MolProbity Ramachandran analysis

(4F7W_rama.pdf)
MolProbity Ramachandran analysis
201302211713_refmac1.pdb, model 1
General case
180
Glycine
180
Psi
Psi
0
0
-180
-180
-180
0
Phi
180
Proline
180
-180
Psi
0
0
-180
Phi
180
Phi
180
Pre-proline
180
Psi
0
-180
-180
0
Phi
180
-180
0
97.8% (2392/2447) of all residues were in favored (98%) regions.
100.0% (2447/2447) of all residues were in allowed (>99.8%) regions.
There were no outliers.
http://kinemage.biochem.duke.edu
Lovell, Davis, et al. Proteins 50:437 (2003)
(4GI7_rama.pdf)
MolProbity Ramachandran analysis
201302211747_refmac2.pdb, model 1
General case
180
Glycine
180
Psi
Psi
0
0
-180
-180
-180
0
Phi
180
Proline
180
-180
Psi
0
0
-180
Phi
180
Phi
180
Pre-proline
180
Psi
0
-180
-180
0
Phi
180
-180
0
97.8% (2386/2440) of all residues were in favored (98%) regions.
100.0% (2440/2440) of all residues were in allowed (>99.8%) regions.
There were no outliers.
http://kinemage.biochem.duke.edu
Lovell, Davis, et al. Proteins 50:437 (2003)
2/25/13
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1.38
100th percentile* (N=576, 2.10Å ± 0.25Å)
All­Atom Clashscore, all atoms:
Contacts Clashscore is the number of serious steric overlaps (> 0.4 Å) per 1000 atoms.
Poor rotamers
1.90%
Goal: <1%
Ramachandran outliers
0.00%
Goal: <0.2%
Ramachandran favored
Protein
Cβ deviations >0.25Å
Geometry
MolProbity score^
97.74% Goal: >98%
1
Goal: 0
1.14
100th percentile* (N=11758, 2.10Å ± 0.25Å)
Residues with bad bonds:
0.00%
Goal: 0%
Residues with bad angles:
0.04%
Goal: <0.1%
* 100th percentile is the best among structures of comparable resolution; 0th percentile is the worst. ^ MolProbity score is defined as the following: 0.42574*log(1+clashscore) + 0.32996*log(1+max(0,pctRotOut­1)) +
0.24979*log(1+max(0,100­pctRamaFavored­2)) + 0.5
#
Res
High Clash >
Ramachandran
B
0.4Å
Avg: Clashscore: Outliers: 0 of
29.59
1.38
2439
0.546Å
Favored
(64.98%)
146 HOH O
General case /
­70.8,­21.8
A1024 ARG 51.79 NH1 with J
A1038 ARG 58.54
A1246 LYS 42.3
­
­
0.752Å
A1258 TYR 50.24 CE1 with
A1291 LEU 22.65
Cβ
Bond
Bond angles.
deviation lengths.
Outliers:
Poor rotamers: 42 of Outliers:
Outliers: 1 of
0 of
2211
1 of 2361
2459
2459
Rotamer
20.6% (ptt­85)
chi angles:
86.4,197.1,174.9,285.2
Favored (70.6%)
0%
General case /
­57.6,­51.8
chi angles:
237.7,248.8,238,190.8
Favored
(73.47%)
0.9%
General case /
­71.6,­40.2
Favored
(63.38%)
A1318 RNH
CAA
General case /
­57.0,­28.1
0.429Å
Favored
(15.68%)
chi angles:
304.1,234.9,73.7,235
30.6% (t80)
chi angles: 195.8,90.8
32.4% (tp)
N with
A1292 PRO
CD
Pre­proline /
­60.7,­34.9
chi angles: 183.2,53.7
0.429Å
Favored
85.3% (Cg_exo)
0.121Å
­
­
0.068Å
­
­
0.04Å
­
­
0.047Å
­
­
0.048Å
­
­
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A1292 PRO 20.23
Viewing 201302211713_refmac1-multi.table - MolProbity
0.429Å
CD with
A1291 LEU
N
Favored
(32.12%)
85.3% (Cg_exo)
0.028Å
­
­
­
­
­
0.062Å
­
­
0.033Å
­
­
0.071Å
­
­
0.026Å
­
­
0.041Å
­
­
chi angles:
283.4,293.3,188.7,181.2
0.032Å
­
­
­
0.031Å
­
­
0.095Å
­
­
0.109Å
­
­
0.07Å
­
­
0.038Å
­
­
chi angles: 331.1
Proline /
­66.3,­12.3
0.752Å
A1318 RNH 35.63
CAA with
A1258 TYR
CE1
0.457Å
C1024 ARG 47.79
NH1 with
C1025 ASP
OD1
C1025 ASP 22.57
OD1 with
C1024 ARG
NH1
0.457Å
C1060 ARG 19.69
C1134 SER 44.94
C1143 LYS 42.95
­
­
­
0.403Å
C1164 LYS 20.16
C1191 ALA 35.91
C1192 GLN 49.51
NZ with
C1224 ASP
OD2
­
Favored
(98.94%)
60.4% (ttp85)
General case /
­63.8,­41.2
Favored (44%)
General case /
­87.9,1.9
Favored
(80.04%)
General case /
­69.5,­39.9
Favored
(60.93%)
General case /
­50.9,­45.5
Favored
(35.44%)
General case /
­85.3,3.0
Favored
(17.46%)
General case /
­77.9,1.8
0.404Å Favored (7.16%)
O with
C1192 GLN
C
General case /
­130.0,101.5
0.404Å Favored (3.42%)
C with
C1191 ALA
O
C1196 LEU 21.51
­
C1224 ASP 13.71
OD2 with
C1164 LYS
NZ
0.403Å
0.43Å
C1258 TYR 51.2
­
chi angles:
170.1,181.6,59.1,80
98% (m­20)
chi angles: 289.8,161.9
0%
chi angles:
196.6,274,165.1,282.4
0.6%
chi angles: 104.6
0.1%
chi angles:
258.6,71.4,106,166.2
67.7% (mmtt)
30.4% (mt­30)
Pre­proline /
37.5,60.3
chi angles:
315.4,194.3,296.2
Favored
(57.83%)
0.6%
General case /
­122.6,123.2
Favored
(32.31%)
General case /
­80.6,­39.2
Favored
(61.59%)
CD2 with
C1318 RNH
General case /
CAA
­64.8,­15.3
chi angles: 182.8,113.2
13.5% (m­20)
chi angles: 297,93.5
1.9% (t80)
chi angles: 215.9,67.5
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CAA
­64.8,­15.3
0.43Å
C1318 RNH 42.36
CAA with
C1258 TYR
CD2
­
B1008 LEU 54.84
­
­
#
Res
High Clash >
Ramachandran
B
0.4Å
Avg: Clashscore: Outliers: 0 of
29.59
1.38
2439
0.421Å
Favored
(57.42%)
O with
G1017 ARG
NH2
General case /
­110.8,135.2
B1034 ASP 76.6
­
Favored
(31.19%)
B1035 GLU 53.56
OE2 with
B1114 ARG
NE
General case /
­52.7,­48.4
­
Favored
(80.18%)
B1014 GLN 46.47
0.451Å
B1040 LYS 64.72
B1060 ARG 52.82
B1085 GLN 72.14
­
­
0.451Å
B1114 ARG 54.46
B1119 ARG 58
B1190 VAL 42.36
General case /
­81.2,­37.4
Favored
(66.34%)
General case /
­60.5,­36.4
Favored
(72.68%)
General case /
­71.7,­41.2
Favored
(44.78%)
General case /
­71.6,148.8
Favored
(52.65%)
NE with
B1035 GLU
OE2
General case /
­87.2,­7.5
­
Favored
(18.11%)
­
General case /
­88.9,­32.0
Favored
(35.84%)
General case /
­108.5,144.0
­
0.3%
chi angles: 43.5,133.3
­
­
­
0.098Å
­
­
Cβ
Bond
Bond angles.
deviation lengths.
Outliers:
Poor rotamers: 42 of Outliers:
Outliers: 1 of
0 of
2211
1 of 2361
2459
2459
Rotamer
5.3% (tt0)
chi angles:
211.4,155.5,292.5
0.9%
chi angles: 274.4,48.8
75.3% (mt­10)
chi angles:
278.5,168.2,177
0.1%
chi angles:
294.6,261.8,110.2,292.3
0%
chi angles:
219.6,272.5,157.8,266.5
0%
chi angles:
52.3,280.8,157.8
0.6%
chi angles:
96.6,218.6,287,277.4
0.2%
chi angles:
324.5,220.6,86.4,119.7
0.9%
chi angles: 137
0.102Å
­
­
0.058Å
­
­
0.067Å
­
­
0.014Å
­
­
0.005Å
­
­
0.064Å
­
­
0.096Å
­
­
0.076Å
­
­
0.124Å
­
­
0.083Å
­
­
0.425Å Favored (9.45%)
B1291 LEU 23.39
N with
Pre­proline /
53.7% (tp)
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B1291 LEU 23.39
B1292 PRO 20.08
D1034 ASP 55.17
D1038 ARG 55.47
N with
B1292 PRO
CD
0.425Å Favored (37.1%)
CD with
B1291 LEU
N
­
­
D1055 TYR 19.84
­
D1060 ARG 17.36
­
0.57Å
D1063 ASN 16.13 ND2 with J
D1067 SER 22.73
Favored
(77.32%)
General case /
­55.8,­45.8
Favored
(73.19%)
General case /
­71.2,­34.5
­
O with
D1142 MET
CE
D1142 MET 40.51
chi angles: 333.1
0.3%
chi angles: 226,77.1
0.2%
chi angles:
263.4,62.7,155.4,70.4
71.7% (m­85)
chi angles: 300.7,110.5
0%
General case /
­65.0,­45.1
Favored
(88.89%)
General case /
­67.1,­39.5
10.1% (t30)
chi angles: 170.6,79
7.6% (t)
chi angles: 196.1
17.3% (mtt180)
chi angles:
285.8,168.8,221.2,121.5
Favored (3.87%)
0%
General case /
­55.4,117.0
chi angles:
19.6,148.9,7.2,103.5
Favored
(78.58%)
84.2% (m­20)
General case /
­59.4,­36.9
Avg: Clashscore: Outliers: 0 of
29.59
1.38
2439
CE with
D1133 ASN
O
75.2% (Cg_exo)
chi angles:
199.7,279.9,165.9,276.5
Favored
(70.04%)
Favored
(92.17%)
General case /
­60.9,­40.1
Favored
0.083Å
­
­
chi angles: 181.3,58.9
General case /
­64.8,­42.8
High Clash >
Ramachandran
B
0.4Å
0.542Å
53.7% (tp)
Favored (96.1%)
Favored
(89.59%)
OG with
D1071 ARG
NH2
0.542Å
Res
General case /
­69.4,­36.4
0.445Å
D1067 SER
OG
#
Favored
(78.83%)
574 HOH O
D1071 ARG 44.03 NH2 with
D1133 ASN 29.8
Proline /
­69.7,­14.8
General case /
­54.5,­40.4
0.445Å
D1086 ARG 70.53
Pre­proline /
­60.9,­32.3
chi angles: 281.3,343.8
1
OUTLIER(S)
0.098Å
­
0.012Å
­
­
0.029Å
­
­
0.259Å
­
­
0.028Å
­
­
0.082Å
­
­
0.034Å
­
­
0.06Å
­
­
0.041Å
­
­
0.08Å
­
­
worst is C­N­
CA: ­4.12
&sigma
Cβ
Bond
Bond angles.
deviation lengths.
Outliers:
Poor rotamers: 42 of Outliers:
Outliers: 1 of
0 of
2211
1 of 2361
2459
2459
Rotamer
14% (mmt)
chi angles:
278.5,292.5,167.5
0.131Å
­
­
0.7%
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D1196 LEU 21.65
Viewing 201302211713_refmac1-multi.table - MolProbity
­
Favored
(63.48%)
General case /
­121.6,132.0
D1259 PHE 49.39
D1310 ASN 31.79
E1037 THR 59.32
E1085 GLN 73.77
E1086 ARG 73.54
­
­
­
­
­
0.414Å
E1136 LEU 35.84
O with
E1141 LEU
N
Favored
(27.46%)
General case /
­92.9,10.0
Favored
(13.27%)
General case /
­117.9,4.2
Favored
(71.27%)
General case /
­69.6,­46.3
Favored
(53.14%)
General case /
­63.3,142.3
Favored
(44.65%)
General case /
­72.8,131.9
Favored
(72.32%)
General case /
­70.3,­32.2
0.414Å Favored (11.8%)
E1141 LEU 33.06
N with
E1136 LEU
O
E1145 LYS 33.63
NZ with
E1175 TYR
OH
General case /
­58.1,128.6
0.462Å
Favored
0.46Å
E1166 GLY 29.73
E1167 VAL 36.28
C with
E1166 GLY
O
0.46Å
E1175 TYR 40.76 OH with
E1145 LYS
NZ
E1233 GLU 54.33
­
0.046Å
­
­
0.072Å
­
­
0.227Å
­
­
0.045Å
­
­
0.041Å
­
­
0.031Å
­
­
0.011Å
­
­
0.019Å
­
­
chi angles:
231.1,175.2,183.1,196.7
0.06Å
­
­
­
­
­
­
27.3% (m)
0.039Å
­
­
0.092Å
­
­
0.086Å
­
­
0.5%
chi angles: 321,68.2
0.1%
chi angles: 57.7,183.9
1%
chi angles: 327.6
0%
chi angles:
322,106.3,127.3
0%
chi angles:
240.5,221.1,207.4,166.5
88.6% (mt)
chi angles: 296,179.6
86% (mt)
General case /
­119.3,19.2
chi angles: 293.1,168.4
Favored
(32.14%)
13.4% (tttt)
O with
(83.25%)
E1167 VAL
Glycine / 87.7,4.0
C
0.462Å
0.7%
chi angles: 189,121.7
Allowed
(1.72%)
Pre­proline /
­40.9,139.3
Favored
(39.31%)
General case /
­106.3,140.6
Favored
(78.87%)
chi angles: 296
51% (t80)
chi angles: 191.4,77.7
0%
General case /
chi angles:
­58.2,­38.8
127.7,174.7,22.9
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E1246 LYS 53.11
E1264 LYS 72.64
E1272 ASP 51.85
E1276 SER 41.23
­
­
­
­
F1030 THR 44.92
­
F1047 SER 27.12
­
#
Res
Favored (84.3%)
0.1%
General case /
­59.4,­47.9
chi angles:
233,149.3,206.2,266.6
Favored
(63.07%)
0%
General case /
­72.4,­21.2
Favored
(90.95%)
General case /
­62.7,­46.3
Favored
(73.53%)
General case /
­71.0,­42.4
Favored
(18.32%)
General case /
­85.9,165.6
Favored (45.5%)
General case /
­71.4,132.7
High Clash >
Ramachandran
B
0.4Å
Avg: Clashscore: Outliers: 0 of
29.59
1.38
2439
F1060 ARG 17.21
­
0.426Å
F1144 LYS 26.62
NZ with
J1066 HOH
O
0.424Å
F1291 LEU 19.75
N with
F1292 PRO
CD
0.424Å
F1292 PRO 18.7
CD with
F1291 LEU
N
G1017 ARG 40.64
NH2 with
B1014 GLN
O
0.421Å
Favored
(83.61%)
General case /
­68.2,­38.1
­
0.9%
chi angles: 259.7,307.2
0.8%
chi angles: 265
0.2%
chi angles: 341.2
0.4%
chi angles: 143.9
0%
chi angles:
200.4,278.2,166,279
71.3% (mmtt)
chi angles:
294.7,287.5,179.9,191.2
Pre­proline /
­58.0,­33.6
Favored
(32.64%)
Proline /
­68.7,­12.4
Favored
(67.88%)
General case /
­56.2,­34.6
(95.53%)
­
0.074Å
­
­
0.021Å
­
­
0.027Å
­
­
0.2Å
­
­
0.027Å
­
­
Cβ
Bond
Bond angles.
deviation lengths.
