HEADER OXIDOREDUCTASE(NAD(A)-CHOH(D)) 24-AUG-93 2OHX COMPND ALCOHOL DEHYDROGENASE (HOLO FORM) (E.C.1.1.1.1) COMPLEX COMPND 2 WITH NADH AND DMSO SOURCE HORSE (EQUUS CABALLUS) LIVER AUTHOR S.AL-KARADAGHI,E.S.CEDERGREN-ZEPPEZAUER REVDAT 1 31-OCT-93 2OHX 0 JRNL AUTH S.AL-KARADAGHI,E.S.CEDERGREN-ZEPPEZAUER,K.PETRATOS, JRNL AUTH 2 S.HOVMOELLER,H.TERRY,Z.DAUTER,K.S.WILSON JRNL TITL REFINED CRYSTAL STRUCTURE OF LIVER ALCOHOL JRNL TITL 2 DEHYDROGENASE-NADH COMPLEX AT 1.8 ANGSTROMS JRNL TITL 3 RESOLUTION JRNL REF TO BE PUBLISHED JRNL REFN 353 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH F.COLONNA-*CESARI,D.PERAHIA,M.KARPLUS,H.EKLUND, REMARK 1 AUTH 2 C.I.BRANDEN,O.TAPIA REMARK 1 TITL INTERDOMAIN MOTION IN LIVER ALCOHOL DEHYDROGENASE. REMARK 1 TITL 2 STRUCTURAL AND ENERGETIC ANALYSIS OF THE HINGE REMARK 1 TITL 3 BENDING MODE REMARK 1 REF J.BIOL.CHEM. V. 261 15273 1986 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 REMARK 1 REFERENCE 2 REMARK 1 AUTH H.EKLUND,J.-*P.SAMAMA,T.A.JONES REMARK 1 TITL CRYSTALLOGRAPHIC INVESTIGATIONS OF NICOTINAMIDE REMARK 1 TITL 2 ADENINE DINUCLEOTIDE BINDING TO HORSE LIVER ALCOHOL REMARK 1 TITL 3 DEHYDROGENASE REMARK 1 REF BIOCHEMISTRY V. 23 5982 1984 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 REMARK 1 REFERENCE 3 REMARK 1 AUTH G.SCHNEIDER,H.EKLUND,E.CEDERGREN-*ZEPPEZAUER, REMARK 1 AUTH 2 M.ZEPPEZAUER REMARK 1 TITL CRYSTAL STRUCTURES OF THE ACTIVE SITE IN REMARK 1 TITL 2 SPECIFICALLY METAL-DEPLETED AND COBALT-SUBSTITUTED REMARK 1 TITL 3 HORSE LIVER ALCOHOL DEHYDROGENASE DERIVATIVES REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 80 5289 1983 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 REMARK 1 REFERENCE 4 REMARK 1 AUTH B.V.PLAPP,H.EKLUND,T.A.JONES,C.-*I.BRANDEN REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF ISONICOTINIMIDYLATED REMARK 1 TITL 2 LIVER ALCOHOL DEHYDROGENASE REMARK 1 REF J.BIOL.CHEM. V. 258 5537 1983 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 REMARK 1 REFERENCE 5 REMARK 1 AUTH E.CEDERGREN-*ZEPPEZAUER REMARK 1 TITL CRYSTAL-*STRUCTURE DETERMINATION OF REDUCED REMARK 1 TITL 2 NICOTINAMIDE ADENINE DINUCLEOTIDE COMPLEX WITH REMARK 1 TITL 3 HORSE LIVER ALCOHOL DEHYDROGENASE MAINTAINED IN ITS REMARK 1 TITL 4 APO CONFORMATION BY ZINC-*BOUND IMIDAZOLE REMARK 1 REF BIOCHEMISTRY V. 22 5761 1983 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 REMARK 1 REFERENCE 6 REMARK 1 AUTH H.EKLUND,B.V.PLAPP,J.-*P.SAMAMA,C.-*I.BRANDEN REMARK 1 TITL BINDING OF SUBSTRATE IN A TERNARY COMPLEX OF HORSE REMARK 1 TITL 2 LIVER ALCOHOL DEHYDROGENASE REMARK 1 REF J.BIOL.CHEM. V. 257 14349 1982 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 REMARK 1 REFERENCE 7 REMARK 1 AUTH E.CEDERGREN-*ZEPPEZAUER,J.