SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 7022699 FitnessBrowser__ANA3:7022699 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

P00392 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Pseudomonas aeruginosa (see paper)
93% identity, 100% coverage: 1:561/561 of query aligns to 1:561/561 of P00392

query
sites
P00392

M
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M

T

T

T

H

L

L

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K

I

I

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G

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M

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T

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C

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D

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Y

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K

A

A

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L

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D

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D

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I

M

G

A

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A

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E

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K

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G

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R

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I

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T

C
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C

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V

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N

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G

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C

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P

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D

E

E

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L

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R

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H

A

A

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K

Y

Y

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E

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D

G

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G

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A

A

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T

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V

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H

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E

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A

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F

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K

D

D

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D

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L

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N

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E

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G

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E

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M

M

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F

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D

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C

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A

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L

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G

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K

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D

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G

M1 (= M1) modified: Initiator methionine, Removed
C136 (= C136) modified: Disulfide link with 141, Redox-active
C141 (= C141) modified: Disulfide link with 136, Redox-active

4k8dA Crystal structure of the c558(464)a/c559(465)a double mutant of tn501 mera in complex with NADPH and hg2+
94% identity, 83% coverage: 96:561/561 of query aligns to 1:466/466 of 4k8dA

query
sites
4k8dA

E

E

R

P

P

P

L

V

Q

Q

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A

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I
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I

G
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G

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G
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G

G
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G

A
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A

A

A

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M

A

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A

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A

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L

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K

A

A

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E

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I
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I

E
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R

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G

T

T

I
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I

G

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G
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G

T
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T

C
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C

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N

N

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V

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G

C
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C

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V

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S

K
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K

I

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M

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E

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P

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D

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M

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T

P
x
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T

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L

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D

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E

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R

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H

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E

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G

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R

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F

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K

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D

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D

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L

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N

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M

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F

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D

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C

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K

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R

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L

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G

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S

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K

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L

L

A

A

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R

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N

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L

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R

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E

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D

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D

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T

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L

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D

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P

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A

A

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L

A

A

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N

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F

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D

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G

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F

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A

A

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E

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I

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L

A

A

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I

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N

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M

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T

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V

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Q

E

E

L

L

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A

D

D

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Q

L

L

F
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F

P

P

Y
|
Y

L

L

T

T

M

M

V

V

E
|
E

G

G

L

L

K

K

L

L

A

A

A

A

Q

Q

T

T

F

F

S

N

K

K

D

D

V

V

K

K

Q

Q

L

L

S

S

C
x
A

C
x
A

A

A

G

G

active site: G13 (= G108), I37 (= I132), C41 (= C136), C46 (= C141), S49 (= S144), V75 (≠ P170), P76 (= P171), V185 (= V280), E189 (= E284), A320 (= A415), F438 (= F533), Y440 (= Y535), E445 (= E540), A463 (≠ C558), A464 (≠ C559)
binding flavin-adenine dinucleotide: I9 (= I104), G10 (= G105), G12 (= G107), G13 (= G108), A14 (= A109), I32 (= I127), E33 (= E128), R34 (= R129), G39 (= G134), T40 (= T135), C41 (= C136), V44 (= V139), G45 (= G140), C46 (= C141), S49 (= S144), K50 (= K145), G114 (= G209), E115 (= E210), A116 (= A211), A144 (= A239), T145 (= T240), G146 (= G241), S165 (= S260), R268 (= R363), G307 (= G402), D308 (= D403), Q314 (= Q409), F315 (= F410), V316 (= V411), Y317 (= Y412), A319 (= A414), F347 (= F442)
binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K50 (= K145), P152 (= P247), S183 (= S278), S184 (= S279), V185 (= V280), V186 (= V281), E189 (= E284), R206 (= R301), N207 (= N302), F211 (= F306), R212 (= R307), A265 (= A360), T266 (= T361), G267 (= G362), R268 (= R363), Q314 (= Q409), F315 (= F410), V345 (= V440), F347 (= F442)

4k7zA Crystal structure of the c136(42)a/c141(47)a double mutant of tn501 mera in complex with NADP and hg2+
94% identity, 83% coverage: 96:561/561 of query aligns to 2:467/467 of 4k7zA

query
sites
4k7zA

E

E

R

P

P

P

L

V

Q

Q

V

V

V

A

V

V

I
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I

G
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G

S

S

G
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G

G
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G

A
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A

A

A

M

M

A

A

A

A

A

A

L

L

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K

A

A

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V

E

E

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Q

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G

A

A

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Q

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T

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L

I
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I

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E

R
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R

G

G

T

T

I
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I

G

G

G
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G

T
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T

C
x
A

V

V

N

N

V

V

G
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G

C
x
A

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V

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S

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K

I

I

M

M

I

I

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R

A

A

A

A

H

H

I

I

A

A

H

H

L

L

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R

R

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E

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S

P

P

F

F

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D

G

G

G

G

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I

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P

A

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T

P
x
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P
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P

