HEADER OXIDOREDUCTASE(CHOH(D)-NAD(A)) 25-NOV-87 1LDM 1LDM 3 COMPND M=4= LACTATE DEHYDROGENASE (E.C.1.1.1.27) TERNARY COMPLEX 1LDM 4 COMPND 2 WITH /NAD$ AND OXAMATE 1LDM 5 SOURCE DOGFISH (SQUALUS $ACANTHIAS) MUSCLE 1LDM 6 AUTHOR J.P.GRIFFITH,M.G.ROSSMANN 1LDM 7 REVDAT 2 15-APR-90 1LDMA 1 FORMUL 1LDMA 1 REVDAT 1 12-JUL-89 1LDM 0 1LDM 8 REMARK 1 1LDM 9 REMARK 1 REFERENCE 1 1LDM 10 REMARK 1 AUTH C.ABAD-*ZAPATERO,J.P.GRIFFITH,J.L.SUSSMAN, 1LDM 11 REMARK 1 AUTH 2 M.G.ROSSMANN 1LDM 12 REMARK 1 TITL REFINED CRYSTAL STRUCTURE OF DOGFISH M=4= 1LDM 13 REMARK 1 TITL 2 APO-LACTATE DEHYDROGENASE 1LDM 14 REMARK 1 REF J.MOL.BIOL. V. 198 445 1987 1LDM 15 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1LDM 16 REMARK 1 REFERENCE 2 1LDM 17 REMARK 1 AUTH J.L.WHITE,M.L.HACKERT,M.BUEHNER,M.J.ADAMS,G.C.FORD, 1LDM 18 REMARK 1 AUTH 2 P.J.LENTZ *JUNIOR,I.E.SMILEY,S.J.STEINDEL, 1LDM 19 REMARK 1 AUTH 3 M.G.ROSSMANN 1LDM 20 REMARK 1 TITL A COMPARISON OF THE STRUCTURES OF APO DOGFISH 1LDM 21 REMARK 1 TITL 2 M=4= LACTATE DEHYDROGENASE AND ITS TERNARY 1LDM 22 REMARK 1 TITL 3 COMPLEXES 1LDM 23 REMARK 1 REF J.MOL.BIOL. V. 102 759 1976 1LDM 24 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1LDM 25 REMARK 1 REFERENCE 3 1LDM 26 REMARK 1 AUTH W.EVENTOFF,M.G.ROSSMANN,S.S.TAYLOR,H.-*J.TORFF, 1LDM 27 REMARK 1 AUTH 2 H.MEYER,W.KEIL,H.-*H.KILTZ 1LDM 28 REMARK 1 TITL STRUCTURAL ADAPTATIONS OF LACTATE DEHYDROGENASE 1LDM 29 REMARK 1 TITL 2 ISOZYMES 1LDM 30 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 74 2677 1977 1LDM 31 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 1LDM 32 REMARK 1 REFERENCE 4 1LDM 33 REMARK 1 AUTH J.WHITE,M.G.ROSSMANN,G.C.FORD 1LDM 34 REMARK 1 TITL A 5 ANGSTROMS X-RAY DIFFRACTION STUDY OF COENZYME- 1LDM 35 REMARK 1 TITL 2 DEFICIENT LACTATE DEHYDROGENASE,/NAD$-PYRUVATE 1LDM 36 REMARK 1 TITL 3 TERNARY COMPLEX 1LDM 37 REMARK 1 REF J.MOL.BIOL. V. 98 259 1975 1LDM 38 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1LDM 39 REMARK 1 REFERENCE 5 1LDM 40 REMARK 1 AUTH W.EVENTOFF,M.L.HACKERT,S.J.STEINDEL,M.G.ROSSMANN 1LDM 41 REMARK 1 TITL A STRUCTURAL COMPARISON OF PORCINE B=4= AND 1LDM 42 REMARK 1 TITL 2 DOGFISH A=4= ISOZYMES OF LACTATE DEHYDROGENASE 1LDM 43 REMARK 1 EDIT C.L.MARKERT 1LDM 44 REMARK 1 REF ISOZYMES-MOLECULAR STRUCTURE V. 1 137 1975 1LDM 45 REMARK 1 PUBL ACADEMIC PRESS,NEW YORK 1LDM 46 REMARK 1 REFN ISBN 