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HEADER HYDROLASE 28-OCT-10 3PFC
TITLE CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL ESTERASE
TITLE 2 LJ0536 S106A MUTANT IN COMPLEX WITH FERULIC ACID
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 3PFC 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 : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 24852
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1245
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 17.6499 - 3.6305 1.00 2809 148 0.1332 0.1403
REMARK 3 2 3.6305 - 2.8858 1.00 2710 143 0.1517 0.1860
REMARK 3 3 2.8858 - 2.5222 0.99 2671 142 0.1604 0.1964
REMARK 3 4 2.5222 - 2.2921 0.99 2668 142 0.1521 0.2015
REMARK 3 5 2.2921 - 2.1281 0.98 2629 140 0.1479 0.1720
REMARK 3 6 2.1281 - 2.0028 0.98 2613 136 0.1491 0.1863
REMARK 3 7 2.0028 - 1.9026 0.97 2582 137 0.1602 0.1713
REMARK 3 8 1.9026 - 1.8199 0.95 2534 134 0.1851 0.2390
REMARK 3 9 1.8199 - 1.7499 0.90 2391 123 0.2326 0.2540
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 49.61
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.43460
REMARK 3 B22 (A**2) : -1.93760
REMARK 3 B33 (A**2) : 0.50310
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.016 2025
REMARK 3 ANGLE : 1.677 2752
REMARK 3 CHIRALITY : 0.120 311
REMARK 3 PLANARITY : 0.010 362
REMARK 3 DIHEDRAL : 13.420 737
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain A and resid -5:179
REMARK 3 ORIGIN FOR THE GROUP (A): -27.5885 -11.5703 -7.3898
REMARK 3 T TENSOR
REMARK 3 T11: 0.1122 T22: 0.1200
REMARK 3 T33: 0.1463 T12: 0.0121
REMARK 3 T13: -0.0375 T23: -0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 0.5539 L22: 2.1455
REMARK 3 L33: 0.3038 L12: 0.3665
REMARK 3 L13: 0.0874 L23: 0.7633
REMARK 3 S TENSOR
REMARK 3 S11: -0.0163 S12: -0.0045 S13: -0.0111
REMARK 3 S21: -0.2326 S22: -0.1122 S23: 0.3349
REMARK 3 S31: -0.0373 S32: -0.0396 S33: 0.1177
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain A and resid 180:244
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5427 -18.4355 -13.6151
REMARK 3 T TENSOR
REMARK 3 T11: 0.1523 T22: 0.1387
REMARK 3 T33: 0.1327 T12: 0.0027
REMARK 3 T13: 0.0191 T23: -0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 0.3360 L22: 1.9449
REMARK 3 L33: 1.1768 L12: -0.1468
REMARK 3 L13: -0.2259 L23: 0.9583
REMARK 3 S TENSOR
REMARK 3 S11: 0.0250 S12: 0.0379 S13: -0.0793
REMARK 3 S21: -0.2860 S22: 0.0577 S23: -0.2101
REMARK 3 S31: -0.0104 S32: 0.1578 S33: -0.0785
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3PFC 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 RCSB062309.
