SitesBLAST
Comparing 3609502 FitnessBrowser__Dino:3609502 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
59% identity, 99% coverage: 4:463/464 of query aligns to 1:465/465 of 3urhB
- active site: Y35 (≠ L38), C39 (= C42), C44 (= C47), S47 (= S50), V183 (= V181), E187 (= E185), H443 (= H441), H445 (= H443), E450 (= E448)
- 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 (≠ W114), G112 (≠ A115), A140 (= A138), T141 (≠ S139), G142 (= G140), I184 (= I182), R273 (= R271), G312 (= G310), D313 (= D311), M319 (= M317), L320 (= L318), A321 (= A319), H322 (= H320)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
55% identity, 100% coverage: 1:463/464 of query aligns to 4:469/470 of 6uziC
- active site: C45 (= C42), C50 (= C47), S53 (= S50), V187 (= V181), E191 (= E185), H448 (= H443), E453 (= E448)
- 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 (≠ W114), G118 (≠ A115), T147 (≠ S139), G148 (= G140), I188 (= I182), R276 (= R271), D316 (= D311), M322 (= M317), L323 (= L318), A324 (= A319)
- binding zinc ion: H448 (= H443), E453 (= E448)
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)
55% identity, 99% coverage: 5:463/464 of query aligns to 39:500/501 of P31023
- 67:76 (vs. 33:42, 70% identical) binding
- C76 (= C42) modified: Disulfide link with 81, Redox-active
- C81 (= C47) modified: Disulfide link with 76, Redox-active
- G149 (≠ A115) binding
- D348 (= D311) binding
- MLAH 354:357 (= MLAH 317:320) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
55% identity, 99% coverage: 5:463/464 of query aligns to 5:466/467 of 1dxlA
- active site: L38 (= L38), C42 (= C42), C47 (= C47), S50 (= S50), Y184 (≠ V181), E188 (= E185), H444 (= H441), H446 (= H443), E451 (= E448)
- 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 (≠ W114), G115 (≠ A115), T144 (≠ S139), G145 (= G140), Y184 (≠ V181), I185 (= I182), R274 (= R271), D314 (= D311), M320 (= M317), L321 (= L318), A322 (= A319), H323 (= H320)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
50% identity, 98% coverage: 5:460/464 of query aligns to 6:467/472 of 1zmdA
- active site: L39 (= L38), C43 (= C42), C48 (= C47), S51 (= S50), V186 (= V181), E190 (= E185), H448 (= H441), H450 (= H443), E455 (= E448)
- 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 (≠ W114), G117 (≠ A115), T146 (≠ S139), G147 (= G140), S166 (= S161), R278 (= R271), F281 (= F274), G317 (= G310), D318 (= D311), M324 (= M317), L325 (= L318), A326 (= A319), H327 (= H320)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (≠ V177), G183 (= G178), G185 (= G180), V186 (= V181), I187 (= I182), E190 (= E185), E206 (= E201), F207 (= F202), L208 (≠ M203), I276 (≠ T269), G277 (= G270), R278 (= R271), M324 (= M317), L325 (= L318), V355 (= V348), Y357 (= Y350)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
50% identity, 98% coverage: 5:460/464 of query aligns to 6:467/472 of 1zmcA
- active site: L39 (= L38), C43 (= C42), C48 (= C47), S51 (= S50), V186 (= V181), E190 (= E185), H448 (= H441), H450 (= H443), E455 (= E448)
- 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 (≠ W114), G117 (≠ A115), T146 (≠ S139), G147 (= G140), S166 (= S161), I187 (= I182), F281 (= F274), G317 (= G310), D318 (= D311), M324 (= M317), L325 (= L318), A326 (= A319), H327 (= H320)
- binding nicotinamide-adenine-dinucleotide: G183 (= G178), G185 (= G180), V205 (≠ I200), E206 (= E201), F207 (= F202), L208 (≠ M203), K240 (vs. gap), V241 (≠ I230), I276 (≠ T269), G277 (= G270), R278 (= R271), R297 (= R290), M324 (= M317)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
50% identity, 98% coverage: 5:460/464 of query aligns to 43:504/509 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 (≠ H65) to T: in dbSNP:rs1130477
- G154 (≠ A115) binding
- TGS 183:185 (≠ SGS 139:141) binding
- 220:227 (vs. 178:185, 75% identical) binding
- E243 (= E201) binding
- V278 (≠ I230) binding
- G314 (= G270) binding
- D355 (= D311) binding
- MLAH 361:364 (= MLAH 317:320) binding
