Residue-by-residue listing for refined_19 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 ASP 1 t - - 184.8 - - - - - - - - 181.1 - 34.5 -
2 PRO 2 T - - - - - -54.5 - - - - - 182.1 - 37.8 -
* *
3 ASN 3 T l - 181.6 - - - - - - - - 181.3 - 33.5 -
4 ALA 4 t b - - - - - - - - - - 181.6 -2.4 34.0 -
5 GLU 5 B 52.5 - - 184.8 - - - - - - 180.9 - 33.1 -
6 PHE 6 B - - -53.2 - - - - - - - 177.2 - 34.3 -
7 ASP 7 B - 185.1 - - - - - - - - 184.1 -.6 35.8 -
+* +*
8 PRO 8 S - - - - - -65.1 - - - - - 178.1 - 36.8 -
9 ASP 9 S A - 186.1 - - - - - - - - 181.9 - 34.0 -
10 LEU 10 g B - - -74.3 - - - - - - - 177.2 - 33.7 -
11 PRO 11 G - - - - - -62.0 - - - - - 180.8 - 38.0 -
* *
12 GLY 12 G - - - - - - - - - - - 182.5 - - -
13 GLY 13 G - - - - - - - - - - - 182.9 -2.1 - -
14 GLY 14 G - - - - - - - - - - - 182.7 -1.7 - -
15 LEU 15 g A - - -62.1 179.7 - - - - - - 178.5 -2.1 34.9 -
16 HIS 16 e B - - -55.7 - - - - - - - 181.4 -.5 34.3 -
** **
17 ARG 17 E B 54.8 - - 176.9 - - - - - - 171.9 - 34.5 -
* *
18 CYS 18 E B - 169.8 - - - - - - - - 184.9 -1.6 33.3 -
19 LEU 19 T A - 183.6 - - - - - - - - 180.7 -.7 35.6 -
+* +*
20 ALA 20 T A - - - - - - - - - - 179.4 - 34.0 -
21 CYS 21 T A - - -65.5 - - - - - - - 179.9 - 30.7 -
22 ALA 22 T l - - - - - - - - - - 182.7 -1.6 33.0 -
Residue-by-residue listing for refined_19 Page 2
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...................................................................................................................................
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
-----------------------------------------------------------------------------------------------------------------------------------
23 ARG 23 E B - - -62.3 - - - - - - - 180.0 -.8 35.4 -
+* +*
24 TYR 24 E B - - -55.7 - - - - - - - 182.4 - 37.3 -
25 PHE 25 e B - - -58.3 - - - - - - - 182.3 -3.2 34.9 -
+* +*
26 ILE 26 S A 55.8 - - 178.0 - - - - - - 183.8 - 33.0 -
27 ASP 27 h B - 187.6 - - - - - - - - 180.7 - 34.7 -
28 SER 28 H A - 178.5 - - - -65.1 -27.5 - - - 177.1 - 33.9 -
* *
29 THR 29 H A 46.5 - - - - -60.3 -44.5 - - - 176.6 - 35.8 -
* *
30 ASN 30 H A - - -78.2 - - -60.4 -43.3 - - - 176.1 - 33.0 -
31 LEU 31 H A - - -87.6 - - -61.9 -54.5 - - - 182.2 -1.4 34.6 -
* * *
32 LYS 32 H A - 185.0 - 173.6 - -60.6 -36.2 - - - 175.8 -3.2 31.5 -
+* +*
33 THR 33 H A - - -55.9 - - -71.9 -34.0 - - - 176.4 -2.5 34.2 -
34 HIS 34 H A - 164.3 - - - -64.3 -37.5 - - - 182.1 -2.1 33.1 -
* *
35 PHE 35 h A - - -51.0 - - - - - - - 178.8 -2.2 32.8 -
* *
36 ARG 36 T A - - -63.1 183.7 - - - - - - 174.3 -1.0 31.7 -
* *
37 SER 37 h B - 180.9 - - - - - - - - 177.7 -.9 35.0 -
* *
38 LYS 38 H A - 178.6 - 181.2 - -60.9 -38.0 - - - 178.1 -.9 34.9 -
+* +*
39 ASP 39 H A - 181.2 - - - -59.9 -37.4 - - - 180.6 - 35.8 -
