HEADER OXIDOREDUCTASE 20-JUN-03 1PS0
TITLE CRYSTAL STRUCTURE OF THE NADP(H)-DEPENDENT CINNAMYL ALCOHOL
TITLE 2 DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE PROTEIN
COMPND 3 IN PRE5-FET4 INTERGENIC REGION;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: CIANNAMYL ALCOHOL DEHYDROGENASE;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: YMR318C (ADH6);
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BJ2168;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PYES2-YMR318C
KEYWDS ADH TOPOLOGY, NADP(H)DEPENDENT, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.VALENCIA,C.LARROY,W.F.OCHOA,X.PARES,I.FITA,J.A.BIOSCA
REVDAT 4 14-FEB-24 1PS0 1 REMARK LINK
REVDAT 3 24-FEB-09 1PS0 1 VERSN
REVDAT 2 17-AUG-04 1PS0 1 JRNL
REVDAT 1 29-JUN-04 1PS0 0
JRNL AUTH E.VALENCIA,C.LARROY,W.F.OCHOA,X.PARES,I.FITA,J.A.BIOSCA
JRNL TITL APO AND HOLO STRUCTURES OF AN NADP(H)-DEPENDENT CINNAMYL
JRNL TITL 2 ALCOHOL DEHYDROGENASE FROM SACCHAROMYCES CEREVISIAE
JRNL REF J.MOL.BIOL. V. 341 1049 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15289102
JRNL DOI 10.1016/J.JMB.2004.06.037
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.VALENCIA,A.ROSELL,C.LARROY,J.FARRES,J.A.BIOSCA,I.FITA,
REMARK 1 AUTH 2 X.PARES,W.F.OCHOA
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF
REMARK 1 TITL 2 NADP(H)-DEPENDENT ALCOHOL DEHYDROGENASES FROM SACCHAROMYCES
REMARK 1 TITL 3 CEREVISIAE AND RANA PEREZI
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 59 334 2003
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S090744490201661X
REMARK 2
REMARK 2 RESOLUTION. 3.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 5.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 12308
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.264
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1327
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2780
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -12.84200
REMARK 3 B22 (A**2) : -12.84200
REMARK 3 B33 (A**2) : 25.68400
REMARK 3 B12 (A**2) : -14.65800
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : NADP_XPLOR.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PS0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019534.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18395
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : 0.08600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 78.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, PH 8.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 99.81133
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 49.90567
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 49.90567
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 99.81133
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER GENERATED BY THE
REMARK 300 CRYSTALLOGRAPHIC TWO FOLD AXIS: X, Y, -Z.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 149.71700
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 5 -87.60 -87.97
REMARK 500 ASP A 33 -28.99 -36.65
REMARK 500 ASP A 35 175.27 -52.57
REMARK 500 ALA A 42 106.49 177.94
REMARK 500 TRP A 57 50.90 -111.43
REMARK 500 PRO A 63 -179.08 -57.17
REMARK 500 LEU A 64 102.36 -172.18
REMARK 500 HIS A 68 41.37 -141.23
