HEADER LYASE 04-MAY-12 4F0M
TITLE UNACTIVATED RUBISCO WITH MAGNESIUM AND A WATER MOLECULE BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RUBISCO LARGE SUBUNIT;
COMPND 5 EC: 4.1.1.39;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: RUBISCO SMALL SUBUNIT;
COMPND 10 EC: 4.1.1.39
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALDIERIA SULPHURARIA;
SOURCE 3 ORGANISM_COMMON: RED ALGA;
SOURCE 4 ORGANISM_TAXID: 130081;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: GALDIERIA SULPHURARIA;
SOURCE 7 ORGANISM_COMMON: RED ALGA;
SOURCE 8 ORGANISM_TAXID: 130081
KEYWDS CATALYTIC DOMAIN TIM BARREL, CARBOXYLASE/OXYGENASE, NITROSYLATION,
KEYWDS 2 CHLOROPLAST, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.STEC
REVDAT 3 13-SEP-23 4F0M 1 REMARK LINK
REVDAT 2 12-DEC-12 4F0M 1 JRNL
REVDAT 1 14-NOV-12 4F0M 0
JRNL AUTH B.STEC
JRNL TITL STRUCTURAL MECHANISM OF RUBISCO ACTIVATION BY CARBAMYLATION
JRNL TITL 2 OF THE ACTIVE SITE LYSINE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 18785 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 23112176
JRNL DOI 10.1073/PNAS.1210754109
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 96.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 25853
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) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1367
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1721
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE SET COUNT : 93
REMARK 3 BIN FREE R VALUE : 0.3730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4658
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 353
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.39000
REMARK 3 B22 (A**2) : -0.39000
REMARK 3 B33 (A**2) : 0.79000
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): 0.342
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.237
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.162
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.710
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4780 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6462 ; 1.774 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 584 ; 7.359 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 220 ;33.780 ;23.682
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 821 ;17.251 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;14.975 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 701 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3615 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2185 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3194 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 303 ; 0.172 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.318 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 167 ; 0.200 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 47 ; 0.179 ; 0.200
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): 2998 ; 1.251 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4680 ; 2.071 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2055 ; 2.818 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1782 ; 4.257 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 27 A 474
REMARK 3 ORIGIN FOR THE GROUP (A): 32.6245 60.7513 12.0016
REMARK 3 T TENSOR
REMARK 3 T11: -0.0257 T22: 0.0036
REMARK 3 T33: 0.0148 T12: -0.0018
REMARK 3 T13: 0.0052 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.1016 L22: 0.1321
REMARK 3 L33: 0.1951 L12: -0.0242
REMARK 3 L13: -0.0447 L23: 0.1323
REMARK 3 S TENSOR
REMARK 3 S11: 0.0004 S12: 0.0019 S13: 0.0103
REMARK 3 S21: -0.0059 S22: -0.0092 S23: 0.0578
REMARK 3 S31: -0.0245 S32: -0.0558 S33: 0.0088
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 501 A 502
REMARK 3 ORIGIN FOR THE GROUP (A): 48.0901 52.9302 39.6310
REMARK 3 T TENSOR
REMARK 3 T11: 0.0009 T22: -0.0112
REMARK 3 T33: -0.0248 T12: -0.0113
REMARK 3 T13: 0.0252 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.2954 L22: 0.3611
REMARK 3 L33: 0.2282 L12: 0.1328
REMARK 3 L13: -0.0141 L23: -0.1203
REMARK 3 S TENSOR
REMARK 3 S11: 0.0120 S12: -0.0533 S13: -0.0148
REMARK 3 S21: 0.0357 S22: -0.0120 S23: 0.0108
REMARK 3 S31: 0.0289 S32: -0.0109 S33: 0.0000
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 4F0M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-12.
