SitesBLAST
Comparing BWI76_RS18905 FitnessBrowser__Koxy:BWI76_RS18905 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)
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
65% identity, 99% coverage: 4:449/452 of query aligns to 8:452/461 of P76037
- Y110 (= Y106) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
26% identity, 93% coverage: 13:432/452 of query aligns to 22:445/458 of 6f34A
- binding arginine: I40 (≠ M31), G42 (≠ P33), T43 (≠ M34), G44 (≠ T35), E115 (≠ D105), Y116 (= Y106), A119 (vs. gap), F228 (= F212), A229 (≠ S213), I231 (≠ L215), V314 (vs. gap)
- binding cholesterol: W201 (≠ Y176), Y202 (≠ G177)
- binding : G28 (≠ T19), F30 (≠ I21), D31 (≠ P22), M34 (= M25), A178 (= A153), R179 (≠ N154), A186 (≠ I161), I187 (≠ L162), A190 (≠ G165), L194 (≠ V169), Q296 (= Q286), V299 (= V289)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
26% identity, 93% coverage: 13:432/452 of query aligns to 20:443/456 of 5oqtA
- binding alanine: I38 (≠ M31), G40 (≠ P33), T41 (≠ M34), G42 (≠ T35), F226 (= F212), A227 (≠ S213), I229 (≠ L215)
- binding : E24 (≠ T17), G26 (≠ T19), F28 (≠ I21), D29 (≠ P22), M32 (= M25), A176 (= A153), R177 (≠ N154), A184 (≠ I161), A188 (≠ G165), L192 (≠ V169), Q294 (= Q286), V297 (= V289)
P30825 High affinity cationic amino acid transporter 1; CAT-1; CAT1; Ecotropic retroviral leukemia receptor homolog; Ecotropic retrovirus receptor homolog; Solute carrier family 7 member 1; System Y+ basic amino acid transporter from Homo sapiens (Human) (see paper)
23% identity, 84% coverage: 8:388/452 of query aligns to 20:438/629 of P30825
- N226 (≠ T186) modified: carbohydrate, N-linked (GlcNAc...) asparagine
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
24% identity, 78% coverage: 51:404/452 of query aligns to 56:422/458 of P24207
- F87 (≠ A82) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y85) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ Q87) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ S89) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ I90) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ A93) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F96) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W100) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (≠ S102) mutation to L: No effect on phenylalanine transport activity.
- W108 (≠ L103) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ Y106) mutation to L: 60% of wild-type phenylalanine transport activity.; mutation to Y: Enables the transport of tryptophan to almost the same steady-state level as that of phenylalanine.
- E118 (≠ N113) mutation E->G,L,V,N: Loss of activity.
- K168 (≠ Q163) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (≠ D218) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (≠ I244) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P336) mutation to A: 5% of wild-type phenylalanine transport activity.; mutation P->G,Q,K,R: Loss of activity.; mutation to S: 3% of wild-type phenylalanine transport activity.; mutation to T: 17% of wild-type phenylalanine transport activity.
Sites not aligning to the query:
- 26 mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- 54 P→A: 50% of wild-type phenylalanine transport activity.; P→G: No change in phenylalanine transport activity.; P→L: 26% of wild-type phenylalanine transport activity.
- 442 P→A: 46% of wild-type phenylalanine transport activity.; P→G: 52% of wild-type phenylalanine transport activity.; P→L: 43% of wild-type phenylalanine transport activity.
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
22% identity, 98% coverage: 8:449/452 of query aligns to 2:464/469 of P46349
- G33 (≠ T39) mutation to D: Lack of activity.
- G42 (≠ D48) mutation to S: Lack of activity.
- G301 (= G301) mutation to V: Lack of activity.
- G338 (≠ V343) mutation to E: Lack of activity.
- F341 (≠ I346) mutation to S: Lack of activity.
- G414 (= G404) mutation to R: Lack of activity.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
24% identity, 71% coverage: 4:325/452 of query aligns to 3:336/489 of P25737
- Y102 (≠ S102) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y106) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (≠ Q163) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F212) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ D218) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E226) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ E275) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-278.
- D278 (vs. gap) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-275.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 438 E→A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 443 D→A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 446 D→A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
P15993 Aromatic amino acid transport protein AroP; Aromatic amino acid:H(+) symporter AroP; General aromatic amino acid permease; General aromatic transport system from Escherichia coli (strain K12) (see paper)
26% identity, 37% coverage: 70:237/452 of query aligns to 67:237/457 of P15993
- Y103 (= Y106) Key residue for tryptophan transport; mutation to F: Decreases tryptophan transport to less than 50% of wild-type levels and reduces the ability of tryptophan to inhibit phenylalanine transport from 95 to 62%.