-*P.SAMAMA,H.EKLUND REMARK 1 TITL CRYSTAL STRUCTURE DETERMINATIONS OF COENZYME REMARK 1 TITL 2 ANALOGUE AND SUBSTRATE COMPLEXES OF LIVER ALCOHOL REMARK 1 TITL 3 DEHYDROGENASE. BINDING OF REMARK 1 TITL 4 1,4,5,6-*TETRAHYDRONICOTINAMIDE ADENINE REMARK 1 TITL 5 DINUCLEOTIDE AND REMARK 1 TITL 6 $TRANS-4-(N,N-*DIMETHYLAMINO)CINNAMALDEHYDE TO THE REMARK 1 TITL 7 ENZYME REMARK 1 REF BIOCHEMISTRY V. 21 4895 1982 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 REMARK 1 REFERENCE 8 REMARK 1 AUTH H.EKLUND,J.-*P.SAMAMA,L.WALLEN REMARK 1 TITL PYRAZOLE BINDING IN CRYSTALLINE BINARY AND TERNARY REMARK 1 TITL 2 COMPLEXES WITH LIVER ALCOHOL DEHYDROGENASE REMARK 1 REF BIOCHEMISTRY V. 21 4858 1982 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 033 REMARK 1 REFERENCE 9 REMARK 1 AUTH J.-*P.SAMAMA,A.D.WRIXON,J.-*F.BIELLMANN REMARK 1 TITL 5-*METHYLNICOTINAMIDE-ADENINE DINUCLEOTIDE. KINETIC REMARK 1 TITL 2 INVESTIGATION WITH MAJOR AND MINOR ISOENZYMES OF REMARK 1 TITL 3 LIVER ALCOHOL DEHYDROGENASE AND STRUCTURAL REMARK 1 TITL 4 DETERMINATION OF ITS BINARY COMPLEX WITH ALCOHOL REMARK 1 TITL 5 DEHYDROGENASE REMARK 1 REF EUR.J.BIOCHEM. V. 118 479 1981 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 262 REMARK 1 REFERENCE 10 REMARK 1 AUTH H.EKLUND,J.-*P.SAMAMA,L.WALLEN,C.-*I.BRANDEN, REMARK 1 AUTH 2 A.AKESON,T.A.JONES REMARK 1 TITL STRUCTURE OF TRICLINIC TERNARY COMPLEX OF HORSE REMARK 1 TITL 2 LIVER ALCOHOL DEHYDROGENASE AT 2.9 ANGSTROMS REMARK 1 TITL 3 RESOLUTION REMARK 1 REF J.MOL.BIOL. V. 146 561 1981 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REFERENCE 11 REMARK 1 AUTH H.EKLUND,C.-*I.BRANDEN REMARK 1 TITL STRUCTURAL DIFFERENCES BETWEEN APO- AND HOLOENZYME REMARK 1 TITL 2 OF HORSE LIVER ALCOHOL DEHYDROGENASE REMARK 1 REF J.BIOL.CHEM. V. 254 3458 1979 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 REMARK 1 REFERENCE 12 REMARK 1 AUTH J.-*F.BIELLMANN,J.-*P.SAMAMA,C.I.BRANDEN,H.EKLUND REMARK 1 TITL X-*RAY STUDIES OF THE BINDING OF CIBACRON BLUE REMARK 1 TITL 2 /F3GA$ TO LIVER ALCOHOL DEHYDROGENASE REMARK 1 REF EUR.J.BIOCHEM. V. 102 107 1979 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 262 REMARK 1 REFERENCE 13 REMARK 1 AUTH B.V.PLAPP,H.EKLUND,C.-*I.BRANDEN REMARK 1 TITL CRYSTALLOGRAPHY OF LIVER ALCOHOL DEHYDROGENASE REMARK 1 TITL 2 COMPLEXED WITH SUBSTRATES REMARK 1 REF J.MOL.BIOL. V. 122 23 1978 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REFERENCE 14 REMARK 1 AUTH B.V.PLAPP,E.ZEPPEZAUER,C.