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HEADER HYDROLASE 17-MAY-11 3S2Z
TITLE CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL ESTERASE
TITLE 2 LJ0536 S106A MUTANT IN COMPLEX WITH CAFFEIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CINNAMOYL ESTERASE;
COMPND 3 CHAIN: A, B;
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: 562;
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
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 3S2Z 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 2011
JRNL REFN ESSN 1932-6203
JRNL DOI 10.1371/JOURNAL.PONE.0023269
REMARK 2
REMARK 2 RESOLUTION. 1.76 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) : 1.76
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 48659
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) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2615
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) : 1.76
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3179
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.1900
REMARK 3 BIN FREE R VALUE SET COUNT : 173
REMARK 3 BIN FREE R VALUE : 0.2820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3916
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 432
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : -2.07000
REMARK 3 B33 (A**2) : 1.81000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.03000
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): 0.113
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.084
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.952
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4045 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5501 ; 1.812 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 505 ; 6.059 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 202 ;33.432 ;25.099
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 653 ;13.731 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;21.877 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 618 ; 0.132 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3139 ; 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): 2494 ; 1.901 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4026 ; 2.925 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1551 ; 4.945 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1472 ; 7.016 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 4045 ; 2.533 ; 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 : 4
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): 23.3753 -1.6300 29.7399
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): 10.0994 -9.3633 35.2647
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 : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -5 B 179
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6774 20.3512 14.3501
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 : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 180 B 244
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3026 27.4973 8.0532
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 3S2Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-11.
REMARK 100 THE RCSB ID CODE IS RCSB065695.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-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) : 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) : 1.54178
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51428
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04700
REMARK 200 FOR THE DATA SET : 21.8600
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 (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.46200
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3PF8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, 0.2 M LITHIUM SULPHATE,
REMARK 280 30% PEG4K, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 36.15900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.08400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 36.15900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 42.08400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -153.0 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 B 596 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 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 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 ARG B -7
REMARK 465 GLU B -6
REMARK 465 ASN B 245
REMARK 465 ASN B 246
REMARK 465 ASN B 247
REMARK 465 ALA B 248
REMARK 465 PHE B 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 B 171 NE - CZ - NH2 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 ALA A 36 -159.60 -93.84
