HEADER OXIDOREDUCTASE(PQQ(A)-CHOH(D)) 13-OCT-93 3AAH 3AAH 2 COMPND METHANOL DEHYDROGENASE (E.C.1.1.99.8) (MEDH) 3AAH 3 SOURCE METHYLOPHILIS W3A1 3AAH 4 AUTHOR F.S.MATHEWS,Z.-X.XIA 3AAH 5 REVDAT 1 30-APR-94 3AAH 0 3AAH 6 JRNL AUTH S.WHITE,G.BOYD,F.S.MATHEWS,Z.-X.XIA,W.-W.DAI, 3AAH 7 JRNL AUTH 2 J.-P.XIONG,V.L.DAVIDSON 3AAH 8 JRNL TITL THE ACTIVE SITE STRUCTURE OF THE CALCIUM-CONTAINING 3AAH 9 JRNL TITL 2 QUINOPROTEIN METHANOL DEHYDROGENASE 3AAH 10 JRNL REF BIOCHEMISTRY V. 32 12955 1993 3AAH 11 JRNL REFN ASTM BICHAW US ISSN 0006-2960 0033 3AAH 12 REMARK 1 3AAH 13 REMARK 1 AUTH Z.-X.XIA,W.-W.DAI,J.-P.XIONG,Z.-P.HAO,V.L.DAVIDSON, 3AAH 14 REMARK 1 AUTH 2 S.WHITE,F.S.MATHEWS 3AAH 15 REMARK 1 TITL THE THREE DIMENSIONAL STRUCTURES OF METHANOL 3AAH 16 REMARK 1 TITL 2 DEHYDROGENASE FROM TWO METHYLOTROPHIC BACTERIA AT 3AAH 17 REMARK 1 TITL 3 2.6 ANGSTROMS RESOLUTION 3AAH 18 REMARK 1 REF J.BIOL.CHEM. V. 267 22289 1992 3AAH 19 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 3AAH 20 REMARK 2 3AAH 21 REMARK 2 RESOLUTION. 2.4 ANGSTROMS. 3AAH 22 REMARK 3 3AAH 23 REMARK 3 REFINEMENT. 3AAH 24 REMARK 3 PROGRAM X-PLOR 3AAH 25 REMARK 3 AUTHORS BRUNGER 3AAH 26 REMARK 3 R VALUE 0.201 3AAH 27 REMARK 3 RMSD BOND DISTANCES 0.009 ANGSTROMS 3AAH 28 REMARK 3 RMSD BOND ANGLES 1.14 DEGREES 3AAH 29 REMARK 3 3AAH 30 REMARK 3 NUMBER OF REFLECTIONS 50907 3AAH 31 REMARK 3 RESOLUTION RANGE 10.0 - 2.4 ANGSTROMS 3AAH 32 REMARK 4 3AAH 33 REMARK 4 THE STRUCTURE WAS SOLVED BY MULTIPLE ISOMORPHOUS 3AAH 34 REMARK 4 REPLACEMENT USING THREE DERIVATIVES. 3AAH 35 REMARK 5 3AAH 36 REMARK 5 METHANOL DEHYDROGENASE IS AN A2B2 TETRAMER. THE ASYMMETRIC 3AAH 37 REMARK 5 UNIT CONTAINS THE TETRAMER, TWO PYRROLOQUINOLINE QUINONE 3AAH 38 REMARK 5 COFACTORS (PQQ) AND 2 CALCIUM COUNTER IONS. A 3AAH 39 REMARK 5 NON-CRYSTALLOGRAPHIC TWO-FOLD AXIS RELATES THE TWO HALVES. 3AAH 40 REMARK 6 3AAH 41 REMARK 6 THE AMINO ACID SEQUENCE OF MEDH FROM W3A1 WAS DETERMINED IN 3AAH 42 REMARK 6 THE LAB OF F.S.MATHEWS. 3AAH 43 REMARK 6 THE SEQUENCE FOR THE SMALLER CHAINS IS AN APPROXIMATION 3AAH 44 REMARK 6 TAKEN FROM THE CLOSELY RELATED (METHYLOPHILUS 3AAH 45 REMARK 6 METHYLOTROPHUS) SEQUENCE. 571 RESIDUES WERE LOCATED FOR 3AAH 46 REMARK 6 THE *A* AND *C* CHAINS AND 57 RESIDUES FOR THE *B* AND *D* 3AAH 47 REMARK 6 CHAINS. 