HEADER TRANSFERASE(KETONE RESIDUES) 22-NOV-93 1TRK 1TRK 2 COMPND TRANSKETOLASE (E.C.2.2.1.1) 1TRK 3 SOURCE BAKER'S YEAST (SACCHAROMYCES CEREVISIAE) 1TRK 4 AUTHOR Y.LINDQVIST,G.SCHNEIDER,M.NIKKOLA 1TRK 5 REVDAT 1 30-APR-94 1TRK 0 1TRK 6 JRNL AUTH M.NIKKOLA,Y.LINDQVIST,G.SCHNEIDER 1TRK 7 JRNL TITL REFINED STRUCTURE OF TRANSKETOLASE FROM 1TRK 8 JRNL TITL 2 SACCHAROMYCES CEREVISIAE AT 2.0 ANGSTROMS 1TRK 9 JRNL TITL 3 RESOLUTION 1TRK 10 JRNL REF TO BE PUBLISHED 1TRK 11 JRNL REFN 353 1TRK 12 REMARK 1 1TRK 13 REMARK 1 REFERENCE 1 1TRK 14 REMARK 1 AUTH M.SUNDSTROM,Y.LINDQVIST,G.SCHNEIDER,U.HELLMAN, 1TRK 15 REMARK 1 AUTH 2 H.RONNE 1TRK 16 REMARK 1 TITL YEAST TKL1 GENE ENCODES A TRANSKETOLASE THAT IS 1TRK 17 REMARK 1 TITL 2 REQUIRED FOR EFFICIENT GLYCOLYSIS AND BIOSYNTHESIS 1TRK 18 REMARK 1 TITL 3 OF AROMATIC AMINO ACIDS 1TRK 19 REMARK 1 REF J.BIOL.CHEM. V. 268 24346 1993 1TRK 20 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 1TRK 21 REMARK 1 REFERENCE 2 1TRK 22 REMARK 1 AUTH Y.LINDQVIST,G.SCHNEIDER,U.ERMLER,M.SUNDSTROM 1TRK 23 REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF TRANSKETOLASE, A 1TRK 24 REMARK 1 TITL 2 THIAMINE DIPHOSPHATE DEPENDENT ENZYME AT 2.5 1TRK 25 REMARK 1 TITL 3 ANGSTROMS RESOLUTION 1TRK 26 REMARK 1 REF /EMBO$ J. V. 11 2373 1992 1TRK 27 REMARK 1 REFN ASTM EMJODG UK ISSN 0261-4189 897 1TRK 28 REMARK 1 REFERENCE 3 1TRK 29 REMARK 1 AUTH G.SCHNEIDER,M.SUNDSTROM,Y.LINDQVIST 1TRK 30 REMARK 1 TITL PRELIMINARY CRYSTALLOGRAPHIC DATA FOR 1TRK 31 REMARK 1 TITL 2 TRANSKETOLASE FROM YEAST 1TRK 32 REMARK 1 REF J.BIOL.CHEM. V. 264 21619 1989 1TRK 33 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 1TRK 34 REMARK 2 1TRK 35 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. 1TRK 36 REMARK 3 1TRK 37 REMARK 3 REFINEMENT. 1TRK 38 REMARK 3 PROGRAM X-PLOR 1TRK 39 REMARK 3 AUTHORS BRUNGER 1TRK 40 REMARK 3 R VALUE 0.157 1TRK 41 REMARK 3 RMSD BOND DISTANCES 0.017 ANGSTROMS 1TRK 42 REMARK 3 RMSD BOND ANGLES 3.1 DEGREES 1TRK 43 REMARK 4 1TRK 44 REMARK 4 SEQUENCE ADVISORY NOTICE: 1TRK 45 REMARK 4 THERE ARE NUMEROUS DIFFERENCES BETWEEN THE SEQUENCE GIVEN 1TRK 46 REMARK 4 IN SWISSPROT ENTRY TKT1_YEAST AND THE SEQUENCE USED IN 1TRK 47 REMARK 4 THIS ENTRY, PROBABLY DUE TO FRAME SHIFTS. SEE THE PAPER 1TRK 48 REMARK 4 CITED AS REFERENCE 1 ABOVE. 