T

T

I

I

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D

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L

L

L

L

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A

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E

D

E

E

L

L

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R

H

H

A

A

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K

Y

Y

E

E

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G

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I

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L

D

G

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G

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A

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T

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G

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E

A
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A

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R

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F

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K

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D

D

D

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Q

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S

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L

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L

N

N

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E

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G

G

G

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E

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M

M

F

F

D

D

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R

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C

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L

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A

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T

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G

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S

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A

A

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P

P

P

I

I

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L

K

K

E

E

S

S

P

P

Y

Y

W

W

T

T

S
|
S

T

T

E

E

A

A

L

L

A

A

S

S

D

D

T

T

I

I

P

P

E

E

R

R

L

L

A

A

V

V

I

I

G

G

S
|
S

S
|
S

V
|
V

V
|
V

A

A

L

L

E
|
E

L

L

A

A

Q

Q

A

A

F

F

A

A

R

R

L

L

G

G

S

S

K

K

V

V

T

T

A

V

L

L

A

A

R
|
R

N
|
N

T

T

L

L

F

F

F
|
F

R
|
R

E

E

D

D

P

P

A

A

I

I

G

G

E

E

A

A

V

V

T

T

A

A

A

A

F

F

R

R

A

A

E

E

G

G

I

I

E

E

V

V

L

L

E

E

H

H

T

T

Q

Q

A

A

S

S

Q

Q

V

V

A

A

H

H

M

M

D

D

G

G

E

E

F

F

V

V

L

L

T

T

T

T

T

T

H

H

G

G

E

E

L

L

R

R

A

A

D

D

K

K

L

L

L

L

V

V

A
|
A

T
|
T

G
|
G

R
|
R

T

T

P

P

N

N

T

T

R

R

S

S

L

L

A

A

L

L

E

D

A

A

A

A

G

G

V

V

A

T

V

V

N

N

A

A

Q

Q

G

G

A

A

I

I

V

V

I

I

D

D

K

Q

G

G

M

M

R

R

T

T

S

S

S

N

P

P

N

N

I

I

Y

Y

A

A

A

A

G
|
G

D
|
D

C

C

T

T

D

D

Q

Q

P

P

Q
|
Q

F
|
F

V
|
V

Y
|
Y

V

V

A
|
A

A
|
A

A

A

A

A

G

G

T

T

R

R

A

A

A

A

I

I

N

N

M

M

T

T

G

G

G

G

D

D

A

A

A

A

L

L

D

D

L

L

T

T

A

A

M

M

P

P

A

A

V
|
V

V

V

F
|
F

T

T

D

D

P

P

Q

Q

V

V

A

A

T

T

V

V

G

G

Y

Y

S

S

E

E

A

A

E

E

A

A

H

H

H

H

D

D

G

G

I

I

E

E

T

T

D

D

S

S

R

R

L

T

L

L

T

T

L

L

D

D

N

N

V

V

P

P

R

R

A

A

L

L

A

A

N

N

F

F

D

D

T

T

R

R

G

G

F

F

I

I

K

K

L

L

V

V

I

I

E

E

E

E

G

G

S

S

G

H

R

R

L

L

I

I

G

G

V

V

Q

Q

A

A

V

V

A

A

P

P

E

E

A

A

G

G

E

E

L

L

I

I

Q

Q

T

T

A

A

V

A

L

L

A

A

I

I

R

R

N

N

R

R

M

M

T

T

V

V

Q

Q

E

E

L

L

A

A

D

D

Q

Q

L

L

F
|
F

P

P

Y
|
Y

L

L

T

T

M

M

V

V

E
|
E

G

G

L

L

K

K

L

L

A

A

A

A

Q

Q

T

T

F

F

S

N

K

K

D

D

V

V

K

K

Q

Q

L

L

S

S

C
|
C

C
|
C

A

A

G

G

active site: G14 (= G108), I38 (= I132), A42 (≠ C136), A47 (≠ C141), S50 (= S144), V76 (≠ P170), P77 (= P171), V186 (= V280), E190 (= E284), A321 (= A415), F439 (= F533), Y441 (= Y535), E446 (= E540), C464 (= C558), C465 (= C559)
binding flavin-adenine dinucleotide: I10 (= I104), G11 (= G105), G13 (= G107), G14 (= G108), A15 (= A109), I33 (= I127), E34 (= E128), R35 (= R129), G40 (= G134), T41 (= T135), A42 (≠ C136), G46 (= G140), A47 (≠ C141), S50 (= S144), K51 (= K145), G115 (= G209), E116 (= E210), A117 (= A211), A145 (= A239), T146 (= T240), G147 (= G241), S166 (= S260), R269 (= R363), G308 (= G402), D309 (= D403), Q315 (= Q409), F316 (= F410), V317 (= V411), Y318 (= Y412), A320 (= A414), F348 (= F442)
binding nadp nicotinamide-adenine-dinucleotide phosphate: K51 (= K145), P153 (= P247), S184 (= S278), S185 (= S279), V186 (= V280), V187 (= V281), E190 (= E284), R207 (= R301), N208 (= N302), F212 (= F306), R213 (= R307), A266 (= A360), T267 (= T361), G268 (= G362), R269 (= R363), Q315 (= Q409), F316 (= F410), V346 (= V440), F348 (= F442)

