HEADER LYASE 17-OCT-08 3EXT
TITLE CRYSTAL STRUCTURE OF KGPDC FROM STREPTOCOCCUS MUTANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RMPD (HEXULOSE-6-PHOSPHATE SYNTHASE);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 3-KETO-L-GULONATE 6-PHOSPHATE DECARBOXYLASE;
COMPND 5 EC: 4.1.1.85;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS MUTANS;
SOURCE 3 ORGANISM_TAXID: 1309;
SOURCE 4 GENE: ULAD;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS BETA BARREL, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.LIU,G.L.LI,L.F.LI,X.D.SU
REVDAT 4 01-NOV-23 3EXT 1 REMARK LINK
REVDAT 3 23-MAY-18 3EXT 1 REMARK
REVDAT 2 13-JUL-11 3EXT 1 VERSN
REVDAT 1 25-AUG-09 3EXT 0
JRNL AUTH G.L.LI,X.LIU,J.NAN,E.BROSTROMER,L.F.LI,X.D.SU
JRNL TITL OPEN-CLOSED CONFORMATIONAL CHANGE REVEALED BY THE CRYSTAL
JRNL TITL 2 STRUCTURES OF 3-KETO-L-GULONATE 6-PHOSPHATE DECARBOXYLASE
JRNL TITL 3 FROM STREPTOCOCCUS MUTANS
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 381 429 2009
JRNL REFN ISSN 0006-291X
JRNL PMID 19222992
JRNL DOI 10.1016/J.BBRC.2009.02.049
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 19853
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1042
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1429
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1579
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 82
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 37.45
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.41000
REMARK 3 B22 (A**2) : 0.41000
REMARK 3 B33 (A**2) : -0.82000
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): 0.144
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.131
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.565
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1603 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2173 ; 1.537 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 209 ; 6.073 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 65 ;34.259 ;25.077
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 269 ;12.357 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;22.250 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 254 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1188 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 701 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1104 ; 0.298 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 81 ; 0.106 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.071 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 28 ; 0.138 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 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): 1074 ; 0.958 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1655 ; 1.455 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 629 ; 2.303 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 518 ; 3.267 ; 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 : 4
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 4 A 129
REMARK 3 ORIGIN FOR THE GROUP (A): 10.8446 39.2063 26.0476
REMARK 3 T TENSOR
REMARK 3 T11: 0.0410 T22: 0.0285
REMARK 3 T33: 0.0897 T12: 0.0383
REMARK 3 T13: 0.0149 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 0.5861 L22: 1.0382
REMARK 3 L33: 1.5716 L12: -0.7766
REMARK 3 L13: -0.0315 L23: -0.0775
REMARK 3 S TENSOR
REMARK 3 S11: 0.2265 S12: -0.0031 S13: 0.0972
REMARK 3 S21: -0.1441 S22: -0.0595 S23: -0.0253
REMARK 3 S31: 0.0650 S32: 0.2027 S33: -0.1670
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 130 A 155
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3148 33.6044 12.2769
REMARK 3 T TENSOR
REMARK 3 T11: 0.1967 T22: 0.0981
REMARK 3 T33: -0.0181 T12: 0.1925
REMARK 3 T13: -0.0077 T23: -0.0418
REMARK 3 L TENSOR
REMARK 3 L11: 0.2526 L22: 5.6287
REMARK 3 L33: 1.6176 L12: -0.1032
REMARK 3 L13: -0.6093 L23: 1.1590
REMARK 3 S TENSOR
REMARK 3 S11: 0.4744 S12: 0.3743 S13: -0.0335
REMARK 3 S21: -0.6760 S22: -0.3519 S23: -0.0762
REMARK 3 S31: 0.0830 S32: 0.1282 S33: -0.1225
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 156 A 192
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0385 26.9224 12.2115
REMARK 3 T TENSOR
REMARK 3 T11: 0.1911 T22: 0.1149
REMARK 3 T33: -0.0149 T12: 0.2336
REMARK 3 T13: -0.0378 T23: -0.0851
REMARK 3 L TENSOR
REMARK 3 L11: 1.6969 L22: 3.7285
REMARK 3 L33: 1.2463 L12: -0.0006
REMARK 3 L13: -0.2257 L23: -0.4229
REMARK 3 S TENSOR
REMARK 3 S11: 0.4842 S12: 0.2566 S13: -0.1516
REMARK 3 S21: -0.5028 S22: -0.3688 S23: -0.1180
REMARK 3 S31: 0.2778 S32: 0.1520 S33: -0.1154
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 193 A 221
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5620 19.5656 25.8154
REMARK 3 T TENSOR
REMARK 3 T11: 0.1727 T22: -0.0064
REMARK 3 T33: 0.1081 T12: 0.1539
REMARK 3 T13: -0.0903 T23: -0.1149
REMARK 3 L TENSOR
REMARK 3 L11: 3.0655 L22: 3.5750
REMARK 3 L33: 3.1530 L12: -2.5279
REMARK 3 L13: -2.5771 L23: 0.9125
REMARK 3 S TENSOR
REMARK 3 S11: 0.1235 S12: 0.1258 S13: -0.1619
REMARK 3 S21: -0.0522 S22: -0.1751 S23: 0.3364
REMARK 3 S31: 0.5644 S32: 0.3367 S33: 0.0517