Outliers:
Poor rotamers: 42 of Outliers:
Outliers: 1 of
0 of
2211
1 of 2361
2459
2459
General case /
­125.8,24.2
Favored
(13.47%)
­
Rotamer
Favored (7.2%)
Favored
G1060 ARG 18.88
chi angles:
177.3,125.4,301.7,88.8
0.034Å
44.7% (tp)
chi angles: 185.1,60.5
44.1% (Cg_exo)
chi angles: 337.5
0.9%
chi angles:
57.4,229.5,293.4,151.4
0.053Å
­
­
0.046Å
­
­
0.068Å
­
­
0.049Å
­
­
0.021Å
­
­
0.043Å
­
­
0%
chi angles:
199.5,276.1,166,276.2
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General case /
­64.9,­43.1
0.422Å
Favored
(76.51%)
935 HOH O
General case /
­58.7,­36.8
0.41Å
Favored
(98.62%)
G1063 ASN 15.52 ND2 with J
G1067 SER 24.19 OG with
G1071 ARG 48.55
G1075 VAL 39.64
G1086 ARG 65.7
chi angles: 192.1
0.41Å
Favored
(77.91%)
2.7% (mtp180)
NH2 with
G1067 SER
OG
General case /
­66.7,­33.3
­
Favored
(94.79%)
­
G1313 ARG 29.97
NH1 with
J1152 HOH
O
0.437Å
0.619Å
H1014 GLN 50.57 OE1 with
General case /
­63.5,­44.8
Favored
(52.35%)
General case /
­59.8,137.5
Favored
(13.38%)
General case /
­85.4,10.4
Favored
(60.57%)
General case /
­115.3,133.3
Favored
(39.97%)
H1311 GLN
NE2
General case /
­98.9,137.4
H1031 LEU 72.52
­
Favored
(15.95%)
H1032 THR 70.61
­
­
0.463Å
H1085 GLN 80.36
10.3% (t)
General case /
­61.7,­42.9
­
H1082 THR 65.02
4.7% (t30)
chi angles: 167.1,87.7
G1071 ARG
NH2
G1143 LYS 43.53
H1047 SER 43.34
199.5,276.1,166,276.2
O with
H1082 THR
CG2
­
General case /
­93.3,158.4
Favored (5.1%)
General case /
­65.1,170.3
Favored
(33.06%)
General case /
­76.2,153.8
Favored
(49.68%)
General case /
­94.2,1.7
chi angles:
254,130.4,41.9,203.6
0.8%
chi angles: 121.5
0%
chi angles:
147.2,281.1,232.5,78
0.4%
chi angles:
323.1,224.8,305.7,150.6
60.9% (mtp180)
chi angles:
291.6,170.4,76.5,212.3
6.3% (mt­30)
chi angles:
296.6,223.5,356
0.8%
chi angles: 320.6,104.2
0.2%
chi angles: 348.1
0%
chi angles: 129
54.4% (m)
chi angles: 294.8
Favored (12.8%)
0.9%
General case /
­57.3,150.6
chi angles:
248.1,61.8,247.5
0.048Å
­
­
0.033Å
­
­
0.031Å
­
­
0.156Å
­
­
0.12Å
­
­
0.014Å
­
­
0.044Å
­
­
0.127Å
­
­
0.047Å
­
­
0.101Å
­
­
0.006Å
­
­
0.046Å
­
­
0.035Å
­
­
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­57.3,150.6
H1133 ASN 38.55
#
Res
0.401Å Favored (90.4%)
CG with
H1142 MET
CE
General case /
­59.0,­43.7
High Clash >
Ramachandran
B
0.4Å
Avg: Clashscore: Outliers: 0 of
29.59
1.38
2439
0.401Å
H1142 MET 49.77
H1196 LEU 24.85
Favored
(67.48%)
CE with
H1133 ASN
CG
General case /
­68.6,­25.0
­
Favored
(58.38%)
9.7% (tpt)
­
0.085Å
­
­
0.097Å
­
­
chi angles:
172,173.3,63.8
0.052Å
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
Favored
(77.73%)
H1014 GLN
OE1
Cβ
Bond
Bond angles.
deviation lengths.
Outliers:
Poor rotamers: 42 of Outliers:
Outliers: 1 of
0 of
2211
1 of 2361
2459
2459
Rotamer
­
0.426Å
H1311 GLN 35.31 NE2 with
­
0.098Å
General case /
­125.0,125.4
General case /
­57.6,­49.5
0.619Å
­
­
422 HOH O
O
0.042Å
­
Favored
(76.96%)
OG1 with
H1275 THR 26.96 J1116 HOH
82.6% (m­20)
chi angles: 285.6,352
0.082Å
0.47Å
H1237 LYS 25.97 NZ with J
248.1,61.8,247.5
chi angles:
202.5,71.7,190.7
0.7%
chi angles: 185.7,121.2
77.9% (tttt)
chi angles:
183.7,176.3,196.4,180.4
61.2% (m)
General case /
­56.2,­42.4
chi angles: 303.8
Favored
(20.64%)
42.8% (tt0)
General case /
­146.4,135.4
0.546Å
J 146 HOH 31.38
O with
A1024 ARG
NH1
0.47Å
J 422 HOH 27.18
O with
H1237 LYS
NZ
0.57Å
J 574 HOH 23.74
O with
D1063 ASN
ND2
0.422Å
J 935 HOH 31.71
O with
G1063 ASN
ND2
0.426Å
J1066 HOH 36.82
O with
F1144 LYS
NZ
0.426Å
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0.426Å
J1116 HOH 26.13
O with
H1275 THR
OG1
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
0.407Å
J1136 HOH 33.97
O with
D1071 ARG
NE
0.437Å
J1152 HOH 28.79
O with
G1313 ARG
NH1
About MolProbity | Website for the Richardson Lab | Internal reference 3.19
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Viewing
201302211713_refmac1_tls­
multi.table
(4F7W_geometry_TLS.pdf)
Hint: Use File | Save As... to save a copy of this page.
When finished, you should close this window .
1.58
100th percentile* (N=576, 2.10Å ± 0.25Å)
All­Atom Clashscore, all atoms:
Contacts Clashscore is the number of serious steric overlaps (> 0.4 Å) per 1000 atoms.
Poor rotamers
1.85%
Goal: <1%
Ramachandran outliers
0.04%
Goal: <0.2%
Ramachandran favored
Protein Cβ deviations >0.25Å
Geometry
MolProbity score^
97.74% Goal: >98%
1
Goal: 0
1.16
100th percentile* (N=11758, 2.10Å ± 0.25Å)
Residues with bad bonds:
0.00%
Goal: 0%
Residues with bad angles:
0.00%
Goal: <0.1%
* 100th percentile is the best among structures of comparable resolution; 0th percentile is the worst. ^ MolProbity score is defined as the following: 0.42574*log(1+clashscore) + 0.32996*log(1+max(0,pctRotOut­1)) +
0.24979*log(1+max(0,100­pctRamaFavored­2)) + 0.5
#
Res
High
Clash > 0.4Å Ramachandran
B
Avg:
29.89
Clashscore:
1.58
Outliers: 1 of
2439
0.45Å
Favored
(68.49%)
HOH O
General case /
­67.6,­25.2
A1024 ARG 57.56 NH1 with J 146
A1038 ARG 56.55
A1184 PRO 48.43
­
­
0.405Å
A1191 ALA 41.41 O with A1192
GLN C
Favored
(79.18%)
General case /
­58.5,­49.1
OUTLIER
(0.15%)
Proline /
­29.0,­65.5
Favored (5%)
General case /
­122.2,95.5
0.405Å
Favored (3.58%)
A1192 GLN 53.34 C with A1191
Pre­proline /
Cβ
Bond Bond
deviation lengths. angles.
Outliers: Outliers:
Poor rotamers: 41 of Outliers:
0 of
0 of
2211
1 of 2361
2459
2459
Rotamer
21.5% (ptt­85)
chi angles:
86.5,195.5,177.2,285.3
0%
chi angles:
237.1,248.8,239.9,188.1
9.4% (Cg_exo)
chi angles: 322.7
­
85.6% (mt­30)
chi angles:
0.132Å
­
­
0.063Å
­
­
0.04Å
­
­
0.04Å
­
­
0.015Å
­
­
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ALA O
39.0,64.2
283.5,167.9,331.2
0.816Å
Favored
(71.05%)
36.8% (t80)
RNH CAA
General case /
­61.5,­29.3
0.423Å
Favored (19.9%)
A1258 TYR 49.47 CE1 with A1318
A1291 LEU 22.36
N with A1292
PRO CD
chi angles: 194.1,88.3
32.4% (tp)
Pre­proline /
­60.7,­35.8
chi angles: 182.1,53.3
0.423Å
Favored
(35.47%)
74.1% (Cg_exo)
LEU N
Proline /
­64.5,­13.6
chi angles: 332.9
­
­
Favored
(99.78%)
62.4% (ttp85)
A1292 PRO 21.45 CD with A1291
0.047Å
­
­
0.052Å
­
­
0.042Å
­
­
­
­
­
0.057Å
­
­
0.044Å
­
­
0.053Å
­
­
0.067Å
­
­
0.114Å
­
­
0.068Å
­
­
0.05Å
­
­
0.026Å
­
­
0.816Å
A1318 RNH 35.82
CAA with
A1258 TYR
CE1
0.567Å
C1024 ARG 45.94
NH1 with
C1025 ASP OD1
C1025 ASP 27.21
OD1 with
C1024 ARG
NH1
General case /
­89.3,2.6
­
Favored
(85.21%)
0.567Å
C1060 ARG 19.98
C1085 GLN 64.81
C1143 LYS 43.32
Favored
(44.38%)
General case /
­68.1,­40.3
0.414Å
Favored
(99.39%)
ARG NH1
General case /
­63.3,­42.3
0.414Å
Favored
(84.35%)
C1067 SER 23.2 OG with C1071
C1071 ARG 39.1
General case /
­63.1,­41.4
NH1 with
C1067 SER OG
­
­
General case /
­68.2,­41.4
Favored
(46.87%)
General case /
­71.4,143.2
Favored
(44.27%)
General case /
­86.8,1.3
0.402Å
Favored
(10.95%)
HOH O
General case /
­120.5,19.6
C1144 LYS 29.16 NZ with J 563
0.426Å
Favored
chi angles:
173.4,181.7,54.4,80.8
99.5% (m­20)
chi angles: 287.8,166.6
0%
chi angles:
198.4,275.9,164.9,277.6
27.6% (t)
chi angles: 185.4
45.4% (mtm­85)
chi angles:
284.8,178.4,312.5,252
0.7%
chi angles:
137.9,176.3,77.3
0.1%
chi angles:
259.3,72.4,102.8,158.4
61.8% (mmtt)
chi angles:
292.6,283.2,164,184.3
69.8% (mmtt)
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C1164 LYS 20.65 NZ with C1224
ASP OD2
(12.98%)
General case /
­75.0,1.1
0.431Å
Favored (7.25%)
C1191 ALA 37.59 O with C1192
General case /
GLN C
0.431Å
C1192 GLN 46.52 C with C1191
ALA O
#
Res
C1196 LEU 20.93
C1224 ASP 15.13
0.02Å
­
­
0.08Å
­
­
chi angles:
313.6,188.9,300.1
­
C1258 TYR 50.26 CD2 with C1318
­
41.5% (mt­30)
Favored
(55.43%)
0.448Å
­
Pre­proline /
39.3,58.8
Outliers: 1 of
2439
OD2 with
C1164 LYS NZ
­
Favored (4%)
Clashscore:
1.58
0.426Å
0.071Å
­129.2,101.4
High
Clash > 0.4Å Ramachandran
B
Avg:
29.89
chi angles:
284.7,294,189,179.9
General case /
­124.6,122.7
Favored
(33.36%)
General case /
­80.2,­39.7
Favored
(64.94%)
Cβ
Bond Bond
deviation lengths. angles.
Outliers: Outliers:
Poor rotamers: 41 of Outliers:
0 of
0 of
2211
1 of 2361
2459
2459
Rotamer
0.7%
chi angles: 183,120.6
15.6% (m­20)
chi angles: 298.1,95.4
1.7% (t80)
General case /
­65.0,­16.9
chi angles: 216.4,65.6
C1318 RNH 38.8
CAA with
C1258 TYR
CD2
­
­
B1008 LEU 55.77
­
­
0.435Å
Favored
(55.93%)
ARG NH2
General case /
­107.4,134.4
RNH CAA
0.087Å
­
­
0.07Å
­
­
0.032Å
­
­
­
­
­
0.078Å
­
­
0.111Å
­
­
0.072Å
­
­
0.063Å
­
­
0.018Å
­
­
0.448Å
B1014 GLN 41.23 O with G1017
B1017 ARG 30.02
­
General case /
­53.0,­41.9
0.5Å
Favored
(62.27%)
ARG NE
General case /
­51.8,­48.7
B1035 GLU 58.2 OE2 with B1114
B1040 LYS 57.5
Favored
(66.79%)
­
Favored
(78.85%)
General case /
­59.5,­36.9
Favored
(78.02%)
0.2%
chi angles: 42.3,136.4
3.4% (tt0)
chi angles:
215.8,156.5,285
0.2%
chi angles:
155.9,162.7,217.4,106.7
64.4% (mt­10)
chi angles:
276.3,164.6,176.9
0%
chi angles:
292.7,257.5,109.5,297.6
0%
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B1060 ARG 46.66
­
B1085 GLN 64.49
­
B1190 VAL 42.54
B1196 LEU 23.19
chi angles:
220.1,272.2,157.8,264.5
Favored (43.2%)
0%
General case /
­73.7,147.0
chi angles:
51,282.3,152.7
0.5Å
Favored
(43.51%)
1.1% (ptm180)
GLU OE2
General case /
­89.7,­9.6
B1114 ARG 55.85 NE with B1035
B1119 ARG 58.9
General case /
­69.9,­41.4
­
­
­
Favored
(22.02%)
General case /
­85.8,­31.3
Favored
(30.95%)
General case /
­104.7,145.0
Favored
(63.12%)
General case /
­119.4,127.4
0.542Å
Favored (3.17%)
B1258 TYR 59.72 CD1 with B1318 General case /
RNH CAA
­47.4,­27.3
chi angles:
92.7,217.7,286.9,277.5
0.1%
chi angles:
330.5,222.4,77.3,134.4
0.9%
chi angles: 136.9
1%
chi angles: 186.7,125.1
13.5% (t80)
chi angles: 202.7,88.1
0.011Å
­
­
0.068Å
­
­
0.114Å
­
­
0.069Å
­
­
0.131Å
­
­
0.011Å
­
­
0.09Å
­
­
0.542Å
B1318 RNH 48.83
D1034 ASP 53.84
D1038 ARG 58.59
D1060 ARG 18.26
#
Res
CAA with
B1258 TYR
CD1
­
­
­
­
­
­
­
­
Favored
(89.49%)
0.2%
0.022Å
­
­
0.05Å
­
­
0.012Å
­
­
General case /
­67.1,­41.0
Favored
(91.41%)
General case /
­59.5,­45.1
Favored
(97.76%)
0%
General case /
­61.5,­43.6
Clashscore:
1.58
Outliers: 1 of
2439
0.555Å
Favored
(71.82%)
D1063 ASN 18.31 ND2 with J 574
HOH O
0.1%
chi angles:
264.3,61.6,157,67
High
Clash > 0.4Å Ramachandran
B
Avg:
29.89
chi angles: 229.8,80.6
General case /
­55.2,­40.0
chi angles:
201.8,277.5,166.6,276.4
Cβ
Bond Bond
deviation lengths. angles.