-*I.BRANDEN REMARK 1 TITL CRYSTALLIZATION OF LIVER ALCOHOL DEHYDROGENASE REMARK 1 TITL 2 ACTIVATED BY THE MODIFICATION OF AMINO GROUPS REMARK 1 REF J.MOL.BIOL. V. 119 451 1978 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REFERENCE 15 REMARK 1 AUTH H.JORNVALL,H.EKLUND,C.-*I.BRANDEN REMARK 1 TITL SUBUNIT CONFORMATION OF YEAST ALCOHOL DEHYDROGENASE REMARK 1 REF J.BIOL.CHEM. V. 253 8414 1978 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 REMARK 1 REFERENCE 16 REMARK 1 AUTH J.-*P.SAMAMA,E.ZEPPEZAUER,J.-*F.BIELLMANN, REMARK 1 AUTH 2 C.-*I.BRANDEN REMARK 1 TITL THE CRYSTAL STRUCTURE OF COMPLEXES BETWEEN HORSE REMARK 1 TITL 2 LIVER ALCOHOL DEHYDROGENASE AND THE COENZYME REMARK 1 TITL 3 ANALOGUES 3-*IODOPYRIDINE-ADENINE DINUCLEOTIDE REMARK 1 TITL 4 AND PYRIDINE-ADENINE DINUCLEOTIDE REMARK 1 REF EUR.J.BIOCHEM. V. 81 403 1977 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 262 REMARK 1 REFERENCE 17 REMARK 1 AUTH T.BOIWE,C.-*I.BRANDEN REMARK 1 TITL X-*RAY INVESTIGATION OF THE BINDING OF REMARK 1 TITL 2 1,10-*PHENANTHROLINE AND IMIDAZOLE TO HORSE-*LIVER REMARK 1 TITL 3 ALCOHOL DEHYDROGENASE REMARK 1 REF EUR.J.BIOCHEM. V. 77 173 1977 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 262 REMARK 1 REFERENCE 18 REMARK 1 AUTH H.EKLUND,B.NORDSTROM,E.ZEPPEZAUER,G.SODERLUND, REMARK 1 AUTH 2 I.OHLSSON,T.BOIWE,B.-*O.SODERBERG,O.TAPIA, REMARK 1 AUTH 3 C.-*I.BRANDEN,A.AKESON REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF HORSE LIVER ALCOHOL REMARK 1 TITL 2 DEHYDROGENASE AT 2.4 ANGSTROMS RESOLUTION REMARK 1 REF J.MOL.BIOL. V. 102 27 1976 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REFERENCE 19 REMARK 1 AUTH H.EKLUND,C.-*I.BRANDEN,H.JORNVALL REMARK 1 TITL STRUCTURAL COMPARISONS OF MAMMALIAN, YEAST AND REMARK 1 TITL 2 BACILLAR ALCOHOL DEHYDROGENASES REMARK 1 REF J.MOL.BIOL. V. 102 61 1976 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REFERENCE 20 REMARK 1 AUTH B.NORDSTROM,C.-*I.BRANDEN REMARK 1 TITL THE BINDING OF NUCLEOTIDES TO HORSE LIVER ALCOHOL REMARK 1 TITL 2 DEHYDROGENASE REMARK 1 EDIT M.SUNDARALINGAM,S.T.RAO REMARK 1 REF STRUCTURE AND CONFORMATION 387 1975 REMARK 1 REF 2 OF NUCLEIC ACIDS AND REMARK 1 REF 3 PROTEIN-NUCLEIC ACID REMARK 1 REF 4 INTERACTIONS REMARK 1 PUBL UNIVERSITY PARK PRESS, BALTIMORE REMARK 1 REFN ISBN 0-8391-0764-1 992 REMARK 1 REFERENCE 21 REMARK 1 AUTH C.-*I.BRANDEN,H.JORNVALL,H.EKLUND,B.FURUGREN REMARK 1 TITL ALCOHOL DEHYDROGENASES REMARK 1 EDIT P.D.BOYER REMARK 1 REF THE ENZYMES,THIRD EDITION V. 11 103 1975 REMARK 1 PUBL ACADEMIC PRESS,NEW YORK REMARK 1 REFN ISBN 0-12-122711-1 436 REMARK 1 REFERENCE 22 REMARK 1 AUTH M.A.ABDALLAH,J.-*F.BIELLMANN,B.NORDSTROM, REMARK 1 AUTH 2 C.