P16171 Mercuric reductase; Hg(II) reductase; EC 1.16.1.1 from Bacillus cereus (see paper)
41% identity, 99% coverage: 4:561/561 of query aligns to 85:631/631 of P16171

query
sites
P16171

L

L

K

N

I

V

T

E

G

G

M

M

T

T

C

C

D

T

S

G

C

C

A

E

A

E

H

H

V

I

K

A

E

V

A

A

L

L

E

E

K

N

V

A

P

-

G

G

V

A

Q

K

S

G

A

I

L

E

V

V

S

D

Y

F

P

R

K

R

G

G

T

E

A

A

Q

L

L

F

A

E

I

L

E

P

A

Y

G

D

T

V

S

D

S

I

D

D

A

I

L

A

T

K

T

T

A

A

V

I

A

T

G

D

L

A

G

Q

Y

Y

E

Q

A

-

T

-

L

-

A

-

D

-

A

-

P

P

P

G

T

E

D

A

N

E

R

E

A

I

G

Q

L

V

L

Q

D

S

K

E

M

K

R

R

G

T

W

D

I

V

G

S

A

L

A

N

D

D

K

E

P

-

S

-

G

G

N

N

E

-

R

Y

P

D

L

Y

Q

D

V

Y

V

I

V

I

I

I

G

G

S

S

G

G

G

G

A

A

A

A

M

F

A

S

A

S

A

A

L

I

K

E

A

A

V

V

E

A

Q

L

G

N

A

A

Q

K

V

V

T

A

L

M

I

I

E

E

R

R

G

G

T

T

I

V

G

G

G

G

T

T

C

C

V

V

N

N

V

V

G

G

C

C

V

V

P

P

S

S

K

K

I

T

M

L

I

L

R

R

A

A

A

G

H

E

I

I

A

N

H

H

L

L

R

A

R

K

E

N

S

N

P

P

F

F

D

-

G

V

G

G

M

L

P

H

P

T

T

S

P

A

P

S

T

N

I

V

L

D

R

L

E

A

R

P

L

L

L

V

A

K

Q

Q

Q

K

Q

N

A

D

R

L

V

V

E

T

E

E

L

M

R

R

H

N

A

E

K

K

Y
|
Y

E

V

G

N

I

L

L

I

D

D

G

-

N

D

S

Y

A

G

I

F

T

E

V

L

L

I

H

K

G

G

E

E

A

S

R

K

F

F

K

V

D

N

D

E

Q

N

S

T

L

V

I

E

V

V

S

N

L

G

N

N

E

Q

G

-

G

-

E

-

R

-

V

-

V

I

M

T

F

A

D

K

R

R

C

F

L

L

V

I

A

A

T

T

G

G

A

A

S

S

P

S

A

T

V

A

P

P

P

N

I

I

P

P

G

G

L

L

K

D

E

E

S

V

P

D

Y

Y

W

L

T

T

S

S

T

T

E

S

A

L

L

L

A

E

S

L

D

K

T

K

I

V

P

P

E

N

R

R

L

L

A

T

V

V

I

I

G

G

S

S

S

G

V

Y

V

I

A

G

L

M

E

E

L

L

A

G

Q

Q

A

L

F

F

A

H

R

N

L

L

G

G

S

S

K

E

V

V

T

T

A

L

L

I

A

Q

R

R

N

S

T

E

L

R

F

L

F

L

R

K

E

E

-

Y

D

D

P

P

A

E

I

I

G

S

E

E

A

A

V

I

T

T

A

K

A

A

F

L

R

T

A

E

E

Q

G

G

I

I

E

N

V

L

L

V

E

T

H

G

T

A

Q

T

A

Y

S

E

Q

R

V

V

A

-

H

E

M

Q

D

D

G

G

E

D

F

I

-

K

-

K

V

V

L

H

T

V

T

E

T

I

H

N

G

G

E

K

L

K

R

R

-

I

-

I

-

E

A

A

D

E

K

Q

L

L

L

L

V

I

A

A

T

T

G

G

R

R

T

K

P

P

N

I

T

Q

R

T

S

S

L

L

A

N

L

L

E

H

A

A

A

A

G

G

V

V

A

E

V

V

N

G

A

S

Q

R

G

G

A

E

I

I

V

V

I

I

D

D

K

D

G

Y

M

L

R

K

T

T

S

T

S

N

P

S

N

R

I

I

Y

Y

A

S

A

A

G

G

D

D

C

V

T

T

D

P

Q

G

P

P

Q

Q

F

F

V

V

Y

Y

V

V

A

A

A

A

A

Y

A

E

G

G

T

G

R

L

A

A

A

A

I

R

N

N

M

A

T

I

G

G

G

G

-

L

D

N

A

Q

A

K

L

V

D

N

L

L

T

E

A

V

M

V

P

P

A

G

V

V

V

T

F

F

T

T

D

S

P

P

Q

S

V

I

A

A

T

T

V

V

G

G

Y

L

S

T

E

E

A

Q

E

Q

A

A

H

K

H

E

D

K

G

G

I

Y

E

E

T

V

D

K

S

T

R

S

L

V

L

L

T

P

L

L

D

D

N

A

V

V

P

P

R

R

A

A

L

L

A

V

N

N

F

R

D

E

T

T

R

T

G

G

F

V

I

F

K

K

L

L

V

V

I

A

E

D

E

A

G

K

S

T

G

L

R

K

L

V

I

L

G

G

V

A

Q

H

A

V

V

V

A

A

P

E

E

N

A

A

G

G

E

D

L

V

I

I

Q

Y

T

A

A

A

V

T

L

L

A

A

I

V

R

K

N

F

R

G

M

L

T

T

V

V

Q

G

E

D

L

L

A

R

D

E

Q

T

L

M

F

A

P

P

Y
|
Y

L

L

T

T

M

M

V

A

E

E

G

G

L

L

K

K

L

L

A

A

A

V

Q

L

T

T

F

F

S

D

K

K

D

D

V

V

K

S

Q

K

L

L

S

S

C

C

C

C

A

A

G

G

Y264 (= Y194) mutation to F: 30-fold decrease in activity. 300-fold decrease in activity; when associated with F-605.
Y605 (= Y535) mutation to F: 10-fold decrease in activity. 300-fold decrease in activity; when associated with F-264.; mutation to H: 2-fold decrease in activity.