Outliers: Outliers:
Poor rotamers: 41 of Outliers:
0 of
0 of
2211
1 of 2361
2459
2459
Rotamer
8.5% (t30)
chi angles: 170.1,81.2
0.094Å
­
­
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Viewing 201302211713_refmac1_tls-multi.table - MolProbity
0.533Å
D1067 SER 22.96 OG with D1071
D1071 ARG 36.35
D1086 ARG 62.51
ARG NH2
General case /
­63.9,­44.0
0.533Å
Favored
(97.01%)
NH2 with
D1067 SER OG
­
0.546Å
D1133 ASN 31.41 O with D1142
Favored
(11.17%)
General case /
­61.6,120.1
Favored
(77.66%)
MET CE
0.546Å
Favored
(93.84%)
ASN O
General case /
­60.3,­42.0
­
D1259 PHE 50.31
­
D1310 ASN 30.59
­
E1010 THR 35.46
­
E1038 ARG 76.27
General case /
­65.1,­41.1
General case /
­58.3,­38.0
D1142 MET 40.02 CE with D1133
D1196 LEU 21.09
Favored
(95.73%)
­
E1085 GLN 70.5
­
E1086 ARG 68.21
­
Favored
(63.94%)
General case /
­120.8,130.6
Favored
(22.46%)
General case /
­90.7,10.5
Favored (14.6%)
General case /
­116.4,5.3
Favored (10.2%)
8% (t)
chi angles: 195.5
13.3% (mtt180)
chi angles:
276.7,168.3,227.3,125.8
0%
chi angles:
18.9,146.5,6.1,109.9
83.8% (m­20)
chi angles: 281.8,347.1
11.1% (mmt)
chi angles:
276,297.6,163.4
0.8%
chi angles: 190.6,123.7
0.6%
chi angles: 320.7,68.7
0.1%
chi angles: 58.8,184.5
0.7%
Pre­proline /
­128.8,170.8
chi angles: 93.2
Favored
(18.53%)
0%
General case /
­46.7,­49.3
Favored
(50.25%)
General case /
­66.5,144.2
chi angles:
242.4,197,211.5,73.4
0%
chi angles:
324.5,108.8,123.9
Favored (45.8%)
0%
General case /
­74.6,133.7
chi angles:
244,229.6,220,155.6
0.401Å
Favored
(19.81%)
14.7% (tttt)
TYR OH
General case /
­55.3,126.2
0.488Å
Favored
E1145 LYS 35.69 NZ with E1175
chi angles:
227.6,170.3,186,196.6
0.041Å
­
­
0.074Å
­
­
0.04Å
­
­
0.088Å
­
­
0.159Å
­
­
0.031Å
­
­
0.082Å
­
­
0.211Å
­
­
0.04Å
­
­
0.057Å
­
­
0.041Å
­
­
0.029Å
­
­
0.044Å
­
­
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E1166 GLY 30.55 O with E1167
E1167 VAL 35.6
Glycine / 89.6,1.7
0.488Å
Allowed
(1.08%)
C with E1166
GLY O
0.401Å
E1175 TYR 37.82 OH with E1145
LYS NZ
E1199 GLU 29.8
E1233 GLU 48.2
E1246 LYS 48.98
#
Res
(80.51%)
VAL C
­
­
­
Pre­proline /
­39.5,141.1
Favored
(47.35%)
General case /
­104.5,136.1
Favored
(60.06%)
General case /
­108.0,123.3
Favored
(72.53%)
General case /
­55.0,­41.5
Favored
(81.85%)
General case /
­59.3,­48.6
High
Clash > 0.4Å Ramachandran
B
Avg:
29.89
E1250 GLY 44.7
Clashscore:
1.58
Outliers: 1 of
2439
0.456Å
Allowed
(1.62%)
O with E1253
THR OG1
0.456Å
Favored
(60.21%)
GLY O
General case /
­74.0,­14.3
E1253 THR 45.22 OG1 with E1250
E1264 LYS 58.83
E1272 ASP 43.91
E1276 SER 38.03
Glycine /
­122.7,­102.9
­
­
­
Favored
(56.93%)
General case /
­76.4,­19.2
Favored
(79.97%)
General case /
­61.7,­49.2
Favored
(85.75%)
General case /
­67.4,­43.0
0.4Å
Favored (3.91%)
PRO CD
Pre­proline /
­122.7,174.6
F1010 THR 29.04 CB with F1011
­
21.3% (m)
chi angles: 292.8
49.3% (t80)
chi angles: 191.8,77
0.9%
chi angles:
182.9,264.3,276.1
0%
chi angles:
128.8,174.7,20.7
0%
chi angles:
237.2,153.2,200.4,263.6
­
­
­
0.057Å
­
­
0.097Å
­
­
0.088Å
­
­
0.083Å
­
­
0.021Å
­
­
Cβ
Bond Bond
deviation lengths. angles.
Outliers: Outliers:
Poor rotamers: 41 of Outliers:
0 of
0 of
2211
1 of 2361
2459
2459
Rotamer
­
25.8% (p)
chi angles: 50.5
0%
chi angles:
178.1,126.3,301.4,81.8
0.6%
chi angles: 255.7,309.4
0.5%
chi angles: 263.7
20.8% (p)
chi angles: 73.1
­
­
­
0.115Å
­
­
0.058Å
­
­
0.008Å
­
­
0.055Å
­
­
0.035Å
­
­
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0.4Å
Favored (12%)
F1011 PRO 21.71 CD with F1010
Proline / ­69.0,­2.6
THR CB
0.437Å
Favored
(59.48%)
GLN OE1
General case /
­108.8,122.1
F1014 GLN 34.11 NE2 with F1311
F1030 THR 45.98
F1047 SER
27
F1060 ARG 19.16
F1071 ARG 37.5
­
­
­
­
Favored
(17.04%)
General case /
­88.1,164.6
Favored
(43.86%)
General case /
­77.4,131.8
Favored
(89.84%)
General case /
­66.7,­39.1
Favored
(70.02%)
General case /
­72.8,­34.9
0.405Å
Favored (6.56%)
F1144 LYS 29.29 NZ with J1066
General case /
F1196 LEU 20.8
HOH O
­127.1,23.8
­
Favored
(62.95%)
General case /
­120.8,127.1
0.437Å
Favored (7.22%)
F1311 GLN 22.19 OE1 with F1014 General case /
G1017 ARG 43.22
G1060 ARG 19.38
GLN NE2
­157.6,131.6
29.4% (Cg_exo)
chi angles: 341.4
10.2% (tt0)
chi angles:
175,169.8,130.8
0.2%
chi angles: 348.9
0.3%
chi angles: 143.2
0%
chi angles:
200.7,277.8,165,277.9
0.4%
chi angles:
251.1,134.2,25.2,206
72.2% (mmtt)
chi angles:
295.7,286.9,181.2,188.8
1%
chi angles: 183.5,124.7
6.4% (tt0)
chi angles:
187.5,191.2,187.8
0.435Å
Favored (73.8%)
0.5%
NH2 with
B1014 GLN O
General case /
­59.5,­34.1
chi angles:
55.8,231.3,288.6,152.1
­
Favored
(98.44%)
0%
General case /
­64.2,­41.2
0.482Å
Favored
(79.89%)
HOH O
General case /
­61.8,­35.2
0.487Å
Favored
(96.38%)
ARG NH2
General case /
­60.7,­42.6
G1063 ASN 18.48 ND2 with J 935
G1067 SER 23.31 OG with G1071
0.487Å
Favored
chi angles:
198.5,278.3,166,275.3
3.5% (t30)
chi angles: 166.2,90.2
23.1% (t)
chi angles: 187.1
0.056Å
­
­
0.047Å
­
­
0.258Å
­
­
0.046Å
­
­
0.045Å
­
­
0.027Å
­
­
0.031Å
­
­
0.035Å
­
­
0.032Å
­
­
0.017Å
­
­
0.07Å
­
­
0.037Å
­
­
0.021Å
­
­
2.5% (mtp180)
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G1071 ARG 44.24
#
Res
NH2 with
G1067 SER OG
General case /
­66.8,­35.1
High
Clash > 0.4Å Ramachandran
B
Avg:
29.89
G1075 VAL 37.92
Clashscore:
1.58
Outliers: 1 of
2439
­
Favored
(95.53%)
G1086 ARG 59.23
H1082 THR 61.5
H1083 ASN 72.4
­
0.041Å
­
­
0.123Å
­
­
0.074Å
­
­
chi angles:
325.2,226.6,304.8,151.3
0.024Å
­
­
­
­
­
­
0.132Å
­
­
0.126Å
­
­
0.014Å
­
­
0.026Å
­
­
0.047Å
­
­
General case /
­73.0,106.1
chi angles:
165.2,180.6,37.9
0%
General case /
­57.9,137.4
chi angles:
152.1,280.1,236.5,76.6
0.401Å
Favored
(65.98%)
42.5% (mt­10)
HOH O
General case /
­69.5,­19.6
­
General case /
­85.7,10.9
Favored
(57.38%)
GLN NE2
Glycine / 88.7,18.6
0.585Å
Favored
(41.13%)
GLN NE2
General case /
­101.8,137.6
H1014 GLN 43.97 OE1 with H1311
H1047 SER 40.91
­
GLY O
Favored
(12.77%)
­
­
0.401Å
O with H1082
THR CG2
0.412Å
O with H1084
GLY C
Favored
(18.89%)
General case /
­74.0,167.2
Favored
(32.35%)
General case /
­77.5,152.2
Favored
(48.15%)
General case /
­92.8,­2.9
Favored
(79.27%)
General case /
­
0.173Å
39.6% (tt0)
0.416Å
G1166 GLY 29.88 O with G1085
73
0.8%
Favored (4.91%)
­
­
Cβ
Bond Bond
deviation lengths. angles.
Outliers: Outliers:
Poor rotamers: 41 of Outliers:
0 of
0 of
2211
1 of 2361
2459
2459
0.416Å
Favored
(46.25%)
0.032Å
Rotamer
chi angles: 120.8
G1117 GLU 39.98 CD with J 339
G1143 LYS 43.98
chi angles:
248.6,130.7,42,206.2
General case /
­64.1,­43.9
G1085 GLN 77.18 NE2 with G1166
H1032 THR
(81.74%)
chi angles:
276.4,175.2,29.8
0.1%
6.4% (mt­30)
chi angles:
290.9,223.8,352.7
0.2%
chi angles: 341.6
0.1%
chi angles: 135.8
85% (m)
chi angles: 301.5
52.1% (m­20)
chi angles: 295.6,358.4
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­69.8,­40.0
H1084 GLY
66
H1085 GLN 82.43
H1196 LEU 25.1
0.412Å
Favored (3.51%)
C with H1083
ASN O
Glycine /
­38.5,136.9
­
­
­
­
0.048Å
­
­
0.09Å
­
­
0.072Å
­
­
chi angles:
172.2,173.8,63.8
0.043Å
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
Favored (6.23%)
1%
General case /
­56.3,155.0
chi angles:
252.7,60.8,242.8
Favored
(56.92%)
­
General case /
­126.6,125.5
0.54Å
Favored
(85.48%)
HOH O
General case /
­61.3,­47.9
0.585Å
Favored
(22.07%)
GLN OE1
General case /
­146.0,136.2
H1237 LYS 28.08 NZ with J 422
H1311 GLN 32.93 NE2 with H1014
0.45Å
J 146 HOH 29.68 O with A1024
­
0.8%
chi angles: 185.2,122.4
76.3% (tttt)
chi angles:
179.6,177.9,197.3,176.8
43.3% (tt0)
ARG NH1
0.401Å
J 339 HOH 26.64 O with G1117
GLU CD
0.54Å
J 422 HOH 26.35 O with H1237
LYS NZ
0.402Å
J 563 HOH 36.79 O with C1144
LYS NZ
#
Res
High
Clash > 0.4Å Ramachandran
B
Avg:
29.89
Clashscore:
1.58
0.555Å
J 574 HOH 26.13 O with D1063
Outliers: 1 of
2439
Cβ
Bond Bond
deviation lengths. angles.
Outliers: Outliers:
Poor rotamers: 41 of Outliers:
0 of
0 of
2211
1 of 2361
2459
2459
Rotamer
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
ASN ND2
0.482Å
J 935 HOH 34.11 O with G1063
ASN ND2
0.405Å
J1066 HOH 35.58 O with F1144
LYS NZ
About MolProbity | Website for the Richardson Lab | Internal reference 3.19
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201302211713_refmac1_ncs­
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1.73
100th percentile* (N=576, 2.10Å ± 0.25Å)
All­Atom Clashscore, all atoms:
Contacts Clashscore is the number of serious steric overlaps (> 0.4 Å) per 1000 atoms.