REMARK 100 THE DEPOSITION ID IS D_1000072304.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JAN-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : CONFOCAL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27220
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 96.230
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.75100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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: PDB ENTRY 3RUB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M POTASSIUM PHOSPHATE, 26%
REMARK 280 AMMONIUM SULFATE, PH 7.5, VAPOR DIFFUSION, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
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 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 68.16250
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 68.16250
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 60.76200
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 68.16250
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 68.16250
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 60.76200
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 68.16250
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 68.16250
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 60.76200
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 68.16250
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 68.16250
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 60.76200
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 68.16250
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 68.16250
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 60.76200
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 68.16250
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 68.16250
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 60.76200
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 68.16250
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 68.16250
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 60.76200
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 68.16250
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 68.16250
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 60.76200
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: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 108110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 128140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -726.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 136.32500
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 136.32500
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 136.32500
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 136.32500
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 136.32500
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 6 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 0.000000 -1.000000 0.000000 136.32500
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 7 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 8 0.000000 -1.000000 0.000000 136.32500
REMARK 350 BIOMT2 8 -1.000000 0.000000 0.000000 136.32500
REMARK 350 BIOMT3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CL CL B 701 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 819 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 884 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 924 LIES ON A SPECIAL POSITION.
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 SER A 2
REMARK 465 GLN A 3
REMARK 465 SER A 4
REMARK 465 LEU A 5
REMARK 465 GLU A 6
REMARK 465 GLU A 7
REMARK 465 LYS A 8
REMARK 465 SER A 9
REMARK 465 VAL A 10
REMARK 465 GLN A 11
REMARK 465 GLU A 12
REMARK 465 ARG A 13
REMARK 465 THR A 14
REMARK 465 ARG A 15
REMARK 465 ILE A 16
REMARK 465 LYS A 17
REMARK 465 ASN A 18
REMARK 465 SER A 19
REMARK 465 ARG A 20
REMARK 465 TYR A 21
REMARK 465 GLU A 22
REMARK 465 SER A 23
REMARK 465 GLY A 24
REMARK 465 VAL A 25
REMARK 465 ILE A 26
REMARK 465 PHE A 475
REMARK 465 ASN A 476
REMARK 465 TYR A 477
REMARK 465 THR A 478
REMARK 465 SER A 479
REMARK 465 THR A 480
REMARK 465 ASP A 481
REMARK 465 THR A 482
REMARK 465 SER A 483
REMARK 465 ASP A 484
REMARK 465 PHE A 485
REMARK 465 VAL A 486
REMARK 465 GLU A 487
REMARK 465 THR A 488
REMARK 465 PRO A 489
REMARK 465 THR A 490
REMARK 465 ALA A 491
REMARK 465 ASN A 492
REMARK 465 ILE A 493
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 HOH B 907 O HOH B 912 2.03
REMARK 500 O HOH B 854 O HOH B 909 2.09
REMARK 500 O HOH A 734 O HOH B 860 2.13
REMARK 500 OE2 GLU B 549 O HOH B 840 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 257 CG GLU A 257 CD 0.097
REMARK 500 GLU B 517 CG GLU B 517 CD 0.097
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 LEU A 343 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 ARG A 351 NE - CZ - NH1 ANGL. DEV. = 3.1 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 SER A 71 -131.29 -143.20
REMARK 500 ALA A 73 103.24 -54.90
REMARK 500 VAL A 77 110.57 77.02
REMARK 500 ASN A 101 17.61 102.85
REMARK 500 ASN A 102 88.69 -161.15
REMARK 500 VAL A 133 85.57 -61.44
REMARK 500 PHE A 134 -158.21 -101.16
REMARK 500 PHE A 136 -57.68 -16.40
REMARK 500 ASN A 216 -91.76 -122.17
REMARK 500 MET A 221 119.42 -175.00
REMARK 500 THR A 308 -36.32 -29.96
REMARK 500 TYR A 309 39.28 -76.31
REMARK 500 SER A 310 -108.02 -102.03
REMARK 500 ARG A 311 61.91 -65.23
REMARK 500 VAL A 340 -168.76 -101.79
REMARK 500 ASN A 365 98.80 -165.87
REMARK 500 THR A 414 -61.98 -123.02
REMARK 500 ILE A 473 -64.61 -137.95
REMARK 500 ASN B 577 34.02 -99.25
REMARK 500 ILE B 591 -70.05 -115.48
REMARK 500 ASP B 616 -145.19 -119.97
REMARK 500 SER B 618 -114.22 47.81
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 MG A 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 702 O
REMARK 620 2 HOH A 735 O 134.2
REMARK 620 3 HOH A 751 O 99.2 93.1
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 703
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4F0H RELATED DB: PDB
REMARK 900 RELATED ID: 4F0K RELATED DB: PDB
DBREF 4F0M A 1 493 UNP P23755 RBL_GALSU 1 493
DBREF 4F0M B 501 638 UNP P23756 RBS_GALSU 1 138
SEQRES 1 A 493 MET SER GLN SER LEU GLU GLU LYS SER VAL GLN GLU ARG
SEQRES 2 A 493 THR ARG ILE LYS ASN SER ARG TYR GLU SER GLY VAL ILE
SEQRES 3 A 493 PRO TYR ALA LYS MET GLY TYR TRP ASN PRO ASP TYR GLN
SEQRES 4 A 493 VAL LYS ASP THR ASP VAL LEU ALA LEU PHE ARG VAL THR
