SitesBLAST
Comparing GFF3862 FitnessBrowser__Phaeo:GFF3862 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)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
54% identity, 99% coverage: 4:459/460 of query aligns to 1:465/465 of 3urhB
- active site: Y35 (≠ L38), C39 (= C42), C44 (= C47), S47 (= S50), V183 (= V178), E187 (= E182), H443 (= H437), H445 (= H439), E450 (= E444)
- binding flavin-adenine dinucleotide: I6 (= I9), G7 (= G10), G9 (= G12), P10 (= P13), G11 (= G14), E30 (= E33), K31 (≠ G34), G37 (= G40), T38 (= T41), C39 (= C42), G43 (= G46), C44 (= C47), K48 (= K51), T111 (≠ W113), G112 (≠ A114), A140 (= A137), T141 (= T138), G142 (= G139), I184 (= I179), R273 (= R268), G312 (= G307), D313 (= D308), M319 (= M314), L320 (= L315), A321 (= A316), H322 (= H317)
P31023 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; Pyruvate dehydrogenase complex E3 subunit; E3; PDC-E3; EC 1.8.1.4 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see 2 papers)
53% identity, 99% coverage: 5:459/460 of query aligns to 39:500/501 of P31023
- 67:76 (vs. 33:42, 80% identical) binding
- C76 (= C42) modified: Disulfide link with 81, Redox-active
- C81 (= C47) modified: Disulfide link with 76, Redox-active
- G149 (≠ A114) binding
- D348 (= D308) binding
- MLAH 354:357 (= MLAH 314:317) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
53% identity, 99% coverage: 5:459/460 of query aligns to 5:466/467 of 1dxlA
- active site: L38 (= L38), C42 (= C42), C47 (= C47), S50 (= S50), Y184 (≠ V178), E188 (= E182), H444 (= H437), H446 (= H439), E451 (= E444)
- binding flavin-adenine dinucleotide: I9 (= I9), P13 (= P13), G14 (= G14), E33 (= E33), K34 (≠ G34), R35 (= R35), G40 (= G40), T41 (= T41), C42 (= C42), G46 (= G46), C47 (= C47), K51 (= K51), Y114 (≠ W113), G115 (≠ A114), T144 (= T138), G145 (= G139), Y184 (≠ V178), I185 (= I179), R274 (= R268), D314 (= D308), M320 (= M314), L321 (= L315), A322 (= A316), H323 (= H317)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
51% identity, 100% coverage: 1:459/460 of query aligns to 4:469/470 of 6uziC
- active site: C45 (= C42), C50 (= C47), S53 (= S50), V187 (= V178), E191 (= E182), H448 (= H439), E453 (= E444)
- binding flavin-adenine dinucleotide: I12 (= I9), G13 (= G10), G15 (= G12), P16 (= P13), G17 (= G14), E36 (= E33), K37 (≠ G34), G43 (= G40), T44 (= T41), C45 (= C42), G49 (= G46), C50 (= C47), S53 (= S50), K54 (= K51), V117 (≠ W113), G118 (≠ A114), T147 (= T138), G148 (= G139), I188 (= I179), R276 (= R268), D316 (= D308), M322 (= M314), L323 (= L315), A324 (= A316)
- binding zinc ion: H448 (= H439), E453 (= E444)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
51% identity, 99% coverage: 5:459/460 of query aligns to 6:471/472 of 1zmdA
- active site: L39 (= L38), C43 (= C42), C48 (= C47), S51 (= S50), V186 (= V178), E190 (= E182), H448 (= H437), H450 (= H439), E455 (= E444)