3AAH 48 REMARK 7 3AAH 49 REMARK 7 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL 3AAH 50 REMARK 7 YIELD APPROXIMATE COORDINATES FOR CHAINS *C* AND *D* WHEN 3AAH 51 REMARK 7 APPLIED TO CHAINS *A* AND *B*. 3AAH 52 SEQRES 1 A 571 ASP ALA ASP LEU ASP LYS GLN THR ASN THR ALA GLY ALA 3AAH 53 SEQRES 2 A 571 TRP PRO ILE ALA THR GLY GLY TYR TYR SER GLN HIS ASN 3AAH 54 SEQRES 3 A 571 SER PRO LEU ALA GLN ILE ASN LYS SER ASN VAL LYS ASN 3AAH 55 SEQRES 4 A 571 VAL LYS ALA ALA TRP SER PHE SER THR GLY VAL LEU ASN 3AAH 56 SEQRES 5 A 571 GLY HIS GLU GLY ALA PRO LEU VAL ILE GLY ASP MET MET 3AAH 57 SEQRES 6 A 571 TYR VAL HIS SER ALA PHE PRO ASN ASN THR TYR ALA LEU 3AAH 58 SEQRES 7 A 571 ASN LEU ASN ASP PRO GLY LYS ILE VAL TRP GLN HIS LYS 3AAH 59 SEQRES 8 A 571 PRO LYS GLN ASP ALA SER THR LYS ALA VAL MET CYS CYS 3AAH 60 SEQRES 9 A 571 ASP VAL VAL ASP ARG GLY LEU ALA TYR GLY ALA GLY GLN 3AAH 61 SEQRES 10 A 571 ILE VAL LYS LYS GLN ALA ASN GLY HIS LEU LEU ALA LEU 3AAH 62 SEQRES 11 A 571 ASP ALA LYS THR GLY LYS ILE ASN TRP GLU VAL GLU VAL 3AAH 63 SEQRES 12 A 571 CYS ASP PRO LYS VAL GLY SER THR LEU THR GLN ALA PRO 3AAH 64 SEQRES 13 A 571 PHE VAL ALA LYS ASP THR VAL LEU MET GLY CYS SER GLY 3AAH 65 SEQRES 14 A 571 ALA GLU LEU GLY VAL ARG GLY ALA VAL ASN ALA PHE ASP 3AAH 66 SEQRES 15 A 571 LEU LYS THR GLY GLU LEU LYS TRP ARG ALA PHE ALA THR 3AAH 67 SEQRES 16 A 571 GLY SER ASP ASP SER VAL ARG LEU ALA LYS ASP PHE ASN 3AAH 68 SEQRES 17 A 571 SER ALA ASN PRO HIS TYR GLY GLN PHE GLY LEU GLY THR 3AAH 69 SEQRES 18 A 571 LYS THR TRP GLU GLY ASP ALA TRP LYS ILE GLY GLY GLY 3AAH 70 SEQRES 19 A 571 THR ASN TRP GLY TRP TYR ALA TYR ASP PRO LYS LEU ASN 3AAH 71 SEQRES 20 A 571 LEU PHE TYR TYR GLY SER GLY ASN PRO ALA PRO TRP ASN 3AAH 72 SEQRES 21 A 571 GLU THR MET ARG PRO GLY ASP ASN LYS TRP THR MET THR 3AAH 73 SEQRES 22 A 571 ILE TRP GLY ARG ASP LEU ASP THR GLY MET ALA LYS TRP 3AAH 74 SEQRES 23 A 571 GLY TYR GLN LYS THR PRO HIS ASP GLU TRP ASP PHE ALA 3AAH 75 SEQRES 24 A 571 GLY VAL ASN GLN MET VAL LEU THR ASP GLN PRO VAL ASN 3AAH 76 SEQRES 25 A 571 ALA LYS MET THR PRO LEU LEU SER HIS ILE ASP ARG ASN 3AAH 77 SEQRES 26 A 571 GLY ILE LEU TYR THR LEU ASN ARG GLU ASN GLY ASN LEU 3AAH 78 SEQRES 27 A 571 ILE VAL ALA GLU LYS VAL ASP PRO ALA VAL ASN VAL PHE 3AAH 79 SEQRES 28 A 571 LYS LYS