-*I.BRANDEN REMARK 1 TITL THE CONFORMATION OF ADENOSINE DIPHOSPHORIBOSE AND REMARK 1 TITL 2 8-*BROMOADENOSINE DIPHOSPHORIBOSE WHEN BOUND TO REMARK 1 TITL 3 LIVER ALCOHOL DEHYDROGENASE REMARK 1 REF EUR.J.BIOCHEM. V. 50 475 1975 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 262 REMARK 1 REFERENCE 23 REMARK 1 AUTH H.EKLUND,B.NORDSTROM,E.ZEPPEZAUER,G.SODERLUND, REMARK 1 AUTH 2 I.OHLSSON,T.BOIWE,C.-*I.BRANDEN REMARK 1 TITL THE STRUCTURE OF HORSE LIVER ALCOHOL DEHYDROGENASE REMARK 1 REF /FEBS$ LETT. V. 44 200 1974 REMARK 1 REFN ASTM FEBLAL NE ISSN 0014-5793 165 REMARK 1 REFERENCE 24 REMARK 1 AUTH I.OHLSSON,B.NORDSTROM,C.-*I.BRANDEN REMARK 1 TITL STRUCTURAL AND FUNCTIONAL SIMILARITIES WITHIN THE REMARK 1 TITL 2 COENZYME BINDING DOMAINS OF DEHYDROGENASES REMARK 1 REF J.MOL.BIOL. V. 89 339 1974 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REFERENCE 25 REMARK 1 AUTH R.EINARSSON,H.EKLUND,E.ZEPPEZAUER,T.BOIWE, REMARK 1 AUTH 2 C.-*I.BRANDEN REMARK 1 TITL BINDING OF SALICYLATE IN THE ADENOSINE-*BINDING REMARK 1 TITL 2 POCKET OF DEHYDROGENASES REMARK 1 REF EUR.J.BIOCHEM. V. 49 41 1974 REMARK 1 REFN ASTM EJBCAI IX ISSN 0014-2956 262 REMARK 1 REFERENCE 26 REMARK 1 AUTH C.-*I.BRANDEN,H.EKLUND,B.NORDSTROM,T.BOIWE, REMARK 1 AUTH 2 G.SODERLUND,E.ZEPPEZAUER,I.OHLSSON,A.AKESON REMARK 1 TITL STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE AT REMARK 1 TITL 2 2.9-*ANGSTROMS RESOLUTION REMARK 1 REF PROC.NAT.ACAD.SCI.USA V. 70 2439 1973 REMARK 1 REFN ASTM PNASA6 US ISSN 0027-8424 040 REMARK 1 REFERENCE 27 REMARK 1 AUTH C.-*I.BRANDEN REMARK 1 TITL STRUCTURE OF HORSE LIVER ALCOHOL DEHYDROGENASE. I. REMARK 1 TITL 2 STRUCTURAL SYMMETRY AND CONFORMATIONAL CHANGES REMARK 1 REF ARCH.BIOCHEM.BIOPHYS. V. 112 215 1965 REMARK 1 REFN ASTM ABBIA4 US ISSN 0003-9861 158 REMARK 1 REFERENCE 28 REMARK 1 EDIT M.O.DAYHOFF REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 145 1972 REMARK 1 REF 2 AND STRUCTURE (DATA SECTION) REMARK 1 PUBL NATIONAL BIOMEDICAL RESEARCH FOUNDATION, REMARK 1 PUBL 2 SILVER SPRING,MD. REMARK 1 REFN ISBN 0-912466-02-2 435 REMARK 2 REMARK 2 RESOLUTION. 1.8 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM X-PLOR REMARK 3 AUTHORS BRUNGER REMARK 3 R VALUE 0.173 REMARK 3 RMSD BOND DISTANCES 0.014 ANGSTROMS REMARK 3 RMSD BOND ANGLES 2.91 DEGREES REMARK 3 REMARK 3 RESOLUTION RANGE 10.0 - 1.8 ANGSTROMS REMARK 3 DATA CUTOFF 0.0 SIGMA(F) REMARK 3 REMARK 3 NUMBER OF PROTEIN ATOMS 5576 REMARK 3 NUMBER OF SOLVENT ATOMS 459 REMARK 4 REMARK 4 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL REMARK 4 YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO REMARK 4 CHAIN *A*. REMARK 4 REMARK 4 CORRESPONDING EULERIAN ANGLES (THETA1,THETA2,THETA3) REMARK 4 312.0201 171.9573 229.7686 