HEADER OXIDOREDUCTASE 06-FEB-14 4OPT
TITLE CONSTRUCTING TAILORED ISOPRENOID PRODUCTS BY STRUCTURE-GUIDED
TITLE 2 MODIFICATION OF GERANYLGERANYL REDUCTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED ARCHAEAL PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GERANYLGERANYL REDUCTASE;
COMPND 5 EC: 1.3.1.83;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS ACIDOCALDARIUS;
SOURCE 3 ORGANISM_TAXID: 330779;
SOURCE 4 STRAIN: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
SOURCE 5 GENE: SACI_0986;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ROSSMANN FOLD, OXIDOREDUCTASE, ARCHAEAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.P.MCANDREW,Y.KUNG,X.XIE,C.LIU,J.H.PEREIRA,J.D.KEASLING,P.D.ADAMS
REVDAT 2 23-JUL-14 4OPT 1 JRNL
REVDAT 1 09-JUL-14 4OPT 0
JRNL AUTH Y.KUNG,R.P.MCANDREW,X.XIE,C.C.LIU,J.H.PEREIRA,P.D.ADAMS,
JRNL AUTH 2 J.D.KEASLING
JRNL TITL CONSTRUCTING TAILORED ISOPRENOID PRODUCTS BY
JRNL TITL 2 STRUCTURE-GUIDED MODIFICATION OF GERANYLGERANYL REDUCTASE.
JRNL REF STRUCTURE V. 22 1028 2014
JRNL REFN ISSN 0969-2126
JRNL PMID 24954619
JRNL DOI 10.1016/J.STR.2014.05.007
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1525)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.7
REMARK 3 NUMBER OF REFLECTIONS : 14560
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 729
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 45.4984 - 4.4396 1.00 3543 187 0.1621 0.1871
REMARK 3 2 4.4396 - 3.5242 1.00 3371 178 0.1849 0.1970
REMARK 3 3 3.5242 - 3.0789 0.93 3124 164 0.2256 0.2947
REMARK 3 4 3.0789 - 2.7974 0.71 2362 125 0.2519 0.2671
REMARK 3 5 2.7974 - 2.6000 0.43 1431 75 0.2637 0.3133
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.230
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 3746
REMARK 3 ANGLE : 0.575 5064
REMARK 3 CHIRALITY : 0.023 530
REMARK 3 PLANARITY : 0.002 647
REMARK 3 DIHEDRAL : 12.493 1425
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resid 1 through 224 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.2615 24.9481 -8.3373
REMARK 3 T TENSOR
REMARK 3 T11: 0.2778 T22: 0.2988
REMARK 3 T33: 0.4103 T12: -0.0252
REMARK 3 T13: -0.0176 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 3.1444 L22: 1.7171
REMARK 3 L33: 4.4078 L12: 0.3965
REMARK 3 L13: -1.1720 L23: -0.5720
REMARK 3 S TENSOR
REMARK 3 S11: 0.1729 S12: -0.1800 S13: 0.5576
REMARK 3 S21: -0.0952 S22: 0.0784 S23: 0.2068
REMARK 3 S31: -0.4406 S32: 0.1165 S33: -0.2053
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resid 225 through 356 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.4476 16.1305 -12.8021
REMARK 3 T TENSOR
REMARK 3 T11: 0.2719 T22: 0.2598
REMARK 3 T33: 0.1952 T12: -0.0035
REMARK 3 T13: -0.0447 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 2.9251 L22: 1.0841
REMARK 3 L33: 2.9082 L12: -0.0476
REMARK 3 L13: -0.5347 L23: -0.0103
REMARK 3 S TENSOR
REMARK 3 S11: -0.1558 S12: 0.1171 S13: 0.0474
REMARK 3 S21: -0.1425 S22: 0.0548 S23: -0.0723
REMARK 3 S31: 0.0927 S32: 0.1441 S33: 0.0695
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resid 357 through 452 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.7588 2.0863 -24.6668
REMARK 3 T TENSOR
REMARK 3 T11: 0.5044 T22: 0.3311
REMARK 3 T33: 0.4664 T12: 0.0869
REMARK 3 T13: 0.0300 T23: -0.1538
REMARK 3 L TENSOR
REMARK 3 L11: 2.4636 L22: 0.3863
REMARK 3 L33: 7.5894 L12: 0.6901
REMARK 3 L13: -1.7896 L23: -0.8321
REMARK 3 S TENSOR
REMARK 3 S11: 0.0281 S12: 0.6102 S13: -0.4518
REMARK 3 S21: -0.1094 S22: -0.0322 S23: 0.3329
REMARK 3 S31: 0.1958 S32: -0.4563 S33: 0.0266
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4OPT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-FEB-14.