VAL ASP LEU LYS THR GLY THR PRO VAL ARG ASP 3AAH 80 SEQRES 29 A 571 PRO GLU PHE ALA THR ARG MET ASP HIS LYS GLY THR ASN 3AAH 81 SEQRES 30 A 571 ILE CYS PRO SER ALA MET GLY PHE HIS ASN GLN GLY VAL 3AAH 82 SEQRES 31 A 571 ASP SER TYR ASP PRO GLU SER ARG THR LEU TYR ALA GLY 3AAH 83 SEQRES 32 A 571 LEU ASN HIS ILE CYS MET ASP TRP GLU PRO PHE MET LEU 3AAH 84 SEQRES 33 A 571 PRO TYR ARG ALA GLY GLN PHE PHE VAL GLY ALA THR LEU 3AAH 85 SEQRES 34 A 571 ALA MET TYR PRO GLY PRO ASN GLY PRO THR LYS LYS GLU 3AAH 86 SEQRES 35 A 571 MET GLY GLN ILE ARG ALA PHE ASP LEU THR THR GLY LYS 3AAH 87 SEQRES 36 A 571 ALA LYS TRP THR LYS TRP GLU LYS PHE ALA ALA TRP GLY 3AAH 88 SEQRES 37 A 571 GLY THR LEU TYR THR LYS GLY GLY LEU VAL TRP TYR ALA 3AAH 89 SEQRES 38 A 571 THR LEU ASP GLY TYR LEU LYS ALA LEU ASP ASN LYS ASP 3AAH 90 SEQRES 39 A 571 GLY LYS GLU LEU TRP ASN PHE LYS MET PRO SER GLY GLY 3AAH 91 SEQRES 40 A 571 ILE GLY SER PRO MET THR TYR SER PHE LYS GLY LYS GLN 3AAH 92 SEQRES 41 A 571 TYR ILE GLY SER MET TYR GLY VAL GLY GLY TRP PRO GLY 3AAH 93 SEQRES 42 A 571 VAL GLY LEU VAL PHE ASP LEU THR ASP PRO SER ALA GLY 3AAH 94 SEQRES 43 A 571 LEU GLY ALA VAL GLY ALA PHE ARG GLU LEU GLN ASN HIS 3AAH 95 SEQRES 44 A 571 THR GLN MET GLY GLY GLY LEU MET VAL PHE SER LEU 3AAH 96 SEQRES 1 B 57 TYR ASP GLY GLN THR CYS LYS GLU ALA GLY ASN CYS TRP 3AAH 97 SEQRES 2 B 57 GLU ALA LYS PRO GLY TYR PRO GLU LYS ILE ALA GLY SER 3AAH 98 SEQRES 3 B 57 LYS TYR ASP PRO LYS HIS ASP PRO VAL GLU LEU ASN LYS 3AAH 99 SEQRES 4 B 57 GLN GLU GLN ALA ILE LYS ALA MET ASP GLU ARG ASN ALA 3AAH 100 SEQRES 5 B 57 ALA ARG ILE ALA ASN 3AAH 101 SEQRES 1 C 571 ASP ALA ASP LEU ASP LYS GLN THR ASN THR ALA GLY ALA 3AAH 102 SEQRES 2 C 571 TRP PRO ILE ALA THR GLY GLY TYR TYR SER GLN HIS ASN 3AAH 103 SEQRES 3 C 571 SER PRO LEU ALA GLN ILE ASN LYS SER ASN VAL LYS ASN 3AAH 104 SEQRES 4 C 571 VAL LYS ALA ALA TRP SER PHE SER THR GLY VAL LEU ASN 3AAH 105 SEQRES 5 C 571 GLY HIS GLU GLY ALA PRO LEU VAL ILE GLY ASP MET MET 3AAH 106 SEQRES 6 C 571 TYR VAL HIS SER ALA PHE PRO ASN ASN THR TYR ALA LEU 3AAH 107 SEQRES 7 C 571 ASN LEU ASN ASP PRO GLY LYS ILE VAL TRP GLN HIS LYS 3AAH 108 SEQRES 8 C 571 PRO LYS GLN ASP ALA SER THR LYS ALA VAL MET CYS CYS 3AAH 109 SEQRES 9 C 571 ASP VAL VAL ASP ARG GLY LEU ALA TYR GLY ALA GLY GLN 3AAH 110 