0-12-472701-8 979 1LDM 47 REMARK 1 REFERENCE 6 1LDM 48 REMARK 1 AUTH J.J.HOLBROOK,A.LILJAS,S.J.STEINDEL,M.G.ROSSMANN 1LDM 49 REMARK 1 TITL LACTATE DEHYDROGENASE 1LDM 50 REMARK 1 EDIT P.D.BOYER 1LDM 51 REMARK 1 REF THE ENZYMES,THIRD EDITION V. 11 191 1975 1LDM 52 REMARK 1 PUBL ACADEMIC PRESS,NEW YORK 1LDM 53 REMARK 1 REFN ISBN 0-12-122711-1 436 1LDM 54 REMARK 1 REFERENCE 7 1LDM 55 REMARK 1 AUTH A.LILJAS,M.G.ROSSMANN 1LDM 56 REMARK 1 TITL X-RAY STUDIES OF PROTEIN INTERACTIONS 1LDM 57 REMARK 1 REF ANNU.REV.BIOCHEM. V. 43 475 1974 1LDM 58 REMARK 1 REFN ASTM ARBOAW US ISSN 0066-4154 413 1LDM 59 REMARK 1 REFERENCE 8 1LDM 60 REMARK 1 AUTH M.G.ROSSMANN,D.MORAS,K.W.OLSEN 1LDM 61 REMARK 1 TITL CHEMICAL AND BIOLOGICAL EVOLUTION OF A NUCLEOTIDE 1LDM 62 REMARK 1 TITL 2 BINDING PROTEIN 1LDM 63 REMARK 1 REF NATURE V. 250 194 1974 1LDM 64 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 1LDM 65 REMARK 1 REFERENCE 9 1LDM 66 REMARK 1 AUTH M.G.ROSSMANN,A.LILJAS 1LDM 67 REMARK 1 TITL RECOGNITION OF STRUCTURAL DOMAINS IN GLOBULAR 1LDM 68 REMARK 1 TITL 2 PROTEINS 1LDM 69 REMARK 1 REF J.MOL.BIOL. V. 85 177 1974 1LDM 70 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1LDM 71 REMARK 1 REFERENCE 10 1LDM 72 REMARK 1 AUTH M.J.ADAMS,G.C.FORD,A.LILJAS,M.G.ROSSMANN 1LDM 73 REMARK 1 TITL ATOMIC CO-ORDINATES FOR DOGFISH M=4= APO-LACTATE 1LDM 74 REMARK 1 TITL 2 DEHYDROGENASE 1LDM 75 REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMM. V. 53 46 1973 1LDM 76 REMARK 1 REFN ASTM BBRCA9 US ISSN 0006-291X 146 1LDM 77 REMARK 1 REFERENCE 11 1LDM 78 REMARK 1 AUTH M.J.ADAMS,M.BUEHNER,K.CHANDRASEKHAR,G.C.FORD, 1LDM 79 REMARK 1 AUTH 2 M.L.HACKERT,A.LILJAS,M.G.ROSSMANN,I.E.SMILEY, 1LDM 80 REMARK 1 AUTH 3 W.S.ALLISON,J.EVERSE,N.O.KAPLAN,S.S.TAYLOR 1LDM 81 REMARK 1 TITL STRUCTURE-FUNCTION RELATIONSHIPS IN LACTATE 1LDM 82 REMARK 1 TITL 2 DEHYDROGENASE 1LDM 83 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 70 1968 1973 1LDM 84 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 1LDM 85 REMARK 1 REFERENCE 12 1LDM 86 REMARK 1 AUTH S.S.TAYLOR,S.S.OXLEY,W.S.ALLISON,N.O.KAPLAN 1LDM 87 REMARK 1 TITL AMINO-ACID SEQUENCE OF DOGFISH M=4= LACTATE 1LDM 88 REMARK 1 TITL 2 DEHYDROGENASE 1LDM 89 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 70 1790 1973 1LDM 90 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 1LDM 91 REMARK 1 REFERENCE 13 