1TRK 49 REMARK 5 1TRK 50 REMARK 5 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL 1TRK 51 REMARK 5 YIELD APPROXIMATE COORDINATES FOR CHAIN B WHEN APPLIED TO 1TRK 52 REMARK 5 CHAIN A. 1TRK 53 SEQRES 1 A 680 MET THR GLN PHE THR ASP ILE ASP LYS LEU ALA VAL SER 1TRK 54 SEQRES 2 A 680 THR ILE ARG ILE LEU ALA VAL ASP THR VAL SER LYS ALA 1TRK 55 SEQRES 3 A 680 ASN SER GLY HIS PRO GLY ALA PRO LEU GLY MET ALA PRO 1TRK 56 SEQRES 4 A 680 ALA ALA HIS VAL LEU TRP SER GLN MET ARG MET ASN PRO 1TRK 57 SEQRES 5 A 680 THR ASN PRO ASP TRP ILE ASN ARG ASP ARG PHE VAL LEU 1TRK 58 SEQRES 6 A 680 SER ASN GLY HIS ALA VAL ALA LEU LEU TYR SER MET LEU 1TRK 59 SEQRES 7 A 680 HIS LEU THR GLY TYR ASP LEU SER ILE GLU ASP LEU LYS 1TRK 60 SEQRES 8 A 680 GLN PHE ARG GLN LEU GLY SER ARG THR PRO GLY HIS PRO 1TRK 61 SEQRES 9 A 680 GLU PHE GLU LEU PRO GLY VAL GLU VAL THR THR GLY PRO 1TRK 62 SEQRES 10 A 680 LEU GLY GLN GLY ILE SER ASN ALA VAL GLY MET ALA MET 1TRK 63 SEQRES 11 A 680 ALA GLN ALA ASN LEU ALA ALA THR TYR ASN LYS PRO GLY 1TRK 64 SEQRES 12 A 680 PHE THR LEU SER ASP ASN TYR THR TYR VAL PHE LEU GLY 1TRK 65 SEQRES 13 A 680 ASP GLY CYS LEU GLN GLU GLY ILE SER SER GLU ALA SER 1TRK 66 SEQRES 14 A 680 SER LEU ALA GLY HIS LEU LYS LEU GLY ASN LEU ILE ALA 1TRK 67 SEQRES 15 A 680 ILE TYR ASP ASP ASN LYS ILE THR ILE ASP GLY ALA THR 1TRK 68 SEQRES 16 A 680 SER ILE SER PHE ASP GLU ASP VAL ALA LYS ARG TYR GLU 1TRK 69 SEQRES 17 A 680 ALA TYR GLY TRP GLU VAL LEU TYR VAL GLU ASN GLY ASN 1TRK 70 SEQRES 18 A 680 GLU ASP LEU ALA GLY ILE ALA LYS ALA ILE ALA GLN ALA 1TRK 71 SEQRES 19 A 680 LYS LEU SER LYS ASP LYS PRO THR LEU ILE LYS MET THR 1TRK 72 SEQRES 20 A 680 THR THR ILE GLY TYR GLY SER LEU HIS ALA GLY SER HIS 1TRK 73 SEQRES 21 A 680 SER VAL HIS GLY ALA PRO LEU LYS ALA ASP ASP VAL LYS 1TRK 74 SEQRES 22 A 680 GLN LEU LYS SER LYS PHE GLY PHE ASN PRO ASP LYS SER 1TRK 75 SEQRES 23 A 680 PHE VAL VAL PRO GLN GLU VAL TYR ASP HIS TYR GLN LYS 1TRK 76 SEQRES 24 A 680 THR ILE LEU LYS PRO GLY VAL GLU ALA ASN ASN LYS TRP 1TRK 77 SEQRES 25 A 680 ASN LYS LEU PHE SER GLU TYR GLN LYS LYS PHE PRO