HEADER TRANSFERASE(PHOSPHOTRANSFERASE) 25-JAN-88 1PFK 1PFK 3 COMPND PHOSPHOFRUCTOKINASE (E.C.2.7.1.11) (R-STATE) COMPLEX WITH 1PFK 4 COMPND 2 FRUCTOSE-1,6-BISPHOSPHATE AND /ADP$(SLASH)*MG++ 1PFK 5 SOURCE (ESCHERICHIA $COLI) 1PFK 6 AUTHOR Y.SHIRAKIHARA,P.R.EVANS 1PFK 7 REVDAT 4 15-OCT-92 1PFKC 1 SEQRES 1PFKC 1 REVDAT 3 15-JUL-90 1PFKB 1 REMARK 1PFKB 1 REVDAT 2 19-APR-89 1PFKA 1 JRNL 1PFKA 1 REVDAT 1 09-JAN-89 1PFK 0 1PFK 8 JRNL AUTH Y.SHIRAKIHARA,P.R.EVANS 1PFK 9 JRNL TITL CRYSTAL STRUCTURE OF THE COMPLEX OF 1PFK 10 JRNL TITL 2 PHOSPHOFRUCTOKINASE FROM ESCHERICHIA $COLI WITH ITS 1PFK 11 JRNL TITL 3 REACTION PRODUCTS 1PFK 12 JRNL REF J.MOL.BIOL. V. 204 973 1988 1PFKA 2 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 1PFKA 3 REMARK 1 1PFK 15 REMARK 1 REFERENCE 1 1PFKB 2 REMARK 1 AUTH W.R.RYPNIEWSKI,P.R.EVANS 1PFKB 3 REMARK 1 TITL CRYSTAL STRUCTURE OF UNLIGANDED PHOSPHOFRUCTOKINASE 1PFKB 4 REMARK 1 TITL 2 FROM ESCHERICHIA $COLI 1PFKB 5 REMARK 1 REF J.MOL.BIOL. V. 207 805 1989 1PFKB 6 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1PFKB 7 REMARK 1 REFERENCE 2 1PFKB 8 REMARK 1 AUTH P.R.EVANS,G.W.FARRANTS,M.C.LAWRENCE 1PFK 17 REMARK 1 TITL CRYSTALLOGRAPHIC STRUCTURE OF ALLOSTERICALLY 1PFK 18 REMARK 1 TITL 2 INHIBITED PHOSPHOFRUCTOKINASE AT 7 ANGSTROMS 1PFK 19 REMARK 1 TITL 3 RESOLUTION 1PFK 20 REMARK 1 REF J.MOL.BIOL. V. 191 713 1986 1PFK 21 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1PFK 22 REMARK 1 REFERENCE 3 1PFKB 9 REMARK 1 AUTH H.W.HELLINGA,P.R.EVANS 1PFK 24 REMARK 1 TITL NUCLEOTIDE SEQUENCE AND HIGH-LEVEL EXPRESSION OF 1PFK 25 REMARK 1 TITL 2 THE MAJOR ESCHERICHIA $COLI PHOSPHOFRUCTOKINASE 1PFK 26 REMARK 1 REF EUR.J.BIOCHEM. V. 149 363 1985 1PFK 27 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 262 1PFK 28 REMARK 1 REFERENCE 4 1PFKB 10 REMARK 1 AUTH P.R.EVANS,G.W.FARRANTS,P.J.HUDSON 1PFK 30 REMARK 1 TITL PHOSPHOFRUCTOKINASE. STRUCTURE AND CONTROL 1PFK 31 REMARK 1 REF PHILOS.TRANS.R.SOC.LONDON, V. 293 53 1981 1PFK 32 REMARK 1 REF 2 SER.B 1PFK 33 REMARK 1 REFN ASTM PTRBAE UK ISSN 0080-4622 441 1PFK 34 REMARK 1 REFERENCE 5 1PFKB 11 REMARK 1 AUTH P.R.EVANS,P.J.HUDSON 1PFK 36 REMARK 1 TITL STRUCTURE AND CONTROL OF PHOSPHOFRUCTOKINASE FROM 1PFK 37 REMARK 1 TITL 2 BACILLUS $STEAROTHERMOPHILUS 1PFK 38 REMARK 1 REF NATURE V. 279 500 1979 1PFK 39 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 