- E375 (= E331) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (= H339) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (= D404) 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 (= E422) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ F429) 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 (= D435) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (= R438) 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 (= H441) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P444) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S447) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E448) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (= R451) to G: in DLDD; loss of enzyme activity; reduced interaction with PDHX; dbSNP:rs121964989
Sites not aligning to the query:
- 505 K→M: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
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)
51% identity, 99% coverage: 3:463/464 of query aligns to 26:498/499 of P09624
- 56:65 (vs. 33:42, 70% identical) binding
- C65 (= C42) modified: Disulfide link with 70, Redox-active
- C70 (= C47) modified: Disulfide link with 65, Redox-active
- K74 (= K51) binding
- G139 (≠ A115) binding
- D346 (= D311) binding
- MLAH 352:355 (= MLAH 317:320) binding
- H478 (= H443) 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+
51% identity, 99% coverage: 3:463/464 of query aligns to 5:477/478 of 1v59A
- active site: L40 (= L38), C44 (= C42), C49 (= C47), S52 (= S50), I193 (≠ V181), E197 (= E185), T349 (≠ G335), H455 (= H441), H457 (= H443), E462 (= E448)
- 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 (≠ W114), G118 (≠ A115), T153 (≠ S139), G154 (= G140), R285 (= R271), Y288 (≠ F274), G324 (= G310), D325 (= D311), M331 (= M317), L332 (= L318), A333 (= A319), H334 (= H320), Y364 (= Y350)
- binding nicotinamide-adenine-dinucleotide: I189 (≠ V177), G190 (= G178), E213 (= E201), F214 (= F202), K246 (≠ A234), V283 (≠ T269)
1jehA Crystal structure of yeast e3, lipoamide dehydrogenase (see paper)
51% identity, 99% coverage: 3:463/464 of query aligns to 5:477/478 of 1jehA
- active site: L40 (= L38), C44 (= C42), C49 (= C47), S52 (= S50), I193 (≠ V181), E197 (= E185), T349 (≠ G335), H455 (= H441), H457 (= H443), E462 (= E448)
- 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 (≠ A115), T153 (≠ S139), G154 (= G140), I194 (= I182), R285 (= R271), Y288 (≠ F274), L292 (= L278), G324 (= G310), D325 (= D311), M331 (= M317), L332 (= L318), A333 (= A319), H334 (= H320)
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
50% identity, 98% coverage: 5:460/464 of query aligns to 16:477/482 of 6hg8B
- active site: C53 (= C42), C58 (= C47), S61 (= S50), V196 (= V181), E200 (= E185), H460 (= H443), E465 (= E448)
- 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 (≠ W114), G127 (≠ A115), T156 (≠ S139), G157 (= G140), I197 (= I182), R288 (= R271), F291 (= F274), G327 (= G310), D328 (= D311), M334 (= M317), L335 (= L318), A336 (= A319), H337 (= H320)
2qaeA Crystal structure analysis of trypanosoma cruzi lipoamide dehydrogenase
54% identity, 94% coverage: 19:456/464 of query aligns to 18:457/465 of 2qaeA
- active site: L37 (= L38), C41 (= C42), C46 (= C47), S49 (= S50), V184 (= V181), E188 (= E185), H442 (= H441), H444 (= H443), E449 (= E448)
- binding flavin-adenine dinucleotide: E32 (= E33), K33 (≠ G34), R34 (= R35), G39 (= G40), T40 (= T41), C41 (= C42), G45 (= G46), C46 (= C47), K50 (= K51), E114 (≠ W114), G115 (≠ A115), T144 (≠ S139), G145 (= G140), S164 (= S161), I185 (= I182), F274 (= F274), G310 (= G310), D311 (= D311), M318 (= M317), L319 (= L318), A320 (= A319), H321 (= H320)
Sites not aligning to the query:
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
51% identity, 99% coverage: 4:463/464 of query aligns to 2:454/455 of 2yquB
- active site: P11 (= P13), L36 (= L38), C40 (= C42), C45 (= C47), S48 (= S50), G72 (≠ A76), V73 (≠ P77), V177 (= V181), E181 (= E185), S314 (≠ E323), H432 (= H441), H434 (= H443), E439 (= E448)
- binding carbonate ion: A310 (= A319), S314 (≠ E323), S423 (≠ A432), D426 (= D435)
- 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 (≠ W114), A111 (= A115), T137 (≠ S139), G138 (= G140), I178 (= I182), Y265 (≠ F274), G301 (= G310), D302 (= D311), M308 (= M317), L309 (= L318), A310 (= A319), H311 (= H320)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
51% identity, 99% coverage: 4:463/464 of query aligns to 2:454/455 of 2yquA