GLU 1TRK 78 SEQRES 26 A 680 LEU GLY ALA GLU LEU ALA ARG ARG LEU SER GLY GLN LEU 1TRK 79 SEQRES 27 A 680 PRO ALA ASN TRP GLU SER LYS LEU PRO THR TYR THR ALA 1TRK 80 SEQRES 28 A 680 LYS ASP SER ALA VAL ALA THR ARG LYS LEU SER GLU THR 1TRK 81 SEQRES 29 A 680 VAL LEU GLU ASP VAL TYR ASN GLN LEU PRO GLU LEU ILE 1TRK 82 SEQRES 30 A 680 GLY GLY SER ALA ASP LEU THR PRO SER ASN LEU THR ARG 1TRK 83 SEQRES 31 A 680 TRP LYS GLU ALA LEU ASP PHE GLN PRO PRO SER SER GLY 1TRK 84 SEQRES 32 A 680 SER GLY ASN TYR SER GLY ARG TYR ILE ARG TYR GLY ILE 1TRK 85 SEQRES 33 A 680 ARG GLU HIS ALA MET GLY ALA ILE MET ASN GLY ILE SER 1TRK 86 SEQRES 34 A 680 ALA PHE GLY ALA ASN TYR LYS PRO TYR GLY GLY THR PHE 1TRK 87 SEQRES 35 A 680 LEU ASN PHE VAL SER TYR ALA ALA GLY ALA VAL ARG LEU 1TRK 88 SEQRES 36 A 680 SER ALA LEU SER GLY HIS PRO VAL ILE TRP VAL ALA THR 1TRK 89 SEQRES 37 A 680 HIS ASP SER ILE GLY VAL GLY GLU ASP GLY PRO THR HIS 1TRK 90 SEQRES 38 A 680 GLN PRO ILE GLU THR LEU ALA HIS PHE ARG SER LEU PRO 1TRK 91 SEQRES 39 A 680 ASN ILE GLN VAL TRP ARG PRO ALA ASP GLY ASN GLU VAL 1TRK 92 SEQRES 40 A 680 SER ALA ALA TYR LYS ASN SER LEU GLU SER LYS HIS THR 1TRK 93 SEQRES 41 A 680 PRO SER ILE ILE ALA LEU SER ARG GLN ASN LEU PRO GLN 1TRK 94 SEQRES 42 A 680 LEU GLU GLY SER SER ILE GLU SER ALA SER LYS GLY GLY 1TRK 95 SEQRES 43 A 680 TYR VAL LEU GLN ASP VAL ALA ASN PRO ASP ILE ILE LEU 1TRK 96 SEQRES 44 A 680 VAL ALA THR GLY SER GLU VAL SER LEU SER VAL GLU ALA 1TRK 97 SEQRES 45 A 680 ALA LYS THR LEU ALA ALA LYS ASN ILE LYS ALA ARG VAL 1TRK 98 SEQRES 46 A 680 VAL SER LEU PRO ASP PHE PHE THR PHE ASP LYS GLN PRO 1TRK 99 SEQRES 47 A 680 LEU GLU TYR ARG LEU SER VAL LEU PRO ASP ASN VAL PRO 1TRK 100 SEQRES 48 A 680 ILE MET SER VAL GLU VAL LEU ALA THR THR CYS TRP GLY 1TRK 101 SEQRES 49 A 680 LYS TYR ALA HIS GLN SER PHE GLY ILE ASP ARG PHE GLY 1TRK 102 SEQRES 50 A 680 ALA SER GLY LYS ALA PRO GLU VAL PHE LYS PHE PHE GLY 1TRK 103 SEQRES 51 A 680 PHE THR PRO GLU GLY VAL ALA GLU ARG ALA GLN LYS THR 1TRK 104 SEQRES 52 A 680 ILE ALA PHE TYR LYS GLY ASP LYS LEU ILE SER PRO LEU 1TRK 105 SEQRES 53 A 680 LYS LYS ALA PHE 1TRK 106 SEQRES 1 B 680 MET THR GLN PHE THR ASP ILE ASP LYS LEU ALA VAL SER 1TRK 