HEADER HYDROLASE 20-OCT-15 5ECU
TITLE THE UNLIGANDED STRUCTURE OF CALDICELLULOSIRUPTOR SACCHAROLYTICUS GH5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELLULASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 30-576;
COMPND 5 EC: 3.2.1.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CALDICELLULOSIRUPTOR SACCHAROLYTICUS;
SOURCE 3 ORGANISM_TAXID: 44001;
SOURCE 4 GENE: CSAC_0678;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CALDICELLULOSIRUPTOR, GH5, TIM-BARREL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.M.ALAHUHTA,V.V.LUNIN
REVDAT 3 27-SEP-23 5ECU 1 LINK
REVDAT 2 15-FEB-17 5ECU 1 LINK
REVDAT 1 02-NOV-16 5ECU 0
JRNL AUTH P.M.ALAHUHTA,V.V.LUNIN
JRNL TITL THE STRUCTURE OF CALDICELLULOSIRUPTOR SACCHAROLYTICUS GH5
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 79213
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) : 0.087
REMARK 3 R VALUE (WORKING SET) : 0.085
REMARK 3 FREE R VALUE : 0.115
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4144
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5828
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.1120
REMARK 3 BIN FREE R VALUE SET COUNT : 310
REMARK 3 BIN FREE R VALUE : 0.1570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2769
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 193
REMARK 3 SOLVENT ATOMS : 392
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.035
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.037
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.021
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.197
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.988
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.981
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3214 ; 0.028 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3048 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4312 ; 2.681 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7037 ; 1.288 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 392 ; 6.766 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 148 ;37.888 ;25.743
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 512 ;12.159 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;18.909 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 444 ; 0.173 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3668 ; 0.014 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 698 ; 0.004 ; 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): 1515 ; 2.060 ; 3.434
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1507 ; 2.015 ;70.155
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1920 ; 2.314 ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1921 ; 2.314 ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1699 ; 9.622 ; 1.884
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1700 ; 9.619 ; 1.885
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2393 ; 7.742 ; 2.569
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4141 ; 6.999 ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3923 ; 6.802 ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 3059 ; 9.166 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 12 ;16.867 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3084 ;20.579 ; 5.000