SEQRES 10 C 571 ILE VAL LYS LYS GLN ALA ASN GLY HIS LEU LEU ALA LEU 3AAH 111 SEQRES 11 C 571 ASP ALA LYS THR GLY LYS ILE ASN TRP GLU VAL GLU VAL 3AAH 112 SEQRES 12 C 571 CYS ASP PRO LYS VAL GLY SER THR LEU THR GLN ALA PRO 3AAH 113 SEQRES 13 C 571 PHE VAL ALA LYS ASP THR VAL LEU MET GLY CYS SER GLY 3AAH 114 SEQRES 14 C 571 ALA GLU LEU GLY VAL ARG GLY ALA VAL ASN ALA PHE ASP 3AAH 115 SEQRES 15 C 571 LEU LYS THR GLY GLU LEU LYS TRP ARG ALA PHE ALA THR 3AAH 116 SEQRES 16 C 571 GLY SER ASP ASP SER VAL ARG LEU ALA LYS ASP PHE ASN 3AAH 117 SEQRES 17 C 571 SER ALA ASN PRO HIS TYR GLY GLN PHE GLY LEU GLY THR 3AAH 118 SEQRES 18 C 571 LYS THR TRP GLU GLY ASP ALA TRP LYS ILE GLY GLY GLY 3AAH 119 SEQRES 19 C 571 THR ASN TRP GLY TRP TYR ALA TYR ASP PRO LYS LEU ASN 3AAH 120 SEQRES 20 C 571 LEU PHE TYR TYR GLY SER GLY ASN PRO ALA PRO TRP ASN 3AAH 121 SEQRES 21 C 571 GLU THR MET ARG PRO GLY ASP ASN LYS TRP THR MET THR 3AAH 122 SEQRES 22 C 571 ILE TRP GLY ARG ASP LEU ASP THR GLY MET ALA LYS TRP 3AAH 123 SEQRES 23 C 571 GLY TYR GLN LYS THR PRO HIS ASP GLU TRP ASP PHE ALA 3AAH 124 SEQRES 24 C 571 GLY VAL ASN GLN MET VAL LEU THR ASP GLN PRO VAL ASN 3AAH 125 SEQRES 25 C 571 ALA LYS MET THR PRO LEU LEU SER HIS ILE ASP ARG ASN 3AAH 126 SEQRES 26 C 571 GLY ILE LEU TYR THR LEU ASN ARG GLU ASN GLY ASN LEU 3AAH 127 SEQRES 27 C 571 ILE VAL ALA GLU LYS VAL ASP PRO ALA VAL ASN VAL PHE 3AAH 128 SEQRES 28 C 571 LYS LYS VAL ASP LEU LYS THR GLY THR PRO VAL ARG ASP 3AAH 129 SEQRES 29 C 571 PRO GLU PHE ALA THR ARG MET ASP HIS LYS GLY THR ASN 3AAH 130 SEQRES 30 C 571 ILE CYS PRO SER ALA MET GLY PHE HIS ASN GLN GLY VAL 3AAH 131 SEQRES 31 C 571 ASP SER TYR ASP PRO GLU SER ARG THR LEU TYR ALA GLY 3AAH 132 SEQRES 32 C 571 LEU ASN HIS ILE CYS MET ASP TRP GLU PRO PHE MET LEU 3AAH 133 SEQRES 33 C 571 PRO TYR ARG ALA GLY GLN PHE PHE VAL GLY ALA THR LEU 3AAH 134 SEQRES 34 C 571 ALA MET TYR PRO GLY PRO ASN GLY PRO THR LYS LYS GLU 3AAH 135 SEQRES 35 C 571 MET GLY GLN ILE ARG ALA PHE ASP LEU THR THR GLY LYS 3AAH 136 SEQRES 36 C 571 ALA LYS TRP THR LYS TRP GLU LYS PHE ALA ALA TRP GLY 3AAH 137 SEQRES 37 C 571 GLY THR LEU TYR THR LYS GLY GLY LEU VAL TRP TYR ALA 3AAH 138 SEQRES 38 C 571 THR LEU ASP GLY TYR LEU LYS ALA LEU ASP ASN LYS ASP 3AAH 139 SEQRES 39 C 571 GLY LYS GLU LEU TRP ASN PHE LYS MET PRO