HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 28-JUN-02 1M3S
TITLE CRYSTAL STRUCTURE OF YCKF FROM BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN YCKF;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: YCKF;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, MIDWEST
KEYWDS 2 CENTER FOR STRUCTURAL GENOMICS, MCSG, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SANISHVILI,R.WU,D.E.KIM,F.COLLART,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 7 14-FEB-24 1M3S 1 SEQADV
REVDAT 6 24-JUL-19 1M3S 1 REMARK
REVDAT 5 11-OCT-17 1M3S 1 REMARK
REVDAT 4 24-FEB-09 1M3S 1 VERSN
REVDAT 3 18-JAN-05 1M3S 1 AUTHOR KEYWDS REMARK
REVDAT 2 28-SEP-04 1M3S 1 JRNL
REVDAT 1 21-JAN-03 1M3S 0
JRNL AUTH R.SANISHVILI,R.WU,D.E.KIM,J.D.WATSON,F.COLLART,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF BACILLUS SUBTILIS YCKF: STRUCTURAL AND
JRNL TITL 2 FUNCTIONAL EVOLUTION.
JRNL REF J.STRUCT.BIOL. V. 148 98 2004
JRNL REFN ISSN 1047-8477
JRNL PMID 15363790
JRNL DOI 10.1016/J.JSB.2004.04.006
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 26023
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) : 0.187
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1389
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1745
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2020
REMARK 3 BIN FREE R VALUE SET COUNT : 101
REMARK 3 BIN FREE R VALUE : 0.2690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2724
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 203
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.45000
REMARK 3 B22 (A**2) : 0.45000
REMARK 3 B33 (A**2) : -0.68000
REMARK 3 B12 (A**2) : 0.23000
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): 0.175
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.154
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.109
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.878
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2861 ; 0.024 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2646 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3873 ; 1.814 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6209 ; 1.176 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 378 ; 5.646 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 543 ;19.146 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 457 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3158 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 504 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 600 ; 0.244 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2913 ; 0.268 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1607 ; 0.092 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 127 ; 0.178 ; 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): 25 ; 0.246 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 132 ; 0.284 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.207 ; 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): 1835 ; 1.129 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2947 ; 1.875 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1026 ; 2.941 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 917 ; 4.486 ; 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 : 3
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 0 A 185
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1916 51.8158 16.3063
REMARK 3 T TENSOR
REMARK 3 T11: 0.1880 T22: 0.0094
REMARK 3 T33: 0.1331 T12: -0.0354
REMARK 3 T13: 0.0849 T23: 0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 2.5311 L22: 1.8310
REMARK 3 L33: 2.6660 L12: 0.2270
REMARK 3 L13: 0.0972 L23: 0.3202
REMARK 3 S TENSOR
REMARK 3 S11: 0.1483 S12: 0.0400 S13: 0.3375
REMARK 3 S21: -0.1638 S22: -0.0291 S23: -0.2212
REMARK 3 S31: -0.3502 S32: 0.1268 S33: -0.1192
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 0 B 185
