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HEADER LYASE 12-MAR-18 6COC
TITLE ATHNL ENANTIOSELECTIVITY MUTANT AT-A9-H7 APO, Y13C,Y121L,P126F,L128W,
TITLE 2 C131T,F179L,A209I WITH BENZALDEHYDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-HYDROXYNITRILE LYASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: ATHNL;
COMPND 5 SYNONYM: ATHNL,(R)-HYDROXYNITRILE LYASE,(R)-OXYNITRILASE,
COMPND 6 METHYLESTERASE 5,ATMES5;
COMPND 7 EC: 4.1.2.10;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: HNL, MES5, AT5G10300, F18D22_70;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS ALPHA BETA HYDROLASE GLOBULAR HYDROXYNITRILE LYASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.J.JONES,R.J.KAZLAUSKAS,R.DESROULEAUX
REVDAT 1 20-MAR-19 6COC 0
JRNL AUTH B.J.JONES,R.DESROULEAUX,R.J.KAZLAUSKAS
JRNL TITL ATHNL ENANTIOSELECTIVITY MUTANTS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.93 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 38317
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) : 0.141
REMARK 3 R VALUE (WORKING SET) : 0.138
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2006
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) : 1.93
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2774
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 132
REMARK 3 BIN FREE R VALUE : 0.2530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4124
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 68
REMARK 3 SOLVENT ATOMS : 343
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.53000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : 0.56000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.132
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.130
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.090
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.412
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4419 ; 0.025 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4213 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5971 ; 2.360 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9744 ; 1.184 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 545 ; 6.693 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 189 ;31.928 ;24.074
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 788 ;14.918 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;16.087 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 641 ; 0.148 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4965 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1025 ; 0.003 ; 0.020
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 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 1 A 260
REMARK 3 ORIGIN FOR THE GROUP (A): -8.1272 -2.5637 3.3448
REMARK 3 T TENSOR
REMARK 3 T11: 0.0150 T22: 0.0192
REMARK 3 T33: 0.0094 T12: -0.0040
REMARK 3 T13: -0.0008 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.6117 L22: 0.2682
REMARK 3 L33: 0.4172 L12: 0.0265
REMARK 3 L13: 0.0353 L23: 0.2085
REMARK 3 S TENSOR
REMARK 3 S11: -0.0118 S12: 0.0840 S13: 0.0583
REMARK 3 S21: -0.0351 S22: -0.0160 S23: 0.0034
REMARK 3 S31: -0.0110 S32: -0.0279 S33: 0.0279
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 : B 1 B 259
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4710 -7.5111 32.9928
REMARK 3 T TENSOR
REMARK 3 T11: 0.0070 T22: 0.0266
REMARK 3 T33: 0.0252 T12: -0.0049
REMARK 3 T13: -0.0067 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.8548 L22: 0.5002
REMARK 3 L33: 0.0749 L12: 0.0662
REMARK 3 L13: 0.2354 L23: -0.0522
