HEADER HYDROLASE 03-JUN-94 3GLY 3GLY 2 COMPND GLUCOAMYLASE-471 (1,4-ALPHA-D-GLUCAN GLUCOHYDROLASE) 3GLY 3 COMPND 2 (E.C.3.2.1.3) 3GLY 4 SOURCE (ASPERGILLUS AWAMORI) VARIANT X100 3GLY 5 AUTHOR A.E.ALESHIN,C.HOFFMAN,L.M.FIRSOV,R.B.HONZATKO 3GLY 6 REVDAT 1 01-NOV-94 3GLY 0 3GLY 7 SPRSDE 01-NOV-94 3GLY 1GLY 3GLY 8 JRNL AUTH A.E.ALESHIN,C.HOFFMAN,L.M.FIRSOV,R.B.HONZATKO 3GLY 9 JRNL TITL REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM 3GLY 10 JRNL TITL 2 ASPERGILLUS AWAMORI VAR. X100 3GLY 11 JRNL REF J.MOL.BIOL. V. 238 575 1994 3GLY 12 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 0070 3GLY 13 REMARK 1 3GLY 14 REMARK 1 REFERENCE 1 3GLY 15 REMARK 1 AUTH A.E.ALESHIN,L.M.FIRSOV,R.B.HONZATKO 3GLY 16 REMARK 1 TITL REFINED STRUCTURE FOR THE COMPLEX OF ACARBOSE WITH 3GLY 17 REMARK 1 TITL 2 GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100 TO 3GLY 18 REMARK 1 TITL 3 2.4 ANGSTROMS RESOLUTION 3GLY 19 REMARK 1 REF J.BIOL.CHEM. V. 269 15631 1994 3GLY 20 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 3GLY 21 REMARK 1 REFERENCE 2 3GLY 22 REMARK 1 AUTH E.M.S.HARRIS,A.E.ALESHIN,L.M.FIRSOV,R.B.HONZATKO 3GLY 23 REMARK 1 TITL REFINED STRUCTURE OF THE COMPLEX OF 3GLY 24 REMARK 1 TITL 2 1-DEOXYNOJIRIMYCIN WITH GLUCOAMYLASE FROM 3GLY 25 REMARK 1 TITL 3 ASPERGILLUS AWAMORI VAR. X100 TO 2.4 ANGSTROMS 3GLY 26 REMARK 1 TITL 4 RESOLUTION 3GLY 27 REMARK 1 REF BIOCHEMISTRY V. 32 1618 1993 3GLY 28 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 3GLY 29 REMARK 1 REFERENCE 3 3GLY 30 REMARK 1 AUTH A.E.ALESHIN,A.GOLUBEV,L.M.FIRSOV,R.B.HONZATKO 3GLY 31 REMARK 1 TITL CRYSTAL STRUCTURE OF GLUCOAMYLASE FROM 3GLY 32 REMARK 1 TITL 2 ASPERGILLUS AWAMORI VAR. X100 TO 2.2 ANGSTROMS 3GLY 33 REMARK 1 TITL 3 RESOLUTION 3GLY 34 REMARK 1 REF J.BIOL.CHEM. V. 267 19291 1992 3GLY 35 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 3GLY 36 REMARK 2 3GLY 37 REMARK 2 RESOLUTION. 2.2 ANGSTROMS. 3GLY 38 REMARK 3 3GLY 39 REMARK 3 REFINEMENT. 3GLY 40 REMARK 3 PROGRAM PROLSQ 3GLY 41 REMARK 3 AUTHORS KONNERT,HENDRICKSON 3GLY 42 REMARK 3 R VALUE 0.141 3GLY 43 REMARK 3 RMSD BOND DISTANCES 0.014 ANGSTROMS 3GLY 44 REMARK 3 RMSD BOND ANGLES 1.3 DEGREES 3GLY 45 REMARK 3 3GLY 46 REMARK 3 NUMBER OF REFLECTIONS 30205 3GLY 47 REMARK 3 RESOLUTION RANGE 10.0 - 2.2 ANGSTROMS 3GLY 48 REMARK 3 DATA CUTOFF 1.0 SIGMA(F) 3GLY 49 REMARK 3 PERCENT COMPLETION 88 3GLY 50 REMARK 3 3GLY 51 REMARK 3 NUMBER OF PROTEIN ATOMS 4517 3GLY 52 REMARK 3 NUMBER OF SOLVENT ATOMS 673 3GLY 53 REMARK 