SEQRES 5 A 493 PRO GLN PRO GLY VAL ASP PRO ILE GLU ALA ALA ALA ALA
SEQRES 6 A 493 VAL ALA GLY GLU SER SER THR ALA THR TRP THR VAL VAL
SEQRES 7 A 493 TRP THR ASP LEU LEU THR ALA ALA ASP LEU TYR ARG ALA
SEQRES 8 A 493 LYS ALA TYR LYS VAL ASP GLN VAL PRO ASN ASN PRO GLU
SEQRES 9 A 493 GLN TYR PHE ALA TYR ILE ALA TYR GLU LEU ASP LEU PHE
SEQRES 10 A 493 GLU GLU GLY SER ILE ALA ASN LEU THR ALA SER ILE ILE
SEQRES 11 A 493 GLY ASN VAL PHE GLY PHE LYS ALA VAL LYS ALA LEU ARG
SEQRES 12 A 493 LEU GLU ASP MET ARG LEU PRO PHE ALA TYR ILE LYS THR
SEQRES 13 A 493 PHE GLN GLY PRO ALA THR GLY VAL ILE LEU GLU ARG GLU
SEQRES 14 A 493 ARG LEU ASP LYS PHE GLY ARG PRO LEU LEU GLY SNC THR
SEQRES 15 A 493 THR LYS PRO LYS LEU GLY LEU SER GLY LYS ASN TYR GLY
SEQRES 16 A 493 ARG VAL VAL TYR GLU ALA LEU LYS GLY GLY LEU ASP PHE
SEQRES 17 A 493 VAL LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE MET
SEQRES 18 A 493 ARG TRP ARG GLU ARG TYR LEU PHE VAL MET GLU ALA VAL
SEQRES 19 A 493 ASN LYS ALA ALA ALA ALA THR GLY GLU VAL LYS GLY HIS
SEQRES 20 A 493 TYR LEU ASN VAL THR ALA ALA THR MET GLU GLU MET TYR
SEQRES 21 A 493 ALA ARG ALA GLN LEU ALA LYS GLU LEU GLY SER VAL ILE
SEQRES 22 A 493 ILE MET ILE ASP LEU VAL ILE GLY TYR THR ALA ILE GLN
SEQRES 23 A 493 THR MET ALA LYS TRP ALA ARG ASP ASN ASP MET ILE LEU
SEQRES 24 A 493 HIS LEU HIS ARG ALA GLY ASN SER THR TYR SER ARG GLN
SEQRES 25 A 493 LYS ASN HIS GLY MET ASN PHE ARG VAL ILE CYS LYS TRP
SEQRES 26 A 493 MET ARG MET ALA GLY VAL ASP HIS ILE HIS ALA GLY THR
SEQRES 27 A 493 VAL VAL GLY LYS LEU GLU GLY ASP PRO ILE ILE THR ARG
SEQRES 28 A 493 GLY PHE TYR LYS THR LEU LEU LEU PRO LYS LEU GLU ARG
SEQRES 29 A 493 ASN LEU GLN GLU GLY LEU PHE PHE ASP MET ASP TRP ALA
SEQRES 30 A 493 SER LEU ARG LYS VAL MET PRO VAL ALA SER GLY GLY ILE
SEQRES 31 A 493 HIS ALA GLY GLN MET HIS GLN LEU ILE HIS TYR LEU GLY
SEQRES 32 A 493 GLU ASP VAL VAL LEU GLN PHE GLY GLY GLY THR ILE GLY
SEQRES 33 A 493 HIS PRO ASP GLY ILE GLN SER GLY ALA THR ALA ASN ARG
SEQRES 34 A 493 VAL ALA LEU GLU ALA MET ILE LEU ALA ARG ASN GLU ASN
SEQRES 35 A 493 ARG ASP PHE LEU THR GLU GLY PRO GLU ILE LEU ARG GLU
SEQRES 36 A 493 ALA ALA LYS ASN SNC GLY ALA LEU ARG THR ALA LEU ASP
SEQRES 37 A 493 LEU TRP LYS ASP ILE THR PHE ASN TYR THR SER THR ASP
SEQRES 38 A 493 THR SER ASP PHE VAL GLU THR PRO THR ALA ASN ILE
SEQRES 1 B 138 MET ARG ILE THR GLN GLY THR PHE SER PHE LEU PRO ASP
SEQRES 2 B 138 LEU THR ASP GLU GLN ILE LYS LYS GLN ILE ASP TYR MET
SEQRES 3 B 138 ILE SER LYS LYS LEU ALA ILE GLY ILE GLU TYR THR ASN
SEQRES 4 B 138 ASP ILE HIS PRO ARG ASN SER PHE TRP GLU MET TRP GLY
SEQRES 5 B 138 LEU PRO LEU PHE GLU VAL THR ASP PRO ALA PRO VAL LEU
SEQRES 6 B 138 PHE GLU ILE ASN ALA CYS ARG LYS ALA LYS SER ASN PHE
SEQRES 7 B 138 TYR ILE LYS VAL VAL GLY PHE SER SER GLU ARG GLY ILE
SEQRES 8 B 138 GLU SER THR ILE ILE SER PHE ILE VAL ASN ARG PRO LYS
SEQRES 9 B 138 HIS GLU PRO GLY PHE ASN LEU ILE ARG GLN GLU ASP LYS
SEQRES 10 B 138 SER ARG SER ILE LYS TYR SER ILE GLN ALA TYR GLU THR
SEQRES 11 B 138 TYR LYS PRO GLU ASP GLN ARG TYR
MODRES 4F0M SNC A 181 CYS S-NITROSO-CYSTEINE
MODRES 4F0M SNC A 460 CYS S-NITROSO-CYSTEINE
HET SNC A 181 8
HET SNC A 460 8
HET MG A 501 1
HET GOL A 502 6