REMARK 3 S TENSOR
REMARK 3 S11: 0.0121 S12: -0.1203 S13: -0.0152
REMARK 3 S21: 0.0205 S22: -0.0158 S23: -0.0550
REMARK 3 S31: 0.0012 S32: -0.0331 S33: 0.0037
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 6COC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1000231834.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-NOV-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40386
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.84200
REMARK 200 R SYM FOR SHELL (I) : NULL
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: PDBID 3DQZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 17% PEG 3350, PH 6.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 24.78000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.01500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.36000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.01500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.78000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.36000
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: 3020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 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 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 LEU B 260
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 NH2 ARG B 47 O HOH B 401 1.81
REMARK 500 NH2 ARG A 47 O HOH A 401 1.82
REMARK 500 O HOH A 528 O HOH A 538 1.98
REMARK 500 O HOH B 553 O HOH B 557 2.00
REMARK 500 OG SER A 29 O HOH A 402 2.02
REMARK 500 O HOH B 510 O HOH B 550 2.07
REMARK 500 OE1 GLU B 2 O HOH B 402 2.08
REMARK 500 O HOH A 458 O HOH A 554 2.11
REMARK 500 O HOH A 444 O HOH A 548 2.15
REMARK 500 O HOH A 540 O HOH A 563 2.17
REMARK 500 OG SER B 29 O HOH B 403 2.19
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 193 CD GLU A 193 OE2 0.067
REMARK 500 GLU B 38 CD GLU B 38 OE1 -0.087
REMARK 500 GLU B 138 CD GLU B 138 OE1 0.118
REMARK 500 GLU B 182 CD GLU B 182 OE1 0.070
REMARK 500 GLU B 193 CD GLU B 193 OE1 0.073
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 200 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 200 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP A 256 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP A 256 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG B 47 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 GLU B 138 CG - CD - OE2 ANGL. DEV. = -12.6 DEGREES
REMARK 500 MET B 144 CG - SD - CE ANGL. DEV. = -11.5 DEGREES
REMARK 500 ARG B 157 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG B 175 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ASP B 221 CB - CG - OD2 ANGL. DEV. = -8.6 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 HIS A 15 -155.85 -122.19
REMARK 500 SER A 81 -119.50 58.80
REMARK 500 HIS B 15 -159.34 -121.03
REMARK 500 PRO B 46 45.17 -82.46
REMARK 500 ARG B 47 119.41 -171.22
REMARK 500 ASN B 72 -0.20 62.45
REMARK 500 SER B 81 -120.94 55.43
REMARK 500 ASN B 105 51.10 37.75
REMARK 500 LYS B 242 54.24 -140.02
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 GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HBX A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HBX A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HBX A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HBX B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HBX B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HBX B 305
DBREF 6COC A 1 258 UNP Q9LFT6 HNL_ARATH 1 258
DBREF 6COC B 1 258 UNP Q9LFT6 HNL_ARATH 1 258
SEQADV 6COC CYS A 14 UNP Q9LFT6 TYR 14 ENGINEERED MUTATION