1LDM 92 REMARK 1 AUTH M.G.ROSSMANN,M.J.ADAMS,M.BUEHNER,G.C.FORD, 1LDM 93 REMARK 1 AUTH 2 M.L.HACKERT,A.LILJAS,S.T.RAO,L.J.BANASZAK,E.HILL, 1LDM 94 REMARK 1 AUTH 3 D.TSERNOGLOU,L.WEBB 1LDM 95 REMARK 1 TITL MOLECULAR SYMMETRY AXES AND SUBUNIT INTERFACES IN 1LDM 96 REMARK 1 TITL 2 CERTAIN DEHYDROGENASES 1LDM 97 REMARK 1 REF J.MOL.BIOL. V. 76 533 1973 1LDM 98 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1LDM 99 REMARK 1 REFERENCE 14 1LDM 100 REMARK 1 AUTH M.J.ADAMS,A.LILJAS,M.G.ROSSMANN 1LDM 101 REMARK 1 TITL FUNCTIONAL ANION BINDING SITES IN DOGFISH M=4= 1LDM 102 REMARK 1 TITL 2 LACTATE DEHYDROGENASE 1LDM 103 REMARK 1 REF J.MOL.BIOL. V. 76 519 1973 1LDM 104 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1LDM 105 REMARK 1 REFERENCE 15 1LDM 106 REMARK 1 AUTH A.MC*PHERSON *JUNIOR 1LDM 107 REMARK 1 TITL BINDING OF OXAMATE TO THE APOENZYME OF DOGFISH 1LDM 108 REMARK 1 TITL 2 M=4= LACTATE DEHYDROGENASE 1LDM 109 REMARK 1 REF J.MOL.BIOL. V. 76 528 1973 1LDM 110 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1LDM 111 REMARK 1 REFERENCE 16 1LDM 112 REMARK 1 AUTH K.CHANDRASEKHAR,A.MC*PHERSON *JUNIOR,M.J.ADAMS, 1LDM 113 REMARK 1 AUTH 2 M.G.ROSSMANN 1LDM 114 REMARK 1 TITL CONFORMATION OF COENZYME FRAGMENTS WHEN BOUND TO 1LDM 115 REMARK 1 TITL 2 LACTATE DEHYDROGENASE 1LDM 116 REMARK 1 REF J.MOL.BIOL. V. 76 503 1973 1LDM 117 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1LDM 118 REMARK 1 REFERENCE 17 1LDM 119 REMARK 1 AUTH I.E.SMILEY,R.KOEKOEK,M.J.ADAMS,M.G.ROSSMANN 1LDM 120 REMARK 1 TITL THE 5 ANGSTROMS RESOLUTION STRUCTURE OF AN 1LDM 121 REMARK 1 TITL 2 ABORTIVE TERNARY COMPLEX OF LACTATE DEHYDROGENASE 1LDM 122 REMARK 1 TITL 3 AND ITS COMPARISON WITH THE APO-$ENZYME 1LDM 123 REMARK 1 REF J.MOL.BIOL. V. 55 467 1971 1LDM 124 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1LDM 125 REMARK 1 REFERENCE 18 1LDM 126 REMARK 1 AUTH M.J.ADAMS,G.C.FORD,R.KOEKOEK,P.J.LENTZ *JUNIOR, 1LDM 127 REMARK 1 AUTH 2 A.MC*PHERSON *JUNIOR,M.G.ROSSMANN,I.E.SMILEY, 1LDM 128 REMARK 1 AUTH 3 R.W.SCHEVITZ,A.J.WONACOTT 1LDM 129 REMARK 1 TITL STRUCTURE OF LACTATE DEHYDROGENASE AT 1LDM 130 REMARK 1 TITL 2 2.8 ANGSTROMS RESOLUTION 1LDM 131 REMARK 1 REF NATURE V. 227 1098 1970 1LDM 132 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 1LDM 133 REMARK 1 REFERENCE 19 1LDM 134 REMARK 1 AUTH M.J.ADAMS,D.J.HAAS,B.A.JEFFERY, 1LDM 135 