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HEADER LYASE 12-MAR-18 6COE
TITLE ATHNL ENANTIOSELECTIVITY MUTANT AT-A9-H7 APO Y13C,Y121L,P126F,L128W,
TITLE 2 C131T,F179L,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 6COE 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. 1.84 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) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 42949
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) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2245
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) : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.89
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2940
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 146
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4112
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 82
REMARK 3 SOLVENT ATOMS : 336
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.21
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) : -0.08000
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): 0.127
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.124
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.084
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.523
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4385 ; 0.026 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4157 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5922 ; 2.259 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9626 ; 1.175 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 537 ; 6.438 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 189 ;36.676 ;24.392
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 775 ;15.572 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;19.136 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 641 ; 0.160 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4885 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 998 ; 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 258
REMARK 3 ORIGIN FOR THE GROUP (A): -8.0078 -2.7194 3.0469
REMARK 3 T TENSOR
REMARK 3 T11: 0.0174 T22: 0.0697
REMARK 3 T33: 0.0215 T12: -0.0167
REMARK 3 T13: -0.0103 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.6156 L22: 0.1069
REMARK 3 L33: 0.7867 L12: 0.0941
REMARK 3 L13: 0.0002 L23: 0.1560
REMARK 3 S TENSOR
REMARK 3 S11: -0.0890 S12: 0.1673 S13: 0.0462
REMARK 3 S21: -0.0259 S22: 0.0239 S23: -0.0076
REMARK 3 S31: -0.0558 S32: -0.0699 S33: 0.0651
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): 9.3664 -7.0640 33.0550
REMARK 3 T TENSOR
REMARK 3 T11: 0.0154 T22: 0.0333
REMARK 3 T33: 0.0301 T12: 0.0004
REMARK 3 T13: -0.0163 T23: -0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 0.7043 L22: 0.3378
REMARK 3 L33: 0.2917 L12: 0.1432
REMARK 3 L13: 0.1463 L23: -0.0149
REMARK 3 S TENSOR
REMARK 3 S11: 0.0130 S12: -0.0816 S13: -0.0132
REMARK 3 S21: 0.0356 S22: 0.0045 S23: -0.0285
REMARK 3 S31: -0.0113 S32: 0.0134 S33: -0.0175
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 6COE 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_1000231844.
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 : 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 : 45246
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.844
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 (%) : 95.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.42200
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: NULL
REMARK 200 STARTING MODEL: PDBID 3DQZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 16% PEG 3350, PH 6.4,
REMARK 280 VAPOR DIFFUSION, SITTING 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 25.01200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.64150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.61550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.64150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.01200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.61550
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: 3320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 GLY A 259
REMARK 465 LEU A 260
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 OE2 GLU B 53 O HOH B 401 2.02
REMARK 500 O HOH A 555 O HOH A 557 2.04
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 38 CD GLU A 38 OE1 -0.082
REMARK 500 GLU A 73 CD GLU A 73 OE1 0.072
REMARK 500 GLY A 127 N GLY A 127 CA 0.098
REMARK 500 SER A 135 CB SER A 135 OG -0.094
REMARK 500 GLU A 182 CD GLU A 182 OE1 0.072
REMARK 500 GLU B 38 CD GLU B 38 OE2 -0.076
REMARK 500 GLU B 53 CD GLU B 53 OE2 -0.080
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 33 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ASP A 56 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 157 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 157 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 CYS A 213 CB - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP A 232 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG B 3 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 33 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 157 NE - CZ - NH1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG B 157 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B 175 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 CYS B 213 CB - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 ASP B 221 CB - CG - OD2 ANGL. DEV. = -6.0 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 CYS A 14 -1.97 75.62
REMARK 500 HIS A 15 -160.85 -118.64
REMARK 500 ASN A 72 -0.12 74.43
REMARK 500 SER A 81 -123.30 63.57
REMARK 500 GLU B 2 150.10 -49.14
REMARK 500 HIS B 15 -157.88 -119.43
REMARK 500 SER B 81 -117.24 61.34
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 GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL 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 GOL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues MNN A 306 and MXN A
REMARK 800 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues MNN A 306 and MXN A
REMARK 800 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues MNN A 306 and MXN A
REMARK 800 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues MNN A 306 and MXN A
REMARK 800 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues MNN A 306 and MXN A
REMARK 800 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues MNN A 306 and MXN A
REMARK 800 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues MNN A 306 and MXN A
REMARK 800 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues MNN A 306 and MXN A
REMARK 800 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues MNN B 304 and MXN B
REMARK 800 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues MNN B 304 and MXN B
REMARK 800 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues MNN B 304 and MXN B
REMARK 800 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues MNN B 304 and MXN B
REMARK 800 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues MNN B 304 and MXN B
REMARK 800 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues MNN B 304 and MXN B
REMARK 800 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues MNN B 304 and MXN B
REMARK 800 305
DBREF 6COE A 1 258 UNP Q9LFT6 HNL_ARATH 1 258
DBREF 6COE B 1 258 UNP Q9LFT6 HNL_ARATH 1 258
SEQADV 6COE CYS A 14 UNP Q9LFT6 TYR 14 ENGINEERED MUTATION
SEQADV 6COE LEU A 122 UNP Q9LFT6 TYR 122 ENGINEERED MUTATION
SEQADV 6COE PHE A 126 UNP Q9LFT6 PRO 126 ENGINEERED MUTATION
SEQADV 6COE TRP A 129 UNP Q9LFT6 LEU 129 ENGINEERED MUTATION
SEQADV 6COE THR A 132 UNP Q9LFT6 CYS 132 ENGINEERED MUTATION
SEQADV 6COE LEU A 179 UNP Q9LFT6 PHE 179 ENGINEERED MUTATION
SEQADV 6COE ILE A 210 UNP Q9LFT6 ALA 210 ENGINEERED MUTATION
SEQADV 6COE GLY A 259 UNP Q9LFT6 EXPRESSION TAG
SEQADV 6COE LEU A 260 UNP Q9LFT6 EXPRESSION TAG
SEQADV 6COE CYS B 14 UNP Q9LFT6 TYR 14 ENGINEERED MUTATION
SEQADV 6COE LEU B 122 UNP Q9LFT6 TYR 122 ENGINEERED MUTATION
SEQADV 6COE PHE B 126 UNP Q9LFT6 PRO 126 ENGINEERED MUTATION
SEQADV 6COE TRP B 129 UNP Q9LFT6 LEU 129 ENGINEERED MUTATION
SEQADV 6COE THR B 132 UNP Q9LFT6 CYS 132 ENGINEERED MUTATION
SEQADV 6COE LEU B 179 UNP Q9LFT6 PHE 179 ENGINEERED MUTATION
SEQADV 6COE ILE B 210 UNP Q9LFT6 ALA 210 ENGINEERED MUTATION
SEQADV 6COE GLY B 259 UNP Q9LFT6 EXPRESSION TAG
SEQADV 6COE 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 GOL A 303 6
HET CL A 304 1
HET HBX A 305 8
HET MNN A 306 10
HET MXN A 307 10
HET GOL B 301 6
HET CL B 302 1
HET HBX B 303 8
HET MNN B 304 10
HET MXN B 305 10
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM HBX BENZALDEHYDE
HETNAM MNN (S)-MANDELIC ACID NITRILE
HETNAM MXN (2R)-HYDROXY(PHENYL)ETHANENITRILE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN MNN (S)-HYDROXY(PHENYL)ACETONITRILE
HETSYN MXN (R)-MANDELONITRILE
FORMUL 3 GOL 4(C3 H8 O3)
FORMUL 6 CL 2(CL 1-)
FORMUL 7 HBX 2(C7 H6 O)
FORMUL 8 MNN 2(C8 H7 N O)
FORMUL 9 MXN 2(C8 H7 N O)
FORMUL 15 HOH *336(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 68 1 15
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 187 1 8
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 ALA A 36 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 LEU A 77
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 ALA B 36 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 8
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 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 2 GLU B 133 THR B 139 0
SHEET 2 AA4 2 GLY B 142 LYS B 148 -1 O LEU B 146 N SER B 135
LINK C1 MNN A 306 C6 MXN A 307 1555 1555 1.25
LINK C7 MNN A 306 C5 MXN A 307 1555 1555 1.55
LINK C8 MNN A 306 C7 MXN A 307 1555 1555 1.06
LINK C8 MNN A 306 O10 MXN A 307 1555 1555 1.38
LINK C8 MNN A 306 C1 MXN A 307 1555 1555 1.23
LINK C8 MNN A 306 C6 MXN A 307 1555 1555 1.62
LINK O10 MNN A 306 C1 MXN A 307 1555 1555 1.22
LINK O10 MNN A 306 C3 MXN A 307 1555 1555 1.34
LINK C1 MNN B 304 C5 MXN B 305 1555 1555 1.18
LINK C6 MNN B 304 C5 MXN B 305 1555 1555 1.25
LINK C7 MNN B 304 C5 MXN B 305 1555 1555 1.50
LINK C8 MNN B 304 C7 MXN B 305 1555 1555 1.15
LINK C8 MNN B 304 C6 MXN B 305 1555 1555 1.53
LINK O10 MNN B 304 C2 MXN B 305 1555 1555 1.39
LINK O10 MNN B 304 C1 MXN B 305 1555 1555 1.46
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 432 HOH A 467
SITE 1 AC2 2 HIS A 137 GLU A 138
SITE 1 AC3 4 GLY A 128 GLY A 130 PHE A 153 ARG A 157
SITE 1 AC4 6 ASN A 12 ALA A 13 SER A 81 PHE A 82
SITE 2 AC4 6 MNN A 306 MXN A 307
SITE 1 AC5 1 HOH A 408
SITE 1 AC6 7 GLU B 53 THR B 139 ARG B 140 ASN B 161
SITE 2 AC6 7 GLY B 233 LYS B 242 HOH B 401
SITE 1 AC7 6 ASN B 12 ALA B 13 SER B 81 PHE B 82
SITE 2 AC7 6 MNN B 304 MXN B 305
SITE 1 AC8 11 ASN A 12 ALA A 13 SER A 81 PHE A 82
SITE 2 AC8 11 PHE A 107 LEU A 122 TRP A 129 MET A 149
SITE 3 AC8 11 ILE A 210 HIS A 236 CL A 304
SITE 1 AC9 11 ASN A 12 ALA A 13 SER A 81 PHE A 82
SITE 2 AC9 11 PHE A 107 LEU A 122 TRP A 129 MET A 149
SITE 3 AC9 11 ILE A 210 HIS A 236 CL A 304
SITE 1 AD1 11 ASN A 12 ALA A 13 SER A 81 PHE A 82
SITE 2 AD1 11 PHE A 107 LEU A 122 TRP A 129 MET A 149
SITE 3 AD1 11 ILE A 210 HIS A 236 CL A 304
SITE 1 AD2 11 ASN A 12 ALA A 13 SER A 81 PHE A 82
SITE 2 AD2 11 PHE A 107 LEU A 122 TRP A 129 MET A 149
SITE 3 AD2 11 ILE A 210 HIS A 236 CL A 304
SITE 1 AD3 11 ASN A 12 ALA A 13 SER A 81 PHE A 82
SITE 2 AD3 11 PHE A 107 LEU A 122 TRP A 129 MET A 149
SITE 3 AD3 11 ILE A 210 HIS A 236 CL A 304
SITE 1 AD4 11 ASN A 12 ALA A 13 SER A 81 PHE A 82
SITE 2 AD4 11 PHE A 107 LEU A 122 TRP A 129 MET A 149
SITE 3 AD4 11 ILE A 210 HIS A 236 CL A 304
SITE 1 AD5 11 ASN A 12 ALA A 13 SER A 81 PHE A 82
SITE 2 AD5 11 PHE A 107 LEU A 122 TRP A 129 MET A 149
SITE 3 AD5 11 ILE A 210 HIS A 236 CL A 304
SITE 1 AD6 11 ASN A 12 ALA A 13 SER A 81 PHE A 82
SITE 2 AD6 11 PHE A 107 LEU A 122 TRP A 129 MET A 149
SITE 3 AD6 11 ILE A 210 HIS A 236 CL A 304
SITE 1 AD7 11 ASN B 12 ALA B 13 SER B 81 PHE B 82
SITE 2 AD7 11 PHE B 107 MET B 123 PHE B 126 TRP B 129
SITE 3 AD7 11 MET B 149 HIS B 236 CL B 302
SITE 1 AD8 11 ASN B 12 ALA B 13 SER B 81 PHE B 82
SITE 2 AD8 11 PHE B 107 MET B 123 PHE B 126 TRP B 129
SITE 3 AD8 11 MET B 149 HIS B 236 CL B 302
SITE 1 AD9 11 ASN B 12 ALA B 13 SER B 81 PHE B 82
SITE 2 AD9 11 PHE B 107 MET B 123 PHE B 126 TRP B 129
SITE 3 AD9 11 MET B 149 HIS B 236 CL B 302
SITE 1 AE1 11 ASN B 12 ALA B 13 SER B 81 PHE B 82
SITE 2 AE1 11 PHE B 107 MET B 123 PHE B 126 TRP B 129
SITE 3 AE1 11 MET B 149 HIS B 236 CL B 302
SITE 1 AE2 11 ASN B 12 ALA B 13 SER B 81 PHE B 82
SITE 2 AE2 11 PHE B 107 MET B 123 PHE B 126 TRP B 129
SITE 3 AE2 11 MET B 149 HIS B 236 CL B 302
SITE 1 AE3 11 ASN B 12 ALA B 13 SER B 81 PHE B 82
SITE 2 AE3 11 PHE B 107 MET B 123 PHE B 126 TRP B 129
SITE 3 AE3 11 MET B 149 HIS B 236 CL B 302
SITE 1 AE4 11 ASN B 12 ALA B 13 SER B 81 PHE B 82
SITE 2 AE4 11 PHE B 107 MET B 123 PHE B 126 TRP B 129
SITE 3 AE4 11 MET B 149 HIS B 236 CL B 302
CRYST1 50.024 87.231 123.283 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 0.019990 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011464 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008111 0.00000
TER 2078 MET A 258
TER 4198 GLY B 259
MASTER 481 0 12 27 16 0 56 6 4530 2 83 40
END |