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HEADER HYDROLASE 03-SEP-12 4B9A
TITLE STRUCTURE OF A PUTATIVE EPOXIDE HYDROLASE FROM PSEUDOMONAS
TITLE 2 AERUGINOSA.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PA2086;
COMPND 5 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: PET28
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.W.SCHMIDBERGER,R.SCHNELL,G.SCHNEIDER
REVDAT 1 06-FEB-13 4B9A 0
JRNL AUTH L.MOYNIE,R.SCHNELL,S.A.MCMAHON,T.SANDALOVA,W.A.BOULKEROU,
JRNL AUTH 2 J.W.SCHMIDBERGER,M.ALPHEY,C.CUKIER,F.DUTHIE,J.KOPEC,H.LIU,
JRNL AUTH 3 A.JACEWICZ,W.N.HUNTER,J.H.NAISMITH,G.SCHNEIDER
JRNL TITL THE AEROPATH PROJECT TARGETING PSEUDOMONAS AERUGINOSA:
JRNL TITL 2 CRYSTALLOGRAPHIC STUDIES FOR ASSESSMENT OF POTENTIAL
JRNL TITL 3 TARGETS IN EARLY-STAGE DRUG DISCOVERY.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 69 25 2013
JRNL REFN ISSN 1744-3091
JRNL PMID 23295481
JRNL DOI 10.1107/S1744309112044739
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.95
REMARK 3 NUMBER OF REFLECTIONS : 84909
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) : 0.11199
REMARK 3 R VALUE (WORKING SET) : 0.11059
REMARK 3 FREE R VALUE : 0.13771
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 4482
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) : 1.450
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.488
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6126
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.246
REMARK 3 BIN FREE R VALUE SET COUNT : 317
REMARK 3 BIN FREE R VALUE : 0.267
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2436
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 89
REMARK 3 SOLVENT ATOMS : 436
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.725
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08
REMARK 3 B22 (A**2) : 0.08
REMARK 3 B33 (A**2) : -0.16
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.037
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.038
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.023
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.391
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.984
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.978
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2586 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2410 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3542 ; 1.758 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5512 ; 0.885 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 323 ; 5.324 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 129 ;31.153 ;22.093
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 388 ;10.784 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;16.047 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 383 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2938 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 640 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1072 ; 0.290 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2081 ; 0.218 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1177 ; 0.189 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1216 ; 0.107 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 78 ; 0.204 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.397 ; 0.200
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): 81 ; 0.374 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 77 ; 0.258 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.127 ; 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): 2586 ;12.386 ; 1.344
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2409 ;11.727 ; 1.400
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3532 ;15.587 ; 1.983
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 4995 ; 3.841 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 104 ;51.279 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5267 ;13.645 ; 5.000
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
REMARK 3 RIDING POSITIONS. RESIDUES 75 AND 76 ARE DISORDERED.
REMARK 4
REMARK 4 4B9A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-SEP-12.
REMARK 100 THE PDBE ID CODE IS EBI-53956.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95373
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 315R)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89489
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.45
REMARK 200 RESOLUTION RANGE LOW (A) : 72.08
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.6
REMARK 200 R MERGE (I) : 0.10
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.7
REMARK 200 R MERGE FOR SHELL (I) : 0.80
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1Y37
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.5
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M LISO4, 1.25 M (NH4)2SO4,
REMARK 280 0.1M TRIS HCL, PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.36500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.95500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.95500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 35.18250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.95500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.95500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 105.54750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.95500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.95500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 35.18250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.95500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.95500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 105.54750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
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 70.36500
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: 8110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -341.2 KCAL/MOL
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 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 A2250 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 SER A 0
REMARK 465 MET A 1
REMARK 465 ASN A 2
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 OD2 ASP A 107 O2 B SO4 A 1312 2.19
REMARK 500 NH1B ARG A 180 O HOH A 2288 2.14
REMARK 500 O3 B SO4 A 1312 O HOH A 2432 1.59
REMARK 500 O HOH A 2083 O HOH A 2220 2.20
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 2074 O HOH A 2297 3555 2.19
REMARK 500 O HOH A 2118 O HOH A 2337 7555 2.16
REMARK 500 O HOH A 2118 O HOH A 2333 7555 1.95
REMARK 500 O HOH A 2264 O HOH A 2284 7555 2.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 195 CD GLU A 195 OE2 -0.069
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 199 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG A 246 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 246 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 279 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 296 NE - CZ - NH1 ANGL. DEV. = 5.0 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 PRO A 40 58.19 -101.25
REMARK 500 GLN A 41 -162.78 -118.48
REMARK 500 ASP A 107 -133.66 59.20
REMARK 500 THR A 131 -11.47 77.91
REMARK 500 ALA A 150 42.51 -108.04
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 SO4 A1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1309
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1310
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1311
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1312
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1313
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1314
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1315
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1316
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4B9E RELATED DB: PDB
REMARK 900 STRUCTURE OF A PUTATIVE EPOXIDE HYDROLASE FROM
REMARK 900 PSEUDOMONAS AERUGINOSA, WITH BOUND MFA.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CLONING AND CUTTING OF THE HIS TAG LEAVES AND EXTRA N-
REMARK 999 TERMINAL SERINE.
