HEADER OXIDOREDUCTASE 29-JAN-08 3C3X
TITLE THE MULTIPLE PHENYLPROPENE SYNTHASES IN BOTH CLARKIA
TITLE 2 BREWERI AND PETUNIA HYBRIDA REPRESENT TWO DISTINCT LINEAGES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUGENOL SYNTHASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.-.-.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OCIMUM BASILICUM;
SOURCE 3 ORGANISM_COMMON: SWEET BASIL;
SOURCE 4 ORGANISM_TAXID: 39350;
SOURCE 5 GENE: EGS1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHIS8
KEYWDS EUGENOL, PHENYLPROPENE, PIP REDUCTASE, SHORT-CHAIN
KEYWDS 2 DEHYDROGENASE/REDUCTASE, NADP, OXIDOREDUCTASE,
KEYWDS 3 PHENYLPROPANOID METABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR G.V.LOUIE,J.P.NOEL,M.E.BOWMAN
REVDAT 2 24-FEB-09 3C3X 1 VERSN
REVDAT 1 06-MAY-08 3C3X 0
JRNL AUTH T.KOEDUKA,G.V.LOUIE,I.ORLOVA,C.M.KISH,M.IBDAH,
JRNL AUTH 2 C.G.WILKERSON,M.E.BOWMAN,T.J.BAIGA,J.P.NOEL,
JRNL AUTH 3 N.DUDAREVA,E.PICHERSKY
JRNL TITL THE MULTIPLE PHENYLPROPENE SYNTHASES IN BOTH
JRNL TITL 2 CLARKIA BREWERI AND PETUNIA HYBRIDA REPRESENT TWO
JRNL TITL 3 DISTINCT PROTEIN LINEAGES.
JRNL REF PLANT J. V. 54 362 2008
JRNL REFN ISSN 0960-7412
JRNL PMID 18208524
JRNL DOI 10.1111/J.1365-313X.2008.03412.X
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.3
REMARK 3 NUMBER OF REFLECTIONS : 33097
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) : 0.255
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1664
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 : 4954
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 158
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.99000
REMARK 3 B22 (A**2) : 5.56400
REMARK 3 B33 (A**2) : -11.55300
REMARK 3 B12 (A**2) : 0.00000
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) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.28
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.898 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.888 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.022 ; 2.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.359 ; 4.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 48.72
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NDP.PAR
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.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 3C3X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-08.
REMARK 100 THE RCSB ID CODE IS RCSB046309.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45628
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.518
REMARK 200 RESOLUTION RANGE LOW (A) : 57.947
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.9
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.18000
REMARK 200 R SYM (I) : 0.18000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.8
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.01500
REMARK 200 R SYM FOR SHELL (I) : 0.01500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 2QX7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM SUCCINATE, 21% PEG