40 HIS 40 H A - 184.3 - - - -70.8 -45.5 - - - 181.6 - 35.5 -
41 LYS 41 H A - - -58.1 192.4 - -71.6 -28.1 - - - 168.9 -2.1 28.1 -
+* +* +*
42 LYS 42 H A - 176.0 - 182.9 - -62.1 -44.5 - - - 175.6 -2.3 34.7 -
43 ARG 43 H A - 168.3 - - - -54.1 -33.9 - - - 180.4 -2.0 35.5 -
44 LEU 44 H A - - -65.4 179.7 - -68.3 -38.0 - - - 177.6 -1.4 34.1 -
45 LYS 45 H A - - -62.5 182.1 - -73.3 -30.9 - - - 176.0 -1.3 32.7 -
* *
46 GLN 46 H A - - -62.4 179.9 - -69.9 -45.4 - - - 179.3 -2.0 34.7 -
47 LEU 47 H A - 183.3 - - - -71.7 -18.6 - - - 177.2 -3.0 34.6 -
+* * +*
48 SER 48 h ~l - - -58.3 - - - - - - - 176.5 -.9 30.7 -
** * **
49 VAL 49 A - 179.5 - - - - - - - - 180.1 - 35.1 -
50 GLU 50 ~l - 179.5 - 190.3 - - - - - - 175.4 - 33.2 -
** **
51 PRO 51 - - - - - -63.8 - - - - - 180.6 - 38.8 -
* *
52 TYR 52 B 49.3 - - - - - - - - - 183.1 - 31.3 -
53 SER 53 b - - -55.3 - - - - - - - 180.7 - 35.4 -
54 GLN 54 S ~p - 193.9 - 180.2 - - - - - - 178.9 - 32.7 -
** **
55 GLU 55 S XX - 185.6 - - - - - - - - 178.6 - 32.4 -
**** ****
56 GLU 56 S A - - -65.6 183.5 - - - - - - 176.1 -3.1 33.9 -
* *
57 ALA 57 B - - - - - - - - - - 182.9 - 33.6 -
58 GLU 58 A - - -59.3 178.7 - - - - - - 179.1 - 34.4 -
59 ARG 59 B 60.8 - - 179.5 - - - - - - 177.1 - 33.5 -
Residue-by-residue listing for refined_19 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
-----------------------------------------------------------------------------------------------------------------------------------
60 ALA 60 A - - - - - - - - - - 179.6 - 34.4 -
61 ALA 61 a - - - - - - - - - - 179.7 - 33.8 -
62 GLY 62 - - - - - - - - - - - 180.4 - - -
63 MET 63 B - 178.0 - 179.8 - - - - - - 177.3 - 33.5 -
64 GLY 64 - - - - - - - - - - - 180.8 -.5 - -
** **
65 SER 65 l - - -55.3 - - - - - - - 186.8 - 32.5 -
* *
66 TYR 66 B 48.8 - - - - - - - - - 179.3 - 33.9 -
67 VAL 67 - - 181.9 - - - - - - - - - - 34.0 -
-----------------------------------------------------------------------------------------------------------------------------------
Max deviations: **** * * * +* +* ** +* ****
-----------------------------------------------------------------------------------------------------------------------------------
Mean values: 52.6 180.8 -62.0 181.5 -61.3 -65.1 -37.5 - - - 179.5 -1.7 34.1
Standard deviations: 4.9 6.5 8.6 4.5 4.7 5.7 8.5 - - - 3.1 .8 1.8
Numbers of values: 7 23 22 18 4 17 17 0 0 0 66 29 62 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_19 Page 4
----------------------------------------
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 ASP 1 - 1.233 1.528 1.547 1.464 - 119.58 119.05 112.12 107.82 109.15 121.28
+* * * * * +*
2 PRO 2 1.362 1.242 1.522 1.509 1.465 122.18 114.52 121.27 109.53 112.97 105.11 124.21
* * +* +* +* +*
3 ASN 3 1.325 1.233 1.560 1.525 1.467 125.37 115.70 122.23 113.00 111.58 108.00 121.97