1PFK 40 REMARK 1 REFERENCE 6 1PFKB 12 REMARK 1 AUTH P.R.EVANS,P.J.HUDSON 1PFK 42 REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF 1PFK 43 REMARK 1 TITL 2 PHOSPHOFRUCTOKINASE FROM BACILLUS 1PFK 44 REMARK 1 TITL 3 STEAROTHERMOPHILUS 1PFK 45 REMARK 1 REF PROC./FEBS$ MEET. V. 52 349 1978 1PFK 46 REMARK 1 REFN ASTM FEBPBY UK ISSN 0071-4402 924 1PFK 47 REMARK 2 1PFK 48 REMARK 2 RESOLUTION. 2.4 ANGSTROMS. 1PFK 49 REMARK 3 1PFK 50 REMARK 3 REFINEMENT. BY THE RESTRAINED LEAST SQUARES PROCEDURE OF J. 1PFK 51 REMARK 3 KONNERT AND W. HENDRICKSON (PROGRAM *PROLSQ*) WITH THE 1PFK 52 REMARK 3 X-RAY CONTRIBUTION CALCULATED BY THE METHOD OF A. JACK 1PFK 53 REMARK 3 (PROGRAM *DERIV*). THE R VALUE IS 0.165 FOR ALL DATA 1PFK 54 REMARK 3 IN THE RESOLUTION RANGE 100 TO 2.4 ANGSTROMS INCLUDING A 1PFK 55 REMARK 3 BULK SOLVENT CONTRIBUTION. THE RMS DEVIATION FROM 1PFK 56 REMARK 3 IDEALITY OF THE BOND LENGTHS IS 0.008 ANGSTOMS. THE RMS 1PFK 57 REMARK 3 DEVIATION FROM IDEALITY OF THE BOND ANGLE DISTANCES IS 1PFK 58 REMARK 3 0.03 ANGSTROMS. 1PFK 59 REMARK 4 1PFK 60 REMARK 4 THIS CRYSTAL STRUCTURE REPRESENTS THE ACTIVE (R-STATE) 1PFK 61 REMARK 4 CONFORMATION OF E. COLI PFK. THE CRYSTALS WERE GROWN WITH 1PFK 62 REMARK 4 FRUCTOSE-6-PHOSPHATE AND ADP/MG++, BUT A SUBSTANTIAL 1PFK 63 REMARK 4 PROPORTION OF THE REACTION PRODUCT 1PFK 64 REMARK 4 FRUCTOSE-1,6-BISPHOSPHATE IS OBSERVED IN THE STRUCTURE. 1PFK 65 REMARK 4 THE 1-PHOSPHATE GROUP HAS BEEN ASSIGNED AN OCCUPANCY OF 1PFK 66 REMARK 4 0.5 IN THIS ENTRY BUT THIS IS VERY APPROXIMATE. 1PFK 67 REMARK 5 1PFK 68 REMARK 5 ADP A 324 AND ADP B 324 ARE THE PRODUCTS OF THE CATALYTIC 1PFK 69 REMARK 5 REACTION ATP + F6P --> ADP + F-1,6-DP. ADP A 326 AND 1PFK 70 REMARK 5 ADP B 326 ARE THE ALLOSTERIC ACTIVATORS. 1PFK 71 REMARK 6 1PFK 72 REMARK 6 THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT CONTAINS TWO SUBUNITS 1PFK 73 REMARK 6 OF THE TETRAMER. THESE SUBUNITS HAVE BEEN ASSIGNED CHAIN 1PFK 74 REMARK 6 IDENTIFIERS *A* AND *B* AND HAVE DIFFERENT CONFORMATIONS. 