REMARK 280 3350, 0.3 M KCL, 2 MM DITHIOTHREITOL, 5 MM NADP+, PH 5.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 -1.000000 0.000000 0.000000 39.58400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.54100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.52300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.54100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.58400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.52300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: BIOLOGICAL UNIT IS A MONOMER (HALF OF THE ASYMMETRIC
REMARK 300 UNIT)
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 GLU A 3
REMARK 465 ASN A 4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 GLU B 3
REMARK 465 ASN B 4
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 ASN A 41 32.18 -75.71
REMARK 500 LYS A 44 40.15 -97.38
REMARK 500 ASP A 111 -88.90 -112.48
REMARK 500 ARG A 118 8.83 -151.23
REMARK 500 ASN A 152 -152.73 63.81
REMARK 500 PRO A 168 33.12 -66.19
REMARK 500 PRO A 252 -166.62 -72.75
REMARK 500 MET A 272 -3.53 -143.15
REMARK 500 ASP A 305 77.92 -168.31
REMARK 500 ASN B 41 32.77 -78.96
REMARK 500 LYS B 44 46.78 -98.35
REMARK 500 ASP B 111 -84.99 -116.86
REMARK 500 ARG B 118 5.08 -161.40
REMARK 500 ASN B 152 -155.27 65.23
REMARK 500 ARG B 164 57.32 38.90
REMARK 500 PRO B 168 40.29 -70.30
REMARK 500 PRO B 252 -168.68 -71.22
REMARK 500 ASP B 305 78.88 -168.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 401
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3C1O RELATED DB: PDB
REMARK 900 EUGENOL SYNTHASE 1 FROM CLARKIA BREWERI
REMARK 900 RELATED ID: 2QX7 RELATED DB: PDB
REMARK 900 EUGENOL SYNTHASE FROM OCIMUM BASILICUM
DBREF 3C3X A 1 314 UNP Q15GI4 EGS1_OCIBA 1 314
DBREF 3C3X B 1 314 UNP Q15GI4 EGS1_OCIBA 1 314
SEQADV 3C3X GLY A -3 UNP Q15GI4 EXPRESSION TAG
SEQADV 3C3X SER A -2 UNP Q15GI4 EXPRESSION TAG
SEQADV 3C3X HIS A -1 UNP Q15GI4 EXPRESSION TAG
SEQADV 3C3X GLY A 0 UNP Q15GI4 EXPRESSION TAG
SEQADV 3C3X VAL A 85 UNP Q15GI4 PHE 85 ENGINEERED
SEQADV 3C3X TYR A 88 UNP Q15GI4 ILE 88 ENGINEERED
SEQADV 3C3X GLY B -3 UNP Q15GI4 EXPRESSION TAG
SEQADV 3C3X SER B -2 UNP Q15GI4 EXPRESSION TAG
SEQADV 3C3X HIS B -1 UNP Q15GI4 EXPRESSION TAG
SEQADV 3C3X GLY B 0 UNP Q15GI4 EXPRESSION TAG
SEQADV 3C3X VAL B 85 UNP Q15GI4 PHE 85 ENGINEERED
SEQADV 3C3X TYR B 88 UNP Q15GI4 ILE 88 ENGINEERED
SEQRES 1 A 318 GLY SER HIS GLY MET GLU GLU ASN GLY MET LYS SER LYS
SEQRES 2 A 318 ILE LEU ILE PHE GLY GLY THR GLY TYR ILE GLY ASN HIS
SEQRES 3 A 318 MET VAL LYS GLY SER LEU LYS LEU GLY HIS PRO THR TYR
SEQRES 4 A 318 VAL PHE THR ARG PRO ASN SER SER LYS THR THR LEU LEU
SEQRES 5 A 318 ASP GLU PHE GLN SER LEU GLY ALA ILE ILE VAL LYS GLY
SEQRES 6 A 318 GLU LEU ASP GLU HIS GLU LYS LEU VAL GLU LEU MET LYS
SEQRES 7 A 318 LYS VAL ASP VAL VAL ILE SER ALA LEU ALA VAL PRO GLN
SEQRES 8 A 318 TYR LEU ASP GLN PHE LYS ILE LEU GLU ALA ILE LYS VAL
SEQRES 9 A 318 ALA GLY ASN ILE LYS ARG PHE LEU PRO SER ASP PHE GLY
SEQRES 10 A 318 VAL GLU GLU ASP ARG ILE ASN ALA LEU PRO PRO PHE GLU
SEQRES 11 A 318 ALA LEU ILE GLU ARG LYS ARG MET ILE ARG ARG ALA ILE