107 SEQRES 2 B 680 THR ILE ARG ILE LEU ALA VAL ASP THR VAL SER LYS ALA 1TRK 108 SEQRES 3 B 680 ASN SER GLY HIS PRO GLY ALA PRO LEU GLY MET ALA PRO 1TRK 109 SEQRES 4 B 680 ALA ALA HIS VAL LEU TRP SER GLN MET ARG MET ASN PRO 1TRK 110 SEQRES 5 B 680 THR ASN PRO ASP TRP ILE ASN ARG ASP ARG PHE VAL LEU 1TRK 111 SEQRES 6 B 680 SER ASN GLY HIS ALA VAL ALA LEU LEU TYR SER MET LEU 1TRK 112 SEQRES 7 B 680 HIS LEU THR GLY TYR ASP LEU SER ILE GLU ASP LEU LYS 1TRK 113 SEQRES 8 B 680 GLN PHE ARG GLN LEU GLY SER ARG THR PRO GLY HIS PRO 1TRK 114 SEQRES 9 B 680 GLU PHE GLU LEU PRO GLY VAL GLU VAL THR THR GLY PRO 1TRK 115 SEQRES 10 B 680 LEU GLY GLN GLY ILE SER ASN ALA VAL GLY MET ALA MET 1TRK 116 SEQRES 11 B 680 ALA GLN ALA ASN LEU ALA ALA THR TYR ASN LYS PRO GLY 1TRK 117 SEQRES 12 B 680 PHE THR LEU SER ASP ASN TYR THR TYR VAL PHE LEU GLY 1TRK 118 SEQRES 13 B 680 ASP GLY CYS LEU GLN GLU GLY ILE SER SER GLU ALA SER 1TRK 119 SEQRES 14 B 680 SER LEU ALA GLY HIS LEU LYS LEU GLY ASN LEU ILE ALA 1TRK 120 SEQRES 15 B 680 ILE TYR ASP ASP ASN LYS ILE THR ILE ASP GLY ALA THR 1TRK 121 SEQRES 16 B 680 SER ILE SER PHE ASP GLU ASP VAL ALA LYS ARG TYR GLU 1TRK 122 SEQRES 17 B 680 ALA TYR GLY TRP GLU VAL LEU TYR VAL GLU ASN GLY ASN 1TRK 123 SEQRES 18 B 680 GLU ASP LEU ALA GLY ILE ALA LYS ALA ILE ALA GLN ALA 1TRK 124 SEQRES 19 B 680 LYS LEU SER LYS ASP LYS PRO THR LEU ILE LYS MET THR 1TRK 125 SEQRES 20 B 680 THR THR ILE GLY TYR GLY SER LEU HIS ALA GLY SER HIS 1TRK 126 SEQRES 21 B 680 SER VAL HIS GLY ALA PRO LEU LYS ALA ASP ASP VAL LYS 1TRK 127 SEQRES 22 B 680 GLN LEU LYS SER LYS PHE GLY PHE ASN PRO ASP LYS SER 1TRK 128 SEQRES 23 B 680 PHE VAL VAL PRO GLN GLU VAL TYR ASP HIS TYR GLN LYS 1TRK 129 SEQRES 24 B 680 THR ILE LEU LYS PRO GLY VAL GLU ALA ASN ASN LYS TRP 1TRK 130 SEQRES 25 B 680 ASN LYS LEU PHE SER GLU TYR GLN LYS LYS PHE PRO GLU 1TRK 131 SEQRES 26 B 680 LEU GLY ALA GLU LEU ALA ARG ARG LEU SER GLY GLN LEU 1TRK 132 SEQRES 27 B 680 PRO ALA ASN TRP GLU SER LYS LEU PRO THR TYR THR ALA 1TRK 133 SEQRES 28 B 680 LYS ASP SER ALA VAL ALA THR ARG LYS LEU SER GLU THR 1TRK 134 SEQRES 29 B 680 VAL LEU GLU ASP VAL TYR ASN GLN LEU PRO GLU LEU ILE 1TRK 135 SEQRES 30 B 680 GLY GLY SER ALA