HEADER TRANSFERASE 28-JAN-13 3ZL6
TITLE NATIVE STRUCTURE OF FARNESYL PYROPHOSPHATE SYNTHASE FROM PSEUDOMONAS
TITLE 2 AERUGINOSA PAO1, WITH BOUND FRAGMENT KM10833.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GERANYLTRANSTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PA4043;
COMPND 5 EC: 2.5.1.10;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA PAO1;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET-28 BASED VECTOR
KEYWDS TRANSFERASE, KM10833, MAYBRIDGE FRAGMENT LIBRARY
EXPDTA X-RAY DIFFRACTION
AUTHOR J.W.SCHMIDBERGER,R.SCHNELL,G.SCHNEIDER
REVDAT 4 20-DEC-23 3ZL6 1 REMARK LINK
REVDAT 3 25-MAR-15 3ZL6 1 JRNL
REVDAT 2 11-MAR-15 3ZL6 1 JRNL
REVDAT 1 12-FEB-14 3ZL6 0
JRNL AUTH J.W.SCHMIDBERGER,R.SCHNELL,G.SCHNEIDER
JRNL TITL STRUCTURAL CHARACTERIZATION OF SUBSTRATE AND INHIBITOR
JRNL TITL 2 BINDING TO FARNESYL PYROPHOSPHATE SYNTHASE FROM PSEUDOMONAS
JRNL TITL 3 AERUGINOSA.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 71 721 2015
JRNL REFN ISSN 0907-4449
JRNL PMID 25760619
JRNL DOI 10.1107/S1399004715001121
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 31.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 44882
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2339
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) : 3289
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 182
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4086
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 429
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.57000
REMARK 3 B22 (A**2) : -0.85000
REMARK 3 B33 (A**2) : 0.28000
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): 0.137
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.134
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.088
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.929
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4188 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4074 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5676 ; 1.775 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9295 ; 1.276 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 544 ; 5.146 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 188 ;34.405 ;22.979
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 660 ;14.085 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;20.173 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 648 ; 0.109 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4838 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 940 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1559 ; 0.267 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3400 ; 0.222 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2113 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2193 ; 0.100 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 83 ; 0.166 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.076 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 6 ; 0.085 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 50 ; 0.342 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 57 ; 0.237 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.112 ; 0.200
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.20
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.
REMARK 4
REMARK 4 3ZL6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JAN-13.
REMARK 100 THE DEPOSITION ID IS D_1290055675.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00319
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47364
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 32.260
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.2000
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 : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.72000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIR
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 3ZCD
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MGCL2, 20% PEG6000, 0.1 M TRISCL
REMARK 280 PH 8
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.77500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.77500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 42.58000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.42000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 42.58000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.42000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 65.77500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 42.58000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.42000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 65.77500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 42.58000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 49.42000
REMARK 290 SMTRY3 8 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.4 KCAL/MOL
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2180 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2009 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2012 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2198 LIES ON A SPECIAL POSITION.
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 VAL A 164
REMARK 465 GLY A 165
REMARK 465 VAL A 166
REMARK 465 GLU A 228
REMARK 465 SER A 229
REMARK 465 ASP A 230
REMARK 465 THR A 231
REMARK 465 ALA A 232
REMARK 465 THR A 233
REMARK 465 LEU A 234
REMARK 465 GLY A 235
REMARK 465 LYS A 236
REMARK 465 THR A 237
REMARK 465 GLN A 238
REMARK 465 GLY A 239
REMARK 465 LYS A 240
REMARK 465 ASP A 241
REMARK 465 GLN A 242
REMARK 465 ALA A 243
REMARK 465 HIS A 244
REMARK 465 ASN A 245
REMARK 465 LYS A 246
REMARK 465 ASN A 295
REMARK 465 GLU B 228
REMARK 465 SER B 229
REMARK 465 ASP B 230
REMARK 465 THR B 231
REMARK 465 ALA B 232
REMARK 465 THR B 233
REMARK 465 LEU B 234
REMARK 465 GLY B 235
REMARK 465 LYS B 236
REMARK 465 THR B 237
REMARK 465 GLN B 238
REMARK 465 GLY B 239
REMARK 465 LYS B 240
REMARK 465 ASP B 241
REMARK 465 GLN B 242
REMARK 465 ALA B 243
REMARK 465 HIS B 244
REMARK 465 ASN B 245
REMARK 465 LYS B 246
REMARK 465 ARG B 293
REMARK 465 ARG B 294
REMARK 465 ASN B 295
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 VAL A 227 CG1 CG2
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 OD1 ASP A 18 NH1 ARG A 36 1.95
REMARK 500 OD1 ASP B 18 NH1 ARG B 36 2.00
REMARK 500 O HOH A 2076 O HOH A 2198 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 178 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 178 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 178 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
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 MET A 88 -108.71 -112.84
REMARK 500 PHE A 104 -97.59 -114.67
REMARK 500 LEU A 168 112.67 53.30
REMARK 500 MET B 88 -111.56 -107.93
REMARK 500 PHE B 104 -95.34 -109.48
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 B2012 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B2198 DISTANCE = 5.88 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 (1,2-BENZISOXAZOL-3-YL)ACETIC ACID (NVU): FRAGMENT FROM
REMARK 600 MAYBRIDGE LIBRARY KM10833
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 MG A1296 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 223 OD1
REMARK 620 2 HOH A2165 O 90.9
REMARK 620 3 HOH A2194 O 87.8 86.1
REMARK 620 4 HOH A2200 O 93.9 109.6 164.1
REMARK 620 5 HOH A2201 O 86.3 168.0 82.0 82.3
REMARK 620 6 HOH A2231 O 170.5 80.2 88.2 92.3 101.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1295 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 89 OD2
REMARK 620 2 ASP B 91 OD2 85.5
REMARK 620 3 HOH B2090 O 91.8 85.7
REMARK 620 4 HOH B2094 O 82.0 166.8 90.7
REMARK 620 5 HOH B2098 O 74.8 86.1 164.8 94.5
