HEADER ELECTRON TRANSPORT 17-DEC-93 2BBK 2BBK 2 COMPND METHYLAMINE DEHYDROGENASE (MADH) (E.C.1.4.99.3) 2BBK 3 SOURCE (PARACOCCUS DENITRIFICANS) 2BBK 4 AUTHOR L.CHEN,F.S.MATHEWS 2BBK 5 REVDAT 1 31-JAN-94 2BBK 0 2BBK 6 JRNL AUTH L.CHEN,M.DOI,F.S.MATHEWS,A.Y.CHISTOSERDOV, 2BBK 7 JRNL AUTH 2 M.E.LIDSTROM 2BBK 8 JRNL TITL CRYSTAL STRUCTURE OF THE QUINOPROTEIN METHYLAMINE 2BBK 9 JRNL TITL 2 DEHYDROGENASE FROM PARACOCCUS DENITRIFICANS AT 2BBK 10 JRNL TITL 3 1.75 ANGSTROMS 2BBK 11 JRNL REF TO BE PUBLISHED 2BBK 12 JRNL REFN 353 2BBK 13 REMARK 1 2BBK 14 REMARK 1 REFERENCE 1 2BBK 15 REMARK 1 AUTH L.CHEN,F.S.MATHEWS,V.L.DAVIDSON,E.G.HUIZINGA, 2BBK 16 REMARK 1 AUTH 2 F.M.D.VELLIEUX,W.G.J.HOL 2BBK 17 REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE QUINOPROTEIN 2BBK 18 REMARK 1 TITL 2 METHYLAMINE DEHYDROGENASE FROM PARACOCCUS 2BBK 19 REMARK 1 TITL 3 DENITRIFICANS DETERMINED BY MOLECULAR REPLACEMENT 2BBK 20 REMARK 1 TITL 4 AT 2.8 ANGSTROMS RESOLUTION 2BBK 21 REMARK 1 REF PROTEINS.STRUCT.,FUNCT., V. 14 288 1992 2BBK 22 REMARK 1 REF 2 GENET. 2BBK 23 REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 867 2BBK 24 REMARK 1 REFERENCE 2 2BBK 25 REMARK 1 AUTH A.Y.CHISTOSERDOV,J.BOYD,F.S.MATHEWS,M.E.LIDSTROM 2BBK 26 REMARK 1 TITL THE GENETIC ORGANIZATION OF THE MAU GENE CLUSTER 2BBK 27 REMARK 1 TITL 2 OF THE FACULTATIVE AUTOTROPH PARACOCCUS 2BBK 28 REMARK 1 TITL 3 DENITRIFICANS 2BBK 29 REMARK 1 REF BIOCHEM.BIOPHYS.RES.COMM. V. 184 1181 1992 2BBK 30 REMARK 1 REFN ASTM BBRCA9 US ISSN 0006-291X 146 2BBK 31 REMARK 1 REFERENCE 3 2BBK 32 REMARK 1 AUTH L.CHEN,F.S.MATHEWS,V.L.DAVIDSON,E.G.HUIZINGA, 2BBK 33 REMARK 1 AUTH 2 F.M.D.VELLIEUX,J.A.DUINE,W.G.J.HOL 2BBK 34 REMARK 1 TITL CRYSTALLOGRAPHIC INVESTIGATIONS OF THE 2BBK 35 REMARK 1 TITL 2 TRYPTOPHAN-DERIVED COFACTOR IN THE QUINOPROTEIN 2BBK 36 REMARK 1 TITL 3 METHYLAMINE DEHYDROGENASE 2BBK 37 REMARK 1 REF /FEBS$ LETT. V. 287 163 1991 2BBK 38 REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 165 2BBK 39 REMARK 1 REFERENCE 4 2BBK 40 REMARK 1 AUTH F.M.D.VELLIEUX,F.HUITEMA,H.GROENDIJK,K.H.KALK, 2BBK 41 REMARK 1 AUTH 2 J.FRANK JZN.,J.A.JONGEJAN,J.A.DUINE,K.PETRATOS, 2BBK 42 REMARK 1 AUTH 3 J.DRENTH,W.G.J.HOL 2BBK 43 REMARK 1 TITL STRUCTURE OF QUINOPROTEIN METHYLAMINE 2BBK 44 REMARK 1 TITL 2 DEHYDROGENASE AT 2.25 ANGSTROMS RESOLUTION 2BBK 45 REMARK 1 REF /EMBO$ J. V. 8 2171 1989 2BBK 46 REMARK 1 REFN ASTM EMJODG UK ISSN 0261-4189 897 2BBK 47 REMARK 2 2BBK 48 REMARK 2 RESOLUTION. 