HEADER PLANT PROTEIN 17-AUG-07 2QZZ
TITLE STRUCTURE OF EUGENOL SYNTHASE FROM OCIMUM BASILICUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EUGENOL SYNTHASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: 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, PLANT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.V.LOUIE,J.P.NOEL,M.E.BOWMAN
REVDAT 2 24-FEB-09 2QZZ 1 VERSN
REVDAT 1 15-JAN-08 2QZZ 0
JRNL AUTH G.V.LOUIE,T.J.BAIGA,M.E.BOWMAN,T.KOEDUKA,
JRNL AUTH 2 J.H.TAYLOR,S.M.SPASSOVA,E.PICHERSKY,J.P.NOEL
JRNL TITL STRUCTURE AND REACTION MECHANISM OF BASIL EUGENOL
JRNL TITL 2 SYNTHASE
JRNL REF PLOS ONE V. 2 E993 2007
JRNL REFN ESSN 1932-6203
JRNL PMID 17912370
JRNL DOI 10.1371/JOURNAL.PONE.0000993
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.12
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) (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 85858
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) : 0.259
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4303
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 : 130
REMARK 3 SOLVENT ATOMS : 374
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.98900
REMARK 3 B22 (A**2) : -2.82900
REMARK 3 B33 (A**2) : 3.81800
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.83600
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) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.30
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) : 1.567 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.187 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.488 ; 2.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.568 ; 4.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 48.84
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 : NDP.PAR
REMARK 3 PARAMETER FILE 3 : EMF.PAR
REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 5 : 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 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2QZZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-SEP-07.
REMARK 100 THE RCSB ID CODE IS RCSB044257.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUN-06
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 : 104313
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 34.139
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.13300
REMARK 200 R SYM (I) : 0.13300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.68100
REMARK 200 R SYM FOR SHELL (I) : 0.68100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 2QW8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
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 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 42.69350
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 SER A -3
REMARK 465 GLY 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 SER B -3
REMARK 465 GLY 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 LYS A 44 36.52 -81.17
REMARK 500 ASP A 111 -87.07 -99.46
REMARK 500 ASN A 152 -151.88 62.86
REMARK 500 ILE A 267 -50.41 -120.54
REMARK 500 ASP A 305 70.05 -162.49
REMARK 500 LYS B 44 40.01 -77.85
REMARK 500 ASP B 111 -86.38 -101.79
REMARK 500 ASN B 152 -154.40 65.46
REMARK 500 ASP B 305 73.40 -157.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1385 DISTANCE = 5.19 ANGSTROMS
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 EMF A 601
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 401
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EMF B 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QW8 RELATED DB: PDB
REMARK 900 EUGENOL SYNTHASE, NADP+ MONOCLINIC FORM
REMARK 900 RELATED ID: 2QX7 RELATED DB: PDB
REMARK 900 EUGENOL SYNTHASE, NADP+ ORTHORHOMBIC FORM
REMARK 900 RELATED ID: 2QZ2 RELATED DB: PDB
REMARK 900 EUGENOL SYNTHASE, NADP+, EMDF TERNARY COMPLEX
REMARK 900 RELATED ID: 2R2G RELATED DB: PDB
REMARK 900 EUGENOL SYNTHASE, EMDF
REMARK 900 RELATED ID: 2QYS RELATED DB: PDB
REMARK 900 EUGENOL SYNTHASE, APO FORM
DBREF 2QZZ A 1 314 UNP Q15GI4 Q15GI4_OCIBA 1 314
DBREF 2QZZ B 1 314 UNP Q15GI4 Q15GI4_OCIBA 1 314