1PFK 75 REMARK 6 CHAIN A IS A *CLOSED* SUBUNIT WITH THE MG++ ION BRIDGING 1PFK 76 REMARK 6 THE TWO PRODUCTS. CHAIN B IS AN *OPEN* SUBUNIT WITH THE 1PFK 77 REMARK 6 MG++ BOUND TO ADP ONLY. THERE ARE TWO WATER CHAINS, ONE 1PFK 78 REMARK 6 CORRESPONDING TO EACH SUBUNIT, AND EQUIVALENT WATER 1PFK 79 REMARK 6 MOLECULES IN EACH CHAIN HAVE BEEN ASSIGNED THE SAME RESIDUE 1PFK 80 REMARK 6 NUMBER. THE TETRAMER CAN BE COMPLETED FROM THE DIMER IN 1PFK 81 REMARK 6 THIS ENTRY BY ROTATING 180 DEGREES ABOUT Z 1PFK 82 REMARK 6 (I.E. -X, -Y, Z). THE STORED ORTHOGONAL CRYSTALLOGRAPHIC 1PFK 83 REMARK 6 COORDINATES IN THIS ENTRY MAY BE CONVERTED TO THE MOLECULAR 1PFK 84 REMARK 6 PQR FRAME (WITH THE MOLECULAR DIADS ALONG P,Q,R) BY THE 1PFK 85 REMARK 6 TRANSFORMATION 1PFK 86 REMARK 6 0.87831 0.47808 0.00000 0.00000 1PFK 87 REMARK 6 0.00000 0.00000 -1.00000 -2.71300 1PFKB 13 REMARK 6 -0.47808 0.87831 0.00000 0.00000 1PFKB 14 REMARK 7 1PFK 90 REMARK 7 THE SIDE CHAINS OF RESIDUES LYS A 214, LYS A 236, 1PFK 91 REMARK 7 LYS B 236, AND LYS B 304 ARE DISORDERED AND HAVE BEEN 1PFK 92 REMARK 7 OMITTED. 1PFK 93 REMARK 8 1PFK 94 REMARK 8 THE TRANSFORMATION SPECIFIED ON THE *MTRIX* RECORDS BELOW 1PFK 95 REMARK 8 WILL YIELD APPROXIMATE COORDINATES FOR THE B CHAIN WHEN 1PFK 96 REMARK 8 APPLIED TO THE A CHAIN. IT WILL ALSO YIELD APPROXIMATE 1PFK 97 REMARK 8 COORDINATES FOR THE A CHAIN WHEN APPLIED TO THE B CHAIN. 1PFK 98 REMARK 9 1PFK 99 REMARK 9 COORDINATES FOR OTHER FORMS OF PHOSPHOFRUCTOKINASE ARE 1PFK 100 REMARK 9 AVAILABLE FROM THE PROTEIN DATA BANK AS SEPARATE ENTRIES. 1PFK 101 REMARK 10 1PFK 102 REMARK 10 STRUCTURE FACTORS CORRESPONDING TO THIS ENTRY ARE AVAILABLE 1PFK 103 REMARK 10 FROM THE PROTEIN DATA BANK AS A SEPARATE ENTRY. 1PFK 104 REMARK 11 1PFKA 4 REMARK 11 CORRECTION. UPDATE JRNL REFERENCE TO REFLECT PUBLICATION. 1PFKA 5 REMARK 11 19-APR-89. 1PFKA 6 REMARK 12 1PFKB 15 REMARK 12 CORRECTION. CORRECT TRANSFORMATION PRESENTED IN REMARK 6. 1PFKB 16 REMARK 12 INSERT NEW PUBLICATION AS REFERENCE 1 AND RENUMBER THE 1PFKB 17 REMARK 12 OTHERS. 15-JUL-90. 1PFKB 18 REMARK 13 1PFKC 2 REMARK 13 CORRECTION. CORRECT TWO RESIDUES IN EACH CHAIN ON THE 1PFKC 3 REMARK 13 SEQRES RECORDS. 15-OCT-92. 1PFKC 4 SEQRES 1 A 320 MET ILE LYS LYS ILE GLY VAL LEU THR SER GLY GLY ASP 1PFK 105 SEQRES 2 A 320 ALA PRO GLY MET ASN ALA ALA ILE ARG GLY VAL VAL ARG 1PFK 106 SEQRES 3 A 320 SER ALA LEU THR GLU GLY LEU GLU VAL MET GLY ILE TYR 1PFK 107 SEQRES 4 A 320 ASP GLY TYR LEU GLY LEU TYR GLU ASP ARG MET VAL GLN 1PFK 108 SEQRES 5 A 320 LEU ASP ARG TYR SER VAL SER ASP MET ILE ASN ARG GLY 1PFK 109 SEQRES 6 A 320 GLY THR PHE LEU GLY SER ALA ARG PHE PRO GLU PHE ARG 1PFK 110 SEQRES 7 A 320 ASP GLU ASN ILE ARG ALA VAL ALA