B - - -62.6 - - - - - - - 181.8 -2.7 32.7 -
99 THR 99 E B - 191.0 - - - - - - - - 184.9 - 32.3 -
100 VAL 100 E B - - -64.3 - - - - - - - 178.0 -3.2 34.8 -
+* +*
101 GLY 101 E - - - - - - - - - - - 180.2 - - -
102 ILE 102 E B 54.8 - - - - - - - - - 180.2 -2.5 31.8 -
103 VAL 103 E B - 183.5 - - - - - - - - 181.3 -2.4 33.9 -
104 ARG 104 E B - 174.2 - 174.0 - - - - - - 180.8 -3.0 35.0 -
* *
105 GLU 105 e A - - -57.4 - - - - - - - 187.3 -2.1 38.2 -
* * *
106 ASP 106 T A - 178.9 - - - - - - - - 182.7 -.8 33.0 -
+* +*
107 ASN 107 T a 65.5 - - - - - - - - - 180.8 - 33.4 -
108 SER 108 T l - 187.4 - - - - - - - - 177.4 -2.0 31.5 -
109 GLU 109 E B - - -72.0 - - - - - - - 182.6 -.7 34.8 -
+* +*
110 LYS 110 E B - - -60.7 173.0 - - - - - - 183.0 - 34.9 -
111 MET 111 E B - - -66.9 171.3 - - - - - - 179.4 -3.5 34.1 -
+* +*
112 ALA 112 E B - - - - - - - - - - 185.2 - 34.1 -
113 VAL 113 E B - - -60.8 - - - - - - - 175.5 -2.6 35.1 -
114 LYS 114 E B - - -63.5 - - - - - - - 179.5 -1.8 33.4 -
115 THR 115 E B - 191.9 - - - - - - - - 183.2 -2.9 33.2 -
* *
116 TYR 116 E B - - -55.1 - - - - - - - 180.9 -.5 34.8 -
** **
117 MET 117 E B 64.6 - - 174.5 - - - - - - 179.9 -1.1 33.1 -
* *
118 TRP 118 t B - 191.7 - - - - - - - - 188.2 -3.2 35.5 -
* +* +*
119 ILE 119 T A - - -57.5 - - - - - - - 181.9 - 32.9 -
120 ASN 120 T A - 183.5 - - - - - - - - 178.3 - 33.1 -
121 LYS 121 t XX 62.4 - - 185.1 - - - - - - 174.1 -.8 27.2 -
**** * +* +* ****
122 ALA 122 S b - - - - - - - - - - 183.9 -3.3 33.3 -
+* +*
123 ASP 123 B - 188.4 - - - - - - - - 183.2 -1.1 34.5 -
* *
124 PRO 124 S - - - - - -74.3 - - - - - 184.2 - 39.2 -
+* +*
125 ASP 125 S A - - -72.1 - - - - - - - 179.0 - 31.4 -
126 MET 126 B 55.5 - - - - - - - - - 176.8 - 29.5 -
* *
127 PHE 127 b 59.3 - - - - - - - - - 179.4 - 33.7 -
128 GLY 128 - - - - - - - - - - - 179.3 - - -
Residue-by-residue listing for refined_15 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
-----------------------------------------------------------------------------------------------------------------------------------
129 GLU 129 B - - -60.7 177.2 - - - - - - 174.5 - 35.9 -
130 TRP 130 h B - 204.3 - - - - - - - - 183.9 - 32.3 -
* *
131 ASN 131 H A - - -59.1 - - -42.3 -54.8 - - - 180.0 - 33.9 -
+* * +*
132 PHE 132 H A - - -64.0 - - -66.2 -38.1 - - - 184.0 - 33.0 -
133 GLU 133 H A - - -54.0 - - -70.2 -29.3 - - - 178.2 - 34.3 -
134 GLU 134 H A - 184.4 - 177.2 - -68.2 -52.8 - - - 177.4 -2.4 33.9 -
* *
135 TRP 135 H A - 174.7 - - - -63.1 -30.5 - - - 178.6 -1.7 33.5 -
136 LYS 136 H A - 203.2 - - - -57.0 -50.4 - - - 180.5 -2.2 36.2 -
* *
137 ARG 137 H A 63.8 - - 170.9 - -69.8 -30.6 - - - 176.9 -1.9 29.4 -
* *
138 LEU 138 H A - - -81.3 - - -67.8 -31.2 - - - 173.6 -1.5 32.8 -
* *
139 HIS 139 H A - 175.1 - - - -79.2 -33.8 - - - 178.4 -2.0 33.5 -
* *
140 LYS 140 H A - 175.4 - 167.7 - -61.0 -33.4 - - - 178.9 -2.3 31.8 -
141 LYS 141 H A - - -63.4 177.0 - -48.8 -32.6 - - - 176.0 -1.7 34.2 -
* *
142 LYS 142 H A - 178.9 - - - -58.7 -48.2 - - - 185.9 -1.2 37.5 -
* * * *
143 PHE 143 H A - 198.0 - - - -76.1 -32.8 - - - 180.0 -.9 37.3 -
* *
144 ILE 144 H A - - -61.6 - - -61.6 -32.7 - - - 180.8 -2.6 31.8 -
145 GLU 145 H A - - -61.0 186.0 - -51.9 -41.3 - - - 179.1 -1.2 33.6 -
* * *
146 THR 146 H A - - -51.0 - - -71.0 -47.5 - - - 182.1 -.8 36.1 -
* +* +*
147 PHE 147 H A - - -75.3 - - -70.2 -29.8 - - - 175.9 -1.4 28.2 -
+* +*
148 LYS 148 H A - 182.1 - - - -59.4 -42.5 - - - 179.7 -3.5 34.8 -
** **
149 LYS 149 H A - 179.8 - 180.3 - -64.0 -40.4 - - - 179.6 -1.1 35.0 -
