HEADER TRANSFERASE 23-JUL-10 2XM5
TITLE STRUCTURAL AND MECHANISTIC ANALYSIS OF THE MAGNESIUM-INDEPENDENT
TITLE 2 AROMATIC PRENYLTRANSFERASE CLOQ FROM THE CLOROBIOCIN BIOSYNTHETIC
TITLE 3 PATHWAY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CLOQ;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AROMATIC PRENYLTRANSFERASE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: C215S MUTANT SOAKED IN 4-HYDROXYPHENYL PYRUVATE.
COMPND 8 UNINTERPRETABLE RESIDUAL ELECTRON DENSITY IN ACTIVE SITE PRESUMED TO
COMPND 9 BE THIS LIGAND.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES ROSEOCHROMOGENES SUBSP. OSCITANS;
SOURCE 3 ORGANISM_TAXID: 149682;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28A;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: CLOQ-PET28A
KEYWDS TRANSFERASE, PT-BARREL, ANTIBIOTIC BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR U.METZGER,S.KELLER,C.E.M.STEVENSON,L.HEIDE,D.M.LAWSON
REVDAT 4 20-DEC-23 2XM5 1 REMARK
REVDAT 3 06-MAR-19 2XM5 1 REMARK
REVDAT 2 08-DEC-10 2XM5 1 JRNL
REVDAT 1 27-OCT-10 2XM5 0
JRNL AUTH U.METZGER,S.KELLER,C.E.M.STEVENSON,L.HEIDE,D.M.LAWSON
JRNL TITL STRUCTURE AND MECHANISM OF THE MAGNESIUM-INDEPENDENT
JRNL TITL 2 AROMATIC PRENYLTRANSFERASE CLOQ FROM THE CLOROBIOCIN
JRNL TITL 3 BIOSYNTHETIC PATHWAY.
JRNL REF J.MOL.BIOL. V. 404 611 2010
JRNL REFN ISSN 0022-2836
JRNL PMID 20946900
JRNL DOI 10.1016/J.JMB.2010.09.067
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0091
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 37537
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 + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1967
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2706
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 150
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2412
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 269
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.00000
REMARK 3 B22 (A**2) : -1.00000
REMARK 3 B33 (A**2) : 2.01000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.100
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.096
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.060
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.945
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2661 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1815 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3629 ; 1.447 ; 1.935
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4374 ; 0.907 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 348 ; 6.111 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 132 ;31.849 ;22.348
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 404 ;12.988 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;14.513 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 386 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3069 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 611 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1641 ; 0.915 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 667 ; 0.249 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2613 ; 1.676 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1020 ; 2.572 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1002 ; 4.166 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY.
REMARK 4
REMARK 4 2XM5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1290044746.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980
REMARK 200 MONOCHROMATOR : NULL
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 : 39516
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 44.090
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.18
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.47
REMARK 200 R MERGE FOR SHELL (I) : 0.54000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.430
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: PDB ENTRY 2XLQ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION. PROTEIN (10 MG/ML)
REMARK 280 WAS MIXED WITH AN EQUAL VOLUME OF 3 M SODIUM FORMATE, 2 MM
REMARK 280 DITHIOTHREITOL, 100 MM HEPES PH 6.5 .
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 -X+1/2,Y,-Z+3/4
REMARK 290 6555 X,-Y+1/2,-Z+1/4
REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X,-Y,Z