HET CL B 701 1
HET GOL B 702 6
HET GOL B 703 6
HETNAM SNC S-NITROSO-CYSTEINE
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 SNC 2(C3 H6 N2 O3 S)
FORMUL 3 MG MG 2+
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 5 CL CL 1-
FORMUL 8 HOH *353(H2 O)
HELIX 1 1 ASP A 58 SER A 70 1 13
HELIX 2 2 VAL A 78 THR A 84 5 7
HELIX 3 3 ALA A 85 ARG A 90 5 6
HELIX 4 4 GLU A 113 PHE A 117 5 5
HELIX 5 5 SER A 121 GLY A 131 1 11
HELIX 6 6 PRO A 150 LYS A 155 1 6
HELIX 7 7 GLY A 163 ASP A 172 1 10
HELIX 8 8 SER A 190 GLY A 205 1 16
HELIX 9 9 ARG A 222 GLY A 242 1 21
HELIX 10 10 THR A 255 LEU A 269 1 15
HELIX 11 11 GLY A 281 ASN A 295 1 15
HELIX 12 12 ASN A 318 GLY A 330 1 13
HELIX 13 13 ASP A 346 LEU A 359 1 14
HELIX 14 14 ASN A 365 GLY A 369 5 5
HELIX 15 15 HIS A 391 GLY A 393 5 3
HELIX 16 16 GLN A 394 GLY A 403 1 10
HELIX 17 17 GLY A 411 GLY A 416 1 6
HELIX 18 18 GLY A 420 GLU A 441 1 22
HELIX 19 19 ASP A 444 LYS A 458 1 15
HELIX 20 20 SNC A 460 ILE A 473 1 14
HELIX 21 21 THR B 515 LYS B 529 1 15
HELIX 22 22 PRO B 561 LYS B 575 1 15
HELIX 23 23 GLU B 629 LYS B 632 5 4
HELIX 24 24 PRO B 633 ARG B 637 5 5
SHEET 1 A 5 LYS A 92 GLN A 98 0
SHEET 2 A 5 TYR A 106 TYR A 112 -1 O PHE A 107 N ASP A 97
SHEET 3 A 5 VAL A 45 PRO A 53 -1 N VAL A 51 O TYR A 106
SHEET 4 A 5 VAL A 139 ARG A 148 -1 O ARG A 143 N ARG A 50
SHEET 5 A 5 GLY A 316 MET A 317 1 O GLY A 316 N LEU A 144
SHEET 1 B 8 LEU A 178 GLY A 180 0
SHEET 2 B 8 VAL A 407 GLN A 409 1 O LEU A 408 N LEU A 178
SHEET 3 B 8 MET A 383 SER A 387 1 N ALA A 386 O GLN A 409
SHEET 4 B 8 HIS A 333 HIS A 335 1 N ILE A 334 O MET A 383
SHEET 5 B 8 ILE A 298 HIS A 302 1 N LEU A 301 O HIS A 333
SHEET 6 B 8 ILE A 273 ASP A 277 1 N ILE A 276 O HIS A 302
SHEET 7 B 8 GLY A 246 ASN A 250 1 N LEU A 249 O MET A 275
SHEET 8 B 8 PHE A 208 LYS A 210 1 N VAL A 209 O TYR A 248
SHEET 1 C 2 LYS A 361 LEU A 362 0
SHEET 2 C 2 MET A 374 ASP A 375 -1 O MET A 374 N LEU A 362
SHEET 1 D 4 GLU B 549 MET B 550 0
SHEET 2 D 4 ALA B 532 THR B 538 -1 N TYR B 537 O GLU B 549
SHEET 3 D 4 TYR B 579 SER B 586 -1 O VAL B 583 N GLY B 534
SHEET 4 D 4 SER B 593 ASN B 601 -1 O VAL B 600 N ILE B 580
SHEET 1 E 2 PHE B 609 GLU B 615 0
SHEET 2 E 2 ILE B 621 ALA B 627 -1 O LYS B 622 N GLN B 614
LINK C GLY A 180 N SNC A 181 1555 1555 1.32
LINK C SNC A 181 N THR A 182 1555 1555 1.33
LINK C ASN A 459 N SNC A 460 1555 1555 1.34
LINK C SNC A 460 N GLY A 461 1555 1555 1.33
LINK MG MG A 501 O HOH A 702 1555 1555 1.75
LINK MG MG A 501 O HOH A 735 1555 1555 1.76
LINK MG MG A 501 O HOH A 751 1555 1555 1.78
CISPEP 1 LYS A 184 PRO A 185 0 -5.16
SITE 1 AC1 4 HIS A 302 HOH A 702 HOH A 735 HOH A 751
SITE 1 AC2 4 GLN A 312 LYS A 313 ASN A 314 HIS A 315
SITE 1 AC3 1 GLN B 614
SITE 1 AC4 7 ARG A 170 PHE A 229 HOH A 810 ARG B 544
SITE 2 AC4 7 HOH B 809 HOH B 816 HOH B 821
SITE 1 AC5 7 ALA A 239 ALA A 240 HOH A 761 PRO B 607
SITE 2 AC5 7 PHE B 609 TYR B 628 GLU B 634
CRYST1 136.325 136.325 121.524 90.00 90.00 90.00 I 4 2 2 16
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 0.007335 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007335 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008229 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
