HEADER GLYCOGEN PHOSPHORYLASE 04-JUN-90 4GPB 4GPB 2 COMPND GLYCOGEN PHOSPHORYLASE $B (E.C.2.4.1.1) (T STATE) COMPLEX 4GPB 3 COMPND 2 WITH 2-FLUORO-2-DEOXY-ALPHA-*D-GLUCOSE-1-PHOSPHATE 4GPB 4 SOURCE RABBIT (ORYCTOLAGUS $CUNICULUS) MUSCLE 4GPB 5 AUTHOR J.L.MARTIN,L.N.JOHNSON 4GPB 6 REVDAT 1 15-OCT-92 4GPB 0 4GPB 7 JRNL AUTH J.L.MARTIN,L.N.JOHNSON,S.G.WITHERS 4GPB 8 JRNL TITL COMPARISON OF THE BINDING OF GLUCOSE AND 4GPB 9 JRNL TITL 2 GLUCOSE-1-PHOSPHATE DERIVATIVES TO T-STATE 4GPB 10 JRNL TITL 3 GLYCOGEN PHOSPHORYLASE $B 4GPB 11 JRNL REF BIOCHEMISTRY V. 29 10745 1990 4GPB 12 JRNL REFN ASTM BICHAW US ISSN 0006-2960 033 4GPB 13 REMARK 1 4GPB 14 REMARK 1 REFERENCE 1 4GPB 15 REMARK 1 AUTH K.R.ACHARYA,D.I.STUART,K.M.VARVILL,L.N.JOHNSON 4GPB 16 REMARK 1 TITL GLYCOGEN PHOSPHORYLASE $B: DESCRIPTION OF THE 4GPB 17 REMARK 1 TITL 2 PROTEIN STRUCTURE 1 1991 4GPB 18 REMARK 1 REF GLYCOGEN PHOSPHORYLASE $B: 4GPB 19 REMARK 1 REF 2 DESCRIPTION OF THE 4GPB 20 REMARK 1 REF 3 PROTEIN STRUCTURE 4GPB 21 REMARK 1 PUBL WORLD SCIENTIFIC PUBLISHING CO.,SINGAPORE 4GPB 22 REMARK 1 REFN ISBN 981-02-0540-6 789 4GPB 23 REMARK 1 REFERENCE 2 4GPB 24 REMARK 1 AUTH D.BARFORD,S.-*H.HU,L.N.JOHNSON 4GPB 25 REMARK 1 TITL STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE 4GPB 26 REMARK 1 TITL 2 CONTROL BY PHOSPHORYLATION AND /AMP$ 4GPB 27 REMARK 1 REF J.MOL.BIOL. V. 218 233 1991 4GPB 28 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 4GPB 29 REMARK 1 REFERENCE 3 4GPB 30 REMARK 1 AUTH L.N.JOHNSON,K.R.ACHARYA,M.D.JORDAN,P.J.MC*LAUGHLIN 4GPB 31 REMARK 1 TITL REFINED CRYSTAL STRUCTURE OF THE 4GPB 32 REMARK 1 TITL 2 PHOSPHORYLASE-*HEPTULOSE 4GPB 33 REMARK 1 TITL 3 2-*PHOSPHATE-*OLIGOSACCHARIDE-/AMP$ COMPLEX 4GPB 34 REMARK 1 REF J.MOL.BIOL. V. 211 645 1990 4GPB 35 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 4GPB 36 REMARK 1 REFERENCE 4 4GPB 37 REMARK 1 AUTH D.BARFORD,L.N.JOHNSON 4GPB 38 REMARK 1 TITL THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE 4GPB 39 REMARK 1 REF NATURE V. 340 609 1989 4GPB 40 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 