SitesBLAST

Q7ZVE3 Fructose-2,6-bisphosphatase TIGAR B; TP53-induced glycolysis and apoptosis regulator B; EC 3.1.3.46 from Danio rerio (Zebrafish) (Brachydanio rerio) (see paper)
35% identity, 60% coverage: 6:135/215 of query aligns to 8:138/257 of Q7ZVE3

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Q7ZVE3

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H11 (= H9) active site, Tele-phosphohistidine intermediate

4ij6A Crystal structure of a novel-type phosphoserine phosphatase mutant (h9a) from hydrogenobacter thermophilus tk-6 in complex with l-phosphoserine (see paper)
29% identity, 76% coverage: 1:164/215 of query aligns to 1:164/207 of 4ij6A

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active site: R8 (= R8), A9 (≠ H9), N15 (= N15), R58 (= R58), E82 (= E82), H150 (= H150)
binding phosphoserine: R8 (= R8), Q21 (= Q21), R58 (= R58), E82 (= E82), H85 (≠ M85), H150 (= H150), T151 (≠ G151)

Q9NQ88 Fructose-2,6-bisphosphatase TIGAR; TP53-induced glycolysis and apoptosis regulator; TP53-induced glycolysis regulatory phosphatase; EC 3.1.3.46 from Homo sapiens (Human) (see 4 papers)
41% identity, 42% coverage: 6:96/215 of query aligns to 8:103/270 of Q9NQ88

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Q9NQ88

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H11 (= H9) mutation to A: Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-102. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-102 and A-198. Loss of the ability to protect against cell death during hypoxia; when associated with A-102; A-198 and 258-N--D-261 Del.
E102 (≠ S95) mutation to A: Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-198. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-11 and A-198. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-198 and 258-N--D-261 Del.

Sites not aligning to the query:

198 H→A: Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-102. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-11 and A-102. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-102 and 258-N--D-261 Del.
258:261 mutation Missing: Inhibits the ability to interact and enhance HK2 activity, to localize to the mitochondria, to protect against the decrease of mitochondrial membrane potential and to limit mitochondrial ROS level increase during hypoxia. Does not abolish the ability to lower cellular fructose-2,6-bisphosphate levels during hypoxia. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-102 and A-198.

Q9HIJ2 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; BPG-dependent PGAM; PGAM; Phosphoglyceromutase; dPGM; EC 5.4.2.11 from Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) (see paper)
27% identity, 90% coverage: 6:198/215 of query aligns to 6:190/200 of Q9HIJ2

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Q9HIJ2

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H9 (= H9) mutation to A: Loss of activity.

1tipA The bisphosphatase domain of the bifunctional rat liver 6- phosphofructo-2-kinase/fructose-2,6-bisphosphatase (see paper)
31% identity, 75% coverage: 1:162/215 of query aligns to 1:155/191 of 1tipA

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active site: R8 (= R8), H9 (= H9), N15 (= N15), R58 (= R58), E78 (= E82), H143 (= H150)
binding 6-O-phosphono-beta-D-fructofuranose: I20 (= I20), Y89 (≠ I93), R103 (= R104), K107 (≠ T111), Y118 (≠ M122), R148 (≠ G155)

1c81A Michaelis complex of fructose-2,6-bisphosphatase
31% identity, 75% coverage: 1:162/215 of query aligns to 1:155/191 of 1c81A

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active site: R8 (= R8), H9 (= H9), N15 (= N15), R58 (= R58), E78 (= E82), H143 (= H150)
binding 2,5-anhydro-1-deoxy-1-phosphono-6-O-phosphono-D-glucitol: R8 (= R8), H9 (= H9), N15 (= N15), I20 (= I20), R58 (= R58), E78 (= E82), H143 (= H150), Q144 (≠ G151), R148 (≠ G155)

1c80A Regulatory complex of fructose-2,6-bisphosphatase
31% identity, 75% coverage: 1:162/215 of query aligns to 1:155/191 of 1c80A

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active site: R8 (= R8), H9 (= H9), N15 (= N15), R58 (= R58), E78 (= E82), H143 (= H150)
binding guanosine-5'-triphosphate: I20 (= I20), E78 (= E82), I79 (≠ L83), Y89 (≠ I93), F100 (≠ E101), R103 (= R104), Y112 (≠ I116), Y118 (≠ M122), Q144 (≠ G151), A145 (≠ I152), R148 (≠ G155)