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 : MASK
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
REMARK 4
REMARK 4 5ECU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214668.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97945
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83455
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 59.00
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 42.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 40.00
REMARK 200 R MERGE FOR SHELL (I) : 0.88700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1G01
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M SODIUM MALONATE PH 7.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 73.33000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 73.33000
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 73.33000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 73.33000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 73.33000
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 73.33000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 73.33000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 73.33000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 73.33000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 73.33000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 73.33000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 73.33000
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 73.33000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 73.33000
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 73.33000
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 73.33000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 73.33000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 73.33000
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 73.33000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 73.33000
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 73.33000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 73.33000
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 73.33000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 73.33000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 73.33000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 73.33000
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 73.33000
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 73.33000
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 73.33000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 73.33000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 73.33000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 73.33000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 73.33000
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 73.33000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 73.33000
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 73.33000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ASN A 30
REMARK 465 LYS A 381
REMARK 465 ILE A 382
REMARK 465 SER A 383
REMARK 465 GLN A 384
REMARK 465 ASP A 385
REMARK 465 GLN A 386
REMARK 465 VAL A 387
REMARK 465 ALA A 388
REMARK 465 CYS A 389
REMARK 465 ALA A 390
REMARK 465 PRO A 391
REMARK 465 ILE A 392
REMARK 465 GLY A 393
REMARK 465 GLN A 394
REMARK 465 PRO A 395
REMARK 465 ILE A 396
REMARK 465 LEU A 397
REMARK 465 PRO A 398
REMARK 465 SER A 399
REMARK 465 ASP A 400
REMARK 465 PHE A 401
REMARK 465 GLU A 402
REMARK 465 ASP A 403
REMARK 465 GLY A 404
REMARK 465 THR A 405
REMARK 465 ARG A 406
REMARK 465 GLN A 407
REMARK 465 GLY A 408
REMARK 465 TRP A 409
REMARK 465 ASP A 410
REMARK 465 TRP A 411
REMARK 465 ASP A 412
REMARK 465 GLY A 413
REMARK 465 PRO A 414
REMARK 465 SER A 415
REMARK 465 GLY A 416
REMARK 465 VAL A 417
REMARK 465 LYS A 418
REMARK 465 GLY A 419
REMARK 465 ALA A 420
REMARK 465 LEU A 421
REMARK 465 THR A 422
REMARK 465 ILE A 423
REMARK 465 GLU A 424
REMARK 465 GLU A 425
REMARK 465 ALA A 426
REMARK 465 ASN A 427
REMARK 465 GLY A 428
REMARK 465 SER A 429
REMARK 465 ASN A 430
REMARK 465 ALA A 431
REMARK 465 LEU A 432
REMARK 465 SER A 433
REMARK 465 TRP A 434
REMARK 465 GLU A 435
REMARK 465 VAL A 436
REMARK 465 GLU A 437
REMARK 465 TYR A 438
REMARK 465 PRO A 439
REMARK 465 GLU A 440
REMARK 465 LYS A 441
REMARK 465 LYS A 442
REMARK 465 LEU A 443
REMARK 465 GLN A 444
REMARK 465 ASP A 445
REMARK 465 GLY A 446
REMARK 465 TRP A 447
REMARK 465 ALA A 448
REMARK 465 SER A 449
REMARK 465 ALA A 450
REMARK 465 PRO A 451
REMARK 465 ARG A 452
REMARK 465 LEU A 453
REMARK 465 ILE A 454
REMARK 465 LEU A 455
REMARK 465 ARG A 456
REMARK 465 ASN A 457
REMARK 465 ILE A 458
REMARK 465 ASN A 459
REMARK 465 THR A 460
REMARK 465 THR A 461
REMARK 465 ARG A 462
REMARK 465 GLY A 463
REMARK 465 ASP A 464
REMARK 465 CYS A 465
REMARK 465 LYS A 466
REMARK 465 TYR A 467
REMARK 465 LEU A 468
REMARK 465 CYS A 469
REMARK 465 PHE A 470
REMARK 465 ASP A 471
REMARK 465 PHE A 472
REMARK 465 TYR A 473
REMARK 465 LEU A 474
REMARK 465 LYS A 475
REMARK 465 PRO A 476
REMARK 465 LYS A 477
REMARK 465 GLN A 478
REMARK 465 ALA A 479
REMARK 465 THR A 480
REMARK 465 LYS A 481
REMARK 465 GLY A 482
REMARK 465 GLU A 483
REMARK 465 LEU A 484
REMARK 465 ALA A 485
REMARK 465 ILE A 486
REMARK 465 PHE A 487
REMARK 465 LEU A 488
REMARK 465 ALA A 489
REMARK 465 PHE A 490
REMARK 465 ALA A 491
REMARK 465 PRO A 492
REMARK 465 PRO A 493
REMARK 465 SER A 494
REMARK 465 LEU A 495
REMARK 465 ASN A 496
REMARK 465 TYR A 497
REMARK 465 TRP A 498
REMARK 465 ALA A 499
REMARK 465 GLN A 500
REMARK 465 ALA A 501
REMARK 465 GLU A 502
REMARK 465 ASP A 503
REMARK 465 SER A 504
REMARK 465 PHE A 505
REMARK 465 ASN A 506
REMARK 465 ILE A 507
REMARK 465 ASP A 508
REMARK 465 LEU A 509
REMARK 465 THR A 510
REMARK 465 ASN A 511
REMARK 465 LEU A 512
REMARK 465 SER A 513
REMARK 465 THR A 514
REMARK 465 LEU A 515
REMARK 465 LYS A 516
REMARK 465 LYS A 517
REMARK 465 THR A 518
REMARK 465 PRO A 519
REMARK 465 ASP A 520
REMARK 465 ASP A 521
REMARK 465 LEU A 522
REMARK 465 TYR A 523
REMARK 465 SER A 524
REMARK 465 PHE A 525
REMARK 465 LYS A 526
REMARK 465 ILE A 527
REMARK 465 SER A 528
REMARK 465 PHE A 529
REMARK 465 ASP A 530
REMARK 465 LEU A 531
REMARK 465 ASP A 532
REMARK 465 LYS A 533
REMARK 465 ILE A 534
REMARK 465 LYS A 535
REMARK 465 GLU A 536
REMARK 465 GLY A 537
REMARK 465 LYS A 538
REMARK 465 ILE A 539
REMARK 465 ILE A 540
REMARK 465 GLY A 541
REMARK 465 PRO A 542
REMARK 465 ASP A 543
REMARK 465 THR A 544