REMARK 620 6 HOH B2100 O 167.8 87.8 97.9 105.3 94.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1294 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 223 OD1
REMARK 620 2 HOH B2145 O 95.3
REMARK 620 3 HOH B2170 O 81.4 101.9
REMARK 620 4 HOH B2171 O 166.7 77.8 88.9
REMARK 620 5 HOH B2172 O 77.1 170.5 71.6 108.5
REMARK 620 6 HOH B2174 O 93.1 95.1 162.4 98.7 90.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1295
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1296
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NVU A 1297
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 1293
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NVU A 1298
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1294
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1295
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE IS AN N-TERMINAL ADDITIONAL SERINE RESULTING FROM
REMARK 999 CLONING AND CLEAVAGE OF HIS TAG.
DBREF 3ZL6 A 1 295 UNP Q9HWY4 Q9HWY4_PSEAE 1 295
DBREF 3ZL6 B 1 295 UNP Q9HWY4 Q9HWY4_PSEAE 1 295
SEQADV 3ZL6 SER A 0 UNP Q9HWY4 EXPRESSION TAG
SEQADV 3ZL6 SER B 0 UNP Q9HWY4 EXPRESSION TAG
SEQRES 1 A 296 SER MET ILE ALA ALA TYR GLN ALA ARG CYS GLN ALA ARG
SEQRES 2 A 296 VAL ASP ALA ALA LEU ASP ALA LEU PHE VAL ALA PRO ARG
SEQRES 3 A 296 GLU GLU LEU GLN ARG LEU TYR GLU ALA MET ARG TYR SER
SEQRES 4 A 296 VAL MET ASN GLY GLY LYS ARG VAL ARG PRO LEU LEU ALA
SEQRES 5 A 296 TYR ALA ALA CYS GLU ALA LEU GLY GLY ALA PRO GLN ARG
SEQRES 6 A 296 ALA ASP ALA ALA ALA CYS ALA VAL GLU LEU ILE HIS ALA
SEQRES 7 A 296 TYR SER LEU VAL HIS ASP ASP LEU PRO ALA MET ASP ASP
SEQRES 8 A 296 ASP ASP LEU ARG ARG GLY GLN PRO THR THR HIS ARG ALA
SEQRES 9 A 296 PHE ASP GLU ALA THR ALA ILE LEU ALA ALA ASP GLY LEU
SEQRES 10 A 296 GLN ALA LEU ALA PHE GLU VAL LEU ALA ASP THR ARG ARG
SEQRES 11 A 296 ASN PRO GLN GLU HIS ALA VAL CYS LEU GLU MET LEU THR
SEQRES 12 A 296 ARG LEU ALA ARG ALA ALA GLY SER ALA GLY MET VAL GLY
SEQRES 13 A 296 GLY GLN ALA ILE ASP LEU GLY SER VAL GLY VAL ALA LEU
SEQRES 14 A 296 ASP GLN ALA ALA LEU GLU VAL MET HIS ARG HIS LYS THR
SEQRES 15 A 296 GLY ALA LEU ILE GLU ALA SER VAL ARG LEU GLY ALA LEU
SEQRES 16 A 296 ALA SER GLY ARG ALA GLU PRO ALA SER LEU ALA ALA LEU
SEQRES 17 A 296 GLU ARG TYR ALA GLU ALA ILE GLY LEU ALA PHE GLN VAL
SEQRES 18 A 296 GLN ASP ASP ILE LEU ASP VAL GLU SER ASP THR ALA THR
SEQRES 19 A 296 LEU GLY LYS THR GLN GLY LYS ASP GLN ALA HIS ASN LYS
SEQRES 20 A 296 PRO THR TYR PRO ALA LEU LEU GLY LEU GLU ALA ALA LYS
SEQRES 21 A 296 GLY TYR ALA LEU GLU LEU ARG ASP LEU ALA LEU ALA ALA
SEQRES 22 A 296 LEU ASP GLY PHE PRO PRO SER ALA ASP PRO LEU ARG GLN
SEQRES 23 A 296 LEU ALA ARG TYR ILE VAL GLU ARG ARG ASN
SEQRES 1 B 296 SER MET ILE ALA ALA TYR GLN ALA ARG CYS GLN ALA ARG
SEQRES 2 B 296 VAL ASP ALA ALA LEU ASP ALA LEU PHE VAL ALA PRO ARG
SEQRES 3 B 296 GLU GLU LEU GLN ARG LEU TYR GLU ALA MET ARG TYR SER
SEQRES 4 B 296 VAL MET ASN GLY GLY LYS ARG VAL ARG PRO LEU LEU ALA
SEQRES 5 B 296 TYR ALA ALA CYS GLU ALA LEU GLY GLY ALA PRO GLN ARG
SEQRES 6 B 296 ALA ASP ALA ALA ALA CYS ALA VAL GLU LEU ILE HIS ALA
SEQRES 7 B 296 TYR SER LEU VAL HIS ASP ASP LEU PRO ALA MET ASP ASP
SEQRES 8 B 296 ASP ASP LEU ARG ARG GLY GLN PRO THR THR HIS ARG ALA
SEQRES 9 B 296 PHE ASP GLU ALA THR ALA ILE LEU ALA ALA ASP GLY LEU
SEQRES 10 B 296 GLN ALA LEU ALA PHE GLU VAL LEU ALA ASP THR ARG ARG
SEQRES 11 B 296 ASN PRO GLN GLU HIS ALA VAL CYS LEU GLU MET LEU THR
SEQRES 12 B 296 ARG LEU ALA ARG ALA ALA GLY SER ALA GLY MET VAL GLY
SEQRES 13 B 296 GLY GLN ALA ILE ASP LEU GLY SER VAL GLY VAL ALA LEU
SEQRES 14 B 296 ASP GLN ALA ALA LEU GLU VAL MET HIS ARG HIS LYS THR
SEQRES 15 B 296 GLY ALA LEU ILE GLU ALA SER VAL ARG LEU GLY ALA LEU
SEQRES 16 B 296 ALA SER GLY ARG ALA GLU PRO ALA SER LEU ALA ALA LEU
SEQRES 17 B 296 GLU ARG TYR ALA GLU ALA ILE GLY LEU ALA PHE GLN VAL