4GPB 41 REMARK 1 REFERENCE 5 4GPB 42 REMARK 1 AUTH S.R.SPRANG,K.R.ACHARYA,E.J.GOLDSMITH,D.I.STUART, 4GPB 43 REMARK 1 AUTH 2 K.VARVILL,R.J.FLETTERICK,N.B.MADSEN,L.N.JOHNSON 4GPB 44 REMARK 1 TITL STRUCTURAL CHANGES IN GLYCOGEN PHOSPHORYLASE 4GPB 45 REMARK 1 TITL 2 INDUCED BY PHOSPHORYLATION 4GPB 46 REMARK 1 REF NATURE V. 336 215 1988 4GPB 47 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 4GPB 48 REMARK 2 4GPB 49 REMARK 2 RESOLUTION. 2.3 ANGSTROMS. 4GPB 50 REMARK 3 4GPB 51 REMARK 3 REFINEMENT. MOLECULAR DYNAMICS REFINEMENT BY 4GPB 52 REMARK 3 THE METHOD OF A. BRUNGER, J. KURIYAN, AND M. KARPLUS 4GPB 53 REMARK 3 (PROGRAM *XPLOR*). THE R VALUE IS 0.180 FOR 26600 4GPB 54 REMARK 3 REFLECTIONS IN THE RESOLUTION RANGE 8.0 TO 2.2 ANGSTROMS. 4GPB 55 REMARK 3 THE RMS DEVIATION FROM IDEALITY OF THE BOND LENGTHS IS 4GPB 56 REMARK 3 0.016 ANGSTROMS. THE RMS DEVIATION FROM IDEALITY OF THE 4GPB 57 REMARK 3 BOND ANGLES IS 3.5 DEGREES. 4GPB 58 REMARK 4 4GPB 59 REMARK 4 PLP FORMS A SCHIFF'S BASE WITH NZ OF LYS 680. 4GPB 60 REMARK 5 4GPB 61 REMARK 5 RESIDUE 380 IS LEU IN THE SEQUENCE (K.NAKANO,P.K.HWANG, 4GPB 62 REMARK 5 R.J.FLETTERICK, FEBS LETT., V. 204, P. 283, 1986) BUT IT 4GPB 63 REMARK 5 HAS BEEN PRESENTED AS ILE IN THIS ENTRY. THIS ASSIGNMENT 4GPB 64 REMARK 5 WAS MADE IN THE ORIGINAL STRUCTURE DETERMINATION AT 1.9 4GPB 65 REMARK 5 ANGSTROMS (PRESENTED IN PROTEIN DATA BANK ENTRY 1GPB) AND 4GPB 66 REMARK 5 CARRIED THROUGH TO THE OTHER ENTRIES. ILE IS MORE 4GPB 67 REMARK 5 CONSISTENT WITH THE ELECTRON DENSITY. HOWEVER, THE 4GPB 68 REMARK 5 RESOLUTION AT 1.9 ANGSTROMS DOES NOT ALLOW A DEFINITIVE 4GPB 69 REMARK 5 ASSIGNMENT. 4GPB 70 SEQRES 1 842 SER ARG PRO LEU SER ASP GLN GLU LYS ARG LYS GLN ILE 4GPB 71 SEQRES 2 842 SER VAL ARG GLY LEU ALA GLY VAL GLU ASN VAL THR GLU 4GPB 72 SEQRES 3 842 LEU LYS LYS ASN PHE ASN ARG HIS LEU HIS PHE THR LEU 4GPB 73 SEQRES 4 842 VAL LYS ASP ARG ASN VAL ALA THR PRO ARG ASP TYR TYR 4GPB 74 SEQRES 5 842 PHE ALA LEU ALA HIS THR VAL ARG ASP HIS LEU VAL GLY 4GPB 75 SEQRES 6 842 ARG TRP