3 3GLY 54 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 3GLY 55 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 3GLY 56 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 3GLY 57 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 3GLY 58 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 3GLY 59 REMARK 3 BOND DISTANCE 0.014(0.020) 3GLY 60 REMARK 3 ANGLE DISTANCE 0.029(0.030) 3GLY 61 REMARK 3 PLANAR 1-4 DISTANCE 0.039(0.050) 3GLY 62 REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.012(0.020) 3GLY 63 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.138(0.150) 3GLY 64 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 3GLY 65 REMARK 3 SINGLE TORSION CONTACT 0.221(0.250) 3GLY 66 REMARK 3 MULTIPLE TORSION CONTACT 0.155(0.250) 3GLY 67 REMARK 3 POSSIBLE HYDROGEN BOND 0.192(0.250) 3GLY 68 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 3GLY 69 REMARK 3 PLANAR 2.300(3.000) 3GLY 70 REMARK 3 STAGGERED 13.60(15.00) 3GLY 71 REMARK 3 ORTHONORMAL 27.60(20.00) 3GLY 72 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) 3GLY 73 REMARK 3 MAIN-CHAIN BOND 0.628(1.000) 3GLY 74 REMARK 3 MAIN-CHAIN ANGLE 1.018(1.500) 3GLY 75 REMARK 3 SIDE-CHAIN BOND 1.898(2.000) 3GLY 76 REMARK 3 SIDE-CHAIN ANGLE 2.739(3.000) 3GLY 77 REMARK 4 3GLY 78 REMARK 4 THE POLYPEPTIDE CHAIN FOLDS INTO AN ALPHA/ALPHA-BARREL, 3GLY 79 REMARK 4 COMPRISING 12 HELICES. THE SEQUENCE USED IN THE 3GLY 80 REMARK 4 MODELING IS THAT OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI 3GLY 81 REMARK 4 VAR. KAWACHI (SEE REFERENCE 3). RESIDUE NUMBERS ARE 3GLY 82 REMARK 4 DISCONTINUOUS. RESIDUE NUMBER 102 IS SKIPPED SO THAT THE 3GLY 83 REMARK 4 NUMBERING OF THE RESIDUES IS CONSISTENT WITH GLUCOAMYLASE 3GLY 84 REMARK 4 FROM ASPERGILLUS NIGER. RESIDUE NUMBERS 141, 240, 319, 3GLY 85 REMARK 4 320 AND 445 HAVE THE AMINO ACID TYPE CORRESPONDING TO THE 3GLY 86 REMARK 4 GLUCOAMYLASE FROM ASPERGILLUS NIGER, RATHER THAN THAT OF 3GLY 87 REMARK 4 ASPERGILLUS AWAMORI VAR. KAWACHI. 3GLY 88 REMARK 5 3GLY 89 REMARK 5 ACTIVE SITE: RESIDUES THAT BIND ACARBOSE AND 3GLY 90 REMARK 5 1-DEOXYNOJIRIMYCIN AT SUBSITE 1 OF THE ACTIVE SITE ARE OD1 3GLY 91 REMARK 5 ASP 55, OD2 ASP 55, NH1 ARG 305, CARBONYL 177, NE ARG 54, 3GLY 92 REMARK 5 AND NH2 ARG 54. GLU 179 IS THE CATALYTIC ACID AND RESIDUE 3GLY 93 REMARK 5 GLU 400 IS THE CATALYTIC BASE. WATER 500 IS THE 3GLY 94 REMARK 5 NUCLEOPHILE. 