HEADER HYDROLASE 06-APR-04 1SZO
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE 6-OXO CAMPHOR HYDROLASE HIS122ALA
TITLE 2 MUTANT BOUND TO ITS NATURAL PRODUCT (2S,4S)-ALPHA-CAMPHOLINIC ACID
CAVEAT 1SZO CHIRALITY ERROR IN RESIDUES THR F 120 AND VAL H 232
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 6-OXOCAMPHOR HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP. NCIMB 9784;
SOURCE 3 ORGANISM_TAXID: 157732;
SOURCE 4 GENE: CAMK;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
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: PET-26B (NOVAGEN)
KEYWDS ENZYME-PRODUCT COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.M.LEONARD,G.GROGAN
REVDAT 5 23-AUG-23 1SZO 1 REMARK
REVDAT 4 27-OCT-21 1SZO 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1SZO 1 VERSN
REVDAT 2 03-AUG-04 1SZO 1 JRNL
REVDAT 1 29-JUN-04 1SZO 0
JRNL AUTH P.M.LEONARD,G.GROGAN
JRNL TITL STRUCTURE OF 6-OXO CAMPHOR HYDROLASE H122A MUTANT BOUND TO
JRNL TITL 2 ITS NATURAL PRODUCT, (2S,4S)-ALPHA-CAMPHOLINIC ACID: MUTANT
JRNL TITL 3 STRUCTURE SUGGESTS AN ATYPICAL MODE OF TRANSITION STATE
JRNL TITL 4 BINDING FOR A CROTONASE HOMOLOG.
JRNL REF J.BIOL.CHEM. V. 279 31312 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15138275
JRNL DOI 10.1074/JBC.M403514200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.L.WHITTINGHAM,J.P.TURKENBURG,C.S.VERMA,M.A.WALSH,G.GROGAN
REMARK 1 TITL THE 2- CRYSTAL STRUCTURE OF 6-OXO CAMPHOR HYDROLASE. NEW
REMARK 1 TITL 2 STRUCTURAL DIVERSITY IN THE CROTONASE SUPERFAMILY.
REMARK 1 REF J.BIOL.CHEM. V. 278 1744 2003
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.M211188200
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.GROGAN,G.A.ROBERTS,D.BOUGIOUKOU,N.J.TURNER,S.L.FLITSCH
REMARK 1 TITL THE DESYMMETRIZATION OF BICYCLIC BETA-DIKETONES BY AN
REMARK 1 TITL 2 ENZYMATIC RETRO-CLAISEN REACTION. A NEW REACTION OF THE
REMARK 1 TITL 3 CROTONASE SUPERFAMILY.
REMARK 1 REF J.BIOL.CHEM. V. 276 12565 2001
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.M011538200
REMARK 1 REFERENCE 3
REMARK 1 AUTH G.GROGAN,J.GRAF,A.JONES,S.PARSONS,N.J.TURNER,S.L.FLITSCH
REMARK 1 TITL AN ASYMMETRIC ENZYME-CATALYSED RETRO-CLAISEN REACTION FOR
REMARK 1 TITL 2 THE DESYMMETRISATION OF CYCLIC BETA-DIKETONES.
REMARK 1 REF ANGEW.CHEM.INT.ED.ENGL. V. 40 1111 2001
REMARK 1 REFN ESSN 0570-0833
REMARK 1 DOI 10.1002/1521-3773(20010316)40:6<1111::AID-ANIE11110>3.3.CO;2
REMARK 1 DOI 2 -U
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 218036
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 11502
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2010
REMARK 3 BIN FREE R VALUE SET COUNT : 828
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23068
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 160
REMARK 3 SOLVENT ATOMS : 1929
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.38000
REMARK 3 B22 (A**2) : 0.66000
REMARK 3 B33 (A**2) : 0.68000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.30000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; 0.018 ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; 1.663 ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SZO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022130.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220)
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 229538
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : 0.04700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.28200
REMARK 200 R SYM FOR SHELL (I) : 0.24100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1O8U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MME 2000, CALCIUM ACETATE, MES, PH
REMARK 280 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 66.00400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TRIMER, OF WHICH THERE ARE
REMARK 300 FOUR COMPLETE COPIES IN THE ASYMMETRIC UNIT.
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, L
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
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 28070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L
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
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 28000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 MET A 1
REMARK 465 LYS A 2
REMARK 465 GLN A 3
REMARK 465 MET A 253
REMARK 465 GLU A 254
REMARK 465 SER A 255
REMARK 465 GLU A 256
REMARK 465 GLN A 257
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 GLN B 3
REMARK 465 GLY B 252
REMARK 465 MET B 253
REMARK 465 GLU B 254
REMARK 465 SER B 255
REMARK 465 GLU B 256
REMARK 465 GLN B 257
REMARK 465 MET C 1
REMARK 465 LYS C 2
REMARK 465 GLN C 3
REMARK 465 GLY C 252
REMARK 465 MET C 253
REMARK 465 GLU C 254
REMARK 465 SER C 255
REMARK 465 GLU C 256
REMARK 465 GLN C 257
REMARK 465 MET D 1
REMARK 465 MET D 253
REMARK 465 GLU D 254
REMARK 465 SER D 255
REMARK 465 GLU D 256
REMARK 465 GLN D 257
REMARK 465 MET E 1
REMARK 465 LYS E 2
REMARK 465 GLN E 3
REMARK 465 GLY E 252
REMARK 465 MET E 253
REMARK 465 GLU E 254
REMARK 465 SER E 255
REMARK 465 GLU E 256
REMARK 465 GLN E 257
REMARK 465 MET F 1
REMARK 465 LYS F 2
REMARK 465 GLN F 3
REMARK 465 LEU F 4
REMARK 465 MET F 253
REMARK 465 GLU F 254
REMARK 465 SER F 255
REMARK 465 GLU F 256
REMARK 465 GLN F 257
REMARK 465 MET G 1
REMARK 465 LYS G 2
REMARK 465 GLN G 3
REMARK 465 MET G 253
REMARK 465 GLU G 254
REMARK 465 SER G 255
REMARK 465 GLU G 256
REMARK 465 GLN G 257
REMARK 465 MET H 1
REMARK 465 LYS H 2
REMARK 465 GLN H 3
REMARK 465 GLY H 252
REMARK 465 MET H 253
REMARK 465 GLU H 254
REMARK 465 SER H 255
REMARK 465 GLU H 256
REMARK 465 GLN H 257
REMARK 465 MET I 1
REMARK 465 LYS I 2
REMARK 465 GLN I 3
REMARK 465 MET I 253
REMARK 465 GLU I 254
REMARK 465 SER I 255
REMARK 465 GLU I 256
REMARK 465 GLN I 257
REMARK 465 MET J 1
REMARK 465 LYS J 2
REMARK 465 GLN J 3
REMARK 465 MET J 253
REMARK 465 GLU J 254
REMARK 465 SER J 255
REMARK 465 GLU J 256
REMARK 465 GLN J 257
REMARK 465 MET K 1
REMARK 465 LYS K 2
REMARK 465 GLN K 3
REMARK 465 MET K 253
REMARK 465 GLU K 254
REMARK 465 SER K 255
REMARK 465 GLU K 256
REMARK 465 GLN K 257
REMARK 465 MET L 1
REMARK 465 LYS L 2
REMARK 465 GLN L 3
REMARK 465 LEU L 4
REMARK 465 MET L 253
REMARK 465 GLU L 254
REMARK 465 SER L 255
REMARK 465 GLU L 256
REMARK 465 GLN L 257
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU A 4 CG CD1 CD2
REMARK 470 LYS A 36 CE NZ
REMARK 470 GLN A 197 CD OE1 NE2
REMARK 470 GLU A 212 CD OE1 OE2
REMARK 470 LYS B 14 NZ
REMARK 470 LYS C 36 CE NZ
REMARK 470 LYS D 2 CG CD CE NZ
REMARK 470 GLN D 3 CG CD OE1 NE2
REMARK 470 GLU D 10 CG CD OE1 OE2
REMARK 470 LYS D 36 CE NZ
REMARK 470 GLN D 197 CG CD OE1 NE2
REMARK 470 GLU E 10 CG CD OE1 OE2
REMARK 470 LYS E 36 NZ
REMARK 470 ARG E 99 CD NE NH1 NH2
REMARK 470 LYS F 36 CE NZ
REMARK 470 LYS G 14 CG CD CE NZ
REMARK 470 GLU G 196 CG CD OE1 OE2
REMARK 470 GLN G 197 CD OE1 NE2
REMARK 470 GLN H 9 CG CD OE1 NE2
REMARK 470 ARG H 19 NE CZ NH1 NH2
REMARK 470 LYS H 36 CE NZ
REMARK 470 GLN H 197 CD OE1 NE2
REMARK 470 GLU H 198 CG CD OE1 OE2
REMARK 470 GLU H 212 CD OE1 OE2
REMARK 470 LEU I 4 CB CG CD1 CD2
REMARK 470 GLN I 197 CG CD OE1 NE2
REMARK 470 LYS J 14 CG CD CE NZ
REMARK 470 LYS J 36 CE NZ
REMARK 470 ARG J 59 CG CD NE CZ NH1 NH2
REMARK 470 GLU J 60 CD OE1 OE2
REMARK 470 ARG J 182 CD NE CZ NH1 NH2
REMARK 470 GLN J 197 CD OE1 NE2
REMARK 470 LEU J 200 CD1 CD2
REMARK 470 LEU K 4 CG CD1 CD2
REMARK 470 GLN K 9 CG CD OE1 NE2
REMARK 470 LYS K 36 CE NZ
REMARK 470 GLU K 196 CG CD OE1 OE2
REMARK 470 GLN K 197 CD OE1 NE2
REMARK 470 ARG K 208 NH1 NH2
REMARK 470 GLN L 9 CG CD OE1 NE2
REMARK 470 GLU L 10 CG CD OE1 OE2
REMARK 470 LYS L 14 CE NZ
REMARK 470 LYS L 36 CD CE NZ
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 GLU G 34 N GLY G 35 1.70
REMARK 500 O LYS C 213 O HOH C 5031 1.99
REMARK 500 OD1 ASP A 186 O HOH A 5038 2.01
REMARK 500 O HOH B 5045 O HOH B 5124 2.02
REMARK 500 NE2 GLN A 228 NH1 ARG A 231 2.05
REMARK 500 OE1 GLU L 124 O HOH L 5083 2.06
REMARK 500 OG SER A 148 O HOH A 5156 2.07
REMARK 500 O HOH B 5085 O HOH B 5148 2.11
REMARK 500 OD1 ASP J 89 O HOH J 5079 2.13
REMARK 500 O HOH E 5059 O HOH F 5059 2.16
REMARK 500 OD2 ASP B 89 O HOH B 5182 2.16
REMARK 500 NE ARG B 218 O HOH B 5180 2.17
REMARK 500 OG SER I 148 O HOH I 5112 2.17
REMARK 500 O HOH J 5109 O HOH K 5104 2.17
REMARK 500 O GLU A 10 O HOH A 5109 2.17
REMARK 500 OE2 GLU C 124 O HOH C 5032 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 5179 O HOH F 5165 1655 1.98
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 GLN B 228 CB GLN B 228 CG 0.191
REMARK 500 GLN B 228 CG GLN B 228 CD 0.139
REMARK 500 GLN D 228 CB GLN D 228 CG 0.174
REMARK 500 GLU G 34 C GLU G 34 O -0.207
REMARK 500 GLN L 228 CB GLN L 228 CG 0.179
REMARK 500 GLN L 228 CG GLN L 228 CD 0.139
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 99 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ASP A 154 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG A 231 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 231 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP A 236 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG B 99 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 99 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP B 142 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG B 208 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP C 54 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP C 91 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG C 99 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG C 99 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP C 142 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG C 231 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG C 231 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ASP D 23 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP D 89 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP D 91 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG D 99 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ASP D 142 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP D 186 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG D 231 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG D 231 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ASP E 142 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP E 250 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP F 23 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 THR F 120 CA - CB - CG2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 GLU G 34 CA - C - N ANGL. DEV. = 19.4 DEGREES
REMARK 500 GLU G 34 O - C - N ANGL. DEV. = -24.8 DEGREES
REMARK 500 GLY G 35 N - CA - C ANGL. DEV. = 17.4 DEGREES
REMARK 500 ARG G 59 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP G 180 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG G 231 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ASP H 91 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP H 142 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG H 231 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG H 231 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG I 99 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG I 99 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG I 231 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG I 231 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP J 78 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP J 89 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG J 208 NE - CZ - NH2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG J 231 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG J 231 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP K 91 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP K 142 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG K 231 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 59 ANGLE DEVIATIONS.
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 74 104.62 -165.45
REMARK 500 HIS A 145 -106.22 -100.09
REMARK 500 CYS B 74 101.22 -165.17
REMARK 500 HIS B 145 -102.55 -99.26
REMARK 500 CYS C 74 103.07 -166.56
REMARK 500 HIS C 145 -103.29 -101.05
REMARK 500 CYS D 74 103.43 -166.97
REMARK 500 HIS D 145 -104.24 -102.23
REMARK 500 CYS E 74 102.87 -163.18
REMARK 500 HIS E 145 -103.20 -98.54
REMARK 500 CYS F 74 104.98 -164.31
REMARK 500 HIS F 145 -105.22 -100.89
REMARK 500 GLU G 34 137.76 48.45
REMARK 500 CYS G 74 104.31 -166.55
REMARK 500 HIS G 145 -101.14 -101.62
REMARK 500 CYS H 74 104.58 -165.53
REMARK 500 HIS H 145 -105.42 -98.32
REMARK 500 CYS I 74 105.09 -166.33
REMARK 500 HIS I 145 -104.62 -98.20
REMARK 500 CYS J 74 104.35 -165.42
REMARK 500 HIS J 145 -104.40 -98.66
REMARK 500 CYS K 74 103.78 -165.75
REMARK 500 HIS K 145 -101.66 -100.40
REMARK 500 CYS L 74 104.83 -164.29
REMARK 500 HIS L 145 -105.47 -100.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLU G 34 26.56
REMARK 500
REMARK 500 REMARK: NULL
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 CA B2001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A5058 O
REMARK 620 2 HOH A5059 O 90.0
REMARK 620 3 HOH B5092 O 78.9 88.2
REMARK 620 4 HOH B5108 O 172.0 95.8 95.6
REMARK 620 5 HOH C5039 O 78.9 168.1 85.5 94.9
REMARK 620 6 HOH C5077 O 87.1 94.4 165.8 98.0 89.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F2002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D5090 O
REMARK 620 2 HOH E5022 O 88.6
REMARK 620 3 HOH E5074 O 164.1 94.8
REMARK 620 4 HOH E5152 O 86.5 86.4 78.2
REMARK 620 5 HOH F5112 O 93.5 97.1 101.5 176.4
REMARK 620 6 HOH F5132 O 84.9 166.1 88.3 80.9 95.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I2003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH G5045 O
REMARK 620 2 HOH G5129 O 87.0
REMARK 620 3 HOH H5116 O 94.5 92.4
REMARK 620 4 HOH I5057 O 100.1 170.5 93.4
REMARK 620 5 HOH I5066 O 95.3 79.1 166.7 93.8
REMARK 620 6 HOH I5069 O 165.5 79.5 91.4 92.8 77.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA K2004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH J5051 O
REMARK 620 2 HOH J5102 O 78.5
REMARK 620 3 HOH J5111 O 82.7 90.8
REMARK 620 4 HOH K5065 O 169.0 99.0 86.6
REMARK 620 5 HOH K5066 O 91.3 78.6 168.7 98.7
REMARK 620 6 HOH L5143 O 94.9 172.3 92.1 88.2 97.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA I 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA K 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAX A 5001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAX B 5002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAX C 5003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAX D 5004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAX E 5005
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAX F 5006
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAX G 5007
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAX H 5008
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAX I 5009
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAX J 5010
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAX K 5011
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAX L 5012
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1O8U RELATED DB: PDB
REMARK 900 6-OXO CAMPHOR HYDROLASE
REMARK 900 RELATED ID: 1DUB RELATED DB: PDB
REMARK 900 ENOYL-COA HYDRATASE
DBREF 1SZO A 1 257 UNP Q93TU6 Q93TU6_9NOCA 1 257
DBREF 1SZO B 1 257 UNP Q93TU6 Q93TU6_9NOCA 1 257
DBREF 1SZO C 1 257 UNP Q93TU6 Q93TU6_9NOCA 1 257
DBREF 1SZO D 1 257 UNP Q93TU6 Q93TU6_9NOCA 1 257
DBREF 1SZO E 1 257 UNP Q93TU6 Q93TU6_9NOCA 1 257
DBREF 1SZO F 1 257 UNP Q93TU6 Q93TU6_9NOCA 1 257
DBREF 1SZO G 1 257 UNP Q93TU6 Q93TU6_9NOCA 1 257
DBREF 1SZO H 1 257 UNP Q93TU6 Q93TU6_9NOCA 1 257
DBREF 1SZO I 1 257 UNP Q93TU6 Q93TU6_9NOCA 1 257
DBREF 1SZO J 1 257 UNP Q93TU6 Q93TU6_9NOCA 1 257
DBREF 1SZO K 1 257 UNP Q93TU6 Q93TU6_9NOCA 1 257
DBREF 1SZO L 1 257 UNP Q93TU6 Q93TU6_9NOCA 1 257
SEQADV 1SZO ALA A 122 UNP Q93TU6 HIS 122 ENGINEERED MUTATION
SEQADV 1SZO ALA B 122 UNP Q93TU6 HIS 122 ENGINEERED MUTATION
SEQADV 1SZO ALA C 122 UNP Q93TU6 HIS 122 ENGINEERED MUTATION
SEQADV 1SZO ALA D 122 UNP Q93TU6 HIS 122 ENGINEERED MUTATION
SEQADV 1SZO ALA E 122 UNP Q93TU6 HIS 122 ENGINEERED MUTATION
SEQADV 1SZO ALA F 122 UNP Q93TU6 HIS 122 ENGINEERED MUTATION
SEQADV 1SZO ALA G 122 UNP Q93TU6 HIS 122 ENGINEERED MUTATION
SEQADV 1SZO ALA H 122 UNP Q93TU6 HIS 122 ENGINEERED MUTATION
SEQADV 1SZO ALA I 122 UNP Q93TU6 HIS 122 ENGINEERED MUTATION
SEQADV 1SZO ALA J 122 UNP Q93TU6 HIS 122 ENGINEERED MUTATION
SEQADV 1SZO ALA K 122 UNP Q93TU6 HIS 122 ENGINEERED MUTATION
SEQADV 1SZO ALA L 122 UNP Q93TU6 HIS 122 ENGINEERED MUTATION
SEQRES 1 A 257 MET LYS GLN LEU ALA THR PRO PHE GLN GLU TYR SER GLN
SEQRES 2 A 257 LYS TYR GLU ASN ILE ARG LEU GLU ARG ASP GLY GLY VAL
SEQRES 3 A 257 LEU LEU VAL THR VAL HIS THR GLU GLY LYS SER LEU VAL
SEQRES 4 A 257 TRP THR SER THR ALA HIS ASP GLU LEU ALA TYR CYS PHE
SEQRES 5 A 257 HIS ASP ILE ALA CYS ASP ARG GLU ASN LYS VAL VAL ILE
SEQRES 6 A 257 LEU THR GLY THR GLY PRO SER PHE CYS ASN GLU ILE ASP
SEQRES 7 A 257 PHE THR SER PHE ASN LEU GLY THR PRO HIS ASP TRP ASP
SEQRES 8 A 257 GLU ILE ILE PHE GLU GLY GLN ARG LEU LEU ASN ASN LEU
SEQRES 9 A 257 LEU SER ILE GLU VAL PRO VAL ILE ALA ALA VAL ASN GLY
SEQRES 10 A 257 PRO VAL THR ASN ALA PRO GLU ILE PRO VAL MET SER ASP
SEQRES 11 A 257 ILE VAL LEU ALA ALA GLU SER ALA THR PHE GLN ASP GLY
SEQRES 12 A 257 PRO HIS PHE PRO SER GLY ILE VAL PRO GLY ASP GLY ALA
SEQRES 13 A 257 HIS VAL VAL TRP PRO HIS VAL LEU GLY SER ASN ARG GLY
SEQRES 14 A 257 ARG TYR PHE LEU LEU THR GLY GLN GLU LEU ASP ALA ARG
SEQRES 15 A 257 THR ALA LEU ASP TYR GLY ALA VAL ASN GLU VAL LEU SER
SEQRES 16 A 257 GLU GLN GLU LEU LEU PRO ARG ALA TRP GLU LEU ALA ARG
SEQRES 17 A 257 GLY ILE ALA GLU LYS PRO LEU LEU ALA ARG ARG TYR ALA
SEQRES 18 A 257 ARG LYS VAL LEU THR ARG GLN LEU ARG ARG VAL MET GLU
SEQRES 19 A 257 ALA ASP LEU SER LEU GLY LEU ALA HIS GLU ALA LEU ALA
SEQRES 20 A 257 ALA ILE ASP LEU GLY MET GLU SER GLU GLN
SEQRES 1 B 257 MET LYS GLN LEU ALA THR PRO PHE GLN GLU TYR SER GLN
SEQRES 2 B 257 LYS TYR GLU ASN ILE ARG LEU GLU ARG ASP GLY GLY VAL
SEQRES 3 B 257 LEU LEU VAL THR VAL HIS THR GLU GLY LYS SER LEU VAL
SEQRES 4 B 257 TRP THR SER THR ALA HIS ASP GLU LEU ALA TYR CYS PHE
SEQRES 5 B 257 HIS ASP ILE ALA CYS ASP ARG GLU ASN LYS VAL VAL ILE
SEQRES 6 B 257 LEU THR GLY THR GLY PRO SER PHE CYS ASN GLU ILE ASP
SEQRES 7 B 257 PHE THR SER PHE ASN LEU GLY THR PRO HIS ASP TRP ASP
SEQRES 8 B 257 GLU ILE ILE PHE GLU GLY GLN ARG LEU LEU ASN ASN LEU
SEQRES 9 B 257 LEU SER ILE GLU VAL PRO VAL ILE ALA ALA VAL ASN GLY
SEQRES 10 B 257 PRO VAL THR ASN ALA PRO GLU ILE PRO VAL MET SER ASP
SEQRES 11 B 257 ILE VAL LEU ALA ALA GLU SER ALA THR PHE GLN ASP GLY
SEQRES 12 B 257 PRO HIS PHE PRO SER GLY ILE VAL PRO GLY ASP GLY ALA
SEQRES 13 B 257 HIS VAL VAL TRP PRO HIS VAL LEU GLY SER ASN ARG GLY
SEQRES 14 B 257 ARG TYR PHE LEU LEU THR GLY GLN GLU LEU ASP ALA ARG
SEQRES 15 B 257 THR ALA LEU ASP TYR GLY ALA VAL ASN GLU VAL LEU SER
SEQRES 16 B 257 GLU GLN GLU LEU LEU PRO ARG ALA TRP GLU LEU ALA ARG
SEQRES 17 B 257 GLY ILE ALA GLU LYS PRO LEU LEU ALA ARG ARG TYR ALA
SEQRES 18 B 257 ARG LYS VAL LEU THR ARG GLN LEU ARG ARG VAL MET GLU
SEQRES 19 B 257 ALA ASP LEU SER LEU GLY LEU ALA HIS GLU ALA LEU ALA
SEQRES 20 B 257 ALA ILE ASP LEU GLY MET GLU SER GLU GLN
SEQRES 1 C 257 MET LYS GLN LEU ALA THR PRO PHE GLN GLU TYR SER GLN
SEQRES 2 C 257 LYS TYR GLU ASN ILE ARG LEU GLU ARG ASP GLY GLY VAL
SEQRES 3 C 257 LEU LEU VAL THR VAL HIS THR GLU GLY LYS SER LEU VAL
SEQRES 4 C 257 TRP THR SER THR ALA HIS ASP GLU LEU ALA TYR CYS PHE
SEQRES 5 C 257 HIS ASP ILE ALA CYS ASP ARG GLU ASN LYS VAL VAL ILE
SEQRES 6 C 257 LEU THR GLY THR GLY PRO SER PHE CYS ASN GLU ILE ASP
SEQRES 7 C 257 PHE THR SER PHE ASN LEU GLY THR PRO HIS ASP TRP ASP
SEQRES 8 C 257 GLU ILE ILE PHE GLU GLY GLN ARG LEU LEU ASN ASN LEU
SEQRES 9 C 257 LEU SER ILE GLU VAL PRO VAL ILE ALA ALA VAL ASN GLY
SEQRES 10 C 257 PRO VAL THR ASN ALA PRO GLU ILE PRO VAL MET SER ASP
SEQRES 11 C 257 ILE VAL LEU ALA ALA GLU SER ALA THR PHE GLN ASP GLY
SEQRES 12 C 257 PRO HIS PHE PRO SER GLY ILE VAL PRO GLY ASP GLY ALA
SEQRES 13 C 257 HIS VAL VAL TRP PRO HIS VAL LEU GLY SER ASN ARG GLY
SEQRES 14 C 257 ARG TYR PHE LEU LEU THR GLY GLN GLU LEU ASP ALA ARG
SEQRES 15 C 257 THR ALA LEU ASP TYR GLY ALA VAL ASN GLU VAL LEU SER
SEQRES 16 C 257 GLU GLN GLU LEU LEU PRO ARG ALA TRP GLU LEU ALA ARG
SEQRES 17 C 257 GLY ILE ALA GLU LYS PRO LEU LEU ALA ARG ARG TYR ALA
SEQRES 18 C 257 ARG LYS VAL LEU THR ARG GLN LEU ARG ARG VAL MET GLU
SEQRES 19 C 257 ALA ASP LEU SER LEU GLY LEU ALA HIS GLU ALA LEU ALA
SEQRES 20 C 257 ALA ILE ASP LEU GLY MET GLU SER GLU GLN
SEQRES 1 D 257 MET LYS GLN LEU ALA THR PRO PHE GLN GLU TYR SER GLN
SEQRES 2 D 257 LYS TYR GLU ASN ILE ARG LEU GLU ARG ASP GLY GLY VAL
SEQRES 3 D 257 LEU LEU VAL THR VAL HIS THR GLU GLY LYS SER LEU VAL
SEQRES 4 D 257 TRP THR SER THR ALA HIS ASP GLU LEU ALA TYR CYS PHE
SEQRES 5 D 257 HIS ASP ILE ALA CYS ASP ARG GLU ASN LYS VAL VAL ILE
SEQRES 6 D 257 LEU THR GLY THR GLY PRO SER PHE CYS ASN GLU ILE ASP
SEQRES 7 D 257 PHE THR SER PHE ASN LEU GLY THR PRO HIS ASP TRP ASP
SEQRES 8 D 257 GLU ILE ILE PHE GLU GLY GLN ARG LEU LEU ASN ASN LEU
SEQRES 9 D 257 LEU SER ILE GLU VAL PRO VAL ILE ALA ALA VAL ASN GLY
SEQRES 10 D 257 PRO VAL THR ASN ALA PRO GLU ILE PRO VAL MET SER ASP
SEQRES 11 D 257 ILE VAL LEU ALA ALA GLU SER ALA THR PHE GLN ASP GLY
SEQRES 12 D 257 PRO HIS PHE PRO SER GLY ILE VAL PRO GLY ASP GLY ALA
SEQRES 13 D 257 HIS VAL VAL TRP PRO HIS VAL LEU GLY SER ASN ARG GLY
SEQRES 14 D 257 ARG TYR PHE LEU LEU THR GLY GLN GLU LEU ASP ALA ARG
SEQRES 15 D 257 THR ALA LEU ASP TYR GLY ALA VAL ASN GLU VAL LEU SER
SEQRES 16 D 257 GLU GLN GLU LEU LEU PRO ARG ALA TRP GLU LEU ALA ARG
SEQRES 17 D 257 GLY ILE ALA GLU LYS PRO LEU LEU ALA ARG ARG TYR ALA
SEQRES 18 D 257 ARG LYS VAL LEU THR ARG GLN LEU ARG ARG VAL MET GLU
SEQRES 19 D 257 ALA ASP LEU SER LEU GLY LEU ALA HIS GLU ALA LEU ALA
SEQRES 20 D 257 ALA ILE ASP LEU GLY MET GLU SER GLU GLN
SEQRES 1 E 257 MET LYS GLN LEU ALA THR PRO PHE GLN GLU TYR SER GLN
SEQRES 2 E 257 LYS TYR GLU ASN ILE ARG LEU GLU ARG ASP GLY GLY VAL
SEQRES 3 E 257 LEU LEU VAL THR VAL HIS THR GLU GLY LYS SER LEU VAL
SEQRES 4 E 257 TRP THR SER THR ALA HIS ASP GLU LEU ALA TYR CYS PHE
SEQRES 5 E 257 HIS ASP ILE ALA CYS ASP ARG GLU ASN LYS VAL VAL ILE
SEQRES 6 E 257 LEU THR GLY THR GLY PRO SER PHE CYS ASN GLU ILE ASP
SEQRES 7 E 257 PHE THR SER PHE ASN LEU GLY THR PRO HIS ASP TRP ASP
SEQRES 8 E 257 GLU ILE ILE PHE GLU GLY GLN ARG LEU LEU ASN ASN LEU
SEQRES 9 E 257 LEU SER ILE GLU VAL PRO VAL ILE ALA ALA VAL ASN GLY
SEQRES 10 E 257 PRO VAL THR ASN ALA PRO GLU ILE PRO VAL MET SER ASP
SEQRES 11 E 257 ILE VAL LEU ALA ALA GLU SER ALA THR PHE GLN ASP GLY
SEQRES 12 E 257 PRO HIS PHE PRO SER GLY ILE VAL PRO GLY ASP GLY ALA
SEQRES 13 E 257 HIS VAL VAL TRP PRO HIS VAL LEU GLY SER ASN ARG GLY
SEQRES 14 E 257 ARG TYR PHE LEU LEU THR GLY GLN GLU LEU ASP ALA ARG
SEQRES 15 E 257 THR ALA LEU ASP TYR GLY ALA VAL ASN GLU VAL LEU SER
SEQRES 16 E 257 GLU GLN GLU LEU LEU PRO ARG ALA TRP GLU LEU ALA ARG
SEQRES 17 E 257 GLY ILE ALA GLU LYS PRO LEU LEU ALA ARG ARG TYR ALA
SEQRES 18 E 257 ARG LYS VAL LEU THR ARG GLN LEU ARG ARG VAL MET GLU
SEQRES 19 E 257 ALA ASP LEU SER LEU GLY LEU ALA HIS GLU ALA LEU ALA
SEQRES 20 E 257 ALA ILE ASP LEU GLY MET GLU SER GLU GLN
SEQRES 1 F 257 MET LYS GLN LEU ALA THR PRO PHE GLN GLU TYR SER GLN
SEQRES 2 F 257 LYS TYR GLU ASN ILE ARG LEU GLU ARG ASP GLY GLY VAL
SEQRES 3 F 257 LEU LEU VAL THR VAL HIS THR GLU GLY LYS SER LEU VAL
SEQRES 4 F 257 TRP THR SER THR ALA HIS ASP GLU LEU ALA TYR CYS PHE
SEQRES 5 F 257 HIS ASP ILE ALA CYS ASP ARG GLU ASN LYS VAL VAL ILE
SEQRES 6 F 257 LEU THR GLY THR GLY PRO SER PHE CYS ASN GLU ILE ASP
SEQRES 7 F 257 PHE THR SER PHE ASN LEU GLY THR PRO HIS ASP TRP ASP
SEQRES 8 F 257 GLU ILE ILE PHE GLU GLY GLN ARG LEU LEU ASN ASN LEU
SEQRES 9 F 257 LEU SER ILE GLU VAL PRO VAL ILE ALA ALA VAL ASN GLY
SEQRES 10 F 257 PRO VAL THR ASN ALA PRO GLU ILE PRO VAL MET SER ASP
SEQRES 11 F 257 ILE VAL LEU ALA ALA GLU SER ALA THR PHE GLN ASP GLY
SEQRES 12 F 257 PRO HIS PHE PRO SER GLY ILE VAL PRO GLY ASP GLY ALA
SEQRES 13 F 257 HIS VAL VAL TRP PRO HIS VAL LEU GLY SER ASN ARG GLY
SEQRES 14 F 257 ARG TYR PHE LEU LEU THR GLY GLN GLU LEU ASP ALA ARG
SEQRES 15 F 257 THR ALA LEU ASP TYR GLY ALA VAL ASN GLU VAL LEU SER
SEQRES 16 F 257 GLU GLN GLU LEU LEU PRO ARG ALA TRP GLU LEU ALA ARG
SEQRES 17 F 257 GLY ILE ALA GLU LYS PRO LEU LEU ALA ARG ARG TYR ALA
SEQRES 18 F 257 ARG LYS VAL LEU THR ARG GLN LEU ARG ARG VAL MET GLU
SEQRES 19 F 257 ALA ASP LEU SER LEU GLY LEU ALA HIS GLU ALA LEU ALA
SEQRES 20 F 257 ALA ILE ASP LEU GLY MET GLU SER GLU GLN
SEQRES 1 G 257 MET LYS GLN LEU ALA THR PRO PHE GLN GLU TYR SER GLN
SEQRES 2 G 257 LYS TYR GLU ASN ILE ARG LEU GLU ARG ASP GLY GLY VAL
SEQRES 3 G 257 LEU LEU VAL THR VAL HIS THR GLU GLY LYS SER LEU VAL
SEQRES 4 G 257 TRP THR SER THR ALA HIS ASP GLU LEU ALA TYR CYS PHE
SEQRES 5 G 257 HIS ASP ILE ALA CYS ASP ARG GLU ASN LYS VAL VAL ILE
SEQRES 6 G 257 LEU THR GLY THR GLY PRO SER PHE CYS ASN GLU ILE ASP
SEQRES 7 G 257 PHE THR SER PHE ASN LEU GLY THR PRO HIS ASP TRP ASP
SEQRES 8 G 257 GLU ILE ILE PHE GLU GLY GLN ARG LEU LEU ASN ASN LEU
SEQRES 9 G 257 LEU SER ILE GLU VAL PRO VAL ILE ALA ALA VAL ASN GLY
SEQRES 10 G 257 PRO VAL THR ASN ALA PRO GLU ILE PRO VAL MET SER ASP
SEQRES 11 G 257 ILE VAL LEU ALA ALA GLU SER ALA THR PHE GLN ASP GLY
SEQRES 12 G 257 PRO HIS PHE PRO SER GLY ILE VAL PRO GLY ASP GLY ALA
SEQRES 13 G 257 HIS VAL VAL TRP PRO HIS VAL LEU GLY SER ASN ARG GLY
SEQRES 14 G 257 ARG TYR PHE LEU LEU THR GLY GLN GLU LEU ASP ALA ARG
SEQRES 15 G 257 THR ALA LEU ASP TYR GLY ALA VAL ASN GLU VAL LEU SER
SEQRES 16 G 257 GLU GLN GLU LEU LEU PRO ARG ALA TRP GLU LEU ALA ARG
SEQRES 17 G 257 GLY ILE ALA GLU LYS PRO LEU LEU ALA ARG ARG TYR ALA
SEQRES 18 G 257 ARG LYS VAL LEU THR ARG GLN LEU ARG ARG VAL MET GLU
SEQRES 19 G 257 ALA ASP LEU SER LEU GLY LEU ALA HIS GLU ALA LEU ALA
SEQRES 20 G 257 ALA ILE ASP LEU GLY MET GLU SER GLU GLN
SEQRES 1 H 257 MET LYS GLN LEU ALA THR PRO PHE GLN GLU TYR SER GLN
SEQRES 2 H 257 LYS TYR GLU ASN ILE ARG LEU GLU ARG ASP GLY GLY VAL
SEQRES 3 H 257 LEU LEU VAL THR VAL HIS THR GLU GLY LYS SER LEU VAL
SEQRES 4 H 257 TRP THR SER THR ALA HIS ASP GLU LEU ALA TYR CYS PHE
SEQRES 5 H 257 HIS ASP ILE ALA CYS ASP ARG GLU ASN LYS VAL VAL ILE
SEQRES 6 H 257 LEU THR GLY THR GLY PRO SER PHE CYS ASN GLU ILE ASP
SEQRES 7 H 257 PHE THR SER PHE ASN LEU GLY THR PRO HIS ASP TRP ASP
SEQRES 8 H 257 GLU ILE ILE PHE GLU GLY GLN ARG LEU LEU ASN ASN LEU
SEQRES 9 H 257 LEU SER ILE GLU VAL PRO VAL ILE ALA ALA VAL ASN GLY
SEQRES 10 H 257 PRO VAL THR ASN ALA PRO GLU ILE PRO VAL MET SER ASP
SEQRES 11 H 257 ILE VAL LEU ALA ALA GLU SER ALA THR PHE GLN ASP GLY
SEQRES 12 H 257 PRO HIS PHE PRO SER GLY ILE VAL PRO GLY ASP GLY ALA
SEQRES 13 H 257 HIS VAL VAL TRP PRO HIS VAL LEU GLY SER ASN ARG GLY
SEQRES 14 H 257 ARG TYR PHE LEU LEU THR GLY GLN GLU LEU ASP ALA ARG
SEQRES 15 H 257 THR ALA LEU ASP TYR GLY ALA VAL ASN GLU VAL LEU SER
SEQRES 16 H 257 GLU GLN GLU LEU LEU PRO ARG ALA TRP GLU LEU ALA ARG
SEQRES 17 H 257 GLY ILE ALA GLU LYS PRO LEU LEU ALA ARG ARG TYR ALA
SEQRES 18 H 257 ARG LYS VAL LEU THR ARG GLN LEU ARG ARG VAL MET GLU
SEQRES 19 H 257 ALA ASP LEU SER LEU GLY LEU ALA HIS GLU ALA LEU ALA
SEQRES 20 H 257 ALA ILE ASP LEU GLY MET GLU SER GLU GLN
SEQRES 1 I 257 MET LYS GLN LEU ALA THR PRO PHE GLN GLU TYR SER GLN
SEQRES 2 I 257 LYS TYR GLU ASN ILE ARG LEU GLU ARG ASP GLY GLY VAL
SEQRES 3 I 257 LEU LEU VAL THR VAL HIS THR GLU GLY LYS SER LEU VAL
SEQRES 4 I 257 TRP THR SER THR ALA HIS ASP GLU LEU ALA TYR CYS PHE
SEQRES 5 I 257 HIS ASP ILE ALA CYS ASP ARG GLU ASN LYS VAL VAL ILE
SEQRES 6 I 257 LEU THR GLY THR GLY PRO SER PHE CYS ASN GLU ILE ASP
SEQRES 7 I 257 PHE THR SER PHE ASN LEU GLY THR PRO HIS ASP TRP ASP
SEQRES 8 I 257 GLU ILE ILE PHE GLU GLY GLN ARG LEU LEU ASN ASN LEU
SEQRES 9 I 257 LEU SER ILE GLU VAL PRO VAL ILE ALA ALA VAL ASN GLY
SEQRES 10 I 257 PRO VAL THR ASN ALA PRO GLU ILE PRO VAL MET SER ASP
SEQRES 11 I 257 ILE VAL LEU ALA ALA GLU SER ALA THR PHE GLN ASP GLY
SEQRES 12 I 257 PRO HIS PHE PRO SER GLY ILE VAL PRO GLY ASP GLY ALA
SEQRES 13 I 257 HIS VAL VAL TRP PRO HIS VAL LEU GLY SER ASN ARG GLY
SEQRES 14 I 257 ARG TYR PHE LEU LEU THR GLY GLN GLU LEU ASP ALA ARG
SEQRES 15 I 257 THR ALA LEU ASP TYR GLY ALA VAL ASN GLU VAL LEU SER
SEQRES 16 I 257 GLU GLN GLU LEU LEU PRO ARG ALA TRP GLU LEU ALA ARG
SEQRES 17 I 257 GLY ILE ALA GLU LYS PRO LEU LEU ALA ARG ARG TYR ALA
SEQRES 18 I 257 ARG LYS VAL LEU THR ARG GLN LEU ARG ARG VAL MET GLU
SEQRES 19 I 257 ALA ASP LEU SER LEU GLY LEU ALA HIS GLU ALA LEU ALA
SEQRES 20 I 257 ALA ILE ASP LEU GLY MET GLU SER GLU GLN
SEQRES 1 J 257 MET LYS GLN LEU ALA THR PRO PHE GLN GLU TYR SER GLN
SEQRES 2 J 257 LYS TYR GLU ASN ILE ARG LEU GLU ARG ASP GLY GLY VAL
SEQRES 3 J 257 LEU LEU VAL THR VAL HIS THR GLU GLY LYS SER LEU VAL
SEQRES 4 J 257 TRP THR SER THR ALA HIS ASP GLU LEU ALA TYR CYS PHE
SEQRES 5 J 257 HIS ASP ILE ALA CYS ASP ARG GLU ASN LYS VAL VAL ILE
SEQRES 6 J 257 LEU THR GLY THR GLY PRO SER PHE CYS ASN GLU ILE ASP
SEQRES 7 J 257 PHE THR SER PHE ASN LEU GLY THR PRO HIS ASP TRP ASP
SEQRES 8 J 257 GLU ILE ILE PHE GLU GLY GLN ARG LEU LEU ASN ASN LEU
SEQRES 9 J 257 LEU SER ILE GLU VAL PRO VAL ILE ALA ALA VAL ASN GLY
SEQRES 10 J 257 PRO VAL THR ASN ALA PRO GLU ILE PRO VAL MET SER ASP
SEQRES 11 J 257 ILE VAL LEU ALA ALA GLU SER ALA THR PHE GLN ASP GLY
SEQRES 12 J 257 PRO HIS PHE PRO SER GLY ILE VAL PRO GLY ASP GLY ALA
SEQRES 13 J 257 HIS VAL VAL TRP PRO HIS VAL LEU GLY SER ASN ARG GLY
SEQRES 14 J 257 ARG TYR PHE LEU LEU THR GLY GLN GLU LEU ASP ALA ARG
SEQRES 15 J 257 THR ALA LEU ASP TYR GLY ALA VAL ASN GLU VAL LEU SER
SEQRES 16 J 257 GLU GLN GLU LEU LEU PRO ARG ALA TRP GLU LEU ALA ARG
SEQRES 17 J 257 GLY ILE ALA GLU LYS PRO LEU LEU ALA ARG ARG TYR ALA
SEQRES 18 J 257 ARG LYS VAL LEU THR ARG GLN LEU ARG ARG VAL MET GLU
SEQRES 19 J 257 ALA ASP LEU SER LEU GLY LEU ALA HIS GLU ALA LEU ALA
SEQRES 20 J 257 ALA ILE ASP LEU GLY MET GLU SER GLU GLN
SEQRES 1 K 257 MET LYS GLN LEU ALA THR PRO PHE GLN GLU TYR SER GLN
SEQRES 2 K 257 LYS TYR GLU ASN ILE ARG LEU GLU ARG ASP GLY GLY VAL
SEQRES 3 K 257 LEU LEU VAL THR VAL HIS THR GLU GLY LYS SER LEU VAL
SEQRES 4 K 257 TRP THR SER THR ALA HIS ASP GLU LEU ALA TYR CYS PHE
SEQRES 5 K 257 HIS ASP ILE ALA CYS ASP ARG GLU ASN LYS VAL VAL ILE
SEQRES 6 K 257 LEU THR GLY THR GLY PRO SER PHE CYS ASN GLU ILE ASP
SEQRES 7 K 257 PHE THR SER PHE ASN LEU GLY THR PRO HIS ASP TRP ASP
SEQRES 8 K 257 GLU ILE ILE PHE GLU GLY GLN ARG LEU LEU ASN ASN LEU
SEQRES 9 K 257 LEU SER ILE GLU VAL PRO VAL ILE ALA ALA VAL ASN GLY
SEQRES 10 K 257 PRO VAL THR ASN ALA PRO GLU ILE PRO VAL MET SER ASP
SEQRES 11 K 257 ILE VAL LEU ALA ALA GLU SER ALA THR PHE GLN ASP GLY
SEQRES 12 K 257 PRO HIS PHE PRO SER GLY ILE VAL PRO GLY ASP GLY ALA
SEQRES 13 K 257 HIS VAL VAL TRP PRO HIS VAL LEU GLY SER ASN ARG GLY
SEQRES 14 K 257 ARG TYR PHE LEU LEU THR GLY GLN GLU LEU ASP ALA ARG
SEQRES 15 K 257 THR ALA LEU ASP TYR GLY ALA VAL ASN GLU VAL LEU SER
SEQRES 16 K 257 GLU GLN GLU LEU LEU PRO ARG ALA TRP GLU LEU ALA ARG
SEQRES 17 K 257 GLY ILE ALA GLU LYS PRO LEU LEU ALA ARG ARG TYR ALA
SEQRES 18 K 257 ARG LYS VAL LEU THR ARG GLN LEU ARG ARG VAL MET GLU
SEQRES 19 K 257 ALA ASP LEU SER LEU GLY LEU ALA HIS GLU ALA LEU ALA
SEQRES 20 K 257 ALA ILE ASP LEU GLY MET GLU SER GLU GLN
SEQRES 1 L 257 MET LYS GLN LEU ALA THR PRO PHE GLN GLU TYR SER GLN
SEQRES 2 L 257 LYS TYR GLU ASN ILE ARG LEU GLU ARG ASP GLY GLY VAL
SEQRES 3 L 257 LEU LEU VAL THR VAL HIS THR GLU GLY LYS SER LEU VAL
SEQRES 4 L 257 TRP THR SER THR ALA HIS ASP GLU LEU ALA TYR CYS PHE
SEQRES 5 L 257 HIS ASP ILE ALA CYS ASP ARG GLU ASN LYS VAL VAL ILE
SEQRES 6 L 257 LEU THR GLY THR GLY PRO SER PHE CYS ASN GLU ILE ASP
SEQRES 7 L 257 PHE THR SER PHE ASN LEU GLY THR PRO HIS ASP TRP ASP
SEQRES 8 L 257 GLU ILE ILE PHE GLU GLY GLN ARG LEU LEU ASN ASN LEU
SEQRES 9 L 257 LEU SER ILE GLU VAL PRO VAL ILE ALA ALA VAL ASN GLY
SEQRES 10 L 257 PRO VAL THR ASN ALA PRO GLU ILE PRO VAL MET SER ASP
SEQRES 11 L 257 ILE VAL LEU ALA ALA GLU SER ALA THR PHE GLN ASP GLY
SEQRES 12 L 257 PRO HIS PHE PRO SER GLY ILE VAL PRO GLY ASP GLY ALA
SEQRES 13 L 257 HIS VAL VAL TRP PRO HIS VAL LEU GLY SER ASN ARG GLY
SEQRES 14 L 257 ARG TYR PHE LEU LEU THR GLY GLN GLU LEU ASP ALA ARG
SEQRES 15 L 257 THR ALA LEU ASP TYR GLY ALA VAL ASN GLU VAL LEU SER
SEQRES 16 L 257 GLU GLN GLU LEU LEU PRO ARG ALA TRP GLU LEU ALA ARG
SEQRES 17 L 257 GLY ILE ALA GLU LYS PRO LEU LEU ALA ARG ARG TYR ALA
SEQRES 18 L 257 ARG LYS VAL LEU THR ARG GLN LEU ARG ARG VAL MET GLU
SEQRES 19 L 257 ALA ASP LEU SER LEU GLY LEU ALA HIS GLU ALA LEU ALA
SEQRES 20 L 257 ALA ILE ASP LEU GLY MET GLU SER GLU GLN
HET CAX A5001 13
HET CA B2001 1
HET CAX B5002 13
HET CAX C5003 13
HET CAX D5004 13
HET CAX E5005 13
HET CA F2002 1
HET CAX F5006 13
HET CAX G5007 13
HET CAX H5008 13
HET CA I2003 1
HET CAX I5009 13
HET CAX J5010 13
HET CA K2004 1
HET CAX K5011 13
HET CAX L5012 13
HETNAM CAX (2S,4S)-4-(2,2-DIHYDROXYETHYL)-2,3,3-
HETNAM 2 CAX TRIMETHYLCYCLOPENTANONE
HETNAM CA CALCIUM ION
HETSYN CAX (2S,4S)-ALPHA-CAMPHOLINIC ACID
FORMUL 13 CAX 12(C10 H18 O3)
FORMUL 14 CA 4(CA 2+)
FORMUL 29 HOH *1929(H2 O)
HELIX 1 1 PRO A 7 SER A 12 1 6
HELIX 2 2 THR A 41 ASP A 58 1 18
HELIX 3 3 PHE A 79 PHE A 82 5 4
HELIX 4 4 THR A 86 ILE A 107 1 22
HELIX 5 5 PRO A 123 MET A 128 1 6
HELIX 6 6 HIS A 145 GLY A 149 5 5
HELIX 7 7 GLY A 155 GLY A 165 1 11
HELIX 8 8 GLY A 165 THR A 175 1 11
HELIX 9 9 ALA A 181 TYR A 187 1 7
HELIX 10 10 SER A 195 GLU A 212 1 18
HELIX 11 11 PRO A 214 THR A 226 1 13
HELIX 12 12 THR A 226 GLY A 252 1 27
HELIX 13 13 PRO B 7 SER B 12 1 6
HELIX 14 14 THR B 41 ASP B 58 1 18
HELIX 15 15 PHE B 79 PHE B 82 5 4
HELIX 16 16 THR B 86 ILE B 107 1 22
HELIX 17 17 PRO B 123 MET B 128 1 6
HELIX 18 18 HIS B 145 GLY B 149 5 5
HELIX 19 19 GLY B 155 GLY B 165 1 11
HELIX 20 20 GLY B 165 THR B 175 1 11
HELIX 21 21 ALA B 181 TYR B 187 1 7
HELIX 22 22 SER B 195 GLU B 212 1 18
HELIX 23 23 PRO B 214 THR B 226 1 13
HELIX 24 24 THR B 226 LEU B 251 1 26
HELIX 25 25 PRO C 7 SER C 12 1 6
HELIX 26 26 THR C 41 ASP C 58 1 18
HELIX 27 27 PHE C 79 PHE C 82 5 4
HELIX 28 28 THR C 86 ILE C 107 1 22
HELIX 29 29 PRO C 123 MET C 128 1 6
HELIX 30 30 HIS C 145 GLY C 149 5 5
HELIX 31 31 GLY C 155 GLY C 165 1 11
HELIX 32 32 GLY C 165 THR C 175 1 11
HELIX 33 33 ALA C 181 TYR C 187 1 7
HELIX 34 34 SER C 195 GLU C 212 1 18
HELIX 35 35 PRO C 214 THR C 226 1 13
HELIX 36 36 THR C 226 LEU C 251 1 26
HELIX 37 37 PRO D 7 SER D 12 1 6
HELIX 38 38 THR D 41 ASP D 58 1 18
HELIX 39 39 PHE D 79 PHE D 82 5 4
HELIX 40 40 THR D 86 SER D 106 1 21
HELIX 41 41 PRO D 123 MET D 128 1 6
HELIX 42 42 HIS D 145 GLY D 149 5 5
HELIX 43 43 GLY D 155 GLY D 165 1 11
HELIX 44 44 GLY D 165 THR D 175 1 11
HELIX 45 45 ALA D 181 TYR D 187 1 7
HELIX 46 46 SER D 195 GLU D 212 1 18
HELIX 47 47 PRO D 214 THR D 226 1 13
HELIX 48 48 THR D 226 GLY D 252 1 27
HELIX 49 49 PRO E 7 SER E 12 1 6
HELIX 50 50 THR E 41 ASP E 58 1 18
HELIX 51 51 PHE E 79 PHE E 82 5 4
HELIX 52 52 THR E 86 ILE E 107 1 22
HELIX 53 53 PRO E 123 MET E 128 1 6
HELIX 54 54 HIS E 145 GLY E 149 5 5
HELIX 55 55 GLY E 155 GLY E 165 1 11
HELIX 56 56 GLY E 165 THR E 175 1 11
HELIX 57 57 ALA E 181 TYR E 187 1 7
HELIX 58 58 SER E 195 GLU E 212 1 18
HELIX 59 59 PRO E 214 THR E 226 1 13
HELIX 60 60 THR E 226 LEU E 251 1 26
HELIX 61 61 PRO F 7 SER F 12 1 6
HELIX 62 62 THR F 41 ASP F 58 1 18
HELIX 63 63 PHE F 79 PHE F 82 5 4
HELIX 64 64 THR F 86 ILE F 107 1 22
HELIX 65 65 PRO F 123 MET F 128 1 6
HELIX 66 66 HIS F 145 GLY F 149 5 5
HELIX 67 67 GLY F 155 GLY F 165 1 11
HELIX 68 68 GLY F 165 THR F 175 1 11
HELIX 69 69 ALA F 181 TYR F 187 1 7
HELIX 70 70 GLU F 198 GLU F 212 1 15
HELIX 71 71 PRO F 214 THR F 226 1 13
HELIX 72 72 THR F 226 GLY F 252 1 27
HELIX 73 73 PRO G 7 SER G 12 1 6
HELIX 74 74 THR G 41 ASP G 58 1 18
HELIX 75 75 PHE G 79 PHE G 82 5 4
HELIX 76 76 THR G 86 ILE G 107 1 22
HELIX 77 77 PRO G 123 MET G 128 1 6
HELIX 78 78 HIS G 145 GLY G 149 5 5
HELIX 79 79 GLY G 155 GLY G 165 1 11
HELIX 80 80 GLY G 165 THR G 175 1 11
HELIX 81 81 ALA G 181 TYR G 187 1 7
HELIX 82 82 GLU G 198 GLU G 212 1 15
HELIX 83 83 PRO G 214 THR G 226 1 13
HELIX 84 84 THR G 226 GLY G 252 1 27
HELIX 85 85 PRO H 7 SER H 12 1 6
HELIX 86 86 THR H 41 ASP H 58 1 18
HELIX 87 87 PHE H 79 PHE H 82 5 4
HELIX 88 88 THR H 86 ILE H 107 1 22
HELIX 89 89 PRO H 123 MET H 128 1 6
HELIX 90 90 HIS H 145 GLY H 149 5 5
HELIX 91 91 GLY H 155 GLY H 165 1 11
HELIX 92 92 GLY H 165 THR H 175 1 11
HELIX 93 93 ALA H 181 TYR H 187 1 7
HELIX 94 94 GLU H 198 GLU H 212 1 15
HELIX 95 95 PRO H 214 THR H 226 1 13
HELIX 96 96 THR H 226 LEU H 251 1 26
HELIX 97 97 PRO I 7 SER I 12 1 6
HELIX 98 98 THR I 41 ASP I 58 1 18
HELIX 99 99 PHE I 79 PHE I 82 5 4
HELIX 100 100 THR I 86 ILE I 107 1 22
HELIX 101 101 PRO I 123 MET I 128 1 6
HELIX 102 102 HIS I 145 GLY I 149 5 5
HELIX 103 103 GLY I 155 GLY I 165 1 11
HELIX 104 104 GLY I 165 THR I 175 1 11
HELIX 105 105 ALA I 181 TYR I 187 1 7
HELIX 106 106 SER I 195 GLU I 212 1 18
HELIX 107 107 PRO I 214 THR I 226 1 13
HELIX 108 108 THR I 226 GLY I 252 1 27
HELIX 109 109 PRO J 7 SER J 12 1 6
HELIX 110 110 THR J 41 ASP J 58 1 18
HELIX 111 111 PHE J 79 PHE J 82 5 4
HELIX 112 112 THR J 86 ILE J 107 1 22
HELIX 113 113 PRO J 123 MET J 128 1 6
HELIX 114 114 HIS J 145 GLY J 149 5 5
HELIX 115 115 GLY J 155 GLY J 165 1 11
HELIX 116 116 GLY J 165 THR J 175 1 11
HELIX 117 117 ALA J 181 TYR J 187 1 7
HELIX 118 118 GLU J 198 GLU J 212 1 15
HELIX 119 119 PRO J 214 THR J 226 1 13
HELIX 120 120 THR J 226 GLY J 252 1 27
HELIX 121 121 PRO K 7 SER K 12 1 6
HELIX 122 122 THR K 41 ASP K 58 1 18
HELIX 123 123 PHE K 79 PHE K 82 5 4
HELIX 124 124 THR K 86 ILE K 107 1 22
HELIX 125 125 PRO K 123 MET K 128 1 6
HELIX 126 126 HIS K 145 GLY K 149 5 5
HELIX 127 127 GLY K 155 GLY K 165 1 11
HELIX 128 128 GLY K 165 THR K 175 1 11
HELIX 129 129 ALA K 181 TYR K 187 1 7
HELIX 130 130 SER K 195 GLU K 212 1 18
HELIX 131 131 PRO K 214 THR K 226 1 13
HELIX 132 132 THR K 226 GLY K 252 1 27
HELIX 133 133 PRO L 7 SER L 12 1 6
HELIX 134 134 THR L 41 ASP L 58 1 18
HELIX 135 135 PHE L 79 PHE L 82 5 4
HELIX 136 136 THR L 86 ILE L 107 1 22
HELIX 137 137 PRO L 123 MET L 128 1 6
HELIX 138 138 HIS L 145 GLY L 149 5 5
HELIX 139 139 GLY L 155 GLY L 165 1 11
HELIX 140 140 GLY L 165 THR L 175 1 11
HELIX 141 141 ALA L 181 TYR L 187 1 7
HELIX 142 142 SER L 195 GLU L 212 1 18
HELIX 143 143 PRO L 214 THR L 226 1 13
HELIX 144 144 THR L 226 GLY L 252 1 27
SHEET 1 A 6 ILE A 18 ASP A 23 0
SHEET 2 A 6 VAL A 26 VAL A 31 -1 O LEU A 28 N GLU A 21
SHEET 3 A 6 VAL A 63 THR A 67 1 O ILE A 65 N VAL A 29
SHEET 4 A 6 VAL A 111 VAL A 115 1 O ILE A 112 N VAL A 64
SHEET 5 A 6 ILE A 131 ALA A 135 1 O LEU A 133 N VAL A 115
SHEET 6 A 6 GLU A 192 LEU A 194 1 O LEU A 194 N ALA A 134
SHEET 1 B 2 VAL A 39 TRP A 40 0
SHEET 2 B 2 GLU A 76 ILE A 77 1 O GLU A 76 N TRP A 40
SHEET 1 C 2 THR A 139 GLN A 141 0
SHEET 2 C 2 GLU A 178 ASP A 180 -1 O LEU A 179 N PHE A 140
SHEET 1 D 6 ILE B 18 ASP B 23 0
SHEET 2 D 6 VAL B 26 VAL B 31 -1 O LEU B 28 N GLU B 21
SHEET 3 D 6 VAL B 63 THR B 67 1 O ILE B 65 N VAL B 29
SHEET 4 D 6 VAL B 111 VAL B 115 1 O ALA B 114 N LEU B 66
SHEET 5 D 6 ILE B 131 ALA B 135 1 O LEU B 133 N VAL B 115
SHEET 6 D 6 GLU B 192 LEU B 194 1 O GLU B 192 N ALA B 134
SHEET 1 E 2 VAL B 39 TRP B 40 0
SHEET 2 E 2 GLU B 76 ILE B 77 1 O GLU B 76 N TRP B 40
SHEET 1 F 2 THR B 139 PHE B 140 0
SHEET 2 F 2 LEU B 179 ASP B 180 -1 O LEU B 179 N PHE B 140
SHEET 1 G 6 ILE C 18 ASP C 23 0
SHEET 2 G 6 VAL C 26 VAL C 31 -1 O LEU C 28 N GLU C 21
SHEET 3 G 6 VAL C 63 THR C 67 1 O ILE C 65 N VAL C 29
SHEET 4 G 6 VAL C 111 VAL C 115 1 O ILE C 112 N VAL C 64
SHEET 5 G 6 ILE C 131 ALA C 135 1 O LEU C 133 N VAL C 115
SHEET 6 G 6 GLU C 192 LEU C 194 1 O GLU C 192 N ALA C 134
SHEET 1 H 2 VAL C 39 TRP C 40 0
SHEET 2 H 2 GLU C 76 ILE C 77 1 O GLU C 76 N TRP C 40
SHEET 1 I 2 THR C 139 GLN C 141 0
SHEET 2 I 2 GLU C 178 ASP C 180 -1 O LEU C 179 N PHE C 140
SHEET 1 J 6 ILE D 18 ASP D 23 0
SHEET 2 J 6 VAL D 26 VAL D 31 -1 O LEU D 28 N GLU D 21
SHEET 3 J 6 VAL D 63 THR D 67 1 O ILE D 65 N VAL D 29
SHEET 4 J 6 VAL D 111 VAL D 115 1 O ILE D 112 N VAL D 64
SHEET 5 J 6 ILE D 131 ALA D 135 1 O LEU D 133 N VAL D 115
SHEET 6 J 6 GLU D 192 LEU D 194 1 O LEU D 194 N ALA D 134
SHEET 1 K 2 VAL D 39 TRP D 40 0
SHEET 2 K 2 GLU D 76 ILE D 77 1 O GLU D 76 N TRP D 40
SHEET 1 L 2 THR D 139 PHE D 140 0
SHEET 2 L 2 LEU D 179 ASP D 180 -1 O LEU D 179 N PHE D 140
SHEET 1 M 6 ILE E 18 ASP E 23 0
SHEET 2 M 6 VAL E 26 VAL E 31 -1 O LEU E 28 N GLU E 21
SHEET 3 M 6 VAL E 63 THR E 67 1 O ILE E 65 N VAL E 29
SHEET 4 M 6 VAL E 111 VAL E 115 1 O ILE E 112 N VAL E 64
SHEET 5 M 6 ILE E 131 ALA E 135 1 O LEU E 133 N VAL E 115
SHEET 6 M 6 GLU E 192 LEU E 194 1 O GLU E 192 N ALA E 134
SHEET 1 N 2 VAL E 39 TRP E 40 0
SHEET 2 N 2 GLU E 76 ILE E 77 1 O GLU E 76 N TRP E 40
SHEET 1 O 2 THR E 139 PHE E 140 0
SHEET 2 O 2 LEU E 179 ASP E 180 -1 O LEU E 179 N PHE E 140
SHEET 1 P 6 ILE F 18 ASP F 23 0
SHEET 2 P 6 VAL F 26 VAL F 31 -1 O LEU F 28 N GLU F 21
SHEET 3 P 6 VAL F 63 THR F 67 1 O ILE F 65 N VAL F 29
SHEET 4 P 6 VAL F 111 VAL F 115 1 O ALA F 114 N LEU F 66
SHEET 5 P 6 ILE F 131 ALA F 135 1 O LEU F 133 N VAL F 115
SHEET 6 P 6 GLU F 192 LEU F 194 1 O LEU F 194 N ALA F 134
SHEET 1 Q 2 VAL F 39 TRP F 40 0
SHEET 2 Q 2 GLU F 76 ILE F 77 1 O GLU F 76 N TRP F 40
SHEET 1 R 2 THR F 139 PHE F 140 0
SHEET 2 R 2 LEU F 179 ASP F 180 -1 O LEU F 179 N PHE F 140
SHEET 1 S 6 ILE G 18 ASP G 23 0
SHEET 2 S 6 VAL G 26 VAL G 31 -1 O LEU G 28 N GLU G 21
SHEET 3 S 6 VAL G 63 THR G 67 1 O ILE G 65 N VAL G 29
SHEET 4 S 6 VAL G 111 VAL G 115 1 O ILE G 112 N VAL G 64
SHEET 5 S 6 ILE G 131 ALA G 135 1 O LEU G 133 N VAL G 115
SHEET 6 S 6 GLU G 192 LEU G 194 1 O LEU G 194 N ALA G 134
SHEET 1 T 2 VAL G 39 TRP G 40 0
SHEET 2 T 2 GLU G 76 ILE G 77 1 O GLU G 76 N TRP G 40
SHEET 1 U 2 THR G 139 PHE G 140 0
SHEET 2 U 2 LEU G 179 ASP G 180 -1 O LEU G 179 N PHE G 140
SHEET 1 V 6 ILE H 18 ASP H 23 0
SHEET 2 V 6 VAL H 26 VAL H 31 -1 O LEU H 28 N GLU H 21
SHEET 3 V 6 VAL H 63 THR H 67 1 O ILE H 65 N VAL H 29
SHEET 4 V 6 VAL H 111 VAL H 115 1 O ILE H 112 N LEU H 66
SHEET 5 V 6 ILE H 131 ALA H 135 1 O LEU H 133 N VAL H 115
SHEET 6 V 6 GLU H 192 LEU H 194 1 O LEU H 194 N ALA H 134
SHEET 1 W 2 VAL H 39 TRP H 40 0
SHEET 2 W 2 GLU H 76 ILE H 77 1 O GLU H 76 N TRP H 40
SHEET 1 X 2 THR H 139 PHE H 140 0
SHEET 2 X 2 LEU H 179 ASP H 180 -1 O LEU H 179 N PHE H 140
SHEET 1 Y 6 ILE I 18 ASP I 23 0
SHEET 2 Y 6 VAL I 26 VAL I 31 -1 O LEU I 28 N GLU I 21
SHEET 3 Y 6 VAL I 63 THR I 67 1 O ILE I 65 N VAL I 29
SHEET 4 Y 6 VAL I 111 VAL I 115 1 O ILE I 112 N VAL I 64
SHEET 5 Y 6 ILE I 131 ALA I 135 1 O ILE I 131 N ALA I 113
SHEET 6 Y 6 GLU I 192 LEU I 194 1 O LEU I 194 N ALA I 134
SHEET 1 Z 2 VAL I 39 TRP I 40 0
SHEET 2 Z 2 GLU I 76 ILE I 77 1 O GLU I 76 N TRP I 40
SHEET 1 AA 2 THR I 139 PHE I 140 0
SHEET 2 AA 2 LEU I 179 ASP I 180 -1 O LEU I 179 N PHE I 140
SHEET 1 AB 6 ILE J 18 ASP J 23 0
SHEET 2 AB 6 VAL J 26 VAL J 31 -1 O LEU J 28 N GLU J 21
SHEET 3 AB 6 VAL J 63 THR J 67 1 O ILE J 65 N VAL J 29
SHEET 4 AB 6 VAL J 111 VAL J 115 1 O ILE J 112 N VAL J 64
SHEET 5 AB 6 ILE J 131 ALA J 135 1 O LEU J 133 N ALA J 113
SHEET 6 AB 6 GLU J 192 LEU J 194 1 O LEU J 194 N ALA J 134
SHEET 1 AC 2 VAL J 39 TRP J 40 0
SHEET 2 AC 2 GLU J 76 ILE J 77 1 O GLU J 76 N TRP J 40
SHEET 1 AD 2 THR J 139 GLN J 141 0
SHEET 2 AD 2 GLU J 178 ASP J 180 -1 O LEU J 179 N PHE J 140
SHEET 1 AE 6 ILE K 18 ASP K 23 0
SHEET 2 AE 6 VAL K 26 VAL K 31 -1 O LEU K 28 N GLU K 21
SHEET 3 AE 6 VAL K 63 THR K 67 1 O ILE K 65 N VAL K 29
SHEET 4 AE 6 VAL K 111 VAL K 115 1 O ILE K 112 N LEU K 66
SHEET 5 AE 6 ILE K 131 ALA K 135 1 O LEU K 133 N VAL K 115
SHEET 6 AE 6 GLU K 192 LEU K 194 1 O LEU K 194 N ALA K 134
SHEET 1 AF 2 VAL K 39 TRP K 40 0
SHEET 2 AF 2 GLU K 76 ILE K 77 1 O GLU K 76 N TRP K 40
SHEET 1 AG 2 THR K 139 GLN K 141 0
SHEET 2 AG 2 GLU K 178 ASP K 180 -1 O LEU K 179 N PHE K 140
SHEET 1 AH 6 ILE L 18 ASP L 23 0
SHEET 2 AH 6 VAL L 26 VAL L 31 -1 O LEU L 28 N GLU L 21
SHEET 3 AH 6 VAL L 63 THR L 67 1 O ILE L 65 N VAL L 29
SHEET 4 AH 6 VAL L 111 VAL L 115 1 O ILE L 112 N VAL L 64
SHEET 5 AH 6 ILE L 131 ALA L 135 1 O LEU L 133 N VAL L 115
SHEET 6 AH 6 GLU L 192 LEU L 194 1 O LEU L 194 N ALA L 134
SHEET 1 AI 2 VAL L 39 TRP L 40 0
SHEET 2 AI 2 GLU L 76 ILE L 77 1 O GLU L 76 N TRP L 40
SHEET 1 AJ 2 THR L 139 GLN L 141 0
SHEET 2 AJ 2 GLU L 178 ASP L 180 -1 O LEU L 179 N PHE L 140
LINK O HOH A5058 CA CA B2001 1555 1555 2.39
LINK O HOH A5059 CA CA B2001 1555 1555 2.14
LINK CA CA B2001 O HOH B5092 1555 1555 2.44
LINK CA CA B2001 O HOH B5108 1555 1555 2.07
LINK CA CA B2001 O HOH C5039 1555 1555 2.62
LINK CA CA B2001 O HOH C5077 1555 1555 2.07
LINK O HOH D5090 CA CA F2002 1555 1555 2.49
LINK O HOH E5022 CA CA F2002 1555 1555 2.11
LINK O HOH E5074 CA CA F2002 1555 1555 2.83
LINK O HOH E5152 CA CA F2002 1555 1555 2.75
LINK CA CA F2002 O HOH F5112 1555 1555 2.15
LINK CA CA F2002 O HOH F5132 1555 1555 2.46
LINK O HOH G5045 CA CA I2003 1555 1555 2.10
LINK O HOH G5129 CA CA I2003 1555 1555 2.66
LINK O HOH H5116 CA CA I2003 1555 1555 2.19
LINK CA CA I2003 O HOH I5057 1555 1555 2.15
LINK CA CA I2003 O HOH I5066 1555 1555 2.62
LINK CA CA I2003 O HOH I5069 1555 1555 2.73
LINK O HOH J5051 CA CA K2004 1555 1555 2.26
LINK O HOH J5102 CA CA K2004 1555 1555 2.62
LINK O HOH J5111 CA CA K2004 1555 1555 2.21
LINK CA CA K2004 O HOH K5065 1555 1555 2.07
LINK CA CA K2004 O HOH K5066 1555 1555 3.04
LINK CA CA K2004 O HOH L5143 1555 1555 2.23
SITE 1 AC1 7 HOH A5058 HOH A5059 ASP B 186 HOH B5092
SITE 2 AC1 7 HOH B5108 HOH C5039 HOH C5077
SITE 1 AC2 7 HOH D5090 HOH E5022 HOH E5074 HOH E5152
SITE 2 AC2 7 ASP F 186 HOH F5112 HOH F5132
SITE 1 AC3 6 HOH G5045 HOH G5129 HOH H5116 HOH I5057
SITE 2 AC3 6 HOH I5066 HOH I5069
SITE 1 AC4 6 HOH J5051 HOH J5102 HOH J5111 HOH K5065
SITE 2 AC4 6 HOH K5066 HOH L5143
SITE 1 AC5 9 TRP A 40 HIS A 45 ILE A 77 PHE A 82
SITE 2 AC5 9 ILE A 93 HIS A 145 ASP A 154 GLU A 244
SITE 3 AC5 9 HOH A5007
SITE 1 AC6 8 TRP B 40 HIS B 45 ILE B 77 PHE B 82
SITE 2 AC6 8 HIS B 145 ASP B 154 GLU B 244 HOH B5032
SITE 1 AC7 9 TRP C 40 HIS C 45 ILE C 77 PHE C 82
SITE 2 AC7 9 ILE C 93 HIS C 145 ASP C 154 GLU C 244
SITE 3 AC7 9 HOH C5034
SITE 1 AC8 9 TRP D 40 HIS D 45 ILE D 77 PHE D 82
SITE 2 AC8 9 ILE D 93 HIS D 145 ASP D 154 GLU D 244
SITE 3 AC8 9 HOH D5021
SITE 1 AC9 9 TRP E 40 HIS E 45 ILE E 77 PHE E 82
SITE 2 AC9 9 ILE E 93 HIS E 145 ASP E 154 GLU E 244
SITE 3 AC9 9 HOH E5036
SITE 1 BC1 10 TRP F 40 HIS F 45 ILE F 77 PHE F 82
SITE 2 BC1 10 ILE F 93 HIS F 145 ASP F 154 GLU F 244
SITE 3 BC1 10 HOH F5034 HOH F5087
SITE 1 BC2 9 TRP G 40 HIS G 45 ILE G 77 PHE G 82
SITE 2 BC2 9 ILE G 93 HIS G 145 ASP G 154 GLU G 244
SITE 3 BC2 9 HOH G5052
SITE 1 BC3 10 TRP H 40 HIS H 45 ILE H 77 PHE H 82
SITE 2 BC3 10 ILE H 93 HIS H 145 ASP H 154 GLU H 244
SITE 3 BC3 10 HOH H5026 HOH H5035
SITE 1 BC4 9 TRP I 40 HIS I 45 ILE I 77 PHE I 82
SITE 2 BC4 9 ILE I 93 HIS I 145 ASP I 154 GLU I 244
SITE 3 BC4 9 HOH I5027
SITE 1 BC5 9 TRP J 40 HIS J 45 ILE J 77 PHE J 82
SITE 2 BC5 9 ILE J 93 HIS J 145 ASP J 154 GLU J 244
SITE 3 BC5 9 HOH J5024
SITE 1 BC6 9 TRP K 40 HIS K 45 ILE K 77 PHE K 82
SITE 2 BC6 9 ILE K 93 HIS K 145 ASP K 154 GLU K 244
SITE 3 BC6 9 HOH K5044
SITE 1 BC7 9 TRP L 40 HIS L 45 ILE L 77 PHE L 82
SITE 2 BC7 9 ILE L 93 HIS L 145 ASP L 154 GLU L 244
SITE 3 BC7 9 HOH L5066
CRYST1 83.280 132.008 135.424 90.00 94.11 90.00 P 1 21 1 24
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 0.012008 0.000000 0.000864 0.00000
SCALE2 0.000000 0.007575 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007403 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