REMARK 3 ORIGIN FOR THE GROUP (A): 13.0884 18.3364 8.9573
REMARK 3 T TENSOR
REMARK 3 T11: 0.2748 T22: 0.0406
REMARK 3 T33: 0.1784 T12: 0.0418
REMARK 3 T13: -0.0494 T23: -0.0601
REMARK 3 L TENSOR
REMARK 3 L11: 3.3124 L22: 1.3045
REMARK 3 L33: 1.6703 L12: 0.4034
REMARK 3 L13: -0.4512 L23: -0.1724
REMARK 3 S TENSOR
REMARK 3 S11: 0.1409 S12: 0.2074 S13: -0.4953
REMARK 3 S21: -0.2093 S22: -0.0337 S23: 0.0100
REMARK 3 S31: 0.3463 S32: 0.0926 S33: -0.1073
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 186 B 203
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8071 35.7110 12.5807
REMARK 3 T TENSOR
REMARK 3 T11: 0.2486 T22: 0.2028
REMARK 3 T33: 0.2320 T12: -0.0022
REMARK 3 T13: 0.0224 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 1.0395 L22: 1.1398
REMARK 3 L33: 0.8797 L12: 0.1262
REMARK 3 L13: 0.0962 L23: 0.1678
REMARK 3 S TENSOR
REMARK 3 S11: 0.1100 S12: 0.0873 S13: -0.0222
REMARK 3 S21: -0.2398 S22: -0.0561 S23: -0.0435
REMARK 3 S31: -0.0380 S32: -0.0066 S33: -0.0539
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 1M3S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000016561.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAR-02; 07-JUN-02
REMARK 200 TEMPERATURE (KELVIN) : 110; 110
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 19-ID; 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795, 0.9793, 0.9537; 1.0332
REMARK 200 MONOCHROMATOR : SI(111); SI(111)
REMARK 200 OPTICS : SAGITALLY FOCUSING DOUBLE
REMARK 200 CRYSTAL MONOCHROMATOR AND
REMARK 200 VERTICALLY FOCUSING MIRROR;
REMARK 200 SAGITALLY FOCUSING DOUBLE
REMARK 200 CRYSTAL MONOCHROMATOR AND
REMARK 200 VERTICALLY FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE; CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, D*TREK, DTDISPLAY
REMARK 200 DATA SCALING SOFTWARE : D*TREK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28572
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.46800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, NA CACODYLATE, CA ACETATE,
REMARK 280 GLYCEROL, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 163.70667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 81.85333
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 122.78000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 40.92667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 204.63333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 163.70667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 81.85333
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 40.92667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 122.78000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 204.63333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -114.0 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 0.500000 -0.866025 0.000000 36.04000
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 62.42311
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 40.92667
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 0.500000 -0.866025 0.000000 36.04000
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 62.42311
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 40.92667
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 GLN A 136
REMARK 465 SER A 137
REMARK 465 ASN A 138
REMARK 465 GLY A 139
REMARK 465 SER A 140
REMARK 465 ASP B 173
REMARK 465 SER B 174
REMARK 465 GLU B 175
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 LYS A 2 CD CE NZ
REMARK 470 GLU A 24 CG CD OE1 OE2
REMARK 470 LYS B 121 CG CD CE NZ
REMARK 470 LYS B 134 CG CD CE NZ
REMARK 470 THR B 176 OG1 CG2
REMARK 470 MET B 177 CG SD CE
REMARK 470 PHE B 178 CG CD1 CD2 CE1 CE2 CZ
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 ASP A 135 CB - CG - OD2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 ASP A 160 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 57 NE - CZ - NH2 ANGL. DEV. = -4.4 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 ALA A 19 18.63 -64.27