3GLY 95 REMARK 6 3GLY 96 REMARK 6 THE FOLLOWING WATER MOLECULES MAKE CLOSE CONTACTS: 3GLY 97 REMARK 6 O HOH 638 O HOH 870 - 2.07 3GLY 98 REMARK 6 O HOH 773 O HOH 1203 - 2.07 3GLY 99 REMARK 6 O HOH 868 O HOH 1208 - 1.81 3GLY 100 REMARK 6 O HOH 958 O HOH 959 - 2.08 3GLY 101 REMARK 6 O HOH 960 O HOH 1201 - 2.09 3GLY 102 REMARK 7 3GLY 103 REMARK 7 CROSS REFERENCE TO SEQUENCE DATABASE 3GLY 104 REMARK 7 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 3GLY 105 REMARK 7 AMYG_ASPSH 3GLY 106 REMARK 8 3GLY 107 REMARK 8 SEQUENCE ADVISORY NOTICE 3GLY 108 REMARK 8 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 3GLY 109 REMARK 8 3GLY 110 REMARK 8 SWISS-PROT ENTRY NAME: AMYG_ASPSH 3GLY 111 REMARK 8 3GLY 112 REMARK 8 SWISS-PROT RESIDUE PDB SEQRES 3GLY 113 REMARK 8 3GLY 114 REMARK 8 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 3GLY 115 REMARK 8 ILE 82 LEU 58 3GLY 116 REMARK 8 LEU 84 ILE 60 3GLY 117 REMARK 8 ALA 140 THR 117 3GLY 118 SEQRES 1 470 ALA THR LEU ASP SER TRP LEU SER ASN GLU ALA THR VAL 3GLY 119 SEQRES 2 470 ALA ARG THR ALA ILE LEU ASN ASN ILE GLY ALA ASP GLY 3GLY 120 SEQRES 3 470 ALA TRP VAL SER GLY ALA ASP SER GLY ILE VAL VAL ALA 3GLY 121 SEQRES 4 470 SER PRO SER THR ASP ASN PRO ASP TYR PHE TYR THR TRP 3GLY 122 SEQRES 5 470 THR ARG ASP SER GLY LEU VAL ILE LYS THR LEU VAL ASP 3GLY 123 SEQRES 6 470 LEU PHE ARG ASN GLY ASP THR ASP LEU LEU SER THR ILE 3GLY 124 SEQRES 7 470 GLU HIS TYR ILE SER SER GLN ALA ILE ILE GLN GLY VAL 3GLY 125 SEQRES 8 470 SER ASN PRO SER GLY ASP LEU SER SER GLY GLY LEU GLY 3GLY 126 SEQRES 9 470 GLU PRO LYS PHE ASN VAL ASP GLU THR ALA TYR THR GLY 3GLY 127 SEQRES 10 470 SER TRP GLY ARG PRO GLN ARG ASP GLY PRO ALA LEU ARG 3GLY 128 SEQRES 11 470 ALA THR ALA MET ILE GLY PHE GLY GLN TRP LEU LEU ASP 3GLY 129 SEQRES 12 470 ASN GLY TYR THR SER ALA ALA THR GLU ILE VAL TRP PRO 3GLY 130 SEQRES 13 470 LEU VAL ARG ASN ASP LEU SER TYR VAL ALA GLN TYR TRP 3GLY 131 SEQRES 14 470 ASN GLN THR GLY TYR ASP LEU TRP GLU GLU VAL ASN GLY 3GLY 132 SEQRES 15 470 SER SER PHE PHE THR ILE ALA VAL GLN HIS ARG ALA LEU 3GLY 133 SEQRES 16 470 VAL GLU GLY SER ALA PHE ALA THR ALA VAL GLY SER SER 3GLY 134 SEQRES 17 470 CYS SER TRP CYS ASP SER GLN ALA PRO GLN ILE LEU CYS 3GLY 135 SEQRES 18 470 TYR LEU GLN SER PHE TRP THR GLY SER TYR ILE LEU ALA 3GLY 136 SEQRES 19 470 ASN PHE ASP SER SER ARG SER GLY LYS ASP THR ASN THR 3GLY 137 SEQRES 20 470 LEU LEU GLY SER ILE HIS THR PHE ASP PRO GLU ALA GLY 3GLY 138 SEQRES 21 470 CYS ASP ASP SER THR PHE GLN PRO CYS SER PRO ARG ALA 3GLY 139 SEQRES 22 470 LEU ALA ASN HIS LYS GLU VAL VAL ASP SER