REMARK 100 THE RCSB ID CODE IS RCSB084798.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL, CYLINDRICALLY
REMARK 200 BENT, SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17900
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
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) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
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: PHENIX (PHENIX.PHASER: DEV_1525)
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 7.5, 10% PEG 3350 AND
REMARK 280 0.2 M L-PROLINE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 31.82600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.18150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.09900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.18150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.82600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.09900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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 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 HIS A 0
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 ARG A 161 52.85 33.47
REMARK 500 ASP A 207 114.76 -165.85
REMARK 500 SER A 211 68.82 -159.28
REMARK 500 LYS A 260 50.43 -118.54
REMARK 500 LEU A 262 -61.61 -97.87
REMARK 500 ASN A 281 105.69 -56.85
REMARK 500 TYR A 340 -25.50 -158.49
REMARK 500 ALA A 379 -74.04 -70.90
REMARK 500 SER A 380 30.90 -80.06
REMARK 500 ASN A 425 42.93 -101.39
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 FDA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GRG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OPC RELATED DB: PDB
REMARK 900 SAGGR BOUND TO PG
REMARK 900 RELATED ID: 4OPD RELATED DB: PDB
REMARK 900 SAGGR BOUND TO GGPP
REMARK 900 RELATED ID: 4OPG RELATED DB: PDB
REMARK 900 SAGGR L377H
REMARK 900 RELATED ID: 4OPI RELATED DB: PDB
REMARK 900 SAGGR F219L
REMARK 900 RELATED ID: 4OPL RELATED DB: PDB
REMARK 900 SAGGR I206F
REMARK 900 RELATED ID: 4OPU RELATED DB: PDB
DBREF 4OPT A 1 452 UNP Q4JA33 Q4JA33_SULAC 1 452
SEQADV 4OPT HIS A 0 UNP Q4JA33 EXPRESSION TAG
SEQADV 4OPT PHE A 206 UNP Q4JA33 ILE 206 ENGINEERED MUTATION
SEQADV 4OPT HIS A 377 UNP Q4JA33 LEU 377 ENGINEERED MUTATION
SEQRES 1 A 453 HIS MET LYS GLU LEU LYS TYR ASP VAL LEU ILE ILE GLY
SEQRES 2 A 453 GLY GLY PHE ALA GLY SER SER ALA ALA TYR GLN LEU SER
SEQRES 3 A 453 ARG ARG GLY LEU LYS ILE LEU LEU VAL ASP SER LYS PRO
SEQRES 4 A 453 TRP ASN ARG ILE GLY ASP LYS PRO CYS GLY ASP ALA VAL
SEQRES 5 A 453 SER LYS ALA HIS PHE ASP LYS LEU GLY MET PRO TYR PRO