REMARK 465 HIS A 545
REMARK 465 LEU A 546
REMARK 465 ARG A 547
REMARK 465 ASP A 548
REMARK 465 ILE A 549
REMARK 465 ILE A 550
REMARK 465 ILE A 551
REMARK 465 VAL A 552
REMARK 465 VAL A 553
REMARK 465 ALA A 554
REMARK 465 ASP A 555
REMARK 465 VAL A 556
REMARK 465 ASN A 557
REMARK 465 SER A 558
REMARK 465 ASP A 559
REMARK 465 PHE A 560
REMARK 465 LYS A 561
REMARK 465 GLY A 562
REMARK 465 ARG A 563
REMARK 465 MET A 564
REMARK 465 TYR A 565
REMARK 465 LEU A 566
REMARK 465 ASP A 567
REMARK 465 ASN A 568
REMARK 465 VAL A 569
REMARK 465 ARG A 570
REMARK 465 PHE A 571
REMARK 465 THR A 572
REMARK 465 ASN A 573
REMARK 465 MET A 574
REMARK 465 LEU A 575
REMARK 465 PHE A 576
REMARK 465 LEU A 577
REMARK 465 GLU A 578
REMARK 465 HIS A 579
REMARK 465 HIS A 580
REMARK 465 HIS A 581
REMARK 465 HIS A 582
REMARK 465 HIS A 583
REMARK 465 HIS A 584
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 ASP A 36 CB CG OD1 OD2
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 OE1 GLN A 219 O1 EDO A 616 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 NZ LYS A 135 OE2 GLU A 269 23455 2.15
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 ARG A 65 CZ ARG A 65 NH2 0.085
REMARK 500 GLU A 159 CD GLU A 159 OE1 0.090
REMARK 500 GLU A 159 CD GLU A 159 OE2 0.105
REMARK 500 GLU A 200 CB GLU A 200 CG 0.157
REMARK 500 GLU A 200 CB GLU A 200 CG 0.118
REMARK 500 GLU A 200 CG GLU A 200 CD 0.100
REMARK 500 GLU A 200 CD GLU A 200 OE1 0.123
REMARK 500 GLU A 223 CG GLU A 223 CD 0.105
REMARK 500 GLU A 223 CD GLU A 223 OE1 0.106
REMARK 500 GLU A 285 CD GLU A 285 OE2 0.073
REMARK 500 GLU A 290 CD GLU A 290 OE2 -0.119
REMARK 500 GLU A 307 CD GLU A 307 OE1 0.068
REMARK 500 GLY A 347 C GLY A 347 O 0.111
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 55 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 110 NE - CZ - NH1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG A 110 NE - CZ - NH2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 VAL A 126 CG1 - CB - CG2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 ASP A 141 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP A 166 CB - CG - OD2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 ASP A 193 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG A 236 NE - CZ - NH2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ASP A 248 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 LYS A 249 CD - CE - NZ ANGL. DEV. = 16.2 DEGREES
REMARK 500 LYS A 249 CD - CE - NZ ANGL. DEV. = 16.9 DEGREES
REMARK 500 ASP A 264 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP A 349 CB - CG - OD2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 ASP A 353 CB - CG - OD1 ANGL. DEV. = 13.6 DEGREES
REMARK 500 ARG A 367 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG A 378 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 378 NE - CZ - NH2 ANGL. DEV. = -5.0 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 ASN A 44 22.20 -149.93
REMARK 500 ASN A 44 28.98 -149.93
REMARK 500 LEU A 151 -58.09 -157.59
REMARK 500 CYS A 186 92.73 -161.78
REMARK 500 TYR A 298 79.95 -118.21
REMARK 500 VAL A 338 -57.66 -130.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 110 0.09 SIDE CHAIN
REMARK 500 GLU A 290 0.09 SIDE CHAIN