1c7zA Regulatory complex of fructose-2,6-bisphosphatase
31% identity, 75% coverage: 1:162/215 of query aligns to 1:155/191 of 1c7zA

query
sites
1c7zA

M

M

L

R

Q

S

V

I

Y

Y

L

L

V

C

R
|
R

H
|
H

G

G

E

E

T

S

Q

E

W

L

N
|
N

A

L

E

R

R

G

R

R

I

I

Q

G

G

G

Q

-

S

-

D

D

S

S

P

G

L

L

T

S

A

A

K

R

G

G

E

K

Q

Q

Q

Y

A

A

M

Y

Q

A

V

L

A

A

T

N

R

F

A

I

K

R

E

S

L

Q

G

G

I

I

T

S

-

S

-

L

H

K

I

V

I

W

S

T

S

S

D

H

L

M

G

K

R
|
R

T

T

R

I

R

Q

T

T

A

A

E

E

I

-

A

-

Q

-

A

A

C

L

G

G

C

V

D

P

I

Y

I

E

F

Q

D

W

S

K

R

A

L

L

R

N

E
|
E

L

I

N

D

M

A

G

G

V

V

L

C

E

E

K

E

R

M

H

T

I
x
Y

D

E

S

E

L

I

T

Q

E

E

-

H

-

Y

-

P

E

E

E

F

N

A

W

L

R
|
R

R

D

Q

Q

L

-

V

-

N

-

G

D

T
x
K

V

Y

D

R

G

Y

R

R

I

Y

P

P

E

K

G

G

E

E

S

S

M
x
Y

Q

E

E

D

L

L

S

V

D

Q

R

R

V

L

N

E

A

P

A

V

L

I

E

-

S

-

C

-

R

M

D

E

L

L

P

E

Q

R

G

Q

S

E

R

N

P

V

L

L

L

V

V

I

S

C

H
|
H

G
x
Q

I
x
A

A

V

L

M

G
x
R

C

C

L

L

V

L

S

A

T

Y

I

F

L

L

active site: R8 (= R8), H9 (= H9), N15 (= N15), R58 (= R58), E78 (= E82), H143 (= H150)
binding glyceraldehyde-3-phosphate: Y89 (≠ I93), R103 (= R104), K107 (≠ T111), Y118 (≠ M122), Q144 (≠ G151), A145 (≠ I152), R148 (≠ G155)

1k6mA Crystal structure of human liver 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase (see paper)
30% identity, 74% coverage: 4:162/215 of query aligns to 215:366/432 of 1k6mA

query
sites
1k6mA

V

I

Y

Y

L

L

V

C

R
|
R

H
|
H

G

G

E

E

T

S

Q

E

W

L

N
|
N

A

I

E

R

R

G

R

R

I

I

Q

G

G

G

Q

-

S

-

D

D

S

S

P

G

L

L

T

S

A

V

K

R

G

G

E

K

Q

Q

Q

Y

A

A

M

Y

Q

A

V

L

A

A

T

N

R

F

A

I

K

Q

E

S

L

Q

G

G

I

I

T

S

-

S

-

L

H

K

I

V

I

F

S

T

S

S

D

R

L

M

G

K

R
|
R

T

T

R

I

R

Q

T

T

A

A

E

E

I

-

A

-

Q

-

A

A

C

L

G

G

C

V

D

P

I

Y

I

E

F

Q

D

F

S

K

R

A

L

L

R

N

E
|
E

L

I

N

D

M

A

G

G

V

V

L

C

E

E

K

E

R

M

H

T

I

Y

D

E

S

E

L

I

T

Q

E

E

-

H

-

Y

-

P

E

E

E

F

N

A

W

L

R

R

R

D

Q

Q

L

-

V

-

N

-

G

D

T

K

V

Y

D

R

G

Y

R

R

I

Y

P

P

E

K

G

G

E

E

S

S

M

Y

Q

E

E

D

L

L

S

V

D

Q

R

R

V

L

N

E

A

P

A

V

L

I

E

-

S

-

C

-

R

M

D

E

L

L

P

E

Q

R

G

Q

S

E

R

N

P

V

L

L

L

V

V

I

S

C

H
|
H

G

Q

I

A

A

V

L

M

G

R

C

C

L

L

V

L

S

A

T

Y

I

F

L

L

active site: R219 (= R8), H220 (= H9), N226 (= N15), R269 (= R58), E289 (= E82), H354 (= H150)

Sites not aligning to the query:

binding phosphothiophosphoric acid-adenylate ester: 13, 14, 15, 16, 17, 18, 92, 120, 131, 134, 135, 136, 184, 210