SEQADV 2QZZ SER A -3 UNP Q15GI4 EXPRESSION TAG
SEQADV 2QZZ GLY A -2 UNP Q15GI4 EXPRESSION TAG
SEQADV 2QZZ HIS A -1 UNP Q15GI4 EXPRESSION TAG
SEQADV 2QZZ GLY A 0 UNP Q15GI4 EXPRESSION TAG
SEQADV 2QZZ SER B -3 UNP Q15GI4 EXPRESSION TAG
SEQADV 2QZZ GLY B -2 UNP Q15GI4 EXPRESSION TAG
SEQADV 2QZZ HIS B -1 UNP Q15GI4 EXPRESSION TAG
SEQADV 2QZZ GLY B 0 UNP Q15GI4 EXPRESSION TAG
SEQRES 1 A 318 SER GLY 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 PHE PRO GLN
SEQRES 8 A 318 ILE 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 SER GLY 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 PHE PRO GLN
SEQRES 8 B 318 ILE 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 EMF A 601 17
HET NAP B 401 48
HET EMF B 602 17
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM EMF ETHYL (1S,2S)-2-(4-HYDROXY-3-METHOXYPHENYL)
HETNAM 2 EMF CYCLOPROPANECARBOXYLATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 3 NAP 2(C21 H28 N7 O17 P3)
FORMUL 4 EMF 2(C13 H16 O4)
FORMUL 7 HOH *374(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 LEU A 122 ALA A 142 1 21
HELIX 7 7 ALA A 155 ARG A 164 1 10
HELIX 8 8 TYR A 186 ASP A 200 1 15
HELIX 9 9 PRO A 201 LEU A 204 5 4
HELIX 10 10 PRO A 212 THR A 214 5 3
HELIX 11 11 GLN A 219 GLY A 231 1 13
HELIX 12 12 PRO A 240 LEU A 251 1 12
HELIX 13 13 GLU A 255 ILE A 267 1 13
HELIX 14 14 SER A 284 LEU A 286 5 3
HELIX 15 15 THR A 294 ASP A 305 1 12
HELIX 16 16 ILE B 19 LEU B 30 1 12
HELIX 17 17 LYS B 44 LEU B 54 1 11
HELIX 18 18 GLU B 65 LYS B 74 1 10
HELIX 19 19 ALA B 84 LEU B 89 5 6
HELIX 20 20 ASP B 90 GLY B 102 1 13
HELIX 21 21 LEU B 122 ALA B 142 1 21
HELIX 22 22 ALA B 155 ARG B 164 1 10
HELIX 23 23 TYR B 186 ASP B 200 1 15
HELIX 24 24 PRO B 201 LEU B 204 5 4
HELIX 25 25 PRO B 212 THR B 214 5 3
HELIX 26 26 GLN B 219 GLY B 231 1 13
HELIX 27 27 PRO B 240 LEU B 251 1 12
HELIX 28 28 GLU B 255 ILE B 267 1 13
HELIX 29 29 SER B 284 LEU B 286 5 3
HELIX 30 30 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 THR A 34 O ILE A 57
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 VAL A 78 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 TYR A 148
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 VAL A 174
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 VAL B 78 N LEU B 11
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 TYR B 148
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 VAL B 174
CISPEP 1 GLU A 253 PRO A 254 0 0.11
CISPEP 2 GLU B 253 PRO B 254 0 0.75
SITE 1 AC1 33 GLY A 14 THR A 16 GLY A 17 TYR A 18
SITE 2 AC1 33 ILE A 19 THR A 38 ARG A 39 SER A 42
SITE 3 AC1 33 LYS A 44 ALA A 82 LEU A 83 PHE A 85
SITE 4 AC1 33 GLN A 87 SER A 110 ASP A 111 PHE A 112
SITE 5 AC1 33 GLY A 113 LYS A 132 ASN A 152 PHE A 154
SITE 6 AC1 33 PHE A 158 EMF A 601 HOH A1002 HOH A1006
SITE 7 AC1 33 HOH A1015 HOH A1023 HOH A1041 HOH A1078
SITE 8 AC1 33 HOH A1086 HOH A1092 HOH A1126 HOH A1211
SITE 9 AC1 33 HOH A1217
SITE 1 AC2 14 PHE A 85 GLY A 113 VAL A 114 ASN A 152
SITE 2 AC2 14 TYR A 157 PHE A 158 PRO A 258 ILE A 261
SITE 3 AC2 14 LEU A 262 LEU A 265 ALA A 312 PHE A 314
SITE 4 AC2 14 NAP A 401 HOH A1464
SITE 1 AC3 33 THR B 16 GLY B 17 TYR B 18 ILE B 19
SITE 2 AC3 33 THR B 38 ARG B 39 SER B 42 LYS B 44
SITE 3 AC3 33 ALA B 82 LEU B 83 ALA B 84 PHE B 85
SITE 4 AC3 33 GLN B 87 SER B 110 ASP B 111 PHE B 112
SITE 5 AC3 33 GLY B 113 LYS B 132 ASN B 152 PHE B 154
SITE 6 AC3 33 PHE B 158 EMF B 602 HOH B1012 HOH B1018
SITE 7 AC3 33 HOH B1029 HOH B1032 HOH B1046 HOH B1061
SITE 8 AC3 33 HOH B1081 HOH B1094 HOH B1231 HOH B1487
SITE 9 AC3 33 HOH B1488
SITE 1 AC4 15 PHE B 85 GLY B 113 VAL B 114 ASN B 152
SITE 2 AC4 15 CYS B 153 TYR B 157 PHE B 158 PRO B 258
SITE 3 AC4 15 ILE B 261 LEU B 262 LEU B 265 ALA B 312
SITE 4 AC4 15 PHE B 314 NAP B 401 HOH B1477
CRYST1 54.033 85.387 76.876 90.00 107.51 90.00 P 1 21 1 4
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 0.018507 0.000000 0.005839 0.00000
SCALE2 0.000000 0.011711 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013640 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