REMARK 500 ARG A 98 -78.55 -95.03
REMARK 500 ALA A 106 -120.73 61.86
REMARK 500 LYS A 161 -115.68 56.48
REMARK 500 ASP A 229 -116.34 63.21
REMARK 500 ASP B 9 -128.01 57.81
REMARK 500 THR B 35 -0.50 70.10
REMARK 500 ARG B 98 -87.01 -96.37
REMARK 500 ALA B 106 -121.29 54.32
REMARK 500 HIS B 153 59.74 -142.68
REMARK 500 LYS B 161 -129.60 55.67
REMARK 500 ASP B 229 -126.62 61.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLN B 244 24.6 L L OUTSIDE RANGE
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 B 928 DISTANCE = 5.07 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 254
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 255
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 258
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DHC A 259
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 253
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 254
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 255
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DHC B 257
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: 3PF9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL
REMARK 900 ESTERASE LJ0536 S106A MUTANT
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 3S2Z A 1 249 UNP D3YEX6 D3YEX6_LACJO 1 249
DBREF 3S2Z B 1 249 UNP D3YEX6 D3YEX6_LACJO 1 249
SEQADV 3S2Z MET A -20 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z GLY A -19 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z SER A -18 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z SER A -17 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z HIS A -16 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z HIS A -15 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z HIS A -14 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z HIS A -13 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z HIS A -12 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z HIS A -11 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z SER A -10 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z SER A -9 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z GLY A -8 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z ARG A -7 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z GLU A -6 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z ASN A -5 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z LEU A -4 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z TYR A -3 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z PHE A -2 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z GLN A -1 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z GLY A 0 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z ALA A 106 UNP D3YEX6 SER 106 ENGINEERED MUTATION
SEQADV 3S2Z MET B -20 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z GLY B -19 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z SER B -18 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z SER B -17 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z HIS B -16 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z HIS B -15 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z HIS B -14 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z HIS B -13 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z HIS B -12 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z HIS B -11 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z SER B -10 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z SER B -9 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z GLY B -8 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z ARG B -7 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z GLU B -6 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z ASN B -5 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z LEU B -4 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z TYR B -3 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z PHE B -2 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z GLN B -1 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z GLY B 0 UNP D3YEX6 EXPRESSION TAG
SEQADV 3S2Z ALA B 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
SEQRES 1 B 270 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 270 ARG GLU ASN LEU TYR PHE GLN GLY MET ALA THR ILE THR
SEQRES 3 B 270 LEU GLU ARG ASP GLY LEU GLN LEU VAL GLY THR ARG GLU
SEQRES 4 B 270 GLU PRO PHE GLY GLU ILE TYR ASP MET ALA ILE ILE PHE
SEQRES 5 B 270 HIS GLY PHE THR ALA ASN ARG ASN THR SER LEU LEU ARG