REMARK 4 CORRESPONDING SPHERICAL POLAR ANGLES (PSI,PHI,KAPPA) REMARK 4 48.9973 5.3312 179.8746 REMARK 4 CORRESPONDING ROTATION ANGLE 179.8746 ABOUT AXIS REMARK 4 0.7514 0.6561 -0.0701 REMARK 5 REMARK 5 GLY 181 - VAL 189 IS A PI-HELIX (CLASS 3, 1.5 TURNS) AT REMARK 5 HELIX IDENTIFICATION HAA AND HAB. REMARK 6 REMARK 6 SITE *DMA* COMPRISES THE RESIDUES OF THE *A* CHAIN REMARK 6 INTERACTING WITH THE DMSO OF THE *A* CHAIN. SITE *DMB* REMARK 6 COMPRISES THE RESIDUES OF THE *B* CHAIN INTERACTING WITH REMARK 6 THE DMSO OF THE *B* CHAIN. SITE *NAA* COMPRISES THE REMARK 6 RESIDUES OF THE *A* CHAIN INTERACTING WITH THE NAD OF THE REMARK 6 *A* CHAIN. SITE *NAB* COMPRISES THE RESIDUES OF THE *B* REMARK 6 CHAIN INTERACTING WITH THE NAD OF THE *B* CHAIN. SEQRES 1 A 374 SER THR ALA GLY LYS VAL ILE LYS CYS LYS ALA ALA VAL SEQRES 2 A 374 LEU TRP GLU GLU LYS LYS PRO PHE SER ILE GLU GLU VAL SEQRES 3 A 374 GLU VAL ALA PRO PRO LYS ALA HIS GLU VAL ARG ILE LYS SEQRES 4 A 374 MET VAL ALA THR GLY ILE CYS ARG SER ASP ASP HIS VAL SEQRES 5 A 374 VAL SER GLY THR LEU VAL THR PRO LEU PRO VAL ILE ALA SEQRES 6 A 374 GLY HIS GLU ALA ALA GLY ILE VAL GLU SER ILE GLY GLU SEQRES 7 A 374 GLY VAL THR THR VAL ARG PRO GLY ASP LYS VAL ILE PRO SEQRES 8 A 374 LEU PHE THR PRO GLN CYS GLY LYS CYS ARG VAL CYS LYS SEQRES 9 A 374 HIS PRO GLU GLY ASN PHE CYS LEU LYS ASN ASP LEU SER SEQRES 10 A 374 MET PRO ARG GLY THR MET GLN ASP GLY THR SER ARG PHE SEQRES 11 A 374 THR CYS ARG GLY LYS PRO ILE HIS HIS PHE LEU GLY THR SEQRES 12 A 374 SER THR PHE SER GLN TYR THR VAL VAL ASP GLU ILE SER SEQRES 13 A 374 VAL ALA LYS ILE ASP ALA ALA SER PRO LEU GLU LYS VAL SEQRES 14 A 374 CYS LEU ILE GLY CYS GLY PHE SER THR GLY TYR GLY SER SEQRES 15 A 374 ALA VAL LYS VAL ALA LYS VAL THR GLN GLY SER THR CYS SEQRES 16 A 374 ALA VAL PHE GLY LEU GLY GLY VAL GLY LEU SER VAL ILE SEQRES 17 A 374 MET GLY CYS LYS ALA ALA GLY ALA ALA ARG ILE ILE GLY SEQRES 18 A 374 VAL ASP ILE ASN LYS ASP LYS PHE ALA LYS ALA LYS GLU SEQRES 19 A 374 VAL GLY ALA THR GLU CYS VAL ASN PRO GLN ASP TYR LYS SEQRES 20 A 374 LYS PRO ILE GLN GLU VAL LEU THR GLU MET SER ASN GLY SEQRES 21 A 374 GLY VAL ASP PHE SER PHE GLU VAL ILE GLY ARG LEU ASP SEQRES 22 A 374 THR MET VAL THR ALA LEU SER CYS CYS GLN GLU ALA TYR SEQRES 23 A 374 GLY VAL SER VAL ILE VAL GLY VAL PRO PRO ASP SER GLN SEQRES 24 A 374 ASN LEU SER MET ASN PRO MET LEU LEU LEU SER GLY ARG SEQRES 25 A 374 THR TRP LYS GLY ALA ILE PHE GLY GLY PHE LYS SER LYS SEQRES 26 A 374 ASP SER VAL PRO LYS LEU VAL ALA ASP PHE MET ALA LYS SEQRES 27 A 374 LYS PHE ALA LEU ASP PRO LEU ILE THR HIS VAL LEU PRO SEQRES 28 A 374 PHE GLU LYS ILE ASN GLU GLY PHE ASP LEU LEU ARG SER SEQRES 