ILE ARG THR GLN GLN HIS TYR TYR GLU LYS ASP 4GPB 76 SEQRES 7 842 PRO LYS ARG ILE TYR TYR LEU SER LEU GLU PHE TYR MET 4GPB 77 SEQRES 8 842 GLY ARG THR LEU GLN ASN THR MET VAL ASN LEU ALA LEU 4GPB 78 SEQRES 9 842 GLU ASN ALA CYS ASP GLU ALA THR TYR GLN LEU GLY LEU 4GPB 79 SEQRES 10 842 ASP MET GLU GLU LEU GLU GLU ILE GLU GLU ASP ALA GLY 4GPB 80 SEQRES 11 842 LEU GLY ASN GLY GLY LEU GLY ARG LEU ALA ALA CYS PHE 4GPB 81 SEQRES 12 842 LEU ASP SER MET ALA THR LEU GLY LEU ALA ALA TYR GLY 4GPB 82 SEQRES 13 842 TYR GLY ILE ARG TYR GLU PHE GLY ILE PHE ASN GLN LYS 4GPB 83 SEQRES 14 842 ILE CYS GLY GLY TRP GLN MET GLU GLU ALA ASP ASP TRP 4GPB 84 SEQRES 15 842 LEU ARG TYR GLY ASN PRO TRP GLU LYS ALA ARG PRO GLU 4GPB 85 SEQRES 16 842 PHE THR LEU PRO VAL HIS PHE TYR GLY ARG VAL GLU HIS 4GPB 86 SEQRES 17 842 THR SER GLN GLY ALA LYS TRP VAL ASP THR GLN VAL VAL 4GPB 87 SEQRES 18 842 LEU ALA MET PRO TYR ASP THR PRO VAL PRO GLY TYR ARG 4GPB 88 SEQRES 19 842 ASN ASN VAL VAL ASN THR MET ARG LEU TRP SER ALA LYS 4GPB 89 SEQRES 20 842 ALA PRO ASN ASP PHE ASN LEU LYS ASP PHE ASN VAL GLY 4GPB 90 SEQRES 21 842 GLY TYR ILE GLN ALA VAL LEU ASP ARG ASN LEU ALA GLU 4GPB 91 SEQRES 22 842 ASN ILE SER ARG VAL LEU TYR PRO ASN ASP ASN PHE PHE 4GPB 92 SEQRES 23 842 GLU GLY LYS GLU LEU ARG LEU LYS GLN GLU TYR PHE VAL 4GPB 93 SEQRES 24 842 VAL ALA ALA THR LEU GLN ASP ILE ILE ARG ARG PHE LYS 4GPB 94 SEQRES 25 842 SER SER LYS PHE GLY CYS ARG ASP PRO VAL ARG THR ASN 4GPB 95 SEQRES 26 842 PHE ASP ALA PHE PRO ASP LYS VAL ALA ILE GLN LEU ASN 4GPB 96 SEQRES 27 842 ASP THR HIS PRO SER LEU ALA ILE PRO GLU LEU MET ARG 4GPB 97 SEQRES 28 842 VAL LEU VAL ASP LEU GLU ARG LEU ASP TRP ASP LYS ALA 4GPB 98 SEQRES 29 842 TRP GLU VAL THR VAL LYS THR CYS ALA TYR THR ASN HIS 4GPB 99 SEQRES 30 842 THR VAL ILE PRO GLU ALA LEU GLU ARG TRP PRO VAL HIS 4GPB 100 SEQRES 31 842 LEU LEU GLU THR LEU LEU PRO ARG HIS LEU GLN ILE ILE 4GPB 101 SEQRES 32 842 TYR GLU ILE ASN GLN ARG PHE LEU ASN ARG VAL ALA ALA 4GPB 102 SEQRES 33 842 ALA PHE PRO GLY ASP VAL ASP ARG LEU ARG ARG MET SER 4GPB 103 