HEADER STRUCTURAL PROTEIN 13-AUG-09 3IO0
TITLE CRYSTAL STRUCTURE OF ETUB FROM CLOSTRIDIUM KLUYVERI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ETUB PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 75-304;
COMPND 5 SYNONYM: PREDICTED MICROCOMPARTMENT PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM KLUYVERI DSM 555;
SOURCE 3 ORGANISM_TAXID: 431943;
SOURCE 4 STRAIN: ATCC8527, DSM555, NCIMB 10680;
SOURCE 5 GENE: 1073;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET14B
KEYWDS TAMDEM REPEAT OF BACTERIAL MICROCOMPARTMENT DOMAIN IN A SINGLE
KEYWDS 2 POLYPEPTIDE CHAIN, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.W.PICKERSGILL,M.J.WARREN
REVDAT 2 21-FEB-24 3IO0 1 REMARK
REVDAT 1 15-SEP-09 3IO0 0
JRNL AUTH D.HELDT,S.FRANK,A.SEYEDARABI,D.LADAKIS,J.B.PARSONS,
JRNL AUTH 2 M.J.WARREN,R.W.PICKERSGILL
JRNL TITL STRUCTURE OF A TRIMERIC BACTERIAL MICROCOMPARTMENT SHELL
JRNL TITL 2 PROTEIN, ETUB, ASSOCIATED WITH ETHANOL UTILISATION IN
JRNL TITL 3 CLOSTRIDIUM KLUYVERI.
JRNL REF BIOCHEM.J. V. 423 199 2009
JRNL REFN ISSN 0264-6021
JRNL PMID 19635047
JRNL DOI 10.1042/BJ20090780
REMARK 2
REMARK 2 RESOLUTION. 3.00 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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 17475
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 883
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1216
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3060
REMARK 3 BIN FREE R VALUE SET COUNT : 71
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1657
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 1
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 68.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.234
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.196
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.140
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.877
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
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): 1680 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2277 ; 1.823 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 228 ; 9.112 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 57 ;38.939 ;24.386
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 278 ;21.236 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;19.852 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 277 ; 0.134 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1224 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 864 ; 0.245 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1180 ; 0.315 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 54 ; 0.127 ; 0.200
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): 52 ; 0.189 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.132 ; 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): 1143 ; 0.425 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1799 ; 0.788 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 577 ; 1.117 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 478 ; 1.979 ; 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 : 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 3IO0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054648.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97620
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : SI (111)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17475
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 86.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 187378.
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.70
REMARK 200 R MERGE (I) : 0.15100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.90
REMARK 200 R MERGE FOR SHELL (I) : 0.64000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 86.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 9.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4M FORMATE IN WATER, 8MG/ML PROTEIN,
REMARK 280 EQUAL VOLUMES OF RESERVOIR AND PROTEIN FORMED THE DROP, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y,-Z
REMARK 290 16555 X,-Y,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z,-X,-Y+1/2
REMARK 290 19555 -Z,-X+1/2,Y
REMARK 290 20555 -Z+1/2,X,-Y
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z,-X
REMARK 290 23555 Y,-Z,-X+1/2
REMARK 290 24555 -Y,-Z+1/2,X
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 86.70500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 86.70500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 86.70500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 86.70500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 86.70500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 86.70500
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 86.70500
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 86.70500
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 86.70500
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 86.70500
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 86.70500
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 86.70500
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 86.70500