Poor rotamers
2.22%
Goal: <1%
Ramachandran outliers
0.04%
Goal: <0.2%
Ramachandran favored
98.07% Goal: >98%
Protein Cβ deviations >0.25Å
Geometry
MolProbity score^
11
Goal: 0
1.19
100th percentile* (N=11758, 2.10Å ± 0.25Å)
Residues with bad bonds:
0.00%
Goal: 0%
Residues with bad angles:
0.08%
Goal: <0.1%
* 100th percentile is the best among structures of comparable resolution; 0th percentile is the worst. ^ MolProbity score is defined as the following: 0.42574*log(1+clashscore) + 0.32996*log(1+max(0,pctRotOut­1)) +
0.24979*log(1+max(0,100­pctRamaFavored­2)) + 0.5
#
Res
High Clash >
Ramachandran
B
0.4Å
Avg: Clashscore: Outliers: 1 of
30.71
1.73
2439
0.552Å
Favored
(66.69%)
146 HOH O
General case /
­69.9,­25.6
A1024 ARG 50.99 NH1 with J
Favored
(79.58%)
A1038 ARG 65.22
­
A1077 GLU 34.74
OE2 with
H1071 ARG
NH1
General case /
­60.6,­19.5
­
Favored
(54.16%)
0.45Å
A1085 GLN 69.24
General case /
­56.4,­45.1
Favored
(56.37%)
General case /
­66.0,141.3
Favored
A1114 ARG 71.66
­
(83.62%)
Cβ
Bond
Bond angles.
deviation lengths.
Outliers: Outliers:
Poor rotamers: 49 of
Outliers: 2 of
11 of
0 of
2211
2459
2361
2459
Rotamer
19.7% (ptt­85)
chi angles:
89.2,191.4,175.1,284
0%
chi angles:
241.1,237.8,244.1,186
51.1% (mt­10)
chi angles:
273.4,168.3,9
0.9%
chi angles:
318.5,109.7,280.5
0.08Å
­
­
0.124Å
­
­
0.067Å
­
­
0.041Å
­
­
0.322Å
­
­
0.3%
chi angles:
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A1114 ARG 71.66
Viewing 201302211713_refmac1_ncs-multi.table - MolProbity
­
(83.62%)
General case /
­62.9,­35.8
Favored
(80.03%)
chi angles:
293.2,160.9,131.7,234.8
0.7%
A1115 TRP 44.42
­
Pre­proline /
­80.3,128.8
chi angles: 262.3,273.6
0.404Å
Favored
(16.77%)
66.5% (mm­40)
A1122 GLU 34.39
OE2 with
A1188 LYS
NZ
General case /
­97.8,158.8
0.441Å Favored (36.4%)
A1175 TYR 28.81 N with J 635
HOH O
0.404Å
A1188 LYS 44.16
NZ with
A1122 GLU
OE2
A1246 LYS 47.07
­
A1258 TYR 50.85
CE1 with
A1318 RNH
CAA
A1291 LEU 24.53
N with
A1292 PRO
CD
0.418Å
A1292 PRO 20.99
A1308 SER 27.77
CD with
A1291 LEU
N
­
73.4% (t80)
General case /
­114.2,147.2
chi angles: 184,84
Favored (58.9%)
14.2% (tttm)
General case /
­104.9,126.5
chi angles:
181.2,173.2,180.5,341.9
Favored
(90.63%)
General case /
­66.8,­40.6
0.817Å Favored (66.6%)
0.418Å
chi angles:
289.4,285.8,167.1
General case /
­59.6,­26.1
Favored
(23.76%)
Pre­proline /
­59.2,­36.1
Favored
(29.03%)
Proline /
­67.2,­11.2
Favored
(39.87%)
0.1%
chi angles:
292,233.3,94.9,231
37.2% (t80)
chi angles: 192.7,92.3
51.2% (tp)
chi angles: 182.4,58.6
61.8% (Cg_exo)
chi angles: 334.2
0.3%
General case /
­76.7,128.4
chi angles: 142.3
­
­
Favored
(91.62%)
56.5% (ttp85)
0.322Å
­
­
0.05Å
­
­
0.046Å
­
­
0.112Å
­
­
0.114Å
­
­
0.016Å
­
­
0.074Å
­
­
0.099Å
­
­
0.035Å
­
­
0.156Å
­
­
­
­
­
0.051Å
­
­
0.026Å
­
­
0.817Å
A1318 RNH 37.14 CAA with
A1258 TYR
CE1
0.645Å
C1024 ARG 54.46 NH1 with
C1025 ASP
OD1
C1025 ASP 23.59
General case /
­61.6,­39.1
0.645Å Favored (48.2%)
OD1 with
C1024 ARG
NH1
chi angles:
172.7,190.3,54.9,80.5
97.4% (m­20)
General case /
­88.3,0.5
chi angles: 290.8,161.8
Favored
0%
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C1060 ARG 20.05
­
Favored
(82.87%)
General case /
­68.7,­40.1
0.409Å
C1122 GLU 27.36 OE2 with
C1188 LYS
NZ
C1134 SER 45.34
#
Res
­
Favored
(17.56%)
General case /
­99.2,158.2
Favored (67.7%)
General case /
­52.8,­45.8
High Clash >
Ramachandran
B
0.4Å
Avg: Clashscore: Outliers: 1 of
30.71
1.73
2439
0.482Å
C1137 LYS 55.7
CG with
C1142 MET
CE
0.482Å
C1142 MET 54.98
C1143 LYS 47.8
CE with
C1137 LYS
CG
­
0.409Å
C1188 LYS 42.17
C1196 LEU 24.7
Favored
(13.73%)
General case /
­51.9,­57.1
Favored
(76.65%)
0.9%
chi angles: 102.7
16.8% (mmtt)
chi angles:
272.6,257.9,180.2,164.4
10% (tpp)
General case /
­82.1,8.9
chi angles:
273.4,69.7,119.3,155.5
Favored
(58.45%)
14.7% (tttm)
General case /
­121.4,126.2
Favored
(60.18%)
­
­
0.051Å
­
­
0.06Å
­
­
Cβ
Bond
Bond angles.
deviation lengths.
Outliers: Outliers:
Poor rotamers: 49 of
Outliers: 2 of
11 of
0 of
2211
2459
2361
2459
0%
­
0.081Å
Rotamer
Favored (10.8%)
Favored
(61.77%)
CD2 with
C1318 RNH
CAA
chi angles:
290.3,286.1,168.7
chi angles:
215.1,55.5,82.5
General case /
­104.3,126.9
C1258 TYR 58.7
67.1% (mm­40)
General case /
­64.0,­32.6
NZ with
C1122 GLU
OE2
0.661Å
0%
chi angles:
197.4,280.1,162.9,277.7
chi angles:
181.5,173.5,181,341.3
1%
chi angles: 185,124.3
5.5% (t80)
0.041Å
­
­
0.088Å
­
­
0.07Å
­
­
0.103Å
­
­
0.048Å
­
­
0.03Å
­
­
General case /
­62.5,­17.9
chi angles: 208.1,74.8
C1318 RNH 44.32
CAA with
C1258 TYR
CD2
­
­
­
­
­
B1008 LEU 57.39
­
­
0.1%
0.127Å
­
­
­
Favored
(83.26%)
chi angles:
289.1,250.6,126.5,276.3
0.008Å
­
­
0%
0.061Å
­
­
0.661Å
B1040 LYS 70.9
General case /
­60.9,­37.1
chi angles: 29.4,147.8
0.2%
Favored
B1060 ARG 59.52
­
(74.21%)
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B1060 ARG 59.52
B1085 GLN 77.85
B1119 ARG 66.72
­
­
­
0.635Å
B1134 SER 36.64 OG with
B1137 LYS 61.71
B1196 LEU 24.62
B1233 GLU 52.35
Res
Favored
(47.92%)
General case /
­69.4,146.0
Favored
(46.67%)
General case /
­78.9,­31.7
Favored
(69.69%)
Favored
(16.55%)
CG with
B1142 MET
CE
CE with
B1137 LYS
CG
CG with
B1189 THR
CG2
General case /
­52.5,­56.7
Favored
(77.09%)
General case /
­61.5,­34.1
Favored
(25.38%)
General case /
­149.8,143.0
Favored
(54.61%)
CG2 with
B1169 GLN
CG
General case /
­100.9,130.1
­
Favored
(63.87%)
0.1%
chi angles:
312.1,230.3,103.2,129.2
23.2% (p)
chi angles: 79.7
63.8% (mttt)
chi angles:
274.9,160.8,185.4,164
11.6% (tpp)
chi angles:
215.6,55.6,70.1
10.3% (tt0)
chi angles:
179.9,196.8,125.3
23.4% (m)
chi angles: 291.1
1%
chi angles: 185.1,124.9
Favored (70.1%)
9.9% (pt­20)
­
General case /
­56.5,­36.0
chi angles:
70.9,166.6,115
0.431Å
Favored
(85.63%)
27.5% (ttpt)
985 HOH O
General case /
­59.3,­47.4
High Clash >
Ramachandran
B
0.4Å
Avg: Clashscore: Outliers: 1 of
30.71
1.73
2439
B1246 LYS 50.17
0%
chi angles:
61.1,265.9,167.3
General case /
­119.8,129.4
B1237 LYS 39.71 NZ with J
#
chi angles:
202.6,281.8,161.7,271.8
0.632Å
0.45Å
B1189 THR 39.8
General case /
­71.2,­41.0
General case /
­53.5,­44.2
0.45Å
B1169 GLN 49.94
0%
J1133 HOH
O
0.632Å
B1142 MET 53.27
(74.21%)
­
chi angles:
172.6,157,52,188.1
0.061Å
­
­
0.114Å
­
­
0.074Å
­
­
0.11Å
­
­
0.025Å
­
­
0.095Å
­
­
0.236Å
­
­
0.051Å
­
­
0.027Å
­
­
0.27Å
­
­
0.048Å
­
­
Cβ
Bond
Bond angles.
deviation lengths.
Outliers: Outliers:
Poor rotamers: 49 of
Outliers: 2 of
11 of
0 of
2211
2459
2361
2459
Rotamer
Favored
(90.48%)
chi angles:
General case /
298.1,328.1,259.7,263.3
0.2%
0.063Å
­
­
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General case /
­66.4,­42.4
0.441Å
B1291 LEU 25.41
N with
B1292 PRO
CD
0.441Å
B1292 PRO 19.51
B1301 MET 34.55
D1034 ASP 61.57
D1038 ARG 63.23
D1044 GLU 46.5
D1060 ARG 17.59
CD with
B1291 LEU
N
­
­
­
­
­
Favored
(15.08%)
Pre­proline /
­59.5,­34.4
Favored
(33.81%)
Proline /
­68.9,­12.9
Favored
(33.56%)
General case /
­111.9,113.0
Favored
(99.84%)
General case /
­63.0,­41.3
Favored
(73.28%)
General case /
­54.6,­44.9
Favored
(70.34%)
General case /
­58.1,­33.4
Favored
(88.21%)
General case /
­67.2,­41.6
298.1,328.1,259.7,263.3
48.5% (tp)
chi angles: 181.4,57.1
77.6% (Cg_exo)
chi angles: 333.4
0.3%
chi angles:
192.9,180.6,8.9
0.1%
chi angles: 239.5,47.7
0.3%
chi angles:
263.8,68.4,148.8,76.6
2.4% (tt0)
chi angles:
239.4,169.2,52.6
0%
chi angles:
198.2,282.2,163.3,275.3
0.492Å Favored (67.9%)
7.8% (t30)
D1063 ASN 16.97 ND2 with J General case /
chi angles: 170.2,82.8
574 HOH O
­53.5,­41.5
0.538Å
D1067 SER 23.47
OG with
D1071 ARG
NH2
0.538Å
D1071 ARG 46.04 NH2 with
D1067 SER
OG
D1086 ARG 78.37
Favored
(93.19%)
General case /
­61.4,­45.8
Favored
(93.18%)
General case /
­66.0,­41.4
11.4% (t)
chi angles: 191.4
19.3% (mtt180)
chi angles:
278.8,169.3,215,126
Favored (25.5%)
0%
General case /
­77.7,120.6
chi angles:
3.4,155.5,17.9,109.1
0.416Å
Favored
(62.93%)
44% (mtt85)
463 HOH O
General case /
­75.5,­31.5
0.413Å
Favored
(17.82%)
­
D1119 ARG 44.36 NE with J
D1122 GLU 27.63 OE2 with
D1188 LYS
General case /
NZ
­99.8,158.1
chi angles:
298.9,204.2,161.4,91.4
64.3% (mm­40)
chi angles:
288.4,287,169.4
0.092Å
­
­
0.039Å
­
­
0.089Å
­
­
0.08Å
­
­
0.022Å
­
­
0.354Å
­
­
0.066Å
­
­
0.071Å
­
­
0.075Å
­
­
0.081Å
­
­
0.089Å
­
­
0.061Å
­
­
0.047Å
­
­
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Viewing 201302211713_refmac1_ncs-multi.table - MolProbity
0.684Å
D1133 ASN 31.02
O with
D1142 MET
CE
0.684Å
D1142 MET 44.29
D1186 GLY 74.1
D1301 MET 27.79
D1310 ASN 33.26
#
Res
General case /
­53.1,­42.8
Favored
(75.85%)
CE with
D1133 ASN
O
General case /
­60.8,­34.1
­
OUTLIER
(0.18%)
0.413Å
D1188 LYS 41.85
Favored
(67.64%)
Glycine /
­115.0,82.1
Favored
(57.88%)
NZ with
D1122 GLU
OE2
General case /
­103.7,127.5
­
Favored
(40.15%)
­
General case /
­114.4,115.8
Favored
(11.15%)
General case /
­115.3,­4.8
High Clash >
Ramachandran
B
0.4Å
Avg: Clashscore: Outliers: 1 of
30.71
1.73
2439
E1008 LEU 74.27
E1031 LEU 82.91
E1033 GLU 89.22
E1036 ILE 71.27
E1038 ARG 90.07
E1085 GLN 77.45
­
­
­
Favored
(42.76%)
­
­
­
­
General case /
­63.6,146.6
Favored
(99.06%)
General case /
­63.2,­40.7
Favored
(83.17%)
General case /
­58.0,­47.1
Favored
(73.89%)
General case /
­54.8,­45.3
Favored
89.8% (m­20)
chi angles: 287.4,349.9
6.3% (mmt)
chi angles:
270.5,304.6,162.7
­
14.3% (tttm)
chi angles:
181.8,173.7,180.4,341.9
0.3%
chi angles:
191.6,188.8,355.6
0.1%
chi angles: 57.8,181.7
0.078Å
­
­
0.141Å
­
­
1
OUTLIER(S)
­
­
0.096Å
­
­
0.091Å
­
­
0.258Å
­
­
worst is N­CA­
C: ­4.049
&sigma
Cβ
Bond
Bond angles.
deviation lengths.