REMARK 500 MET A 147 -77.67 -18.36
REMARK 500 MET B 1 142.70 178.10
REMARK 500 GLU B 78 135.18 -39.63
REMARK 500 MET B 147 -140.15 47.78
REMARK 500 LYS B 170 -155.54 -102.94
REMARK 500 PHE B 178 66.17 -66.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC1056 RELATED DB: TARGETDB
DBREF 1M3S A 1 185 UNP P42404 HXLB_BACSU 1 185
DBREF 1M3S B 1 185 UNP P42404 HXLB_BACSU 1 185
SEQADV 1M3S GLY A 0 UNP P42404 EXPRESSION TAG
SEQADV 1M3S GLY B 0 UNP P42404 EXPRESSION TAG
SEQRES 1 A 186 GLY MET LYS THR THR GLU TYR VAL ALA GLU ILE LEU ASN
SEQRES 2 A 186 GLU LEU HIS ASN SER ALA ALA TYR ILE SER ASN GLU GLU
SEQRES 3 A 186 ALA ASP GLN LEU ALA ASP HIS ILE LEU SER SER HIS GLN
SEQRES 4 A 186 ILE PHE THR ALA GLY ALA GLY ARG SER GLY LEU MET ALA
SEQRES 5 A 186 LYS SER PHE ALA MET ARG LEU MET HIS MET GLY PHE ASN
SEQRES 6 A 186 ALA HIS ILE VAL GLY GLU ILE LEU THR PRO PRO LEU ALA
SEQRES 7 A 186 GLU GLY ASP LEU VAL ILE ILE GLY SER GLY SER GLY GLU
SEQRES 8 A 186 THR LYS SER LEU ILE HIS THR ALA ALA LYS ALA LYS SER
SEQRES 9 A 186 LEU HIS GLY ILE VAL ALA ALA LEU THR ILE ASN PRO GLU
SEQRES 10 A 186 SER SER ILE GLY LYS GLN ALA ASP LEU ILE ILE ARG MET
SEQRES 11 A 186 PRO GLY SER PRO LYS ASP GLN SER ASN GLY SER TYR LYS
SEQRES 12 A 186 THR ILE GLN PRO MET GLY SER LEU PHE GLU GLN THR LEU
SEQRES 13 A 186 LEU LEU PHE TYR ASP ALA VAL ILE LEU LYS LEU MET GLU
SEQRES 14 A 186 LYS LYS GLY LEU ASP SER GLU THR MET PHE THR HIS HIS
SEQRES 15 A 186 ALA ASN LEU GLU
SEQRES 1 B 186 GLY MET LYS THR THR GLU TYR VAL ALA GLU ILE LEU ASN
SEQRES 2 B 186 GLU LEU HIS ASN SER ALA ALA TYR ILE SER ASN GLU GLU
SEQRES 3 B 186 ALA ASP GLN LEU ALA ASP HIS ILE LEU SER SER HIS GLN
SEQRES 4 B 186 ILE PHE THR ALA GLY ALA GLY ARG SER GLY LEU MET ALA
SEQRES 5 B 186 LYS SER PHE ALA MET ARG LEU MET HIS MET GLY PHE ASN
SEQRES 6 B 186 ALA HIS ILE VAL GLY GLU ILE LEU THR PRO PRO LEU ALA
SEQRES 7 B 186 GLU GLY ASP LEU VAL ILE ILE GLY SER GLY SER GLY GLU
SEQRES 8 B 186 THR LYS SER LEU ILE HIS THR ALA ALA LYS ALA LYS SER
SEQRES 9 B 186 LEU HIS GLY ILE VAL ALA ALA LEU THR ILE ASN PRO GLU
SEQRES 10 B 186 SER SER ILE GLY LYS GLN ALA ASP LEU ILE ILE ARG MET
SEQRES 11 B 186 PRO GLY SER PRO LYS ASP GLN SER ASN GLY SER TYR LYS
SEQRES 12 B 186 THR ILE GLN PRO MET GLY SER LEU PHE GLU GLN THR LEU
SEQRES 13 B 186 LEU LEU PHE TYR ASP ALA VAL ILE LEU LYS LEU MET GLU
SEQRES 14 B 186 LYS LYS GLY LEU ASP SER GLU THR MET PHE THR HIS HIS
SEQRES 15 B 186 ALA ASN LEU GLU
FORMUL 3 HOH *203(H2 O)
HELIX 1 1 LYS A 2 ALA A 19 1 18
HELIX 2 2 SER A 22 SER A 36 1 15
HELIX 3 3 ALA A 44 MET A 61 1 18
HELIX 4 4 THR A 91 LEU A 104 1 14
HELIX 5 5 SER A 117 ALA A 123 1 7
HELIX 6 6 GLY A 148 LYS A 170 1 23
HELIX 7 7 LYS B 2 ILE B 21 1 20
HELIX 8 8 SER B 22 SER B 36 1 15
HELIX 9 9 ALA B 44 MET B 61 1 18
HELIX 10 10 THR B 91 LEU B 104 1 14
HELIX 11 11 SER B 117 ALA B 123 1 7
HELIX 12 12 SER B 132 ASN B 138 1 7
HELIX 13 13 GLY B 148 LYS B 170 1 23
SHEET 1 A 5 ALA A 65 ILE A 67 0
SHEET 2 A 5 ILE A 39 ALA A 42 1 N THR A 41 O HIS A 66
SHEET 3 A 5 LEU A 81 GLY A 85 1 O LEU A 81 N PHE A 40
SHEET 4 A 5 ILE A 107 THR A 112 1 O ALA A 109 N ILE A 84
SHEET 5 A 5 LEU A 125 ARG A 128 1 O LEU A 125 N ALA A 110
SHEET 1 B 5 ALA B 65 ILE B 67 0
SHEET 2 B 5 ILE B 39 ALA B 42 1 N ILE B 39 O HIS B 66
SHEET 3 B 5 LEU B 81 GLY B 85 1 O ILE B 83 N PHE B 40
SHEET 4 B 5 ILE B 107 THR B 112 1 O ILE B 107 N VAL B 82
SHEET 5 B 5 LEU B 125 ARG B 128 1 O ILE B 127 N ALA B 110
CRYST1 72.080 72.080 245.560 90.00 90.00 120.00 P 65 2 2 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 0.013873 0.008010 0.000000 0.00000
SCALE2 0.000000 0.016020 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004072 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
