HEADER LYASE(ALDEHYDE) 08-JUN-92 1FBA COMPND FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE (E.C.4.1.2.13) SOURCE (DROSOPHILA MELANOGASTER, STRAIN SEVELEN) (WILD TYPE, PUPEA) AUTHOR K.PIONTEK,G.HESTER REVDAT 1 31-OCT-93 1FBA 0 JRNL AUTH G.HESTER,O.BRENNER-HOLZACH,F.A.ROSSI, JRNL AUTH 2 M.STRUCK-DONATZ,K.H.WINTERHALTER,J.D.G.SMIT, JRNL AUTH 3 K.PIONTEK JRNL TITL THE CRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATE JRNL TITL 2 ALDOLASE FROM DROSOPHILA JRNL TITL 3 MELANOGASTER AT 2.5 ANGSTROMS RESOLUTION JRNL REF /FEBS$ LETT. V. 292 237 1991 JRNL REFN ASTM FEBLAL NE ISSN 0014-5793 165 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.A.MALEK,M.HY,A.HONEGGER,K.ROSE,O.BRENNER-HOLZACH REMARK 1 TITL FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM REMARK 1 TITL 2 DROSOPHILA MELANOGASTER: PRIMARY STRUCTURE REMARK 1 TITL 3 ANALYSIS, SECONDARY STRUCTURE PREDICTION, AND REMARK 1 TITL 4 COMPARISON WITH VERTEBRATE ALDOLASES REMARK 1 REF ARCH.BIOCHEM.BIOPHYS. V. 266 10 1988 REMARK 1 REFN ASTM ABBIA4 US ISSN 0003-9861 158 REMARK 2 REMARK 2 RESOLUTION. 1.9 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM PROLSQ REMARK 3 AUTHORS KONNERT,HENDRICKSON REMARK 3 R VALUE 0.179 REMARK 3 RMSD BOND DISTANCES 0.010 ANGSTROMS REMARK 3 RMSD BOND ANGLE DISTANCES 0.021 ANGSTROMS REMARK 3 REMARK 3 RESOLUTION RANGE 8.0 - 1.9 ANGSTROMS REMARK 3 REMARK 3 NUMBER OF PROTEIN ATOMS 10980 REMARK 3 NUMBER OF SOLVENT ATOMS 1816 REMARK 3 REMARK 3 FOR REFINEMENT WITH X-PLOR THE STANDARD PARAMETER FILE REMARK 3 WAS NOT USED INSTEAD THE PARAMETER FILE PROLSQ.PRO WAS REMARK 3 USED. THIS PARAMETER FILE MIMICS PROLSQ WEIGHTING. REMARK 4 REMARK 4 THE TRANSFORMATION PRESENTED ON *MTRIX 1* RECORDS BELOW REMARK 4 WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *A* WHEN REMARK 4 APPLIED TO CHAIN *B*. REMARK 4 THE TRANSFORMATION PRESENTED ON *MTRIX 1* RECORDS BELOW REMARK 4 WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *A* WHEN REMARK 4 APPLIED TO CHAIN *C*. REMARK 4 THE TRANSFORMATION PRESENTED ON *MTRIX 1* RECORDS BELOW REMARK 4 WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *A* WHEN REMARK 4 APPLIED TO CHAIN *D*. REMARK 5 REMARK 5 THE SEQUENCE IS DESCRIBED IN REFERENCE 1 ABOVE. SEQRES 1 A 361 ACE THR THR TYR PHE ASN TYR PRO SER LYS GLU LEU GLN SEQRES 2 A 361 ASP GLU LEU ARG GLU ILE ALA GLN LYS ILE VAL ALA PRO SEQRES 3 A 361 GLY LYS GLY ILE LEU ALA ALA ASP GLU SER GLY PRO THR SEQRES 4 A 361 MET GLY LYS ARG LEU GLN ASP ILE GLY VAL GLU