REMARK 1 AUTH 2 A.MC*PHERSON *JUNIOR,H.L.MERMALL,M.G.ROSSMANN, 1LDM 136 REMARK 1 AUTH 3 R.W.SCHEVITZ,A.J.WONACOTT 1LDM 137 REMARK 1 TITL LOW RESOLUTION STUDY OF CRYSTALLINE L-LACTATE 1LDM 138 REMARK 1 TITL 2 DEHYDROGENASE 1LDM 139 REMARK 1 REF J.MOL.BIOL. V. 41 159 1969 1LDM 140 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1LDM 141 REMARK 1 REFERENCE 20 1LDM 142 REMARK 1 AUTH M.G.ROSSMANN,B.A.JEFFERY,P.MAIN,S.WARREN 1LDM 143 REMARK 1 TITL THE CRYSTAL STRUCTURE OF LACTIC DEHYDROGENASE 1LDM 144 REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 57 515 1967 1LDM 145 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 1LDM 146 REMARK 2 1LDM 147 REMARK 2 RESOLUTION. 2.1 ANGSTROMS. 1LDM 148 REMARK 3 1LDM 149 REMARK 3 REFINEMENT. BY THE RESTRAINED LEAST SQUARES PROCEDURE OF J. 1LDM 150 REMARK 3 KONNERT AND W. HENDRICKSON (PROGRAM *PROLSQ*). THE R 1LDM 151 REMARK 3 VALUE IS 0.173 FOR REFLECTIONS IN THE RESOLUTION 1LDM 152 REMARK 3 RANGE 6.0 TO 2.1 ANGSTROMS. ATOMS WITH THERMAL FACTORS 1LDM 153 REMARK 3 WHICH CALCULATE LESS THAN 2.00 ARE ASSIGNED THIS VALUE. 1LDM 154 REMARK 3 THIS IS THE LOWEST VALUE ALLOWED BY THE REFINEMENT 1LDM 155 REMARK 3 PROGRAM. 1LDM 156 REMARK 3 1LDM 157 REMARK 3 NUMBER OF PROTEIN ATOMS 2542 1LDM 158 REMARK 3 NUMBER OF SOLVENT ATOMS 245 1LDM 159 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 1LDM 160 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 1LDM 161 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 1LDM 162 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 1LDM 163 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 1LDM 164 REMARK 3 BOND DISTANCE 0.018(0.030) 1LDM 165 REMARK 3 ANGLE DISTANCE 0.048(0.040) 1LDM 166 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 1LDM 167 REMARK 3 SINGLE TORSION CONTACT 0.213(0.500) 1LDM 168 REMARK 3 MULTIPLE TORSION CONTACT 0.267(0.500) 1LDM 169 REMARK 3 POSSIBLE HYDROGEN BOND 0.260(0.500) 1LDM 170 REMARK 4 1LDM 171 REMARK 4 THE COORDINATES OF THIS ENTRY ARE BASED ON THE RIGHT-HANDED 1LDM 172 REMARK 4 P,Q,R AXES DEFINED IN REFERENCE 13 ABOVE. THE *SCALE* 1LDM 173 REMARK 4 TRANSFORMATION GIVEN BELOW CAN BE USED TO EXPRESS THIS 1LDM 174 REMARK 4 STRUCTURE IN FRACTIONAL COORDINATES WITH RESPECT TO A SET 1LDM 175 REMARK 4 OF LEFT-HANDED AXES IN SPACE GROUP C 4 21 2 . 