* *
150 ILE 150 H A - - -59.0 174.2 - -68.6 -41.6 - - - 177.9 -1.5 33.6 -
151 MET 151 H A - - -65.5 - - -64.4 -42.6 - - - 177.2 -3.2 32.9 -
+* +*
152 GLU 152 H A - - -60.6 179.2 - -67.6 -30.8 - - - 178.1 -2.7 33.7 -
153 CYS 153 H A - 179.8 - - - -65.7 -37.6 - - - 177.3 -1.6 34.4 -
154 LYS 154 H A - - -61.3 182.3 - -79.2 -37.8 - - - 177.9 -1.8 34.2 -
* *
155 LYS 155 h l - 181.7 - 180.5 - - - - - - 177.2 -2.8 31.2 -
* *
156 LYS 156 B 58.5 - - 179.4 - - - - - - 180.0 - 33.9 -
157 PRO 157 - - - - - -55.0 - - - - - 181.3 - 38.6 -
* *
158 GLN 158 B 55.6 - - 180.4 - - - - - - 178.2 - 35.0 -
159 GLY 159 - - - - - - - - - - - 178.3 - - -
160 GLN 160 B - 185.4 - 180.2 - - - - - - 182.4 - 34.7 -
161 GLY 161 - - - - - - - - - - - 182.8 -.6 - -
+* +*
162 ASN 162 B - 186.0 - - - - - - - - 178.7 - 34.8 -
163 ASP 163 B - 175.5 - - - - - - - - 178.2 - 35.4 -
164 ASP 164 B - 177.4 - - - - - - - - 178.1 - 34.2 -
Residue-by-residue listing for refined_15 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
-----------------------------------------------------------------------------------------------------------------------------------
165 ILE 165 B - 181.7 - 178.1 - - - - - - 178.6 -.6 31.9 -
+* +*
166 SER 166 B - - -59.7 - - - - - - - 178.6 -.6 35.5 -
+* +*
167 HIS 167 B 71.4 - - - - - - - - - 175.8 - 32.8 -
168 VAL 168 B - - -64.4 - - - - - - - 180.5 - 33.6 -
169 LEU 169 B 56.0 - - 167.9 - - - - - - 176.7 - 31.1 -
170 ARG 170 B - 184.2 - 184.7 - - - - - - 183.1 -.5 35.6 -
** **
171 GLU 171 B - 184.5 - 179.2 - - - - - - 177.1 -.9 33.6 -
+* +*
172 ASP 172 B 60.2 - - - - - - - - - 181.0 -.7 32.2 -
+* +*
173 GLN 173 - 55.9 - - 182.6 - - - - - - - - 31.4 -
-----------------------------------------------------------------------------------------------------------------------------------
Max deviations: **** +* * +* +* +* +* ** ** +* ****
-----------------------------------------------------------------------------------------------------------------------------------
Mean values: 58.6 183.3 -62.2 177.4 -67.4 -65.2 -39.1 - - - 179.8 -1.9 34.0
Standard deviations: 7.4 7.4 8.3 5.4 9.4 8.1 8.0 - - - 3.9 .9 2.2
Numbers of values: 24 57 69 42 7 42 42 0 0 0 172 101 161 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_15 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 - 1.235 1.499 - 1.464 - 116.74 120.04 - 110.85 - 123.21
2 HIS 2 1.325 1.227 1.526 1.537 1.449 121.68 115.62 120.59 111.21 107.54 109.99 123.79
* *
3 HIS 3 1.310 1.231 1.514 1.535 1.462 123.80 114.19 121.97 110.59 116.65 112.67 123.84
* * * +* * +*
4 HIS 4 1.299 1.232 1.495 1.528 1.440 124.34 116.66 120.12 109.52 105.87 112.26 123.18
** * * +* * **
5 HIS 5 1.292 1.233 1.513 1.537 1.437 121.14 116.08 120.90 110.60 110.50 110.46 123.02
+** * +**
6 HIS 6 1.302 1.226 1.503 1.540 1.439 121.06 116.93 120.49 110.60 107.81 112.07 122.56
+* * * +*
7 HIS 7 1.291 1.232 1.501 1.556 1.446 121.32 116.14 120.50 109.09 109.15 111.43 123.34
+** * * +**
8 LEU 8 1.291 1.240 1.511 1.537 1.427 121.41 116.50 120.32 110.22 108.15 110.65 123.16
+** +* * +**
9 GLU 9 1.293 1.242 1.497 1.524 1.439 122.44 116.06 120.64 109.80 107.82 111.40 123.12
+** * * +**
10 CYS 10 1.301 1.239 1.516 1.540 1.435 121.73 116.65 120.39 108.58 109.90 109.32 122.94
+* * +*
11 SER 11 1.311 1.220 1.532 1.547 1.427 120.90 116.02 120.98 111.99 106.03 110.34 122.94
* +* +* +*
Residue-by-residue listing for refined_15 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 1.309 1.237 1.537 1.553 1.450 122.67 116.77 119.97 111.31 112.59 109.09 123.26