ASN THR SEQRES 5 A 361 GLU ASP ASN ARG ARG ALA TYR ARG GLN LEU LEU PHE SER SEQRES 6 A 361 THR ASP PRO LYS LEU ALA GLU ASN ILE SER GLY VAL ILE SEQRES 7 A 361 LEU PHE HIS GLU THR LEU TYR GLN LYS ALA ASP ASP GLY SEQRES 8 A 361 THR PRO PHE ALA GLU ILE LEU LYS LYS LYS GLY ILE ILE SEQRES 9 A 361 LEU GLY ILE LYS VAL ASP LYS GLY VAL VAL PRO LEU PHE SEQRES 10 A 361 GLY SER GLU ASP GLU VAL THR THR GLN GLY LEU ASP ASP SEQRES 11 A 361 LEU ALA ALA ARG CYS ALA GLN TYR LYS LYS ASP GLY CYS SEQRES 12 A 361 ASP PHE ALA LYS TRP ARG CYS VAL LEU LYS ILE GLY LYS SEQRES 13 A 361 ASN THR PRO SER TYR GLN SER ILE LEU GLU ASN ALA ASN SEQRES 14 A 361 VAL LEU ALA ARG TYR ALA SER ILE CYS GLN SER GLN ARG SEQRES 15 A 361 ILE VAL PRO ILE VAL GLU PRO GLU VAL LEU PRO ASP GLY SEQRES 16 A 361 ASP HIS ASP LEU ASP ARG ALA GLN LYS VAL THR GLU THR SEQRES 17 A 361 VAL LEU ALA ALA VAL TYR LYS ALA LEU SER ASP HIS HIS SEQRES 18 A 361 VAL TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET VAL SEQRES 19 A 361 THR ALA GLY GLN SER ALA LYS LYS ASN THR PRO GLU GLU SEQRES 20 A 361 ILE ALA LEU ALA THR VAL GLN ALA LEU ARG ARG THR VAL SEQRES 21 A 361 PRO ALA ALA VAL THR GLY VAL THR PHE LEU SER GLY GLY SEQRES 22 A 361 GLN SER GLU GLU GLU ALA THR VAL ASN LEU SER ALA ILE SEQRES 23 A 361 ASN ASN VAL PRO LEU ILE ARG PRO TRP ALA LEU THR PHE SEQRES 24 A 361 SER TYR GLY ARG ALA LEU GLN ALA SER VAL LEU ARG ALA SEQRES 25 A 361 TRP ALA GLY LYS LYS GLU ASN ILE ALA ALA GLY GLN ASN SEQRES 26 A 361 GLU LEU LEU LYS ARG ALA LYS ALA ASN GLY ASP ALA ALA SEQRES 27 A 361 GLN GLY LYS TYR VAL ALA GLY SER ALA GLY ALA GLY SER SEQRES 28 A 361 GLY SER LEU PHE VAL ALA ASN HIS ALA TYR SEQRES 1 B 361 ACE THR THR TYR PHE ASN TYR PRO SER LYS GLU LEU GLN SEQRES 2 B 361 ASP GLU LEU ARG GLU ILE ALA GLN LYS ILE VAL ALA PRO SEQRES 3 B 361 GLY LYS GLY ILE LEU ALA ALA ASP GLU SER GLY PRO THR SEQRES 4 B 361 MET GLY LYS ARG LEU GLN ASP ILE GLY VAL GLU ASN THR SEQRES 5 B 361 GLU ASP ASN ARG ARG ALA TYR ARG GLN LEU LEU PHE SER SEQRES 6 B 361 THR ASP PRO LYS LEU ALA GLU ASN ILE SER GLY VAL ILE SEQRES 7 B 361 LEU PHE HIS GLU THR LEU TYR GLN LYS ALA ASP ASP GLY SEQRES 8 B 361 THR PRO PHE ALA GLU ILE LEU LYS LYS LYS GLY ILE ILE SEQRES 9 B 361 LEU GLY ILE LYS VAL ASP LYS GLY VAL VAL PRO LEU PHE SEQRES 10 B 361 GLY SER GLU ASP GLU VAL THR THR GLN GLY LEU ASP ASP SEQRES 11 B 361 LEU ALA ALA ARG CYS ALA GLN TYR LYS LYS ASP GLY CYS SEQRES 12 B 361 ASP PHE ALA LYS TRP ARG CYS VAL LEU LYS ILE GLY LYS SEQRES 13 B 361 ASN THR PRO SER TYR GLN SER ILE LEU GLU ASN ALA ASN SEQRES 14 B 361 VAL LEU ALA ARG TYR ALA SER ILE CYS GLN SER GLN ARG SEQRES 15 B 361 ILE VAL PRO ILE VAL GLU PRO GLU VAL LEU PRO ASP GLY SEQRES 16 B 361 ASP HIS ASP LEU ASP ARG ALA GLN LYS VAL THR GLU THR SEQRES 17 B 361 VAL LEU ALA ALA VAL TYR LYS ALA LEU SER ASP HIS HIS SEQRES 18 B 361 VAL TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET VAL SEQRES 19 B 361 THR ALA GLY GLN SER ALA LYS LYS ASN THR PRO GLU GLU SEQRES 20 B 361 ILE ALA LEU ALA THR VAL GLN ALA LEU ARG ARG THR VAL SEQRES 21 B 361 PRO ALA ALA VAL THR GLY VAL THR PHE LEU SER GLY GLY SEQRES 22 B 361 GLN SER GLU GLU GLU ALA THR VAL ASN LEU SER ALA ILE SEQRES 23 B 361 ASN ASN VAL PRO LEU ILE ARG PRO TRP ALA LEU THR PHE SEQRES 24 B 361 SER TYR GLY ARG ALA LEU GLN ALA SER VAL LEU ARG ALA SEQRES 25 B 361 TRP ALA GLY LYS LYS GLU ASN ILE ALA ALA GLY GLN ASN SEQRES 26 B 361 GLU LEU LEU LYS ARG ALA LYS ALA ASN GLY ASP ALA ALA SEQRES 27 B 361 GLN GLY LYS TYR VAL ALA GLY SER ALA GLY ALA GLY SER SEQRES 28 B 361 GLY SER LEU PHE VAL ALA ASN HIS ALA TYR SEQRES 1 C 361 ACE THR THR TYR PHE ASN TYR PRO SER LYS GLU LEU GLN SEQRES 2 C 361 ASP GLU LEU ARG GLU ILE ALA GLN LYS ILE VAL ALA PRO SEQRES 3 C 361 GLY LYS GLY ILE LEU ALA ALA ASP GLU SER GLY PRO THR SEQRES 4 C 361 MET GLY LYS ARG LEU GLN ASP ILE GLY VAL GLU ASN THR SEQRES 5 C 361 GLU ASP ASN ARG ARG ALA TYR ARG GLN LEU LEU PHE SER SEQRES 6 C 361 THR ASP PRO LYS LEU ALA GLU ASN ILE SER GLY VAL ILE SEQRES 7 C 361 LEU PHE HIS GLU THR LEU TYR GLN LYS ALA ASP ASP GLY SEQRES 8 C 361 THR PRO PHE ALA GLU ILE LEU LYS LYS LYS GLY ILE ILE SEQRES 9 C 361 LEU GLY ILE LYS VAL ASP LYS GLY VAL VAL PRO LEU PHE SEQRES 10 C 361 GLY SER GLU ASP GLU VAL THR THR GLN GLY LEU ASP ASP SEQRES 11 C 361 LEU ALA ALA ARG CYS ALA GLN TYR LYS LYS ASP GLY CYS SEQRES 12 C 361 ASP PHE ALA LYS TRP ARG CYS VAL LEU LYS ILE GLY LYS SEQRES 13 C 361 ASN THR PRO SER TYR GLN SER ILE LEU GLU ASN ALA ASN SEQRES 14 C 361 VAL LEU ALA ARG TYR ALA SER ILE CYS GLN SER GLN ARG SEQRES 15 C 361 ILE VAL PRO ILE VAL GLU PRO GLU VAL LEU PRO ASP GLY SEQRES 16 C 361 ASP HIS ASP LEU ASP ARG ALA GLN LYS VAL THR GLU THR SEQRES 17 C 361 VAL LEU ALA ALA VAL TYR LYS ALA LEU SER ASP HIS HIS SEQRES 18 C 361 VAL TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET VAL SEQRES 19 C 361 THR ALA GLY GLN SER ALA LYS LYS ASN THR PRO GLU GLU SEQRES 20 C 361 ILE ALA LEU ALA THR VAL GLN ALA LEU ARG ARG THR VAL SEQRES 21 C 361 PRO ALA ALA VAL THR GLY VAL THR PHE LEU SER GLY GLY SEQRES 22 C 361 GLN SER GLU GLU GLU ALA THR VAL ASN LEU SER ALA ILE SEQRES 23 C 361 ASN ASN VAL PRO LEU ILE ARG PRO TRP ALA LEU THR PHE SEQRES 24 C 361 SER TYR GLY ARG ALA LEU GLN ALA SER VAL LEU ARG ALA SEQRES 25 C 361 TRP ALA GLY LYS LYS GLU ASN ILE ALA ALA GLY GLN ASN SEQRES 26 C 361 GLU LEU LEU LYS ARG ALA LYS ALA ASN GLY ASP ALA ALA SEQRES 27 C 361 GLN GLY LYS TYR VAL ALA GLY SER ALA GLY ALA GLY SER SEQRES 28 C 361 GLY SER LEU PHE VAL ALA ASN HIS ALA TYR SEQRES 1 D 361 ACE THR THR TYR PHE ASN TYR PRO SER LYS GLU LEU GLN SEQRES 2 D 361 ASP GLU LEU ARG GLU ILE ALA GLN LYS ILE VAL ALA PRO SEQRES 3 D 361 GLY LYS GLY ILE LEU ALA ALA ASP GLU SER GLY PRO THR SEQRES 4 D 361 MET GLY LYS ARG LEU GLN ASP ILE GLY VAL GLU ASN THR SEQRES 5 D 361 GLU ASP ASN ARG ARG ALA TYR ARG GLN LEU LEU PHE SER SEQRES 6 D 361 THR ASP PRO LYS LEU ALA GLU ASN ILE SER GLY VAL ILE SEQRES 7 D 361 LEU PHE HIS GLU THR LEU TYR GLN LYS ALA ASP ASP GLY SEQRES 8 D 361 THR PRO PHE ALA GLU ILE LEU LYS LYS LYS GLY ILE ILE SEQRES 9 D 361 LEU GLY ILE LYS VAL ASP LYS GLY VAL VAL PRO LEU PHE SEQRES 10 D 361 GLY SER GLU ASP GLU VAL THR THR GLN GLY LEU ASP ASP SEQRES 11 D 361 LEU ALA ALA ARG CYS ALA GLN TYR LYS LYS ASP GLY CYS SEQRES 12 D 361 ASP PHE ALA LYS TRP ARG CYS VAL LEU LYS ILE GLY LYS SEQRES 13 D 361 ASN THR PRO SER TYR GLN SER ILE LEU GLU ASN ALA ASN SEQRES 14 D 361 VAL LEU ALA ARG TYR ALA SER ILE CYS GLN SER GLN ARG SEQRES 15 D 361 ILE VAL PRO ILE VAL GLU PRO GLU VAL LEU PRO ASP GLY SEQRES 16 D 361 ASP HIS ASP LEU ASP ARG ALA GLN LYS VAL THR GLU THR SEQRES 17 D 361 VAL LEU ALA ALA VAL TYR LYS ALA LEU SER ASP HIS HIS SEQRES 18 D 361 VAL TYR LEU GLU GLY THR LEU LEU LYS PRO ASN MET VAL SEQRES 19 D 361 THR ALA GLY GLN SER ALA LYS LYS ASN THR PRO GLU GLU SEQRES 20 D 361 ILE ALA LEU ALA THR VAL GLN ALA LEU ARG ARG THR VAL SEQRES 21 D 361 PRO ALA ALA VAL THR GLY VAL THR PHE LEU SER GLY GLY SEQRES 22 D 361 GLN SER GLU GLU GLU ALA THR VAL ASN LEU SER ALA ILE SEQRES 23 D 361 ASN ASN VAL PRO LEU ILE ARG PRO TRP ALA LEU THR PHE SEQRES 24 D 361 SER TYR GLY ARG ALA LEU GLN ALA SER VAL LEU ARG ALA SEQRES 25 D 361 TRP ALA GLY LYS LYS GLU ASN ILE ALA ALA GLY GLN ASN SEQRES 26 D 361 GLU LEU LEU LYS ARG ALA LYS ALA ASN GLY ASP ALA ALA SEQRES 27 D 361 GLN GLY LYS TYR VAL ALA GLY SER ALA GLY ALA GLY SER SEQRES 28 D 361 GLY SER LEU PHE VAL ALA ASN HIS ALA TYR FTNOTE 1 FTNOTE 1 RESIDUE 158 IS A CIS PROLINE IN ALL FOUR CHAINS. FORMUL 5 HOH *1816(H2 O1) HELIX 1 1I LYS A 9 ILE A 22 1 SUBUNIT 1 HELIX 2 