1LDM 176 REMARK 5 1LDM 177 REMARK 5 SPACE GROUP C 4 21 2 (WHICH, MORE PROPERLY, SHOULD BE NAMED 1LDM 178 REMARK 5 C 4 2 21) IS A NON-STANDARD REPRESENTATION OF SPACE GROUP 1LDM 179 REMARK 5 P 4 21 2. IN THIS CASE THE AXES OF THE UNIT CELL ARE 1LDM 180 REMARK 5 CONSIDERED TO BE LEFT-HANDED. 1LDM 181 REMARK 6 1LDM 182 REMARK 6 NON-CRYSTALLOGRAPHIC SYMMETRY ELEMENTS CORRESPONDING TO THE 1LDM 183 REMARK 6 THREE ORTHOGONAL MOLECULAR SYMMETRY AXES ARE PRESENTED ON 1LDM 184 REMARK 6 THE *MTRIX* RECORDS BELOW. 1LDM 185 REMARK 7 1LDM 186 REMARK 7 THE RESIDUES IN THIS ENTRY ARE NUMBERED SEQUENTIALLY FROM 1LDM 187 REMARK 7 1 - 329. SEE THE PAPER CITED AS REFERENCE 1 ABOVE FOR AN 1LDM 188 REMARK 7 EXPLANATION OF THE NUMBERING SYSTEM USED IN SOME EARLIER 1LDM 189 REMARK 7 LDH ENTRIES. 1LDM 190 REMARK 8 1LDM 191 REMARK 8 THERE ARE SEVERAL SEQUENCE DIFFERENCES BETWEEN *PIR* AND 1LDM 192 REMARK 8 THIS ENTRY AS FOLLOWS 1LDM 193 REMARK 8 1LDM 194 REMARK 8 RESIDUE PIR ENTRY 1LDM 195 REMARK 8 205 TRP ASN 1LDM 196 REMARK 8 206 ASN VAL 1LDM 197 REMARK 8 208 LEU SER 1LDM 198 REMARK 8 209 LYS ILE 1LDM 199 REMARK 8 210 GLU LYS 1LDM 200 REMARK 8 214 GLU LEU 1LDM 201 REMARK 8 215 LEU ASP 1LDM 202 REMARK 8 308 ASP ASN 1LDM 203 REMARK 8 1LDM 204 REMARK 8 SEE REFERENCE 1 ABOVE FOR A DISCUSSION OF SOME OF THESE 1LDM 205 REMARK 8 DIFFERENCES. 1LDM 206 REMARK 9 1LDM 207 REMARK 9 STRUCTURE FACTORS CORRESPONDING TO THIS ENTRY ARE AVAILABLE 1LDM 208 REMARK 9 FROM THE PROTEIN DATA BANK AS A SEPARATE ENTRY. 1LDM 209 REMARK 10 1LDMA 2 REMARK 10 CORRECTION. CORRECT FORMAT OF *FORMUL* RECORDS. 15-APR-90. 1LDMA 3 SEQRES 1 329 ALA THR LEU LYS ASP LYS LEU ILE GLY HIS LEU ALA THR 1LDM 210 SEQRES 2 329 SER GLN GLU PRO ARG SER TYR ASN LYS ILE THR VAL VAL 1LDM 211 SEQRES 3 329 GLY VAL GLY ALA VAL GLY MET ALA CYS ALA ILE SER ILE 1LDM 212 SEQRES 4 329 LEU MET LYS ASP LEU ALA ASP GLU VAL ALA LEU VAL ASP 1LDM 213 SEQRES 5 329 VAL MET GLU ASP LYS LEU LYS GLY GLU MET MET ASP LEU 1LDM 214 SEQRES 6 329 GLN HIS GLY SER LEU PHE LEU HIS THR ALA LYS ILE VAL 1LDM 215 SEQRES 7 329 SER GLY LYS ASP TYR SER VAL SER ALA GLY SER LYS LEU 1LDM 216 SEQRES 8 329 VAL VAL ILE THR ALA GLY ALA ARG GLN GLN GLU GLY GLU 1LDM 217 SEQRES 9 329 SER ARG LEU ASN LEU VAL GLN ARG ASN VAL ASN ILE PHE 1LDM 218 SEQRES 10 329 LYS PHE ILE ILE PRO ASN ILE VAL LYS HIS SER PRO ASP 1LDM 219 SEQRES 11 329 CYS ILE ILE LEU VAL VAL SER ASN PRO VAL ASP VAL LEU 