SEQRES 12 A 318 GLU GLU ALA ASN ILE PRO TYR THR TYR VAL SER ALA ASN
SEQRES 13 A 318 CYS PHE ALA SER TYR PHE ILE ASN TYR LEU LEU ARG PRO
SEQRES 14 A 318 TYR ASP PRO LYS ASP GLU ILE THR VAL TYR GLY THR GLY
SEQRES 15 A 318 GLU ALA LYS PHE ALA MET ASN TYR GLU GLN ASP ILE GLY
SEQRES 16 A 318 LEU TYR THR ILE LYS VAL ALA THR ASP PRO ARG ALA LEU
SEQRES 17 A 318 ASN ARG VAL VAL ILE TYR ARG PRO SER THR ASN ILE ILE
SEQRES 18 A 318 THR GLN LEU GLU LEU ILE SER ARG TRP GLU LYS LYS ILE
SEQRES 19 A 318 GLY LYS LYS PHE LYS LYS ILE HIS VAL PRO GLU GLU GLU
SEQRES 20 A 318 ILE VAL ALA LEU THR LYS GLU LEU PRO GLU PRO GLU ASN
SEQRES 21 A 318 ILE PRO ILE ALA ILE LEU HIS CYS LEU PHE ILE ASP GLY
SEQRES 22 A 318 ALA THR MET SER TYR ASP PHE LYS GLU ASN ASP VAL GLU
SEQRES 23 A 318 ALA SER THR LEU TYR PRO GLU LEU LYS PHE THR THR ILE
SEQRES 24 A 318 ASP GLU LEU LEU ASP ILE PHE VAL HIS ASP PRO PRO PRO
SEQRES 25 A 318 PRO ALA SER ALA ALA PHE
SEQRES 1 B 318 GLY SER HIS GLY MET GLU GLU ASN GLY MET LYS SER LYS
SEQRES 2 B 318 ILE LEU ILE PHE GLY GLY THR GLY TYR ILE GLY ASN HIS
SEQRES 3 B 318 MET VAL LYS GLY SER LEU LYS LEU GLY HIS PRO THR TYR
SEQRES 4 B 318 VAL PHE THR ARG PRO ASN SER SER LYS THR THR LEU LEU
SEQRES 5 B 318 ASP GLU PHE GLN SER LEU GLY ALA ILE ILE VAL LYS GLY
SEQRES 6 B 318 GLU LEU ASP GLU HIS GLU LYS LEU VAL GLU LEU MET LYS
SEQRES 7 B 318 LYS VAL ASP VAL VAL ILE SER ALA LEU ALA VAL PRO GLN
SEQRES 8 B 318 TYR LEU ASP GLN PHE LYS ILE LEU GLU ALA ILE LYS VAL
SEQRES 9 B 318 ALA GLY ASN ILE LYS ARG PHE LEU PRO SER ASP PHE GLY
SEQRES 10 B 318 VAL GLU GLU ASP ARG ILE ASN ALA LEU PRO PRO PHE GLU
SEQRES 11 B 318 ALA LEU ILE GLU ARG LYS ARG MET ILE ARG ARG ALA ILE
SEQRES 12 B 318 GLU GLU ALA ASN ILE PRO TYR THR TYR VAL SER ALA ASN
SEQRES 13 B 318 CYS PHE ALA SER TYR PHE ILE ASN TYR LEU LEU ARG PRO
SEQRES 14 B 318 TYR ASP PRO LYS ASP GLU ILE THR VAL TYR GLY THR GLY
SEQRES 15 B 318 GLU ALA LYS PHE ALA MET ASN TYR GLU GLN ASP ILE GLY
SEQRES 16 B 318 LEU TYR THR ILE LYS VAL ALA THR ASP PRO ARG ALA LEU
SEQRES 17 B 318 ASN ARG VAL VAL ILE TYR ARG PRO SER THR ASN ILE ILE
SEQRES 18 B 318 THR GLN LEU GLU LEU ILE SER ARG TRP GLU LYS LYS ILE
SEQRES 19 B 318 GLY LYS LYS PHE LYS LYS ILE HIS VAL PRO GLU GLU GLU
SEQRES 20 B 318 ILE VAL ALA LEU THR LYS GLU LEU PRO GLU PRO GLU ASN
SEQRES 21 B 318 ILE PRO ILE ALA ILE LEU HIS CYS LEU PHE ILE ASP GLY
SEQRES 22 B 318 ALA THR MET SER TYR ASP PHE LYS GLU ASN ASP VAL GLU
SEQRES 23 B 318 ALA SER THR LEU TYR PRO GLU LEU LYS PHE THR THR ILE
SEQRES 24 B 318 ASP GLU LEU LEU ASP ILE PHE VAL HIS ASP PRO PRO PRO
SEQRES 25 B 318 PRO ALA SER ALA ALA PHE
HET NAP A 401 48
HET NAP B 401 48
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 3 NAP 2(C21 H28 N7 O17 P3)
FORMUL 5 HOH *158(H2 O)
HELIX 1 1 ILE A 19 LEU A 30 1 12
HELIX 2 2 LYS A 44 LEU A 54 1 11
HELIX 3 3 GLU A 65 LYS A 74 1 10
HELIX 4 4 ALA A 84 LEU A 89 5 6
HELIX 5 5 ASP A 90 GLY A 102 1 13
HELIX 6 6 GLU A 115 ILE A 119 5 5
HELIX 7 7 LEU A 122 ALA A 142 1 21
HELIX 8 8 ALA A 155 ARG A 164 1 10
