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HEADER HYDROLASE 28-OCT-10 3PF9
TITLE CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL ESTERASE
TITLE 2 LJ0536 S106A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CINNAMOYL ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS JOHNSONII;
SOURCE 3 ORGANISM_TAXID: 33959;
SOURCE 4 GENE: LJ0536;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P15TV-L
KEYWDS ALPHA/BETA HYDROLASE FOLD, ESTERASE, HYDROLASE, CINNAMOYL/FERULOYL
KEYWDS 2 ESTERASE, HYDROXYCINAMMATES, EXTRACELLULAR
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,K.K.LAI,C.VU,X.XU,H.CUI,S.MOLLOY,C.F.GONZALEZ,A.YAKUNIN,
AUTHOR 2 A.SAVCHENKO
REVDAT 1 31-AUG-11 3PF9 0
JRNL AUTH K.K.LAI,P.J.STOGIOS,C.VU,X.XU,H.CUI,S.MOLLOY,A.SAVCHENKO,
JRNL AUTH 2 A.YAKUNIN,C.F.GONZALEZ
JRNL TITL AN INSERTED ALPHA/BETA SUBDOMAIN SHAPES THE CATALYTIC POCKET
JRNL TITL 2 OF LACTOBACILLUS JOHNSONII CINNAMOYL ESTERASE
JRNL REF PLOS ONE V. 6 2011
JRNL REFN ESSN 1932-6203
JRNL DOI 10.1371/JOURNAL.PONE.0023269
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 24675
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) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.142
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1310
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1762
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.63
REMARK 3 BIN R VALUE (WORKING SET) : 0.2360
REMARK 3 BIN FREE R VALUE SET COUNT : 74
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1962
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 275
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.22000
REMARK 3 B22 (A**2) : -1.08000
REMARK 3 B33 (A**2) : -0.13000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.108
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.073
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.133
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
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): 2033 ; 0.025 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2772 ; 1.843 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 260 ; 6.039 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 102 ;35.642 ;25.196
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 334 ;13.779 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;20.923 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 316 ; 0.142 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1573 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1260 ; 1.909 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2041 ; 2.872 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 773 ; 4.773 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 726 ; 6.696 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2033 ; 2.602 ; 3.000
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -5 A 179
REMARK 3 ORIGIN FOR THE GROUP (A): -28.0564 -11.2655 -7.8493
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: 0.0000
REMARK 3 T33: 0.0000 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: -0.0000
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 180 A 245
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6832 -18.7138 -13.8719
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: 0.0000
REMARK 3 T33: 0.0000 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: -0.0000
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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
REMARK 4
REMARK 4 3PF9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB062306.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-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) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26002
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05700
REMARK 200 FOR THE DATA SET : 37.8700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.46000
REMARK 200 FOR SHELL : 3.750
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: CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII
REMARK 200 CINNAMOYL ESTERASE LJ0536
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE PH 6.5, 0.2 M
REMARK 280 CALCIUM ACETATE, 9% PEG8K, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
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 40.94450
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 40.94450
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 36.37000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.85100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 36.37000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.85100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 40.94450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 36.37000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.85100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 40.94450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 36.37000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.85100
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: 3500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 MET A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 ARG A -7
REMARK 465 GLU A -6
REMARK 465 ASN A 246
REMARK 465 ASN A 247
REMARK 465 ALA A 248
REMARK 465 PHE A 249
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 98 NE - CZ - NH1 ANGL. DEV. = 3.5 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 ARG A 98 -85.18 -90.26
REMARK 500 ALA A 106 -124.85 64.66
REMARK 500 ALA A 132 48.06 -79.88
REMARK 500 HIS A 153 73.98 -152.41
REMARK 500 LYS A 161 -115.34 49.52
REMARK 500 ASP A 229 -114.01 56.90
REMARK 500
REMARK 500 REMARK: NULL
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 NA A 250 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 66 O
REMARK 620 2 HOH A 293 O 75.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 253 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 212 O
REMARK 620 2 SER A 215 OG 106.7
REMARK 620 3 HOH A 435 O 67.6 140.7
REMARK 620 4 ASP A 209 O 99.0 74.1 68.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 251 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 326 O
REMARK 620 2 HOH A 316 O 88.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 252 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 457 O
REMARK 620 2 HOH A 366 O 101.3
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 253
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PF8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL
REMARK 900 ESTERASE LJ0536
REMARK 900 RELATED ID: 3PFA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL
REMARK 900 ESTERASE LJ0536 S106A MUTANT IN COMPLEX WITH CAFFEIC ACID
REMARK 900 RELATED ID: 3PFB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL
REMARK 900 ESTERASE LJ0536 S106A MUTANT IN COMPLEX WITH ETHYLFERULATE
REMARK 900 RELATED ID: 3PFC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL
REMARK 900 ESTERASE LJ0536 S106A MUTANT IN COMPLEX WITH FERULIC ACID
DBREF 3PF9 A 1 249 UNP D3YEX6 D3YEX6_LACJO 1 249
SEQADV 3PF9 MET A -20 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 GLY A -19 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 SER A -18 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 SER A -17 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 HIS A -16 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 HIS A -15 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 HIS A -14 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 HIS A -13 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 HIS A -12 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 HIS A -11 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 SER A -10 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 SER A -9 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 GLY A -8 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 ARG A -7 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 GLU A -6 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 ASN A -5 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 LEU A -4 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 TYR A -3 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 PHE A -2 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 GLN A -1 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 GLY A 0 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PF9 ALA A 106 UNP D3YEX6 SER 106 ENGINEERED MUTATION