SEQRES 6 A 453 LYS GLY GLU GLU LEU GLU ASN LYS ILE ASN GLY ILE LYS
SEQRES 7 A 453 LEU TYR SER PRO ASP MET GLN THR VAL TRP THR VAL ASN
SEQRES 8 A 453 GLY GLU GLY PHE GLU LEU ASN ALA PRO LEU TYR ASN GLN
SEQRES 9 A 453 ARG VAL LEU LYS GLU ALA GLN ASP ARG GLY VAL GLU ILE
SEQRES 10 A 453 TRP ASP LEU THR THR ALA MET LYS PRO ILE PHE GLU ASP
SEQRES 11 A 453 GLY TYR VAL LYS GLY ALA VAL LEU PHE ASN ARG ARG THR
SEQRES 12 A 453 ASN GLU GLU LEU THR VAL TYR SER LYS VAL VAL VAL GLU
SEQRES 13 A 453 ALA THR GLY TYR SER ARG SER PHE ARG SER LYS LEU PRO
SEQRES 14 A 453 PRO GLU LEU PRO ILE THR GLU ASP LEU ASP ASP LYS ASP
SEQRES 15 A 453 ALA ASP VAL ALA TYR ARG GLU VAL LEU LEU THR LYS GLU
SEQRES 16 A 453 ASP ILE GLU ASP HIS ASP TYR LEU ARG ILE PHE PHE ASP
SEQRES 17 A 453 GLN GLU THR SER PRO GLY GLY TYR TRP TRP TYR PHE PRO
SEQRES 18 A 453 LYS GLY LYS ASN LYS VAL ASN VAL GLY LEU GLY ILE GLN
SEQRES 19 A 453 GLY GLY MET GLY TYR PRO SER ILE HIS GLU TYR TYR LYS
SEQRES 20 A 453 LYS TYR LEU ASP LYS TYR ALA PRO ASP VAL ASP LYS SER
SEQRES 21 A 453 LYS LEU LEU VAL LYS GLY GLY ALA LEU VAL PRO THR ARG
SEQRES 22 A 453 ARG PRO LEU TYR THR MET ALA TRP ASN GLY ILE ILE VAL
SEQRES 23 A 453 ILE GLY ASP SER GLY PHE THR VAL ASN PRO VAL HIS GLY
SEQRES 24 A 453 GLY GLY LYS GLY SER ALA MET ILE SER GLY TYR CYS ALA
SEQRES 25 A 453 ALA LYS ALA ILE LEU SER ALA PHE GLU THR GLY ASP PHE
SEQRES 26 A 453 SER ALA SER GLY LEU TRP ASP MET ASN ILE CYS TYR VAL
SEQRES 27 A 453 ASN GLU TYR GLY ALA LYS GLN ALA SER LEU ASP ILE PHE
SEQRES 28 A 453 ARG ARG PHE LEU GLN LYS LEU SER ASN ASP ASP ILE ASN
SEQRES 29 A 453 TYR GLY MET LYS LYS LYS ILE ILE LYS GLU GLU ASP LEU
SEQRES 30 A 453 HIS GLU ALA SER GLU LYS GLY ASP LEU HIS LEU SER VAL
SEQRES 31 A 453 ALA ASP LYS ALA MET ARG VAL ILE SER GLY LEU GLY ARG
SEQRES 32 A 453 PRO SER LEU LEU PHE LYS LEU LYS ALA VAL ALA GLU SER
SEQRES 33 A 453 MET LYS LYS ILE LYS GLU LEU TYR LEU ASN TYR PRO ARG
SEQRES 34 A 453 SER PRO SER SER LEU GLY SER TRP ARG ARG GLU VAL ASP
SEQRES 35 A 453 ASN VAL LEU THR GLU PHE ASN LYS SER LEU SER
HET FDA A 501 53
HET GRG A 502 29
HET SO4 A 503 5
HETNAM FDA DIHYDROFLAVINE-ADENINE DINUCLEOTIDE
HETNAM GRG GERANYLGERANYL DIPHOSPHATE
HETNAM SO4 SULFATE ION
FORMUL 2 FDA C27 H35 N9 O15 P2
FORMUL 3 GRG C20 H36 O7 P2
FORMUL 4 SO4 O4 S 2-
FORMUL 5 HOH *17(H2 O)
HELIX 1 1 GLY A 14 SER A 25 1 12
HELIX 2 2 PRO A 38 ILE A 42 5 5
HELIX 3 3 LYS A 53 GLY A 60 1 8
HELIX 4 4 LYS A 65 GLU A 67 5 3
HELIX 5 5 ASN A 97 ARG A 112 1 16
HELIX 6 6 THR A 157 ARG A 161 5 5