29 A 374 GLY GLU SER ILE ARG THR ILE LEU THR PHE SEQRES 1 B 374 SER THR ALA GLY LYS VAL ILE LYS CYS LYS ALA ALA VAL SEQRES 2 B 374 LEU TRP GLU GLU LYS LYS PRO PHE SER ILE GLU GLU VAL SEQRES 3 B 374 GLU VAL ALA PRO PRO LYS ALA HIS GLU VAL ARG ILE LYS SEQRES 4 B 374 MET VAL ALA THR GLY ILE CYS ARG SER ASP ASP HIS VAL SEQRES 5 B 374 VAL SER GLY THR LEU VAL THR PRO LEU PRO VAL ILE ALA SEQRES 6 B 374 GLY HIS GLU ALA ALA GLY ILE VAL GLU SER ILE GLY GLU SEQRES 7 B 374 GLY VAL THR THR VAL ARG PRO GLY ASP LYS VAL ILE PRO SEQRES 8 B 374 LEU PHE THR PRO GLN CYS GLY LYS CYS ARG VAL CYS LYS SEQRES 9 B 374 HIS PRO GLU GLY ASN PHE CYS LEU LYS ASN ASP LEU SER SEQRES 10 B 374 MET PRO ARG GLY THR MET GLN ASP GLY THR SER ARG PHE SEQRES 11 B 374 THR CYS ARG GLY LYS PRO ILE HIS HIS PHE LEU GLY THR SEQRES 12 B 374 SER THR PHE SER GLN TYR THR VAL VAL ASP GLU ILE SER SEQRES 13 B 374 VAL ALA LYS ILE ASP ALA ALA SER PRO LEU GLU LYS VAL SEQRES 14 B 374 CYS LEU ILE GLY CYS GLY PHE SER THR GLY TYR GLY SER SEQRES 15 B 374 ALA VAL LYS VAL ALA LYS VAL THR GLN GLY SER THR CYS SEQRES 16 B 374 ALA VAL PHE GLY LEU GLY GLY VAL GLY LEU SER VAL ILE SEQRES 17 B 374 MET GLY CYS LYS ALA ALA GLY ALA ALA ARG ILE ILE GLY SEQRES 18 B 374 VAL ASP ILE ASN LYS ASP LYS PHE ALA LYS ALA LYS GLU SEQRES 19 B 374 VAL GLY ALA THR GLU CYS VAL ASN PRO GLN ASP TYR LYS SEQRES 20 B 374 LYS PRO ILE GLN GLU VAL LEU THR GLU MET SER ASN GLY SEQRES 21 B 374 GLY VAL ASP PHE SER PHE GLU VAL ILE GLY ARG LEU ASP SEQRES 22 B 374 THR MET VAL THR ALA LEU SER CYS CYS GLN GLU ALA TYR SEQRES 23 B 374 GLY VAL SER VAL ILE VAL GLY VAL PRO PRO ASP SER GLN SEQRES 24 B 374 ASN LEU SER MET ASN PRO MET LEU LEU LEU SER GLY ARG SEQRES 25 B 374 THR TRP LYS GLY ALA ILE PHE GLY GLY PHE LYS SER LYS SEQRES 26 B 374 ASP SER VAL PRO LYS LEU VAL ALA ASP PHE MET ALA LYS SEQRES 27 B 374 LYS PHE ALA LEU ASP PRO LEU ILE THR HIS VAL LEU PRO SEQRES 28 B 374 PHE GLU LYS ILE ASN GLU GLY PHE ASP LEU LEU ARG SER SEQRES 29 B 374 GLY GLU SER ILE ARG THR ILE LEU THR PHE FTNOTE 1 FTNOTE 1 RESIDUES PRO A 62 AND PRO B 62 ARE CIS PROLINES. FTNOTE 2 FTNOTE 2 THE FOLLOWING RESIDUES WERE DISCRETELY DISORDERED: FTNOTE 2 CYS A 281, CYS A 282, AND CYS B 282 HET ZN A 401 1 ZINC(II) CATALYTICALLY ACTIVE METAL ION HET ZN A 402 1 ZINC(II) CATALYTICALLY ACTIVE METAL ION HET NAD A 403 44 NICOTINAMIDE-ADENINE-DINUCLEOTIDE HET DMS A 404 4 DIMETHYL SULFOXIDE HET ZN B 401 1 ZINC(II) CATALYTICALLY ACTIVE METAL ION HET ZN B 402 1 ZINC(II) CATALYTICALLY ACTIVE METAL ION HET NAD B 403 44 NICOTINAMIDE-ADENINE-DINUCLEOTIDE HET DMS B 404 4 DIMETHYL SULFOXIDE FORMUL 3 ZN 4(ZN1 ++) FORMUL 4 NAD 2(C21 H28 N7 O14 P2) FORMUL 5 DMS 2(C2 