HELIX 9 9 TYR A 186 ALA A 198 1 13
HELIX 10 10 THR A 199 LEU A 204 5 6
HELIX 11 11 PRO A 212 THR A 214 5 3
HELIX 12 12 GLN A 219 GLY A 231 1 13
HELIX 13 13 PRO A 240 LEU A 251 1 12
HELIX 14 14 GLU A 255 ILE A 267 1 13
HELIX 15 15 SER A 284 LEU A 286 5 3
HELIX 16 16 THR A 294 ASP A 305 1 12
HELIX 17 17 ILE B 19 LEU B 30 1 12
HELIX 18 18 LYS B 44 LEU B 54 1 11
HELIX 19 19 GLU B 65 LYS B 74 1 10
HELIX 20 20 ALA B 84 LEU B 89 5 6
HELIX 21 21 ASP B 90 GLY B 102 1 13
HELIX 22 22 LEU B 122 ALA B 142 1 21
HELIX 23 23 ALA B 155 ARG B 164 1 10
HELIX 24 24 TYR B 186 ASP B 200 1 15
HELIX 25 25 PRO B 201 LEU B 204 5 4
HELIX 26 26 PRO B 212 THR B 214 5 3
HELIX 27 27 GLN B 219 GLY B 231 1 13
HELIX 28 28 PRO B 240 LEU B 251 1 12
HELIX 29 29 GLU B 255 ILE B 267 1 13
HELIX 30 30 SER B 284 LEU B 286 5 3
HELIX 31 31 THR B 294 ASP B 305 1 12
SHEET 1 A 5 ILE A 57 LYS A 60 0
SHEET 2 A 5 THR A 34 THR A 38 1 N VAL A 36 O VAL A 59
SHEET 3 A 5 ILE A 10 PHE A 13 1 N ILE A 10 O TYR A 35
SHEET 4 A 5 VAL A 78 SER A 81 1 O ILE A 80 N LEU A 11
SHEET 5 A 5 ARG A 106 LEU A 108 1 O LEU A 108 N SER A 81
SHEET 1 B 3 THR A 147 SER A 150 0
SHEET 2 B 3 ARG A 206 ILE A 209 1 O VAL A 208 N SER A 150
SHEET 3 B 3 VAL A 281 GLU A 282 1 O VAL A 281 N ILE A 209
SHEET 1 C 3 CYS A 153 PHE A 154 0
SHEET 2 C 3 LYS A 181 ASN A 185 1 O ASN A 185 N CYS A 153
SHEET 3 C 3 ILE A 216 THR A 218 -1 O ILE A 217 N PHE A 182
SHEET 1 D 2 GLU A 171 TYR A 175 0
SHEET 2 D 2 LYS A 235 VAL A 239 1 O ILE A 237 N ILE A 172
SHEET 1 E 5 ILE B 57 LYS B 60 0
SHEET 2 E 5 THR B 34 THR B 38 1 N THR B 34 O ILE B 57
SHEET 3 E 5 ILE B 10 PHE B 13 1 N ILE B 10 O TYR B 35
SHEET 4 E 5 VAL B 78 SER B 81 1 O ILE B 80 N PHE B 13
SHEET 5 E 5 ARG B 106 LEU B 108 1 O LEU B 108 N SER B 81
SHEET 1 F 3 THR B 147 SER B 150 0
SHEET 2 F 3 ARG B 206 ILE B 209 1 O VAL B 208 N SER B 150
SHEET 3 F 3 VAL B 281 GLU B 282 1 O VAL B 281 N ILE B 209
SHEET 1 G 3 CYS B 153 PHE B 154 0
SHEET 2 G 3 LYS B 181 ASN B 185 1 O ASN B 185 N CYS B 153
SHEET 3 G 3 ILE B 216 THR B 218 -1 O ILE B 217 N PHE B 182
SHEET 1 H 2 GLU B 171 TYR B 175 0
SHEET 2 H 2 LYS B 235 VAL B 239 1 O ILE B 237 N ILE B 172
CISPEP 1 GLU A 253 PRO A 254 0 0.17
CISPEP 2 GLU B 253 PRO B 254 0 0.11
SITE 1 AC1 20 GLY A 14 THR A 16 GLY A 17 TYR A 18
SITE 2 AC1 20 ILE A 19 THR A 38 ARG A 39 LYS A 44
SITE 3 AC1 20 ALA A 82 LEU A 83 GLN A 87 TYR A 88
SITE 4 AC1 20 SER A 110 ASP A 111 PHE A 112 GLY A 113
SITE 5 AC1 20 ASN A 152 CYS A 153 PHE A 154 PHE A 158
SITE 1 AC2 20 GLY B 14 THR B 16 GLY B 17 TYR B 18
SITE 2 AC2 20 ILE B 19 THR B 38 ARG B 39 ALA B 82
SITE 3 AC2 20 LEU B 83 ALA B 84 GLN B 87 TYR B 88
SITE 4 AC2 20 SER B 110 ASP B 111 PHE B 112 GLY B 113
SITE 5 AC2 20 ASN B 152 CYS B 153 PHE B 154 PHE B 158
CRYST1 79.168 85.046 99.082 90.00 90.00 90.00 P 21 21 21 8
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 0.012631 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011758 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010093 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