Q9UPY5 Cystine/glutamate transporter; Amino acid transport system xc-; Calcium channel blocker resistance protein CCBR1; Solute carrier family 7 member 11; xCT from Homo sapiens (Human) (see 4 papers)
20% identity, 85% coverage: 1:386/452 of query aligns to 27:413/501 of Q9UPY5
- C86 (≠ A58) mutation to S: Does not affect L-cystine transport activity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- R135 (vs. gap) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ A123) modified: Interchain (with C-210 in SLC3A2); mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- Q191 (≠ N156) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ L162) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435.
- K198 (≠ Q163) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ F212) binding
- F254 (≠ S222) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ F239) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- C327 (≠ V297) mutation to A: Does not affect L-glutamate transport activity. Does not affect location at cell membrane Does not affect expression level.; mutation to L: Loss of L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Loss of inhibitio nof L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid. Decrease L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to T: Does not affect L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.
- F336 (≠ A306) mutation to A: Decreases L-cystine transport activity about 50%. Increases sensitivity to erastin-induced ferroptosis. Significantly decreases the L-cystine transport activity.; mutation to Y: Does not affect L-cystine transport activity.
- R396 (≠ A369) mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.; mutation to N: Loss of L-cystine transport activity.
Sites not aligning to the query:
- 414 C→S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- 435 C→S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
P82251 b(0,+)-type amino acid transporter 1; b(0,+)AT1; Glycoprotein-associated amino acid transporter b0,+AT1; Solute carrier family 7 member 9 from Homo sapiens (Human) (see 11 papers)
22% identity, 75% coverage: 66:402/452 of query aligns to 80:415/487 of P82251
- Y99 (= Y85) to H: in CSNU; uncertain significance
- G105 (≠ S91) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W100) to R: in CSNU; uncertain significance
- I120 (vs. gap) to L: in CSNU; uncertain significance
- T123 (vs. gap) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ F121) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ A123) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ I149) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ I161) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G177) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (= L210) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ C211) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (vs. gap) to D: in CSNU; decreased amino acid transport activity
- W230 (vs. gap) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ L215) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F217) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ G219) mutation to A: Reduces amino acid transport activity.
- G259 (vs. gap) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ T241) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ F266) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ H305) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ V308) to E: in CSNU; uncertain significance
- V330 (= V314) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M315) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (= R317) to Q: in CSNU; decreased amino acid transport activity; dbSNP:rs769576205; to W: in CSNU; severe loss of amino acid transport activity; dbSNP:rs121908484
- A354 (≠ N339) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ A366) mutation to A: Markedly reduces amino acid transport activity.
- A382 (= A369) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ F370) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ V373) mutation to A: Loss of amino acid transport activity.
- K401 (≠ N388) to E: in CSNU; uncertain significance; dbSNP:rs760264924
Sites not aligning to the query:
- 40 V → M: in CSNU; uncertain significance
- 43:47 binding
- 44 I → T: in CSNU; type I; dbSNP:rs121908485
- 51 S → F: in CSNU; uncertain significance
- 52 P → L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- 70 A → V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- 426 L → P: in CSNU; uncertain significance
- 482 P → L: in CSNU; severe loss of amino acid transport activity; no effect on localization to the apical membrane; dbSNP:rs146815072; mutation P->A,G,S,V: No effect on amino acid transport activity.; mutation P->F,I,M,W: Decreased amino acid transport activity.