SER GLY GLY 3AAH 140 SEQRES 40 C 571 ILE GLY SER PRO MET THR TYR SER PHE LYS GLY LYS GLN 3AAH 141 SEQRES 41 C 571 TYR ILE GLY SER MET TYR GLY VAL GLY GLY TRP PRO GLY 3AAH 142 SEQRES 42 C 571 VAL GLY LEU VAL PHE ASP LEU THR ASP PRO SER ALA GLY 3AAH 143 SEQRES 43 C 571 LEU GLY ALA VAL GLY ALA PHE ARG GLU LEU GLN ASN HIS 3AAH 144 SEQRES 44 C 571 THR GLN MET GLY GLY GLY LEU MET VAL PHE SER LEU 3AAH 145 SEQRES 1 D 57 TYR ASP GLY GLN THR CYS LYS GLU ALA GLY ASN CYS TRP 3AAH 146 SEQRES 2 D 57 GLU ALA LYS PRO GLY TYR PRO GLU LYS ILE ALA GLY SER 3AAH 147 SEQRES 3 D 57 LYS TYR ASP PRO LYS HIS ASP PRO VAL GLU LEU ASN LYS 3AAH 148 SEQRES 4 D 57 GLN GLU GLN ALA ILE LYS ALA MET ASP GLU ARG ASN ALA 3AAH 149 SEQRES 5 D 57 ALA ARG ILE ALA ASN 3AAH 150 FTNOTE 1 3AAH 151 FTNOTE 1 CIS PROLINE - PRO A 72 3AAH 152 FTNOTE 2 3AAH 153 FTNOTE 2 CIS PROLINE - PRO A 258 3AAH 154 FTNOTE 3 3AAH 155 FTNOTE 3 TRP A 270 - THR A 271 OMEGA = 147.38 3AAH 156 FTNOTE 3 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3AAH 157 FTNOTE 4 3AAH 158 FTNOTE 4 CIS PROLINE - PRO A 380 3AAH 159 FTNOTE 5 3AAH 160 FTNOTE 5 PHE C 71 - PRO C 72 OMEGA = 31.62 3AAH 161 FTNOTE 5 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3AAH 162 FTNOTE 6 3AAH 163 FTNOTE 6 CYS C 103 - CYS C 104 OMEGA = 210.76 3AAH 164 FTNOTE 6 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3AAH 165 FTNOTE 7 3AAH 166 FTNOTE 7 CIS PROLINE - PRO C 258 3AAH 167 FTNOTE 8 3AAH 168 FTNOTE 8 TRP C 270 - THR C 271 OMEGA = 147.10 3AAH 169 FTNOTE 8 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3AAH 170 FTNOTE 9 3AAH 171 FTNOTE 9 CIS PROLINE - PRO C 380 3AAH 172 HET PQQ A 101 24 PYRROLOQUINOLINE QUINONE 3AAH 173 HET CA A 201 1 CALCIUM +2 COUNTER ION 3AAH 174 HET PQQ C 101 24 PYRROLOQUINOLINE QUINONE 3AAH 175 HET CA C 201 1 CALCIUM +2 COUNTER ION 3AAH 176 FORMUL 5 PQQ 2(C14 H4 N2 O8) 3AAH 177 FORMUL 6 CA 2(CA1) 3AAH 178 HELIX 1 H1 ASP A 3 ASN A 9 1 3AAH 179 HELIX 2 H2 VAL A 37 ASN A 39 5 3AAH 180 HELIX 3 H3 ALA A 96 VAL A 101 5 3AAH 181 HELIX 4 H4 LEU A 219 LYS A 222 1 3AAH 182 HELIX 5 H5 GLY A 226 ILE A 231 5 3AAH 183 HELIX 6 H6 VAL A 534 PHE A 538 1 3AAH 184 HELIX 7 H7 ALA A 549 ALA A 552 1 3AAH 185 HELIX 8 H8 LEU A 556 ASN A 558 5 3AAH 186 HELIX 9 H1 PRO B 34 ILE B 55 1 IN BETA SUBUNIT 3AAH 187 HELIX 10 H1 ASP C 3 THR