PHE ARG SER 3GLY 140 SEQRES 23 470 ILE TYR THR LEU ASN ASP GLY LEU SER ASP SER GLU ALA 3GLY 141 SEQRES 24 470 VAL ALA VAL GLY ARG TYR PRO GLU ASP SER TYR TYR ASN 3GLY 142 SEQRES 25 470 GLY ASN PRO TRP PHE LEU CYS THR LEU ALA ALA ALA GLU 3GLY 143 SEQRES 26 470 GLN LEU TYR ASP ALA LEU TYR GLN TRP ASP LYS GLN GLY 3GLY 144 SEQRES 27 470 SER LEU GLU ILE THR ASP VAL SER LEU ASP PHE PHE LYS 3GLY 145 SEQRES 28 470 ALA LEU TYR SER GLY ALA ALA THR GLY THR TYR SER SER 3GLY 146 SEQRES 29 470 SER SER SER THR TYR SER SER ILE VAL SER ALA VAL LYS 3GLY 147 SEQRES 30 470 THR PHE ALA ASP GLY PHE VAL SER ILE VAL GLU THR HIS 3GLY 148 SEQRES 31 470 ALA ALA SER ASN GLY SER LEU SER GLU GLN PHE ASP LYS 3GLY 149 SEQRES 32 470 SER ASP GLY ASP GLU LEU SER ALA ARG ASP LEU THR TRP 3GLY 150 SEQRES 33 470 SER TYR ALA ALA LEU LEU THR ALA ASN ASN ARG ARG ASN 3GLY 151 SEQRES 34 470 SER VAL VAL PRO PRO SER TRP GLY GLU THR SER ALA SER 3GLY 152 SEQRES 35 470 SER VAL PRO GLY THR CYS ALA ALA THR SER ALA SER GLY 3GLY 153 SEQRES 36 470 THR TYR SER SER VAL THR VAL THR SER TRP PRO SER ILE 3GLY 154 SEQRES 37 470 VAL ALA 3GLY 155 FTNOTE 1 3GLY 156 FTNOTE 1 GLY 23 - ALA 24 OMEGA = 0.50 3GLY 157 FTNOTE 1 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3GLY 158 FTNOTE 2 3GLY 159 FTNOTE 2 CIS PROLINE - PRO 46 3GLY 160 FTNOTE 3 3GLY 161 FTNOTE 3 CIS PROLINE - PRO 123 3GLY 162 FTNOTE 4 3GLY 163 FTNOTE 4 RESIDUES ASN 171 AND ASN 395 ARE SITES OF N-GLYCOSYLATION. 3GLY 164 FTNOTE 5 3GLY 165 FTNOTE 5 RESIDUES SER 443, SER 444, THR 452, SER 453, SER 455, 3GLY 166 FTNOTE 5 THR 457, SER 459, SER 460, THR 462 AND THR 464 ARE SITES OF 3GLY 167 FTNOTE 5 O-GLYCOSYLATION. 3GLY 168 HET NAG 171A 14 N-ACETYL-D-GLUCOSAMINE 3GLY 169 HET NAG 171B 14 N-ACETYL-D-GLUCOSAMINE 3GLY 170 HET MAN 171C 11 ALPHA-D-MANNOSE 3GLY 171 HET MAN 171D 11 ALPHA-D-MANNOSE 3GLY 172 HET MAN 171G 11 ALPHA-D-MANNOSE 3GLY 173 HET NAG 395A 14 N-ACETYL-D-GLUCOSAMINE 3GLY 174 HET NAG 395B 14 N-ACETYL-D-GLUCOSAMINE 3GLY 175 HET MAN 395C 11 ALPHA-D-MANNOSE 3GLY 176 HET MAN 395D 11 ALPHA-D-MANNOSE 3GLY 177 HET MAN 395E 11 ALPHA-D-MANNOSE 3GLY 178 HET MAN 395F 11 ALPHA-D-MANNOSE 3GLY 179 HET MAN 395G 11 ALPHA-D-MANNOSE 3GLY 180 HET MAN 395I 11 ALPHA-D-MANNOSE 3GLY 181 HET MAN 443A 11 ALPHA-D-MANNOSE 3GLY 182 HET MAN 444A 12 ALPHA-D-MANNOSE 3GLY 183 HET MAN 453A 11 ALPHA-D-MANNOSE 3GLY 184 HET MAN 455A 11 ALPHA-D-MANNOSE 3GLY 185 HET MAN 452A 11 ALPHA-D-MANNOSE 3GLY 186 HET MAN 457A 11 ALPHA-D-MANNOSE 3GLY 187 HET MAN 459A 11 ALPHA-D-MANNOSE 