5x1yB Structure of mercuric reductase from lysinibacillus sphaericus (see paper)
44% identity, 81% coverage: 96:549/561 of query aligns to 1:453/454 of 5x1yB

query
sites
5x1yB

E

E

R

D

P

N

L

Y

Q

D

V

L

V

L

V

I

I
|
I

G
|
G

S
|
S

G
|
G

G
x
A

A
|
A

A

A

M

F

A

S

A

S

A

A

L

I

K

K

A

A

V

I

E

E

Q

Y

G

G

A

A

Q

K

V

V

T

G

L

M

I
|
I

E
|
E

R
|
R

G

G

T

T

I
x
V

G

G

G
|
G

T
|
T

C
|
C

V

V

N

N

V
x
I

G
|
G

C
|
C

V

V

P

P

S
|
S

K
|
K

I

T

M

L

I

L

R

R

A

A

A

G

H

E

I

I

A

I

H

H

L

L

R

S

R

K

E

D

S

N

P

P

F

F

D

I

G

G

G

-

M

L

P

Q

P

T

T

S

P
x
A

P
x
G

T

E

I

V

L

D

R

L

E

A

R

S

L

L

L

I

A

T

Q

Q

Q

K

Q

D

A

K

R

L

V

V

E

S

E

E

L

L

R

R

H

N

A

Q

K

K

Y

Y

E

M

G

D

I

L

L

I

D

D

G

-

N

E

S

Y

A

N

I

F

T

D

V

L

L

I

H

K

G
|
G

E
|
E

A
|
A

R

K

F

F

K

V

D

D

D

A

Q

S

S

T

L

V

I

E

V

V

S

N

L

-

N

-

E

-

G

-

G

G

E

A

R

K

V

L

V

S

M

A

F

-

D

K

R

R

C

F

L

L

V

I

A
|
A

T
|
T

G
|
G

A

A

S

S

P

P

A

S

V

L

P

P

P

Q

I

I

P

S

G

G

L

L

K

E

E

K

S

M

P

D

Y

Y

W

L

T

T

S
|
S

T

T

E

T

A

L

L

L

A

E

S

L

D

K

T

K

I

I

P

P

E

K

R

R

L

L

A

T

V

V

I

I

G

G

S

S

S

G

V
x
Y

V
x
I

A

G

L

M

E
|
E

L

L

A

G

Q

Q

A

L

F

F

A

H

R

H

L

L

G

G

S

S

K

E

V

I

T

T

A

L

L

M

A

Q

R

R

N

S

T

E

L

R

F

L

F

L

R

K

E

E

-

Y

D

D

P

P

A

E

I

I

G

S

E

E

A

S

V

V

T

E

A

K

A

A

F

L

R

I

A

E

E

Q

G

G

I

I

E

N

V

L

L

V

E

K

H

G

T

A

Q

T

A

F

S

E

Q

R

V

V

A

E

H

Q

M

-

D

S

G

G

E

E

F

I

-

K

-

R

V

V

L

Y

T

V

T

T

T

V

H

N

G

G

E

S

-

R

-

E

-

V

L

I

R

E

A

S

D

D

K

Q

L

L

L

L

V

V

A

A

T

T

G

G

R
|
R

T

K

P

P

N

N

T

T

R

D

S

S

L
|
L

A

N

L

L

E

S

A

A

A

A

G

G

V

V

A

E

V

T

N

G

A

K

Q

N

G

N

A

E

I

I

V

L

I

I

D

N

K

D

G

F

M

G

R

Q

T

T

S

S

S

N

P

E

N

K

I

I

Y

Y

A

A

A

A

G
|
G

D
|
D

C

V

T

T

D

L

Q

G

P

P

Q
|
Q

F
|
F

V
|
V

Y
|
Y

V

V

A
|
A

A
|
A

A

Y

A

E

G

G

T

G

R

I

A

I

A

T

I

D

N

N

M

A

T

I

G

G

G

G

-

L

D

N

A

K

A

K

L

I

D

D

L

L

T

S

A

V

M

V

P

P

A

A

V

V

V

T

F

F

T

T

D

N

P

P

Q

T

V

V

A

A

T

T

V

V

G

G

Y

L

S

T

E

E

A

E

E

Q

A

A

H

K

H

E

D

K

G

G

I

Y

E

D

T

V

D

K

S

T

R

S

L

V

L

L

T

P

L

L

D

D

N

A

V

V

P

P

R

R

A

A

L

I

A

V

N

N

F

R

D

E

T

T

R

T

G

G

F

V

I

F

K

K

L

L

V

V

I

A

E

D

E

A

G

E

S

T

G

L

R

K

L

V

I

L

G

G

V

V

Q

H

A

I

V

V

A

S

P

E

E

N

A

A

G

G

E

D

L

V

I

I

Q

Y

T

A

A

A

V

S

L

L

A

A

I

V

R

K

N

F

R

G

M

L

T

T

V

V

Q

E

E

D

L

L

A

T

D

E

Q

T

L

L

F
x
A

P

P

Y
|
Y

L

L

T

T

M

M

V

A

E
|
E

G

G

L

L

K

K

L

L

A

A

A

A

Q

L

T

T

F

F

active site: A13 (≠ G108), V37 (≠ I132), C41 (= C136), C46 (= C141), S49 (= S144), A74 (≠ P170), G75 (≠ P171), Y178 (≠ V280), E182 (= E284), A318 (= A415), A437 (≠ F533), Y439 (= Y535), E444 (= E540)
binding flavin-adenine dinucleotide: I9 (= I104), G10 (= G105), S11 (= S106), G12 (= G107), A13 (≠ G108), A14 (= A109), I32 (= I127), E33 (= E128), R34 (= R129), G39 (= G134), T40 (= T135), C41 (= C136), I44 (≠ V139), G45 (= G140), C46 (= C141), K50 (= K145), G112 (= G209), E113 (= E210), A114 (= A211), A137 (= A239), T138 (= T240), G139 (= G241), S158 (= S260), Y178 (≠ V280), I179 (≠ V281), R266 (= R363), L273 (= L370), G305 (= G402), D306 (= D403), Q312 (= Q409), F313 (= F410), V314 (= V411), Y315 (= Y412), A317 (= A414)

4ywoA Mercuric reductase from metallosphaera sedula (see paper)
37% identity, 81% coverage: 100:552/561 of query aligns to 7:444/444 of 4ywoA