H6 O1 S1) FORMUL 6 HOH *459(H2 O1) HELIX 1 H1A CYS A 46 THR A 56 1 HELIX 2 H2A PRO A 165 PHE A 176 1 HELIX 3 HAA SER A 177 VAL A 189 1 HELIX 4 HBA GLY A 201 ALA A 216 1 HELIX 5 HCA ASN A 225 ALA A 237 1 HELIX 6 HDA PRO A 249 GLY A 260 1 HELIX 7 HEA ARG A 271 CYS A 282 1 HELIX 8 S5A ASN A 304 GLY A 311 5 3/10 HELIX HELIX 9 H3A LYS A 323 LYS A 338 1 HELIX 10 H4A LYS A 354 GLY A 365 1 HELIX 11 H1B CYS B 46 THR B 56 1 HELIX 12 H2B PRO B 165 PHE B 176 1 HELIX 13 HAB SER B 177 VAL B 189 1 SEE REMARK 4 HELIX 14 HBB GLY B 201 ALA B 216 1 HELIX 15 HCB ASN B 225 ALA B 237 1 HELIX 16 HDB PRO B 249 GLY B 260 1 HELIX 17 HEB ARG B 271 CYS B 282 1 HELIX 18 S5B ASN B 304 GLY B 311 5 3/10 HELIX HELIX 19 H3B LYS B 323 LYS B 338 1 HELIX 20 H4B LYS B 354 GLY B 365 1 SHEET 1 S1A 4 GLU A 68 ALA A 70 0 SHEET 2 S1A 4 VAL A 41 ILE A 45 -1 N ALA A 42 O ALA A 70 SHEET 3 S1A 4 ARG A 369 PHE A 374 -1 N LEU A 372 O THR A 43 SHEET 4 S1A 4 LEU A 345 PHE A 352 1 N LEU A 350 O ILE A 371 SHEET 1 S2A 5 GLN A 148 VAL A 152 0 SHEET 2 S2A 5 GLU A 35 MET A 40 -1 N ILE A 38 O THR A 150 SHEET 3 S2A 5 GLY A 71 GLY A 77 -1 N GLU A 74 O ARG A 37 SHEET 4 S2A 5 GLY A 86 LEU A 92 -1 O ASP A 87 N VAL A 73 SHEET 5 S2A 5 SER A 156 ILE A 160 -1 N ALA A 158 O ILE A 90 SHEET 1 S3A 6 ILE A 7 VAL A 13 0 SHEET 2 S3A 6 SER A 22 ALA A 29 -1 O GLU A 24 N ALA A 11 SHEET 3 S3A 6 ARG A 129 CYS A 132 -1 O THR A 131 N GLU A 27 SHEET 4 S3A 6 LYS A 135 HIS A 138 -1 O LYS A 135 N CYS A 132 SHEET 5 S3A 6 PRO A 62 GLY A 66 1 O PRO A 62 N HIS A 138 SHEET 6 S3A 6 THR A 145 PHE A 146 1 N THR A 145 O GLY A 66 SHEET 1 S4A 6 THR A 238 VAL A 241 0 SHEET 2 S4A 6 GLY A 215 ASP A 223 1 O ILE A 219 N THR A 238 SHEET 3 S4A 6 GLY A 192 GLY A 199 1 O CYS A 195 N ILE A 220 SHEET 4 S4A 6 VAL A 262 VAL A 268 1 O PHE A 264 N ALA A 196 SHEET 5 S4A 6 GLY A 287 GLY A 293 1 O VAL A 290 N GLU A 267 SHEET 6 S4A 6 THR A 313 ALA A 317 1 O THR A 313 N SER A 289 SHEET 1 S1B 4 GLU B 68 ALA B 70 0 SHEET 2 S1B 4 VAL B 41 ILE B 45 -1 N ALA B 42 O ALA B 70 SHEET 3 S1B 4 ARG B 369 PHE B 374 -1 N LEU B 372 O THR B 43 SHEET 4 S1B 4 LEU B 345 PHE B 352 1 N LEU B 350 O ILE B 371 SHEET 1 S2B 5 GLN B 148 VAL B 152 0 SHEET 2 S2B 5 GLU B 35 MET B 40 -1 N ILE B 38 O THR B 150 SHEET 3 S2B 5 GLY B 71 GLY B 77 -1 N GLU B 74 O ARG B 37 SHEET 4 S2B 5 GLY B 86 LEU B 92 -1 O ASP B 87 N VAL B 73 SHEET 5 S2B 5 SER B 156 ILE B 160 -1 N ALA B 158 O ILE B 90 SHEET 1 S3B 6 ILE B 7 VAL B 13 0 SHEET 2 S3B 6 SER B 22 ALA B 29 -1 O GLU B 24 N ALA B 11 SHEET 3 S3B 6 ARG B 129 CYS B 132 -1 O THR B 131 N GLU B 27 SHEET 4 S3B 6 LYS B 135 HIS B 138 -1 O LYS B 135 N CYS B 132 SHEET 5 S3B 6 PRO B 62 GLY B 66 1 O PRO B 62 N HIS B 138 