ASP LEU THR PRO SER ASN LEU THR ARG 1TRK 136 SEQRES 31 B 680 TRP LYS GLU ALA LEU ASP PHE GLN PRO PRO SER SER GLY 1TRK 137 SEQRES 32 B 680 SER GLY ASN TYR SER GLY ARG TYR ILE ARG TYR GLY ILE 1TRK 138 SEQRES 33 B 680 ARG GLU HIS ALA MET GLY ALA ILE MET ASN GLY ILE SER 1TRK 139 SEQRES 34 B 680 ALA PHE GLY ALA ASN TYR LYS PRO TYR GLY GLY THR PHE 1TRK 140 SEQRES 35 B 680 LEU ASN PHE VAL SER TYR ALA ALA GLY ALA VAL ARG LEU 1TRK 141 SEQRES 36 B 680 SER ALA LEU SER GLY HIS PRO VAL ILE TRP VAL ALA THR 1TRK 142 SEQRES 37 B 680 HIS ASP SER ILE GLY VAL GLY GLU ASP GLY PRO THR HIS 1TRK 143 SEQRES 38 B 680 GLN PRO ILE GLU THR LEU ALA HIS PHE ARG SER LEU PRO 1TRK 144 SEQRES 39 B 680 ASN ILE GLN VAL TRP ARG PRO ALA ASP GLY ASN GLU VAL 1TRK 145 SEQRES 40 B 680 SER ALA ALA TYR LYS ASN SER LEU GLU SER LYS HIS THR 1TRK 146 SEQRES 41 B 680 PRO SER ILE ILE ALA LEU SER ARG GLN ASN LEU PRO GLN 1TRK 147 SEQRES 42 B 680 LEU GLU GLY SER SER ILE GLU SER ALA SER LYS GLY GLY 1TRK 148 SEQRES 43 B 680 TYR VAL LEU GLN ASP VAL ALA ASN PRO ASP ILE ILE LEU 1TRK 149 SEQRES 44 B 680 VAL ALA THR GLY SER GLU VAL SER LEU SER VAL GLU ALA 1TRK 150 SEQRES 45 B 680 ALA LYS THR LEU ALA ALA LYS ASN ILE LYS ALA ARG VAL 1TRK 151 SEQRES 46 B 680 VAL SER LEU PRO ASP PHE PHE THR PHE ASP LYS GLN PRO 1TRK 152 SEQRES 47 B 680 LEU GLU TYR ARG LEU SER VAL LEU PRO ASP ASN VAL PRO 1TRK 153 SEQRES 48 B 680 ILE MET SER VAL GLU VAL LEU ALA THR THR CYS TRP GLY 1TRK 154 SEQRES 49 B 680 LYS TYR ALA HIS GLN SER PHE GLY ILE ASP ARG PHE GLY 1TRK 155 SEQRES 50 B 680 ALA SER GLY LYS ALA PRO GLU VAL PHE LYS PHE PHE GLY 1TRK 156 SEQRES 51 B 680 PHE THR PRO GLU GLY VAL ALA GLU ARG ALA GLN LYS THR 1TRK 157 SEQRES 52 B 680 ILE ALA PHE TYR LYS GLY ASP LYS LEU ILE SER PRO LEU 1TRK 158 SEQRES 53 B 680 LYS LYS ALA PHE 1TRK 159 HET CA A 681 1 CALCIUM +2 COUNTER ION 1TRK 160 HET TPP A 682 26 THIAMIN DIPHOSPHATE 1TRK 161 HET CA B 681 1 CALCIUM +2 COUNTER ION 1TRK 162 HET TPP B 682 26 THIAMIN DIPHOSPHATE 1TRK 163 FORMUL 3 CA 2(CA1) 1TRK 164 FORMUL 4 TPP 2(C12 H18 N4 O7 P2 S1) 1TRK 165 FORMUL 5 HOH *1021(H2 O1) 1TRK 166 HELIX 1 A1 ASP A 6 ALA A 26 1 N-TERMINAL DOMAIN 1TRK 167 HELIX 2 A2 GLY A 32 PRO A 39 1 N-TERMINAL DOMAIN 1TRK 