1fbtA The bisphosphatase domain of the bifunctional rat liver 6- phosphofructo-2-kinase/fructose-2,6-bisphosphatase (see paper)
31% identity, 74% coverage: 4:162/215 of query aligns to 3:154/190 of 1fbtA

query
sites
1fbtA

V

I

Y

Y

L

L

V

C

R
|
R

H
|
H

G

G

E

E

T

S

Q

E

W

L

N
|
N

A

L

E

R

R

G

R

R

I

I

Q

G

G

G

Q

-

S

-

D

D

S

S

P

G

L

L

T

S

A

A

K

R

G

G

E

K

Q

Q

Q

Y

A

A

M

Y

Q

A

V

L

A

A

T

N

R

F

A

I

K

R

E

S

L

Q

G

G

I

I

T

S

-

S

-

L

H

K

I

V

I

W

S

T

S

S

D

H

L

M

G

K

R
|
R

T

T

R

I

R

Q

T

T

A

A

E

E

I

-

A

-

Q

-

A

A

C

L

G

G

C

V

D

P

I

Y

I

E

F

Q

D

W

S

K

R

A

L

L

R

N

E
|
E

L

I

N

D

M

A

G

G

V

V

L

C

E

E

K

E

R

M

H

T

I

Y

D

E

S

E

L

I

T

Q

E

E

-

H

-

Y

-

P

E

E

E

F

N

A

W

L

R

R

R

D

Q

Q

L

-

V

-

N

-

G

D

T

K

V

Y

D

R

G

Y

R

R

I

Y

P

P

E

K

G

G

E

E

S

S

M

Y

Q

E

E

D

L

L

S

V

D

Q

R

R

V

L

N

E

A

P

A

V

L

I

E

-

S

-

C

-

R

M

D

E

L

L

P

E

Q

R

G

Q

S

E

R

N

P

V

L

L

L

V

V

I

S

C

H
|
H

G
x
Q

I

A

A

V

L

M

G

R

C

C

L

L

V

L

S

A

T

Y

I

F

L

L

active site: R7 (= R8), H8 (= H9), N14 (= N15), R57 (= R58), E77 (= E82), H142 (= H150)
binding phosphate ion: R7 (= R8), H8 (= H9), R57 (= R58), E77 (= E82), H142 (= H150), Q143 (≠ G151)

P07953 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1; 6PF-2-K/Fru-2,6-P2ase 1; PFK/FBPase 1; 6PF-2-K/Fru-2,6-P2ase liver isozyme; EC 2.7.1.105; EC 3.1.3.46 from Rattus norvegicus (Rat) (see 3 papers)
31% identity, 74% coverage: 4:162/215 of query aligns to 254:405/471 of P07953

query
sites
P07953

V

I

Y

Y

L

L

V

C

R

R

H
|
H

G

G

E

E

T

S

Q

E

W

L

N

N

A

L

E

R

R

G

R

R

I

I

Q
x
G

G

G

Q

-

S

-

D

D

S

S

P

G

L

L

T

S

A

A

K

R

G

G

E

K

Q

Q

Q

Y

A

A

M

Y

Q

A

V

L

A

A

T

N

R

F

A

I

K

R

E

S

L

Q

G

G

I

I

T

S

-

S

-

L

H

K

I

V

I

W

S

T

S

S

D

H

L

M

G

K

R

R

T

T

R

I

R

Q

T

T

A

A

E

E

I

-

A

-

Q

-

A

A

C

L

G

G

C

V

D

P

I

Y

I

E

F

Q

D

W

S

K

R

A

L

L

R

N

E
|
E

L

I

N

D

M

A

G

G

V

V

L

C

E

E

K

E

R

M

H

T

I
x
Y

D

E

S

E

L

I

T

Q

E

E

-

H

-

Y

-

P

E

E

E
x
F

N
x
A

W
x
L

R
|
R

R

D

Q

Q

L

-

V

-

N

-

G

D

T
x
K

V

Y

D

R

G

Y

R

R

I

Y

P

P

E

K

G

G

E

E

S

S

M
x
Y

Q

E

E

D

L

L

S

V

D

Q

R

R

V

L

N

E

A

P

A

V

L

I

E

-

S

-

C

-

R

M

D

E

L

L

P

E

Q

R

G

Q

S

E

R

N

P

V

L

L

L

V

V

I

S

C

H

H

G
x
Q

I
x
A

A
x
V

L
x
M

G
x
R

C

C

L

L

V

L

S

A

T

Y

I

F

L

L

H259 (= H9) active site, Tele-phosphohistidine intermediate
G271 (≠ Q21) binding
E328 (= E82) active site, Proton donor/acceptor
Y339 (≠ I93) binding
FALR 350:353 (≠ ENWR 101:104) binding
R353 (= R104) binding
K357 (≠ T111) binding
Y368 (≠ M122) binding
Q394 (≠ G151) binding
QAVMR 394:398 (≠ GIALG 151:155) binding
R398 (≠ G155) binding