Outliers: Outliers:
Poor rotamers: 49 of
Outliers: 2 of
11 of
0 of
2211
2459
2361
2459
0.3%
0.082Å
­
­
Rotamer
chi angles: 290.6,343.8
6.5% (mt)
chi angles: 303.4,149.3
0.7%
chi angles:
239.5,153.5,306
0.7%
chi angles: 293.6,240.7
0%
chi angles:
240.8,198.9,213.9,76.7
0%
1
OUTLIER(S)
0.08Å
­
0.168Å
­
­
0.117Å
­
­
0.13Å
­
­
0.041Å
­
­
worst is CA­C­
N: 4.361
&sigma
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E1085 GLN 77.45
Viewing 201302211713_refmac1_ncs-multi.table - MolProbity
­
0.041Å
­
­
0.064Å
­
­
0.065Å
­
­
0.269Å
­
­
0.155Å
­
­
0.097Å
­
­
0.105Å
­
­
0.317Å
­
­
0.024Å
­
­
0.059Å
­
­
0.059Å
­
­
0.034Å
­
­
chi angles:
3.5,165.2,194.4,156.8
0.116Å
­
­
Favored
(98.26%)
0.7%
0.054Å
­
­
General case /
chi angles:
(55.67%)
General case /
­64.6,140.4
E1115 TRP 54.37
E1134 SER 48.09
E1249 GLU 71.11
­
­
­
Favored
(73.76%)
Pre­proline /
­83.1,130.6
Favored
(61.66%)
General case /
­51.0,­47.1
Favored
(59.23%)
F1008 LEU 63.43
­
­
­
Favored
(28.68%)
F1086 ARG 86.52
F1246 LYS 56.38
0.4%
General case /
­112.5,113.9
chi angles:
192,180.3,9.3
General case /
­78.9,156.6
Favored
(99.14%)
­
Favored
(81.43%)
General case /
­69.1,­40.1
Favored
(96.25%)
F1071 ARG
NH1
General case /
­61.5,­44.7
0.403Å
Favored
(86.61%)
NH1 with
F1067 SER
OG
General case /
­67.7,­39.0
­
Favored
(28.68%)
­
chi angles:
177.9,121.1,286.2,108.4
Favored (35.8%)
General case /
­62.7,­41.0
F1067 SER 23.82 OG with
F1071 ARG 41.91
General case /
­83.6,­19.4
J1063 HOH
O
0.403Å
39.8% (mt­10)
0%
­
F1060 ARG 17.25
chi angles: 106.4
Favored
(37.41%)
E1301 MET 36.23
F1049 GLU 25.17 OE1 with
0.4%
chi angles:
279.8,180.2,45.6
­
0.416Å
0.8%
chi angles: 263.2,273.1
General case /
­76.1,­27.9
E1264 LYS 84.64
F1030 THR 46.95
chi angles:
320.6,112.5,118
General case /
­80.3,121.2
0.4%
chi angles: 221.9,22.5
0.8%
chi angles: 328.1
37.6% (tt0)
chi angles:
168.7,188.8,149.6
0%
chi angles:
199.5,282.3,163.9,276.6
10% (t)
chi angles: 192.3
0.4%
chi angles:
270.8,149.1,357.9,216.4
0%
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2/25/13
Viewing 201302211713_refmac1_ncs-multi.table - MolProbity
F1301 MET 31.47
#
Res
­
General case /
­63.7,­43.1
chi angles:
284.8,302.5,279.5,246.9
Favored
(50.21%)
1.1% (ptm)
General case /
­108.7,117.5
High Clash >
Ramachandran
B
0.4Å
Avg: Clashscore: Outliers: 1 of
30.71
1.73
2439
G1017 ARG 40.3
G1060 ARG 19.09
­
­
Favored
(87.28%)
General case /
­67.6,­40.3
Favored
(65.04%)
935 HOH O
General case /
­52.6,­42.0
0.5Å
Favored
(88.66%)
G1067 SER 25.06 OG with
G1071 ARG
NH2
0.5Å
NH2 with
G1067 SER
OG
0.502Å
G1086 ARG 71.74 NH1 with
chi angles:
61.8,231.4,289.2,153.5
0%
chi angles:
198.5,282,163.7,275.8
8.8% (t30)
chi angles: 170.2,81
8.5% (t)
0.5%
General case /
­77.1,130.9
0.467Å
Favored
(67.63%)
339 HOH O
General case /
­64.7,­20.9
0.44Å
Favored
(17.73%)
G1122 GLU 29.26 OE2 with
0.6%
Favored
(92.43%)
Favored
(43.59%)
G1188 LYS
NZ
General case /
­99.9,158.4
­
Favored
(64.19%)
General case /
­51.7,­46.5
­
­
Cβ
Bond
Bond angles.
deviation lengths.
Outliers: Outliers:
Poor rotamers: 49 of
Outliers: 2 of
11 of
0 of
2211
2459
2361
2459
chi angles: 194.2
General case /
­66.0,­39.8
0.341Å
Rotamer
General case /
­59.5,­46.4
G1194 ASP
OD1
G1117 GLU 45.47 CD with J
G1134 SER 47.94
General case /
­64.0,­30.7
0.417Å
G1063 ASN 15.94 ND2 with J
G1071 ARG 53.85
Favored
(73.93%)
chi angles:
39.1,158.5,247.2
chi angles:
271.2,148.8,358,217.1
0%
chi angles:
153.6,275.2,238.2,75.8
87.4% (mt­10)
chi angles:
287.1,174.6,11.9
65.1% (mm­40)
chi angles:
289,286,168.7
0.4%
chi angles: 107.2
0.063Å
­
­
0.048Å
­
­
0.062Å
­
­
0.07Å
­
­
0.036Å
­
­
0.299Å
­
­
0.096Å
­
­
0.044Å
­
­
0.039Å
­
­
0.051Å
­
­
Favored
G1143 LYS 46.13
­
(11.41%)
0.8%
General case /
chi angles:
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0.44Å
G1188 LYS 40.99
NZ with
G1122 GLU
OE2
G1192 GLN 76.76
­
G1194 ASP 20.06
OD1 with
G1086 ARG
NH1
0.502Å
0.408Å
G1291 LEU 24.1
N with
G1292 PRO
CD
0.408Å
G1292 PRO 21.54
G1310 ASN 24.64
CD with
G1291 LEU
N
­
0.448Å
G1313 ARG 31.45 NH1 with
H1014 GLN 52.53
chi angles:
308,225.2,323.6,148.9
Favored
(58.77%)
14.8% (tttm)
General case /
­104.7,126.5
Favored
(80.68%)
General case /
­69.1,­37.7
Favored
(39.66%)
Pre­proline /
­58.5,­38.0
Favored
(30.27%)
Proline /
­64.0,­12.4
Favored (13.2%)
#
Res
0.076Å
­
­
0.07Å
­
­
0.059Å
­
­
0.31Å
­
­
0.031Å
­
­
chi angles:
306.5,214.4,342.1
0.209Å
­
­
­
0.086Å
­
­
10.3% (mt)
0.216Å
­
­
61.4% (m­20)
chi angles: 300,123
47.7% (tp)
chi angles: 182.6,57.4
52.4% (Cg_exo)
chi angles: 336.2
18.6% (m­20)
Favored
(62.04%)
52.8% (mtp180)
General case /
­108.3,136.7
Favored
(45.93%)
General case /
­60.8,­17.5
­
Avg: Clashscore: Outliers: 1 of
30.71
1.73
2439
H1071 ARG 43.72 NH1 with
­
chi angles: 276,11.5
High Clash >
B
0.4Å Ramachandran
0.45Å
­
General case /
­108.2,­17.4
Favored
(51.93%)
C with
H1022 ALA
O
0.094Å
0.8%
0.427Å
H1023 LEU 46.51
­
chi angles:
233.7,143.4,230.9
0.466Å
O with
H1023 LEU
C
­
Pre­proline /
42.2,58.3
General case /
­115.6,131.7
OE1 with
H1311 GLN
NE2
0.112Å
chi angles:
181.5,172.9,181.2,340.9
Favored (5.08%)
J1152 HOH
O
0.427Å
H1022 ALA 53.34
General case /
­85.1,11.1
Favored
(91.14%)
A1077 GLU
General case /
OE2
­66.5,­41.7
chi angles:
282.7,173.8,79,212.6
12.8% (mt­30)
chi angles: 291.1,200.1
Rotamer
Cβ
Bond
deviation lengths. Bond angles.
Poor rotamers: 49 of
2211
Outliers: Outliers:
Outliers: 2 of
11 of
0 of
2459
2361
2459
74.1% (mtt­85)
chi angles:
281,168.7,193.8,269.2
0.073Å
­
­
Favored
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Viewing 201302211713_refmac1_ncs-multi.table - MolProbity
0.627Å
Favored
(77.33%)
653 HOH O
General case /
­62.0,­49.9
chi angles: 298.7
Favored (7.54%)
0.1%
General case /
­89.1,17.2
chi angles:
206.8,196.5,115.3,107.3
Allowed
(1.68%)
17.4% (m­85)
H1103 THR 32.95 OG1 with J
H1143 LYS 54.12
­
H1180 TYR 37.75
­
H1185 ASP 81.46
­
H1192 GLN 80.35
­
H1196 LEU 25.82
­
H1311 GLN 41.21
NE2 with
H1014 GLN
OE1
0.466Å
99.2% (m)
0.019Å
­
­
0.279Å
­
­
0.335Å
­
­
0.065Å
­
­
0.107Å
­
­
0.062Å
­
­
chi angles:
183.7,178.7,54.1
0.017Å
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
General case /
37.8,57.6
Favored (4.55%)
chi angles: 290.5,139.1
0.6%
General case /
­126.5,33.8
chi angles: 270.8,53.8
Favored (4.31%)
0%
Pre­proline /
40.7,57.2
chi angles:
231.5,148,62.2
Favored
(61.83%)
General case /
­123.0,127.0
Favored
(11.81%)
General case /
­154.6,135.8
1%
chi angles: 184.7,124.2
54.2% (tt0)
0.552Å
J 146 HOH 30.26
O with
A1024 ARG
NH1
0.467Å
J 339 HOH 25.31
O with
G1117 GLU
CD
0.416Å
J 463 HOH 42.85
O with
D1119 ARG
NE
0.492Å
J 574 HOH 24.4
O with
D1063 ASN
ND2
0.441Å
J 635 HOH 25.04
O with
A1175 TYR
N
0.627Å
J 653 HOH 26.73
O with
H1103 THR
OG1
0.417Å
J 935 HOH 33.51
O with
G1063 ASN
ND2
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10/11
2/25/13
ND2
Viewing 201302211713_refmac1_ncs-multi.table - MolProbity
0.431Å
O with
J 985 HOH 24.7 B1237 LYS
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
­
NZ
0.416Å
J1063 HOH 35.9
O with
F1049 GLU
OE1
0.635Å
J1133 HOH 35.42
O with
B1134 SER
OG
0.448Å
J1152 HOH 29.74
O with
G1313 ARG
NH1
About MolProbity | Website for the Richardson Lab | Internal reference 3.19
molprobity.biochem.duke.edu/viewtable.php?MolProbSID=9e6kaqcpbvihgtkhud3f0dp54idqht80&file=/Library/WebServer/Doc…
11/11
4F7W_pdb_valid.pdf
CLOSE CONTACTS
-------------==> Close contacts in same asymmetric unit. Distances smaller than 2.2
Angstroms are considered as close contacts.
none
==> Close contacts based on crystal symmetry. Distances smaller than 2.2
Angstroms are considered as close contacts.
none
BOND DISTANCES AND ANGLES
------------------------==> Bond and angle checks are performed by first computing the average rms
error for all bonds and angles relative to standard values for nucleotide
units [L. Clowney et al., Geometric Parameters in Nucleic Acids: Nitrogenous
Bases, J.Am.Chem.Soc. 1996, 118, 509-518; A. Gelbin et al., Geometric
Parameters in Nucleic Acids: Sugar and Phosphate Constituents, J.Am.Chem.Soc.
1996, 118, 519-529] and amino acid units [R.A. Engh and R. Huber, Structure
quality and target parameters, International Tables for Crystallography,
Volume F, 2001, 382-392]. Any bond or angle which deviates from the
dictionary values by more than six times this computed rms error is
identified as an outlier.
*** Covalent Bond Lengths:
The overall RMS deviation for covalent bonds relative to the standard
dictionary is
0.013 Angstroms
The following table contains a list of the covalent bonds
greater than 6 times standard deviation.
Deviation
Residue Chain Sequence AT1 - AT2
Bond
Dictionary Standard
Name
ID
Number
Distance
Value
Deviation
---------------------------------------------------------------------------------0.067
GLU
D
1117
CD
- OE1
1.319
1.252
0.011
1 out of total 20361 covalent bonds (0.005%) have greater than 6 times
standard deviation.
*** Covalent Angle Values:
The overall RMS deviation for covalent angles relative to the standard
dictionary is
1.4 degrees.
All covalent bond angles lie within a 6.0*RMSD range about the
standard dictionary values.
TORSION ANGLES
-------------The torsion angle distributions have been checked. Refer to the
Procheck and/or Nucheck results on the PDB Validation Report page.
==> The following table contains a list of torsion angles outside the expected
Ramachandran regions [GJ. Kleywegt and TA. Jones, PHI/PSI-chology:
Ramachandran Revisited, Structure 1996, 4, 1395 - 1400].
Residue
SER
HIS
GLN
ASP
ASP
SER
MET
ILE
HIS
GLN
ASP
ILE
SER
VAL
ILE
SER
HIS
GLN
ASP
ASP
SER
ILE
HIS
GLN
ASP
ILE
HIS
ASP
ILE
PRO
MET
ILE
GLN
ASP
ILE
MET
ILE
HIS
ASP
ALA
ILE
HIS
TYR
GLN
ASP
ASP
SER
Chain
A
A
A
A
A
A
C
C
C
C
C
C
C
B
B
B
B
B
B
B
B
D
D
D
D
D
E
E
E
F
F
F
F
F
F
G
G
G
G
H
H
H
H
H
H
H
H
Sequence
1026
1118
1192
1213
1254
1304
1029
1054
1118
1192
1213
1281
1304
1027
1054
1113
1118
1192
1213
1254
1304
1054
1118
1192
1213
1281
1118
1213
1281
1011
1029
1054
1192
1213
1281
1029
1054
1118
1213
1022
1054
1118
1180
1192
1213
1254
1304
PSI
-35.42
72.91
65.12
72.08
85.82
-158.20
24.13
-60.77
68.92
60.28
77.70
-70.55
-159.02
114.32
-54.90
-17.95
81.74
62.10
75.51
82.14
-156.15
-59.60
66.39
69.66
72.71
-70.20
74.71
81.76
-65.16
0.45
27.86
-57.07
54.85
75.76
-72.03
29.73
-59.01
69.33
73.28
3.46
-61.06
81.48
59.91
58.15
77.10
66.29
-162.22
PHI
-37.42
-152.25
39.49
-168.00
-155.67
-123.65
-144.79
-125.00
-152.15
37.49
-160.83
-114.41
-124.72
-160.37
-121.64
-49.65
-155.61
39.13
-161.91
-160.34
-123.81
-127.27
-153.00
37.63
-165.59
-111.52
-154.69
-162.00
-123.10
-69.67
-144.74
-123.04
39.53
-168.03
-111.66
-143.60
-120.14
-152.32
-167.52
-68.19
-124.34
-155.89
37.67
37.40
-163.24
-166.64
-119.94
CHIRALITY
--------The chirality has been checked. O1P, O2P, and hydrogen atoms which do not
follow the conventions defined by IUBMB (Liebecq, C. Compendium of
Biochemical Nomenclature and Related Documents, 2nd ed.; Portland Press:
London and Chapel Hill, 1992) and IUPAC (J.L. Markley, A. Bax,
Y. Arata, C.W. Hilbers, R. Kaptein, B.D. Sykes, P.E. Wright and K. Wuthrich,
Recommendations for the Presentation of NMR Structures of Proteins and
Nucleic Acids, Pure & Appl. Chem., Vol. 70, pp. 117-142, 1998) will be
standardized at the time of processing; there is no need to change these
labels in your coordinate file. Any other stereochemical violations are
listed below.
none
SOLVENT
------The following solvent molecules are further than 3.5 Angstroms away from
macromolecule atoms in the asymmetric unit that are available for
hydrogen bonding. Solvent molecules in extended hydration shells
separated by 3.5 Angstroms or less are not listed.
none
We have replaced the coordinates for solvent molecules which could be
translated back into the asymmetric unit. Please review all solvent
molecules in your file and contact us if you have any serious objections.