HELIX 7 7 PHE A 163 LEU A 167 5 5
HELIX 8 8 LEU A 171 GLU A 175 5 5
HELIX 9 9 ASP A 178 LYS A 180 5 3
HELIX 10 10 SER A 240 ALA A 253 1 14
HELIX 11 11 GLY A 287 PHE A 291 5 5
HELIX 12 12 GLY A 300 GLY A 322 1 23
HELIX 13 13 TRP A 330 TYR A 340 1 11
HELIX 14 14 TYR A 340 GLN A 355 1 16
HELIX 15 15 SER A 358 LYS A 368 1 11
HELIX 16 16 LYS A 372 GLY A 383 1 12
HELIX 17 17 HIS A 386 SER A 398 1 13
HELIX 18 18 SER A 404 PHE A 407 5 4
HELIX 19 19 LYS A 408 ASN A 425 1 18
HELIX 20 20 SER A 429 SER A 431 5 3
HELIX 21 21 SER A 432 LEU A 451 1 20
SHEET 1 A 4 GLU A 3 LYS A 5 0
SHEET 2 A 4 GLU A 144 TYR A 149 1 O TYR A 149 N LEU A 4
SHEET 3 A 4 TYR A 131 ASN A 139 -1 N LEU A 137 O LEU A 146
SHEET 4 A 4 THR A 120 GLU A 128 -1 N LYS A 124 O VAL A 136
SHEET 1 B 6 GLU A 115 ASP A 118 0
SHEET 2 B 6 ILE A 31 ASP A 35 1 N LEU A 33 O GLU A 115
SHEET 3 B 6 VAL A 8 ILE A 11 1 N ILE A 10 O LEU A 32
SHEET 4 B 6 VAL A 152 GLU A 155 1 O VAL A 154 N ILE A 11
SHEET 5 B 6 ILE A 283 VAL A 285 1 O ILE A 284 N GLU A 155
SHEET 6 B 6 ALA A 279 TRP A 280 -1 N TRP A 280 O ILE A 283
SHEET 1 C 8 ALA A 50 SER A 52 0
SHEET 2 C 8 VAL A 86 LEU A 96 -1 O PHE A 94 N VAL A 51
SHEET 3 C 8 LEU A 69 TYR A 79 -1 N ASN A 71 O GLU A 95
SHEET 4 C 8 TYR A 201 PHE A 205 1 O LEU A 202 N LYS A 77
SHEET 5 C 8 TRP A 216 PRO A 220 -1 O TRP A 216 N PHE A 205
SHEET 6 C 8 LYS A 225 GLN A 233 -1 O ASN A 227 N PHE A 219
SHEET 7 C 8 ALA A 182 THR A 192 -1 N GLU A 188 O VAL A 228
SHEET 8 C 8 VAL A 256 PRO A 270 -1 O ASP A 257 N LEU A 191
SSBOND 1 CYS A 310 CYS A 335 1555 1555 2.03
SITE 1 AC1 30 GLY A 12 GLY A 14 PHE A 15 ALA A 16
SITE 2 AC1 30 ASP A 35 SER A 36 LYS A 37 LYS A 45
SITE 3 AC1 30 PRO A 46 CYS A 47 GLY A 48 ASP A 49
SITE 4 AC1 30 ALA A 50 THR A 120 THR A 121 ALA A 122
SITE 5 AC1 30 ALA A 156 THR A 157 GLY A 158 SER A 162
SITE 6 AC1 30 ALA A 185 ALA A 267 VAL A 269 GLY A 287
SITE 7 AC1 30 ASP A 288 GLY A 299 GLY A 300 LYS A 301
SITE 8 AC1 30 GRG A 502 HOH A 605
SITE 1 AC2 16 ALA A 50 VAL A 51 SER A 52 ALA A 54
SITE 2 AC2 16 ASN A 90 GLY A 91 GLU A 92 GLY A 93
SITE 3 AC2 16 TYR A 215 TRP A 217 HIS A 297 GLY A 298
SITE 4 AC2 16 GLY A 299 HIS A 377 GLU A 381 FDA A 501
SITE 1 AC3 5 HIS A 55 HIS A 297 TYR A 340 LYS A 343
SITE 2 AC3 5 SER A 380
CRYST1 63.652 82.198 106.363 90.00 90.00 90.00 P 21 21 21 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 0.015710 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012166 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009402 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