* * *
13 ASP 13 1.346 1.232 1.491 1.548 1.491 123.98 115.51 120.73 111.18 109.29 115.17 123.75
* +* +* * +** +**
14 SER 14 1.309 1.238 1.528 1.519 1.420 122.36 117.93 119.77 110.49 105.36 108.35 122.29
* +* ** * **
15 LEU 15 1.305 1.235 1.514 1.536 1.413 120.73 114.74 120.73 111.94 114.21 112.02 124.38
+* ** * **
16 GLN 16 1.344 1.249 1.534 1.526 1.470 124.66 115.60 121.76 108.15 113.40 108.33 122.59
* +* * * +*
17 LEU 17 1.318 1.243 1.489 1.523 1.414 121.14 116.24 120.66 109.51 106.62 113.98 123.05
+* ** +* ** **
18 HIS 18 1.269 1.236 1.487 1.542 1.431 120.87 115.42 120.53 109.04 109.10 110.51 124.04
**** +* * ****
19 ASN 19 1.285 1.232 1.504 1.549 1.422 122.30 114.75 121.64 114.70 111.44 114.72 123.55
*** +* ** ** ***
20 VAL 20 1.310 1.225 1.520 1.569 1.452 123.25 116.32 120.36 109.29 109.92 110.32 123.31
* * *
21 PHE 21 1.308 1.239 1.518 1.533 1.441 122.41 116.21 120.74 111.14 108.51 108.93 123.05
* *
22 VAL 22 1.302 1.236 1.526 1.551 1.446 121.75 115.53 121.29 111.20 111.82 112.02 123.18
+* +*
23 TYR 23 1.324 1.243 1.522 1.526 1.457 122.29 117.45 120.16 111.03 114.99 111.23 122.39
* *
24 GLY 24 1.306 1.212 1.495 - 1.439 118.73 116.63 120.00 - 113.39 - 123.34
+* * * +*
25 SER 25 1.317 1.226 1.536 1.513 1.461 122.71 116.77 120.93 109.69 112.73 108.42 122.27
* *
26 PHE 26 1.315 1.216 1.523 1.536 1.449 121.14 117.61 120.43 110.42 111.49 109.80 121.92
27 GLN 27 1.327 1.239 1.523 1.555 1.462 119.22 115.27 121.21 113.50 112.26 113.01 123.52
* * +* * +*
28 ASP 28 1.312 1.235 1.517 1.528 1.446 122.60 117.76 120.20 110.07 109.20 110.39 122.04
* *
29 PRO 29 1.346 1.230 1.526 1.528 1.462 122.63 117.11 120.72 110.51 113.33 104.25 122.15
* *
30 ASP 30 1.316 1.234 1.523 1.523 1.451 120.64 115.59 120.89 111.42 109.36 111.37 123.45
31 VAL 31 1.330 1.231 1.521 1.560 1.465 122.61 115.73 121.02 108.90 109.86 111.74 123.22
32 ILE 32 1.314 1.232 1.542 1.544 1.436 122.50 117.05 120.62 112.43 110.63 109.66 122.25
* * +* * +*
33 ASN 33 1.325 1.223 1.514 1.532 1.470 121.03 116.05 120.99 108.24 111.13 112.63 122.94
* *
34 VAL 34 1.308 1.237 1.537 1.560 1.445 121.43 117.69 120.31 110.48 112.17 111.55 122.01
+* +*
35 MET 35 1.325 1.224 1.527 1.543 1.441 120.22 117.77 120.18 111.35 110.25 110.36 121.97
36 LEU 36 1.323 1.235 1.521 1.559 1.450 119.03 117.61 119.61 112.17 114.46 114.66 122.75
* * * * ** **
37 ASP 37 1.329 1.229 1.509 1.549 1.485 121.58 115.86 121.12 109.65 111.40 110.90 123.01
* *
38 ARG 38 1.306 1.225 1.498 1.546 1.457 122.21 117.22 119.75 110.34 108.78 111.76 123.01
+* * +*
39 THR 39 1.307 1.241 1.528 1.527 1.430 120.91 117.23 120.46 108.57 111.69 110.13 122.26
+* * +*
40 PRO 40 1.341 1.243 1.530 1.534 1.461 123.03 117.35 119.77 110.33 109.26 103.31 122.82
* *
Residue-by-residue listing for refined_15 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
-----------------------------------------------------------------------------------------------------------------------------------
41 GLU 41 1.318 1.227 1.526 1.518 1.459 121.06 115.19 121.52 110.53 112.12 112.46 123.29
* *
42 ILE 42 1.297 1.244 1.519 1.551 1.435 122.66 115.99 120.85 107.87 109.26 110.18 123.16
** * **
43 VAL 43 1.295 1.227 1.528 1.557 1.434 121.98 116.72 120.51 109.73 109.30 112.56 122.73
** * **
44 SER 44 1.292 1.243 1.541 1.521 1.429 121.78 116.86 120.35 110.83 109.51 108.69 122.77
+** +* * +**
45 ALA 45 1.319 1.235 1.529 1.502 1.458 122.23 115.37 121.11 109.74 112.47 110.13 123.52