1.75 ANGSTROMS. 2BBK 49 REMARK 3 2BBK 50 REMARK 3 REFINEMENT. 2BBK 51 REMARK 3 PROGRAM TNT 2BBK 52 REMARK 3 AUTHORS TRONRUD,TEN EYCK,MATTHEWS 2BBK 53 REMARK 3 R VALUE 0.167 2BBK 54 REMARK 3 RMSD BOND DISTANCES 0.007 ANGSTROMS 2BBK 55 REMARK 3 RMSD BOND ANGLES 2.30 DEGREES 2BBK 56 REMARK 3 2BBK 57 REMARK 3 NUMBER OF REFLECTIONS 111755 2BBK 58 REMARK 3 RESOLUTION RANGE 11.0 - 1.75 ANGSTROMS 2BBK 59 REMARK 3 DATA CUTOFF 2.7 SIGMA(F) 2BBK 60 REMARK 3 PERCENT COMPLETION 96.8 2BBK 61 REMARK 3 2BBK 62 REMARK 3 NUMBER OF PROTEIN ATOMS 8030 2BBK 63 REMARK 3 NUMBER OF SOLVENT ATOMS 556 2BBK 64 REMARK 3 2BBK 65 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (TNT VALUES) 2BBK 66 REMARK 3 RMS VALUE(TOTAL #) 2BBK 67 REMARK 3 BOND DISTANCE (ANGSTROMS) 0.007 (7726) 2BBK 68 REMARK 3 ANGLE DISTANCE (DEGREE) 2.298 (10510) 2BBK 69 REMARK 3 TORSION ANGLES (DEGREE) 16.913 (4464) 2BBK 70 REMARK 3 TRIGONAL ATOM NON-PLANARITY 0.011 (192) 2BBK 71 REMARK 3 PLANAR GROUPS 0.020 (1132) 2BBK 72 REMARK 3 BAD CONTACTS (ANGSTROMS) 0.030 (73) 2BBK 73 REMARK 3 CHIRAL CENTER NO VIOLATION(1000) 2BBK 74 REMARK 4 2BBK 75 REMARK 4 THE ENZYME IS AN H2L2 HETERO-HEXAMER, WITH TWO DIFFERENT 2BBK 76 REMARK 4 SUBUNITS, HEAVY(H) AND LIGHT(L), FORMING TWO IDENTICAL HL 2BBK 77 REMARK 4 DIMERS RELATED BY A MOLECULAR TWO-FOLD AXIS. 2BBK 78 REMARK 4 THE HEAVY CHAINS HAVE BEEN ASSIGNED CHAIN INDICATORS H AND 2BBK 79 REMARK 4 J. THE LIGHT CHAINS HAVE BEEN ASSIGNED CHAIN INDICATORS 2BBK 80 REMARK 4 L AND M. THE CURRENT MODEL CONTAINS ONE H2L2 TETRAMER. 2BBK 81 REMARK 4 THIS INCLUDES RESIDUES 19 - 373 OF CHAINS H AND J, RESIDUES 2BBK 82 REMARK 4 7 - 131 OF CHAINS L AND M, PLUS 556 SOLVENT MOLECULES. 2BBK 83 REMARK 5 2BBK 84 REMARK 5 THE REDOX CENTERS OF MADH ARE LOCATED ON EACH L SUBUNIT. 2BBK 85 REMARK 5 EACH IS COMPOSED OF THE SIDE CHAINS OF TWO TRYPTOPHANS ON 2BBK 86 REMARK 5 THE L SUBUNIT, LINKED BY COVALENT BOND BETWEEN TWO INDOLE 2BBK 87 REMARK 5 RINGS. ONE INDOLE RING HAS AN ORTHO-QUINONE STRUCTURE. 