C 8 1 3AAH 188 HELIX 11 H2 VAL C 37 ASN C 39 5 3AAH 189 HELIX 12 H3 ALA C 96 VAL C 101 5 3AAH 190 HELIX 13 H4 LEU C 219 LYS C 222 1 3AAH 191 HELIX 14 H5 ALA C 228 ILE C 231 5 3AAH 192 HELIX 15 H6 VAL C 534 VAL C 537 1 3AAH 193 HELIX 16 H7 ALA C 549 ALA C 552 1 3AAH 194 HELIX 17 H8 LEU C 556 ASN C 558 5 3AAH 195 HELIX 18 H1 PRO D 34 ALA D 56 1 IN BETA SUBUNIT 3AAH 196 SHEET 1 W1A 4 LEU A 59 ILE A 61 0 3AAH 197 SHEET 2 W1A 4 MET A 64 HIS A 68 -1 3AAH 198 SHEET 3 W1A 4 THR A 75 ASN A 79 -1 3AAH 199 SHEET 4 W1A 4 ILE A 86 HIS A 90 -1 3AAH 200 SHEET 1 W2A 4 ALA A 112 GLY A 114 0 3AAH 201 SHEET 2 W2A 4 GLN A 117 LYS A 121 -1 3AAH 202 SHEET 3 W2A 4 HIS A 126 ASP A 131 -1 3AAH 203 SHEET 4 W2A 4 ILE A 137 GLU A 142 -1 3AAH 204 SHEET 1 W3A 4 PHE A 157 ALA A 159 0 3AAH 205 SHEET 2 W3A 4 THR A 162 MET A 165 -1 3AAH 206 SHEET 3 W3A 4 ALA A 177 ASP A 182 -1 3AAH 207 SHEET 4 W3A 4 LEU A 188 PHE A 193 -1 3AAH 208 SHEET 1 W4A 4 ALA A 241 ASP A 243 0 3AAH 209 SHEET 2 W4A 4 LEU A 248 GLY A 252 -1 3AAH 210 SHEET 3 W4A 4 THR A 273 ASP A 278 -1 3AAH 211 SHEET 4 W4A 4 ALA A 284 GLN A 289 -1 3AAH 212 SHEET 1 W5A 4 VAL A 305 VAL A 311 0 3AAH 213 SHEET 2 W5A 4 LYS A 314 ILE A 322 -1 3AAH 214 SHEET 3 W5A 4 ILE A 327 ASN A 332 -1 3AAH 215 SHEET 4 W5A 4 LEU A 338 LYS A 343 -1 3AAH 216 SHEET 1 W6A 4 SER A 392 ASP A 394 0 3AAH 217 SHEET 2 W6A 4 THR A 399 ASN A 405 -1 3AAH 218 SHEET 3 W6A 4 GLY A 444 PHE A 449 -1 3AAH 219 SHEET 4 W6A 4 ALA A 456 GLU A 462 -1 3AAH 220 SHEET 1 W7A 4 LEU A 471 THR A 473 0 3AAH 221 SHEET 2 W7A 4 LEU A 477 ALA A 481 -1 3AAH 222 SHEET 3 W7A 4 TYR A 486 ASP A 491 -1 3AAH 223 SHEET 4 W7A 4 LYS A 496 LYS A 502 -1 3AAH 224 SHEET 1 W8A 4 LYS A 41 SER A 47 0 3AAH 225 SHEET 2 W8A 4 GLY A 565 SER A 570 -1 3AAH 226 SHEET 3 W8A 4 LYS A 519 TYR A 526 -1 3AAH 227 SHEET 4 W8A 4 MET A 512 PHE A 516 -1 3AAH 228 SHEET 1 S1A 5 PHE A 351 ASP A 355 0 3AAH 229 SHEET 2 S1A 5 THR A 360 ARG A 363 -1 3AAH 230 SHEET 3 S1A 5 GLY A 375 CYS A 379 -1 3AAH 231 SHEET 4 S1A 5 ILE A 407 PRO A 413 -1 3AAH 232 SHEET 5 S1A 5 ALA A 427 PRO A 433 -1 3AAH 233 SHEET 1 W1C 4 LEU C 59 ILE C 61 0 3AAH 234 SHEET 2 W1C 4 MET C 64 HIS C 68 -1 3AAH 235 SHEET 3 W1C 4 THR C 75 ASN C 79 -1 3AAH 236 SHEET 4 W1C 4 ILE C 86 HIS C 90 -1 3AAH 237 SHEET 1 W2C 4 ALA C 112 GLY C 114 0 3AAH 238 SHEET 2 W2C 4 