46 THR 46 1.311 1.227 1.528 1.555 1.447 123.82 116.66 120.21 106.22 109.86 111.07 123.12
* * * *
47 LEU 47 1.300 1.224 1.530 1.536 1.438 122.57 117.71 120.60 111.20 108.39 110.83 121.58
** * * **
48 PRO 48 1.335 1.242 1.533 1.526 1.455 122.45 116.06 120.96 110.90 112.66 102.94 122.98
49 GLY 49 1.322 1.232 1.502 - 1.443 120.61 115.60 121.10 - 111.74 - 123.30
50 PHE 50 1.306 1.204 1.487 1.544 1.439 123.72 118.24 119.17 109.89 106.84 111.36 122.58
+* * +* * * +* +*
51 GLN 51 1.293 1.239 1.505 1.534 1.445 120.27 115.92 120.49 109.65 109.87 110.29 123.54
+** +**
52 ARG 52 1.316 1.233 1.497 1.546 1.429 121.21 115.47 121.17 111.30 109.69 113.32 123.36
* * +* +*
53 PHE 53 1.287 1.223 1.495 1.533 1.430 121.97 117.66 119.58 110.35 108.21 109.43 122.69
*** * * * ***
54 ARG 54 1.306 1.224 1.485 1.553 1.446 120.86 114.46 121.31 111.89 112.14 114.24 124.22
+* +* * ** **
55 LEU 55 1.292 1.233 1.520 1.553 1.415 123.85 117.68 119.55 112.31 103.09 109.36 122.68
+** * ** * * +** +**
56 LYS 56 1.302 1.230 1.526 1.527 1.450 120.58 118.08 119.92 110.61 114.40 109.85 121.99
+* * +*
57 GLY 57 1.309 1.229 1.501 - 1.450 119.19 115.95 120.20 - 113.51 - 123.79
* *
58 ARG 58 1.340 1.239 1.518 1.577 1.468 125.24 115.13 121.77 115.80 110.73 111.76 123.07
** +* +** +**
59 LEU 59 1.288 1.230 1.520 1.534 1.408 122.39 117.08 119.69 113.83 107.57 111.99 123.23
+** +** +* * +**
60 TYR 60 1.305 1.236 1.532 1.546 1.443 121.89 117.72 120.12 108.97 109.83 107.71 122.16
+* +* +*
61 PRO 61 1.353 1.245 1.568 1.545 1.491 124.09 115.69 120.75 109.54 112.89 101.83 123.41
** +* * * **
62 CYS 62 1.322 1.252 1.551 1.529 1.464 125.32 114.38 121.72 110.04 114.84 108.54 123.90
* * ** * * **
63 ILE 63 1.340 1.218 1.511 1.571 1.467 124.89 117.33 119.55 105.96 108.53 110.34 123.11
* +* * +*
64 VAL 64 1.309 1.242 1.522 1.573 1.466 122.78 118.29 119.55 107.92 107.72 114.16 122.13
* * * * +* +*
65 PRO 65 1.335 1.238 1.542 1.537 1.460 122.18 116.15 121.08 110.96 112.05 103.95 122.74
66 SER 66 1.314 1.226 1.513 1.532 1.437 122.48 116.33 120.64 110.49 109.22 111.10 123.03
* * *
67 GLU 67 1.309 1.230 1.531 1.556 1.456 122.35 115.93 121.02 108.14 110.02 111.38 123.03
* * * *
68 LYS 68 1.326 1.232 1.524 1.559 1.459 121.74 117.82 120.12 108.24 112.34 111.82 122.05
* *
69 GLY 69 1.313 1.247 1.505 - 1.437 118.24 113.79 121.87 - 115.11 - 124.34
* * * *
Residue-by-residue listing for refined_15 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 1.298 1.227 1.518 1.545 1.430 125.79 118.14 119.61 111.09 104.46 110.95 122.21
** * ** ** **
71 VAL 71 1.283 1.222 1.489 1.548 1.437 120.17 117.01 120.51 107.90 110.30 111.60 122.45
*** +* * ***
72 HIS 72 1.287 1.226 1.498 1.527 1.430 119.47 115.82 121.36 111.97 108.70 111.78 122.81
+** * * * +**
73 GLY 73 1.288 1.233 1.476 - 1.417 120.44 116.28 120.64 - 111.03 - 123.07
+** ** ** +**
74 LYS 74 1.286 1.234 1.489 1.530 1.422 120.94 113.63 121.69 110.75 113.32 113.65 124.67
*** +* +* * +* * ***
75 VAL 75 1.288 1.226 1.524 1.545 1.434 124.13 115.72 120.69 109.05 110.94 110.30 123.59
+** * * +**
76 LEU 76 1.310 1.224 1.517 1.539 1.444 123.18 117.40 119.76 108.21 108.40 109.90 122.76
* *
77 MET 77 1.312 1.223 1.511 1.499 1.433 122.30 116.95 120.39 108.41 109.70 108.96 122.66
* +* * +*
78 GLY 78 1.313 1.239 1.504 - 1.439 120.08 115.44 120.98 - 111.53 - 123.58
* *
79 VAL 79 1.320 1.231 1.506 1.556 1.445 122.42 116.80 120.43 108.06 109.43 111.29 122.78
80 THR 80 1.288 1.243 1.526 1.545 1.421 120.87 116.89 120.37 110.65 108.50 111.59 122.73