SEQRES 34 842 LEU VAL GLU GLU GLY ALA VAL LYS ARG ILE ASN MET ALA 4GPB 104 SEQRES 35 842 HIS LEU CYS ILE ALA GLY SER HIS ALA VAL ASN GLY VAL 4GPB 105 SEQRES 36 842 ALA ARG ILE HIS SER GLU ILE LEU LYS LYS THR ILE PHE 4GPB 106 SEQRES 37 842 LYS ASP PHE TYR GLU LEU GLU PRO HIS LYS PHE GLN ASN 4GPB 107 SEQRES 38 842 LYS THR ASN GLY ILE THR PRO ARG ARG TRP LEU VAL LEU 4GPB 108 SEQRES 39 842 CYS ASN PRO GLY LEU ALA GLU ILE ILE ALA GLU ARG ILE 4GPB 109 SEQRES 40 842 GLY GLU GLU TYR ILE SER ASP LEU ASP GLN LEU ARG LYS 4GPB 110 SEQRES 41 842 LEU LEU SER TYR VAL ASP ASP GLU ALA PHE ILE ARG ASP 4GPB 111 SEQRES 42 842 VAL ALA LYS VAL LYS GLN GLU ASN LYS LEU LYS PHE ALA 4GPB 112 SEQRES 43 842 ALA TYR LEU GLU ARG GLU TYR LYS VAL HIS ILE ASN PRO 4GPB 113 SEQRES 44 842 ASN SER LEU PHE ASP VAL GLN VAL LYS ARG ILE HIS GLU 4GPB 114 SEQRES 45 842 TYR LYS ARG GLN LEU LEU ASN CYS LEU HIS VAL ILE THR 4GPB 115 SEQRES 46 842 LEU TYR ASN ARG ILE LYS LYS GLU PRO ASN LYS PHE VAL 4GPB 116 SEQRES 47 842 VAL PRO ARG THR VAL MET ILE GLY GLY LYS ALA ALA PRO 4GPB 117 SEQRES 48 842 GLY TYR HIS MET ALA LYS MET ILE ILE LYS LEU ILE THR 4GPB 118 SEQRES 49 842 ALA ILE GLY ASP VAL VAL ASN HIS ASP PRO VAL VAL GLY 4GPB 119 SEQRES 50 842 ASP ARG LEU ARG VAL ILE PHE LEU GLU ASN TYR ARG VAL 4GPB 120 SEQRES 51 842 SER LEU ALA GLU LYS VAL ILE PRO ALA ALA ASP LEU SER 4GPB 121 SEQRES 52 842 GLU GLN ILE SER THR ALA GLY THR GLU ALA SER GLY THR 4GPB 122 SEQRES 53 842 GLY ASN MET LYS PHE MET LEU ASN GLY ALA LEU THR ILE 4GPB 123 SEQRES 54 842 GLY THR MET ASP GLY ALA ASN VAL GLU MET ALA GLU GLU 4GPB 124 SEQRES 55 842 ALA GLY GLU GLU ASN PHE PHE ILE PHE GLY MET ARG VAL 4GPB 125 SEQRES 56 842 GLU ASP VAL ASP ARG LEU ASP GLN ARG GLY TYR ASN ALA 4GPB 126 SEQRES 57 842 GLN GLU TYR TYR ASP ARG ILE PRO GLU LEU ARG GLN ILE 4GPB 127 SEQRES 58 842 ILE GLU GLN LEU SER SER GLY PHE PHE SER PRO LYS GLN 4GPB 128 SEQRES 59 842 PRO ASP LEU PHE LYS ASP ILE VAL ASN MET LEU MET HIS 4GPB 129 SEQRES 60 842 HIS ASP ARG PHE LYS VAL PHE ALA ASP TYR GLU GLU TYR 4GPB 130 SEQRES 61 842 VAL LYS CYS GLN