3GLY 188 HET MAN 460A 11 ALPHA-D-MANNOSE 3GLY 189 HET MAN 462A 11 ALPHA-D-MANNOSE 3GLY 190 HET MAN 464A 11 ALPHA-D-MANNOSE 3GLY 191 FORMUL 2 NAG 4(C8 H15 N1 O6) 3GLY 192 FORMUL 3 MAN 19(C6 H12 O6) 3GLY 193 FORMUL 4 HOH *673(H2 O1) 3GLY 194 HELIX 1 H1 ALA 1 ASN 21 1 3GLY 195 HELIX 2 H2 THR 53 ARG 68 1 3GLY 196 HELIX 3 H3 THR 72 GLY 90 1 3GLY 197 HELIX 4 H4 ASP 126 ASN 145 1 3GLY 198 HELIX 5 H5 THR 148 TYR 169 1 3GLY 199 HELIX 6 H6 PHE 186 VAL 206 1 3GLY 200 HELIX 7 H7 SER 211 PHE 227 1 3GLY 201 HELIX 8 H8 THR 246 THR 255 1 3GLY 202 HELIX 9 H9 PRO 272 SER 287 1 3GLY 203 HELIX 10 H10 PHE 318 GLN 338 1 3GLY 204 HELIX 11 H11 ASP 345 LEU 354 1 NOT PART OF THE BARREL 3GLY 205 HELIX 12 H12 SER 368 HIS 391 1 3GLY 206 HELIX 13 H13 THR 416 ASN 430 1 3GLY 207 SHEET 1 S1 2 ASN 21 GLY 23 0 3GLY 208 SHEET 2 S1 2 GLY 35 VAL 38 -1 O ILE 36 N GLY 23 3GLY 209 SHEET 1 S2 3 PHE 49 TRP 52 0 3GLY 210 SHEET 2 S2 3 PRO 107 ASN 110 -1 O PHE 109 N THR 51 3GLY 211 SHEET 3 S2 3 GLU 113 TYR 116 -1 O THR 114 N ASN 110 3GLY 212 SHEET 1 S3 2 VAL 91 ASN 93 0 3GLY 213 SHEET 2 S3 2 GLY 96 ASP 97 -1 O GLY 96 N ASN 93 3GLY 214 SHEET 1 S4 2 THR 173 ASP 176 0 3GLY 215 SHEET 2 S4 2 VAL 181 GLY 183 -1 N GLY 183 O GLY 174 3GLY 216 SHEET 1 S5 2 SER 184 SER 185 0 3GLY 217 SHEET 2 S5 2 ALA 235 PHE 237 -1 N PHE 237 O SER 184 3GLY 218 SHEET 1 S6 2 CYS 262 ASP 264 0 3GLY 219 SHEET 2 S6 2 PHE 267 GLN 268 -1 N PHE 267 O ASP 264 3GLY 220 SHEET 1 S7 2 GLY 339 THR 344 0 3GLY 221 SHEET 2 S7 2 THR 360 SER 365 -1 N TYR 363 O LEU 341 3GLY 222 SHEET 1 S8 2 ALA 392 ALA 393 0 3GLY 223 SHEET 2 S8 2 GLY 396 SER 397 -1 N GLY 396 O ALA 393 3GLY 224 SHEET 1 S9 2 LEU 398 ASP 403 0 3GLY 225 SHEET 2 S9 2 GLY 407 LEU 415 -1 O ALA 412 N GLU 400 3GLY 226 TURN 1 T1 GLY 23 GLY 26 DA DISTANCE 5.29 ANGSTROMS 3GLY 227 TURN 2 T2 GLY 26 VAL 29 DA DISTANCE 3.52 ANGSTROMS 3GLY 228 TURN 3 T3 ALA 27 SER 30 DA DISTANCE 4.86 ANGSTROMS 3GLY 229 TURN 4 T4 VAL 29 ALA 32 DA DISTANCE 2.88 ANGSTROMS 3GLY 230 TURN 5 T5 ASP 33 ILE 36 DA DISTANCE 3.29 ANGSTROMS 3GLY 231 TURN 6 T6 THR 43 PRO 46 DA DISTANCE 6.67 ANGSTROMS 3GLY 232 TURN 7 T7 ASP 44 ASP 47 DA DISTANCE 4.81 ANGSTROMS 3GLY 233 TURN 8 T8 ARG 68 ASP 71 DA DISTANCE 6.15 ANGSTROMS 3GLY 234 TURN 9 T9 ASN 93 GLY 96 DA DISTANCE 2.91 ANGSTROMS 3GLY 235 TURN 10 T10 ASP 97 SER 100 DA DISTANCE 3.14 ANGSTROMS 3GLY 236 TURN 11 T11 LEU 98 GLY 101 DA DISTANCE 4.54 ANGSTROMS 3GLY 237 TURN 12 T12 SER 99 GLY 103 DA DISTANCE 6.50 ANGSTROMS 3GLY 238 TURN 13 T13 GLY 101 LEU 104 DA