GLN C 117 LYS C 121 -1 3AAH 239 SHEET 3 W2C 4 HIS C 126 ASP C 131 -1 3AAH 240 SHEET 4 W2C 4 ILE C 137 GLU C 142 -1 3AAH 241 SHEET 1 W3C 4 PHE C 157 ALA C 159 0 3AAH 242 SHEET 2 W3C 4 THR C 162 GLY C 166 -1 3AAH 243 SHEET 3 W3C 4 ALA C 177 ASP C 182 -1 3AAH 244 SHEET 4 W3C 4 LEU C 188 PHE C 193 -1 3AAH 245 SHEET 1 W4C 4 ALA C 241 ASP C 243 0 3AAH 246 SHEET 2 W4C 4 LEU C 248 GLY C 252 -1 3AAH 247 SHEET 3 W4C 4 THR C 273 ASP C 278 -1 3AAH 248 SHEET 4 W4C 4 ALA C 284 GLN C 289 -1 3AAH 249 SHEET 1 W5C 4 VAL C 305 VAL C 311 0 3AAH 250 SHEET 2 W5C 4 LYS C 314 ILE C 322 -1 3AAH 251 SHEET 3 W5C 4 ILE C 327 ASN C 332 -1 3AAH 252 SHEET 4 W5C 4 LEU C 338 LYS C 343 -1 3AAH 253 SHEET 1 W6C 4 SER C 392 ASP C 394 0 3AAH 254 SHEET 2 W6C 4 THR C 399 ASN C 405 -1 3AAH 255 SHEET 3 W6C 4 GLY C 444 ASP C 450 -1 3AAH 256 SHEET 4 W6C 4 LYS C 455 GLU C 462 -1 3AAH 257 SHEET 1 W7C 4 LEU C 471 THR C 473 0 3AAH 258 SHEET 2 W7C 4 LEU C 477 ALA C 481 -1 3AAH 259 SHEET 3 W7C 4 TYR C 486 ASP C 491 -1 3AAH 260 SHEET 4 W7C 4 GLU C 497 LYS C 502 -1 3AAH 261 SHEET 1 W8C 4 LYS C 41 SER C 47 0 3AAH 262 SHEET 2 W8C 4 GLY C 565 SER C 570 -1 3AAH 263 SHEET 3 W8C 4 LYS C 519 TYR C 526 -1 3AAH 264 SHEET 4 W8C 4 MET C 512 PHE C 516 -1 3AAH 265 SHEET 1 S1C 5 PHE C 351 VAL C 354 0 3AAH 266 SHEET 2 S1C 5 PRO C 361 ARG C 363 -1 3AAH 267 SHEET 3 S1C 5 GLY C 375 ILE C 378 -1 3AAH 268 SHEET 4 S1C 5 ILE C 407 PRO C 413 -1 3AAH 269 SHEET 5 S1C 5 ALA C 427 PRO C 433 -1 3AAH 270 SSBOND 1 CYS A 103 CYS A 104 3AAH 271 SSBOND 2 CYS A 144 CYS A 167 3AAH 272 SSBOND 3 CYS A 379 CYS A 408 3AAH 273 SSBOND 4 CYS B 6 CYS B 12 3AAH 274 SSBOND 5 CYS C 103 CYS C 104 3AAH 275 SSBOND 6 CYS C 144 CYS C 167 3AAH 276 SSBOND 7 CYS C 379 CYS C 408 3AAH 277 SSBOND 8 CYS D 6 CYS D 12 3AAH 278 CRYST1 124.900 62.700 85.000 90.00 93.40 90.00 P 21 4 3AAH 279 ORIGX1 1.000000 0.000000 0.000000 0.00000 3AAH 280 ORIGX2 0.000000 1.000000 0.000000 0.00000 3AAH 281 ORIGX3 0.000000 0.000000 1.000000 0.00000 3AAH 282 SCALE1 0.008006 0.000000 0.000476 0.00000 3AAH 283 SCALE2 0.000000 0.015949 0.000000 0.00000 3AAH 284 SCALE3 0.000000 0.000000 0.011785 0.00000 3AAH 285 MTRIX1 1 -0.995206 -0.096998 0.012534 -61.54386 1 3AAH 286 MTRIX2 1 -0.095040 0.989356 0.110190 -2.87807 1 3AAH 287 MTRIX3 1 -0.023089 0.108471 -0.993832 -1.53508 1 3AAH 288