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 A 644 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 92 O
REMARK 620 2 HOH A 760 O 92.6
REMARK 620 3 HOH A 904 O 101.6 165.1
REMARK 620 4 HOH A 925 O 84.3 93.4 92.4
REMARK 620 5 HOH A1047 O 95.7 75.4 98.5 168.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 643 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 188 OE1
REMARK 620 2 GLU A 188 OE2 46.1
REMARK 620 3 GLU A 285 OE2 141.1 100.0
REMARK 620 4 EDO A 614 O2 127.6 172.2 84.1
REMARK 620 5 EDO A 614 O2 95.8 136.7 104.0 35.5
REMARK 620 6 HOH A 768 O 52.7 96.3 163.2 79.2 60.6
REMARK 620 7 HOH A 786 O 81.1 86.4 78.0 88.0 64.4 99.0
REMARK 620 8 HOH A 913 O 72.9 62.4 111.7 122.4 135.2 79.7 148.2
REMARK 620 9 HOH A1002 O 88.7 106.6 124.3 76.0 88.8 53.5 149.9 48.7
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 627
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 629
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 630
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 631
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 632
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 633
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 634
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 635
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 636
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 637
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 638
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 639
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 640
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 641
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 642
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 643
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 644
DBREF 5ECU A 30 576 UNP A4XHB2 A4XHB2_CALS8 30 576
SEQADV 5ECU LEU A 346 UNP A4XHB2 PRO 346 CONFLICT
SEQADV 5ECU LEU A 577 UNP A4XHB2 EXPRESSION TAG
SEQADV 5ECU GLU A 578 UNP A4XHB2 EXPRESSION TAG
SEQADV 5ECU HIS A 579 UNP A4XHB2 EXPRESSION TAG
SEQADV 5ECU HIS A 580 UNP A4XHB2 EXPRESSION TAG
SEQADV 5ECU HIS A 581 UNP A4XHB2 EXPRESSION TAG
SEQADV 5ECU HIS A 582 UNP A4XHB2 EXPRESSION TAG
SEQADV 5ECU HIS A 583 UNP A4XHB2 EXPRESSION TAG
SEQADV 5ECU HIS A 584 UNP A4XHB2 EXPRESSION TAG
SEQRES 1 A 555 ASN THR ALA TYR GLU LYS ASP LYS TYR PRO HIS LEU ILE
SEQRES 2 A 555 GLY ASN SER LEU VAL LYS LYS PRO SER VAL ALA GLY ARG
SEQRES 3 A 555 LEU GLN ILE ILE LYS GLN ASN GLY ARG ARG ILE LEU ALA
SEQRES 4 A 555 ASP GLN ASN GLY GLU PRO ILE GLN LEU ARG GLY MET SER
SEQRES 5 A 555 THR HIS GLY LEU GLN TRP PHE PRO GLN ILE ILE ASN ASN
SEQRES 6 A 555 ASN ALA PHE ALA ALA LEU ALA ASN ASP TRP GLY CYS ASN
SEQRES 7 A 555 VAL ILE ARG LEU ALA MET TYR ILE GLY GLU GLY GLY TYR
SEQRES 8 A 555 ALA THR ASN PRO GLN VAL LYS ASP LYS VAL ILE GLU GLY
SEQRES 9 A 555 ILE LYS LEU ALA ILE GLN ASN ASP MET TYR VAL ILE VAL
SEQRES 10 A 555 ASP TRP HIS VAL LEU ASN PRO GLY ASP PRO ASN ALA GLU
SEQRES 11 A 555 ILE TYR LYS GLY ALA LYS ASP PHE PHE LYS GLU ILE ALA
SEQRES 12 A 555 GLN LYS PHE PRO ASN ASP PHE HIS ILE ILE TYR GLU LEU
SEQRES 13 A 555 CYS ASN GLU PRO ASN PRO THR ASP PRO GLY VAL THR ASN
SEQRES 14 A 555 ASP GLU ALA GLY TRP LYS LYS VAL LYS ALA TYR ALA GLU