1LDM 220 SEQRES 12 329 THR TYR VAL ALA TRP LYS LEU SER GLY LEU PRO MET HIS 1LDM 221 SEQRES 13 329 ARG ILE ILE GLY SER GLY CYS ASN LEU ASP SER ALA ARG 1LDM 222 SEQRES 14 329 PHE ARG TYR LEU MET GLY GLU ARG LEU GLY VAL HIS SER 1LDM 223 SEQRES 15 329 CYS SER CYS HIS GLY TRP VAL ILE GLY GLU HIS GLY ASP 1LDM 224 SEQRES 16 329 SER VAL PRO SER VAL TRP SER GLY MET ASN VAL ALA SER 1LDM 225 SEQRES 17 329 ILE LYS LEU HIS PRO LEU ASP GLY THR ASN LYS ASP LYS 1LDM 226 SEQRES 18 329 GLN ASP TRP LYS LYS LEU HIS LYS ASP VAL VAL ASP SER 1LDM 227 SEQRES 19 329 ALA TYR GLU VAL ILE LYS LEU LYS GLY TYR THR SER TRP 1LDM 228 SEQRES 20 329 ALA ILE GLY LEU SER VAL ALA ASP LEU ALA GLU THR ILE 1LDM 229 SEQRES 21 329 MET LYS ASN LEU CYS ARG VAL HIS PRO VAL SER THR MET 1LDM 230 SEQRES 22 329 VAL LYS ASP PHE TYR GLY ILE LYS ASP ASN VAL PHE LEU 1LDM 231 SEQRES 23 329 SER LEU PRO CYS VAL LEU ASN ASP HIS GLY ILE SER ASN 1LDM 232 SEQRES 24 329 ILE VAL LYS MET LYS LEU LYS PRO ASN GLU GLU GLN GLN 1LDM 233 SEQRES 25 329 LEU GLN LYS SER ALA THR THR LEU TRP ASP ILE GLN LYS 1LDM 234 SEQRES 26 329 ASP LEU LYS PHE 1LDM 235 FTNOTE 1 1LDM 236 FTNOTE 1 RESIDUE PRO 139 IS A CIS PROLINE. 1LDM 237 HET NAD 1 44 NICOTINAMIDE-ADENINE-DINUCLEOTIDE 1LDM 238 HET OXM 2 6 OXAMATE 1LDM 239 HET OXM 3 6 OXAMATE 1LDM 240 FORMUL 2 NAD C21 H28 N7 O14 P2 1LDMA 4 FORMUL 3 OXM 2(C2 H3 N1 O3) 1LDMA 5 FORMUL 4 HOH *245(H2 O1) 1LDM 243 HELIX 1 AA THR 2 ILE 8 1 1LDM 244 HELIX 2 AB GLY 29 ASP 43 1 1LDM 245 HELIX 3 AC MET 54 SER 69 1 1LDM 246 HELIX 4 AD GLY 103 ILE 121 1 3/10 HELIX 103-111 1LDM 247 HELIX 5 AE PHE 119 SER 128 1 CONTIGUOUS WITH HELIX AD 1LDM 248 HELIX 6 A1F VAL 140 GLY 152 1 SHORTER IN APO 1LDM 249 HELIX 7 A2F CYS 163 GLY 179 1 3 H BONDS IN MIDDL ABSENT APO 1LDM 250 HELIX 8 A1G TRP 224 TYR 236 1 3/10 H-BOND 234-237 1LDM 251 HELIX 9 A2G VAL 238 GLY 243 5 1LDM 252 HELIX 10 A3G ALA 248 ASN 263 1 3/10 H-BOND 248-251 1LDM 253 HELIX 11 AH PRO 307 ILE 323 1 1LDM 254 SHEET 1 SH1 6 LYS 76 GLY 80 0 1LDM 255 SHEET 2 SH1 6 GLU 47 VAL 51 1 N LEU 50 O VAL 78 1LDM 256 SHEET 3 SH1 6 ASN 21 VAL 26 1 N VAL 25 O ALA 49 1LDM 257 SHEET 4 SH1 6 LYS 90 ILE 94 1 N VAL 93 O THR 24 1LDM 258 SHEET 5 SH1 6 ILE 132 VAL 136 1 N LEU 134 O VAL 92 1LDM 259 SHEET 6 SH1 6 ARG 157 GLY 160 1 N ILE 159 O ILE 133 1LDM 260 SHEET 1 SH2 3 SER 184 TRP 188 0 1LDM 261 SHEET 2 SH2 3 GLY 203 VAL 206 -1 N ASN 205 O SER 