GLU ARG VAL SER ALA LEU TYR LYS ASN 4GPB 131 SEQRES 62 842 PRO ARG GLU TRP THR ARG MET VAL ILE ARG ASN ILE ALA 4GPB 132 SEQRES 63 842 THR SER GLY LYS PHE SER SER ASP ARG THR ILE ALA GLN 4GPB 133 SEQRES 64 842 TYR ALA ARG GLU ILE TRP GLY VAL GLU PRO SER ARG GLN 4GPB 134 SEQRES 65 842 ARG LEU PRO ALA PRO ASP GLU LYS ILE PRO 4GPB 135 FTNOTE 1 4GPB 136 FTNOTE 1 RESIDUE 380 IS LEU IN THE SEQUENCE (K.NAKANO,P.K.HWANG, 4GPB 137 FTNOTE 1 R.J.FLETTERICK, FEBS LETT., V. 204, P. 283, 1986) BUT IT 4GPB 138 FTNOTE 1 HAS BEEN PRESENTED AS ILE IN THIS ENTRY. THIS ASSIGNMENT 4GPB 139 FTNOTE 1 WAS MADE IN THE ORIGINAL STRUCTURE DETERMINATION AT 1.9 4GPB 140 FTNOTE 1 ANGSTROMS (PRESENTED IN PROTEIN DATA BANK ENTRY 1GPB) AND 4GPB 141 FTNOTE 1 CARRIED THROUGH TO THE OTHER ENTRIES. ILE IS MORE 4GPB 142 FTNOTE 1 CONSISTENT WITH THE ELECTRON DENSITY. HOWEVER, THE 4GPB 143 FTNOTE 1 RESOLUTION AT 1.9 ANGSTROMS DOES NOT ALLOW A DEFINITIVE 4GPB 144 FTNOTE 1 ASSIGNMENT. 4GPB 145 HET PLP 999 15 PYRIDOXAL 5(PRIME)-PHOSPHATE 4GPB 146 HET GFP 900 16 ALPHA-D-GLUCOSE-1-PHOSPHATE 4GPB 147 HET GFP 901 16 ALPHA-D-GLUCOSE-1-PHOSPHATE 4GPB 148 FORMUL 2 PLP C8 H10 N1 O6 P1 4GPB 149 FORMUL 3 G1P 2(C6 H10 O8 F1 P1) 4GPB 150 FORMUL 4 HOH *604(H2 O1) 4GPB 151 HELIX 1 H1 GLY 20 THR 38 1 4GPB 152 HELIX 2 H2 THR 47 ASP 78 1 4GPB 153 HELIX 3 H3 THR 94 LEU 102 1 4GPB 154 HELIX 4 H4 LEU 104 LEU 115 1 4GPB 155 HELIX 5 H5 ASP 118 GLU 124 1 4GPB 156 HELIX 6 H6 GLY 134 LEU 150 1 4GPB 157 HELIX 7 H7 GLY 261 ASN 274 1 4GPB 158 HELIX 8 H8 LYS 289 SER 314 1 4GPB 159 HELIX 9 H8B ALA 328 VAL 333 1 4GPB 160 HELIX 10 H9 LEU 344 ASP 355 1 4GPB 161 HELIX 11 H10 ASP 360 CYS 372 1 4GPB 162 HELIX 12 H11 PRO 388 LEU 396 1 4GPB 163 HELIX 13 H12 LEU 396 PHE 418 1 4GPB 164 HELIX 14 H13 GLY 420 SER 429 1 4GPB 165 HELIX 15 H14 ASN 440 GLY 448 1 4GPB 166 HELIX 16 H15 ALA 456 THR 466 1 4GPB 167 HELIX 17 15B PHE 468 GLU 475 1 4GPB 168 HELIX 18 PI PRO 488 CYS 495 3 4GPB 169 HELIX 19 H16 ASN 496 GLY 508 1 4GPB 170 HELIX 20 3TA GLU 509 ASP 514 5 4GPB 171 HELIX 21 3TB ASP 514 VAL 525 5 4GPB 172 