MISSING RESIDUES
---------------==> The following residues are missing:
(Note: The SEQ number starts from 1 for each chain according to SEQRES
sequence record.)
RES MOD#C SEQ
MET(
HIS(
HIS(
HIS(
HIS(
HIS(
HIS(
SER(
SER(
GLY(
ARG(
GLU(
ASN(
LEU(
TYR(
PHE(
GLN(
GLY(
MET(
SER(
GLN(
LYS(
GLU(
GLN(
THR(
MET(
HIS(
HIS(
HIS(
HIS(
HIS(
HIS(
SER(
SER(
GLY(
ARG(
GLU(
ASN(
LEU(
TYR(
A 983
A 984
A 985
A 986
A 987
A 988
A 989
A 990
A 991
A 992
A 993
A 994
A 995
A 996
A 997
A 998
A 999
A1000
A1001
A1002
A1003
A1004
A1005
A1006
A1007
C 983
C 984
C 985
C 986
C 987
C 988
C 989
C 990
C 991
C 992
C 993
C 994
C 995
C 996
C 997
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
PHE(
GLN(
GLY(
MET(
SER(
GLN(
LYS(
GLU(
GLN(
THR(
MET(
HIS(
HIS(
HIS(
HIS(
HIS(
HIS(
SER(
SER(
GLY(
ARG(
GLU(
ASN(
LEU(
TYR(
PHE(
GLN(
GLY(
MET(
SER(
GLN(
LYS(
GLU(
GLN(
THR(
MET(
HIS(
HIS(
HIS(
HIS(
HIS(
HIS(
SER(
SER(
GLY(
ARG(
GLU(
ASN(
LEU(
TYR(
PHE(
GLN(
GLY(
MET(
SER(
GLN(
LYS(
GLU(
GLN(
THR(
LEU(
MET(
HIS(
HIS(
HIS(
HIS(
HIS(
HIS(
C 998
C 999
C1000
C1001
C1002
C1003
C1004
C1005
C1006
C1007
B 983
B 984
B 985
B 986
B 987
B 988
B 989
B 990
B 991
B 992
B 993
B 994
B 995
B 996
B 997
B 998
B 999
B1000
B1001
B1002
B1003
B1004
B1005
B1006
B1007
D 983
D 984
D 985
D 986
D 987
D 988
D 989
D 990
D 991
D 992
D 993
D 994
D 995
D 996
D 997
D 998
D 999
D1000
D1001
D1002
D1003
D1004
D1005
D1006
D1007
D1008
E 983
E 984
E 985
E 986
E 987
E 988
E 989
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
SER(
SER(
GLY(
ARG(
GLU(
ASN(
LEU(
TYR(
PHE(
GLN(
GLY(
MET(
SER(
GLN(
LYS(
GLU(
GLN(
THR(
ASP(
SER(
VAL(
PRO(
MET(
MET(
HIS(
HIS(
HIS(
HIS(
HIS(
HIS(
SER(
SER(
GLY(
ARG(
GLU(
ASN(
LEU(
TYR(
PHE(
GLN(
GLY(
MET(
SER(
GLN(
LYS(
GLU(
GLN(
THR(
MET(
HIS(
HIS(
HIS(
HIS(
HIS(
HIS(
SER(
SER(
GLY(
ARG(
GLU(
ASN(
LEU(
TYR(
PHE(
GLN(
GLY(
MET(
SER(
E 990
E 991
E 992
E 993
E 994
E 995
E 996
E 997
E 998
E 999
E1000
E1001
E1002
E1003
E1004
E1005
E1006
E1007
E1025
E1026
E1027
E1028
E1029
F 983
F 984
F 985
F 986
F 987
F 988
F 989
F 990
F 991
F 992
F 993
F 994
F 995
F 996
F 997
F 998
F 999
F1000
F1001
F1002
F1003
F1004
F1005
F1006
F1007
G 983
G 984
G 985
G 986
G 987
G 988
G 989
G 990
G 991
G 992
G 993
G 994
G 995
G 996
G 997
G 998
G 999
G1000
G1001
G1002
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
GLN(
LYS(
GLU(
GLN(
THR(
LEU(
MET(
HIS(
HIS(
HIS(
HIS(
HIS(
HIS(
SER(
SER(
GLY(
ARG(
GLU(
ASN(
LEU(
TYR(
PHE(
GLN(
GLY(
MET(
SER(
GLN(
LYS(
GLU(
GLN(
THR(
ARG(
ASP(
SER(
VAL(
PRO(
MET(
G1003
G1004
G1005
G1006
G1007
G1008
H 983
H 984
H 985
H 986
H 987
H 988
H 989
H 990
H 991
H 992
H 993
H 994
H 995
H 996
H 997
H 998
H 999
H1000
H1001
H1002
H1003
H1004
H1005
H1006
H1007
H1024
H1025
H1026
H1027
H1028
H1029
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
PDB Chain_ID: A
1
15
SEQRES: MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN LEU TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
?
?
?
?
?
16
30
SEQRES: PHE GLN GLY MET SER GLN LYS GLU GLN THR LEU MET THR PRO TYR
COORDS:
?
?
?
?
?
?
?
?
?
? LEU MET THR PRO TYR
1008
1012
31
45
SEQRES: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
COORDS: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
1013
1027
46
60
SEQRES: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
COORDS: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
1028
1042
61
75
SEQRES: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
COORDS: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
1043
1057
76
90
SEQRES: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
COORDS: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
1058
1072
91
105
SEQRES: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
COORDS: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
1073
1087
106
120
SEQRES: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
COORDS: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
1088
1102
121
135
SEQRES: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
COORDS: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
1103
1117
136
150
SEQRES: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
COORDS: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
1118
1132
151
165
SEQRES: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
COORDS: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
1133
1147
166
180
SEQRES: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
COORDS: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
1148
1162
181
195
SEQRES: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
COORDS: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
1163
1177
196
210
SEQRES: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
COORDS: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
1178
1192
211
225
SEQRES: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
COORDS: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
1193
1207
226
240
SEQRES: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
COORDS: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
1208
1222
241
255
SEQRES: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
COORDS: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
1223
1237
256
270
SEQRES: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
COORDS: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
1238
1252
271
285
SEQRES: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
COORDS: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
1253
1267
286
300
SEQRES: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
COORDS: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
1268
1282
301
315
SEQRES: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
COORDS: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
1283
1297
316
330
SEQRES: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
COORDS: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
1298
1312
331
334
SEQRES: ARG LEU ARG LYS
COORDS: ARG LEU ARG LYS
1313
1316
PDB Chain_ID: C
1
15
SEQRES: MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN LEU TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
?
?
?
?
?
16
30
SEQRES: PHE GLN GLY MET SER GLN LYS GLU GLN THR LEU MET THR PRO TYR
COORDS:
?
?
?
?
?
?
?
?
?
? LEU MET THR PRO TYR
1008
1012
31
45
SEQRES: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
COORDS: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
1013
1027
46
60
SEQRES: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
COORDS: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
1028
1042
61
75
SEQRES: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
COORDS: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
1043
1057
76
90
SEQRES: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
COORDS: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
1058
1072
91
105
SEQRES: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
COORDS: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
1073
1087
106
120
SEQRES: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
COORDS: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
1088
1102
121
135
SEQRES: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
COORDS: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
1103
1117
136
150
SEQRES: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
COORDS: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
1118
1132
151
165
SEQRES: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
COORDS: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
1133
1147
166
180
SEQRES: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
COORDS: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
1148
1162
181
195
SEQRES: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
COORDS: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
1163
1177
196
210
SEQRES: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
COORDS: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
1178
1192
211
225
SEQRES: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
COORDS: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
1193
1207
226
240
SEQRES: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
COORDS: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
1208
1222
241
255
SEQRES: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
COORDS: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
1223
1237
256
270
SEQRES: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
COORDS: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
1238
1252
271
285
SEQRES: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
COORDS: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
1253
1267
286
300
SEQRES: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
COORDS: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
1268
1282
301
315
SEQRES: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
COORDS: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
1283
1297
316
330
SEQRES: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
COORDS: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
1298
1312
331
334
SEQRES: ARG LEU ARG LYS
COORDS: ARG LEU ARG LYS
1313
1316
PDB Chain_ID: B
1
15
SEQRES: MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN LEU TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
?
?
?
?
?
16
30
SEQRES: PHE GLN GLY MET SER GLN LYS GLU GLN THR LEU MET THR PRO TYR
COORDS:
?
?
?
?
?
?
?
?
?
? LEU MET THR PRO TYR
1008
1012
31
45
SEQRES: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
COORDS: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
1013
1027
46
60
SEQRES: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
COORDS: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
1028
1042
61
75
SEQRES: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
COORDS: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
1043
1057
76
90
SEQRES: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
COORDS: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
1058
1072
91
105
SEQRES: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
COORDS: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
1073
1087
106
120
SEQRES: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
COORDS: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
1088
1102
121
135
SEQRES: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
COORDS: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
1103
1117
136
150
SEQRES: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
COORDS: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
1118
1132
151
165
SEQRES: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
COORDS: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
1133
1147
166
180
SEQRES: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
COORDS: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
1148
1162
181
195
SEQRES: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
COORDS: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
1163
1177
196
210
SEQRES: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
COORDS: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
1178
1192
211
225
SEQRES: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
COORDS: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
1193
1207
226
240
SEQRES: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
COORDS: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
1208
1222
241
255
SEQRES: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
COORDS: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
1223
1237
256
270
SEQRES: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
COORDS: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
1238
1252
271
285
SEQRES: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
COORDS: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
1253
1267
286
300
SEQRES: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
COORDS: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
1268
1282
301
315
SEQRES: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
COORDS: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
1283
1297
316
330
SEQRES: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
COORDS: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
1298
1312
331
334
SEQRES: ARG LEU ARG LYS
COORDS: ARG LEU ARG LYS
1313
1316
PDB Chain_ID: D
1
15
SEQRES: MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN LEU TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
?
?
?
?
?
16
30
SEQRES: PHE GLN GLY MET SER GLN LYS GLU GLN THR LEU MET THR PRO TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
? MET THR PRO TYR
1009
1012
31
45
SEQRES: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
COORDS: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
1013
1027
46
60
SEQRES: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
COORDS: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
1028
1042
61
75
SEQRES: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
COORDS: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
1043
1057
76
90
SEQRES: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
COORDS: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
1058
1072
91
105
SEQRES: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
COORDS: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
1073
1087
106
120
SEQRES: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
COORDS: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
1088
1102
121
135
SEQRES: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
COORDS: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
1103
1117
136
150
SEQRES: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
COORDS: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
1118
1132
151
165
SEQRES: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
COORDS: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
1133
1147
166
180
SEQRES: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
COORDS: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
1148
1162
181
195
SEQRES: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
COORDS: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
1163
1177
196
210
SEQRES: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
COORDS: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
1178
1192
211
225
SEQRES: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
COORDS: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
1193
1207
226
240
SEQRES: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
COORDS: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
1208
1222
241
255
SEQRES: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
COORDS: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
1223
1237
256
270
SEQRES: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
COORDS: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
1238
1252
271
285
SEQRES: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
COORDS: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
1253
1267
286
300
SEQRES: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
COORDS: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
1268
1282
301
315
SEQRES: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
COORDS: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
1283
1297
316
330
SEQRES: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
COORDS: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
1298
1312
331
334
SEQRES: ARG LEU ARG LYS
COORDS: ARG LEU ARG LYS
1313
1316
PDB Chain_ID: E
1
15
SEQRES: MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN LEU TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
?
?
?
?
?
16
30
SEQRES: PHE GLN GLY MET SER GLN LYS GLU GLN THR LEU MET THR PRO TYR
COORDS:
?
?
?
?
?
?
?
?
?
? LEU MET THR PRO TYR
1008
1012
31
45
SEQRES: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
COORDS: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG
?
?
?
1013
1024
46
60
SEQRES: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
COORDS:
?
? THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
1030
1042
61
75
SEQRES: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
COORDS: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
1043
1057
76
90
SEQRES: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
COORDS: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
1058
1072
91
105
SEQRES: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
COORDS: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
1073
1087
106
120
SEQRES: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
COORDS: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
1088
1102
121
135
SEQRES: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
COORDS: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
1103
1117
136
150
SEQRES: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
COORDS: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
1118
1132
151
165
SEQRES: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
COORDS: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
1133
1147
166
180
SEQRES: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
COORDS: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
1148
1162
181
195
SEQRES: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
COORDS: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
1163
1177
196
210
SEQRES: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
COORDS: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
1178
1192
211
225
SEQRES: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
COORDS: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
1193
1207
226
240
SEQRES: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
COORDS: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
1208
1222
241
255
SEQRES: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
COORDS: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
1223
1237
256
270
SEQRES: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
COORDS: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
1238
1252
271
285
SEQRES: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
COORDS: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
1253
1267
286
300
SEQRES: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
COORDS: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
1268
1282
301
315
SEQRES: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
COORDS: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
1283
1297
316
330
SEQRES: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
COORDS: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
1298
1312
331
334
SEQRES: ARG LEU ARG LYS
COORDS: ARG LEU ARG LYS
1313
1316
PDB Chain_ID: F
1
15
SEQRES: MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN LEU TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
?
?
?
?
?
16
30
SEQRES: PHE GLN GLY MET SER GLN LYS GLU GLN THR LEU MET THR PRO TYR
COORDS:
?
?
?
?
?
?
?
?
?