168 HELIX 3 A3 ALA A 40 SER A 46 1 N-TERMINAL DOMAIN 1TRK 169 HELIX 4 A4 VAL A 71 LEU A 80 1 N-TERMINAL DOMAIN 1TRK 170 HELIX 5 A5 ILE A 87 LYS A 91 1 N-TERMINAL DOMAIN 1TRK 171 HELIX 6 A6 GLN A 120 TYR A 139 1 N-TERMINAL DOMAIN 1TRK 172 HELIX 7 A7 ASP A 157 GLN A 161 1 N-TERMINAL DOMAIN 1TRK 173 HELIX 8 A8 GLY A 163 LEU A 175 1 N-TERMINAL DOMAIN 1TRK 174 HELIX 9 A9 VAL A 203 ALA A 209 1 N-TERMINAL DOMAIN 1TRK 175 HELIX 10 A10 LEU A 224 LEU A 236 1 N-TERMINAL DOMAIN 1TRK 176 HELIX 11 A11 ALA A 269 LYS A 278 1 N-TERMINAL DOMAIN 1TRK 177 HELIX 12 A12 GLN A 291 PRO A 324 1 N-TERMINAL DOMAIN 1TRK 178 HELIX 13 A13 LEU A 326 LEU A 334 1 MIDDLE DOMAIN 1TRK 179 HELIX 14 A14 THR A 358 VAL A 369 1 MIDDLE DOMAIN 1TRK 180 HELIX 15 A15 THR A 384 ASN A 387 1 MIDDLE DOMAIN 1TRK 181 HELIX 16 A16 GLU A 418 PHE A 431 1 MIDDLE DOMAIN 1TRK 182 HELIX 17 A17 LEU A 443 VAL A 446 1 MIDDLE DOMAIN 1TRK 183 HELIX 18 A18 ARG A 500 ALA A 509 1 MIDDLE DOMAIN 1TRK 184 HELIX 19 A19 THR A 486 ARG A 491 1 MIDDLE DOMAIN 1TRK 185 HELIX 20 A20 GLY A 504 GLU A 516 1 MIDDLE DOMAIN 1TRK 186 HELIX 21 A21 ILE A 539 ALA A 542 1 C-TERMINAL DOMAIN 1TRK 187 HELIX 22 A22 GLU A 565 ALA A 578 1 C-TERMINAL 1TRK 188 HELIX 23 A23 PHE A 591 LYS A 596 1 C-TERMINAL DOMAIN 1TRK 189 HELIX 24 A24 LEU A 599 VAL A 605 1 C-TERMINAL 1TRK 190 HELIX 25 A25 ALA A 642 PHE A 649 1 C-TERMINAL DOMAIN 1TRK 191 HELIX 26 A26 PRO A 653 TYR A 667 1 C-TERMINAL 1TRK 192 HELIX 27 B1 ASP B 6 ALA B 26 1 N-TERMINAL DOMAIN 1TRK 193 HELIX 28 B2 GLY B 32 PRO B 39 1 N-TERMINAL DOMAIN 1TRK 194 HELIX 29 B3 ALA B 40 SER B 46 1 N-TERMINAL DOMAIN 1TRK 195 HELIX 30 B4 VAL B 71 LEU B 80 1 N-TERMINAL DOMAIN 1TRK 196 HELIX 31 B5 ILE B 87 LYS B 91 1 N-TERMINAL DOMAIN 1TRK 197 HELIX 32 B6 GLN B 120 TYR B 139 1 N-TERMINAL DOMAIN 1TRK 198 HELIX 33 B7 ASP B 157 GLN B 161 1 N-TERMINAL DOMAIN 1TRK 199 HELIX 34 B8 GLY B 163 LEU B 175 1 N-TERMINAL DOMAIN 1TRK 200 HELIX 35 B9 VAL B 203 ALA B 209 1 N-TERMINAL DOMAIN 1TRK 201 HELIX 36 B10 LEU B 224 LEU B 236 1 N-TERMINAL DOMAIN 1TRK 202 HELIX 37 B11 ALA B 269 LYS B 278 1 N-TERMINAL DOMAIN 1TRK 203 HELIX 38 B12 GLN B 291 PRO B 324 1 N-TERMINAL DOMAIN 1TRK 204 HELIX 39 B13 LEU B 326 LEU B 334 1 MIDDLE