2BBK 88 REMARK 5 THIS DOUBLE-TRYPTOPHAN SYSTEM IS CALLED TRYPTOPHAN 2BBK 89 REMARK 5 TRYPTOPHYL-QUINONE (TTQ). RESIDUE 57 OF CHAINS L AND M IS 2BBK 90 REMARK 5 ACTUALLY TRYPTOPHYLQUINONE. THE ADDITIONAL OXYGEN ATOMS 2BBK 91 REMARK 5 ARE PRESENTED AS RESIDUE OWQ AT THE END OF THE CHAINS. 2BBK 92 REMARK 6 2BBK 93 REMARK 6 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL 2BBK 94 REMARK 6 YIELD APPROXIMATE COORDINATES FOR CHAINS H AND L WHEN 2BBK 95 REMARK 6 APPLIED TO CHAINS J AND M, RESPECTIVELY. 2BBK 96 REMARK 7 2BBK 97 REMARK 7 THE SG ATOMS OF RESIDUES CYS L 23, CYS L 88, CYS M 23, AND 2BBK 98 REMARK 7 CYS M 88 EACH ARE PRESENTED IN TWO ALTERNATE CONFORMATIONS. 2BBK 99 REMARK 7 DURING REFINEMENT, THE OCCUPANCY WAS LEFT AT 1.0 FOR EACH 2BBK 100 REMARK 7 CONFORMATION WHILE THE B VALUES WERE REFINED. IN THIS 2BBK 101 REMARK 7 ENTRY, THE OCCUPANCY OF THESE ATOMS HAS BEEN SET 2BBK 102 REMARK 7 ARBITRARILY TO 0.5. 2BBK 103 SEQRES 1 H 355 ASP GLU PRO ARG ILE LEU GLU ALA PRO ALA PRO ASP ALA 2BBK 104 SEQRES 2 H 355 ARG ARG VAL TYR VAL ASN ASP PRO ALA HIS PHE ALA ALA 2BBK 105 SEQRES 3 H 355 VAL THR GLN GLN PHE VAL ILE ASP GLY GLU ALA GLY ARG 2BBK 106 SEQRES 4 H 355 VAL ILE GLY MET ILE ASP GLY GLY PHE LEU PRO ASN PRO 2BBK 107 SEQRES 5 H 355 VAL VAL ALA ASP ASP GLY SER PHE ILE ALA HIS ALA SER 2BBK 108 SEQRES 6 H 355 THR VAL PHE SER ARG ILE ALA ARG GLY GLU ARG THR ASP 2BBK 109 SEQRES 7 H 355 TYR VAL GLU VAL PHE ASP PRO VAL THR LEU LEU PRO THR 2BBK 110 SEQRES 8 H 355 ALA ASP ILE GLU LEU PRO ASP ALA PRO ARG PHE LEU VAL 2BBK 111 SEQRES 9 H 355 GLY THR TYR PRO TRP MET THR SER LEU THR PRO ASP GLY 2BBK 112 SEQRES 10 H 355 LYS THR LEU LEU PHE TYR GLN PHE SER PRO ALA PRO ALA 2BBK 113 SEQRES 11 H 355 VAL GLY VAL VAL ASP LEU GLU GLY LYS ALA PHE LYS ARG 2BBK 114 SEQRES 12 H 355 MET LEU ASP VAL PRO ASP CYS TYR HIS ILE PHE PRO THR 2BBK 115 SEQRES 13 H 355 ALA PRO ASP THR PHE PHE MET HIS CYS ARG ASP GLY SER 2BBK 116 SEQRES 14 H 355 LEU ALA LYS VAL ALA PHE GLY THR GLU GLY THR PRO GLU 2BBK 117 SEQRES 15 H 355 ILE THR HIS THR GLU VAL PHE HIS PRO GLU ASP GLU PHE 2BBK 118 SEQRES 16 H 355 LEU ILE ASN HIS PRO ALA TYR SER GLN LYS ALA GLY ARG 2BBK 119 SEQRES 17 H 355 LEU VAL TRP PRO THR TYR THR GLY LYS ILE HIS GLN ILE 2BBK 120 SEQRES 18 H 355 ASP LEU SER SER GLY ASP ALA LYS PHE LEU PRO ALA VAL 2BBK 121 SEQRES 19 H 355 GLU ALA LEU THR GLU ALA GLU ARG ALA ASP GLY TRP ARG 2BBK 122 SEQRES 20 H 355 PRO GLY GLY TRP GLN GLN VAL ALA