- binding flavin-adenine dinucleotide: I10 (= I9), G11 (= G10), G13 (= G12), P14 (= P13), G15 (= G14), E34 (= E33), K35 (≠ G34), N36 (≠ R35), G41 (= G40), T42 (= T41), C43 (= C42), G47 (= G46), C48 (= C47), K52 (= K51), Y116 (≠ W113), G117 (≠ A114), T146 (= T138), G147 (= G139), S166 (= S158), R278 (= R268), F281 (≠ V271), G317 (= G307), D318 (= D308), M324 (= M314), L325 (= L315), A326 (= A316), H327 (= H317)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (≠ V174), G183 (= G175), G185 (= G177), V186 (= V178), I187 (= I179), E190 (= E182), E206 (= E198), F207 (≠ Y199), L208 (= L200), I276 (= I266), G277 (= G267), R278 (= R268), M324 (= M314), L325 (= L315), V355 (≠ I345), Y357 (= Y347)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
51% identity, 99% coverage: 5:459/460 of query aligns to 6:471/472 of 1zmcA
- active site: L39 (= L38), C43 (= C42), C48 (= C47), S51 (= S50), V186 (= V178), E190 (= E182), H448 (= H437), H450 (= H439), E455 (= E444)
- binding flavin-adenine dinucleotide: I10 (= I9), G11 (= G10), G13 (= G12), P14 (= P13), G15 (= G14), E34 (= E33), K35 (≠ G34), N36 (≠ R35), G41 (= G40), T42 (= T41), C43 (= C42), G47 (= G46), C48 (= C47), K52 (= K51), Y116 (≠ W113), G117 (≠ A114), T146 (= T138), G147 (= G139), S166 (= S158), I187 (= I179), F281 (≠ V271), G317 (= G307), D318 (= D308), M324 (= M314), L325 (= L315), A326 (= A316), H327 (= H317)
- binding nicotinamide-adenine-dinucleotide: G183 (= G175), G185 (= G177), V205 (= V197), E206 (= E198), F207 (≠ Y199), L208 (= L200), K240 (≠ R230), V241 (≠ A231), I276 (= I266), G277 (= G267), R278 (= R268), R297 (= R287), M324 (= M314)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
51% identity, 99% coverage: 5:459/460 of query aligns to 43:508/509 of P09622
- 71:80 (vs. 33:42, 70% identical) binding
- K72 (≠ G34) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K51) binding ; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (vs. gap) to T: in dbSNP:rs1130477
- G154 (≠ A114) binding
- TGS 183:185 (= TGS 138:140) binding
- 220:227 (vs. 175:182, 88% identical) binding
- E243 (= E198) binding
- V278 (≠ A231) binding
- G314 (= G267) binding
- D355 (= D308) binding
- MLAH 361:364 (= MLAH 314:317) binding
- E375 (= E328) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (= H336) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ G400) Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex; mutation to A: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.; mutation to N: Does not affect dihydrolipoyl dehydrogenase activity.
- E466 (= E418) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ K425) Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex; mutation to A: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.; mutation to F: Does not affect dihydrolipoyl dehydrogenase activity.; mutation to H: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.
- D479 (≠ E431) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ A434) to G: in DLDD; reduced enzyme activity; dbSNP:rs397514650; mutation to A: Does not affect dihydrolipoyl dehydrogenase activity.; mutation to M: Does not affect interaction with PDHX.