SHEET 6 S3B 6 THR B 145 PHE B 146 1 N THR B 145 O GLY B 66 SHEET 1 S4B 6 THR B 238 VAL B 241 0 SHEET 2 S4B 6 GLY B 215 ASP B 223 1 O ILE B 219 N THR B 238 SHEET 3 S4B 6 GLY B 192 GLY B 199 1 O CYS B 195 N ILE B 220 SHEET 4 S4B 6 VAL B 262 VAL B 268 1 O PHE B 264 N ALA B 196 SHEET 5 S4B 6 GLY B 287 GLY B 293 1 O VAL B 290 N GLU B 267 SHEET 6 S4B 6 THR B 313 ALA B 317 1 O THR B 313 N SER B 289 TURN 1 1A GLU A 16 LYS A 19 TYPE II TURN 2 2A LYS A 32 GLU A 35 TYPE II TURN 3 3A GLY A 77 VAL A 80 TYPE II TURN 4 4A ARG A 84 ASP A 87 TYPE II TURN 5 5A CYS A 111 ASN A 114 TYPE I TURN 6 6A MET A 123 GLY A 126 TYPE I TURN 7 7A CYS A 132 LYS A 135 TYPE I' TURN 8 8A PHE A 140 THR A 143 TYPE I' TURN 9 9A ASP A 153 SER A 156 TYPE I TURN 10 10A ASP A 161 SER A 164 TYPE I TURN 11 11A THR A 190 SER A 193 TYPE II TURN 12 12A GLN A 283 TYR A 286 TYPE I TURN 13 13A PRO A 296 GLN A 299 TYPE II TURN 14 14A PHE A 319 PHE A 322 TYPE I' TURN 15 15A PRO A 351 LYS A 354 TYPE I TURN 16 1B GLU B 16 LYS B 19 TYPE II TURN 17 2B LYS B 32 GLU B 35 TYPE II TURN 18 3B GLY B 77 VAL B 80 TYPE II TURN 19 4B ARG B 84 ASP B 87 TYPE II TURN 20 5B CYS B 111 ASN B 114 TYPE I TURN 21 6B MET B 123 GLY B 126 TYPE I TURN 22 7B CYS B 132 LYS B 135 TYPE I' TURN 23 8B PHE B 140 THR B 143 TYPE I' TURN 24 9B ASP B 153 SER B 156 TYPE I TURN 25 10B ASP B 161 SER B 164 TYPE I TURN 26 11B THR B 190 SER B 193 TYPE II TURN 27 12B GLN B 283 TYR B 286 TYPE I TURN 28 13B PRO B 296 GLN B 299 TYPE II TURN 29 14B PHE B 319 PHE B 322 TYPE I' TURN 30 15B PRO B 351 LYS B 354 TYPE I SITE 1 DMA 8 CYS A 46 SER A 48 HIS A 67 PHE A 93 SITE 2 DMA 8 LEU A 141 CYS A 174 ZN A 401 NAD A 403 SITE 1 NAA 20 ARG A 47 HIS A 51 THR A 178 PHE A 198 SITE 2 NAA 20 GLY A 199 LEU A 200 GLY A 202 VAL A 203 SITE 3 NAA 20 VAL A 222 ASP A 223 ILE A 224 LYS A 228 SITE 4 NAA 20 ILE A 269 GLY A 270 ARG A 271 VAL A 292 SITE 5 NAA 20 GLY A 293 VAL A 294 PHE A 319 ARG A 369 SITE 1 DMB 8 CYS B 46 SER B 48 HIS B 67 PHE B 93 SITE 2 DMB 8 LEU B 141 CYS B 174 ZN B 401 NAD B 403 SITE 1 NAB 20 ARG B 47 HIS B 51 THR B 178 PHE B 198 SITE 2 NAB 20 GLY B 199 LEU B 200 GLY B 202 VAL B 203 SITE 3 NAB 20 VAL B 222 ASP B 223 ILE B 224 LYS B 228 SITE 4 NAB 20 ILE B 269 GLY B 270 ARG B 271 VAL B 292 SITE 5 NAB 20 GLY B 293 VAL B 294 PHE B 319 ARG B 369 CRYST1 51.760 44.540 94.610 104.80 102.30 70.60 P 1 2 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.019320 -0.006804 0.002908 0.00000 SCALE2 0.000000 0.023803 0.004869 0.00000 SCALE3 0.000000 0.000000 0.011042 0.00000 MTRIX1 1 0.129250 0.985840 -0.106810 0.39900 1 MTRIX2 1 0.986150 -0.139080 -0.090370 -0.21490 1 MTRIX3 1 -0.103940 -0.093660 -0.990160 0.44230 1