query
sites
4ywoA

Q

K

V

L

V

A

V

I

I
|
I

G
|
G

S
x
Y

G
|
G

G
x
A

A
|
A

A

G

M

F

A

A

A

A

A

M

L

I

K

K

A

A

V

N

E

E

Q

L

G

G

A

V

Q

K

V

P

T

V

L

L

I
|
I

E
x
G

R
x
K

G
|
G

T

E

I
|
I

G

G

G
|
G

T
|
T

C
|
C

V

V

N

N

V
|
V

G
|
G

C
|
C

V

V

P

P

S
|
S

K
|
K

I

R

M

M

I

L

R

Y

A

I

A

A

H

E

I

I

A

Y

H

K

L

K

R

A

R

R

E

E

S

V

P

T

F

G

D

S

G

E

G

V

M

Y

P

P

P

P

T

F

P

S

P

S

T

-

I

-

L

-

R

-

E

-

R

-

L

-

L

F

A

Q

Q

E

Q

K

Q

D

A

G

R

L

V

V

E

Q

E

E

L

M

R

R

H

K

A

T

K

K

Y

Y

E

E

G

D

I

L

L

L

D

S

G

Y

N

Y

S

D

A

-

I

V

T

E

V

L

L

I

H

Q

G
|
G

E
|
E

A
|
A

R

R

F

F

K

I

D

S

D

P

Q

H

S

A

L

V

I

K

V

V

S

N

L

-

N

-

E

-

G

-

G

-

E

G

R

Q

V

V

V

I

M

E

F

A

D

E

R

K

C

F

L

V

V

I

A
|
A

T
|
T

G
|
G

A

S

S

S

P

P

A

L

V

I

P

P

P

R

I

I

P

P

G

G

L

L

K

D

E

K

S

V

P

G

Y

F

W

W

T

T

S
x
N

T

R

E

E

A

A

L

L

A

S

S

P

D

D

T

R

I

R

P

I

E

D

R

S

L

L

A

A

V

V

I

I

G

G

S

G

S

R

V
x
A

V
x
L

A

A

L

L

E
|
E

L
x
F

A

A

Q

Q

A

M

F

Y

A

S

R

R

L

M

G

K

S

V

K

E

V

V

T

A

A

I

L

L

A

Q

R

R

N

S

T

P

L

V

F

L

F

I

R

P

E

D

-

W

D

E

P

P

A

E

I

A

G

S

E

V

A

E

V

A

T

R

A

R

A

I

F

M

R

E

A

N

E

D

G

G

I

V

E

A

V

V

L

V

E

T

H

G

T

V

Q

N

A

V

S

K

Q

E

V

V

A

R

H

K

M

G

D

A

G

G

E

K

F

I

V

V

L

I

T

-

T

T

T

D

H

K

G

G

E

E

L

V

R

E

A

A

D

D

K

E

L

I

L

L

V

L

A

A

T

T

G

G

R
|
R

T

K

P

P

N

N

T

V

R

-

S

D

L
|
L

A

G

L

L

E

E

A

N

A

A

G

G

V

V

A

R

V

L

N

N

A

E

Q

R

G

G

A

G

I

I

V

K

I

V

D

D

K

D

G

E

M

L

R

R

T

T

S

D

S

N

P

P

N

H

I

I

Y

Y

A

A

A

A

G
|
G

D
|
D

C

V

T

L

D

G

Q

G

P

K

Q
x
M

F
x
L

V
x
E

Y

A

V

L

A
|
A

A
x
G

A

R

A

Q

G

G

T

S

R

I

A

A

A

T

I

E

N

N

-

A

M

L

T

T

G

G

G

S

D

H

A

K

A

R

L

V

D

D

L

E

T

N

A

A

M

V

P

P

A

Q

V

V

V

I

F
|
F

T

T

D

Q

P

P

Q

N

V

L

A

A

T

R

V

V

G

G

Y

L

S

T

E

E

A

A

E

E

A

A

H

R

H

A

D

K

G

E

I

G

E

E

T

V

D

E

S

A

R

R

L

V

L

L

T

P

L

M

D

S

N

S

V

V

P

A

R

K

A

A

L

E

A

I

N

I

F

N

D

S

T

R

R

L

G

G

F

F

I

V

K

K

L

M

V

V

I

T

E

M

E

-

G

-

S

N

G

G

R

R

L

I

I

V

G

G

V

V

Q

H

A

A

V

V

A

G

P

E

E

N

A

V

G

A

E

E

L

M

I

I

Q

G

T

E

A

A

V

A

L

L

A

A

I

I

R

R

N

F

R

G

M

A

T

T

V

V

Q

H

E

D

L

L

A

I

D

D

Q

T

L

V

F
x
H

P

M

Y
x
F

L

P

T

T

M

I

V

A

E
|
E

G

S

L

L

K

R

L

L

A

V

A

A

Q

L

T

A

F

F

S

R

K

S

D

D

active site: A15 (≠ G108), I39 (= I132), C43 (= C136), C48 (= C141), S51 (= S144), A174 (≠ V280), E178 (= E284), G308 (≠ A415), H425 (≠ F533), F427 (≠ Y535), E432 (= E540)
binding flavin-adenine dinucleotide: I11 (= I104), G12 (= G105), Y13 (≠ S106), G14 (= G107), A15 (≠ G108), A16 (= A109), I34 (= I127), G35 (≠ E128), K36 (≠ R129), G37 (= G130), G41 (= G134), T42 (= T135), C43 (= C136), V46 (= V139), G47 (= G140), C48 (= C141), S51 (= S144), K52 (= K145), G108 (= G209), E109 (= E210), A110 (= A211), A133 (= A239), T134 (= T240), G135 (= G241), N154 (≠ S260), L175 (≠ V281), F179 (≠ L285), R257 (= R363), L263 (= L370), G295 (= G402), D296 (= D403), M302 (≠ Q409), L303 (≠ F410), E304 (≠ V411), A307 (= A414), F336 (= F442)

1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
35% identity, 79% coverage: 100:540/561 of query aligns to 5:445/455 of 1ebdA