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 modified: N-acetylserine
33 modified: Phosphoserine; by PKA

P36623 Phosphoglycerate mutase; PGAM; BPG-dependent PGAM; MPGM; Phosphoglyceromutase; EC 5.4.2.11 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
29% identity, 74% coverage: 6:164/215 of query aligns to 12:177/211 of P36623

query
sites
P36623

L

L

V

T

R

R

H

H

G

G

E

E

T

S

Q

E

W

W

N

N

A

K

E

L

R

N

R

L

I

F

Q

T

G

G

Q

W

S

K

D

D

S

P

P

A

L

L

T

S

A

E

K
x
T

G

G

E

I

Q

K

Q

E

A

A

M

K

Q

L

V

G

A

G

T

E

R

R

A

L

K

K

E

S

L

R

G

G

I

Y

T

K

H

F

I

D

I

I

-

A

-

F

S

T

S
|
S

D

A

L

L

G

Q

R

R

T

A

R

Q

R

K

T

T

A

C

E

Q

I

I

A

L

Q

E

A

E

C

V

G

G

-

E

-

P

-

N

C

L

D

E

I

T

I

I

F

K

D

S

S

E

R

K

L

L

R

N

E

E

L

R

N

Y

M
x
Y

G

G

V

D

L

L

E

Q

K

G

R

L

H

N

I

K

D

D

S

D

L

A

-

R

-

K

-

W

-

G

T

A

E

E

E

Q

E

V

E

Q

N

I

W

W

R

R

Q

-

L

-

V

-

N

-

G

-

T

S

V

Y

D

D

G

I

R

A

I

P

P

P

E

N

G

G

E

E

S

S

M

L

Q

K

E

D

L

T

S

A

D

E

R

R

V

V

N

L

A

P

A

Y

L

Y

E

K

S

S

-

T

-

I

C

V

R

P

D

H

L

I

P

L

Q

K

G

G

S

E

R

K

P

V

L

L

L

I

V

A

S

A

H

H

G

G

I

N

A
x
S

L

L

G

R

C

A

L

L

V

I

S

M

T

D

I

L

L

E

G

G

L

L

T37 (≠ K31) modified: Phosphothreonine
S62 (= S54) modified: Phosphoserine
Y96 (≠ M85) modified: Phosphotyrosine
S166 (≠ A153) modified: Phosphoserine

P16118 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1; 6PF-2-K/Fru-2,6-P2ase 1; PFK/FBPase 1; 6PF-2-K/Fru-2,6-P2ase liver isozyme; EC 2.7.1.105; EC 3.1.3.46 from Homo sapiens (Human) (see paper)
30% identity, 74% coverage: 4:162/215 of query aligns to 254:405/471 of P16118

query
sites
P16118

V

I

Y

Y

L

L

V

C

R

R

H

H

G

G

E

E

T

S

Q

E

W

L

N

N

A

I

E

R

R

G

R

R

I

I

Q

G

G

G

Q

-

S

-

D

D

S

S

P

G

L

L

T

S

A

V

K

R

G

G

E

K

Q

Q

Q

Y

A

A

M

Y

Q

A

V

L

A

A

T

N

R

F

A

I

K

Q

E

S

L

Q

G

G

I

I

T

S

-

S

-

L

H

K

I

V

I

W

S

T

S

S

D

H

L

M

G

K

R

R

T

T

R

I

R

Q

T

T

A

A

E

E

I

-

A

-

Q

-

A

A

C

L

G

G

C

V

D

P

I

Y

I

E

F

Q

D

W

S

K

R

A

L

L

R

N

E

E

L

I

N

D

M

A

G

G

V

V

L

C

E

E

K

E

R

M

H

T

I

Y

D

E

S

E

L

I

T

Q

E

E

-

H

-

Y

-

P

E

E

E

F

N

A

W

L

R

R

R

D

Q

Q

L

-

V

-

N

-

G

D

T

K

V

Y

D

R

G

Y

R

R

I

Y

P

P

E

K

G

G

E

E

S

S

M

Y

Q

E

E

D

L

L

S

V

D

Q

R

R

V

L

N

E

A

P

A

V

L

I

E

-

S

-

C

-

R

M

D

E

L

L

P

E

Q

R

G

Q

S

E

R

N

P

V

L

L

L

V

V

I

S

C

H

H

G

Q

I

A

A

V

L

M

G

R

C

C

L

L

V

L

S

A

T

Y

I

F

L

L

Sites not aligning to the query:

