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HEADER LYASE 12-MAR-18 6COH
TITLE ATHNL ENANTIOSELECTIVITY MUTANT AT-A9-H7 APO, Y13C,Y121L,P126F,L128W,
TITLE 2 C131T,A209I WITH BENZALDEHYDE, MANDELIC ACID NITRILE
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 6COH 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. 2.37 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) : 2.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 21683
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) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1178
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) : 2.37
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.43
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1486
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE SET COUNT : 73
REMARK 3 BIN FREE R VALUE : 0.2460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4122
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 159
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : 0.05000
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): 0.367
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.228
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.180
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.771
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4289 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4077 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5792 ; 2.012 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9433 ; 1.083 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 524 ; 6.982 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 190 ;35.620 ;24.316
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 761 ;16.145 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;19.526 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 627 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4759 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 975 ; 0.002 ; 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 259
REMARK 3 ORIGIN FOR THE GROUP (A): 8.0489 90.0349 127.4600
REMARK 3 T TENSOR
REMARK 3 T11: 0.0636 T22: 0.0402
REMARK 3 T33: 0.0141 T12: 0.0031
REMARK 3 T13: 0.0075 T23: -0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 1.6317 L22: 0.7664
REMARK 3 L33: 1.0665 L12: 0.0400
REMARK 3 L13: 0.0166 L23: -0.1356
REMARK 3 S TENSOR
REMARK 3 S11: -0.0308 S12: 0.2224 S13: -0.1214
REMARK 3 S21: -0.1164 S22: -0.0230 S23: -0.0319
REMARK 3 S31: 0.0958 S32: 0.0562 S33: 0.0538
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): -9.6104 95.2603 157.5678
REMARK 3 T TENSOR
REMARK 3 T11: 0.0522 T22: 0.0479
REMARK 3 T33: 0.0088 T12: -0.0007
REMARK 3 T13: 0.0122 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 1.9028 L22: 0.7134
REMARK 3 L33: 0.6562 L12: 0.0124
REMARK 3 L13: -0.1982 L23: 0.0538
REMARK 3 S TENSOR
REMARK 3 S11: 0.0081 S12: -0.2474 S13: -0.0078
REMARK 3 S21: 0.0924 S22: -0.0157 S23: 0.0333
REMARK 3 S31: 0.0026 S32: -0.0052 S33: 0.0076
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 6COH 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_1000231848.
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 : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97741
REMARK 200 MONOCHROMATOR : SI (111) ROSENBAUM-ROCK DOUBLE
REMARK 200 -CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22909
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.367
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 : 6.100
REMARK 200 R MERGE (I) : 0.14900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 3.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.67900
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: REFMAC
REMARK 200 STARTING MODEL: PDBID 3DQZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 20% PEG 3350, PH 6.4,
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 25.13850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.99500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.73150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.99500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.13850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.73150
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: 2160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 A 260
REMARK 465 LEU B 260
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 47 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 MET A 123 CG - SD - CE ANGL. DEV. = -12.2 DEGREES
REMARK 500 ARG A 157 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 MET A 172 CG - SD - CE ANGL. DEV. = -10.3 DEGREES
REMARK 500 ASP B 92 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG B 217 NE - CZ - NH1 ANGL. DEV. = 3.3 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 -164.45 -121.23
REMARK 500 ASN A 72 -1.34 77.39
REMARK 500 SER A 81 -121.37 54.91
REMARK 500 ILE A 210 -53.09 -120.58
REMARK 500 LYS A 227 135.06 -175.87
REMARK 500 HIS B 15 -164.62 -121.04
REMARK 500 SER B 81 -121.09 61.38
REMARK 500 ASN B 105 50.13 33.99
REMARK 500 ASP B 214 -65.61 -9.54
REMARK 500 PHE B 223 97.95 -161.45
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 MXN 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 HBX B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MXN B 302
DBREF 6COH A 1 258 UNP Q9LFT6 HNL_ARATH 1 258
DBREF 6COH B 1 258 UNP Q9LFT6 HNL_ARATH 1 258
SEQADV 6COH CYS A 14 UNP Q9LFT6 TYR 14 ENGINEERED MUTATION
SEQADV 6COH LEU A 122 UNP Q9LFT6 TYR 122 ENGINEERED MUTATION
SEQADV 6COH PHE A 126 UNP Q9LFT6 PRO 126 ENGINEERED MUTATION
SEQADV 6COH TRP A 129 UNP Q9LFT6 LEU 129 ENGINEERED MUTATION
SEQADV 6COH THR A 132 UNP Q9LFT6 CYS 132 ENGINEERED MUTATION
SEQADV 6COH ILE A 210 UNP Q9LFT6 ALA 210 ENGINEERED MUTATION
SEQADV 6COH GLY A 259 UNP Q9LFT6 EXPRESSION TAG
SEQADV 6COH LEU A 260 UNP Q9LFT6 EXPRESSION TAG
SEQADV 6COH CYS B 14 UNP Q9LFT6 TYR 14 ENGINEERED MUTATION
SEQADV 6COH LEU B 122 UNP Q9LFT6 TYR 122 ENGINEERED MUTATION
SEQADV 6COH PHE B 126 UNP Q9LFT6 PRO 126 ENGINEERED MUTATION
SEQADV 6COH TRP B 129 UNP Q9LFT6 LEU 129 ENGINEERED MUTATION
SEQADV 6COH THR B 132 UNP Q9LFT6 CYS 132 ENGINEERED MUTATION
SEQADV 6COH ILE B 210 UNP Q9LFT6 ALA 210 ENGINEERED MUTATION
SEQADV 6COH GLY B 259 UNP Q9LFT6 EXPRESSION TAG
SEQADV 6COH 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 PHE 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 PHE 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 MXN A 301 10
HET GOL A 302 6
HET HBX B 301 8
HET MXN B 302 10
HETNAM MXN (2R)-HYDROXY(PHENYL)ETHANENITRILE
HETNAM GOL GLYCEROL
HETNAM HBX BENZALDEHYDE
HETSYN MXN (R)-MANDELONITRILE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 MXN 2(C8 H7 N O)
FORMUL 4 GOL C3 H8 O3
FORMUL 5 HBX C7 H6 O
FORMUL 7 HOH *159(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 LEU A 69 1 16
HELIX 5 AA5 PHE A 82 PHE A 94 1 13
HELIX 6 AA6 SER A 116 PHE A 126 1 11
HELIX 7 AA7 GLY A 150 LEU A 158 1 9
HELIX 8 AA8 PRO A 163 HIS A 174 1 12
HELIX 9 AA9 PHE A 180 LYS A 186 1 7
HELIX 10 AB1 GLY A 194 VAL A 198 5 5
HELIX 11 AB2 PRO A 212 PHE A 223 1 12
HELIX 12 AB3 MET A 237 LYS A 242 1 6
HELIX 13 AB4 LYS A 242 TYR A 257 1 16
HELIX 14 AB5 GLY B 16 TYR B 21 5 6
HELIX 15 AB6 LYS B 22 ALA B 30 1 9
HELIX 16 AB7 PRO B 48 VAL B 52 5 5
HELIX 17 AB8 THR B 54 SER B 68 1 15
HELIX 18 AB9 PHE B 82 ASP B 92 1 11
HELIX 19 AC1 PHE B 94 ALA B 96 5 3
HELIX 20 AC2 SER B 116 PHE B 126 1 11
HELIX 21 AC3 GLY B 150 LEU B 158 1 9
HELIX 22 AC4 PRO B 163 HIS B 174 1 12
HELIX 23 AC5 PHE B 180 LYS B 186 1 7
HELIX 24 AC6 GLY B 194 VAL B 198 5 5
HELIX 25 AC7 PRO B 212 PHE B 223 1 12
HELIX 26 AC8 MET B 237 LYS B 242 1 6
HELIX 27 AC9 LYS B 242 TYR B 257 1 16
SHEET 1 AA1 6 ARG A 33 VAL A 37 0
SHEET 2 AA1 6 HIS A 6 VAL A 10 1 N PHE A 7 O ARG A 33
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 VAL A 102 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 ILE A 231 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 LEU A 146 N SER A 135
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 ILE B 76 N VAL B 8
SHEET 4 AA3 6 ILE B 98 LEU B 104 1 O VAL B 102 N LEU B 77
SHEET 5 AA3 6 GLN B 199 SER B 205 1 O VAL B 201 N LEU B 101
SHEET 6 AA3 6 VAL B 228 ILE B 231 1 O ILE B 231 N MET B 204
SHEET 1 AA4 3 GLU B 133 THR B 139 0
SHEET 2 AA4 3 GLY B 142 LYS B 148 -1 O MET B 144 N HIS B 137
SHEET 3 AA4 3 GLY B 177 SER B 178 -1 O GLY B 177 N LEU B 147
SITE 1 AC1 7 ASN A 12 ALA A 13 SER A 81 PHE A 82
SITE 2 AC1 7 MET A 149 PHE A 179 HIS A 236
SITE 1 AC2 7 GLU A 53 THR A 139 ASN A 141 MET A 144
SITE 2 AC2 7 ASP A 183 LYS A 186 HOH A 406
SITE 1 AC3 4 PHE B 107 MET B 123 PHE B 179 MXN B 302
SITE 1 AC4 7 ASN B 12 ALA B 13 SER B 81 PHE B 82
SITE 2 AC4 7 MET B 149 HIS B 236 HBX B 301
CRYST1 50.277 87.463 123.990 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 0.019890 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011433 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008065 0.00000
TER 2074 GLY A 259
TER 4150 GLY B 259
MASTER 353 0 4 27 17 0 7 6 4315 2 34 40
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