TYR HIS ARG ALA LEU 2BBK 123 SEQRES 21 H 355 ASP ARG ILE TYR LEU LEU VAL ASP GLN ARG ASP GLU TRP 2BBK 124 SEQRES 22 H 355 ARG HIS LYS THR ALA SER ARG PHE VAL VAL VAL LEU ASP 2BBK 125 SEQRES 23 H 355 ALA LYS THR GLY GLU ARG LEU ALA LYS PHE GLU MET GLY 2BBK 126 SEQRES 24 H 355 HIS GLU ILE ASP SER ILE ASN VAL SER GLN ASP GLU LYS 2BBK 127 SEQRES 25 H 355 PRO LEU LEU TYR ALA LEU SER THR GLY ASP LYS THR LEU 2BBK 128 SEQRES 26 H 355 TYR ILE HIS ASP ALA GLU SER GLY GLU GLU LEU ARG SER 2BBK 129 SEQRES 27 H 355 VAL ASN GLN LEU GLY HIS GLY PRO GLN VAL ILE THR THR 2BBK 130 SEQRES 28 H 355 ALA ASP MET GLY 2BBK 131 SEQRES 1 L 125 THR ASP PRO ARG ALA LYS TRP VAL PRO GLN ASP ASN ASP 2BBK 132 SEQRES 2 L 125 ILE GLN ALA CYS ASP TYR TRP ARG HIS CYS SER ILE ASP 2BBK 133 SEQRES 3 L 125 GLY ASN ILE CYS ASP CYS SER GLY GLY SER LEU THR ASN 2BBK 134 SEQRES 4 L 125 CYS PRO PRO GLY THR LYS LEU ALA THR ALA SER TRP VAL 2BBK 135 SEQRES 5 L 125 ALA SER CYS TYR ASN PRO THR ASP GLY GLN SER TYR LEU 2BBK 136 SEQRES 6 L 125 ILE ALA TYR ARG ASP CYS CYS GLY TYR ASN VAL SER GLY 2BBK 137 SEQRES 7 L 125 ARG CYS PRO CYS LEU ASN THR GLU GLY GLU LEU PRO VAL 2BBK 138 SEQRES 8 L 125 TYR ARG PRO GLU PHE ALA ASN ASP ILE ILE TRP CYS PHE 2BBK 139 SEQRES 9 L 125 GLY ALA GLU ASP ASP ALA MET THR TYR HIS CYS THR ILE 2BBK 140 SEQRES 10 L 125 SER PRO ILE VAL GLY LYS ALA SER 2BBK 141 SEQRES 1 J 355 ASP GLU PRO ARG ILE LEU GLU ALA PRO ALA PRO ASP ALA 2BBK 142 SEQRES 2 J 355 ARG ARG VAL TYR VAL ASN ASP PRO ALA HIS PHE ALA ALA 2BBK 143 SEQRES 3 J 355 VAL THR GLN GLN PHE VAL ILE ASP GLY GLU ALA GLY ARG 2BBK 144 SEQRES 4 J 355 VAL ILE GLY MET ILE ASP GLY GLY PHE LEU PRO ASN PRO 2BBK 145 SEQRES 5 J 355 VAL VAL ALA ASP ASP GLY SER PHE ILE ALA HIS ALA SER 2BBK 146 SEQRES 6 J 355 THR VAL PHE SER ARG ILE ALA ARG GLY GLU ARG THR ASP 2BBK 147 SEQRES 7 J 355 TYR VAL GLU VAL PHE ASP PRO VAL THR LEU LEU PRO THR 2BBK 148 SEQRES 8 J 355 ALA ASP ILE GLU LEU PRO ASP ALA PRO ARG PHE LEU VAL 2BBK 149 SEQRES 9 J 355 GLY THR TYR PRO TRP MET THR SER LEU THR PRO ASP GLY 2BBK 150 SEQRES 10 J 355 LYS THR LEU LEU PHE TYR GLN PHE SER PRO ALA PRO ALA 2BBK 151 SEQRES 11 J 355 VAL GLY VAL VAL ASP LEU GLU GLY LYS ALA PHE LYS ARG 2BBK 152 SEQRES 12 J 355 MET LEU ASP VAL PRO ASP CYS TYR HIS ILE PHE PRO THR 2BBK 153 SEQRES 13 J 355 ALA PRO ASP