query
sites
1ebdA

Q

E

V

T

V

L

V

V

I
x
V

G
|
G

S

A

G
|
G

G
x
P

A
x
G

A

G

M

Y

A

V

A

A

A

A

L

I

K

R

A

A

V

A

E

Q

Q

L

G

G

A

Q

Q

K

V

V

T

T

L

I

I
x
V

E
|
E

R
x
K

G

G

T

N

I
x
L

G

G

G
|
G

T
x
V

C
|
C

V

L

N

N

V
|
V

G
|
G

C
|
C

V

I

P

P

S
|
S

K
|
K

I

A

M

L

I

I

R

S

A

A

A

S

H

H

I

R

A

Y

H

E

L

Q

R

A

R

K

E

H

S

S

P

E

F

-

D

E

G

M

G

G

M

I

P

K

P

A

T

E

P
x
N

P
x
V

T

T

I

I

L

D

R

F

E

A

R

K

L

V

L

Q

A

E

Q

W

Q

K

Q

A

A

S

R

V

V

V

E

K

E

K

L

L

R

T

H

G

A

G

K

-

Y

V

E

E

G

G

I

L

L

L

D

K

G

G

N

N

S

K

A

-

I

V

T

E

V

I

L

V

H

K

G
|
G

E
|
E

A
|
A

R

Y

F

F

K

V

D

D

D

A

Q

N

S

T

L

V

I

R

V

V

S

-

L

V

N

N

E

G

G

D

G

S

E

A

R

Q

V

T

V

Y

M

T

F

F

D

K

R

N

C

A

L

I

V

I

A
|
A

T
|
T

G
|
G

A

S

S

R

P

P

A

I

V

-

P

-

P

E

I

L

P

P

G

N

L

F

K

K

E

F

S

S

P

N

-

R

Y

I

W

L

T

D

S
|
S

T

T

E

G

A

A

L

L

A

N

S

L

D

G

T

E

I

V

P

P

E

K

R

S

L

L

A

V

V

V

I

I

G

G

S

G

S

G

V
x
Y

V
x
I

A

G

L

I

E
|
E

L

L

A

G

Q

T

A

A

F

Y

A

A

R

N

L

F

G

G

S

T

K

K

V

V

T

T

A

I

L

L

-

E

-

G

A

A

R

G

N

E

T

I

L

L

-

S

-

G

F

F

F

E

R

K

E

Q

D

M

P

A

A

A

I

I

G

-

E

-

A

-

V

I

T

K

A

K

A

R

F

L

R

K

A

K

E

K

G

G

I

V

E

E

V

V

L

V

E

T

H

N

T

A

Q

L

A

A

S

K

Q

G

V

A

A

E

H

E

M

R

-

E

D

D

G

G

E

V

F

T

V

V

L

T

T

Y

T

E

T

A

H

N

G

G

E

E

L

T

R

K

-

T

-

I

-

D

A

A

D

D

K

Y

L

V

L

L

V

V

A

T

T

V

G

G

R
|
R

T

R

P

P

N

N

T

T

R

D

S

E

L

L

A

G

L

L

E

E

A

Q

A

I

G

G

V

I

A

K

V

M

N

T

A

N

Q

R

G

G

A

L

I

I

V

E

I

V

D

D

K

Q

G

Q

M

C

R

R

T

T

S

S

S

V

P

P

N

N

I

I

Y

F

A

A

A

I

G
|
G

D
|
D

C

I

T

V

D

P

Q

G

P

P

Q
x
A

F
x
L

V
x
A

Y

H

V

K

A
|
A

A
x
S

A

Y

A

E

G

G

T

K

R

V

A

A

A

A

I

E

N

A

M

I

T

A

G

G

G

H

D

P

A

S

A

A

L

V

D

D

L

Y

T

V

A

A

M

I

P

P

A

A

V

V

V

V

F

F

T

S

D

D

P

P

Q

E

V

C

A

A

T

S

V

V

G

G

Y

Y

S

F

E

E

A

Q

E

Q

A

A

H

K

H

D

D

E

G

G

I

I

E

D

T

V

D

I

S

A

R

A

L

K

L

F

T

P

L

F

D

A

N

A

V

N

P

G

R

R

A

A

L

L

A

A

N

L

F

N

D

D

T

T

R

D

G

G

F

F

I

L

K

K

L

L

V

V

I

V

E

R

E

K

G

E

S

D

G

G

R

V

L

I

I

I

G

G

V

A

Q

Q

A

I

V

I

A

G

P

P

E

N

A

A

G

S

E

D

L

M

I

I

Q

A

T

E

A

L

V

G

L

L

A

A

I

I

R

E

N

A

R

G

M

M

T

T

V

A

Q

E

E

D

L

I

A

A

D

L

Q

T

L

I

F
x
H

P

A

Y
x
H

L
x
P

T

T

M

L

V

G

E
|
E

active site: P13 (≠ G108), L37 (≠ I132), C41 (= C136), C46 (= C141), S49 (= S144), N74 (≠ P170), V75 (≠ P171), Y180 (≠ V280), E184 (= E284), S320 (≠ A415), H438 (≠ F533), H440 (≠ Y535), E445 (= E540)
binding flavin-adenine dinucleotide: V9 (≠ I104), G10 (= G105), G12 (= G107), P13 (≠ G108), G14 (≠ A109), V32 (≠ I127), E33 (= E128), K34 (≠ R129), G39 (= G134), V40 (≠ T135), C41 (= C136), V44 (= V139), G45 (= G140), C46 (= C141), K50 (= K145), G111 (= G209), E112 (= E210), A113 (= A211), A140 (= A239), T141 (= T240), G142 (= G241), S160 (= S260), Y180 (≠ V280), I181 (≠ V281), R268 (= R363), G307 (= G402), D308 (= D403), A314 (≠ Q409), L315 (≠ F410), A316 (≠ V411), A319 (= A414), H440 (≠ Y535), P441 (≠ L536)

P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
35% identity, 79% coverage: 100:540/561 of query aligns to 11:451/470 of P11959