49:57 binding
170:175 binding
430 binding

P9WIC7 Glucosyl-3-phosphoglycerate phosphatase; Mannosyl-3-phosphoglycerate phosphatase; EC 3.1.3.85; EC 3.1.3.70 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
36% identity, 39% coverage: 3:86/215 of query aligns to 5:88/223 of P9WIC7

query
sites
P9WIC7

Q

R

V

L

Y

V

L

M

V

L

R
|
R

H
|
H

G

G

E

Q

T

T

Q

D

W

Y

N
|
N

A

V

E

G

R

S

R

R

I

M

Q

Q

G

G

Q

Q

S

L

D

D

S

T

P

E

L

L

T

S

A

E

K

L

G

G

E

R

Q

T

Q

Q

A

A

M

V

Q

A

V

A

A

A

T

E

R

V

A

L

K

G

E
x
K

L

R

G

Q

I

P

T

L

H

L

I

I

I

V

S

S

D

D

L

L

G

R

R
|
R

T

A

R

Y

R

D

T

T

A

A

E

V

I

K

I

L

A

G

Q

E

A

R

C

T

G

G

C

L

D

V

I

V

I

R

F

V

D

D

S

T

R

R

L

L

R

R

E

E

L

T

N

H

M

L

G

G

R10 (= R8) mutation to A: Loss of phosphatase activity.
H11 (= H9) active site, Tele-phosphohistidine intermediate; mutation to A: Almost completely abolished phosphatase activity.
N17 (= N15) mutation to A: About 5% of wild-type phosphatase activity.
K47 (≠ E45) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
R60 (= R58) mutation to A: Loss of phosphatase activity.

Sites not aligning to the query:

159 H→A: About 5% of wild-type phosphatase activity.
209 L→E: Disrupts dimerization of the enzyme, which exists as a monomer and has lost its ability to perform dephosphorylation.

4qihA The structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c complexes with vo3 (see paper)
36% identity, 39% coverage: 3:86/215 of query aligns to 3:86/209 of 4qihA

query
sites
4qihA

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active site: H9 (= H9), R58 (= R58), E82 (= E82)
binding vanadate ion: R8 (= R8), H9 (= H9), Q21 (= Q21), R58 (= R58)

Sites not aligning to the query:

binding vanadate ion: 157

4pzaB The complex structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c with inorganic phosphate (see paper)
36% identity, 39% coverage: 3:86/215 of query aligns to 4:87/217 of 4pzaB

query
sites
4pzaB

Q

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active site: H10 (= H9), R59 (= R58), E83 (= E82)
binding phosphate ion: R9 (= R8), H10 (= H9), R59 (= R58), E83 (= E82)

Sites not aligning to the query:

binding phosphate ion: 158, 159

6m1xC Crystal structure of phosphoserine phosphatase in complex with 3- phosphoglyceric acid from entamoeba histolytica (see paper)
29% identity, 87% coverage: 1:186/215 of query aligns to 1:182/196 of 6m1xC

query
sites
6m1xC

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binding 3-phosphoglyceric acid: R8 (= R8), H9 (= H9), Q21 (= Q21), R57 (= R58), E79 (= E82), H146 (= H150), G147 (= G151)

5hr5A Bovine heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (pfkfb2) (see paper)
28% identity, 74% coverage: 4:162/215 of query aligns to 226:377/424 of 5hr5A

query
sites
5hr5A

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active site: R230 (= R8), H231 (= H9), N237 (= N15), R280 (= R58), E300 (= E82), H365 (= H150)
binding 6-O-phosphono-beta-D-fructofuranose: H231 (= H9), I242 (= I20), G243 (≠ Q21), E300 (= E82), Y311 (≠ I93), R325 (≠ L107), K329 (≠ T111), Y340 (≠ M122), Q366 (≠ G151), R370 (≠ G155)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 22, 23, 24, 25, 26, 27, 130, 141, 144, 145, 146, 402
binding citrate anion: 49, 52, 76, 103, 104, 171

Query Sequence

>18416 FitnessBrowser__Keio:18416
MLQVYLVRHGETQWNAERRIQGQSDSPLTAKGEQQAMQVATRAKELGITHIISSDLGRTR
RTAEIIAQACGCDIIFDSRLRELNMGVLEKRHIDSLTEEEENWRRQLVNGTVDGRIPEGE
SMQELSDRVNAALESCRDLPQGSRPLLVSHGIALGCLVSTILGLPAWAERRLRLRNCSIS
RVDYQESLWLASGWVVETAGDISHLDAPALDELQR

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory