HEADER OXIDOREDUCTASE(OXYGEN AS ACCEPTOR) 09-NOV-93 1POX 1POX 2 COMPND PYRUVATE OXIDASE (E.C.1.2.3.3) MUTANT WITH PRO 178 1POX 3 COMPND 2 REPLACED BY SER, SER 188 REPLACED BY ASN, AND ALA 458 1POX 4 COMPND 3 REPLACED BY VAL (P178S,S188N,A458V) 1POX 5 SOURCE (LACTOBACILLUS PLANTARUM) 1POX 6 AUTHOR Y.A.MULLER,G.E.SCHULZ 1POX 7 REVDAT 1 31-JAN-94 1POX 0 1POX 8 JRNL AUTH Y.A.MULLER,G.SCHUMACHER,R.RUDOLPH,G.E.SCHULZ 1POX 9 JRNL TITL THE REFINED STRUCTURES OF A STABILIZED MUTANT AND 1POX 10 JRNL TITL 2 OF WILD-TYPE PYRUVATE OXIDASE FROM LACTOBACILLUS 1POX 11 JRNL TITL 3 PLANTARUM 1POX 12 JRNL REF TO BE PUBLISHED 1POX 13 JRNL REFN 353 1POX 14 REMARK 1 1POX 15 REMARK 1 REFERENCE 1 1POX 16 REMARK 1 AUTH Y.A.MULLER,G.E.SCHULZ 1POX 17 REMARK 1 TITL STRUCTURE OF THE THIAMINE- AND FLAVIN- DEPENDENT 1POX 18 REMARK 1 TITL 2 ENZYME PYRUVATE OXIDASE 1POX 19 REMARK 1 REF SCIENCE V. 259 965 1993 1POX 20 REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 038 1POX 21 REMARK 2 1POX 22 REMARK 2 RESOLUTION. 2.1 ANGSTROMS. 1POX 23 REMARK 3 1POX 24 REMARK 3 REFINEMENT. 1POX 25 REMARK 3 PROGRAM X-PLOR 1POX 26 REMARK 3 AUTHORS BRUNGER 1POX 27 REMARK 3 R VALUE 0.162 1POX 28 REMARK 3 RMSD BOND DISTANCES 0.014 ANGSTROMS 1POX 29 REMARK 3 RMSD BOND ANGLES 2.7 DEGREES 1POX 30 REMARK 3 1POX 31 REMARK 3 NUMBER OF REFLECTIONS 87755 1POX 32 REMARK 3 RESOLUTION RANGE 10 - 2.1 ANGSTROMS 1POX 33 REMARK 4 1POX 34 REMARK 4 PYRUVATE OXIDASE IS A HOMO-TETRAMERIC ENZYME. THERE ARE 1POX 35 REMARK 4 TWO SUBUNITS OF THE TETRAMER IN THE CRYSTALLOGRAPHIC 1POX 36 REMARK 4 ASYMMETRIC UNIT, LABELED CHAINS *A* AND *B*, EACH WITH AN 1POX 37 REMARK 4 ASSOCIATED TPP, FAD, AND GOL (GLYCEROL). 1POX 38 REMARK 5 1POX 39 REMARK 5 THE TETRAMER CAN BE GENERATED FROM THE ASYMMETRIC UNIT BY 1POX 40 REMARK 5 APPLYING THE FOLLOWING TRANSFORMATION: 1POX 41 REMARK 5 1 0 0 0 1POX 42 REMARK 5 0 -1 0 155.36 1POX 43 REMARK 5 0 0 -1 0 1POX 44 REMARK 6 1POX 45 REMARK 6 THE FINAL MODEL CONTAINS 739 WATER MOLECULES. SIX OF 1POX 46 REMARK 6 THESE WATER MOLECULES (RESIDUE NUMBERS 801 - 806) ARE 1POX 47 REMARK 6 LOCATED ON THE CRYSTALLOGRAPHIC TWO-FOLD AXES, AS IS THE 1POX 48 REMARK 6 NA+ ION. THE REMAINING WATER MOLECULES (1 - 733) ARE 1POX 49 REMARK 6 SORTED ACCORDING TO DECREASING ELECTRON DENSITY IN THE 1POX 50 REMARK 6 FINAL 2FO-FC DENSITY MAP. 1POX 51 REMARK 7 1POX 52 REMARK 7 THE TWO SUBUNITS OF THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT 1POX 53 REMARK 7 ARE RELATED BY A LOCAL TWOFOLD AXIS. THE TRANSFORMATION 1POX 54 REMARK 7 PRESENTED ON *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE 1POX 55 REMARK 7 COORDINATES FOR CHAIN *B* WHEN APPLIED TO CHAIN *A*. 1POX 56 SEQRES 1 A 585 THR ASN ILE LEU ALA GLY ALA ALA VAL ILE LYS VAL LEU 1POX 57 SEQRES 2 A 585 GLU ALA TRP GLY VAL ASP HIS LEU TYR GLY ILE PRO GLY 1POX 58 SEQRES 3 A 585 GLY SER ILE ASN SER ILE MET ASP ALA LEU SER ALA GLU 1POX 59 SEQRES 4 A 585 ARG ASP ARG ILE HIS TYR ILE GLN VAL ARG HIS GLU GLU 1POX 60 SEQRES 5 A 585 VAL GLY ALA MET ALA ALA ALA ALA ASP ALA LYS LEU THR 1POX 61 SEQRES 6 A 585 GLY LYS ILE GLY VAL CYS PHE GLY SER ALA GLY PRO GLY 1POX 62 SEQRES 7 A 585 GLY THR HIS LEU MET ASN GLY LEU TYR ASP ALA ARG GLU 1POX 63 SEQRES 8 A 585 ASP HIS VAL PRO VAL LEU ALA LEU ILE GLY GLN PHE GLY 1POX 64 SEQRES 9 A 585 THR THR GLY MET ASN MET ASP THR PHE GLN GLU MET ASN 1POX 65 SEQRES 10 A 585 GLU ASN PRO ILE TYR ALA ASP VAL ALA ASP TYR ASN VAL 1POX 66 SEQRES 11 A 585 THR ALA VAL ASN ALA ALA THR LEU PRO HIS VAL ILE ASP 1POX 67 SEQRES 12 A 585 GLU ALA ILE ARG ARG ALA TYR ALA HIS GLN GLY VAL ALA 1POX 68 SEQRES 13 A 585 VAL VAL GLN ILE PRO VAL ASP LEU PRO TRP GLN GLN ILE 1POX 69 SEQRES 14 A 585 SER ALA GLU ASP TRP TYR ALA SER ALA ASN ASN TYR GLN 1POX 70 SEQRES 15 A 585 THR PRO LEU LEU PRO GLU PRO ASP VAL GLN ALA VAL THR 1POX 71 SEQRES 16 A 585 ARG LEU THR GLN THR LEU LEU ALA ALA GLU ARG PRO LEU 1POX 72 SEQRES 17 A 585 ILE TYR TYR GLY ILE GLY ALA ARG LYS ALA GLY LYS GLU 1POX 73 SEQRES 18 A 585 LEU GLU GLN LEU SER LYS THR LEU LYS ILE PRO LEU MET 1POX 74 SEQRES 19 A 585 SER THR TYR PRO ALA LYS GLY ILE VAL ALA ASP ARG TYR 1POX 75 SEQRES 20 A 585 PRO ALA TYR LEU GLY SER ALA ASN ARG VAL ALA GLN LYS 1POX 76 SEQRES 21 A 585 PRO ALA ASN GLU ALA LEU ALA GLN ALA ASP VAL VAL LEU 1POX 77 SEQRES 22 A 585 PHE VAL GLY ASN ASN TYR PRO PHE ALA GLU VAL SER LYS 1POX 78 SEQRES 23 A 585 ALA PHE LYS ASN THR ARG TYR PHE LEU GLN ILE ASP ILE 1POX 79 SEQRES 24 A 585 ASP PRO ALA LYS LEU GLY LYS ARG HIS LYS THR ASP ILE 1POX 80 SEQRES 25 A 585 ALA VAL LEU ALA ASP ALA GLN LYS THR LEU ALA ALA ILE 1POX 81 SEQRES 26 A 585 LEU ALA GLN VAL SER GLU ARG GLU SER THR PRO TRP TRP 1POX 82 SEQRES 27 A 585 GLN ALA ASN LEU ALA ASN VAL LYS ASN TRP ARG ALA TYR 1POX 83 SEQRES 28 A 585 LEU ALA SER LEU GLU ASP LYS GLN GLU GLY PRO LEU GLN 1POX 84 SEQRES 29 A 585 ALA TYR GLN VAL LEU ARG ALA VAL ASN LYS ILE ALA GLU 1POX 85 SEQRES 30 A 585 PRO ASP ALA ILE TYR SER ILE ASP VAL GLY ASP ILE ASN 1POX 86 SEQRES 31 A 585 LEU ASN ALA ASN ARG HIS LEU LYS LEU THR PRO SER ASN 1POX 87 SEQRES 32 A 585 ARG HIS ILE THR SER ASN LEU PHE ALA THR MET GLY VAL 1POX 88 SEQRES 33 A 585 GLY ILE PRO GLY ALA ILE ALA ALA LYS LEU ASN TYR PRO 1POX 89 SEQRES 34 A 585 GLU ARG GLN VAL PHE ASN LEU ALA GLY ASP GLY GLY ALA 1POX 90 SEQRES 35 A 585 SER MET THR MET GLN ASP LEU VAL THR GLN VAL GLN TYR 1POX 91 SEQRES 36 A 585 HIS LEU PRO VAL ILE ASN VAL VAL PHE THR ASN CYS GLN 1POX 92 SEQRES 37 A 585 TYR GLY PHE ILE LYS ASP GLU GLN GLU ASP THR ASN GLN 1POX 93 SEQRES 38 A 585 ASN ASP PHE ILE GLY VAL GLU PHE ASN ASP ILE ASP PHE 1POX 94 SEQRES 39 A 585 SER LYS ILE ALA ASP GLY VAL HIS MET GLN ALA PHE ARG 1POX 95 SEQRES 40 A 585 VAL ASN LYS ILE GLU GLN LEU PRO ASP VAL PHE GLU GLN 1POX 96 SEQRES 41 A 585 ALA LYS ALA ILE ALA GLN HIS GLU PRO VAL LEU ILE ASP 1POX 97 SEQRES 42 A 585 ALA VAL ILE THR GLY ASP ARG PRO LEU PRO ALA GLU LYS 1POX 98 SEQRES 43 A 585 LEU ARG LEU ASP SER ALA MET SER SER ALA ALA ASP ILE 1POX 99 SEQRES 44 A 585 GLU ALA PHE LYS GLN ARG TYR GLU ALA GLN ASP LEU GLN 1POX 100 SEQRES 45 A 585 PRO LEU SER THR TYR LEU LYS GLN PHE GLY LEU ASP ASP 1POX 101 SEQRES 1 B 585 THR ASN ILE LEU ALA GLY ALA ALA VAL ILE LYS VAL LEU 1POX 102 SEQRES 2 B 585 GLU ALA TRP GLY VAL ASP HIS LEU TYR GLY ILE PRO GLY 1POX 103 SEQRES 3 B 585 GLY SER ILE ASN SER ILE MET ASP ALA LEU SER ALA GLU 1POX 104 SEQRES 4 B 585 ARG ASP ARG ILE HIS TYR ILE GLN VAL ARG HIS GLU GLU 1POX 105 SEQRES 5 B 585 VAL GLY ALA MET ALA ALA ALA ALA ASP ALA LYS LEU THR 1POX 106 SEQRES 6 B 585 GLY LYS ILE GLY VAL CYS PHE GLY SER ALA GLY PRO GLY 1POX 107 SEQRES 7 B 585 GLY THR HIS LEU MET ASN GLY LEU TYR ASP ALA ARG GLU 1POX 108 SEQRES 8 B 585 ASP HIS VAL PRO VAL LEU ALA LEU ILE GLY GLN PHE GLY 1POX 109 SEQRES 9 B 585 THR THR GLY MET ASN MET ASP THR PHE GLN GLU MET ASN 1POX 110 SEQRES 10 B 585 GLU ASN PRO ILE TYR ALA ASP VAL ALA ASP TYR ASN VAL 1POX 111 SEQRES 11 B 585 THR ALA VAL ASN ALA ALA THR LEU PRO HIS VAL ILE ASP 1POX 112 SEQRES 12 B 585 GLU ALA ILE ARG ARG ALA TYR ALA HIS GLN GLY VAL ALA 1POX 113 SEQRES 13 B 585 VAL VAL GLN ILE PRO VAL ASP LEU PRO TRP GLN GLN ILE 1POX 114 SEQRES 14 B 585 SER ALA GLU ASP TRP TYR ALA SER ALA ASN ASN TYR GLN 1POX 115 SEQRES 15 B 585 THR PRO LEU LEU PRO GLU PRO ASP VAL GLN ALA VAL THR 1POX 116 SEQRES 16 B 585 ARG LEU THR GLN THR LEU LEU ALA ALA GLU ARG PRO LEU 1POX 117 SEQRES 17 B 585 ILE TYR TYR GLY ILE GLY ALA ARG LYS ALA GLY LYS GLU 1POX 118 SEQRES 18 B 585 LEU GLU GLN LEU SER LYS THR LEU LYS ILE PRO LEU MET 1POX 119 SEQRES 19 B 585 SER THR TYR PRO ALA LYS GLY ILE VAL ALA ASP ARG TYR 1POX 120 SEQRES 20 B 585 PRO ALA TYR LEU GLY SER ALA ASN ARG VAL ALA GLN LYS 1POX 121 SEQRES 21 B 585 PRO ALA ASN GLU ALA LEU ALA GLN ALA ASP VAL VAL LEU 1POX 122 SEQRES 22 B 585 PHE VAL GLY ASN ASN TYR PRO PHE ALA GLU VAL SER LYS 1POX 123 SEQRES 23 B 585 ALA PHE LYS ASN THR ARG TYR PHE LEU GLN ILE ASP ILE 1POX 124 SEQRES 24 B 585 ASP PRO ALA LYS LEU GLY LYS ARG HIS LYS THR ASP ILE 1POX 125 SEQRES 25 B 585 ALA VAL LEU ALA ASP ALA GLN LYS THR LEU ALA ALA ILE 1POX 126 SEQRES 26 B 585 LEU ALA GLN VAL SER GLU ARG GLU SER THR PRO TRP TRP 1POX 127 SEQRES 27 B 585 GLN ALA ASN LEU ALA ASN VAL LYS ASN TRP ARG ALA TYR 1POX 128 SEQRES 28 B 585 LEU ALA SER LEU GLU ASP LYS GLN GLU GLY PRO LEU GLN 1POX 129 SEQRES 29 B 585 ALA TYR GLN VAL LEU ARG ALA VAL ASN LYS ILE ALA GLU 1POX 130 SEQRES 30 B 585 PRO ASP ALA ILE TYR SER ILE ASP VAL GLY ASP ILE ASN 1POX 131 SEQRES 31 B 585 LEU ASN ALA ASN ARG HIS LEU LYS LEU THR PRO SER ASN 1POX 132 SEQRES 32 B 585 ARG HIS ILE THR SER ASN LEU PHE ALA THR MET GLY VAL 1POX 133 SEQRES 33 B 585 GLY ILE PRO GLY ALA ILE ALA ALA LYS LEU ASN TYR PRO 1POX 134 SEQRES 34 B 585 GLU ARG GLN VAL PHE ASN LEU ALA GLY ASP GLY GLY ALA 1POX 135 SEQRES 35 B 585 SER MET THR MET GLN ASP LEU VAL THR GLN VAL GLN TYR 1POX 136 SEQRES 36 B 585 HIS LEU PRO VAL ILE ASN VAL VAL PHE THR ASN CYS GLN 1POX 137 SEQRES 37 B 585 TYR GLY PHE ILE LYS ASP GLU GLN GLU ASP THR ASN GLN 1POX 138 SEQRES 38 B 585 ASN ASP PHE ILE GLY VAL GLU PHE ASN ASP ILE ASP PHE 1POX 139 SEQRES 39 B 585 SER LYS ILE ALA ASP GLY VAL HIS MET GLN ALA PHE ARG 1POX 140 SEQRES 40 B 585 VAL ASN LYS ILE GLU GLN LEU PRO ASP VAL PHE GLU GLN 1POX 141 SEQRES 41 B 585 ALA LYS ALA ILE ALA GLN HIS GLU PRO VAL LEU ILE ASP 1POX 142 SEQRES 42 B 585 ALA VAL ILE THR GLY ASP ARG PRO LEU PRO ALA GLU LYS 1POX 143 SEQRES 43 B 585 LEU ARG LEU ASP SER ALA MET SER SER ALA ALA ASP ILE 1POX 144 SEQRES 44 B 585 GLU ALA PHE LYS GLN ARG TYR GLU ALA GLN ASP LEU GLN 1POX 145 SEQRES 45 B 585 PRO LEU SER THR TYR LEU LYS GLN PHE GLY LEU ASP ASP 1POX 146 FTNOTE 1 1POX 147 FTNOTE 1 THE NA+ ION IS LOCATED ON A CRYSTALLOGRAPHIC TWO-FOLD AXIS. 1POX 148 FTNOTE 2 1POX 149 FTNOTE 2 HOH 801 - 806 ARE LOCATED ON A CRYSTALLOGRAPHIC TWO-FOLD 1POX 150 FTNOTE 2 AXIS. 1POX 151 HET MG A 610 1 MAGNESIUM ++ 1POX 152 HET TPP A 611 26 THIAMIN DIPHOSPHATE 1POX 153 HET FAD A 612 53 FLAVIN-ADENINE DINUCLEOTIDE 1POX 154 HET GOL A 613 6 GLYCEROL 1POX 155 HET NA A 614 1 SODIUM +1 COUNTER ION 1POX 156 HET MG B 610 1 MAGNESIUM ++ 1POX 157 HET TPP B 611 26 THIAMIN DIPHOSPHATE 1POX 158 HET FAD B 612 53 FLAVIN-ADENINE DINUCLEOTIDE 1POX 159 HET GOL B 613 6 GLYCEROL 1POX 160 HET NA B 614 1 SODIUM +1 COUNTER ION 1POX 161 FORMUL 3 MG 2(MG1) 1POX 162 FORMUL 4 TPP 2(C12 H18 N4 O7 P2 S1) 1POX 163 FORMUL 5 FAD 2(C27 H33 N9 O15 P2) 1POX 164 FORMUL 6 GOL 2(C3 H8 O3) 1POX 165 FORMUL 7 NA 2(NA1 +) 1POX 166 FORMUL 8 HOH *739(H2 O1) 1POX 167 HELIX 1 A1 GLY A 14 GLY A 25 1 1POX 168 HELIX 2 A2 ILE A 37 SER A 45 1 1POX 169 HELIX 3 A3 GLU A 59 THR A 73 1 1POX 170 HELIX 4 A4 GLY A 84 HIS A 89 1 1POX 171 HELIX 5 A5 LEU A 90 HIS A 101 1 1POX 172 HELIX 6 A6 THR A 145 GLN A 161 1 1POX 173 HELIX 7 A7 ASP A 198 ALA A 212 1 1POX 174 HELIX 8 A8 ALA A 226 LYS A 238 1 1POX 175 HELIX 9 A9 LYS A 268 GLN A 276 1 1POX 176 HELIX 10 A10 ASP A 325 ALA A 335 1 1POX 177 HELIX 11 A11 THR A 343 ASP A 365 1 1POX 178 HELIX 12 A12 ALA A 373 ALA A 384 1 1POX 179 HELIX 13 A13 ASP A 396 LEU A 405 1 1POX 180 HELIX 14 A14 GLY A 425 TYR A 436 1 1POX 181 HELIX 15 A15 GLY A 446 MET A 454 1 1POX 182 HELIX 16 A16 VAL A 458 HIS A 464 1 1POX 183 HELIX 17 A17 TYR A 477 ASN A 488 1 1POX 184 HELIX 18 A18 ASP A 501 HIS A 510 1 1POX 185 HELIX 19 A19 LEU A 522 ALA A 533 1 1POX 186 HELIX 20 A20 SER A 563 GLU A 575 1 1POX 187 HELIX 21 A21 LEU A 582 GLY A 590 1 1POX 188 HELIX 22 B1 GLY B 14 GLY B 25 1 1POX 189 HELIX 23 B2 ILE B 37 SER B 45 1 1POX 190 HELIX 24 B3 GLU B 59 THR B 73 1 1POX 191 HELIX 25 B4 GLY B 84 HIS B 89 1 1POX 192 HELIX 26 B5 LEU B 90 HIS B 101 1 1POX 193 HELIX 27 B6 THR B 145 GLN B 161 1 1POX 194 HELIX 28 B7 ASP B 198 ALA B 212 1 1POX 195 HELIX 29 B8 ALA B 226 LYS B 238 1 1POX 196 HELIX 30 B9 LYS B 268 GLN B 276 1 1POX 197 HELIX 31 B10 ASP B 325 ALA B 335 1 1POX 198 HELIX 32 B11 THR B 343 ASP B 365 1 1POX 199 HELIX 33 B12 ALA B 373 ALA B 384 1 1POX 200 HELIX 34 B13 ASP B 396 LEU B 405 1 1POX 201 HELIX 35 B14 GLY B 425 TYR B 436 1 1POX 202 HELIX 36 B15 GLY B 446 MET B 454 1 1POX 203 HELIX 37 B16 VAL B 458 HIS B 464 1 1POX 204 HELIX 38 B17 TYR B 477 ASN B 488 1 1POX 205 HELIX 39 B18 ASP B 501 HIS B 510 1 1POX 206 HELIX 40 B19 LEU B 522 ALA B 533 1 1POX 207 HELIX 41 B20 SER B 563 GLU B 575 1 1POX 208 HELIX 42 B21 LEU B 582 GLY B 590 1 1POX 209 SHEET 1 A0 2 THR A 9 ALA A 13 0 1POX 210 SHEET 2 A0 2 GLN A 175 ALA A 179 -1 O GLN A 175 N ALA A 13 1POX 211 SHEET 1 A1 6 HIS A 52 VAL A 56 0 1POX 212 SHEET 2 A1 6 ASP A 27 GLY A 31 1 O ASP A 27 N HIS A 52 1POX 213 SHEET 3 A1 6 GLY A 77 GLY A 81 1 O VAL A 78 N TYR A 30 1POX 214 SHEET 4 A1 6 PRO A 103 GLN A 110 1 O PRO A 103 N GLY A 77 1POX 215 SHEET 5 A1 6 GLY A 162 VAL A 170 1 O GLY A 162 N VAL A 104 1POX 216 SHEET 6 A1 6 TYR A 136 ALA A 140 1 N TYR A 136 O VAL A 163 1POX 217 SHEET 1 A2 6 ALA A 257 GLY A 260 0 1POX 218 SHEET 2 A2 6 PRO A 240 THR A 244 1 N LEU A 241 O ALA A 257 1POX 219 SHEET 3 A2 6 LEU A 216 GLY A 220 1 N ILE A 217 O PRO A 240 1POX 220 SHEET 4 A2 6 ASP A 278 GLY A 284 1 O VAL A 279 N LEU A 216 1POX 221 SHEET 5 A2 6 TYR A 301 ASP A 306 1 N TYR A 301 O ASP A 278 1POX 222 SHEET 6 A2 6 ILE A 320 ALA A 324 1 O ILE A 320 N GLN A 304 1POX 223 SHEET 1 A3 6 ARG A 412 ILE A 414 0 1POX 224 SHEET 2 A3 6 ALA A 388 ASP A 393 1 O ALA A 388 N ARG A 412 1POX 225 SHEET 3 A3 6 GLN A 440 ALA A 445 1 O GLN A 440 N ILE A 389 1POX 226 SHEET 4 A3 6 VAL A 467 THR A 473 1 N ILE A 468 O VAL A 441 1POX 227 SHEET 5 A3 6 VAL A 538 ILE A 544 1 N VAL A 538 O VAL A 467 1POX 228 SHEET 6 A3 6 GLN A 512 VAL A 516 1 O GLN A 512 N LEU A 539 1POX 229 SHEET 1 B0 2 THR B 9 ALA B 13 0 1POX 230 SHEET 2 B0 2 GLN B 175 ALA B 179 -1 O GLN B 175 N ALA B 13 1POX 231 SHEET 1 B1 6 HIS B 52 VAL B 56 0 1POX 232 SHEET 2 B1 6 ASP B 27 GLY B 31 1 O ASP B 27 N HIS B 52 1POX 233 SHEET 3 B1 6 GLY B 77 GLY B 81 1 O VAL B 78 N TYR B 30 1POX 234 SHEET 4 B1 6 PRO B 103 GLN B 110 1 O PRO B 103 N GLY B 77 1POX 235 SHEET 5 B1 6 GLY B 162 VAL B 170 1 O GLY B 162 N VAL B 104 1POX 236 SHEET 6 B1 6 TYR B 136 ALA B 140 1 N TYR B 136 O VAL B 163 1POX 237 SHEET 1 B2 6 ALA B 257 GLY B 260 0 1POX 238 SHEET 2 B2 6 PRO B 240 THR B 244 1 N LEU B 241 O ALA B 257 1POX 239 SHEET 3 B2 6 LEU B 216 GLY B 220 1 N ILE B 217 O PRO B 240 1POX 240 SHEET 4 B2 6 ASP B 278 GLY B 284 1 O VAL B 279 N LEU B 216 1POX 241 SHEET 5 B2 6 TYR B 301 ASP B 306 1 N TYR B 301 O ASP B 278 1POX 242 SHEET 6 B2 6 ILE B 320 ALA B 324 1 O ILE B 320 N GLN B 304 1POX 243 SHEET 1 B3 6 ARG B 412 ILE B 414 0 1POX 244 SHEET 2 B3 6 ALA B 388 ASP B 393 1 O ALA B 388 N ARG B 412 1POX 245 SHEET 3 B3 6 GLN B 440 ALA B 445 1 O GLN B 440 N ILE B 389 1POX 246 SHEET 4 B3 6 VAL B 467 THR B 473 1 N ILE B 468 O VAL B 441 1POX 247 SHEET 5 B3 6 VAL B 538 ILE B 544 1 N VAL B 538 O VAL B 467 1POX 248 SHEET 6 B3 6 GLN B 512 VAL B 516 1 O GLN B 512 N LEU B 539 1POX 249 CRYST1 121.600 155.400 167.100 90.00 90.00 90.00 C 2 2 21 16 1POX 250 ORIGX1 1.000000 0.000000 0.000000 0.00000 1POX 251 ORIGX2 0.000000 1.000000 0.000000 0.00000 1POX 252 ORIGX3 0.000000 0.000000 1.000000 0.00000 1POX 253 SCALE1 0.008224 0.000000 0.000000 0.00000 1POX 254 SCALE2 0.000000 0.006435 0.000000 0.00000 1POX 255 SCALE3 0.000000 0.000000 0.005984 0.00000 1POX 256 MTRIX1 1 -0.999948 0.008221 -0.006109 -9.91500 1 1POX 257 MTRIX2 1 -0.001108 -0.679808 -0.733389 130.53011 1 1POX 258 MTRIX3 1 -0.010182 -0.733344 0.679782 56.62200 1 1POX 259