+* ** +* * **
4 ALA 4 1.307 1.240 1.518 1.520 1.429 123.02 115.03 121.66 111.87 109.06 109.76 123.13
+* +* +*
5 GLU 5 1.303 1.228 1.500 1.512 1.422 122.61 115.61 121.15 111.49 111.96 110.44 123.23
+* * +* +*
6 PHE 6 1.301 1.236 1.507 1.552 1.444 121.10 115.63 120.66 109.99 109.70 111.33 123.71
** * **
7 ASP 7 1.302 1.227 1.505 1.538 1.444 123.52 118.86 119.19 109.27 105.74 110.64 121.95
+* * * +* +*
8 PRO 8 1.328 1.235 1.541 1.531 1.467 122.18 118.20 119.98 111.53 115.18 104.12 121.82
* * *
9 ASP 9 1.319 1.238 1.517 1.522 1.461 119.65 115.57 121.37 109.84 109.93 111.28 123.02
* *
10 LEU 10 1.311 1.227 1.511 1.539 1.449 122.07 117.38 120.54 108.97 111.17 112.51 122.07
* * *
11 PRO 11 1.324 1.245 1.525 1.531 1.457 122.69 115.63 120.96 110.90 111.06 104.20 123.31
* * *
Residue-by-residue listing for refined_19 Page 5
----------------------------------------
...................................................................................................................................
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 GLY 12 1.331 1.233 1.502 - 1.447 121.27 115.50 120.59 - 110.93 - 123.88
13 GLY 13 1.340 1.224 1.504 - 1.449 122.65 115.86 120.84 - 111.91 - 123.30
* *
14 GLY 14 1.325 1.230 1.531 - 1.435 120.70 116.63 120.51 - 112.19 - 122.86
15 LEU 15 1.335 1.223 1.519 1.523 1.449 122.55 116.69 120.97 109.53 111.79 109.83 122.33
16 HIS 16 1.300 1.235 1.495 1.540 1.444 121.41 116.43 120.56 108.90 107.85 112.79 122.95
** * * * **
17 ARG 17 1.294 1.229 1.493 1.513 1.423 121.05 114.11 122.01 108.73 113.10 110.97 123.86
** +* +* * **
18 CYS 18 1.289 1.236 1.508 1.544 1.426 122.20 116.16 120.11 111.80 107.15 111.81 123.73
+** +* * +**
19 LEU 19 1.307 1.230 1.516 1.520 1.441 123.75 115.66 120.93 110.29 111.08 108.33 123.40
+* * * +*
20 ALA 20 1.309 1.224 1.521 1.499 1.461 122.07 117.05 120.71 109.54 112.20 110.61 122.24
* *
21 CYS 21 1.313 1.232 1.505 1.544 1.445 119.91 115.54 120.66 112.95 112.10 112.27 123.81
* * * *
22 ALA 22 1.340 1.231 1.531 1.531 1.469 124.39 116.02 121.11 111.05 111.47 111.01 122.77
* *
23 ARG 23 1.308 1.241 1.488 1.540 1.435 122.28 115.53 120.56 108.58 108.58 111.35 123.91
+* +* * +*
24 TYR 24 1.288 1.234 1.508 1.519 1.397 123.15 117.39 120.06 109.03 106.29 108.43 122.54
+** *** +* * ***
25 PHE 25 1.290 1.229 1.498 1.523 1.437 120.78 115.96 120.57 108.58 109.09 111.69 123.46
+** * * +**
26 ILE 26 1.308 1.226 1.541 1.542 1.432 122.96 118.41 119.82 110.24 114.08 111.05 121.76
+* * * * +*
27 ASP 27 1.329 1.230 1.531 1.541 1.465 119.30 116.69 120.19 110.56 110.80 109.42 123.12
* *
28 SER 28 1.334 1.230 1.526 1.547 1.464 123.69 117.40 119.61 111.21 111.55 109.68 122.99
* *
29 THR 29 1.331 1.229 1.515 1.513 1.415 122.03 114.54 121.59 109.81 110.01 108.90 123.86
* ** +* **