184 1LDM 262 SHEET 3 SH2 3 ILE 209 LEU 211 -1 O ILE 209 N VAL 206 1LDM 263 SHEET 1 SH3 3 LEU 264 MET 273 0 1LDM 264 SHEET 2 SH3 3 ASN 283 ASN 293 -1 N CYS 290 O VAL 267 1LDM 265 SHEET 3 SH3 3 HIS 295 VAL 301 -1 N ASN 299 O CYS 290 1LDM 266 TURN 1 T1 ALA 1 LEU 3 1LDM 267 TURN 2 T2 HIS 10 THR 13 TYPE O (VII) 1LDM 268 TURN 3 T3 ALA 30 MET 33 TYPE NR (IV) 1LDM 269 TURN 4 T4 SER 84 ALA 87 TYPE NR (IV) 1LDM 270 TURN 5 T5 SER 86 SER 89 TYPE O (IV) 1LDM 271 TURN 6 T6 SER 89 VAL 92 TYPE O (IV) 1LDM 272 TURN 7 T7 GLN 101 GLU 104 TYPE O (IV) 1LDM 273 TURN 8 T8 VAL 125 SER 128 TYPE NR (IV) 1LDM 274 TURN 9 T9 HIS 127 ASP 130 TYPE O (VI) 1LDM 275 TURN 10 T10 SER 137 VAL 140 TYPE O (VI) 1LDM 276 TURN 11 T11 MET 155 ILE 158 TYPE NR (IV) 1LDM 277 TURN 12 T12 SER 161 ASN 164 TYPE O (IV) 1LDM 278 TURN 13 T13 VAL 180 CYS 183 TYPE O (VII) 1LDM 279 TURN 14 T14 SER 182 CYS 185 TYPE NR (VI) 1LDM 280 TURN 15 T15 GLY 194 VAL 197 TYPE NR (IV) 1LDM 281 TURN 16 T16 TRP 201 MET 204 TYPE NR (IV) 1LDM 282 TURN 17 T17 VAL 206 ILE 209 TYPE NR (IV) 1LDM 283 TURN 18 T18 HIS 212 ASP 215 TYPE NR (IV) 1LDM 284 TURN 19 T19 PRO 213 GLY 216 TYPE NR (IV) 1LDM 285 TURN 20 T20 ASN 218 LYS 221 TYPE O (IV) 1LDM 286 TURN 21 T21 ILE 239 LYS 242 TYPE NR (IV) 1LDM 287 TURN 22 T22 SER 246 ILE 249 TYPE O (IV) 1LDM 288 TURN 23 T23 THR 259 LYS 262 TYPE NR (IV) 1LDM 289 TURN 24 T24 LEU 292 HIS 295 TYPE NR (IV) 1LDM 290 TURN 25 T25 LYS 306 GLU 309 TYPE NR (IV) 1LDM 291 TURN 26 T26 GLN 324 LEU 327 TYPE NR (IV) 1LDM 292 CRYST1 134.500 134.500 85.900 90.00 90.00 90.00 C 4 21 2 16 1LDM 293 ORIGX1 1.000000 0.000000 0.000000 0.00000 1LDM 294 ORIGX2 0.000000 1.000000 0.000000 0.00000 1LDM 295 ORIGX3 0.000000 0.000000 1.000000 0.00000 1LDM 296 SCALE1 0.007435 0.010515 0.010515 0.00000 1LDM 297 SCALE2 0.007435 0.000000 0.010515 0.00000 1LDM 298 SCALE3 -0.011641 0.000000 0.000000 0.00000 1LDM 299 MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1LDM 300 MTRIX2 1 0.000000 -1.000000 0.000000 0.00000 1LDM 301 MTRIX3 1 0.000000 0.000000 -1.000000 0.00000 1LDM 302 MTRIX1 2 -1.000000 0.000000 0.000000 0.00000 1LDM 303 MTRIX2 2 0.000000 1.000000 0.000000 0.00000 1LDM 304 MTRIX3 2 0.000000 0.000000 -1.000000 0.00000 1LDM 305 MTRIX1 3 -1.000000 0.000000 0.000000 0.00000 1LDM 306 MTRIX2 3 0.000000 -1.000000 0.000000 0.00000 1LDM 307 MTRIX3 3 0.000000 0.000000 1.000000 0.00000 1LDM 308