HELIX 22 H17 ASP 527 TYR 553 1 4GPB 173 HELIX 23 H18 ARG 575 GLU 593 1 4GPB 174 HELIX 24 H19 TYR 613 ASN 631 1 4GPB 175 HELIX 25 H20 ARG 649 ILE 657 1 4GPB 176 HELIX 26 H21 THR 676 ASN 684 1 4GPB 177 HELIX 27 H22 ALA 695 GLY 704 1 4GPB 178 HELIX 28 H23 ARG 714 GLY 725 1 4GPB 179 HELIX 29 H24 ALA 728 ILE 735 1 4GPB 180 HELIX 30 H25 ILE 735 SER 747 1 4GPB 181 HELIX 31 H26 PHE 758 HIS 768 1 4GPB 182 HELIX 32 H27 ASP 776 LYS 792 1 4GPB 183 HELIX 33 H28 ASN 793 ALA 806 1 4GPB 184 HELIX 34 H29 SER 812 TRP 825 1 4GPB 185 SHEET 1 S1 9 LYS 191 ARG 193 0 4GPB 186 SHEET 2 S1 9 LEU 222 GLY 232 -1 N ASP 227 O LYS 191 4GPB 187 SHEET 3 S1 9 VAL 237 LYS 247 -1 N MET 241 O THR 228 4GPB 188 SHEET 4 S1 9 ALA 153 ARG 160 1 N GLY 158 O ARG 242 4GPB 189 SHEET 5 S1 9 ARG 81 SER 86 1 N TYR 84 O TYR 155 4GPB 190 SHEET 6 S1 9 LYS 332 ASP 339 1 N GLN 336 O TYR 83 4GPB 191 SHEET 7 S1 9 THR 371 ASN 376 1 N ALA 373 O ILE 335 4GPB 192 SHEET 8 S1 9 ALA 451 GLY 454 1 N ASN 453 O TYR 374 4GPB 193 SHEET 9 S1 9 LYS 478 ASN 484 1 N GLN 480 O VAL 452 4GPB 194 SHEET 1 S2 2 ASN 167 CYS 171 0 4GPB 195 SHEET 2 S2 2 TRP 174 GLU 178 -1 N MET 176 O LYS 169 4GPB 196 SHEET 1 S3 2 GLU 162 PHE 163 0 4GPB 197 SHEET 2 S3 2 SER 276 LEU 279 1 O SER 276 N GLU 162 4GPB 198 SHEET 1 S4 2 LEU 198 THR 209 0 4GPB 199 SHEET 2 S4 2 GLY 212 ALA 223 -1 N VAL 216 O ARG 205 4GPB 200 SHEET 1 S5 2 PHE 89 GLY 92 0 4GPB 201 SHEET 2 S5 2 ALA 129 LEU 131 -1 O LEU 131 N PHE 89 4GPB 202 SHEET 1 S6 3 GLU 385 VAL 389 0 4GPB 203 SHEET 2 S6 3 LYS 437 MET 441 -1 N ILE 439 O TRP 387 4GPB 204 SHEET 3 S6 3 LEU 430 GLU 432 -1 N GLU 432 O ARG 438 4GPB 205 SHEET 1 S7 6 ARG 639 LEU 645 0 4GPB 206 SHEET 2 S7 6 PRO 600 LYS 608 1 N ILE 605 O ILE 643 4GPB 207 SHEET 3 S7 6 LEU 562 ILE 570 1 N LYS 568 O GLY 606 4GPB 208 SHEET 4 S7 6 ASP 661 GLN 665 1 N LEU 662 O PHE 563 4GPB 209 SHEET 5 S7 6 LEU 687 THR 691 1 N LEU 687 O ASP 661 4GPB 210 SHEET 6 S7 6 PHE 709 PHE 711 1 N PHE 709 O THR 688 4GPB 211 TURN 1 T1 ASP 42 VAL 45 TYPE I 4GPB 212 TURN 2 T2 PHE 89 MET 91 REVERSE GAMMA 4GPB 213 TURN 3 T3 CYS 171 TRP 174 TYPE