- H485 (= H437) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P440) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (≠ A443) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E444) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ K447) to G: in DLDD; loss of enzyme activity; reduced interaction with PDHX; dbSNP:rs121964989
- K505 (≠ R456) mutation to M: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
51% identity, 99% coverage: 5:459/460 of query aligns to 16:481/482 of 6hg8B
- active site: C53 (= C42), C58 (= C47), S61 (= S50), V196 (= V178), E200 (= E182), H460 (= H439), E465 (= E444)
- binding flavin-adenine dinucleotide: I20 (= I9), G23 (= G12), P24 (= P13), G25 (= G14), E44 (= E33), K45 (≠ G34), N46 (≠ R35), G51 (= G40), T52 (= T41), C53 (= C42), G57 (= G46), C58 (= C47), K62 (= K51), Y126 (≠ W113), G127 (≠ A114), T156 (= T138), G157 (= G139), I197 (= I179), R288 (= R268), F291 (≠ V271), G327 (= G307), D328 (= D308), M334 (= M314), L335 (= L315), A336 (= A316), H337 (= H317)
P09624 Dihydrolipoyl dehydrogenase, mitochondrial; DLD; 2-oxoglutarate dehydrogenase complex component E3; OGDC-E3; OGDHC subunit E3; Alpha-ketoglutarate dehydrogenase complex subunit E3; alpha-KGDHC subunit E3; Dihydrolipoamide dehydrogenase; Dihydrolipoamide:NAD(+) oxidoreductase; Glycine decarboxylase complex subunit L; GDC subunit L; Lipoamide dehydrogenase component of pyruvate dehydrogenase complex; Pyruvate dehydrogenase complex E3 component; PDC subunit E3; PDH complex subunit E3; EC 1.8.1.4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
49% identity, 99% coverage: 4:459/460 of query aligns to 27:498/499 of P09624
- 56:65 (vs. 33:42, 80% identical) binding
- C65 (= C42) modified: Disulfide link with 70, Redox-active
- C70 (= C47) modified: Disulfide link with 65, Redox-active
- K74 (= K51) binding
- G139 (≠ A114) binding
- D346 (= D308) binding
- MLAH 352:355 (= MLAH 314:317) binding
- H478 (= H439) active site, Proton acceptor
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
1v59A Crystal structure of yeast lipoamide dehydrogenase complexed with NAD+
49% identity, 99% coverage: 4:459/460 of query aligns to 6:477/478 of 1v59A
- active site: L40 (= L38), C44 (= C42), C49 (= C47), S52 (= S50), I193 (≠ V178), E197 (= E182), T349 (≠ G332), H455 (= H437), H457 (= H439), E462 (= E444)
- binding flavin-adenine dinucleotide: G14 (= G12), P15 (= P13), A16 (≠ G14), E35 (= E33), K36 (≠ G34), R37 (= R35), G42 (= G40), T43 (= T41), C44 (= C42), G48 (= G46), C49 (= C47), K53 (= K51), N117 (≠ W113), G118 (≠ A114), T153 (= T138), G154 (= G139), R285 (= R268), Y288 (≠ V271), G324 (= G307), D325 (= D308), M331 (= M314), L332 (= L315), A333 (= A316), H334 (= H317), Y364 (= Y347)
- binding nicotinamide-adenine-dinucleotide: I189 (≠ V174), G190 (= G175), E213 (= E198), F214 (≠ Y199), K246 (≠ A231), V283 (≠ I266)
1jehA Crystal structure of yeast e3, lipoamide dehydrogenase (see paper)
49% identity, 99% coverage: 4:459/460 of query aligns to 6:477/478 of 1jehA
- active site: L40 (= L38), C44 (= C42), C49 (= C47), S52 (= S50), I193 (≠ V178), E197 (= E182), T349 (≠ G332), H455 (= H437), H457 (= H439), E462 (= E444)
- binding flavin-adenine dinucleotide: I11 (= I9), G14 (= G12), P15 (= P13), A16 (≠ G14), V34 (= V32), E35 (= E33), K36 (≠ G34), R37 (= R35), G42 (= G40), T43 (= T41), C44 (= C42), G48 (= G46), C49 (= C47), K53 (= K51), G118 (≠ A114), T153 (= T138), G154 (= G139), I194 (= I179), R285 (= R268), Y288 (≠ V271), L292 (= L275), G324 (= G307), D325 (= D308), M331 (= M314), L332 (= L315), A333 (= A316), H334 (= H317)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