REMARK 290 11555 -Y+1/2,X,Z+3/4
REMARK 290 12555 Y,-X+1/2,Z+1/4
REMARK 290 13555 -X,Y+1/2,-Z+1/4
REMARK 290 14555 X+1/2,-Y,-Z+3/4
REMARK 290 15555 Y,X,-Z
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 67.72500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 67.72500
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.67000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 67.72500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 24.83500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 67.72500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 74.50500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 67.72500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 74.50500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 67.72500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 24.83500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 67.72500
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 67.72500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 49.67000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 67.72500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 67.72500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 49.67000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 67.72500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 74.50500
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 67.72500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 24.83500
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 67.72500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 24.83500
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 67.72500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 74.50500
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 67.72500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 67.72500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 49.67000
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 215 TO SER
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 -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 ALA A 3
REMARK 465 LEU A 4
REMARK 465 THR A 316
REMARK 465 GLU A 317
REMARK 465 SER A 318
REMARK 465 THR A 319
REMARK 465 MET A 320
REMARK 465 GLY A 321
REMARK 465 GLY A 322
REMARK 465 ALA A 323
REMARK 465 ARG A 324
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 244 NE CZ NH1 NH2
REMARK 470 GLN A 314 CG CD OE1 NE2
REMARK 470 HIS A 315 CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG1 THR A 91 ND1 HIS A 169 2.14
REMARK 500 O GLU A 303 O HOH A 2263 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2176 O HOH A 2239 5655 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 TYR A 284 -72.30 -120.65
REMARK 500 ASN A 287 66.24 70.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 ETHYLENE GLYCOL (EDO): ETHYLENE GLYCOL WAS USED AS A
REMARK 600 CRYOPROTECTANT
REMARK 600 FORMATE (FMT): SODIUM FORMATE WAS A COMPONENT OF THE
REMARK 600 PRECIPITANT
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 10-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 11-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1316
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1319
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1320
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1322
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1324
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 1325
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XLQ RELATED DB: PDB
REMARK 900 STRUCTURAL AND MECHANISTIC ANALYSIS OF THE MAGNESIUM-INDEPENDENT
REMARK 900 AROMATIC PRENYLTRANSFERASE CLOQ FROM THE CLOROBIOCIN BIOSYNTHETIC
REMARK 900 PATHWAY
REMARK 900 RELATED ID: 2XLY RELATED DB: PDB
REMARK 900 STRUCTURAL AND MECHANISTIC ANALYSIS OF THE MAGNESIUM-INDEPENDENT
REMARK 900 AROMATIC PRENYLTRANSFERASE CLOQ FROM THE CLOROBIOCIN BIOSYNTHETIC
REMARK 900 PATHWAY
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE ARE AN ADDITIONAL THREE RESIDUES (WITH SEQUENCE GLY-SER-
REMARK 999 HIS) AT THE N-TERMINUS LEFT OVER AFTER PROTEOLYTIC CLEAVAGE
REMARK 999 OF THE HIS-TAG
DBREF 2XM5 A 1 324 UNP Q8GHB2 Q8GHB2_9ACTO 1 324
SEQADV 2XM5 GLY A -2 UNP Q8GHB2 EXPRESSION TAG
SEQADV 2XM5 SER A -1 UNP Q8GHB2 EXPRESSION TAG