I' 4GPB 214 TURN 4 T4 ASP 181 ARG 184 TYPE I 4GPB 215 TURN 5 T5 TRP 182 TRP 182 REVERSE GAMMA 4GPB 216 TURN 6 T6 LEU 183 GLY 186 TYPE I 4GPB 217 TURN 7 T7 ASN 187 GLU 190 TYPE I 4GPB 218 TURN 8 T8 ARG 193 PHE 196 TYPE I 4GPB 219 TURN 9 T9 THR 209 GLN 211 GAMMA 4GPB 220 TURN 10 T10 ASP 251 ASN 253 GAMMA 4GPB 221 TURN 11 T11 GLU 287 LYS 289 REVERSE GAMMA 4GPB 222 TURN 12 T12 PHE 326 PHE 329 TYPE I 4GPB 223 TURN 13 T13 THR 340 SER 343 TYPE I 4GPB 224 TURN 14 T14 ILE 380 ALA 383 TYPE III 4GPB 225 TURN 15 T15 PRO 381 LEU 384 TYPE I 4GPB 226 TURN 16 T16 PHE 418 ASP 421 TYPE II 4GPB 227 TURN 17 T17 GLY 420 VAL 422 REVERSE GAMMA 4GPB 228 TURN 18 T18 GLU 475 LYS 478 TYPE III 4GPB 229 TURN 19 T19 PRO 476 PHE 479 TYPE III 4GPB 230 TURN 20 T20 TYR 511 ASP 514 TYPE IV 4GPB 231 TURN 21 T21 GLU 572 ARG 575 TYPE III 4GPB 232 TURN 22 T22 GLU 593 LYS 596 TYPE I 4GPB 233 TURN 23 T23 ALA 610 TYR 613 TYPE II 4GPB 234 TURN 24 T24 GLY 612 HIS 614 REVERSE GAMMA 4GPB 235 TURN 25 T25 VAL 630 ASP 633 TYPE I 4GPB 236 TURN 26 T26 ASP 633 VAL 636 TYPE III 4GPB 237 TURN 27 T27 ILE 657 ALA 660 TYPE I 4GPB 238 TURN 28 T28 THR 668 THR 671 TYPE II 4GPB 239 TURN 29 T29 ASP 693 ASN 696 TYPE II' 4GPB 240 TURN 30 T30 GLY 704 ASN 707 TYPE III 4GPB 241 TURN 31 T31 GLU 705 PHE 708 TYPE I 4GPB 242 TURN 32 T32 GLY 748 SER 751 TYPE I 4GPB 243 TURN 33 T33 GLN 754 LEU 757 TYPE I 4GPB 244 TURN 34 T34 ASP 756 LYS 759 TYPE I 4GPB 245 TURN 35 T35 ASP 769 LYS 772 TYPE I 4GPB 246 TURN 36 T36 VAL 773 ASP 776 TYPE III 4GPB 247 TURN 37 T37 PHE 774 TYR 777 TYPE I 4GPB 248 TURN 38 T38 ILE 805 SER 808 TYPE I 4GPB 249 TURN 39 T39 SER 808 PHE 811 TYPE III 4GPB 250 TURN 40 T40 GLY 809 SER 812 TYPE I 4GPB 251 CRYST1 128.500 128.500 116.300 90.00 90.00 90.00 P 43 21 2 8 4GPB 252 ORIGX1 1.000000 0.000000 0.000000 0.00000 4GPB 253 ORIGX2 0.000000 1.000000 0.000000 0.00000 4GPB 254 ORIGX3 0.000000 0.000000 1.000000 0.00000 4GPB 255 SCALE1 0.007782 0.000000 0.000000 0.00000 4GPB 256 SCALE2 0.000000 0.007782 0.000000 0.00000 4GPB 257 SCALE3 0.000000 0.000000 0.008598 0.00000 4GPB 258