1A1 GLY A 36 ASP A 45 1 HELIX 3 1A2 GLU A 52 PHE A 63 1 HELIX 4 1A3 PRO A 67 GLU A 71 5 HELIX 5 1B1 HIS A 80 LEU A 83 1 HELIX 6 1B2 PHE A 93 LYS A 99 1 HELIX 7 1C LEU A 130 LYS A 139 1 HELIX 8 1D TYR A 160 SER A 179 1 HELIX 9 1E1 LEU A 198 ASP A 218 1 HELIX 10 1E2 LEU A 223 GLY A 225 5 HELIX 11 1F PRO A 245 THR A 259 1 HELIX 12 1G GLU A 276 ILE A 286 1 HELIX 13 1H1 ARG A 303 LEU A 305 5 HELIX 14 1H2 ALA A 307 TRP A 313 1 HELIX 15 1H3 ILE A 320 ALA A 337 1 HELIX 16 2I LYS B 9 ILE B 22 1 SUBUNIT 2 HELIX 17 2A1 GLY B 36 GLN B 44 1 HELIX 18 2A2 GLU B 52 PHE B 63 1 HELIX 19 2A3 PRO B 67 GLU B 71 5 HELIX 20 2B1 HIS B 80 LEU B 83 1 HELIX 21 2B2 PHE B 93 LYS B 99 1 HELIX 22 2C LEU B 130 LYS B 139 1 HELIX 23 2D TYR B 160 SER B 179 1 HELIX 24 2E1 LEU B 198 ASP B 218 1 HELIX 25 2E2 LEU B 223 GLY B 225 5 HELIX 26 2F PRO B 245 THR B 259 1 HELIX 27 2G GLU B 276 ILE B 286 1 HELIX 28 2H1 ARG B 303 TRP B 313 1 HELIX 29 2H2 LYS B 317 ASN B 319 5 HELIX 30 2H3 ILE B 320 ALA B 337 1 HELIX 31 3I LYS C 9 ILE C 22 1 SUBUNIT 3 HELIX 32 3A1 GLY C 36 ASP C 45 1 HELIX 33 3A2 GLU C 52 SER C 64 1 HELIX 34 3A3 PRO C 67 GLU C 71 5 HELIX 35 3B1 THR C 82 TYR C 84 5 HELIX 36 3B2 PHE C 93 LYS C 99 1 HELIX 37 3C LEU C 130 LYS C 139 1 HELIX 38 3D TYR C 160 SER C 179 1 HELIX 39 3E1 LEU C 198 ASP C 218 1 HELIX 40 3E2 LEU C 223 GLY C 225 5 HELIX 41 3F PRO C 245 THR C 259 1 HELIX 42 3G GLU C 276 ILE C 286 1 HELIX 43 3H1 ARG C 303 TRP C 313 1 HELIX 44 3H2 LYS C 317 ASN C 319 5 HELIX 45 3H3 ILE C 320 ALA C 337 1 HELIX 46 4I LYS D 9 ILE D 22 1 SUBUNIT 4 HELIX 47 4A1 GLY D 36 ASP D 45 1 HELIX 48 4A2 GLU D 52 PHE D 63 1 HELIX 49 4A3 PRO D 67 GLU D 71 5 HELIX 50 4B1 HIS D 80 LEU D 83 1 HELIX 51 4B2 PHE D 93 LYS D 99 1 HELIX 52 4C LEU D 130 LYS D 139 1 HELIX 53 4D TYR D 160 SER D 179 1 HELIX 54 4E1 LEU D 198 ASP D 218 1 HELIX 55 4E2 LEU D 223 GLY D 225 5 HELIX 56 4F PRO D 245 THR D 259 1 HELIX 57 4G GLU D 276 ILE D 286 1 HELIX 58 4H1 ARG D 303 TRP D 313 1 HELIX 59 4H2 LYS D 317 ASN D 319 5 HELIX 60 4H3 ILE D 320 ALA D 337 1 SHEET 1 PS1 8 ILE A 103 LYS A 107 0 SHEET 2 PS1 8 ILE A 73 LEU A 78 1 O SER A 74 N ILE A 103 SHEET 3 PS1 8 GLY A 28 ALA A 32 1 O GLY A 28 N SER A 74 SHEET 4 PS1 8 ALA A 296 TYR A 301 1 O PHE A 299 N ILE A 29 SHEET 5 PS1 8 GLY A 266 PHE A 269 1 N VAL A 267 O ALA A 296 SHEET 6 PS1 8 LEU A 227 LEU A 228 1 N LEU A 228 O GLY A 266 SHEET 7 PS1 8 VAL A 183 VAL A 190 1 O PRO A 184 N LEU A 227 SHEET 8 PS1 8 CYS A 142 LEU A 151 1 O ASP A 143 N VAL A 183 SHEET 1 AS1 2 VAL A 112 PRO