+** +* +**
81 SER 81 1.300 1.230 1.543 1.518 1.453 122.29 115.95 120.61 111.77 112.13 108.68 123.39
** * **
82 ASP 82 1.321 1.220 1.520 1.528 1.464 123.54 115.54 121.05 109.23 111.03 109.20 123.39
* *
83 GLU 83 1.318 1.216 1.530 1.510 1.470 123.85 116.43 120.80 109.52 109.37 107.67 122.76
* * +* +*
84 LEU 84 1.322 1.235 1.533 1.564 1.461 122.43 116.33 120.63 113.02 109.38 109.30 123.02
+* +* +*
85 GLU 85 1.327 1.214 1.523 1.529 1.457 121.53 115.38 121.06 109.96 109.89 110.93 123.53
86 ASN 86 1.318 1.222 1.532 1.553 1.457 124.38 116.16 120.99 110.95 109.23 107.76 122.85
* * +* +*
87 LEU 87 1.310 1.238 1.515 1.531 1.458 122.68 115.22 121.03 110.15 110.47 110.13 123.74
* *
88 ASP 88 1.319 1.227 1.524 1.531 1.466 123.10 115.52 121.24 110.68 110.68 109.63 123.24
89 ALA 89 1.310 1.228 1.526 1.513 1.445 123.09 116.38 120.61 110.01 110.93 109.53 123.01
* *
90 VAL 90 1.328 1.241 1.541 1.572 1.463 122.07 116.80 120.74 110.23 111.48 111.68 122.41
* *
91 GLU 91 1.312 1.236 1.524 1.522 1.461 121.50 115.94 121.06 111.84 112.82 110.76 122.98
* *
92 GLY 92 1.317 1.222 1.517 - 1.460 122.29 116.91 120.43 - 114.48 - 122.65
93 ASN 93 1.320 1.238 1.528 1.543 1.462 121.67 117.61 120.11 109.91 112.65 112.43 122.28
* *
94 GLU 94 1.331 1.235 1.559 1.524 1.427 120.16 116.57 121.31 113.87 112.14 107.38 122.10
+* +* +* +* +*
95 TYR 95 1.319 1.235 1.512 1.527 1.457 122.31 116.35 120.49 108.96 110.49 111.90 123.15
96 GLU 96 1.320 1.243 1.513 1.534 1.430 121.70 116.11 120.53 111.15 107.40 109.80 123.35
* * *
97 ARG 97 1.304 1.246 1.503 1.529 1.434 121.83 115.77 121.18 109.06 109.27 110.50 123.05
+* * * +*
98 VAL 98 1.288 1.239 1.503 1.538 1.424 121.69 116.68 120.26 111.03 109.86 112.44 123.05
+** * +* +**
99 THR 99 1.293 1.237 1.534 1.573 1.430 120.47 116.26 120.95 112.87 108.96 111.69 122.75
+** * * +* +**
Residue-by-residue listing for refined_15 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 1.565 1.451 122.34 115.96 120.77 108.58 110.62 111.69 123.27
+* +*
101 GLY 101 1.305 1.236 1.509 - 1.429 121.02 116.58 120.36 - 110.97 - 123.06
+* * +*
102 ILE 102 1.304 1.226 1.507 1.577 1.447 122.06 116.98 120.30 111.81 110.63 112.88 122.71
+* * * +*
103 VAL 103 1.293 1.221 1.515 1.551 1.435 121.06 115.48 120.80 110.04 108.94 112.06 123.70
+** * +**
104 ARG 104 1.299 1.233 1.535 1.538 1.445 124.15 115.98 120.22 111.79 111.00 107.84 123.80
** * +* **
105 GLU 105 1.349 1.223 1.514 1.543 1.486 123.88 113.12 121.92 105.01 109.25 110.15 124.94
* * * +* +** * +**
106 ASP 106 1.314 1.227 1.537 1.532 1.460 125.86 118.69 119.73 111.62 115.41 108.92 121.58
* ** * +* **
107 ASN 107 1.318 1.236 1.520 1.544 1.481 118.60 115.86 120.32 110.14 112.39 111.11 123.81
* +* +*
108 SER 108 1.321 1.232 1.545 1.552 1.453 124.06 115.24 121.67 112.52 111.43 111.75 122.95
* * * *
109 GLU 109 1.319 1.229 1.493 1.520 1.449 123.60 116.12 120.48 109.08 108.92 111.33 123.40
+* * +*
110 LYS 110 1.282 1.228 1.515 1.519 1.436 122.13 115.51 121.42 110.66 109.35 109.41 123.07
*** * ***
111 MET 111 1.278 1.229 1.490 1.526 1.452 122.81 115.24 121.20 109.68 110.87 111.28 123.56
+*** +* +***
112 ALA 112 1.284 1.235 1.499 1.512 1.446 121.75 116.22 120.74 110.12 109.23 111.13 123.02
*** * ***
113 VAL 113 1.293 1.229 1.506 1.554 1.438 121.46 115.69 121.22 107.92 110.80 111.91 123.09
+** * +**
114 LYS 114 1.296 1.227 1.507 1.553 1.435 121.74 117.27 120.08 110.59 108.12 112.51 122.63
** * * * * **
115 THR 115 1.293 1.249 1.524 1.561 1.431 121.06 116.28 120.54 110.74 108.89 112.43 123.17