DOMAIN 1TRK 205 HELIX 40 B14 THR B 358 VAL B 369 1 MIDDLE DOMAIN 1TRK 206 HELIX 41 B15 THR B 384 ASN B 387 1 MIDDLE DOMAIN 1TRK 207 HELIX 42 B16 GLU B 418 PHE B 431 1 MIDDLE DOMAIN 1TRK 208 HELIX 43 B17 LEU B 443 VAL B 446 1 MIDDLE DOMAIN 1TRK 209 HELIX 44 B18 ARG B 500 ALA B 509 1 MIDDLE DOMAIN 1TRK 210 HELIX 45 B19 THR B 486 ARG B 491 1 MIDDLE DOMAIN 1TRK 211 HELIX 46 B20 GLY B 504 GLU B 516 1 MIDDLE DOMAIN 1TRK 212 HELIX 47 B21 ILE B 539 ALA B 542 1 C-TERMINAL DOMAIN 1TRK 213 HELIX 48 B22 GLU B 565 ALA B 578 1 C-TERMINAL 1TRK 214 HELIX 49 B23 PHE B 591 LYS B 596 1 C-TERMINAL DOMAIN 1TRK 215 HELIX 50 B24 LEU B 599 VAL B 605 1 C-TERMINAL 1TRK 216 HELIX 51 B25 ALA B 642 PHE B 649 1 C-TERMINAL DOMAIN 1TRK 217 HELIX 52 B26 PRO B 653 TYR B 667 1 C-TERMINAL 1TRK 218 SHEET 1 NA 5 ARG A 62 LEU A 65 0 1TRK 219 SHEET 2 NA 5 THR A 151 ASP A 157 1 N TYR A 152 O ARG A 62 1TRK 220 SHEET 3 NA 5 LEU A 180 ASP A 186 1 N ILE A 181 O THR A 151 1TRK 221 SHEET 4 NA 5 THR A 242 THR A 247 1 N THR A 242 O LEU A 180 1TRK 222 SHEET 5 NA 5 GLU A 213 VAL A 217 1 N LEU A 215 O LEU A 243 1TRK 223 SHEET 1 MA 6 TYR A 411 ARG A 413 0 1TRK 224 SHEET 2 MA 6 LEU A 376 SER A 380 1 O GLY A 378 N ILE A 412 1TRK 225 SHEET 3 MA 6 LYS A 436 PHE A 442 1 N TYR A 438 O ILE A 377 1TRK 226 SHEET 4 MA 6 ILE A 464 THR A 468 1 N VAL A 466 O GLY A 439 1TRK 227 SHEET 5 MA 6 SER A 522 ALA A 525 1 N ILE A 524 O TRP A 465 1TRK 228 SHEET 6 MA 6 GLN A 497 TRP A 499 1 N TRP A 499 O ILE A 523 1TRK 229 SHEET 1 CA 5 TYR A 547 GLN A 550 0 1TRK 230 SHEET 2 CA 5 ALA A 583 SER A 587 -1 N VAL A 585 O GLN A 550 1TRK 231 SHEET 3 CA 5 ILE A 557 ALA A 561 1 N LEU A 559 O ARG A 584 1TRK 232 SHEET 4 CA 5 ILE A 612 VAL A 615 1 N MET A 613 O ILE A 558 1TRK 233 SHEET 5 CA 5 GLN A 629 PHE A 631 1 N PHE A 631 O SER A 614 1TRK 234 SHEET 1 NA 5 ARG A 62 LEU A 65 0 1TRK 235 SHEET 2 NA 5 THR A 151 ASP A 157 1 N TYR A 152 O ARG A 62 1TRK 236 SHEET 3 NA 5 LEU A 180 ASP A 186 1 N ILE A 181 O THR A 151 1TRK 237 SHEET 4 NA 5 THR A 242 THR A 247 1 N THR A 242 O LEU A 180 1TRK 238 SHEET 5 NA 5 GLU A 213 VAL A 217 1 N LEU A 215 O LEU A 243 1TRK 239 SHEET 1 MA 6 TYR A 411 ARG A 413 0 1TRK 240 SHEET 2 MA 6 LEU A 376 SER A 380 1 O