SEQADV 6COC LEU A 122 UNP Q9LFT6 TYR 122 ENGINEERED MUTATION
SEQADV 6COC PHE A 126 UNP Q9LFT6 PRO 126 ENGINEERED MUTATION
SEQADV 6COC TRP A 129 UNP Q9LFT6 LEU 129 ENGINEERED MUTATION
SEQADV 6COC THR A 132 UNP Q9LFT6 CYS 132 ENGINEERED MUTATION
SEQADV 6COC LEU A 179 UNP Q9LFT6 PHE 179 ENGINEERED MUTATION
SEQADV 6COC ILE A 210 UNP Q9LFT6 ALA 210 ENGINEERED MUTATION
SEQADV 6COC GLY A 259 UNP Q9LFT6 EXPRESSION TAG
SEQADV 6COC LEU A 260 UNP Q9LFT6 EXPRESSION TAG
SEQADV 6COC CYS B 14 UNP Q9LFT6 TYR 14 ENGINEERED MUTATION
SEQADV 6COC LEU B 122 UNP Q9LFT6 TYR 122 ENGINEERED MUTATION
SEQADV 6COC PHE B 126 UNP Q9LFT6 PRO 126 ENGINEERED MUTATION
SEQADV 6COC TRP B 129 UNP Q9LFT6 LEU 129 ENGINEERED MUTATION
SEQADV 6COC THR B 132 UNP Q9LFT6 CYS 132 ENGINEERED MUTATION
SEQADV 6COC LEU B 179 UNP Q9LFT6 PHE 179 ENGINEERED MUTATION
SEQADV 6COC ILE B 210 UNP Q9LFT6 ALA 210 ENGINEERED MUTATION
SEQADV 6COC GLY B 259 UNP Q9LFT6 EXPRESSION TAG
SEQADV 6COC LEU B 260 UNP Q9LFT6 EXPRESSION TAG
SEQRES 1 A 260 MET GLU ARG LYS HIS HIS PHE VAL LEU VAL HIS ASN ALA
SEQRES 2 A 260 CYS HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 A 260 LEU GLU SER ALA GLY HIS ARG VAL THR ALA VAL GLU LEU
SEQRES 4 A 260 ALA ALA SER GLY ILE ASP PRO ARG PRO ILE GLN ALA VAL
SEQRES 5 A 260 GLU THR VAL ASP GLU TYR SER LYS PRO LEU ILE GLU THR
SEQRES 6 A 260 LEU LYS SER LEU PRO GLU ASN GLU GLU VAL ILE LEU VAL
SEQRES 7 A 260 GLY PHE SER PHE GLY GLY ILE ASN ILE ALA LEU ALA ALA
SEQRES 8 A 260 ASP ILE PHE PRO ALA LYS ILE LYS VAL LEU VAL PHE LEU
SEQRES 9 A 260 ASN ALA PHE LEU PRO ASP THR THR HIS VAL PRO SER HIS
SEQRES 10 A 260 VAL LEU ASP LYS LEU MET GLU MET PHE GLY GLY TRP GLY
SEQRES 11 A 260 ASP THR GLU PHE SER SER HIS GLU THR ARG ASN GLY THR
SEQRES 12 A 260 MET SER LEU LEU LYS MET GLY PRO LYS PHE MET LYS ALA
SEQRES 13 A 260 ARG LEU TYR GLN ASN CYS PRO ILE GLU ASP TYR GLU LEU
SEQRES 14 A 260 ALA LYS MET LEU HIS ARG GLN GLY SER LEU PHE THR GLU
SEQRES 15 A 260 ASP LEU SER LYS LYS GLU LYS PHE SER GLU GLU GLY TYR
SEQRES 16 A 260 GLY SER VAL GLN ARG VAL TYR VAL MET SER SER GLU ASP
SEQRES 17 A 260 LYS ILE ILE PRO CYS ASP PHE ILE ARG TRP MET ILE ASP
SEQRES 18 A 260 ASN PHE ASN VAL SER LYS VAL TYR GLU ILE ASP GLY GLY
SEQRES 19 A 260 ASP HIS MET VAL MET LEU SER LYS PRO GLN LYS LEU PHE
SEQRES 20 A 260 ASP SER LEU SER ALA ILE ALA THR ASP TYR MET GLY LEU
SEQRES 1 B 260 MET GLU ARG LYS HIS HIS PHE VAL LEU VAL HIS ASN ALA
SEQRES 2 B 260 CYS HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 B 260 LEU GLU SER ALA GLY HIS ARG VAL THR ALA VAL GLU LEU
SEQRES 4 B 260 ALA ALA SER GLY ILE ASP PRO ARG PRO ILE GLN ALA VAL
SEQRES 5 B 260 GLU THR VAL ASP GLU TYR SER LYS PRO LEU ILE GLU THR
SEQRES 6 B 260 LEU LYS SER LEU PRO GLU ASN GLU GLU VAL ILE LEU VAL
SEQRES 7 B 260 GLY PHE SER PHE GLY GLY ILE ASN ILE ALA LEU ALA ALA
SEQRES 8 B 260 ASP ILE PHE PRO ALA LYS ILE LYS VAL LEU VAL PHE LEU
SEQRES 9 B 260 ASN ALA PHE LEU PRO ASP THR THR HIS VAL PRO SER HIS
SEQRES 10 B 260 VAL LEU ASP LYS LEU MET GLU MET PHE GLY GLY TRP GLY
SEQRES 11 B 260 ASP THR GLU PHE SER SER HIS GLU THR ARG ASN GLY THR
SEQRES 12 B 260 MET SER LEU LEU LYS MET GLY PRO LYS PHE MET LYS ALA
SEQRES 13 B 260 ARG LEU TYR GLN ASN CYS PRO ILE GLU ASP TYR GLU LEU
SEQRES 14 B 260 ALA LYS MET LEU HIS ARG GLN GLY SER LEU PHE THR GLU
SEQRES 15 B 260 ASP LEU SER LYS LYS GLU LYS PHE SER GLU GLU GLY TYR
SEQRES 16 B 260 GLY SER VAL GLN ARG VAL TYR VAL MET SER SER GLU ASP
SEQRES 17 B 260 LYS ILE ILE PRO CYS ASP PHE ILE ARG TRP MET ILE ASP
SEQRES 18 B 260 ASN PHE ASN VAL SER LYS VAL TYR GLU ILE ASP GLY GLY