ILE GLU ASN LEU LYS 1PFK 111 SEQRES 8 A 320 LYS ARG GLY ILE ASP ALA LEU VAL VAL ILE GLY GLY ASP 1PFK 112 SEQRES 9 A 320 GLY SER TYR MET GLY ALA MET ARG LEU THR GLU MET GLY 1PFK 113 SEQRES 10 A 320 PHE PRO CYS ILE GLY LEU PRO GLY THR ILE ASP ASN ASP 1PFK 114 SEQRES 11 A 320 ILE LYS GLY THR ASP TYR THR ILE GLY PHE PHE THR ALA 1PFK 115 SEQRES 12 A 320 LEU SER THR VAL VAL GLU ALA ILE ASP ARG LEU ARG ASP 1PFKC 5 SEQRES 13 A 320 THR SER SER SER HIS GLN ARG ILE SER VAL VAL GLU VAL 1PFK 117 SEQRES 14 A 320 MET GLY ARG TYR CYS GLY ASP LEU THR LEU ALA ALA ALA 1PFK 118 SEQRES 15 A 320 ILE ALA GLY GLY CYS GLU PHE VAL VAL VAL PRO GLU VAL 1PFK 119 SEQRES 16 A 320 GLU PHE SER ARG GLU ASP LEU VAL ASN GLU ILE LYS ALA 1PFK 120 SEQRES 17 A 320 GLY ILE ALA LYS GLY LYS LYS HIS ALA ILE VAL ALA ILE 1PFK 121 SEQRES 18 A 320 THR GLU HIS MET CYS ASP VAL ASP GLU LEU ALA HIS PHE 1PFK 122 SEQRES 19 A 320 ILE GLU LYS GLU THR GLY ARG GLU THR ARG ALA THR VAL 1PFK 123 SEQRES 20 A 320 LEU GLY HIS ILE GLN ARG GLY GLY SER PRO VAL PRO TYR 1PFK 124 SEQRES 21 A 320 ASP ARG ILE LEU ALA SER ARG MET GLY ALA TYR ALA ILE 1PFK 125 SEQRES 22 A 320 ASP LEU LEU LEU ALA GLY TYR GLY GLY ARG CYS VAL GLY 1PFK 126 SEQRES 23 A 320 ILE GLN ASN GLU GLN LEU VAL HIS HIS ASP ILE ILE ASP 1PFK 127 SEQRES 24 A 320 ALA ILE GLU ASN MET LYS ARG PRO PHE LYS GLY ASP TRP 1PFK 128 SEQRES 25 A 320 LEU ASP CYS ALA LYS LYS LEU TYR 1PFK 129 SEQRES 1 B 320 MET ILE LYS LYS ILE GLY VAL LEU THR SER GLY GLY ASP 1PFK 130 SEQRES 2 B 320 ALA PRO GLY MET ASN ALA ALA ILE ARG GLY VAL VAL ARG 1PFK 131 SEQRES 3 B 320 SER ALA LEU THR GLU GLY LEU GLU VAL MET GLY ILE TYR 1PFK 132 SEQRES 4 B 320 ASP GLY TYR LEU GLY LEU TYR GLU ASP ARG MET VAL GLN 1PFK 133 SEQRES 5 B 320 LEU ASP ARG TYR SER VAL SER ASP MET ILE ASN ARG GLY 1PFK 134 SEQRES 6 B 320 GLY THR PHE LEU GLY SER ALA ARG PHE PRO GLU PHE ARG 1PFK 135 SEQRES 7 B 320 ASP GLU ASN ILE ARG ALA VAL ALA ILE GLU ASN LEU LYS 1PFK 136 SEQRES 8 B 320 LYS ARG GLY ILE ASP ALA LEU VAL VAL ILE GLY GLY ASP 1PFK 137 SEQRES 9 B 320 GLY SER TYR MET GLY ALA MET ARG LEU THR GLU MET GLY 1PFK 138 SEQRES 10 B 320 PHE PRO CYS ILE GLY LEU PRO GLY THR ILE ASP ASN ASP 1PFK 139 SEQRES 11 B 320 ILE LYS GLY THR ASP TYR THR ILE GLY PHE PHE THR ALA 1PFK 140 SEQRES 12 B 320 LEU SER THR VAL VAL GLU ALA ILE ASP ARG LEU ARG ASP 1PFKC 6 SEQRES 13 B 320 THR SER SER SER HIS GLN ARG ILE SER VAL