? LEU MET THR PRO TYR
1008
1012
31
45
SEQRES: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
COORDS: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
1013
1027
46
60
SEQRES: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
COORDS: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
1028
1042
61
75
SEQRES: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
COORDS: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
1043
1057
76
90
SEQRES: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
COORDS: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
1058
1072
91
105
SEQRES: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
COORDS: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
1073
1087
106
120
SEQRES: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
COORDS: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
1088
1102
121
135
SEQRES: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
COORDS: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
1103
1117
136
150
SEQRES: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
COORDS: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
1118
1132
151
165
SEQRES: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
COORDS: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
1133
1147
166
180
SEQRES: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
COORDS: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
1148
1162
181
195
SEQRES: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
COORDS: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
1163
1177
196
210
SEQRES: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
COORDS: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
1178
1192
211
225
SEQRES: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
COORDS: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
1193
1207
226
240
SEQRES: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
COORDS: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
1208
1222
241
255
SEQRES: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
COORDS: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
1223
1237
256
270
SEQRES: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
COORDS: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
1238
1252
271
285
SEQRES: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
COORDS: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
1253
1267
286
300
SEQRES: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
COORDS: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
1268
1282
301
315
SEQRES: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
COORDS: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
1283
1297
316
330
SEQRES: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
COORDS: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
1298
1312
331
334
SEQRES: ARG LEU ARG LYS
COORDS: ARG LEU ARG LYS
1313
1316
PDB Chain_ID: G
1
15
SEQRES: MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN LEU TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
?
?
?
?
?
16
30
SEQRES: PHE GLN GLY MET SER GLN LYS GLU GLN THR LEU MET THR PRO TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
? MET THR PRO TYR
1009
1012
31
45
SEQRES: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
COORDS: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
1013
1027
46
60
SEQRES: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
COORDS: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
1028
1042
61
75
SEQRES: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
COORDS: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
1043
1057
76
90
SEQRES: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
COORDS: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
1058
1072
91
105
SEQRES: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
COORDS: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
1073
1087
106
120
SEQRES: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
COORDS: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
1088
1102
121
135
SEQRES: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
COORDS: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
1103
1117
136
150
SEQRES: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
COORDS: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
1118
1132
151
165
SEQRES: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
COORDS: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
1133
1147
166
180
SEQRES: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
COORDS: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
1148
1162
181
195
SEQRES: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
COORDS: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
1163
1177
196
210
SEQRES: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
COORDS: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
1178
1192
211
225
SEQRES: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
COORDS: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
1193
1207
226
240
SEQRES: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
COORDS: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
1208
1222
241
255
SEQRES: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
COORDS: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
1223
1237
256
270
SEQRES: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
COORDS: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
1238
1252
271
285
SEQRES: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
COORDS: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
1253
1267
286
300
SEQRES: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
COORDS: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
1268
1282
301
315
SEQRES: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
COORDS: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
1283
1297
316
330
SEQRES: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
COORDS: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
1298
1312
331
334
SEQRES: ARG LEU ARG LYS
COORDS: ARG LEU ARG LYS
1313
1316
PDB Chain_ID: H
1
15
SEQRES: MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN LEU TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
?
?
?
?
?
16
30
SEQRES: PHE GLN GLY MET SER GLN LYS GLU GLN THR LEU MET THR PRO TYR
COORDS:
?
?
?
?
?
?
?
?
?
? LEU MET THR PRO TYR
1008
1012
31
45
SEQRES: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
COORDS: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU
?
?
?
?
1013
1023
46
60
SEQRES: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
COORDS:
?
? THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
1030
1042
61
75
SEQRES: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
COORDS: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
1043
1057
76
90
SEQRES: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
COORDS: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
1058
1072
91
105
SEQRES: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
COORDS: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
1073
1087
106
120
SEQRES: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
COORDS: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
1088
1102
121
135
SEQRES: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
COORDS: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
1103
1117
136
150
SEQRES: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
COORDS: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
1118
1132
151
165
SEQRES: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
COORDS: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
1133
1147
166
180
SEQRES: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
COORDS: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
1148
1162
181
195
SEQRES: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
COORDS: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
1163
1177
196
210
SEQRES: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
COORDS: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
1178
1192
211
225
SEQRES: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
COORDS: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
1193
1207
226
240
SEQRES: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
COORDS: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
1208
1222
241
255
SEQRES: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
COORDS: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
1223
1237
256
270
SEQRES: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
COORDS: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
1238
1252
271
285
SEQRES: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
COORDS: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
1253
1267
286
300
SEQRES: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
COORDS: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
1268
1282
301
315
SEQRES: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
COORDS: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
1283
1297
316
330
SEQRES: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
COORDS: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
1298
1312
331
334
SEQRES: ARG LEU ARG LYS
COORDS: ARG LEU ARG LYS
1313
1316
(4GI7_pdf_valid.pdf)
CLOSE CONTACTS
-------------==> Close contacts in same asymmetric unit. Distances smaller than 2.2
Angstroms are considered as close contacts.
none
==> Close contacts based on crystal symmetry. Distances smaller than 2.2
Angstroms are considered as close contacts.
none
BOND DISTANCES AND ANGLES
------------------------==> Bond and angle checks are performed by first computing the average rms
error for all bonds and angles relative to standard values for nucleotide
units [L. Clowney et al., Geometric Parameters in Nucleic Acids: Nitrogenous
Bases, J.Am.Chem.Soc. 1996, 118, 509-518; A. Gelbin et al., Geometric
Parameters in Nucleic Acids: Sugar and Phosphate Constituents, J.Am.Chem.Soc.
1996, 118, 519-529] and amino acid units [R.A. Engh and R. Huber, Structure
quality and target parameters, International Tables for Crystallography,
Volume F, 2001, 382-392]. Any bond or angle which deviates from the
dictionary values by more than six times this computed rms error is
identified as an outlier.
*** Covalent Bond Lengths:
The overall RMS deviation for covalent bonds relative to the standard
dictionary is
0.011 Angstroms
All covalent bonds lie within a 6.0*RMSD range about the
standard dictionary values.
*** Covalent Angle Values:
The overall RMS deviation for covalent angles relative to the standard
dictionary is
1.3 degrees.
The following table contains a list of the covalent bond angles
greater than 6 times standard deviation.
Deviation
Residue Chain Sequence AT1 - AT2 - AT3
Bond
Dictionary Standard
Name
ID
Number
Angle
Value
Deviation
------------------------------------------------------------------------------------------5.5
ASP
A
1230
CB
- CG
- OD1
123.8
118.3
0.9
18.6
MET
F
1029
CB
- CG
- SD
131.0
112.4
3.0
2 out of total 27624 bond angles (0.007%) have greater than 6 times
standard deviation.
TORSION ANGLES
-------------The torsion angle distributions have been checked. Refer to the
Procheck and/or Nucheck results on the PDB Validation Report page.
==> The following table contains a list of torsion angles outside the expected
Ramachandran regions [GJ. Kleywegt and TA. Jones, PHI/PSI-chology:
Ramachandran Revisited, Structure 1996, 4, 1395 - 1400].
Residue
GLN
ASP
SER
THR
ASN
ILE
GLN
ASP
ILE
SER
SER
ILE
HIS
GLN
ASP
SER
ASN
ILE
HIS
ASP
ALA
ILE
SER
HIS
GLN
ASP
ASN
ILE
HIS
ASP
GLN
ASP
ILE
ASN
ILE
ASN
GLN
HIS
GLN
ASP
ILE
SER
HIS
GLN
ASP
ASP
SER
Chain
A
A
A
C
C
C
C
C
C
C
B
B
B
B
B
B
D
D
D
D
D
D
D
E
E
E
F
F
F
F
F
F
F
G
G
G
G
G
G
G
G
G
H
H
H
H
H
Sequence
1192
1213
1304
1030
1043
1054
1192
1213
1281
1304
1026
1054
1118
1192
1213
1304
1043
1054
1118
1213
1263
1281
1304
1118
1192
1213
1043
1054
1118
1185
1192
1213
1281
1043
1054
1083
1085
1118
1192
1213
1281
1304
1118
1192
1213
1254
1304
PSI
65.15
71.64
-159.56
43.59
119.06
-59.50
64.82
75.83
-70.53
-159.88
-17.06
-55.14
73.54
65.89
74.06
-167.99
113.88
-57.91
66.40
74.78
3.34
-72.39
-164.94
70.02
64.55
74.09
117.12
-59.54
66.97
53.35
57.20
75.68
-70.52
116.08
-58.50
-174.32
102.64
65.95
61.67
76.92
-68.25
-164.06
81.56
62.06
73.40
71.15
-165.82
PHI
38.17
-168.51
-124.92
-106.87
-161.07
-121.74
32.27
-161.63
-111.02
-121.99
79.10
-120.33
-152.49
32.80
-168.38
-123.17
-163.99
-123.65
-157.97
-161.05
-56.28
-107.55
-126.76
-153.12
31.08
-158.77
-162.08
-123.27
-152.46
-157.83
39.88
-163.41
-117.24
-162.04
-123.38
-68.16
-39.36
-153.16
37.70
-167.00
-104.82
-124.38
-154.99
33.02
-166.61
-168.12
-113.41
CHIRALITY
--------The chirality has been checked. O1P, O2P, and hydrogen atoms which do not
follow the conventions defined by IUBMB (Liebecq, C. Compendium of
Biochemical Nomenclature and Related Documents, 2nd ed.; Portland Press:
London and Chapel Hill, 1992) and IUPAC (J.L. Markley, A. Bax,
Y. Arata, C.W. Hilbers, R. Kaptein, B.D. Sykes, P.E. Wright and K. Wuthrich,
Recommendations for the Presentation of NMR Structures of Proteins and
Nucleic Acids, Pure & Appl. Chem., Vol. 70, pp. 117-142, 1998) will be
standardized at the time of processing; there is no need to change these
labels in your coordinate file. Any other stereochemical violations are
listed below.
none
SOLVENT
------The following solvent molecules are further than 3.5 Angstroms away from
macromolecule atoms in the asymmetric unit that are available for
hydrogen bonding. Solvent molecules in extended hydration shells
separated by 3.5 Angstroms or less are not listed.
none
We have replaced the coordinates for solvent molecules which could be
translated back into the asymmetric unit. Please review all solvent
molecules in your file and contact us if you have any serious objections.
MISSING RESIDUES
---------------==> The following residues are missing:
(Note: The SEQ number starts from 1 for each chain according to SEQRES
sequence record.)
RES MOD#C SEQ
MET(
HIS(
HIS(
HIS(
HIS(
HIS(
HIS(
SER(
SER(
GLY(
ARG(
GLU(
ASN(
LEU(
TYR(
PHE(
GLN(
GLY(
MET(
SER(
GLN(
LYS(
GLU(
GLN(
THR(
MET(
HIS(
HIS(
HIS(
HIS(
HIS(
HIS(
SER(
SER(
GLY(
ARG(
GLU(
ASN(
LEU(
TYR(
PHE(
A 983
A 984
A 985
A 986
A 987
A 988
A 989
A 990
A 991
A 992
A 993
A 994
A 995
A 996
A 997
A 998
A 999
A1000
A1001
A1002
A1003
A1004
A1005
A1006
A1007
C 983
C 984
C 985
C 986
C 987
C 988
C 989
C 990
C 991
C 992
C 993
C 994
C 995
C 996
C 997
C 998
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
GLN(
GLY(
MET(
SER(
GLN(
LYS(
GLU(
GLN(
THR(
MET(
HIS(
HIS(
HIS(
HIS(
HIS(
HIS(
SER(
SER(
GLY(
ARG(
GLU(
ASN(
LEU(
TYR(
PHE(
GLN(
GLY(
MET(
SER(
GLN(
LYS(
GLU(
GLN(
THR(
MET(
HIS(
HIS(
HIS(
HIS(
HIS(
HIS(
SER(
SER(
GLY(
ARG(
GLU(
ASN(
LEU(
TYR(
PHE(
GLN(
GLY(
MET(
SER(
GLN(
LYS(
GLU(
GLN(
THR(
LEU(
MET(
HIS(
HIS(
HIS(
HIS(
HIS(
HIS(
SER(
C 999
C1000
C1001
C1002
C1003
C1004
C1005
C1006
C1007
B 983
B 984
B 985
B 986
B 987
B 988
B 989
B 990
B 991
B 992
B 993
B 994
B 995
B 996
B 997
B 998
B 999
B1000
B1001
B1002
B1003
B1004
B1005
B1006
B1007
D 983
D 984
D 985
D 986
D 987
D 988
D 989
D 990
D 991
D 992
D 993
D 994
D 995
D 996
D 997
D 998
D 999
D1000
D1001
D1002
D1003
D1004
D1005
D1006
D1007
D1008
E 983
E 984
E 985
E 986
E 987
E 988
E 989
E 990
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
SER(
GLY(
ARG(
GLU(
ASN(
LEU(
TYR(
PHE(
GLN(
GLY(
MET(
SER(
GLN(
LYS(
GLU(
GLN(
THR(
ASP(
SER(
VAL(
PRO(
MET(
MET(
HIS(
HIS(
HIS(
HIS(
HIS(
HIS(
SER(
SER(
GLY(
ARG(
GLU(
ASN(
LEU(
TYR(
PHE(
GLN(
GLY(
MET(
SER(
GLN(
LYS(
GLU(
GLN(
THR(
MET(
HIS(
HIS(
HIS(
HIS(
HIS(
HIS(
SER(
SER(
GLY(
ARG(
GLU(
ASN(
LEU(
TYR(
PHE(
GLN(
GLY(
MET(
SER(
GLN(
E 991
E 992
E 993
E 994
E 995
E 996
E 997
E 998
E 999
E1000
E1001
E1002
E1003
E1004
E1005
E1006
E1007
E1025
E1026
E1027
E1028
E1029
F 983
F 984
F 985
F 986
F 987
F 988
F 989
F 990
F 991
F 992
F 993
F 994
F 995
F 996
F 997
F 998
F 999
F1000
F1001
F1002
F1003
F1004
F1005
F1006
F1007
G 983
G 984
G 985
G 986
G 987
G 988
G 989
G 990
G 991
G 992
G 993
G 994
G 995
G 996
G 997
G 998
G 999
G1000
G1001
G1002
G1003
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
LYS(
GLU(
GLN(
THR(
LEU(
MET(
HIS(
HIS(
HIS(
HIS(
HIS(
HIS(
SER(
SER(
GLY(
ARG(
GLU(
ASN(
LEU(
TYR(
PHE(
GLN(
GLY(
MET(
SER(
GLN(
LYS(
GLU(
GLN(
THR(
ARG(
ASP(
SER(
VAL(
PRO(
MET(
G1004
G1005
G1006
G1007
G1008
H 983
H 984
H 985
H 986
H 987
H 988
H 989
H 990
H 991
H 992
H 993
H 994
H 995
H 996
H 997
H 998
H 999
H1000
H1001
H1002
H1003
H1004
H1005
H1006
H1007
H1024
H1025
H1026
H1027
H1028
H1029
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
)
PDB Chain_ID: A
1
15
SEQRES: MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN LEU TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
?
?
?
?
?
16
30
SEQRES: PHE GLN GLY MET SER GLN LYS GLU GLN THR LEU MET THR PRO TYR
COORDS:
?
?
?
?
?
?
?
?
?