+** * +**
116 TYR 116 1.302 1.234 1.515 1.538 1.429 122.09 115.78 121.00 111.18 108.81 109.59 123.20
+* +* +*
117 MET 117 1.306 1.245 1.505 1.545 1.447 121.94 115.43 120.57 109.80 109.64 113.14 123.99
+* +* +*
118 TRP 118 1.298 1.238 1.525 1.524 1.429 123.16 116.34 120.50 111.43 108.05 108.21 123.17
** +* * * **
119 ILE 119 1.321 1.248 1.522 1.585 1.470 122.13 115.69 120.92 108.82 111.21 113.93 123.37
+* * +*
120 ASN 120 1.328 1.223 1.532 1.540 1.462 122.48 115.85 120.14 111.16 111.06 110.95 123.97
121 LYS 121 1.352 1.229 1.547 1.563 1.497 126.57 117.43 120.45 113.92 115.21 113.75 122.12
+* * +* ** +** ** * +* +**
122 ALA 122 1.300 1.232 1.505 1.523 1.432 122.06 115.21 121.39 111.21 107.38 112.01 123.20
** * * * **
123 ASP 123 1.304 1.231 1.510 1.535 1.443 121.67 117.47 120.20 110.44 109.04 110.47 122.32
+* +*
124 PRO 124 1.330 1.230 1.529 1.525 1.460 122.83 117.55 120.18 109.82 114.01 102.85 122.27
125 ASP 125 1.318 1.236 1.492 1.526 1.452 120.61 116.85 120.31 110.80 112.74 113.07 122.85
+* +* +*
126 MET 126 1.304 1.239 1.505 1.550 1.428 119.76 113.82 121.85 113.02 112.48 113.73 124.23
+* * +* * * +* +* +*
127 PHE 127 1.296 1.235 1.496 1.561 1.430 125.06 117.54 119.61 111.19 106.02 112.35 122.77
** * +* * +* +* * **
Residue-by-residue listing for refined_15 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
-----------------------------------------------------------------------------------------------------------------------------------
128 GLY 128 1.290 1.228 1.499 - 1.430 119.39 114.58 121.30 - 112.81 - 124.11
+** * +**
129 GLU 129 1.284 1.228 1.486 1.520 1.429 125.04 118.95 119.18 109.28 105.99 110.38 121.82
*** +* +* +* * +* ***
130 TRP 130 1.291 1.224 1.514 1.520 1.424 117.18 117.32 118.85 112.05 106.97 112.80 123.81
+** +* +** * * +* * +**
131 ASN 131 1.326 1.244 1.526 1.531 1.484 123.57 116.35 120.55 109.71 112.62 110.58 123.06
* * *
132 PHE 132 1.320 1.208 1.524 1.533 1.454 121.45 117.00 119.93 110.49 112.05 111.39 122.99
* *
133 GLU 133 1.328 1.239 1.518 1.516 1.472 122.32 116.04 121.06 109.17 111.49 110.93 122.90
134 GLU 134 1.307 1.225 1.525 1.522 1.436 121.15 115.91 120.99 111.57 108.84 110.16 123.02
+* * +*
135 TRP 135 1.325 1.234 1.539 1.544 1.459 122.16 114.88 121.53 112.02 110.27 109.77 123.57
* *
136 LYS 136 1.312 1.220 1.533 1.540 1.450 124.54 118.10 120.07 111.43 108.55 106.97 121.79
* +* ** **
137 ARG 137 1.338 1.225 1.523 1.527 1.464 119.16 116.86 120.17 110.94 112.53 115.36 122.93
* +** +**
138 LEU 138 1.322 1.230 1.519 1.537 1.466 121.33 116.18 120.96 110.94 110.48 111.86 122.86
139 HIS 139 1.313 1.226 1.532 1.546 1.461 121.48 115.56 121.11 111.05 109.52 111.13 123.32
* *
140 LYS 140 1.319 1.209 1.518 1.540 1.453 123.26 117.11 119.90 112.19 112.18 111.49 122.98
* * *
141 LYS 141 1.334 1.236 1.546 1.522 1.483 122.65 116.14 120.51 109.38 112.20 110.47 123.34
* * *
142 LYS 142 1.336 1.230 1.524 1.547 1.468 123.55 113.69 121.88 107.51 109.70 108.69 124.42
* * * * *
143 PHE 143 1.296 1.238 1.539 1.534 1.438 125.28 114.60 121.88 111.00 108.94 105.58 123.51
** * +* +** +**
144 ILE 144 1.326 1.208 1.520 1.569 1.455 123.86 118.14 119.22 110.97 112.65 112.76 122.63
* * * *
145 GLU 145 1.339 1.241 1.530 1.525 1.479 121.08 115.70 120.70 108.98 111.40 112.10 123.59
* *
146 THR 146 1.319 1.228 1.542 1.542 1.436 122.69 116.04 121.31 109.15 109.87 109.14 122.60
* * *
147 PHE 147 1.322 1.212 1.500 1.516 1.454 121.85 117.25 119.74 113.31 115.17 113.27 123.01
* +* * +* +*
148 LYS 148 1.310 1.223 1.523 1.539 1.452 121.82 115.23 120.98 110.22 108.56 110.36 123.65
* *
149 LYS 149 1.329 1.237 1.524 1.538 1.447 122.92 115.32 121.16 110.58 109.45 109.39 123.51
150 ILE 150 1.322 1.237 1.541 1.563 1.452 123.05 116.51 120.76 111.13 110.69 110.72 122.71
151 MET 151 1.323 1.226 1.513 1.535 1.463 122.12 116.68 120.44 110.41 110.76 112.08 122.87
152 GLU 152 1.328 1.229 1.529 1.527 1.461 121.59 115.95 120.86 110.19 110.38 111.18 123.19
153 CYS 153 1.326 1.232 1.532 1.542 1.458 122.88 116.06 121.15 110.76 109.97 109.99 122.78
154 LYS 154 1.320 1.234 1.515 1.512 1.449 121.82 114.81 120.98 110.76 110.05 110.03 124.20
155 LYS 155 1.327 1.238 1.523 1.544 1.458 124.99 115.31 121.72 111.58 112.36 112.69 122.96
+* * +*
156 LYS 156 1.302 1.236 1.529 1.547 1.435 122.03 118.17 119.44 111.48 108.55 110.66 122.35
+* * +*
157 PRO 157 1.354 1.244 1.528 1.533 1.475 122.82 115.65 120.82 110.18 112.36 103.56 123.53
* *
158 GLN 158 1.314 1.237 1.520 1.536 1.443 123.00 117.02 120.19 110.31 109.80 109.72 122.79
* *
159 GLY 159 1.316 1.236 1.506 - 1.437 119.98 116.41 120.70 - 112.46 - 122.89
Residue-by-residue listing for refined_15 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
-----------------------------------------------------------------------------------------------------------------------------------
160 GLN 160 1.311 1.237 1.523 1.538 1.447 121.71 116.69 120.49 110.72 108.23 110.13 122.80
* * *
161 GLY 161 1.303 1.238 1.495 - 1.435 120.91 116.87 120.00 - 110.88 - 123.13
+* * +*
162 ASN 162 1.307 1.234 1.518 1.529 1.446 121.29 115.89 120.80 110.09 110.55 109.90 123.30
+* +*
163 ASP 163 1.308 1.217 1.509 1.533 1.453 123.16 116.99 120.18 109.24 110.13 110.05 122.83
+* +*
164 ASP 164 1.308 1.238 1.502 1.528 1.453 121.31 116.72 120.29 109.41 110.23 111.48 122.98
+* * +*
165 ILE 165 1.308 1.229 1.531 1.570 1.438 120.68 115.93 121.05 111.47 110.34 112.98 122.96
+* * * * +*
166 SER 166 1.305 1.238 1.520 1.541 1.449 123.19 118.22 119.62 109.60 107.86 110.24 122.15
+* * * +*
167 HIS 167 1.311 1.236 1.510 1.560 1.445 119.95 116.02 120.82 110.42 110.69 112.71 123.16
* +* * +*
168 VAL 168 1.295 1.234 1.511 1.550 1.440 121.58 117.00 120.16 110.19 108.66 112.34 122.84
** **
169 LEU 169 1.292 1.233 1.515 1.565 1.435 121.45 115.44 121.21 111.91 111.60 113.17 123.30
+** +* * +* +**
170 ARG 170 1.316 1.243 1.516 1.534 1.445 122.41 117.14 120.52 109.47 107.49 110.20 122.31
* *
171 GLU 171 1.290 1.233 1.508 1.520 1.427 120.19 115.43 121.05 110.85 111.05 110.68 123.50
+** +* +**
172 ASP 172 1.301 1.237 1.509 1.551 1.440 122.78 115.40 121.17 111.60 109.32 112.71 123.36
+* * * +*
173 GLN 173 1.296 - 1.517 1.554 1.435 123.78 - - 113.20 109.33 112.34 -
** * * * +* * **
-----------------------------------------------------------------------------------------------------------------------------------
Max deviations: **** * ** ** +** +** +* * +** +** +** * ****
-----------------------------------------------------------------------------------------------------------------------------------
Residue-by-residue listing for refined_15 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 1.269 1.352 1.310 .015
**** +* *
C-N (Pro) 1.341 .016 7 1.330 1.354 1.342 .009
C-O C-O 1.231 .020 172 1.204 1.252 1.232 .008
* *
CA-C CH1E-C (except Gly) 1.525 .021 161 1.485 1.568 1.519 .015
+* **
CH2G*-C (Gly) 1.516 .018 12 1.476 1.517 1.501 .009
**
CA-CB CH1E-CH3E (Ala) 1.521 .033 4 1.502 1.523 1.512 .007
CH1E-CH1E (Ile,Thr,Val) 1.540 .027 29 1.527 1.585 1.558 .013
+*
CH1E-CH2E (the rest) 1.530 .020 128 1.499 1.577 1.536 .013
+* **
N-CA NH1-CH1E (except Gly,Pro)1.458 .019 154 1.408 1.497 1.447 .016
+** **
NH1-CH2G* (Gly) 1.451 .016 12 1.417 1.464 1.440 .012
**
N-CH1E (Pro) 1.466 .015 7 1.455 1.491 1.466 .012
+*
-------------------------------------------------------------------------------------------------------------
Residue-by-residue listing for refined_15 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 2.0 153 113.12 118.95 116.32 1.05
+* *
CH2G*-C-NH1 (Gly) 116.4 2.1 12 113.79 116.91 115.98 .94
*
CH1E-C-N (Pro) 116.9 1.5 7 115.65 117.55 116.51 .74
O-C-N O-C-NH1 (except Pro) 123.0 1.6 165 121.58 124.94 123.05 .60
*
O-C-N (Pro) 122.0 1.4 7 122.15 123.53 122.84 .48
*
C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 154 117.18 126.57 122.21 1.48
+** +**
C-NH1-CH2G* (Gly) 120.6 1.7 11 118.24 122.29 120.08 1.10
*
C-N-CH1E (Pro) 122.6 5.0 7 122.18 124.09 122.86 .57
CA-C-O CH1E-C-O (except Gly) 120.8 1.7 160 118.85 121.97 120.63 .62
*
CH2G*-C-O (Gly) 120.8 2.1 12 120.00 121.87 120.63 .56
CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 4 109.74 111.21 110.27 .56
CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 29 105.96 112.87 109.63 1.69
* +*
CH2E-CH1E-C (the rest) 110.1 1.9 128 105.01 115.80 110.64 1.47
+** +**
N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 154 103.09 116.65 110.16 2.17
+** +*
NH1-CH2G*-C (Gly) 112.5 2.9 12 110.85 115.11 112.40 1.41
N-CH1E-C (Pro) 111.8 2.5 7 109.26 114.01 112.37 1.40
*
N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 4 109.53 112.01 110.70 .95
*
NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 29 109.14 114.16 111.62 1.18
* +*
N-CH1E-CH2E (Pro) 103.0 1.1 7 101.83 104.25 103.24 .74
* *
NH1-CH1E-CH2E (the rest) 110.5 1.7 121 105.58 115.36 110.86 1.78
+** +**
-------------------------------------------------------------------------------------------------------------
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_15 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] 135 88.2%
Residues in additional allowed regions [a,b,l,p] 13 8.5%
Residues in generously allowed regions [~a,~b,~l,~p] 3 2.0%
Residues in disallowed regions [XX] 2 1.3%
---- ------
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 88.2 83.8 10.0 .4 Inside
b. Omega angle st dev 172 3.9 6.0 3.0 -.7 Inside
c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside
d. Zeta angle st dev 161 2.2 3.1 1.6 -.6 Inside
e. H-bond energy st dev 101 .9 .8 .2 .5 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 24 7.4 18.1 6.5 -1.7 BETTER
b. Chi-1 trans st dev 57 7.4 19.0 5.3 -2.2 BETTER
c. Chi-1 gauche plus st dev 69 8.3 17.5 4.9 -1.9 BETTER
d. Chi-1 pooled st dev 150 8.7 18.2 4.8 -2.0 BETTER
e. Chi-2 trans st dev 42 5.4 20.4 5.0 -3.0 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% 88.2 1
Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.5 1
H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .93 3
Residue-by-residue listing for refined_15 Page 17
----------------------------------------
G - F A C T O R S
Average
Parameter Score Score
--------- ----- -----
Dihedral angles:-
Phi-psi distribution -.42
Chi1-chi2 distribution -.31
Chi1 only .12
Chi3 & chi4 .39
Omega -.08
------ -.16
=====
Main-chain covalent forces:-
Main-chain bond lengths -.03
Main-chain bond angles .35
------ .19
=====
OVERALL AVERAGE -.04
=====
Ideally, scores should be above -0.5. Values below -1.0 may need investigation.