- active site: P11 (= P13), L36 (= L38), C40 (= C42), C45 (= C47), S48 (= S50), G72 (≠ A76), V73 (≠ P77), V177 (= V181), E181 (= E185), S314 (≠ E323), H432 (= H441), H434 (= H443), E439 (= E448)
- 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 (≠ W114), A111 (= A115), T137 (≠ S139), G138 (= G140), S157 (= S161), I178 (= I182), Y265 (≠ F274), G301 (= G310), D302 (= D311), M308 (= M317), L309 (= L318), A310 (= A319)
6aonA 1.72 angstrom resolution crystal structure of 2-oxoglutarate dehydrogenase complex subunit dihydrolipoamide dehydrogenase from bordetella pertussis in complex with fad
49% identity, 98% coverage: 3:456/464 of query aligns to 2:465/473 of 6aonA
- active site: P43 (≠ L38), C47 (= C42), C52 (= C47), S55 (= S50), V191 (= V181), E195 (= E185), H450 (= H441), H452 (= H443), E457 (= E448)
- binding calcium ion: A218 (≠ P208), A220 (≠ Q210), Q222 (≠ L212)
- binding flavin-adenine dinucleotide: I8 (= I9), G11 (= G12), P12 (= P13), G13 (= G14), D32 (vs. gap), A33 (vs. gap), W34 (vs. gap), G45 (= G40), T46 (= T41), C47 (= C42), G51 (= G46), C52 (= C47), K56 (= K51), K119 (≠ W114), G120 (≠ A115), T151 (≠ S139), G152 (= G140), N171 (≠ S161), I192 (= I182), R280 (= R271), Y283 (≠ F274), G319 (= G310), D320 (= D311), M326 (= M317), L327 (= L318), A328 (= A319), H329 (= H320)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
51% identity, 98% coverage: 4:459/464 of query aligns to 2:450/452 of 2eq7A
- active site: P11 (= P13), L36 (= L38), C40 (= C42), C45 (= C47), S48 (= S50), G72 (≠ A76), V73 (≠ P77), V177 (= V181), E181 (= E185), S314 (≠ E323), H432 (= H441), H434 (= H443), E439 (= E448)
- 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 (≠ W114), A111 (= A115), T137 (≠ S139), G138 (= G140), S157 (= S161), I178 (= I182), R262 (= R271), Y265 (≠ F274), D302 (= D311), M308 (= M317), L309 (= L318), A310 (= A319), H311 (= H320), Y341 (= Y350)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ G148), G174 (= G178), G176 (= G180), V177 (= V181), I178 (= I182), E197 (= E201), Y198 (≠ F202), V231 (= V235), V260 (≠ T269), G261 (= G270), R262 (= R271), M308 (= M317), L309 (= L318), V339 (= V348)
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)
51% identity, 99% coverage: 4:463/464 of query aligns to 4:470/472 of 3ladA
- active site: L44 (= L38), C48 (= C42), C53 (= C47), S56 (= S50), V190 (= V181), E194 (= E185), F448 (≠ H441), H450 (= H443), E455 (= E448)
- 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 (≠ W114), G121 (≠ A115), A149 (= A138), S150 (= S139), G151 (= G140), I191 (= I182), R278 (= R271), D318 (= D311), L325 (= L318), A326 (= A319)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
51% identity, 99% coverage: 4:463/464 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 (= D311) binding
- A327 (= A319) binding
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
49% identity, 99% coverage: 4:463/464 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 (≠ A115) binding
- D319 (= D311) binding
- A327 (= A319) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
49% identity, 99% coverage: 4:463/464 of query aligns to 7:473/477 of 5u8uD
- active site: P16 (= P13), L47 (= L38), C51 (= C42), C56 (= C47), S59 (= S50), G85 (≠ A76), V86 (≠ P77), V193 (= V181), E197 (= E185), S333 (≠ E323), F451 (≠ H441), H453 (= H443), E458 (= E448)
- 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 (≠ W114), G124 (≠ A115), A152 (= A138), S153 (= S139), G154 (= G140), I194 (= I182), R281 (= R271), G320 (= G310), D321 (= D311), M327 (= M317), L328 (= L318), A329 (= A319), H330 (= H320), H453 (= H443), P454 (= P444)
Sites not aligning to the query:
Query Sequence
>3609502 FitnessBrowser__Dino:3609502
MASYDVIIIGSGPGGYVGAIRCAQLGLKTACVEGRDTLGGTCLNVGCIPSKALLHASHQV
HEAEHNFEKMGIKVPAPKIDWKTMLAYKDDVIGQNTKGIEFLFKKNKVDWLKGWASIPEA
GKVKVGDETHEAKHIIIASGSEPASIPGAEVEIDEKVVVTSTGALELGKIPKRMVVVGGG
VIGLELGSVYARLGTEVSVIEFMDGITPGQDLEVARQFQKILTKQGLKFITGAAVQKVAA
TKSKAKVTYKMRKDDSEDSLEADIVLVSTGRKPFTEGLGLDALGVKMTERGQIATDGSYR
TNVPGVYAIGDVIEGPMLAHKAEDEGMAVAEMIAGQHPHVNYGVIPGVIYTHPEVASVGK
TEEQLKAEGVAYKVGKFSFMGNGRAKANFAADGFVKLLADKATDRILGAHVIGPMAGDLI
HEVCVAMEFGAAAEDLARTCHAHPTYSEAMREAALACGDGAIHA
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