SEQRES 15 A 555 PRO ILE ILE LYS MET LEU ARG GLN MET GLY ASN GLU ASN
SEQRES 16 A 555 ILE ILE ILE ILE GLY SER PRO ASN TRP SER GLN ARG PRO
SEQRES 17 A 555 ASP PHE ALA ILE LYS ASP PRO ILE ALA ASP ASP LYS VAL
SEQRES 18 A 555 MET TYR SER VAL HIS PHE TYR THR GLY THR HIS LYS VAL
SEQRES 19 A 555 ASP GLY TYR VAL PHE GLU ASN MET LYS MET ALA ILE GLU
SEQRES 20 A 555 ALA GLY VAL PRO VAL PHE VAL THR GLU TRP GLY THR SER
SEQRES 21 A 555 GLU ALA SER GLY ASP GLY GLY PRO TYR LEU ASP GLU ALA
SEQRES 22 A 555 ASP LYS TRP LEU GLU TYR LEU ASN ALA ASN ASN ILE SER
SEQRES 23 A 555 TRP VAL ASN TRP SER LEU THR ASN LYS ASN GLU THR SER
SEQRES 24 A 555 GLY ALA PHE VAL PRO TYR ILE SER GLY VAL SER GLN ALA
SEQRES 25 A 555 THR ASP LEU ASP LEU GLY SER ASP GLN LYS TRP ASP ILE
SEQRES 26 A 555 SER GLU LEU SER ILE SER GLY GLU TYR VAL ARG SER ARG
SEQRES 27 A 555 ILE LYS GLY ILE PRO TYR GLN PRO ILE GLU ARG THR LEU
SEQRES 28 A 555 LYS ILE SER GLN ASP GLN VAL ALA CYS ALA PRO ILE GLY
SEQRES 29 A 555 GLN PRO ILE LEU PRO SER ASP PHE GLU ASP GLY THR ARG
SEQRES 30 A 555 GLN GLY TRP ASP TRP ASP GLY PRO SER GLY VAL LYS GLY
SEQRES 31 A 555 ALA LEU THR ILE GLU GLU ALA ASN GLY SER ASN ALA LEU
SEQRES 32 A 555 SER TRP GLU VAL GLU TYR PRO GLU LYS LYS LEU GLN ASP
SEQRES 33 A 555 GLY TRP ALA SER ALA PRO ARG LEU ILE LEU ARG ASN ILE
SEQRES 34 A 555 ASN THR THR ARG GLY ASP CYS LYS TYR LEU CYS PHE ASP
SEQRES 35 A 555 PHE TYR LEU LYS PRO LYS GLN ALA THR LYS GLY GLU LEU
SEQRES 36 A 555 ALA ILE PHE LEU ALA PHE ALA PRO PRO SER LEU ASN TYR
SEQRES 37 A 555 TRP ALA GLN ALA GLU ASP SER PHE ASN ILE ASP LEU THR
SEQRES 38 A 555 ASN LEU SER THR LEU LYS LYS THR PRO ASP ASP LEU TYR
SEQRES 39 A 555 SER PHE LYS ILE SER PHE ASP LEU ASP LYS ILE LYS GLU
SEQRES 40 A 555 GLY LYS ILE ILE GLY PRO ASP THR HIS LEU ARG ASP ILE
SEQRES 41 A 555 ILE ILE VAL VAL ALA ASP VAL ASN SER ASP PHE LYS GLY
SEQRES 42 A 555 ARG MET TYR LEU ASP ASN VAL ARG PHE THR ASN MET LEU
SEQRES 43 A 555 PHE LEU GLU HIS HIS HIS HIS HIS HIS
HET EDO A 601 4
HET EDO A 602 4
HET EDO A 603 4
HET EDO A 604 4
HET EDO A 605 4
HET EDO A 606 4
HET EDO A 607 4
HET EDO A 608 4
HET EDO A 609 4
HET EDO A 610 4
HET EDO A 611 4
HET EDO A 612 8
HET EDO A 613 4
HET EDO A 614 8
HET EDO A 615 8
HET EDO A 616 8
HET EDO A 617 4
HET EDO A 618 4
HET EDO A 619 4
HET EDO A 620 4
HET EDO A 621 4
HET EDO A 622 8
HET EDO A 623 4
HET EDO A 624 4
HET EDO A 625 4
HET GOL A 626 6
HET GOL A 627 12
HET GOL A 628 6
HET GOL A 629 6
HET GOL A 630 6
HET GOL A 631 6
HET GOL A 632 6
HET MLI A 633 7
HET MLI A 634 7
HET MLI A 635 7
HET ACT A 636 4
HET ACT A 637 4
HET ACT A 638 4
HET ACT A 639 4
HET ACT A 640 4
HET ACT A 641 4
HET ACT A 642 4
HET CA A 643 1
HET CA A 644 1
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETNAM MLI MALONATE ION
HETNAM ACT ACETATE ION
HETNAM CA CALCIUM ION
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 EDO 25(C2 H6 O2)
FORMUL 27 GOL 7(C3 H8 O3)
FORMUL 34 MLI 3(C3 H2 O4 2-)
FORMUL 37 ACT 7(C2 H3 O2 1-)
FORMUL 44 CA 2(CA 2+)
FORMUL 46 HOH *392(H2 O)
HELIX 1 AA1 ALA A 32 TYR A 38 1 7
HELIX 2 AA2 PRO A 39 ILE A 42 5 4
HELIX 3 AA3 LYS A 49 GLY A 54 1 6
HELIX 4 AA4 PHE A 88 ILE A 92 5 5
HELIX 5 AA5 ASN A 93 ASP A 103 1 11
HELIX 6 AA6 GLN A 125 ASN A 140 1 16
HELIX 7 AA7 ALA A 158 LYS A 162 5 5