SEQRES 1 A 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 270 ARG GLU ASN LEU TYR PHE GLN GLY MET ALA THR ILE THR
SEQRES 3 A 270 LEU GLU ARG ASP GLY LEU GLN LEU VAL GLY THR ARG GLU
SEQRES 4 A 270 GLU PRO PHE GLY GLU ILE TYR ASP MET ALA ILE ILE PHE
SEQRES 5 A 270 HIS GLY PHE THR ALA ASN ARG ASN THR SER LEU LEU ARG
SEQRES 6 A 270 GLU ILE ALA ASN SER LEU ARG ASP GLU ASN ILE ALA SER
SEQRES 7 A 270 VAL ARG PHE ASP PHE ASN GLY HIS GLY ASP SER ASP GLY
SEQRES 8 A 270 LYS PHE GLU ASN MET THR VAL LEU ASN GLU ILE GLU ASP
SEQRES 9 A 270 ALA ASN ALA ILE LEU ASN TYR VAL LYS THR ASP PRO HIS
SEQRES 10 A 270 VAL ARG ASN ILE TYR LEU VAL GLY HIS ALA GLN GLY GLY
SEQRES 11 A 270 VAL VAL ALA SER MET LEU ALA GLY LEU TYR PRO ASP LEU
SEQRES 12 A 270 ILE LYS LYS VAL VAL LEU LEU ALA PRO ALA ALA THR LEU
SEQRES 13 A 270 LYS GLY ASP ALA LEU GLU GLY ASN THR GLN GLY VAL THR
SEQRES 14 A 270 TYR ASN PRO ASP HIS ILE PRO ASP ARG LEU PRO PHE LYS
SEQRES 15 A 270 ASP LEU THR LEU GLY GLY PHE TYR LEU ARG ILE ALA GLN
SEQRES 16 A 270 GLN LEU PRO ILE TYR GLU VAL SER ALA GLN PHE THR LYS
SEQRES 17 A 270 PRO VAL CYS LEU ILE HIS GLY THR ASP ASP THR VAL VAL
SEQRES 18 A 270 SER PRO ASN ALA SER LYS LYS TYR ASP GLN ILE TYR GLN
SEQRES 19 A 270 ASN SER THR LEU HIS LEU ILE GLU GLY ALA ASP HIS CYS
SEQRES 20 A 270 PHE SER ASP SER TYR GLN LYS ASN ALA VAL ASN LEU THR
SEQRES 21 A 270 THR ASP PHE LEU GLN ASN ASN ASN ALA PHE
HET NA A 250 1
HET NA A 251 1
HET NA A 252 1
HET NA A 253 1
HETNAM NA SODIUM ION
FORMUL 2 NA 4(NA 1+)
FORMUL 6 HOH *275(H2 O)
HELIX 1 1 THR A 40 GLU A 53 1 14
HELIX 2 2 LYS A 71 MET A 75 5 5
HELIX 3 3 THR A 76 THR A 93 1 18
HELIX 4 4 GLN A 107 TYR A 119 1 13
HELIX 5 5 ALA A 133 GLY A 142 1 10
HELIX 6 6 GLY A 167 GLN A 175 1 9
HELIX 7 7 PRO A 177 ALA A 183 1 7
HELIX 8 8 PRO A 202 TYR A 212 1 11
HELIX 9 9 SER A 228 SER A 230 5 3
HELIX 10 10 TYR A 231 ASN A 245 1 15
SHEET 1 A 8 GLY A 0 ARG A 8 0
SHEET 2 A 8 LEU A 11 GLU A 19 -1 O GLY A 15 N ILE A 4
SHEET 3 A 8 ALA A 56 PHE A 60 -1 O SER A 57 N GLU A 18
SHEET 4 A 8 TYR A 25 PHE A 31 1 N ILE A 30 O VAL A 58
SHEET 5 A 8 VAL A 97 HIS A 105 1 O VAL A 103 N PHE A 31
SHEET 6 A 8 ILE A 123 LEU A 129 1 O LYS A 124 N ILE A 100
SHEET 7 A 8 VAL A 189 GLY A 194 1 O CYS A 190 N LEU A 128
SHEET 8 A 8 SER A 215 ILE A 220 1 O THR A 216 N LEU A 191
SHEET 1 B 2 ASN A 143 THR A 144 0
SHEET 2 B 2 VAL A 147 THR A 148 -1 O VAL A 147 N THR A 144
SHEET 1 C 2 ARG A 157 PHE A 160 0
SHEET 2 C 2 LEU A 163 GLY A 166 -1 O LEU A 163 N PHE A 160
LINK O GLY A 66 NA NA A 250 1555 1555 2.27
LINK NA NA A 250 O HOH A 293 1555 1555 2.42
LINK O TYR A 212 NA NA A 253 1555 1555 2.51
LINK OG SER A 215 NA NA A 253 1555 1555 2.65
LINK NA NA A 251 O HOH A 326 1555 1555 2.70
LINK NA NA A 253 O HOH A 435 1555 1555 2.72
LINK NA NA A 252 O HOH A 457 1555 1555 2.76
LINK O ASP A 209 NA NA A 253 1555 1555 2.79
LINK NA NA A 251 O HOH A 316 1555 1555 2.80
LINK NA NA A 252 O HOH A 366 1555 1555 2.88
SITE 1 AC1 4 GLY A 66 HOH A 256 HOH A 293 HOH A 295
SITE 1 AC2 2 HOH A 316 HOH A 326
SITE 1 AC3 5 GLN A 213 SER A 215 NA A 253 HOH A 366
SITE 2 AC3 5 HOH A 457
SITE 1 AC4 5 ASP A 209 TYR A 212 SER A 215 NA A 252
SITE 2 AC4 5 HOH A 435
CRYST1 72.740 85.702 81.889 90.00 90.00 90.00 C 2 2 21 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 0.013748 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011668 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012212 0.00000
TER 1989 ASN A 245
MASTER 423 0 4 10 12 0 6 6 2241 1 14 21
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