SEQRES 18 B 296 GLN ASP ASP ILE LEU ASP VAL GLU SER ASP THR ALA THR
SEQRES 19 B 296 LEU GLY LYS THR GLN GLY LYS ASP GLN ALA HIS ASN LYS
SEQRES 20 B 296 PRO THR TYR PRO ALA LEU LEU GLY LEU GLU ALA ALA LYS
SEQRES 21 B 296 GLY TYR ALA LEU GLU LEU ARG ASP LEU ALA LEU ALA ALA
SEQRES 22 B 296 LEU ASP GLY PHE PRO PRO SER ALA ASP PRO LEU ARG GLN
SEQRES 23 B 296 LEU ALA ARG TYR ILE VAL GLU ARG ARG ASN
HET DMS A1295 4
HET MG A1296 1
HET NVU A1297 13
HET NVU A1298 13
HET DMS B1293 4
HET MG B1294 1
HET MG B1295 1
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM MG MAGNESIUM ION
HETNAM NVU 2-(1,2-BENZOXAZOL-3-YL)ETHANOIC ACID
FORMUL 3 DMS 2(C2 H6 O S)
FORMUL 4 MG 3(MG 2+)
FORMUL 5 NVU 2(C9 H7 N O3)
FORMUL 10 HOH *429(H2 O)
HELIX 1 1 MET A 1 ALA A 19 1 19
HELIX 2 2 ARG A 25 GLU A 27 5 3
HELIX 3 3 LEU A 28 MET A 40 1 13
HELIX 4 4 ARG A 45 LEU A 58 1 14
HELIX 5 5 ALA A 61 ARG A 64 5 4
HELIX 6 6 ALA A 65 LEU A 85 1 21
HELIX 7 7 THR A 99 PHE A 104 1 6
HELIX 8 8 ASP A 105 ASP A 126 1 22
HELIX 9 9 GLU A 133 GLY A 149 1 17
HELIX 10 10 GLY A 152 SER A 163 1 12
HELIX 11 11 ASP A 169 THR A 181 1 13
HELIX 12 12 THR A 181 SER A 196 1 16
HELIX 13 13 GLU A 200 VAL A 227 1 28
HELIX 14 14 THR A 248 GLY A 254 1 7
HELIX 15 15 GLY A 254 LEU A 273 1 20
HELIX 16 16 PRO A 277 SER A 279 5 3
HELIX 17 17 ALA A 280 ARG A 293 1 14
HELIX 18 18 SER B 0 ALA B 19 1 20
HELIX 19 19 ARG B 25 GLU B 27 5 3
HELIX 20 20 LEU B 28 MET B 40 1 13
HELIX 21 21 ARG B 45 LEU B 58 1 14
HELIX 22 22 ALA B 61 ARG B 64 5 4
HELIX 23 23 ALA B 65 LEU B 85 1 21
HELIX 24 24 THR B 99 PHE B 104 1 6
HELIX 25 25 ASP B 105 ASP B 126 1 22
HELIX 26 26 GLU B 133 GLY B 149 1 17
HELIX 27 27 GLY B 152 GLY B 162 1 11
HELIX 28 28 ASP B 169 THR B 181 1 13
HELIX 29 29 THR B 181 SER B 196 1 16
HELIX 30 30 GLU B 200 VAL B 227 1 28
HELIX 31 31 THR B 248 GLY B 254 1 7
HELIX 32 32 GLY B 254 LEU B 273 1 20
HELIX 33 33 PRO B 277 SER B 279 5 3
HELIX 34 34 ALA B 280 GLU B 292 1 13
SHEET 1 AA 2 LEU A 93 ARG A 94 0
SHEET 2 AA 2 GLN A 97 PRO A 98 -1 O GLN A 97 N ARG A 94
SHEET 1 BA 2 LEU B 93 ARG B 94 0
SHEET 2 BA 2 GLN B 97 PRO B 98 -1 O GLN B 97 N ARG B 94
LINK OD1 ASP A 223 MG MG A1296 1555 1555 1.98
LINK MG MG A1296 O HOH A2165 1555 1555 2.48
LINK MG MG A1296 O HOH A2194 1555 1555 2.06
LINK MG MG A1296 O HOH A2200 1555 1555 2.20
LINK MG MG A1296 O HOH A2201 1555 1555 1.94
LINK MG MG A1296 O HOH A2231 1555 1555 1.83
LINK OD2 ASP B 89 MG MG B1295 1555 1555 2.25
LINK OD2 ASP B 91 MG MG B1295 1555 1555 1.89
LINK OD1 ASP B 223 MG MG B1294 1555 1555 1.93
LINK MG MG B1294 O HOH B2145 1555 1555 2.50
LINK MG MG B1294 O HOH B2170 1555 1555 2.28
LINK MG MG B1294 O HOH B2171 1555 1555 1.99
LINK MG MG B1294 O HOH B2172 1555 1555 2.31
LINK MG MG B1294 O HOH B2174 1555 1555 2.12
LINK MG MG B1295 O HOH B2090 1555 1555 2.16
LINK MG MG B1295 O HOH B2094 1555 1555 2.19
LINK MG MG B1295 O HOH B2098 1555 1555 2.14
LINK MG MG B1295 O HOH B2100 1555 1555 2.01
SITE 1 AC1 4 SER A 79 MET A 153 GLN A 157 HOH A2022
SITE 1 AC2 6 ASP A 223 HOH A2165 HOH A2194 HOH A2200
SITE 2 AC2 6 HOH A2201 HOH A2231
SITE 1 AC3 6 VAL A 46 ARG A 47 ILE A 185 PHE A 218
SITE 2 AC3 6 HOH A2051 HOH A2073
SITE 1 AC4 3 SER B 79 LYS B 180 HOH B2040
SITE 1 AC5 5 ILE A 2 ALA A 3 GLN A 6 LYS A 44
SITE 2 AC5 5 TYR A 289
SITE 1 AC6 6 ASP B 223 HOH B2145 HOH B2170 HOH B2171
SITE 2 AC6 6 HOH B2172 HOH B2174
SITE 1 AC7 6 ASP B 89 ASP B 91 HOH B2090 HOH B2094
SITE 2 AC7 6 HOH B2098 HOH B2100
CRYST1 85.160 98.840 131.550 90.00 90.00 90.00 C 2 2 21 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 0.011743 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010117 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007602 0.00000
MTRIX1 1 -0.217700 -0.963700 -0.154400 52.44000 1
MTRIX2 1 -0.965000 0.188800 0.181900 48.43000 1
MTRIX3 1 -0.146100 0.188600 -0.971100 -37.69000 1
(ATOM LINES ARE NOT SHOWN.)
END