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 86.70500
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 86.70500
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 86.70500
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 86.70500
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 86.70500
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 86.70500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 86.70500
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 86.70500
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 86.70500
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 86.70500
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 86.70500
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 86.70500
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 86.70500
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 86.70500
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 86.70500
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 86.70500
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 86.70500
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 86.70500
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 86.70500
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 86.70500
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 86.70500
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 86.70500
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 86.70500
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL
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 350 BIOMT1 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 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 ALA A 75
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 148 C - N - CA ANGL. DEV. = 16.7 DEGREES
REMARK 500 ARG A 148 N - CA - CB ANGL. DEV. = 11.0 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 THR A 84 104.98 121.49
REMARK 500 ASP A 88 75.22 -109.02
REMARK 500 CYS A 111 86.39 -151.63
REMARK 500 ALA A 123 -50.13 -154.12
REMARK 500 PRO A 147 -178.93 -66.65
REMARK 500 ARG A 148 54.79 93.67
REMARK 500 ASP A 149 -135.61 -141.94
REMARK 500 THR A 150 25.92 83.05
REMARK 500 LYS A 151 65.72 -162.62
REMARK 500 SER A 205 -151.24 -127.45
REMARK 500 THR A 253 -1.24 -144.89
REMARK 500 MET A 299 -27.00 -140.85
REMARK 500 SER A 300 -157.34 80.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER A 298 MET A 299 -68.24
REMARK 500 MET A 299 SER A 300 -34.10
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3IO0 A 75 304 UNP A5N734 A5N734_CLOK5 75 304
SEQRES 1 A 230 ALA PRO THR MET THR GLU PHE VAL GLY THR ALA GLY GLY
SEQRES 2 A 230 ASP THR VAL GLY LEU VAL ILE ALA ASN VAL ASP SER LEU
SEQRES 3 A 230 LEU HIS LYS HIS LEU GLY LEU ASP ASN THR CYS ARG SER
SEQRES 4 A 230 ILE GLY ILE ILE SER ALA ARG VAL GLY ALA PRO ALA GLN
SEQRES 5 A 230 MET MET ALA ALA ASP GLU ALA VAL LYS GLY THR ASN THR
SEQRES 6 A 230 GLU VAL ALA THR ILE GLU LEU PRO ARG ASP THR LYS GLY
SEQRES 7 A 230 GLY ALA GLY HIS GLY ILE PHE ILE VAL LEU LYS ALA ALA
SEQRES 8 A 230 ASP VAL SER ASP ALA ARG ARG ALA VAL GLU ILE ALA LEU
SEQRES 9 A 230 LYS GLN THR ASP LYS TYR LEU GLY ASN VAL TYR LEU CYS
SEQRES 10 A 230 ASP ALA GLY HIS LEU GLU VAL GLN TYR THR ALA ARG ALA
SEQRES 11 A 230 SER LEU ILE PHE GLU LYS ALA PHE GLY ALA PRO SER GLY
SEQRES 12 A 230 GLN ALA PHE GLY ILE MET HIS ALA ALA PRO ALA GLY VAL
SEQRES 13 A 230 GLY MET ILE VAL ALA ASP THR ALA LEU LYS THR ALA ASP
SEQRES 14 A 230 VAL LYS LEU ILE THR TYR GLY SER PRO THR ASN GLY VAL
SEQRES 15 A 230 LEU SER TYR THR ASN GLU ILE LEU ILE THR ILE SER GLY
SEQRES 16 A 230 ASP SER GLY ALA VAL LEU GLN SER LEU THR ALA ALA ARG
SEQRES 17 A 230 LYS ALA GLY LEU SER ILE LEU ARG SER MET GLY GLN ASP
SEQRES 18 A 230 PRO VAL SER MET SER LYS PRO THR PHE
FORMUL 2 HOH *(H2 O)
HELIX 1 1 ASP A 98 HIS A 102 5 5
HELIX 2 2 ALA A 123 GLY A 136 1 14
HELIX 3 3 ASP A 166 GLY A 186 1 21
HELIX 4 4 SER A 205 GLY A 213 1 9
HELIX 5 5 PRO A 227 ALA A 242 1 16
HELIX 6 6 ASP A 270 MET A 292 1 23
SHEET 1 A 5 PHE A 81 ALA A 85 0
SHEET 2 A 5 THR A 89 ILE A 94 -1 O GLY A 91 N GLY A 83
SHEET 3 A 5 SER A 113 ALA A 119 -1 O ILE A 116 N LEU A 92
SHEET 4 A 5 ILE A 158 ALA A 164 -1 O LEU A 162 N GLY A 115
SHEET 5 A 5 GLU A 140 GLU A 145 -1 N THR A 143 O VAL A 161
SHEET 1 B 5 VAL A 188 CYS A 191 0
SHEET 2 B 5 GLY A 194 THR A 201 -1 O LEU A 196 N TYR A 189
SHEET 3 B 5 ALA A 219 ALA A 226 -1 O PHE A 220 N THR A 201
SHEET 4 B 5 ILE A 263 GLY A 269 -1 O ILE A 267 N GLY A 221
SHEET 5 B 5 LYS A 245 GLY A 250 -1 N ILE A 247 O THR A 266
CISPEP 1 GLY A 83 THR A 84 0 -24.37
CISPEP 2 PRO A 147 ARG A 148 0 -12.17
CISPEP 3 THR A 150 LYS A 151 0 10.39
CISPEP 4 LYS A 151 GLY A 152 0 -25.44
CISPEP 5 GLY A 152 GLY A 153 0 -14.98
CISPEP 6 GLY A 153 ALA A 154 0 -3.07
CISPEP 7 HIS A 156 GLY A 157 0 15.16
CISPEP 8 ALA A 226 PRO A 227 0 -1.22
CRYST1 173.410 173.410 173.410 90.00 90.00 90.00 I 21 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 0.005767 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005767 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005767 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