52% identity, 99% coverage: 3:459/460 of query aligns to 1:454/455 of 2yquB
- active site: P11 (= P13), L36 (= L38), C40 (= C42), C45 (= C47), S48 (= S50), G72 (= G75), V73 (≠ A76), V177 (= V178), E181 (= E182), S314 (≠ E320), H432 (= H437), H434 (= H439), E439 (= E444)
- binding carbonate ion: A310 (= A316), S314 (≠ E320), S423 (≠ T428), D426 (≠ E431)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), P11 (= P13), G12 (= G14), E31 (= E33), K32 (≠ G34), G38 (= G40), T39 (= T41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (≠ W113), A111 (= A114), T137 (= T138), G138 (= G139), I178 (= I179), Y265 (≠ V271), G301 (= G307), D302 (= D308), M308 (= M314), L309 (= L315), A310 (= A316), H311 (= H317)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
52% identity, 99% coverage: 3:459/460 of query aligns to 1:454/455 of 2yquA
- active site: P11 (= P13), L36 (= L38), C40 (= C42), C45 (= C47), S48 (= S50), G72 (= G75), V73 (≠ A76), V177 (= V178), E181 (= E182), S314 (≠ E320), H432 (= H437), H434 (= H439), E439 (= E444)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), P11 (= P13), G12 (= G14), E31 (= E33), K32 (≠ G34), G38 (= G40), T39 (= T41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (≠ W113), A111 (= A114), T137 (= T138), G138 (= G139), S157 (= S158), I178 (= I179), Y265 (≠ V271), G301 (= G307), D302 (= D308), M308 (= M314), L309 (= L315), A310 (= A316)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
51% identity, 99% coverage: 3:456/460 of query aligns to 1:451/452 of 2eq7A
- active site: P11 (= P13), L36 (= L38), C40 (= C42), C45 (= C47), S48 (= S50), G72 (= G75), V73 (≠ A76), V177 (= V178), E181 (= E182), S314 (≠ E320), H432 (= H437), H434 (= H439), E439 (= E444)
- binding flavin-adenine dinucleotide: G10 (= G12), P11 (= P13), G12 (= G14), E31 (= E33), K32 (≠ G34), G38 (= G40), T39 (= T41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (≠ W113), A111 (= A114), T137 (= T138), G138 (= G139), S157 (= S158), I178 (= I179), R262 (= R268), Y265 (≠ V271), D302 (= D308), M308 (= M314), L309 (= L315), A310 (= A316), H311 (= H317), Y341 (= Y347)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ G147), G174 (= G175), G176 (= G177), V177 (= V178), I178 (= I179), E197 (= E198), Y198 (= Y199), V231 (≠ L232), V260 (≠ I266), G261 (= G267), R262 (= R268), M308 (= M314), L309 (= L315), V339 (≠ I345)
2qaeA Crystal structure analysis of trypanosoma cruzi lipoamide dehydrogenase
49% identity, 96% coverage: 18:459/460 of query aligns to 17:464/465 of 2qaeA
- active site: L37 (= L38), C41 (= C42), C46 (= C47), S49 (= S50), V184 (= V178), E188 (= E182), H442 (= H437), H444 (= H439), E449 (= E444)
- binding flavin-adenine dinucleotide: E32 (= E33), K33 (≠ G34), R34 (= R35), G39 (= G40), T40 (= T41), C41 (= C42), G45 (= G46), C46 (= C47), K50 (= K51), E114 (≠ W113), G115 (≠ A114), T144 (= T138), G145 (= G139), S164 (= S158), I185 (= I179), F274 (≠ V271), G310 (= G307), D311 (= D308), M318 (= M314), L319 (= L315), A320 (= A316), H321 (= H317)
Sites not aligning to the query:
6aonA 1.72 angstrom resolution crystal structure of 2-oxoglutarate dehydrogenase complex subunit dihydrolipoamide dehydrogenase from bordetella pertussis in complex with fad
46% identity, 99% coverage: 4:459/460 of query aligns to 3:472/473 of 6aonA