30 ASN 30 1.306 1.212 1.505 1.521 1.420 124.02 116.86 120.16 112.42 111.65 109.81 122.96
+* +* * * +*
31 LEU 31 1.319 1.225 1.480 1.515 1.462 121.27 115.19 120.82 107.91 112.42 111.65 123.98
** * **
32 LYS 32 1.281 1.237 1.538 1.531 1.456 121.75 116.49 120.58 112.57 111.86 111.31 122.92
*** * ***
33 THR 33 1.325 1.237 1.542 1.535 1.449 121.92 115.13 121.65 110.82 109.67 110.25 123.20
34 HIS 34 1.317 1.240 1.539 1.565 1.447 123.52 117.68 120.31 111.58 112.17 110.47 122.01
+* * +*
35 PHE 35 1.327 1.214 1.523 1.532 1.458 119.54 117.71 120.19 108.48 111.50 113.79 122.08
* +* +*
36 ARG 36 1.330 1.228 1.527 1.530 1.462 120.52 115.70 121.22 111.60 111.14 112.31 123.08
* *
37 SER 37 1.312 1.246 1.533 1.540 1.428 122.65 115.77 120.92 110.40 108.80 109.96 123.27
* +* +*
38 LYS 38 1.320 1.229 1.518 1.502 1.450 122.99 115.15 121.19 110.42 110.02 109.16 123.61
* *
39 ASP 39 1.327 1.233 1.525 1.530 1.463 123.33 115.11 121.70 109.55 109.91 108.96 123.16
40 HIS 40 1.320 1.217 1.473 1.511 1.460 122.36 115.68 120.99 107.58 111.04 111.14 123.26
** * **
41 LYS 41 1.267 1.226 1.525 1.501 1.408 119.63 116.38 120.97 115.88 111.64 112.63 122.65
**** * +** * *** * ****
Residue-by-residue listing for refined_19 Page 6
----------------------------------------
...................................................................................................................................
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 LYS 42 1.321 1.233 1.534 1.513 1.446 121.20 115.61 120.93 109.29 108.74 111.08 123.44
43 ARG 43 1.347 1.219 1.520 1.535 1.470 123.37 115.42 121.01 110.08 110.51 108.76 123.56
* * *
44 LEU 44 1.301 1.217 1.514 1.518 1.427 123.04 116.58 120.72 111.09 111.13 109.75 122.69
+* +* +*
45 LYS 45 1.313 1.231 1.529 1.535 1.452 121.19 115.91 120.96 111.88 110.08 111.21 123.10
* *
46 GLN 46 1.329 1.234 1.525 1.528 1.462 122.25 115.49 121.26 109.25 109.96 110.84 123.24
47 LEU 47 1.327 1.235 1.528 1.523 1.459 123.24 114.53 121.01 110.66 110.06 109.45 124.45
48 SER 48 1.335 1.233 1.521 1.527 1.449 125.51 114.87 121.69 112.42 113.32 111.98 123.43
** * **
49 VAL 49 1.322 1.233 1.515 1.559 1.448 123.01 114.83 120.75 109.14 108.60 111.26 124.40
50 GLU 50 1.343 1.235 1.527 1.545 1.460 124.06 117.68 120.78 110.10 110.84 112.11 121.52
* *
51 PRO 51 1.332 1.238 1.524 1.542 1.454 122.00 116.23 120.41 110.34 109.87 103.91 123.31
52 TYR 52 1.320 1.247 1.523 1.547 1.454 122.48 115.24 121.28 112.51 112.30 111.70 123.46
* *
53 SER 53 1.307 1.237 1.513 1.534 1.439 122.59 115.78 120.13 109.75 108.99 109.85 124.01
+* * +*
54 GLN 54 1.334 1.241 1.563 1.563 1.463 124.07 117.56 119.69 113.24 108.85 110.28 122.62
+* +* * +* +*
55 GLU 55 1.340 1.228 1.523 1.549 1.480 125.51 114.88 121.67 111.66 110.11 111.80 123.41
* ** **
56 GLU 56 1.291 1.231 1.510 1.529 1.443 123.01 115.24 121.47 110.72 109.28 110.99 123.29
+** +**
57 ALA 57 1.304 1.220 1.503 1.525 1.431 122.35 115.96 120.84 111.41 107.57 111.36 123.05
+* * * * +*
58 GLU 58 1.306 1.229 1.510 1.521 1.442 121.65 116.03 120.71 109.87 110.73 110.51 123.26
+* +*
59 ARG 59 1.313 1.242 1.525 1.543 1.446 121.59 115.95 121.13 110.51 110.75 111.28 122.89
* *
60 ALA 60 1.301 1.233 1.507 1.516 1.436 121.43 115.28 121.06 110.53 108.53 110.59 123.62
+* * +*
61 ALA 61 1.319 1.233 1.507 1.527 1.447 123.35 115.04 121.12 110.66 108.95 111.21 123.80
62 GLY 62 1.299 1.225 1.500 - 1.434 121.71 116.42 120.36 - 111.19 - 123.21
** * **
63 MET 63 1.315 1.238 1.521 1.537 1.455 121.89 115.82 121.06 110.20 111.48 111.25 123.11
* *
64 GLY 64 1.308 1.226 1.505 - 1.432 121.20 115.89 120.18 - 110.70 - 123.89
+* * +*
65 SER 65 1.331 1.232 1.536 1.530 1.459 123.80 115.72 121.63 111.84 110.83 111.07 122.60
* *
66 TYR 66 1.302 1.234 1.526 1.528 1.418 122.74 116.05 120.82 111.90 112.48 108.85 123.12
+* ** **
67 VAL 67 1.314 - 1.516 1.559 1.441 122.36 - - 109.95 108.59 112.18 -
* *
-----------------------------------------------------------------------------------------------------------------------------------
Max deviations: **** ** +* *** ** +* * *** +* +* +* ****
-----------------------------------------------------------------------------------------------------------------------------------
Residue-by-residue listing for refined_19 Page 7
----------------------------------------
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 62 1.267 1.347 1.315 .016
**** *
C-N (Pro) 1.341 .016 4 1.324 1.362 1.337 .015
* *
C-O C-O 1.231 .020 66 1.212 1.247 1.231 .007
CA-C CH1E-C (except Gly) 1.525 .021 62 1.473 1.563 1.519 .016
** +*
CH2G*-C (Gly) 1.516 .018 5 1.500 1.531 1.508 .012
CA-CB CH1E-CH3E (Ala) 1.521 .033 6 1.499 1.531 1.520 .011
CH1E-CH1E (Ile,Thr,Val) 1.540 .027 5 1.513 1.559 1.541 .017
*
CH1E-CH2E (the rest) 1.530 .020 51 1.501 1.565 1.531 .014
* +*
N-CA NH1-CH1E (except Gly,Pro)1.458 .019 58 1.397 1.480 1.446 .017
*** *
NH1-CH2G* (Gly) 1.451 .016 5 1.432 1.449 1.439 .007
*
N-CH1E (Pro) 1.466 .015 4 1.454 1.467 1.461 .005
-------------------------------------------------------------------------------------------------------------
Residue-by-residue listing for refined_19 Page 8
----------------------------------------
+-----------------+
| 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 57 114.11 119.58 116.06 1.09
* +*
CH2G*-C-NH1 (Gly) 116.4 2.1 5 115.50 116.63 116.06 .41
CH1E-C-N (Pro) 116.9 1.5 4 114.52 118.20 116.15 1.34
+*
O-C-N O-C-NH1 (except Pro) 123.0 1.6 62 121.28 124.45 123.10 .67
*
O-C-N (Pro) 122.0 1.4 4 121.82 124.21 123.16 .86
+*
C-N-CA C-NH1-CH1E (except Gly,Pro)121.7 1.8 57 119.30 125.51 122.42 1.40
* **