query
sites
P11959

Q

E

V

T

V

L

V

V

I

V

G

G

S

A

G

G

G

P

A

G

A

G

M

Y

A

V

A

A

A

A

L

I

K

R

A

A

V

A

E

Q

Q

L

G

G

A

Q

Q

K

V

V

T

T

L

I

I

V

E
|
E

R
x
K

G
|
G

T
x
N

I
x
L

G
|
G

G
|
G

T
x
V

C
|
C

V

L

N

N

V

V

G

G

C

C

V

I

P

P

S

S

K
|
K

I

A

M

L

I

I

R

S

A

A

A

S

H

H

I

R

A

Y

H

E

L

Q

R

A

R

K

E

H

S

S

P

E

F

-

D

E

G

M

G

G

M

I

P

K

P

A

T

E

P

N

P

V

T

T

I

I

L

D

R

F

E

A

R

K

L

V

L

Q

A

E

Q

W

Q

K

Q

A

A

S

R

V

V

V

E

K

E

K

L

L

R

T

H

-

A

G

K

G

Y

V

E

E

G

G

I

L

L

L

D

K

G

G

N

N

S

K

A

-

I

V

T

E

V

I

L

V

H

K

G

G

E

E

A

A

R

Y

F

F

K

V

D

D

D

A

Q

N

S

T

L

V

I

R

V

V

S

-

L

V

N

N

E

G

G

D

G

S

E

A

R

Q

V

T

V

Y

M

T

F

F

D

K

R

N

C

A

L

I

V

I

A

A

T

T

G

G

A

S

S

R

P

P

A

I

V

-

P

-

P

E

I

L

P

P

G

N

L

F

K

K

E

F

S

S

P

N

-

R

Y

I

W

L

T

D

S

S

T

T

E

G

A

A

L

L

A

N

S

L

D

G

T

E

I

V

P

P

E

K

R

S

L

L

A

V

V

V

I

I

G

G

S

G

S

G

V

Y

V

I

A

G

L

I

E

E

L

L

A

G

Q

T

A

A

F

Y

A

A

R

N

L

F

G

G

S

T

K

K

V

V

T

T

A

I

L

L

-

E

-

G

A

A

R

G

N

E

T

I

L

L

-

S

-

G

F

F

F

E

R

K

E

Q

D

M

P

A

A

A

I

I

G

-

E

-

A

-

V

I

T

K

A

K

A

R

F

L

R

K

A

K

E

K

G

G

I

V

E

E

V

V

L

V

E

T

H

N

T

A

Q

L

A

A

S

K

Q

G

V

A

A

E

H

E

M

R

-

E

D

D

G

G

E

V

F

T

V

V

L

T

T

Y

T

E

T

A

H

N

G

G

E

E

L

T

R

K

-

T

-

I

-

D

A

A

D

D

K

Y

L

V

L

L

V

V

A

T

T

V

G

G

R

R

T

R

P

P

N

N

T

T

R

D

S

E

L

L

A

G

L

L

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E

A

Q

A

I

G

G

V

I

A

K

V

M

N

T

A

N

Q

R

G

G

A

L

I

I

V

E

I

V

D

D

K

Q

G

Q

M

C

R

R

T

T

S

S

S

V

P

P

N

N

I

I

Y

F

A

A

A

I

G

G

D
|
D

C

I

T

V

D

P

Q

G

P

P

Q

A

F

L

V
x
A

Y

H

V

K

A

A

A

S

A

Y

A

E

G

G

T

K

R

V

A

A

A

A

I

E

N

A

M

I

T

A

G

G

G

H

D

P

A

S

A

A

L

V

D

D

L

Y

T

V

A

A

M

I

P

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A

A

V

V

V

V

F

F

T

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D

D

P

P

Q

E

V

C

A

A

T

S

V

V

G

G

Y

Y

S

F

E

E

A

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E

Q

A

A

H

K

H

D

D

E

G