THR PHE PHE MET HIS CYS ARG ASP GLY SER 2BBK 154 SEQRES 14 J 355 LEU ALA LYS VAL ALA PHE GLY THR GLU GLY THR PRO GLU 2BBK 155 SEQRES 15 J 355 ILE THR HIS THR GLU VAL PHE HIS PRO GLU ASP GLU PHE 2BBK 156 SEQRES 16 J 355 LEU ILE ASN HIS PRO ALA TYR SER GLN LYS ALA GLY ARG 2BBK 157 SEQRES 17 J 355 LEU VAL TRP PRO THR TYR THR GLY LYS ILE HIS GLN ILE 2BBK 158 SEQRES 18 J 355 ASP LEU SER SER GLY ASP ALA LYS PHE LEU PRO ALA VAL 2BBK 159 SEQRES 19 J 355 GLU ALA LEU THR GLU ALA GLU ARG ALA ASP GLY TRP ARG 2BBK 160 SEQRES 20 J 355 PRO GLY GLY TRP GLN GLN VAL ALA TYR HIS ARG ALA LEU 2BBK 161 SEQRES 21 J 355 ASP ARG ILE TYR LEU LEU VAL ASP GLN ARG ASP GLU TRP 2BBK 162 SEQRES 22 J 355 ARG HIS LYS THR ALA SER ARG PHE VAL VAL VAL LEU ASP 2BBK 163 SEQRES 23 J 355 ALA LYS THR GLY GLU ARG LEU ALA LYS PHE GLU MET GLY 2BBK 164 SEQRES 24 J 355 HIS GLU ILE ASP SER ILE ASN VAL SER GLN ASP GLU LYS 2BBK 165 SEQRES 25 J 355 PRO LEU LEU TYR ALA LEU SER THR GLY ASP LYS THR LEU 2BBK 166 SEQRES 26 J 355 TYR ILE HIS ASP ALA GLU SER GLY GLU GLU LEU ARG SER 2BBK 167 SEQRES 27 J 355 VAL ASN GLN LEU GLY HIS GLY PRO GLN VAL ILE THR THR 2BBK 168 SEQRES 28 J 355 ALA ASP MET GLY 2BBK 169 SEQRES 1 M 125 THR ASP PRO ARG ALA LYS TRP VAL PRO GLN ASP ASN ASP 2BBK 170 SEQRES 2 M 125 ILE GLN ALA CYS ASP TYR TRP ARG HIS CYS SER ILE ASP 2BBK 171 SEQRES 3 M 125 GLY ASN ILE CYS ASP CYS SER GLY GLY SER LEU THR ASN 2BBK 172 SEQRES 4 M 125 CYS PRO PRO GLY THR LYS LEU ALA THR ALA SER TRP VAL 2BBK 173 SEQRES 5 M 125 ALA SER CYS TYR ASN PRO THR ASP GLY GLN SER TYR LEU 2BBK 174 SEQRES 6 M 125 ILE ALA TYR ARG ASP CYS CYS GLY TYR ASN VAL SER GLY 2BBK 175 SEQRES 7 M 125 ARG CYS PRO CYS LEU ASN THR GLU GLY GLU LEU PRO VAL 2BBK 176 SEQRES 8 M 125 TYR ARG PRO GLU PHE ALA ASN ASP ILE ILE TRP CYS PHE 2BBK 177 SEQRES 9 M 125 GLY ALA GLU ASP ASP ALA MET THR TYR HIS CYS THR ILE 2BBK 178 SEQRES 10 M 125 SER PRO ILE VAL GLY LYS ALA SER 2BBK 179 FTNOTE 1 2BBK 180 FTNOTE 1 CIS PROLINE - PRO H 145 2BBK 181 FTNOTE 2 2BBK 182 FTNOTE 2 PHE H 193 - GLY H 194 OMEGA =218.52 2BBK 183 FTNOTE 2 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2BBK 184 FTNOTE 3 2BBK 185 FTNOTE 3 CIS PROLINE - PRO J 145 2BBK 186 HET OWQ L 57 2 OXYGENS BOUND TO INDOLE RING OF TRP L 57 2BBK 187 HET OWQ M 57 2 OXYGENS BOUND TO INDOLE RING OF TRP L 57 2BBK 