GLY A 378 N ILE A 412 1TRK 241 SHEET 3 MA 6 LYS A 436 PHE A 442 1 N TYR A 438 O ILE A 377 1TRK 242 SHEET 4 MA 6 ILE A 464 THR A 468 1 N VAL A 466 O GLY A 439 1TRK 243 SHEET 5 MA 6 SER A 522 ALA A 525 1 N ILE A 524 O TRP A 465 1TRK 244 SHEET 6 MA 6 GLN A 497 TRP A 499 1 N TRP A 499 O ILE A 523 1TRK 245 SHEET 1 CA 5 TYR A 547 GLN A 550 0 1TRK 246 SHEET 2 CA 5 ALA A 583 SER A 587 -1 N VAL A 585 O GLN A 550 1TRK 247 SHEET 3 CA 5 ILE A 557 ALA A 561 1 N LEU A 559 O ARG A 584 1TRK 248 SHEET 4 CA 5 ILE A 612 VAL A 615 1 N MET A 613 O ILE A 558 1TRK 249 SHEET 5 CA 5 GLN A 629 PHE A 631 1 N PHE A 631 O SER A 614 1TRK 250 SHEET 1 NB 5 ARG B 62 LEU B 65 0 1TRK 251 SHEET 2 NB 5 THR B 151 ASP B 157 1 N TYR B 152 O ARG B 62 1TRK 252 SHEET 3 NB 5 LEU B 180 ASP B 186 1 N ILE B 181 O THR B 151 1TRK 253 SHEET 4 NB 5 THR B 242 THR B 247 1 N THR B 242 O LEU B 180 1TRK 254 SHEET 5 NB 5 GLU B 213 VAL B 217 1 N LEU B 215 O LEU B 243 1TRK 255 SHEET 1 MB 6 TYR B 411 ARG B 413 0 1TRK 256 SHEET 2 MB 6 LEU B 376 SER B 380 1 O GLY B 378 N ILE B 412 1TRK 257 SHEET 3 MB 6 LYS B 436 PHE B 442 1 N TYR B 438 O ILE B 377 1TRK 258 SHEET 4 MB 6 ILE B 464 THR B 468 1 N VAL B 466 O GLY B 439 1TRK 259 SHEET 5 MB 6 SER B 522 ALA B 525 1 N ILE B 524 O TRP B 465 1TRK 260 SHEET 6 MB 6 GLN B 497 TRP B 499 1 N TRP B 499 O ILE B 523 1TRK 261 SHEET 1 CB 5 TYR B 547 GLN B 550 0 1TRK 262 SHEET 2 CB 5 ALA B 583 SER B 587 -1 N VAL B 585 O GLN B 550 1TRK 263 SHEET 3 CB 5 ILE B 557 ALA B 561 1 N LEU B 559 O ARG B 584 1TRK 264 SHEET 4 CB 5 ILE B 612 VAL B 615 1 N MET B 613 O ILE B 558 1TRK 265 SHEET 5 CB 5 GLN B 629 PHE B 631 1 N PHE B 631 O SER B 614 1TRK 266 CRYST1 76.300 113.300 160.900 90.00 90.00 90.00 P 21 21 21 8 1TRK 267 ORIGX1 1.000000 0.000000 0.000000 0.00000 1TRK 268 ORIGX2 0.000000 1.000000 0.000000 0.00000 1TRK 269 ORIGX3 0.000000 0.000000 1.000000 0.00000 1TRK 270 SCALE1 0.013106 0.000000 0.000000 0.00000 1TRK 271 SCALE2 0.000000 0.008826 0.000000 0.00000 1TRK 272 SCALE3 0.000000 0.000000 0.006215 0.00000 1TRK 273 MTRIX1 1 -0.784000 0.001000 -0.621000 25.04400 1 1TRK 274 MTRIX2 1 0.000000 -1.000000 -0.002000 132.15700 1 1TRK 275 MTRIX3 1 -0.621000 -0.001000 0.786400 8.81300 1 1TRK 276