VAL GLU VAL 1PFK 142 SEQRES 14 B 320 MET GLY ARG TYR CYS GLY ASP LEU THR LEU ALA ALA ALA 1PFK 143 SEQRES 15 B 320 ILE ALA GLY GLY CYS GLU PHE VAL VAL VAL PRO GLU VAL 1PFK 144 SEQRES 16 B 320 GLU PHE SER ARG GLU ASP LEU VAL ASN GLU ILE LYS ALA 1PFK 145 SEQRES 17 B 320 GLY ILE ALA LYS GLY LYS LYS HIS ALA ILE VAL ALA ILE 1PFK 146 SEQRES 18 B 320 THR GLU HIS MET CYS ASP VAL ASP GLU LEU ALA HIS PHE 1PFK 147 SEQRES 19 B 320 ILE GLU LYS GLU THR GLY ARG GLU THR ARG ALA THR VAL 1PFK 148 SEQRES 20 B 320 LEU GLY HIS ILE GLN ARG GLY GLY SER PRO VAL PRO TYR 1PFK 149 SEQRES 21 B 320 ASP ARG ILE LEU ALA SER ARG MET GLY ALA TYR ALA ILE 1PFK 150 SEQRES 22 B 320 ASP LEU LEU LEU ALA GLY TYR GLY GLY ARG CYS VAL GLY 1PFK 151 SEQRES 23 B 320 ILE GLN ASN GLU GLN LEU VAL HIS HIS ASP ILE ILE ASP 1PFK 152 SEQRES 24 B 320 ALA ILE GLU ASN MET LYS ARG PRO PHE LYS GLY ASP TRP 1PFK 153 SEQRES 25 B 320 LEU ASP CYS ALA LYS LYS LEU TYR 1PFK 154 HET FBP A 323 20 FRUCTOSE-1,6-BISPHOSPHATE 1PFK 155 HET ADP A 324 27 ADENOSINE DIPHOSPHATE 1PFK 156 HET MG A 325 1 MAGNESIUM (II) ION 1PFK 157 HET ADP A 326 27 ADENOSINE DIPHOSPHATE 1PFK 158 HET MG A 327 1 MAGNESIUM (II) ION 1PFK 159 HET FBP B 323 20 FRUCTOSE-1,6-BISPHOSPHATE 1PFK 160 HET ADP B 324 27 ADENOSINE DIPHOSPHATE 1PFK 161 HET MG B 325 1 MAGNESIUM (II) ION 1PFK 162 HET ADP B 326 27 ADENOSINE DIPHOSPHATE 1PFK 163 HET MG B 327 1 MAGNESIUM (II) ION 1PFK 164 FORMUL 3 FBP 2(C6 H14 O12 P2) 1PFK 165 FORMUL 4 ADP 4(C10 H15 N5 O10 P2) 1PFK 166 FORMUL 5 MG 4(MG1 ++) 1PFK 167 FORMUL 6 HOH *277(H2 O1) 1PFK 168 HELIX 1 1A GLY A 15 GLU A 30 1 3/10 END 1PFK 169 HELIX 2 2A GLY A 40 ASP A 47 1 3/10 BEGINNING AND END 1PFK 170 HELIX 3 4AA PHE A 73 ASP A 78 5 1PFK 171 HELIX 4 4A ASP A 78 GLY A 93 1 3/10 END 1PFK 172 HELIX 5 5A GLY A 102 GLY A 116 1 1PFK 173 HELIX 6 6A GLY A 138 HIS A 160 1 1PFK 174 HELIX 7 7A THR A 177 GLY A 185 1 1PFK 175 HELIX 8 8A SER A 197 GLY A 212 1 3/10 BEGINNING AND END 1PFK 176 HELIX 9 9A ASP A 226 GLY A 239 1 1PFK 177 HELIX 10 10A GLY A 248 ARG A 252 5 1PFK 178 HELIX 11 11A VAL A 257 GLY A 278 1 3/10 END 1PFK 179 HELIX 12 12A ASP A 295 ASN A 302 1 1PFK 180 HELIX 13 13A LYS A 308 TYR A 319 1 1PFK 181 HELIX 14 1B GLY B 15 GLU B 30 1 3/10 END 1PFK 182 HELIX 15 2B GLY B 40 ASP B 47 1 3/10 BEGINNING AND END 1PFK 183 HELIX 16 4AB PHE B 73 ASP B 78 5 1PFK 184 HELIX 17 4B ASP B 78 GLY B 93 1 3/10 END 