188 FORMUL 5 OWQ 2(O2) 2BBK 189 FORMUL 6 HOH *556(H2 O1) 2BBK 190 HELIX 1 H1 THR H 256 GLY H 263 1 LINKING H4 AND H5 SHEETS 2BBK 191 HELIX 2 H2 THR J 256 GLY J 263 1 LINKING H4 AND H5 SHEETS 2BBK 192 SHEET 1 H1H 5 LEU H 67 ALA H 73 0 2BBK 193 SHEET 2 H1H 5 SER H 77 SER H 87 -1 2BBK 194 SHEET 3 H1H 5 GLY H 92 ASP H 102 -1 2BBK 195 SHEET 4 H1H 5 LEU H 107 LEU H 114 -1 2BBK 196 SHEET 5 H1H 5 ALA H 117 GLY H 123 -1 2BBK 197 SHEET 1 H2H 4 MET H 128 PRO H 133 0 2BBK 198 SHEET 2 H2H 4 LYS H 136 PHE H 143 -1 2BBK 199 SHEET 3 H2H 4 PRO H 147 GLU H 155 -1 2BBK 200 SHEET 4 H2H 4 LYS H 157 PRO H 166 -1 2BBK 201 SHEET 1 H3H 4 CYS H 168 THR H 174 0 2BBK 202 SHEET 2 H3H 4 ASP H 177 CYS H 183 -1 2BBK 203 SHEET 3 H3H 4 GLY H 186 GLY H 194 -1 2BBK 204 SHEET 4 H3H 4 GLY H 197 GLU H 205 -1 2BBK 205 SHEET 1 H4H 4 ASP H 211 SER H 221 0 2BBK 206 SHEET 2 H4H 4 ALA H 224 THR H 231 -1 2BBK 207 SHEET 3 H4H 4 GLY H 234 SER H 242 -1 2BBK 208 SHEET 4 H4H 4 GLY H 244 ALA H 254 -1 2BBK 209 SHEET 1 H5H 4 GLN H 271 ARG H 276 0 2BBK 210 SHEET 2 H5H 4 ASP H 279 LEU H 284 -1 2BBK 211 SHEET 3 H5H 4 ALA H 296 ASP H 304 -1 2BBK 212 SHEET 4 H5H 4 THR H 307 GLU H 319 -1 2BBK 213 SHEET 1 H6H 4 ASP H 321 ASP H 328 0 2BBK 214 SHEET 2 H6H 4 LYS H 330 THR H 338 -1 2BBK 215 SHEET 3 H6H 4 LYS H 341 ALA H 348 -1 2BBK 216 SHEET 4 H6H 4 SER H 350 ASN H 358 -1 2BBK 217 SHEET 1 H7H 4 GLY H 363 MET H 372 0 2BBK 218 SHEET 2 H7H 4 ALA H 31 ALA H 40 -1 2BBK 219 SHEET 3 H7H 4 THR H 46 GLY H 53 -1 2BBK 220 SHEET 4 H7H 4 GLY H 56 GLY H 65 -1 2BBK 221 SHEET 1 L1L 2 SER L 30 ILE L 35 0 2BBK 222 SHEET 2 L1L 2 CYS L 86 ASN L 90 -1 2BBK 223 SHEET 1 L2L 2 GLY L 40 SER L 42 0 2BBK 224 SHEET 2 L2L 2 ASN L 45 PRO L 47 -1 2BBK 225 SHEET 1 L3L 3 THR L 50 PRO L 64 0 2BBK 226 SHEET 2 L3L 3 GLN L 68 CYS L 78 -1 2BBK 227 SHEET 3 L3L 3 HIS L 120 SER L 131 -1 2BBK 228 SHEET 1 H1J 5 LEU J 67 ALA J 73 0 2BBK 229 SHEET 2 H1J 5 SER J 77 SER J 87 -1 2BBK 230 SHEET 3 H1J 5 GLY J 92 ASP J 102 -1 2BBK 231 SHEET 4 H1J 5 LEU J 107 LEU J 114 -1 2BBK 232 SHEET 5 H1J 5 ALA J 117 GLY J 123 -1 2BBK 233 SHEET 1 H2J 4 MET J 128 PRO J 133 0 2BBK 234 SHEET 2 H2J 4 LYS J 136 PHE J 143 -1 2BBK 235 SHEET 3 H2J 4 PRO J 147 GLU J 155 -1 2BBK 236 SHEET 4 H2J 4 LYS J 157 PRO J 166 -1 2BBK 237 SHEET 1 H3J 4 CYS J 168 THR J 174 0 2BBK 238 SHEET 2 H3J 4 ASP