- active site: P43 (≠ L38), C47 (= C42), C52 (= C47), S55 (= S50), V191 (= V178), E195 (= E182), H450 (= H437), H452 (= H439), E457 (= E444)
- binding calcium ion: A218 (≠ P205), A220 (≠ I207), Q222 (≠ G209)
- binding flavin-adenine dinucleotide: I8 (= I9), G11 (= G12), P12 (= P13), G13 (= G14), D32 (≠ E33), A33 (vs. gap), W34 (vs. gap), G45 (= G40), T46 (= T41), C47 (= C42), G51 (= G46), C52 (= C47), K56 (= K51), K119 (≠ W113), G120 (≠ A114), T151 (= T138), G152 (= G139), N171 (≠ S158), I192 (= I179), R280 (= R268), Y283 (≠ V271), G319 (= G307), D320 (= D308), M326 (= M314), L327 (= L315), A328 (= A316), H329 (= H317)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
46% identity, 99% coverage: 4:459/460 of query aligns to 5:471/477 of P18925
- 34:49 (vs. 33:42, 44% identical) binding
- C49 (= C42) modified: Disulfide link with 54, Redox-active
- C54 (= C47) modified: Disulfide link with 49, Redox-active
- K58 (= K51) binding
- D319 (= D308) binding
- A327 (= A316) binding
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
46% identity, 99% coverage: 4:459/460 of query aligns to 5:471/478 of P14218
- 34:49 (vs. 33:42, 44% identical) binding
- C49 (= C42) modified: Disulfide link with 54, Redox-active
- C54 (= C47) modified: Disulfide link with 49, Redox-active
- K58 (= K51) binding
- G122 (≠ A114) binding
- D319 (= D308) binding
- A327 (= A316) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
46% identity, 99% coverage: 4:459/460 of query aligns to 7:473/477 of 5u8uD
- active site: P16 (= P13), L47 (= L38), C51 (= C42), C56 (= C47), S59 (= S50), G85 (= G75), V86 (≠ A76), V193 (= V178), E197 (= E182), S333 (≠ E320), F451 (≠ H437), H453 (= H439), E458 (= E444)
- binding flavin-adenine dinucleotide: I12 (= I9), G15 (= G12), P16 (= P13), G17 (= G14), E36 (= E33), K37 (vs. gap), G49 (= G40), T50 (= T41), C51 (= C42), G55 (= G46), C56 (= C47), K60 (= K51), H123 (≠ W113), G124 (≠ A114), A152 (= A137), S153 (≠ T138), G154 (= G139), I194 (= I179), R281 (= R268), G320 (= G307), D321 (= D308), M327 (= M314), L328 (= L315), A329 (= A316), H330 (= H317), H453 (= H439), P454 (= P440)
Sites not aligning to the query:
3ladA Refined crystal structure of lipoamide dehydrogenase from azotobacter vinelandii at 2.2 angstroms resolution. A comparison with the structure of glutathione reductase (see paper)
46% identity, 99% coverage: 4:459/460 of query aligns to 4:470/472 of 3ladA
- active site: L44 (= L38), C48 (= C42), C53 (= C47), S56 (= S50), V190 (= V178), E194 (= E182), F448 (≠ H437), H450 (= H439), E455 (= E444)
- binding flavin-adenine dinucleotide: I9 (= I9), G10 (= G10), G12 (= G12), P13 (= P13), E33 (= E33), K34 (vs. gap), G46 (= G40), T47 (= T41), C48 (= C42), G52 (= G46), C53 (= C47), H120 (≠ W113), G121 (≠ A114), A149 (= A137), S150 (≠ T138), G151 (= G139), I191 (= I179), R278 (= R268), D318 (= D308), L325 (= L315), A326 (= A316)
Query Sequence
>GFF3862 FitnessBrowser__Phaeo:GFF3862
MSLYDLIVIGGGPGGYVAAIRAAQLGLKVACVEGRGTLGGTCLNVGCIPSKAMLSSSGKY
ESLSHLAGHGIAIEGARLDLDAMMARKDKIVGDLTKGIAFLFQKNGVDLIEGWASIPAVG
KVKVGDEIHETKNILIATGSEPTPLPGVEIDEGDVVSSTGALTLPEVPKHLVVVGAGVIG
LELGQVWSRLGAKVTVVEYLDRILPGIDGEIAKLAQRALSKRGLKFQLGRALKFIDRSDE
GLTLTLDRVGKDKEEQLVADKVLIAIGRRPVIRGLGLEALGVSVNARGFVEVDERFSTSV
EGIYAIGDCVPGPMLAHKAEEDGVACVEMLAGQAGHVDYNTVPGIVYTDPEVASVGKTEE
ALKDAGTDYIVGKFIFMANSRARAQGETDGAVKVLATPEGQILGAHICGAHGGDLIAELV
LAMTKGATVAEVAATCHAHPAMAEAVKEACLDAMGRAIHA
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