? LEU MET THR PRO TYR
1008
1012
31
45
SEQRES: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
COORDS: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
1013
1027
46
60
SEQRES: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
COORDS: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
1028
1042
61
75
SEQRES: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
COORDS: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
1043
1057
76
90
SEQRES: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
COORDS: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
1058
1072
91
105
SEQRES: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
COORDS: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
1073
1087
106
120
SEQRES: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
COORDS: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
1088
1102
121
135
SEQRES: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
COORDS: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
1103
1117
136
150
SEQRES: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
COORDS: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
1118
1132
151
165
SEQRES: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
COORDS: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
1133
1147
166
180
SEQRES: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
COORDS: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
1148
1162
181
195
SEQRES: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
COORDS: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
1163
1177
196
210
SEQRES: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
COORDS: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
1178
1192
211
225
SEQRES: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
COORDS: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
1193
1207
226
240
SEQRES: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
COORDS: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
1208
1222
241
255
SEQRES: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
COORDS: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
1223
1237
256
270
SEQRES: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
COORDS: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
1238
1252
271
285
SEQRES: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
COORDS: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
1253
1267
286
300
SEQRES: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
COORDS: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
1268
1282
301
315
SEQRES: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
COORDS: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
1283
1297
316
330
SEQRES: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
COORDS: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
1298
1312
331
334
SEQRES: ARG LEU ARG LYS
COORDS: ARG LEU ARG LYS
1313
1316
PDB Chain_ID: C
1
15
SEQRES: MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN LEU TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
?
?
?
?
?
16
30
SEQRES: PHE GLN GLY MET SER GLN LYS GLU GLN THR LEU MET THR PRO TYR
COORDS:
?
?
?
?
?
?
?
?
?
? LEU MET THR PRO TYR
1008
1012
31
45
SEQRES: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
COORDS: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
1013
1027
46
60
SEQRES: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
COORDS: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
1028
1042
61
75
SEQRES: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
COORDS: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
1043
1057
76
90
SEQRES: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
COORDS: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
1058
1072
91
105
SEQRES: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
COORDS: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
1073
1087
106
120
SEQRES: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
COORDS: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
1088
1102
121
135
SEQRES: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
COORDS: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
1103
1117
136
150
SEQRES: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
COORDS: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
1118
1132
151
165
SEQRES: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
COORDS: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
1133
1147
166
180
SEQRES: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
COORDS: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
1148
1162
181
195
SEQRES: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
COORDS: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
1163
1177
196
210
SEQRES: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
COORDS: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
1178
1192
211
225
SEQRES: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
COORDS: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
1193
1207
226
240
SEQRES: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
COORDS: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
1208
1222
241
255
SEQRES: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
COORDS: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
1223
1237
256
270
SEQRES: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
COORDS: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
1238
1252
271
285
SEQRES: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
COORDS: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
1253
1267
286
300
SEQRES: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
COORDS: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
1268
1282
301
315
SEQRES: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
COORDS: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
1283
1297
316
330
SEQRES: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
COORDS: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
1298
1312
331
334
SEQRES: ARG LEU ARG LYS
COORDS: ARG LEU ARG LYS
1313
1316
PDB Chain_ID: B
1
15
SEQRES: MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN LEU TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
?
?
?
?
?
16
30
SEQRES: PHE GLN GLY MET SER GLN LYS GLU GLN THR LEU MET THR PRO TYR
COORDS:
?
?
?
?
?
?
?
?
?
? LEU MET THR PRO TYR
1008
1012
31
45
SEQRES: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
COORDS: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
1013
1027
46
60
SEQRES: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
COORDS: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
1028
1042
61
75
SEQRES: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
COORDS: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
1043
1057
76
90
SEQRES: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
COORDS: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
1058
1072
91
105
SEQRES: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
COORDS: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
1073
1087
106
120
SEQRES: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
COORDS: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
1088
1102
121
135
SEQRES: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
COORDS: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
1103
1117
136
150
SEQRES: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
COORDS: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
1118
1132
151
165
SEQRES: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
COORDS: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
1133
1147
166
180
SEQRES: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
COORDS: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
1148
1162
181
195
SEQRES: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
COORDS: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
1163
1177
196
210
SEQRES: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
COORDS: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
1178
1192
211
225
SEQRES: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
COORDS: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
1193
1207
226
240
SEQRES: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
COORDS: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
1208
1222
241
255
SEQRES: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
COORDS: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
1223
1237
256
270
SEQRES: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
COORDS: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
1238
1252
271
285
SEQRES: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
COORDS: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
1253
1267
286
300
SEQRES: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
COORDS: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
1268
1282
301
315
SEQRES: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
COORDS: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
1283
1297
316
330
SEQRES: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
COORDS: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
1298
1312
331
334
SEQRES: ARG LEU ARG LYS
COORDS: ARG LEU ARG LYS
1313
1316
PDB Chain_ID: D
1
15
SEQRES: MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN LEU TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
?
?
?
?
?
16
30
SEQRES: PHE GLN GLY MET SER GLN LYS GLU GLN THR LEU MET THR PRO TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
? MET THR PRO TYR
1009
1012
31
45
SEQRES: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
COORDS: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
1013
1027
46
60
SEQRES: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
COORDS: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
1028
1042
61
75
SEQRES: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
COORDS: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
1043
1057
76
90
SEQRES: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
COORDS: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
1058
1072
91
105
SEQRES: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
COORDS: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
1073
1087
106
120
SEQRES: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
COORDS: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
1088
1102
121
135
SEQRES: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
COORDS: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
1103
1117
136
150
SEQRES: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
COORDS: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
1118
1132
151
165
SEQRES: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
COORDS: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
1133
1147
166
180
SEQRES: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
COORDS: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
1148
1162
181
195
SEQRES: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
COORDS: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
1163
1177
196
210
SEQRES: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
COORDS: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
1178
1192
211
225
SEQRES: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
COORDS: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
1193
1207
226
240
SEQRES: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
COORDS: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
1208
1222
241
255
SEQRES: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
COORDS: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
1223
1237
256
270
SEQRES: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
COORDS: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
1238
1252
271
285
SEQRES: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
COORDS: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
1253
1267
286
300
SEQRES: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
COORDS: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
1268
1282
301
315
SEQRES: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
COORDS: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
1283
1297
316
330
SEQRES: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
COORDS: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
1298
1312
331
334
SEQRES: ARG LEU ARG LYS
COORDS: ARG LEU ARG LYS
1313
1316
PDB Chain_ID: E
1
15
SEQRES: MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN LEU TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
?
?
?
?
?
16
30
SEQRES: PHE GLN GLY MET SER GLN LYS GLU GLN THR LEU MET THR PRO TYR
COORDS:
?
?
?
?
?
?
?
?
?
? LEU MET THR PRO TYR
1008
1012
31
45
SEQRES: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
COORDS: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG
?
?
?
1013
1024
46
60
SEQRES: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
COORDS:
?
? THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
1030
1042
61
75
SEQRES: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
COORDS: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
1043
1057
76
90
SEQRES: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
COORDS: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
1058
1072
91
105
SEQRES: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
COORDS: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
1073
1087
106
120
SEQRES: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
COORDS: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
1088
1102
121
135
SEQRES: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
COORDS: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
1103
1117
136
150
SEQRES: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
COORDS: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
1118
1132
151
165
SEQRES: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
COORDS: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
1133
1147
166
180
SEQRES: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
COORDS: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
1148
1162
181
195
SEQRES: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
COORDS: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
1163
1177
196
210
SEQRES: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
COORDS: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
1178
1192
211
225
SEQRES: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
COORDS: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
1193
1207
226
240
SEQRES: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
COORDS: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
1208
1222
241
255
SEQRES: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
COORDS: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
1223
1237
256
270
SEQRES: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
COORDS: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
1238
1252
271
285
SEQRES: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
COORDS: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
1253
1267
286
300
SEQRES: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
COORDS: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
1268
1282
301
315
SEQRES: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
COORDS: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
1283
1297
316
330
SEQRES: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
COORDS: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
1298
1312
331
334
SEQRES: ARG LEU ARG LYS
COORDS: ARG LEU ARG LYS
1313
1316
PDB Chain_ID: F
1
15
SEQRES: MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN LEU TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
?
?
?
?
?
16
30
SEQRES: PHE GLN GLY MET SER GLN LYS GLU GLN THR LEU MET THR PRO TYR
COORDS:
?
?
?
?
?
?
?
?
?
? LEU MET THR PRO TYR
1008
1012
31
45
SEQRES: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
COORDS: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
1013
1027
46
60
SEQRES: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
COORDS: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
1028
1042
61
75
SEQRES: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
COORDS: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
1043
1057
76
90
SEQRES: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
COORDS: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
1058
1072
91
105
SEQRES: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
COORDS: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
1073
1087
106
120
SEQRES: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
COORDS: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
1088
1102
121
135
SEQRES: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
COORDS: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
1103
1117
136
150
SEQRES: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
COORDS: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
1118
1132
151
165
SEQRES: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
COORDS: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
1133
1147
166
180
SEQRES: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
COORDS: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
1148
1162
181
195
SEQRES: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
COORDS: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
1163
1177
196
210
SEQRES: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
COORDS: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
1178
1192
211
225
SEQRES: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
COORDS: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
1193
1207
226
240
SEQRES: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
COORDS: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
1208
1222
241
255
SEQRES: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
COORDS: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
1223
1237
256
270
SEQRES: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
COORDS: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
1238
1252
271
285
SEQRES: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
COORDS: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
1253
1267
286
300
SEQRES: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
COORDS: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
1268
1282
301
315
SEQRES: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
COORDS: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
1283
1297
316
330
SEQRES: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
COORDS: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
1298
1312
331
334
SEQRES: ARG LEU ARG LYS
COORDS: ARG LEU ARG LYS
1313
1316
PDB Chain_ID: G
1
15
SEQRES: MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN LEU TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
?
?
?
?
?
16
30
SEQRES: PHE GLN GLY MET SER GLN LYS GLU GLN THR LEU MET THR PRO TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
? MET THR PRO TYR
1009
1012
31
45
SEQRES: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
COORDS: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
1013
1027
46
60
SEQRES: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
COORDS: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
1028
1042
61
75
SEQRES: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
COORDS: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
1043
1057
76
90
SEQRES: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
COORDS: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
1058
1072
91
105
SEQRES: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
COORDS: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
1073
1087
106
120
SEQRES: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
COORDS: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
1088
1102
121
135
SEQRES: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
COORDS: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
1103
1117
136
150
SEQRES: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
COORDS: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
1118
1132
151
165
SEQRES: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
COORDS: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
1133
1147
166
180
SEQRES: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
COORDS: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
1148
1162
181
195
SEQRES: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
COORDS: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
1163
1177
196
210
SEQRES: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
COORDS: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
1178
1192
211
225
SEQRES: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
COORDS: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
1193
1207
226
240
SEQRES: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
COORDS: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
1208
1222
241
255
SEQRES: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
COORDS: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
1223
1237
256
270
SEQRES: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
COORDS: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
1238
1252
271
285
SEQRES: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
COORDS: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
1253
1267
286
300
SEQRES: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
COORDS: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
1268
1282
301
315
SEQRES: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
COORDS: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
1283
1297
316
330
SEQRES: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
COORDS: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
1298
1312
331
334
SEQRES: ARG LEU ARG LYS
COORDS: ARG LEU ARG LYS
1313
1316
PDB Chain_ID: H
1
15
SEQRES: MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN LEU TYR
COORDS:
?
?
?
?
?
?
?
?
?
?
?
?
?
?
?
16
30
SEQRES: PHE GLN GLY MET SER GLN LYS GLU GLN THR LEU MET THR PRO TYR
COORDS:
?
?
?
?
?
?
?
?
?
? LEU MET THR PRO TYR
1008
1012
31
45
SEQRES: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU ARG ASP SER VAL
COORDS: LEU GLN PHE ASN ARG HIS GLN TRP ALA ALA LEU
?
?
?
?
1013
1023
46
60
SEQRES: PRO MET THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
COORDS:
?
? THR LEU THR GLU ASP GLU ILE THR ARG LEU LYS GLY ILE
1030
1042
61
75
SEQRES: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
COORDS: ASN GLU ASP LEU SER LEU GLU GLU VAL ALA GLU ILE TYR LEU PRO
1043
1057
76
90
SEQRES: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
COORDS: LEU SER ARG LEU LEU ASN PHE TYR ILE SER SER ASN LEU ARG ARG
1058
1072
91
105
SEQRES: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
COORDS: GLN ALA VAL LEU GLU GLN PHE LEU GLY THR ASN GLY GLN ARG ILE
1073
1087
106
120
SEQRES: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
COORDS: PRO TYR ILE ILE SER ILE ALA GLY SER VAL ALA VAL GLY LYS SER
1088
1102
121
135
SEQRES: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
COORDS: THR THR ALA ARG VAL LEU GLN ALA LEU LEU SER ARG TRP PRO GLU
1103
1117
136
150
SEQRES: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
COORDS: HIS ARG HIS VAL GLU LEU ILE THR THR ASP GLY PHE LEU HIS PRO
1118
1132
151
165
SEQRES: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
COORDS: ASN SER VAL LEU LYS GLU ARG GLY LEU MET LYS LYS LYS GLY PHE
1133
1147
166
180
SEQRES: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
COORDS: PRO GLN SER TYR ASP MET HIS ARG LEU VAL LYS PHE VAL SER ASP
1148
1162
181
195
SEQRES: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
COORDS: LEU LYS SER GLY VAL PRO GLN ALA THR ALA PRO VAL TYR SER HIS
1163
1177
196
210
SEQRES: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
COORDS: LEU ILE TYR ASP VAL ILE PRO ASP GLY ASP LYS THR VAL ALA GLN
1178
1192
211
225
SEQRES: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
COORDS: PRO ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN SER GLY
1193
1207
226
240
SEQRES: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
COORDS: MET ASP TYR PRO HIS ASP PRO HIS HIS VAL PHE VAL SER ASP PHE
1208
1222
241
255
SEQRES: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
COORDS: VAL ASP PHE SER ILE TYR VAL ASP ALA PRO GLU GLU LEU LEU LYS
1223
1237
256
270
SEQRES: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
COORDS: SER TRP TYR ILE ASN ARG PHE LEU LYS PHE ARG GLU GLY ALA PHE
1238
1252
271
285
SEQRES: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
COORDS: THR ASP PRO ASP SER TYR PHE HIS ASN TYR ALA LYS LEU SER LYS
1253
1267
286
300
SEQRES: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
COORDS: GLU GLU ALA VAL ASP ILE ALA THR SER LEU TRP ASN GLU ILE ASN
1268
1282
301
315
SEQRES: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
COORDS: LEU MET ASN LEU LYS GLU ASN ILE LEU PRO THR ARG GLU ARG ALA
1283
1297
316
330
SEQRES: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
COORDS: SER LEU ILE MET THR LYS SER ALA ASN HIS SER VAL ASN GLN VAL
1298
1312
331
334
SEQRES: ARG LEU ARG LYS
COORDS: ARG LEU ARG LYS
1313
1316