G

I

I

E

D

T

V

D

I

S

A

R

A

L

K

L

F

T

P

L

F

D

A

N

A

V

N

P

G

R

R

A

A

L

L

A

A

N

L

F

N

D

D

T

T

R

D

G

G

F

F

I

L

K

K

L

L

V

V

I

V

E

R

E

K

G

E

S

D

G

G

R

V

L

I

I

I

G

G

V

A

Q

Q

A

I

V

I

A

G

P

P

E

N

A

A

G

S

E

D

L

M

I

I

Q

A

T

E

A

L

V

G

L

L

A

A

I

I

R

E

N

A

R

G

M

M

T

T

V

A

Q

E

E

D

L

I

A

A

D

L

Q

T

L

I

F

H

P

A

Y

H

L

P

T

T

M

L

V

G

E

E

39:47 (vs. 128:136, 56% identical) binding
K56 (= K145) binding
D314 (= D403) binding
A322 (≠ V411) binding

6kyyA Cu(ii) complex of hocl-induced flavoprotein disulfide reductase rcla from escherichia coli (see paper)
31% identity, 79% coverage: 100:543/561 of query aligns to 1:425/432 of 6kyyA

query
sites
6kyyA

Q

Q

V

A

V

V

V

I

I
|
I

G
|
G

S
x
F

G
|
G

G
x
K

A

A

A

G

M

K

A

T

A

L

A

A

L

V

K

T

A

L

V

A

E

K

Q

A

G

G

A

W

Q

R

V

V

T

A

L

L

I
|
I

E
|
E

R
x
Q

G

S

T

N

-

A

-
x
M

I

Y

G

G

G
|
G

T
|
T

C
|
C

V

I

N

N

V
x
I

G
|
G

C
|
C

V

I

P

P

S
x
T

K
|
K

I

T

M

L

I

V

R

H

A

D

A

A

H

-

I

-

A

-

H

-

L

-

R

Q

R

Q

E

H

S

T

P

D

F

F

D

-

G

-

G

-

M

-

P

-

P

-

T

-

P

-

P

-

T

-

I

-

L

-

R

-

E

V

R

R

L

A

L

I

A

Q

Q

R

Q

K

Q

N

A

E

R

V

V

V

E

N

E

F

L

L

R

R

H

N

A

K

K

N

Y

F

E

H

G

N

I

L

L

A

D

D

G

M

N

P

S

N

A

-

I

I

T

D

V

V

L

I

H

D

G
|
G

E
x
Q

A
|
A

R

E

F

F

K

I

D

N

D

N

Q

H

S

S

L

L

I

R

V

V

S

H

L

L

N

E

E

I

G

H

G

G

E

E

R

K

V

I

V

-

M

-

F

-

D

-

R

-

C

-

L

F

V

I

A
x
N

T
|
T

G
|
G

A

A

S

Q

P

T

A

V

V

V

P

P

P

P

I

I

P

P

G

G

L

I

K

T

E

T

S

T

P

P

-

G

Y

V

W

Y

T

D

S
|
S

T

T

E

G

A

L

L

L

A

N

S

L

D

K

T

E

I

L

P

P

E

G

R

H

L

L

A

G

V

I

I

L

G

G

S

G

S

G

V
x
Y

V
x
I

A

G

L

V

E
|
E

L

F

A

A

Q

S

A

M

F

F

A

A

R

N

L

F

G

G

S

S

K

K

V

V

T

T

A

I

L

L

A

E

R

A

N

A

T

S

L

L

F

F

F

L

-

P

R

R

E

E

D

D

P

R

A

D

I

I

G

A

E

D

A

N

V

I

T

A

A

T

A

I

F

L

R

R

A

D

E

Q

G

G

I

V

E

D

V

I

L

I

E

L

H

N

T

A

Q

H

A

V

S

E

Q

R

V

I

A

S

H

H

M

H

D

E

G

N

E

Q

F

V

V

Q

L

V

T
x
H

T

S

T

E

H
|
H

G

A

E

Q

L

L

R

A

A

V

D

D

K

A

L

L

L

L

V

I

A

A

T

S

G

G

R
|
R

T

Q

P

P

N

A

T

T

R