REMARK 500 LYS A 76 98.02 167.45
REMARK 500 PRO A 79 -77.19 -35.09
REMARK 500 ASN A 82 129.60 158.07
REMARK 500 SER A 83 -13.10 169.74
REMARK 500 GLU A 102 -31.49 -162.73
REMARK 500 ASN A 110 41.62 -140.29
REMARK 500 SER A 131 148.20 -39.24
REMARK 500 GLN A 132 -145.65 -138.58
REMARK 500 TYR A 135 55.01 -91.71
REMARK 500 GLU A 143 -22.07 -28.97
REMARK 500 ASN A 152 16.11 -64.06
REMARK 500 CYS A 163 -68.44 -134.40
REMARK 500 PRO A 179 133.01 -39.96
REMARK 500 LEU A 188 58.47 -61.65
REMARK 500 GLU A 205 99.09 -57.59
REMARK 500 ARG A 211 -70.23 -80.58
REMARK 500 HIS A 226 150.10 176.59
REMARK 500 ASP A 235 83.10 175.60
REMARK 500 ASP A 256 32.77 -75.71
REMARK 500 PHE A 259 31.89 -99.75
REMARK 500 ILE A 277 84.11 -151.17
REMARK 500 PRO A 278 -162.07 -78.62
REMARK 500 GLN A 280 36.80 -61.30
REMARK 500 LEU A 291 47.74 -86.42
REMARK 500 LEU A 301 -133.06 22.66
REMARK 500 GLU A 316 -79.53 -56.23
REMARK 500 ASP A 318 94.57 40.07
REMARK 500 GLU A 330 -37.04 -17.01
REMARK 500 ALA A 331 -82.67 -77.10
REMARK 500 GLU A 338 -62.65 -103.81
REMARK 500 ARG A 346 37.72 -78.96
REMARK 500 TYR A 347 -56.40 96.02
REMARK 500 ASP A 355 -83.07 -48.81
REMARK 500 LYS A 356 50.45 -69.43
REMARK 500 GLU A 357 -41.38 -140.30
REMARK 500 SER A 359 150.26 64.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 46 SG
REMARK 620 2 HIS A 68 NE2 104.8
REMARK 620 3 CYS A 163 SG 98.1 99.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 100 SG
REMARK 620 2 CYS A 103 SG 119.2
REMARK 620 3 CYS A 106 SG 122.4 88.8
REMARK 620 4 CYS A 114 SG 101.4 124.7 100.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 4292
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PIW RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN A HETERODIMERIC FORM
DBREF 1PS0 A 1 360 UNP Q04894 ADH6_YEAST 1 360
SEQRES 1 A 360 MET SER TYR PRO GLU LYS PHE GLU GLY ILE ALA ILE GLN
SEQRES 2 A 360 SER HIS GLU ASP TRP LYS ASN PRO LYS LYS THR LYS TYR
SEQRES 3 A 360 ASP PRO LYS PRO PHE TYR ASP HIS ASP ILE ASP ILE LYS
SEQRES 4 A 360 ILE GLU ALA CYS GLY VAL CYS GLY SER ASP ILE HIS CYS
SEQRES 5 A 360 ALA ALA GLY HIS TRP GLY ASN MET LYS MET PRO LEU VAL
SEQRES 6 A 360 VAL GLY HIS GLU ILE VAL GLY LYS VAL VAL LYS LEU GLY
SEQRES 7 A 360 PRO LYS SER ASN SER GLY LEU LYS VAL GLY GLN ARG VAL
SEQRES 8 A 360 GLY VAL GLY ALA GLN VAL PHE SER CYS LEU GLU CYS ASP
SEQRES 9 A 360 ARG CYS LYS ASN ASP ASN GLU PRO TYR CYS THR LYS PHE
SEQRES 10 A 360 VAL THR THR TYR SER GLN PRO TYR GLU ASP GLY TYR VAL
SEQRES 11 A 360 SER GLN GLY GLY TYR ALA ASN TYR VAL ARG VAL HIS GLU
SEQRES 12 A 360 HIS PHE VAL VAL PRO ILE PRO GLU ASN ILE PRO SER HIS
SEQRES 13 A 360 LEU ALA ALA PRO LEU LEU CYS GLY GLY LEU THR VAL TYR
SEQRES 14 A 360 SER PRO LEU VAL ARG ASN GLY CYS GLY PRO GLY LYS LYS
SEQRES 15 A 360 VAL GLY ILE VAL GLY LEU GLY GLY ILE GLY SER MET GLY
SEQRES 16 A 360 THR LEU ILE SER LYS ALA MET GLY ALA GLU THR TYR VAL
SEQRES 17 A 360 ILE SER ARG SER SER ARG LYS ARG GLU ASP ALA MET LYS
SEQRES 18 A 360 MET GLY ALA ASP HIS TYR ILE ALA THR LEU GLU GLU GLY
SEQRES 19 A 360 ASP TRP GLY GLU LYS TYR PHE ASP THR PHE ASP LEU ILE
SEQRES 20 A 360 VAL VAL CYS ALA SER SER LEU THR ASP ILE ASP PHE ASN
SEQRES 21 A 360 ILE MET PRO LYS ALA MET LYS VAL GLY GLY ARG ILE VAL