HELIX 8 AA8 GLY A 163 PHE A 175 1 13
HELIX 9 AA9 ASP A 199 MET A 220 1 22
HELIX 10 AB1 SER A 230 GLN A 235 1 6
HELIX 11 AB2 ARG A 236 ILE A 241 5 6
HELIX 12 AB3 GLY A 265 ALA A 277 1 13
HELIX 13 AB4 TYR A 298 ASN A 312 1 15
HELIX 14 AB5 ASP A 353 LEU A 357 5 5
HELIX 15 AB6 SER A 358 GLY A 370 1 13
SHEET 1 AA1 2 GLN A 57 GLN A 61 0
SHEET 2 AA1 2 ARG A 64 ALA A 68 -1 O ARG A 64 N GLN A 61
SHEET 1 AA2 9 ARG A 78 THR A 82 0
SHEET 2 AA2 9 VAL A 108 TYR A 114 1 O ARG A 110 N THR A 82
SHEET 3 AA2 9 TYR A 143 HIS A 149 1 O ILE A 145 N LEU A 111
SHEET 4 AA2 9 ILE A 181 GLU A 184 1 O GLU A 184 N VAL A 146
SHEET 5 AA2 9 ILE A 226 ILE A 228 1 O ILE A 227 N TYR A 183
SHEET 6 AA2 9 VAL A 250 TYR A 257 1 O MET A 251 N ILE A 228
SHEET 7 AA2 9 VAL A 281 GLY A 287 1 O PHE A 282 N TYR A 252
SHEET 8 AA2 9 TRP A 316 LEU A 321 1 O TRP A 319 N TRP A 286
SHEET 9 AA2 9 ARG A 78 THR A 82 1 N SER A 81 O ASN A 318
LINK O ILE A 92 CA CA A 644 1555 1555 2.41
LINK OE1 GLU A 188 CA CA A 643 1555 1555 3.08
LINK OE2 GLU A 188 CA CA A 643 1555 1555 2.34
LINK OE2 GLU A 285 CA CA A 643 1555 1555 2.31
LINK O2 AEDO A 614 CA CA A 643 1555 1555 2.17
LINK O2 BEDO A 614 CA CA A 643 1555 1555 2.57
LINK CA CA A 643 O HOH A 768 1555 1555 2.62
LINK CA CA A 643 O HOH A 786 1555 1555 2.30
LINK CA CA A 643 O BHOH A 913 1555 9555 2.86
LINK CA CA A 643 O AHOH A1002 1555 1555 2.99
LINK CA CA A 643 O BHOH A1002 1555 1555 2.48
LINK CA CA A 644 O HOH A 760 1555 1555 2.28
LINK CA CA A 644 O HOH A 904 1555 1555 2.63
LINK CA CA A 644 O HOH A 925 1555 1555 2.30
LINK CA CA A 644 O HOH A1047 1555 1555 2.29
CISPEP 1 ASN A 152 PRO A 153 0 5.36
CISPEP 2 ASP A 193 PRO A 194 0 -8.63
CISPEP 3 ASP A 193 PRO A 194 0 -14.78
CISPEP 4 GLY A 296 PRO A 297 0 0.20
CISPEP 5 TRP A 319 SER A 320 0 0.36
SITE 1 AC1 7 HIS A 83 SER A 292 TRP A 319 LYS A 324
SITE 2 AC1 7 GLU A 326 EDO A 614 GOL A 626
SITE 1 AC2 7 ARG A 55 LEU A 56 PHE A 179 ILE A 181
SITE 2 AC2 7 ILE A 182 ASN A 224 ILE A 225
SITE 1 AC3 4 ASN A 102 ASN A 140 HOH A 728 HOH A 844
SITE 1 AC4 7 ASP A 103 ARG A 218 GLN A 219 LYS A 369
SITE 2 AC4 7 GOL A 628 HOH A 740 HOH A 789
SITE 1 AC5 6 ASN A 232 VAL A 338 SER A 339 LEU A 380
SITE 2 AC5 6 HOH A 798 HOH A 976
SITE 1 AC6 5 GLU A 211 LYS A 215 ALA A 246 HOH A 800
SITE 2 AC6 5 HOH A1063
SITE 1 AC7 11 ARG A 65 ILE A 66 ILE A 275 PRO A 280
SITE 2 AC7 11 VAL A 281 ILE A 314 HOH A 751 HOH A 801
SITE 3 AC7 11 HOH A 857 HOH A 879 HOH A1013
SITE 1 AC8 6 ARG A 218 ASN A 222 LYS A 351 GOL A 628
SITE 2 AC8 6 HOH A 894 HOH A1008
SITE 1 AC9 9 SER A 51 ILE A 138 ASP A 141 HIS A 180
SITE 2 AC9 9 GOL A 627 HOH A 717 HOH A 729 HOH A 735
SITE 3 AC9 9 HOH A1031
SITE 1 AD1 5 PHE A 88 GLN A 90 ASN A 323 HOH A 825
SITE 2 AD1 5 HOH A 898
SITE 1 AD2 8 GLU A 307 ALA A 311 HOH A 704 HOH A 713
SITE 2 AD2 8 HOH A 720 HOH A 924 HOH A 989 HOH A1077
SITE 1 AD3 5 VAL A 52 ASP A 69 ASN A 71 GLU A 73
SITE 2 AD3 5 HOH A 753
SITE 1 AD4 4 VAL A 263 ASP A 264 LYS A 272 HOH A 713
SITE 1 AD5 12 TYR A 257 GLU A 285 ALA A 291 SER A 292
SITE 2 AD5 12 GLY A 293 TRP A 319 EDO A 601 CA A 643
SITE 3 AD5 12 HOH A 738 HOH A 739 HOH A 768 HOH A 786
SITE 1 AD6 6 ASN A 44 SER A 45 VAL A 47 EDO A 621
SITE 2 AD6 6 HOH A 703 HOH A 793
SITE 1 AD7 9 MET A 216 GLN A 219 MET A 220 ILE A 371