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
22% identity, 75% coverage: 66:402/452 of query aligns to 51:386/458 of 6li9B
Sites not aligning to the query:
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
21% identity, 72% coverage: 63:386/452 of query aligns to 47:369/453 of 7epzB
Sites not aligning to the query:
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
21% identity, 72% coverage: 63:386/452 of query aligns to 47:369/455 of 7p9uB
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
23% identity, 74% coverage: 66:401/452 of query aligns to 62:390/438 of O34739
- C94 (≠ V98) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ T142) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ V169) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ S300) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
Sites not aligning to the query:
- 415 C→S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
6kkrA Human kcc1 structure determined in kcl and detergent gdn (see paper)
24% identity, 46% coverage: 221:426/452 of query aligns to 323:534/537 of 6kkrA
- binding beta-D-glucopyranose: Y521 (≠ I413), Y522 (≠ N414)
- binding chloride ion: Y474 (≠ F370)
- binding 2-[2-[(1~{S},2~{S},4~{S},5'~{R},6~{R},7~{S},8~{R},9~{S},12~{S},13~{R},16~{S})-5',7,9,13-tetramethylspiro[5-oxapentacyclo[10.8.0.0^{2,9}.0^{4,8}.0^{13,18}]icos-18-ene-6,2'-oxane]-16-yl]oxyethyl]propane-1,3-diol: I449 (= I346), Y521 (≠ I413), Y522 (≠ N414), V525 (≠ E417), M532 (≠ L424)
- binding alpha-D-glucopyranose: M461 (≠ L355)
Sites not aligning to the query:
- binding chloride ion: 318, 320
- binding 2-[2-[(1~{S},2~{S},4~{S},5'~{R},6~{R},7~{S},8~{R},9~{S},12~{S},13~{R},16~{S})-5',7,9,13-tetramethylspiro[5-oxapentacyclo[10.8.0.0^{2,9}.0^{4,8}.0^{13,18}]icos-18-ene-6,2'-oxane]-16-yl]oxyethyl]propane-1,3-diol: 88, 96
- binding alpha-D-glucopyranose: 272
- binding potassium ion: 16, 17, 101, 314, 315, 317
7ttiA Human kcc1 bound with vu0463271 in an outward-open state (see paper)
24% identity, 46% coverage: 221:426/452 of query aligns to 324:535/542 of 7ttiA
Sites not aligning to the query:
Q7YQK4 Large neutral amino acids transporter small subunit 1; 4F2 light chain; 4F2 LC; 4F2LC; L-type amino acid transporter 1; LAT1; Solute carrier family 7 member 5 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
24% identity, 46% coverage: 194:402/452 of query aligns to 234:433/503 of Q7YQK4
- W234 (= W194) mutation to L: Decreased KM and Vmax for Trp. Increased KM but decreased Vmax for Phe. Increased KM and Vmax for Phe; when associated with D-219.
- C331 (≠ V297) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
- C377 (≠ G344) mutation to S: No significant effect on inhibition by HgCl(2).
- C403 (≠ F372) mutation to S: No significant effect on inhibition by HgCl(2).
Sites not aligning to the query:
- 88 C→S: No significant effect on inhibition by HgCl(2). Decreased KM and Vmax for Phe. Similar affect on KM and Vmax for Phe; when associated with S-183.
- 98 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe. Slightly less decreased KM and Vmax for Phe; when associated with S-183.
- 160 C→S: No change to KM or Vmax for Phe.
- 172 C→S: No change to KM or Vmax for Phe.
- 174 C→S: No change to KM or Vmax for Phe.
- 183 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe. Similar affect on KM and Vmax for Phe; when associated with S-88. Slightly less decreased KM and Vmax for Phe; when associated with S-98.
- 219 G→D: Decreased KM and Vmax for Trp. Increased KM and Vmax for Phe; when associated with L-234.
- 439 C→S: Prevents insertion into the plasma membrane and possibly protein folding.
- 454 C→S: No significant effect on inhibition by HgCl(2). Slightly increased KM but slightly decreased Vmax for Phe.
- 492 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe.
7dsqB Overall structure of the lat1-4f2hc bound with 3,5-diiodo-l-tyrosine (see paper)
24% identity, 42% coverage: 212:402/452 of query aligns to 209:394/464 of 7dsqB
Sites not aligning to the query:
7dsnB Overall structure of the lat1-4f2hc bound with jx-119 (see paper)
24% identity, 42% coverage: 212:402/452 of query aligns to 209:394/464 of 7dsnB
Sites not aligning to the query:
- binding (2~{S})-2-azanyl-7-[[2-(1,3-benzoxazol-2-yl)phenyl]methoxy]-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid: 19, 20, 22, 23, 24, 97, 104
- binding cholesterol hemisuccinate: 109, 145, 148, 153, 457
7dslB Overall structure of the lat1-4f2hc bound with jx-078 (see paper)
24% identity, 42% coverage: 212:402/452 of query aligns to 209:394/464 of 7dslB
Sites not aligning to the query:
Query Sequence
>BWI76_RS18905 FitnessBrowser__Koxy:BWI76_RS18905
MSHNATPKTSRVELRKTLTLIPVVMMGLAYMQPMTLFDTFGIVSGLTDGHVATAYAFALI
AILFTALSYGKLVRRFPSAGSAYTYAQKSISPAVGFMVGWSSLLDYLFMPMINILLAKIY
FEALVPSIPSWIFVVALVAFMTISNLRSIKTVANFNTLIVILQMGIVAVIVGLIIYGVMH
GEGAGTLTSTRPFWSEGAHVVPMITGATILCFSFLGFDGISSLSEETKDAERVIPKAIFL
TALIGGLIFIGASYFLQLYFPDISRFKDPDASQPEIMLYVAGKTFQWGVLIFSSVTVLAS
GMAAHAGVSRLMYVMGRDGVFPTRFFGYVHPKWRTPAWNVLLVGAIALLAIKFDLVTATA
LINFGALVAFTFVNLSVISQFWIREKRNKTLKDHFNYLILPVCGALTVGALWINLEESSM
VLGLIWGGIGLVYLACVTKSFRNPVPQYEDVA
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