SEQRES 22 A 360 SER ILE SER ILE PRO GLU GLN HIS GLU MET LEU SER LEU
SEQRES 23 A 360 LYS PRO TYR GLY LEU LYS ALA VAL SER ILE SER TYR SER
SEQRES 24 A 360 ALA LEU GLY SER ILE LYS GLU LEU ASN GLN LEU LEU LYS
SEQRES 25 A 360 LEU VAL SER GLU LYS ASP ILE LYS ILE TRP VAL GLU THR
SEQRES 26 A 360 LEU PRO VAL GLY GLU ALA GLY VAL HIS GLU ALA PHE GLU
SEQRES 27 A 360 ARG MET GLU LYS GLY ASP VAL ARG TYR ARG PHE THR LEU
SEQRES 28 A 360 VAL GLY TYR ASP LYS GLU PHE SER ASP
HET ZN A1501 1
HET ZN A1502 1
HET NAP A4292 48
HETNAM ZN ZINC ION
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 NAP C21 H28 N7 O17 P3
HELIX 1 1 CYS A 46 GLY A 55 1 10
HELIX 2 2 CYS A 103 ASN A 108 1 6
HELIX 3 3 ASN A 110 CYS A 114 5 5
HELIX 4 4 PRO A 154 ALA A 159 1 6
HELIX 5 5 PRO A 160 LEU A 162 5 3
HELIX 6 6 CYS A 163 ASN A 175 1 13
HELIX 7 7 GLY A 189 MET A 202 1 14
HELIX 8 8 LYS A 215 MET A 222 1 8
HELIX 9 9 LEU A 231 GLU A 233 5 3
HELIX 10 10 ASP A 235 TYR A 240 1 6
HELIX 11 11 ILE A 261 LYS A 264 5 4
HELIX 12 12 LYS A 287 LEU A 291 5 5
HELIX 13 13 LYS A 305 ASP A 318 1 14
HELIX 14 14 GLY A 329 MET A 340 1 12
HELIX 15 15 GLU A 341 GLY A 343 5 3
HELIX 16 16 TYR A 354 PHE A 358 5 5
SHEET 1 A 2 PHE A 7 ALA A 11 0
SHEET 2 A 2 LYS A 22 TYR A 26 -1 O TYR A 26 N PHE A 7
SHEET 1 B 5 TYR A 138 ARG A 140 0
SHEET 2 B 5 ILE A 36 VAL A 45 -1 N ILE A 38 O VAL A 139
SHEET 3 B 5 ILE A 70 LEU A 77 -1 O LYS A 73 N LYS A 39
SHEET 4 B 5 ARG A 90 VAL A 93 -1 O VAL A 91 N GLY A 72
SHEET 5 B 5 VAL A 147 PRO A 148 -1 O VAL A 147 N GLY A 92
SHEET 1 C 4 TYR A 138 ARG A 140 0
SHEET 2 C 4 ILE A 36 VAL A 45 -1 N ILE A 38 O VAL A 139
SHEET 3 C 4 ARG A 348 VAL A 352 -1 O PHE A 349 N VAL A 45
SHEET 4 C 4 VAL A 323 PRO A 327 1 N GLU A 324 O ARG A 348
SHEET 1 D 2 GLN A 96 PHE A 98 0
SHEET 2 D 2 VAL A 118 THR A 119 -1 O VAL A 118 N PHE A 98
SHEET 1 E 6 TYR A 227 ALA A 229 0
SHEET 2 E 6 GLU A 205 SER A 210 1 N SER A 210 O ILE A 228
SHEET 3 E 6 LYS A 182 VAL A 186 1 N ILE A 185 O ILE A 209
SHEET 4 E 6 PHE A 244 VAL A 249 1 O VAL A 248 N VAL A 186
SHEET 5 E 6 MET A 266 SER A 274 1 O LYS A 267 N PHE A 244
SHEET 6 E 6 VAL A 294 TYR A 298 1 O SER A 295 N ILE A 272
LINK SG CYS A 46 ZN ZN A1502 1555 1555 2.60
LINK NE2 HIS A 68 ZN ZN A1502 1555 1555 2.07
LINK SG CYS A 100 ZN ZN A1501 1555 1555 2.43
LINK SG CYS A 103 ZN ZN A1501 1555 1555 2.30
LINK SG CYS A 106 ZN ZN A1501 1555 1555 2.33
LINK SG CYS A 114 ZN ZN A1501 1555 1555 2.40
LINK SG CYS A 163 ZN ZN A1502 1555 1555 2.53
CISPEP 1 MET A 62 PRO A 63 0 -0.09
SITE 1 AC1 4 CYS A 100 CYS A 103 CYS A 106 CYS A 114
SITE 1 AC2 4 CYS A 46 HIS A 68 CYS A 163 NAP A4292
SITE 1 AC3 29 GLY A 47 SER A 48 HIS A 51 TRP A 57
SITE 2 AC3 29 CYS A 163 THR A 167 GLY A 187 LEU A 188
SITE 3 AC3 29 GLY A 189 GLY A 190 ILE A 191 SER A 210
SITE 4 AC3 29 ARG A 211 LYS A 215 CYS A 250 ALA A 251
SITE 5 AC3 29 SER A 252 SER A 253 THR A 255 ASP A 256
SITE 6 AC3 29 ILE A 257 ILE A 275 ILE A 277 TYR A 298
SITE 7 AC3 29 SER A 299 ALA A 300 LEU A 301 ARG A 348
SITE 8 AC3 29 ZN A1502
CRYST1 102.132 102.132 149.717 90.00 90.00 120.00 P 32 2 1 6
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 0.009791 0.005653 0.000000 0.00000
SCALE2 0.000000 0.011306 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006679 0.00000
(ATOM LINES ARE NOT SHOWN.)
END