C-NH1-CH2G* (Gly) 120.6 1.7 5 120.70 122.65 121.50 .65
*
C-N-CH1E (Pro) 122.6 5.0 4 122.00 122.69 122.26 .26
CA-C-O CH1E-C-O (except Gly) 120.8 1.7 61 119.05 122.23 120.83 .63
*
CH2G*-C-O (Gly) 120.8 2.1 5 120.18 120.84 120.50 .22
CB-CA-C CH3E-CH1E-C (Ala) 110.5 1.5 6 109.54 111.87 110.84 .73
CH1E-CH1E-C (Ile,Thr,Val) 109.1 2.2 5 109.14 110.82 109.99 .55
CH2E-CH1E-C (the rest) 110.1 1.9 51 107.58 115.88 110.64 1.58
* ***
N-CA-C NH1-CH1E-C (except Gly,Pro)111.2 2.8 58 105.74 114.08 110.32 1.72
+* *
NH1-CH2G*-C (Gly) 112.5 2.9 5 110.70 112.19 111.38 .57
N-CH1E-C (Pro) 111.8 2.5 4 109.87 115.18 112.27 2.01
*
N-CA-CB NH1-CH1E-CH3E (Ala) 110.4 1.5 6 109.76 111.36 110.76 .53
NH1-CH1E-CH1E (Ile,Thr,Val) 111.5 1.7 5 108.90 112.18 110.73 1.10
+*
N-CH1E-CH2E (Pro) 103.0 1.1 4 103.91 105.11 104.33 .46
+* *
NH1-CH1E-CH2E (the rest) 110.5 1.7 47 108.00 113.79 110.72 1.30
* +*
-------------------------------------------------------------------------------------------------------------
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_19 Page 9
----------------------------------------
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] 46 82.1%
Residues in additional allowed regions [a,b,l,p] 6 10.7%
Residues in generously allowed regions [~a,~b,~l,~p] 3 5.4%
Residues in disallowed regions [XX] 1 1.8%
---- ------
Number of non-glycine and non-proline residues 56 100.0%
Number of end-residues (excl. Gly and Pro) 2
Number of glycine residues 5
Number of proline residues 4
----
Total number of residues 67
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 56 82.1 83.8 10.0 -.2 Inside
b. Omega angle st dev 66 3.1 6.0 3.0 -1.0 Inside
c. Bad contacts / 100 residues 0 .0 4.2 10.0 -.4 Inside
d. Zeta angle st dev 62 1.8 3.1 1.6 -.8 Inside
e. H-bond energy st dev 29 .8 .8 .2 .1 Inside
f. Overall G-factor 67 .1 -.4 .3 1.5 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 7 4.9 18.1 6.5 -2.0 BETTER
b. Chi-1 trans st dev 23 6.5 19.0 5.3 -2.4 BETTER
c. Chi-1 gauche plus st dev 22 8.6 17.5 4.9 -1.8 BETTER
d. Chi-1 pooled st dev 52 9.1 18.2 4.8 -1.9 BETTER
e. Chi-2 trans st dev 18 4.5 20.4 5.0 -3.2 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% 82.1 1
Chi-1 st.dev. 18.2 6.2 <12.0 <18.2 <24.4 >24.4 9.8 1
H-bond energy st dev .87 .24 < .63 < .87 <1.11 >1.11 .89 3
Residue-by-residue listing for refined_19 Page 10
----------------------------------------
G - F A C T O R S
Average
Parameter Score Score
--------- ----- -----
Dihedral angles:-
Phi-psi distribution -.50
Chi1-chi2 distribution -.03
Chi1 only .30
Chi3 & chi4 .48
Omega .15
------ -.03
=====
Main-chain covalent forces:-
Main-chain bond lengths .06
Main-chain bond angles .39
------ .25
=====
OVERALL AVERAGE .07
=====
Ideally, scores should be above -0.5. Values below -1.0 may need investigation.