DBREF 4B9A A 1 300 UNP Q9I229 Q9I229_PSEAE 1 300
SEQADV 4B9A SER A 0 UNP Q9I229 EXPRESSION TAG
SEQRES 1 A 301 SER MET ASN THR ASP PRO LEU LEU PRO GLY PHE ASP TYR
SEQRES 2 A 301 LEU THR LEU HIS THR SER ALA ALA ARG LEU ARG VAL ALA
SEQRES 3 A 301 VAL LYS GLY SER GLY PRO PRO LEU LEU LEU LEU HIS GLY
SEQRES 4 A 301 TYR PRO GLN THR HIS LEU ALA TRP HIS ARG ILE ALA PRO
SEQRES 5 A 301 ARG LEU ALA GLU ASP TYR SER VAL VAL LEU ALA ASP LEU
SEQRES 6 A 301 ARG GLY TYR GLY GLU SER ARG ALA LEU ASP GLU GLU GLY
SEQRES 7 A 301 ALA ASP TYR SER LYS ALA ALA LEU ALA ARG ASP GLN LEU
SEQRES 8 A 301 GLU THR MET GLY GLN LEU GLY PHE GLU ARG PHE ALA VAL
SEQRES 9 A 301 ILE GLY HIS ASP ARG GLY ALA ARG VAL GLY TYR ARG LEU
SEQRES 10 A 301 ALA LEU ASP HIS PRO GLN ALA VAL ALA ALA PHE VAL SER
SEQRES 11 A 301 LEU THR VAL VAL PRO ILE LEU ASP ASN TRP ALA ALA VAL
SEQRES 12 A 301 ASN LYS VAL PHE ALA LEU ASN ALA TYR HIS TRP PHE LEU
SEQRES 13 A 301 LEU ALA GLN PRO TYR ASP LEU PRO GLU ARG LEU ILE GLY
SEQRES 14 A 301 ALA ASP PRO GLU HIS PHE LEU ASP TYR THR LEU ARG ARG
SEQRES 15 A 301 MET ALA GLN GLY ARG ASP ILE TYR HIS PRO GLN ALA LEU
SEQRES 16 A 301 GLU SER TYR ARG ARG ALA PHE ARG ASP PRO ALA VAL ARG
SEQRES 17 A 301 HIS ALA MET CYS GLU ASP TYR ARG ALA ALA VAL GLY VAL
SEQRES 18 A 301 ASP ALA ASP ALA ASP GLN ALA ASP ARG ASP ALA GLY ARG
SEQRES 19 A 301 ARG LEU GLN CYS PRO VAL GLN VAL LEU TRP GLN GLU ARG
SEQRES 20 A 301 PRO TYR ALA ALA GLY GLN HIS PRO LEU GLU ILE TRP LYS
SEQRES 21 A 301 THR TRP ALA GLY GLN VAL GLU GLY ALA ALA ILE GLY ALA
SEQRES 22 A 301 SER HIS MET LEU PRO GLU ASP ALA PRO ASP ALA VAL LEU
SEQRES 23 A 301 GLU HIS LEU LEU GLY PHE LEU ALA SER HIS ARG GLU ALA
SEQRES 24 A 301 LEU ARG
HET SO4 A1301 5
HET SO4 A1302 5
HET SO4 A1303 5
HET SO4 A1304 5
HET SO4 A1305 5
HET SO4 A1306 5
HET SO4 A1307 5
HET SO4 A1308 5
HET SO4 A1309 5
HET SO4 A1310 5
HET SO4 A1311 5
HET SO4 A1312 10
HET GOL A1313 6
HET GOL A1314 6
HET GOL A1315 6
HET GOL A1316 6
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 SO4 12(O4 S 2-)
FORMUL 3 GOL 4(C3 H8 O3)
FORMUL 4 HOH *436(H2 O)
HELIX 1 1 THR A 42 HIS A 47 5 6
HELIX 2 2 ILE A 49 GLU A 55 1 7
HELIX 3 3 SER A 81 GLY A 97 1 17
HELIX 4 4 ASP A 107 HIS A 120 1 14
HELIX 5 5 PRO A 134 ALA A 141 1 8
HELIX 6 6 ASN A 143 ALA A 150 1 8
HELIX 7 7 ALA A 150 LEU A 156 1 7
HELIX 8 8 ASP A 161 GLY A 168 1 8
HELIX 9 9 ASP A 170 ALA A 183 1 14
HELIX 10 10 HIS A 190 ARG A 202 1 13
HELIX 11 11 ASP A 203 GLY A 219 1 17
HELIX 12 12 GLY A 219 GLY A 232 1 14
HELIX 13 13 HIS A 253 ALA A 262 1 10
HELIX 14 14 MET A 275 ALA A 280 1 6
HELIX 15 15 ALA A 280 HIS A 295 1 16
HELIX 16 16 HIS A 295 ARG A 300 1 6
SHEET 1 AA 2 ASP A 11 HIS A 16 0
SHEET 2 AA 2 ALA A 20 LYS A 27 -1 O LEU A 22 N LEU A 15
SHEET 1 AB 2 ARG A 71 ALA A 72 0
SHEET 2 AB 2 ALA A 20 LYS A 27 1 O ARG A 21 N ARG A 71