1PFK 185 HELIX 18 5B GLY B 102 GLY B 116 1 1PFK 186 HELIX 19 6B GLY B 138 HIS B 160 1 1PFK 187 HELIX 20 7B THR B 177 GLY B 185 1 1PFK 188 HELIX 21 8B SER B 197 GLY B 212 1 3/10 BEGINNING AND END 1PFK 189 HELIX 22 9B ASP B 226 GLY B 239 1 1PFK 190 HELIX 23 10B GLY B 248 ARG B 252 5 1PFK 191 HELIX 24 11B VAL B 257 GLY B 278 1 3/10 END 1PFK 192 HELIX 25 12B ASP B 295 ASN B 302 1 1PFK 193 HELIX 26 13B LYS B 308 TYR B 319 1 1PFK 194 SHEET 1 S1A 7 ARG A 48 LEU A 52 0 1PFK 195 SHEET 2 S1A 7 GLU A 33 TYR A 38 -1 O GLY A 36 N VAL A 50 1PFK 196 SHEET 3 S1A 7 LYS A 2 SER A 9 1 O VAL A 6 N ILE A 37 1PFK 197 SHEET 4 S1A 7 ALA A 96 GLY A 101 1 O VAL A 98 N LEU A 7 1PFK 198 SHEET 5 S1A 7 PRO A 118 LEU A 122 1 O ILE A 120 N VAL A 99 1PFK 199 SHEET 6 S1A 7 GLY A 281 GLN A 287 1 O ARG A 282 N GLY A 121 1PFK 200 SHEET 7 S1A 7 GLN A 290 ASP A 295 -1 O HIS A 294 N CYS A 283 1PFK 201 SHEET 1 S2A 4 PHE A 188 VAL A 190 0 1PFK 202 SHEET 2 S2A 4 ALA A 216 THR A 221 1 O ALA A 219 N VAL A 190 1PFK 203 SHEET 3 S2A 4 ARG A 162 VAL A 168 1 O VAL A 166 N ILE A 220 1PFK 204 SHEET 4 S2A 4 GLU A 241 LEU A 247 1 O THR A 245 N GLU A 167 1PFK 205 SHEET 1 S1B 7 ARG B 48 LEU B 52 0 1PFK 206 SHEET 2 S1B 7 GLU B 33 TYR B 38 -1 O GLY B 36 N VAL B 50 1PFK 207 SHEET 3 S1B 7 LYS B 2 SER B 9 1 O VAL B 6 N ILE B 37 1PFK 208 SHEET 4 S1B 7 ALA B 96 GLY B 101 1 O VAL B 98 N LEU B 7 1PFK 209 SHEET 5 S1B 7 PRO B 118 LEU B 122 1 O ILE B 120 N VAL B 99 1PFK 210 SHEET 6 S1B 7 GLY B 281 GLN B 287 1 O ARG B 282 N GLY B 121 1PFK 211 SHEET 7 S1B 7 GLN B 290 ASP B 295 -1 O HIS B 294 N CYS B 283 1PFK 212 SHEET 1 S2B 4 PHE B 188 VAL B 190 0 1PFK 213 SHEET 2 S2B 4 ALA B 216 THR B 221 1 O ALA B 219 N VAL B 190 1PFK 214 SHEET 3 S2B 4 ARG B 162 VAL B 168 1 O VAL B 166 N ILE B 220 1PFK 215 SHEET 4 S2B 4 GLU B 241 LEU B 247 1 O THR B 245 N GLU B 167 1PFK 216 CRYST1 112.300 85.400 77.100 90.00 90.00 90.00 P 21 21 2 8 1PFK 217 ORIGX1 1.000000 0.000000 0.000000 0.00000 1PFK 218 ORIGX2 0.000000 1.000000 0.000000 0.00000 1PFK 219 ORIGX3 0.000000 0.000000 1.000000 0.00000 1PFK 220 SCALE1 0.008905 0.000000 0.000000 0.00000 1PFK 221 SCALE2 0.000000 0.011710 0.000000 0.00000 1PFK 222 SCALE3 0.000000 0.000000 0.012970 0.00000 1PFK 223 MTRIX1 1 0.542870 0.839820 0.000000 0.00000 1 1PFK 224 MTRIX2 1 0.839820 -0.542870 0.000000 0.00000 1 1PFK 225 MTRIX3 1 0.000000 0.000000 -1.000000 -5.42690 1 1PFK 226