J 177 CYS J 183 -1 2BBK 239 SHEET 3 H3J 4 GLY J 186 GLY J 194 -1 2BBK 240 SHEET 4 H3J 4 GLY J 197 GLU J 205 -1 2BBK 241 SHEET 1 H4J 4 ASP J 211 SER J 221 0 2BBK 242 SHEET 2 H4J 4 ALA J 224 THR J 231 -1 2BBK 243 SHEET 3 H4J 4 GLY J 234 SER J 242 -1 2BBK 244 SHEET 4 H4J 4 GLY J 244 ALA J 254 -1 2BBK 245 SHEET 1 H5J 4 GLN J 271 ARG J 276 0 2BBK 246 SHEET 2 H5J 4 ASP J 279 LEU J 284 -1 2BBK 247 SHEET 3 H5J 4 ALA J 296 ASP J 304 -1 2BBK 248 SHEET 4 H5J 4 THR J 307 GLU J 319 -1 2BBK 249 SHEET 1 H6J 4 ASP J 321 ASP J 328 0 2BBK 250 SHEET 2 H6J 4 LYS J 330 THR J 338 -1 2BBK 251 SHEET 3 H6J 4 LYS J 341 ALA J 348 -1 2BBK 252 SHEET 4 H6J 4 SER J 350 ASN J 358 -1 2BBK 253 SHEET 1 H7J 4 GLY J 363 MET J 372 0 2BBK 254 SHEET 2 H7J 4 ALA J 31 ALA J 40 -1 2BBK 255 SHEET 3 H7J 4 THR J 46 GLY J 53 -1 2BBK 256 SHEET 4 H7J 4 GLY J 56 GLY J 65 -1 2BBK 257 SHEET 1 L1M 2 SER M 30 ILE M 35 0 2BBK 258 SHEET 2 L1M 2 CYS M 86 ASN M 90 -1 2BBK 259 SHEET 1 L2M 2 GLY M 40 SER M 42 0 2BBK 260 SHEET 2 L2M 2 ASN M 45 PRO M 47 -1 2BBK 261 SHEET 1 L3M 3 THR M 50 PRO M 64 0 2BBK 262 SHEET 2 L3M 3 GLN M 68 CYS M 78 -1 2BBK 263 SHEET 3 L3M 3 HIS M 120 SER M 131 -1 2BBK 264 SSBOND 1 CYS H 168 CYS H 183 2BBK 265 SSBOND 2 CYS L 23 CYS L 88 2BBK 266 SSBOND 3 CYS L 29 CYS L 61 2BBK 267 SSBOND 4 CYS L 36 CYS L 121 2BBK 268 SSBOND 5 CYS L 38 CYS L 86 2BBK 269 SSBOND 6 CYS L 46 CYS L 77 2BBK 270 SSBOND 7 CYS L 78 CYS L 109 2BBK 271 SSBOND 8 CYS J 168 CYS J 183 2BBK 272 SSBOND 9 CYS M 23 CYS M 88 2BBK 273 SSBOND 10 CYS M 29 CYS M 61 2BBK 274 SSBOND 11 CYS M 36 CYS M 121 2BBK 275 SSBOND 12 CYS M 38 CYS M 86 2BBK 276 SSBOND 13 CYS M 46 CYS M 77 2BBK 277 SSBOND 14 CYS M 78 CYS M 109 2BBK 278 SITE 1 TQL 2 TRP L 57 TRP L 108 2BBK 279 SITE 1 TQM 2 TRP M 57 TRP M 108 2BBK 280 CRYST1 152.070 135.920 55.260 90.00 90.00 90.00 P 21 21 21 4 2BBK 281 ORIGX1 1.000000 0.000000 0.000000 0.00000 2BBK 282 ORIGX2 0.000000 1.000000 0.000000 0.00000 2BBK 283 ORIGX3 0.000000 0.000000 1.000000 0.00000 2BBK 284 SCALE1 0.006576 0.000000 0.000000 0.00000 2BBK 285 SCALE2 0.000000 0.007357 0.000000 0.00000 2BBK 286 SCALE3 0.000000 0.000000 0.018096 0.00000 2BBK 287 MTRIX1 1 -0.992800 -0.048300 0.109500 119.01200 2BBK 288 MTRIX2 1 -0.040500 -0.725700 -0.686800 49.68700 2BBK 289 MTRIX3 1 0.112700 -0.686300 0.718600 12.33100 2BBK 290