SEQADV 2XM5 HIS A 0 UNP Q8GHB2 EXPRESSION TAG
SEQADV 2XM5 SER A 215 UNP Q8GHB2 CYS 215 ENGINEERED MUTATION
SEQRES 1 A 327 GLY SER HIS MET PRO ALA LEU PRO ILE ASP GLN GLU PHE
SEQRES 2 A 327 ASP CYS GLU ARG PHE ARG ALA ASP ILE ARG ALA THR ALA
SEQRES 3 A 327 ALA ALA ILE GLY ALA PRO ILE ALA HIS ARG LEU THR ASP
SEQRES 4 A 327 THR VAL LEU GLU ALA PHE ARG ASP ASN PHE ALA GLN GLY
SEQRES 5 A 327 ALA THR LEU TRP LYS THR THR SER GLN PRO GLY ASP GLN
SEQRES 6 A 327 LEU SER TYR ARG PHE PHE SER ARG LEU LYS MET ASP THR
SEQRES 7 A 327 VAL SER ARG ALA ILE ASP ALA GLY LEU LEU ASP ALA ALA
SEQRES 8 A 327 HIS PRO THR LEU ALA VAL VAL ASP ALA TRP SER SER LEU
SEQRES 9 A 327 TYR GLY GLY ALA PRO VAL GLN SER GLY ASP PHE ASP ALA
SEQRES 10 A 327 GLY ARG GLY MET ALA LYS THR TRP LEU TYR PHE GLY GLY
SEQRES 11 A 327 LEU ARG PRO ALA GLU ASP ILE LEU THR VAL PRO ALA LEU
SEQRES 12 A 327 PRO ALA SER VAL GLN ALA ARG LEU LYS ASP PHE LEU ALA
SEQRES 13 A 327 LEU GLY LEU ALA HIS VAL ARG PHE ALA ALA VAL ASP TRP
SEQRES 14 A 327 ARG HIS HIS SER ALA ASN VAL TYR PHE ARG GLY LYS GLY
SEQRES 15 A 327 PRO LEU ASP THR VAL GLN PHE ALA ARG ILE HIS ALA LEU
SEQRES 16 A 327 SER GLY SER THR PRO PRO ALA ALA HIS VAL VAL GLU GLU
SEQRES 17 A 327 VAL LEU ALA TYR MET PRO GLU ASP TYR SER VAL ALA ILE
SEQRES 18 A 327 THR LEU ASP LEU HIS SER GLY ASP ILE GLU ARG VAL CYS
SEQRES 19 A 327 PHE TYR ALA LEU LYS VAL PRO LYS ASN ALA LEU PRO ARG
SEQRES 20 A 327 ILE PRO THR ARG ILE ALA ARG PHE LEU GLU VAL ALA PRO
SEQRES 21 A 327 SER HIS ASP VAL GLU GLU CYS ASN VAL ILE GLY TRP SER
SEQRES 22 A 327 PHE GLY ARG SER GLY ASP TYR VAL LYS ALA GLU ARG SER
SEQRES 23 A 327 TYR THR GLY ASN MET ALA GLU ILE LEU ALA GLY TRP ASN
SEQRES 24 A 327 CYS PHE PHE HIS GLY GLU GLU GLY ARG ASP HIS ASP LEU
SEQRES 25 A 327 ARG ALA LEU HIS GLN HIS THR GLU SER THR MET GLY GLY
SEQRES 26 A 327 ALA ARG
HET EDO A1316 4
HET FMT A1317 3
HET FMT A1318 3
HET FMT A1319 3
HET FMT A1320 3
HET FMT A1321 3
HET FMT A1322 3
HET FMT A1323 3
HET FMT A1324 3
HET FMT A1325 3
HETNAM EDO 1,2-ETHANEDIOL
HETNAM FMT FORMIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO C2 H6 O2
FORMUL 3 FMT 9(C H2 O2)
FORMUL 12 HOH *269(H2 O)
HELIX 1 1 ASP A 11 GLY A 27 1 17
HELIX 2 2 ALA A 31 GLY A 49 1 19
HELIX 3 3 ASP A 74 ALA A 82 1 9
HELIX 4 4 THR A 91 ALA A 105 1 15
HELIX 5 5 ALA A 131 THR A 136 1 6
HELIX 6 6 PRO A 141 ALA A 146 1 6
HELIX 7 7 ARG A 147 LEU A 154 1 8
HELIX 8 8 ASP A 182 LEU A 192 1 11
HELIX 9 9 ALA A 199 TYR A 209 1 11
HELIX 10 10 PRO A 238 LEU A 242 5 5
HELIX 11 11 PRO A 246 ALA A 256 1 11
HELIX 12 12 ASN A 287 TRP A 295 1 9
HELIX 13 13 ASP A 306 HIS A 315 1 10
SHEET 1 AA11 ALA A 50 THR A 56 0
SHEET 2 AA11 SER A 64 PHE A 68 -1 O SER A 64 N LYS A 54
SHEET 3 AA11 VAL A 107 ASP A 113 -1 O GLY A 110 N PHE A 67
SHEET 4 AA11 GLY A 117 PRO A 130 -1 O GLY A 117 N ASP A 113
SHEET 5 AA11 HIS A 158 ASP A 165 -1 O VAL A 159 N ARG A 129
SHEET 6 AA11 SER A 170 ARG A 176 -1 O SER A 170 N ASP A 165
SHEET 7 AA11 SER A 215 ASP A 221 -1 O VAL A 216 N PHE A 175
SHEET 8 AA11 ILE A 227 LEU A 235 -1 N GLU A 228 O THR A 219
SHEET 9 AA11 ASN A 265 GLY A 272 -1 O ILE A 267 N ALA A 234
SHEET 10 AA11 TYR A 277 THR A 285 -1 O TYR A 277 N SER A 270
SHEET 11 AA11 ALA A 50 THR A 56 -1 O THR A 51 N THR A 285
CISPEP 1 GLY A 179 PRO A 180 0 2.49
SITE 1 AC1 5 GLU A 40 ALA A 41 ARG A 43 ASP A 44
SITE 2 AC1 5 HOH A2077
SITE 1 AC2 7 LYS A 54 LYS A 120 TRP A 122 ALA A 163
SITE 2 AC2 7 ASN A 172 TYR A 174 HOH A2110
SITE 1 AC3 6 SER A 57 ALA A 199 ALA A 200 TYR A 277
SITE 2 AC3 6 HOH A2178 HOH A2265
SITE 1 AC4 8 ARG A 176 SER A 215 TYR A 233 LEU A 235
SITE 2 AC4 8 CYS A 297 PHE A 298 HOH A2210 HOH A2266
SITE 1 AC5 6 TYR A 124 GLY A 127 ARG A 160 TRP A 295
SITE 2 AC5 6 ASN A 296 HOH A2257
SITE 1 AC6 1 TYR A 102
SITE 1 AC7 4 GLN A 58 ARG A 229 SER A 274 GLY A 275
SITE 1 AC8 4 ASP A 11 CYS A 12 ARG A 43 HOH A2268
SITE 1 AC9 3 ARG A 20 HIS A 32 ASP A 36
SITE 1 BC1 6 GLY A 27 ALA A 31 HIS A 32 ARG A 33
SITE 2 BC1 6 LEU A 34 HOH A2269
CRYST1 135.450 135.450 99.340 90.00 90.00 90.00 I 41 2 2 16
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 0.007383 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007383 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010066 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