SITE 2 AD7 9 PRO A 372 GLN A 374 EDO A 623 HOH A 714
SITE 3 AD7 9 HOH A1027
SITE 1 AD8 8 ARG A 236 TYR A 266 ASN A 270 HOH A 725
SITE 2 AD8 8 HOH A 726 HOH A 750 HOH A 780 HOH A 863
SITE 1 AD9 7 GLU A 377 THR A 379 LEU A 380 HOH A 734
SITE 2 AD9 7 HOH A 742 HOH A 756 HOH A 975
SITE 1 AE1 5 GLY A 116 GLU A 117 ASN A 152 ILE A 160
SITE 2 AE1 5 HOH A 984
SITE 1 AE2 4 TRP A 87 LYS A 324 GOL A 626 HOH A 790
SITE 1 AE3 7 LYS A 48 LYS A 49 VAL A 52 EDO A 615
SITE 2 AE3 7 HOH A 703 HOH A 753 HOH A 933
SITE 1 AE4 8 ILE A 58 ARG A 65 ASP A 248 EDO A 624
SITE 2 AE4 8 ACT A 640 HOH A 705 HOH A 727 HOH A 813
SITE 1 AE5 10 SER A 366 ILE A 371 PRO A 372 TYR A 373
SITE 2 AE5 10 GLN A 374 EDO A 616 HOH A 714 HOH A 758
SITE 3 AE5 10 HOH A 875 HOH A1018
SITE 1 AE6 8 ARG A 65 ALA A 240 EDO A 622 ACT A 640
SITE 2 AE6 8 HOH A 705 HOH A 715 HOH A 791 HOH A 906
SITE 1 AE7 11 GLU A 132 LYS A 135 GLN A 139 GLU A 269
SITE 2 AE7 11 LYS A 272 HOH A 701 HOH A 702 HOH A 733
SITE 3 AE7 11 HOH A 743 HOH A 764 HOH A 809
SITE 1 AE8 7 HIS A 83 TRP A 319 LYS A 324 GLU A 326
SITE 2 AE8 7 EDO A 601 EDO A 620 HOH A 748
SITE 1 AE9 9 ASP A 141 ASP A 238 LYS A 242 MET A 273
SITE 2 AE9 9 EDO A 609 HOH A 728 HOH A 735 HOH A 759
SITE 3 AE9 9 HOH A 853
SITE 1 AF1 10 ASP A 103 ARG A 218 GLN A 219 ARG A 365
SITE 2 AF1 10 LYS A 369 EDO A 604 EDO A 608 HOH A 755
SITE 3 AF1 10 HOH A 789 HOH A 894
SITE 1 AF2 10 GLN A 340 ALA A 341 THR A 342 ASP A 343
SITE 2 AF2 10 GLU A 356 HOH A 709 HOH A 712 HOH A 719
SITE 3 AF2 10 HOH A 730 HOH A 774
SITE 1 AF3 5 LYS A 204 LYS A 242 ASP A 243 HOH A 732
SITE 2 AF3 5 HOH A 736
SITE 1 AF4 14 PRO A 156 ASN A 157 ALA A 158 TYR A 161
SITE 2 AF4 14 LYS A 162 ALA A 164 LYS A 165 TYR A 209
SITE 3 AF4 14 HOH A 723 HOH A 724 HOH A 776 HOH A 788
SITE 4 AF4 14 HOH A 794 HOH A 967
SITE 1 AF5 12 ASN A 44 LYS A 49 ALA A 101 ASN A 102
SITE 2 AF5 12 GLY A 105 LYS A 369 HOH A 708 HOH A 718
SITE 3 AF5 12 HOH A 721 HOH A 731 HOH A 740 HOH A 741
SITE 1 AF6 10 PRO A 333 SER A 358 ILE A 359 ARG A 378
SITE 2 AF6 10 HOH A 782 HOH A 930 HOH A 942 HOH A 987
SITE 3 AF6 10 HOH A 992 HOH A1022
SITE 1 AF7 6 THR A 192 ASP A 193 TYR A 334 HOH A 744
SITE 2 AF7 6 HOH A 754 HOH A 928
SITE 1 AF8 5 ASP A 300 TYR A 373 ACT A 636 HOH A 707
SITE 2 AF8 5 HOH A 710
SITE 1 AF9 6 TYR A 33 LEU A 299 ASP A 300 ASP A 303
SITE 2 AF9 6 TYR A 373 MLI A 635
SITE 1 AG1 2 ASN A 157 HOH A 773
SITE 1 AG2 4 GLN A 61 ASN A 313 ACT A 639 HOH A 763
SITE 1 AG3 6 ASN A 310 ALA A 311 ASN A 313 ACT A 638
SITE 2 AG3 6 HOH A 763 HOH A 932
SITE 1 AG4 5 ILE A 245 ASP A 247 EDO A 622 EDO A 624
SITE 2 AG4 5 HOH A 705
SITE 1 AG5 4 SER A 348 ASP A 349 GLN A 350 HOH A 885
SITE 1 AG6 10 ILE A 115 TYR A 120 ALA A 121 ILE A 160
SITE 2 AG6 10 TYR A 161 LYS A 162 GLY A 163 HOH A 706
SITE 3 AG6 10 HOH A 783 HOH A 950
SITE 1 AG7 7 GLU A 188 GLU A 285 EDO A 614 HOH A 768
SITE 2 AG7 7 HOH A 786 HOH A 913 HOH A1002
SITE 1 AG8 5 ILE A 92 HOH A 760 HOH A 904 HOH A 925
SITE 2 AG8 5 HOH A1047
CRYST1 146.660 146.660 146.660 90.00 90.00 90.00 I 2 3 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 0.006818 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006818 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006818 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