SEQRES 6 B 270 GLU ILE ALA ASN SER LEU ARG ASP GLU ASN ILE ALA SER
SEQRES 7 B 270 VAL ARG PHE ASP PHE ASN GLY HIS GLY ASP SER ASP GLY
SEQRES 8 B 270 LYS PHE GLU ASN MET THR VAL LEU ASN GLU ILE GLU ASP
SEQRES 9 B 270 ALA ASN ALA ILE LEU ASN TYR VAL LYS THR ASP PRO HIS
SEQRES 10 B 270 VAL ARG ASN ILE TYR LEU VAL GLY HIS ALA GLN GLY GLY
SEQRES 11 B 270 VAL VAL ALA SER MET LEU ALA GLY LEU TYR PRO ASP LEU
SEQRES 12 B 270 ILE LYS LYS VAL VAL LEU LEU ALA PRO ALA ALA THR LEU
SEQRES 13 B 270 LYS GLY ASP ALA LEU GLU GLY ASN THR GLN GLY VAL THR
SEQRES 14 B 270 TYR ASN PRO ASP HIS ILE PRO ASP ARG LEU PRO PHE LYS
SEQRES 15 B 270 ASP LEU THR LEU GLY GLY PHE TYR LEU ARG ILE ALA GLN
SEQRES 16 B 270 GLN LEU PRO ILE TYR GLU VAL SER ALA GLN PHE THR LYS
SEQRES 17 B 270 PRO VAL CYS LEU ILE HIS GLY THR ASP ASP THR VAL VAL
SEQRES 18 B 270 SER PRO ASN ALA SER LYS LYS TYR ASP GLN ILE TYR GLN
SEQRES 19 B 270 ASN SER THR LEU HIS LEU ILE GLU GLY ALA ASP HIS CYS
SEQRES 20 B 270 PHE SER ASP SER TYR GLN LYS ASN ALA VAL ASN LEU THR
SEQRES 21 B 270 THR ASP PHE LEU GLN ASN ASN ASN ALA PHE
HET CL A 250 1
HET CL A 251 1
HET CL A 252 1
HET CL A 253 1
HET CL A 254 1
HET CL A 255 1
HET CL A 256 1
HET CL A 257 1
HET CL A 258 1
HET DHC A 259 13
HET CL B 250 1
HET CL B 251 1
HET CL B 252 1
HET CL B 253 1
HET CL B 254 1
HET CL B 255 1
HET CL B 256 1
HET DHC B 257 13
HETNAM CL CHLORIDE ION
HETNAM DHC CAFFEIC ACID
HETSYN DHC 3,4-DIHYDROXYCINNAMIC ACID
FORMUL 3 CL 16(CL 1-)
FORMUL 12 DHC 2(C9 H8 O4)
FORMUL 21 HOH *432(H2 O)
HELIX 1 1 THR A 40 ASP A 52 1 13
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 ALA A 106 TYR A 119 1 14
HELIX 5 5 ALA A 133 GLY A 142 1 10
HELIX 6 6 GLY A 167 LEU A 176 1 10
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
HELIX 11 11 THR B 40 GLU B 53 1 14
HELIX 12 12 LYS B 71 MET B 75 5 5
HELIX 13 13 THR B 76 THR B 93 1 18
HELIX 14 14 GLN B 107 TYR B 119 1 13
HELIX 15 15 THR B 134 GLY B 142 1 9
HELIX 16 16 GLY B 167 LEU B 176 1 10
HELIX 17 17 PRO B 177 ALA B 183 1 7
HELIX 18 18 PRO B 202 TYR B 212 1 11
HELIX 19 19 SER B 230 GLN B 244 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 ASP A 26 O ALA A 56
SHEET 5 A 8 VAL A 97 HIS A 105 1 O TYR A 101 N MET A 27
SHEET 6 A 8 ILE A 123 LEU A 129 1 O LEU A 129 N GLY A 104
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 HIS A 218 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
SHEET 1 D 8 GLY B 0 ARG B 8 0
SHEET 2 D 8 LEU B 11 GLU B 19 -1 O GLU B 19 N GLY B 0
SHEET 3 D 8 ALA B 56 PHE B 60 -1 O SER B 57 N GLU B 18
SHEET 4 D 8 TYR B 25 PHE B 31 1 N ILE B 30 O VAL B 58
SHEET 5 D 8 VAL B 97 HIS B 105 1 O VAL B 103 N PHE B 31
SHEET 6 D 8 ILE B 123 LEU B 129 1 O LYS B 124 N ILE B 100
SHEET 7 D 8 VAL B 189 GLY B 194 1 O CYS B 190 N LEU B 128
SHEET 8 D 8 SER B 215 ILE B 220 1 O THR B 216 N LEU B 191
SHEET 1 E 2 ASN B 143 THR B 144 0
SHEET 2 E 2 VAL B 147 THR B 148 -1 O VAL B 147 N THR B 144
SHEET 1 F 2 ARG B 157 PHE B 160 0
SHEET 2 F 2 LEU B 163 GLY B 166 -1 O LEU B 165 N LEU B 158
SITE 1 AC1 4 ALA A 183 PHE A 185 TYR A 212 GLN A 213
SITE 1 AC2 6 ASN A 85 ASN A 89 TYR A 119 CL A 254
SITE 2 AC2 6 PHE B 168 HOH B1133
SITE 1 AC3 5 ASP A 209 TYR A 212 SER A 215 HOH A 430
SITE 2 AC3 5 HOH A1143
SITE 1 AC4 2 SER A 41 ARG A 44
SITE 1 AC5 6 LYS A 92 TYR A 119 CL A 251 ASP B 156
SITE 2 AC5 6 PHE B 168 HOH B1233
SITE 1 AC6 4 THR A 134 ASP A 138 HOH A1179 HOH A1183
SITE 1 AC7 3 ASP A 196 THR A 198 HIS A 225
SITE 1 AC8 4 PHE A 31 PHE A 60 PHE A 62 HOH A 262
SITE 1 AC9 3 ASN A -5 LEU A -4 HIS A 96
SITE 1 BC1 13 GLY A 33 PHE A 34 ALA A 106 GLN A 107
SITE 2 BC1 13 ALA A 132 LEU A 135 ASP A 138 THR A 144
SITE 3 BC1 13 GLN A 145 TYR A 169 HIS A 225 HOH A1219
SITE 4 BC1 13 HOH A1239
SITE 1 BC2 5 HOH A1174 ASP B 209 TYR B 212 SER B 215
SITE 2 BC2 5 HOH B1131
SITE 1 BC3 7 GLU B 73 ASN B 74 MET B 75 THR B 76
SITE 2 BC3 7 GLY B 166 TYR B 169 HOH B1145
SITE 1 BC4 4 ASP B 196 THR B 198 ASP B 224 HIS B 225
SITE 1 BC5 3 ASN B -5 LEU B -4 HIS B 96
SITE 1 BC6 2 GLY B 0 MET B 1
SITE 1 BC7 4 TYR A -3 HOH A 298 GLU B 180 GLN B 184
SITE 1 BC8 1 SER B 41
SITE 1 BC9 12 GLY B 33 PHE B 34 ALA B 106 GLN B 107
SITE 2 BC9 12 ALA B 132 LEU B 135 ASP B 138 THR B 144
SITE 3 BC9 12 GLN B 145 TYR B 169 HIS B 225 HOH B1240
CRYST1 72.318 84.168 87.604 90.00 97.56 90.00 C 1 2 1 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 0.013828 0.000000 0.001834 0.00000
SCALE2 0.000000 0.011881 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011515 0.00000
TER 1982 ASN A 245
TER 3937 GLN B 244
MASTER 525 0 18 19 24 0 28 6 4390 2 26 42
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