SHEET 1 AC 8 VAL A 265 ILE A 270 0
SHEET 2 AC 8 VAL A 239 GLN A 244 1 O VAL A 239 N GLU A 266
SHEET 3 AC 8 VAL A 124 LEU A 130 1 O PHE A 127 N GLN A 240
SHEET 4 AC 8 PHE A 101 HIS A 106 1 O PHE A 101 N ALA A 125
SHEET 5 AC 8 PRO A 32 LEU A 36 1 O PRO A 32 N ALA A 102
SHEET 6 AC 8 SER A 58 ALA A 62 1 O SER A 58 N LEU A 33
SHEET 7 AC 8 ALA A 20 LYS A 27 -1 O ALA A 25 N LEU A 61
SHEET 8 AC 8 ARG A 71 ALA A 72 1 O ARG A 71 N ARG A 21
SHEET 1 AD 8 VAL A 265 ILE A 270 0
SHEET 2 AD 8 VAL A 239 GLN A 244 1 O VAL A 239 N GLU A 266
SHEET 3 AD 8 VAL A 124 LEU A 130 1 O PHE A 127 N GLN A 240
SHEET 4 AD 8 PHE A 101 HIS A 106 1 O PHE A 101 N ALA A 125
SHEET 5 AD 8 PRO A 32 LEU A 36 1 O PRO A 32 N ALA A 102
SHEET 6 AD 8 SER A 58 ALA A 62 1 O SER A 58 N LEU A 33
SHEET 7 AD 8 ALA A 20 LYS A 27 -1 O ALA A 25 N LEU A 61
SHEET 8 AD 8 ASP A 11 HIS A 16 -1 O ASP A 11 N VAL A 26
LINK O2 SO4 A1311 NE ARG A 229 1555 1555 1.59
CISPEP 1 TYR A 39 PRO A 40 0 -3.23
CISPEP 2 TYR A 160 ASP A 161 0 5.36
SITE 1 AC1 4 ARG A 199 GLN A 226 ARG A 229 HOH A2336
SITE 1 AC2 5 ARG A 48 HIS A 190 HOH A2001 HOH A2003
SITE 2 AC2 5 HOH A2422
SITE 1 AC3 6 HIS A 295 GLU A 297 ALA A 298 HOH A2391
SITE 2 AC3 6 HOH A2418 HOH A2424
SITE 1 AC4 9 ASP A 279 ALA A 280 PRO A 281 ASP A 282
SITE 2 AC4 9 ALA A 283 HOH A2404 HOH A2406 HOH A2425
SITE 3 AC4 9 HOH A2426
SITE 1 AC5 6 HIS A 120 PRO A 121 GLN A 122 ALA A 123
SITE 2 AC5 6 HOH A2226 HOH A2427
SITE 1 AC6 4 ARG A 234 GLN A 236 HOH A2344 HOH A2351
SITE 1 AC7 6 ALA A 19 ARG A 65 ASP A 79 ARG A 87
SITE 2 AC7 6 HOH A2046 HOH A2138
SITE 1 AC8 9 THR A 131 GLN A 244 ARG A 246 TYR A 248
SITE 2 AC8 9 HIS A 274 HOH A2227 HOH A2228 HOH A2360
SITE 3 AC8 9 HOH A2361
SITE 1 AC9 4 ASP A 176 ARG A 180 TYR A 189 LEU A 194
SITE 1 BC1 2 ARG A 198 HOH A2311
SITE 1 BC2 4 ARG A 229 THR A 260 TRP A 261 HOH A2345
SITE 1 BC3 10 ASP A 107 ARG A 108 ARG A 111 HIS A 152
SITE 2 BC3 10 TRP A 153 MET A 182 TYR A 214 HIS A 274
SITE 3 BC3 10 HOH A2228 HOH A2432
SITE 1 BC4 7 PHE A 98 GLU A 99 ARG A 100 HOH A2199
SITE 2 BC4 7 HOH A2207 HOH A2210 HOH A2365
SITE 1 BC5 7 TYR A 12 ARG A 23 GLU A 69 HOH A2058
SITE 2 BC5 7 HOH A2313 HOH A2433 HOH A2434
SITE 1 BC6 8 LEU A 6 LEU A 7 PHE A 10 TYR A 12
SITE 2 BC6 8 LYS A 144 HOH A2022 HOH A2329 HOH A3001
SITE 1 BC7 9 TYR A 12 ARG A 23 HOH A2027 HOH A2057
SITE 2 BC7 9 HOH A2234 HOH A2235 HOH A2237 HOH A2433
SITE 3 BC7 9 HOH A3002
CRYST1 83.910 83.910 140.730 90.00 90.00 90.00 P 41 21 2 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 0.011918 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011918 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007106 0.00000
TER 2437 ARG A 300
MASTER 443 0 16 16 20 0 31 6 2961 1 90 24
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