DISTANCE 3.13 ANGSTROMS 3GLY 239 TURN 14 T14 GLY 103 GLU 106 DA DISTANCE 3.23 ANGSTROMS 3GLY 240 TURN 15 T15 ASN 110 GLU 113 DA DISTANCE 3.01 ANGSTROMS 3GLY 241 TURN 16 T16 TYR 169 GLN 172 DA DISTANCE 3.18 ANGSTROMS 3GLY 242 TURN 17 T17 ASP 176 GLU 179 DA DISTANCE 2.90 ANGSTROMS 3GLY 243 TURN 18 T18 THR 229 TYR 232 DA DISTANCE 5.80 ANGSTROMS 3GLY 244 TURN 19 T19 ASN 236 SER 239 DA DISTANCE 4.39 ANGSTROMS 3GLY 245 TURN 20 T20 ILE 253 PHE 256 DA DISTANCE 3.37 ANGSTROMS 3GLY 246 TURN 21 T21 ASP 257 ALA 260 DA DISTANCE 3.01 ANGSTROMS 3GLY 247 TURN 22 T22 ASP 263 THR 266 DA DISTANCE 3.71 ANGSTROMS 3GLY 248 TURN 23 T23 ASP 264 PHE 267 DA DISTANCE 3.15 ANGSTROMS 3GLY 249 TURN 24 T24 GLN 268 SER 271 DA DISTANCE 2.93 ANGSTROMS 3GLY 250 TURN 25 T25 ARG 286 TYR 289 DA DISTANCE 4.55 ANGSTROMS 3GLY 251 TURN 26 T26 TYR 289 ASN 292 DA DISTANCE 2.73 ANGSTROMS 3GLY 252 TURN 27 T27 THR 290 ASP 293 DA DISTANCE 3.13 ANGSTROMS 3GLY 253 TURN 28 T28 ASN 292 LEU 295 DA DISTANCE 3.20 ANGSTROMS 3GLY 254 TURN 29 T29 SER 296 GLU 299 DA DISTANCE 2.93 ANGSTROMS 3GLY 255 TURN 30 T30 TYR 306 ASP 309 DA DISTANCE 3.16 ANGSTROMS 3GLY 256 TURN 31 T31 SER 310 ASN 313 DA DISTANCE 2.78 ANGSTROMS 3GLY 257 TURN 32 T32 TYR 311 GLY 314 DA DISTANCE 2.74 ANGSTROMS 3GLY 258 TURN 33 T33 ALA 353 SER 356 DA DISTANCE 5.49 ANGSTROMS 3GLY 259 TURN 34 T34 TYR 355 ALA 358 DA DISTANCE 2.86 ANGSTROMS 3GLY 260 TURN 35 T35 SER 364 SER 367 DA DISTANCE 3.16 ANGSTROMS 3GLY 261 TURN 36 T36 ALA 393 GLY 396 DA DISTANCE 2.84 ANGSTROMS 3GLY 262 TURN 37 T37 ASP 403 ASP 406 DA DISTANCE 3.76 ANGSTROMS 3GLY 263 TURN 38 T38 LYS 404 GLY 407 DA DISTANCE 5.74 ANGSTROMS 3GLY 264 TURN 39 T39 ALA 412 LEU 415 DA DISTANCE 4.41 ANGSTROMS 3GLY 265 TURN 40 T22 GLY 438 SER 441 DA DISTANCE 3.12 ANGSTROMS 3GLY 266 TURN 41 T23 GLU 439 ALA 442 DA DISTANCE 2.98 ANGSTROMS 3GLY 267 TURN 42 T42 THR 440 SER 443 DA DISTANCE 5.11 ANGSTROMS 3GLY 268 TURN 43 T43 PRO 446 CYS 449 DA DISTANCE 5.07 ANGSTROMS 3GLY 269 SSBOND 1 CYS 210 CYS 213 3GLY 270 SSBOND 2 CYS 222 CYS 449 3GLY 271 SSBOND 3 CYS 262 CYS 270 3GLY 272 SITE 1 ACT 4 ASP 55 ARG 305 LEU 177 ARG 54 3GLY 273 CRYST1 116.700 104.300 48.490 90.00 90.00 90.00 P 21 21 21 4 3GLY 274 ORIGX1 1.000000 0.000000 0.000000 0.00000 3GLY 275 ORIGX2 0.000000 1.000000 0.000000 0.00000 3GLY 276 ORIGX3 0.000000 0.000000 1.000000 0.00000 3GLY 277 SCALE1 0.008569 0.000000 0.000000 0.00000 3GLY 278 SCALE2 0.000000 0.009588 0.000000 0.00000 3GLY 279 SCALE3 0.000000 0.000000 0.020623 0.00000 3GLY 280