SEQRES 19 B 260 ASP HIS MET VAL MET LEU SER LYS PRO GLN LYS LEU PHE
SEQRES 20 B 260 ASP SER LEU SER ALA ILE ALA THR ASP TYR MET GLY LEU
HET GOL A 301 6
HET GOL A 302 6
HET CL A 303 1
HET HBX A 304 8
HET HBX A 305 8
HET HBX A 306 8
HET GOL B 301 6
HET CL B 302 1
HET HBX B 303 8
HET HBX B 304 8
HET HBX B 305 8
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM HBX BENZALDEHYDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 3(C3 H8 O3)
FORMUL 5 CL 2(CL 1-)
FORMUL 6 HBX 6(C7 H6 O)
FORMUL 14 HOH *343(H2 O)
HELIX 1 AA1 GLY A 16 TYR A 21 5 6
HELIX 2 AA2 LYS A 22 ALA A 30 1 9
HELIX 3 AA3 PRO A 48 VAL A 52 5 5
HELIX 4 AA4 THR A 54 SER A 59 1 6
HELIX 5 AA5 SER A 59 SER A 68 1 10
HELIX 6 AA6 PHE A 82 PHE A 94 1 13
HELIX 7 AA7 SER A 116 PHE A 126 1 11
HELIX 8 AA8 GLY A 150 LEU A 158 1 9
HELIX 9 AA9 PRO A 163 HIS A 174 1 12
HELIX 10 AB1 PHE A 180 LYS A 186 1 7
HELIX 11 AB2 GLY A 194 VAL A 198 5 5
HELIX 12 AB3 PRO A 212 PHE A 223 1 12
HELIX 13 AB4 MET A 237 LYS A 242 1 6
HELIX 14 AB5 LYS A 242 TYR A 257 1 16
HELIX 15 AB6 GLY B 16 TYR B 21 5 6
HELIX 16 AB7 LYS B 22 ALA B 30 1 9
HELIX 17 AB8 PRO B 48 VAL B 52 5 5
HELIX 18 AB9 THR B 54 SER B 59 1 6
HELIX 19 AC1 SER B 59 LEU B 69 1 11
HELIX 20 AC2 PHE B 82 PHE B 94 1 13
HELIX 21 AC3 SER B 116 PHE B 126 1 11
HELIX 22 AC4 GLY B 150 LEU B 158 1 9
HELIX 23 AC5 PRO B 163 HIS B 174 1 12
HELIX 24 AC6 PHE B 180 LYS B 186 1 7
HELIX 25 AC7 GLY B 194 VAL B 198 5 5
HELIX 26 AC8 PRO B 212 PHE B 223 1 12
HELIX 27 AC9 MET B 237 LYS B 242 1 6
HELIX 28 AD1 LYS B 242 TYR B 257 1 16
SHEET 1 AA1 6 ARG A 33 ALA A 36 0
SHEET 2 AA1 6 HIS A 6 VAL A 10 1 N LEU A 9 O THR A 35
SHEET 3 AA1 6 VAL A 75 PHE A 80 1 O VAL A 78 N VAL A 8
SHEET 4 AA1 6 ILE A 98 LEU A 104 1 O LEU A 104 N GLY A 79
SHEET 5 AA1 6 ARG A 200 SER A 205 1 O VAL A 203 N PHE A 103
SHEET 6 AA1 6 VAL A 228 ILE A 231 1 O TYR A 229 N MET A 204
SHEET 1 AA2 2 GLU A 133 THR A 139 0
SHEET 2 AA2 2 GLY A 142 LYS A 148 -1 O LYS A 148 N GLU A 133
SHEET 1 AA3 6 ARG B 33 VAL B 37 0
SHEET 2 AA3 6 HIS B 6 VAL B 10 1 N PHE B 7 O ARG B 33
SHEET 3 AA3 6 VAL B 75 PHE B 80 1 O VAL B 78 N VAL B 10
SHEET 4 AA3 6 ILE B 98 LEU B 104 1 O VAL B 102 N LEU B 77
SHEET 5 AA3 6 ARG B 200 SER B 205 1 O VAL B 203 N PHE B 103
SHEET 6 AA3 6 VAL B 228 ILE B 231 1 O TYR B 229 N MET B 204
SHEET 1 AA4 2 GLU B 133 THR B 139 0
SHEET 2 AA4 2 GLY B 142 LYS B 148 -1 O MET B 144 N HIS B 137
SITE 1 AC1 7 GLU A 53 ASN A 141 MET A 144 ASP A 183
SITE 2 AC1 7 LYS A 186 HOH A 412 HOH A 438
SITE 1 AC2 5 ASP A 92 LYS A 187 GLU A 188 PHE A 190
SITE 2 AC2 5 HOH A 467
SITE 1 AC3 5 ASN A 12 ALA A 13 SER A 81 PHE A 82
SITE 2 AC3 5 HBX A 306
SITE 1 AC4 3 GLY A 128 GLY A 130 ARG A 157
SITE 1 AC5 2 MET A 123 HOH A 430
SITE 1 AC6 8 ASN A 12 ALA A 13 SER A 81 TRP A 129
SITE 2 AC6 8 LEU A 147 MET A 149 HIS A 236 CL A 303
SITE 1 AC7 8 GLU B 53 ASN B 141 THR B 143 MET B 144
SITE 2 AC7 8 PHE B 180 GLU B 182 ASP B 183 LYS B 186
SITE 1 AC8 5 ASN B 12 ALA B 13 SER B 81 PHE B 82
SITE 2 AC8 5 HOH B 505
SITE 1 AC9 8 GLU B 53 THR B 139 ARG B 140 ASN B 161
SITE 2 AC9 8 GLU B 207 GLY B 233 LYS B 242 HOH B 416
SITE 1 AD1 4 GLY B 130 LYS B 152 ALA B 156 ARG B 157
SITE 1 AD2 1 HOH B 567
CRYST1 49.560 86.720 122.030 90.00 90.00 90.00 P 21 21 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 0.020178 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011531 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008195 0.00000
TER 2111 LEU A 260
TER 4242 GLY B 259
MASTER 426 0 11 28 16 0 18 6 4535 2 66 40
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