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 : 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) : 1.5418
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 : 25396
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05800
REMARK 200 FOR THE DATA SET : 22.2000
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 (%) : 94.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.48400
REMARK 200 FOR SHELL : 2.880
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 S106A MUTANT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 0.2 M LITHIUM
REMARK 280 SULFATE, 30% PEG4K, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 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 40.49050
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 40.49050
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 36.02300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.70100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 36.02300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.70100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 40.49050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 36.02300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.70100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 40.49050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 36.02300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.70100
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: 6330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -171.0 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 245
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: 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 O HOH A 353 O HOH A 440 2.09
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 -158.72 -92.35
REMARK 500 ARG A 98 -82.02 -92.11
REMARK 500 ALA A 106 -119.64 59.35
REMARK 500 LYS A 161 -128.22 58.07
REMARK 500 ASP A 229 -117.60 55.07
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 A 244 22.8 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 A 443 DISTANCE = 5.37 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PE4 A 265
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 251 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 358 O
REMARK 620 2 THR A 198 OG1 93.9
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 FER 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 253
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 254
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 255
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 259
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A 265
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: 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 FORM I
REMARK 900 RELATED ID: 3QM1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LACTOBACILLUS JOHNSONII CINNAMOYL
REMARK 900 ESTERASE LJ0536 S106A MUTANT IN COMPLEX WITH ETHYLFERULATE,
REMARK 900 FORM II
DBREF 3PFC A 1 249 UNP D3YEX6 D3YEX6_LACJO 1 249
SEQADV 3PFC MET A -20 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC GLY A -19 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC SER A -18 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC SER A -17 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC HIS A -16 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC HIS A -15 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC HIS A -14 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC HIS A -13 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC HIS A -12 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC HIS A -11 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC SER A -10 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC SER A -9 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC GLY A -8 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC ARG A -7 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC GLU A -6 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC ASN A -5 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC LEU A -4 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC TYR A -3 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC PHE A -2 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC GLN A -1 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC GLY A 0 UNP D3YEX6 EXPRESSION TAG
SEQADV 3PFC 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 FER A 250 14
HET NA A 251 1
HET NA A 252 1
HET NA 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 CL A 259 1
HET CL A 260 1
HET CL A 261 1
HET CL A 262 1
HET CL A 263 1
HET CL A 264 1
HET PE4 A 265 6
HETNAM FER 3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC ACID
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-
HETNAM 2 PE4 ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
HETSYN FER FERULIC ACID
HETSYN PE4 POLYETHYLENE GLYCOL PEG4000
FORMUL 2 FER C10 H10 O4
FORMUL 3 NA 3(NA 1+)
FORMUL 6 CL 11(CL 1-)
FORMUL 17 PE4 C16 H34 O8
FORMUL 18 HOH *214(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 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 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 GLN A 244 1 14
SHEET 1 A 8 GLY A 0 ARG A 8 0
SHEET 2 A 8 LEU A 11 GLU A 19 -1 O GLU A 19 N GLY A 0
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 165 N LEU A 158
LINK NA NA A 253 O HOH A 364 1555 1555 2.90
LINK NA NA A 251 O HOH A 358 1555 1555 3.09
LINK OG1 THR A 198 NA NA A 251 1555 1555 3.14
SITE 1 AC1 12 GLY A 33 PHE A 34 ALA A 106 GLN A 107
SITE 2 AC1 12 LEU A 135 ASP A 138 THR A 144 GLN A 145
SITE 3 AC1 12 TYR A 169 HIS A 225 HOH A 299 HOH A 401
SITE 1 AC2 4 THR A 198 ASP A 224 HIS A 225 HOH A 358
SITE 1 AC3 3 ARG A 98 ASP A 196 HOH A 364
SITE 1 AC4 5 PRO A 20 PHE A 21 ARG A 51 ASN A 54
SITE 2 AC4 5 HOH A 420
SITE 1 AC5 3 ASN A -5 LEU A -4 HIS A 96
SITE 1 AC6 1 TYR A -3
SITE 1 AC7 3 SER A 41 ARG A 44 CL A 258
SITE 1 AC8 3 ARG A 44 ASN A 48 CL A 257
SITE 1 AC9 1 HOH A 445
SITE 1 BC1 4 HIS A 32 GLY A 33 ALA A 36 HIS A 105
SITE 1 BC2 2 SER A 41 HOH A 474
SITE 1 BC3 3 ILE A 4 THR A 5 ASN A 214
SITE 1 BC4 1 GLU A 221
SITE 1 BC5 1 ASN A 99
SITE 1 BC6 2 LEU A -4 GLU A 180
CRYST1 72.046 85.402 80.981 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 0.013880 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011709 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012349 0.00000
TER 1965 GLN A 244
MASTER 440 0 16 10 12 0 18 6 2202 1 25 21
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