A 114 0 SHEET 2 AS1 2 VAL A 122 THR A 124 -1 N THR A 123 O VAL A 113 SHEET 1 PS2 8 ILE B 103 LYS B 107 0 SHEET 2 PS2 8 ILE B 73 LEU B 78 1 O SER B 74 N ILE B 103 SHEET 3 PS2 8 GLY B 28 ALA B 32 1 O GLY B 28 N SER B 74 SHEET 4 PS2 8 ALA B 296 TYR B 301 1 O PHE B 299 N ILE B 29 SHEET 5 PS2 8 GLY B 266 PHE B 269 1 N VAL B 267 O ALA B 296 SHEET 6 PS2 8 LEU B 227 LEU B 228 1 N LEU B 228 O GLY B 266 SHEET 7 PS2 8 VAL B 183 VAL B 190 1 O PRO B 184 N LEU B 227 SHEET 8 PS2 8 CYS B 142 LEU B 151 1 O ASP B 143 N VAL B 183 SHEET 1 AS2 2 VAL B 112 PRO B 114 0 SHEET 2 AS2 2 VAL B 122 THR B 124 -1 N THR B 123 O VAL B 113 SHEET 1 PS3 8 ILE C 103 LYS C 107 0 SHEET 2 PS3 8 ILE C 73 LEU C 78 1 O SER C 74 N ILE C 103 SHEET 3 PS3 8 GLY C 28 ALA C 32 1 O GLY C 28 N SER C 74 SHEET 4 PS3 8 ALA C 296 TYR C 301 1 O PHE C 299 N ILE C 29 SHEET 5 PS3 8 GLY C 266 PHE C 269 1 N VAL C 267 O ALA C 296 SHEET 6 PS3 8 LEU C 227 LEU C 228 1 N LEU C 228 O GLY C 266 SHEET 7 PS3 8 VAL C 183 VAL C 190 1 O PRO C 184 N LEU C 227 SHEET 8 PS3 8 CYS C 142 LEU C 151 1 O ASP C 143 N VAL C 183 SHEET 1 AS3 2 VAL C 112 PRO C 114 0 SHEET 2 AS3 2 VAL C 122 THR C 124 -1 N THR C 123 O VAL C 113 SHEET 1 PS4 8 ILE D 103 LYS D 107 0 SHEET 2 PS4 8 ILE D 73 LEU D 78 1 O SER D 74 N ILE D 103 SHEET 3 PS4 8 GLY D 28 ALA D 32 1 O GLY D 28 N SER D 74 SHEET 4 PS4 8 ALA D 296 TYR D 301 1 O PHE D 299 N ILE D 29 SHEET 5 PS4 8 GLY D 266 PHE D 269 1 N VAL D 267 O ALA D 296 SHEET 6 PS4 8 LEU D 227 LEU D 228 1 N LEU D 228 O GLY D 266 SHEET 7 PS4 8 VAL D 183 VAL D 190 1 O PRO D 184 N LEU D 227 SHEET 8 PS4 8 CYS D 142 LEU D 151 1 O ASP D 143 N VAL D 183 SHEET 1 AS4 2 VAL D 112 PRO D 114 0 SHEET 2 AS4 2 VAL D 122 THR D 124 -1 N THR D 123 O VAL D 113 SITE 1 FBA 1 LYS A 229 SITE 1 FBB 1 LYS B 229 SITE 1 FBC 1 LYS C 229 SITE 1 FBD 1 LYS D 229 CRYST1 86.600 116.800 151.580 90.00 90.00 90.00 P 21 21 21 16 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.011547 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008562 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006597 0.00000 MTRIX1 1 0.916260 -0.048320 -0.397670 14.08994 1 MTRIX2 1 -0.047230 -0.998810 0.012540 26.70957 1 MTRIX3 1 -0.397800 0.007300 -0.917440 64.53925 1 MTRIX1 2 -1.000000 -0.000990 -0.002730 3.28260 1 MTRIX2 2 -0.000360 0.975110 -0.221730 7.69806 1 MTRIX3 2 0.002890 -0.221730 -0.975100 68.96657 1 MTRIX1 3 -0.914350 0.040800 0.402860 -10.83144 1 MTRIX2 3 0.046220 -0.977890 0.203940 19.70642 1 MTRIX3 3 0.402270 0.205090 0.892250 0.22911 1