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 3EXT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049901.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9074
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20739
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.34500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.300
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 1KV8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M KCL, 0.05M HEPES, PH7.5, 35%(V/V)
REMARK 280 PENTAERYTHRITOL PROPOXYLATE (5/4 PO/OH), VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 289K
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 41.89000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 41.89000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 85.81000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 41.89000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 41.89000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 85.81000
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 41.89000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 41.89000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 85.81000
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 41.89000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 41.89000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 85.81000
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 41.89000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 41.89000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 85.81000
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 41.89000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 41.89000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 85.81000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 41.89000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 41.89000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 85.81000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 41.89000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 41.89000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 85.81000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.7 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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 83.78000
REMARK 350 BIOMT3 2 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 HOH A 297 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 THR A 2
REMARK 465 LYS A 3
REMARK 465 ASP A 145
REMARK 465 ALA A 146
REMARK 465 LEU A 147
REMARK 465 LEU A 148
REMARK 465 ALA A 149
REMARK 465 GLY A 150
REMARK 465 GLU A 151
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 GLN A 4 CB CG CD OE1 NE2
REMARK 470 THR A 152 OG1 CG2
REMARK 470 LYS A 156 CG CD CE NZ
REMARK 470 GLU A 166 CG CD OE1 OE2
REMARK 470 ASP A 180 CG OD1 OD2
REMARK 470 LYS A 203 CG CD CE NZ
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 TRP A 153 70.81 40.61
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 222 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 35 OE2
REMARK 620 2 ASP A 64 OD2 90.2
REMARK 620 3 HOH A 301 O 95.2 92.0
REMARK 620 4 HOH A 302 O 87.8 174.4 82.9
REMARK 620 5 HOH A 303 O 92.6 89.1 172.1 96.3
REMARK 620 6 HOH A 304 O 171.9 96.5 89.2 86.0 82.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 222
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EXR RELATED DB: PDB
REMARK 900 RELATED ID: 3EXS RELATED DB: PDB
DBREF 3EXT A 1 221 UNP Q93DA8 Q93DA8_STRMU 1 221
SEQRES 1 A 221 MET THR LYS GLN LEU PRO ASN LEU GLN VAL ALA LEU ASP
SEQRES 2 A 221 HIS SER ASN LEU LYS GLY ALA ILE THR ALA ALA VAL SER
SEQRES 3 A 221 VAL GLY ASN GLU VAL ASP VAL ILE GLU ALA GLY THR VAL
SEQRES 4 A 221 CYS LEU LEU GLN VAL GLY SER GLU LEU VAL GLU VAL LEU
SEQRES 5 A 221 ARG SER LEU PHE PRO ASP LYS ILE ILE VAL ALA ASP THR
SEQRES 6 A 221 LYS CYS ALA ASP ALA GLY GLY THR VAL ALA LYS ASN ASN
SEQRES 7 A 221 ALA VAL ARG GLY ALA ASP TRP MET THR CYS ILE CYS SER
SEQRES 8 A 221 ALA THR ILE PRO THR MET LYS ALA ALA ARG LYS ALA ILE
SEQRES 9 A 221 GLU ASP ILE ASN PRO ASP LYS GLY GLU ILE GLN VAL GLU
SEQRES 10 A 221 LEU TYR GLY ASP TRP THR TYR ASP GLN ALA GLN GLN TRP
SEQRES 11 A 221 LEU ASP ALA GLY ILE SER GLN ALA ILE TYR HIS GLN SER
SEQRES 12 A 221 ARG ASP ALA LEU LEU ALA GLY GLU THR TRP GLY GLU LYS
SEQRES 13 A 221 ASP LEU ASN LYS VAL LYS LYS LEU ILE GLU MET GLY PHE
SEQRES 14 A 221 ARG VAL SER VAL THR GLY GLY LEU SER VAL ASP THR LEU
SEQRES 15 A 221 LYS LEU PHE GLU GLY VAL ASP VAL PHE THR PHE ILE ALA
SEQRES 16 A 221 GLY ARG GLY ILE THR GLU ALA LYS ASN PRO ALA GLY ALA
SEQRES 17 A 221 ALA ARG ALA PHE LYS ASP GLU ILE LYS ARG ILE TRP GLY
HET MG A 222 1
HETNAM MG MAGNESIUM ION
FORMUL 2 MG MG 2+
FORMUL 3 HOH *82(H2 O)
HELIX 1 1 ASN A 16 GLY A 28 1 13
HELIX 2 2 ASN A 29 VAL A 31 5 3
HELIX 3 3 GLY A 37 GLY A 45 1 9
HELIX 4 4 SER A 46 PHE A 56 1 11
HELIX 5 5 ALA A 70 VAL A 80 1 11
HELIX 6 6 THR A 93 ASN A 108 1 16
HELIX 7 7 THR A 123 ALA A 133 1 11
HELIX 8 8 GLY A 154 GLY A 168 1 15
HELIX 9 9 THR A 181 GLU A 186 5 6
HELIX 10 10 GLY A 196 GLU A 201 1 6
HELIX 11 11 ASN A 204 GLY A 221 1 18
SHEET 1 A 9 ASN A 7 LEU A 12 0
SHEET 2 A 9 VAL A 33 ALA A 36 1 O GLU A 35 N VAL A 10
SHEET 3 A 9 ILE A 60 CYS A 67 1 O VAL A 62 N ALA A 36
SHEET 4 A 9 TRP A 85 ILE A 89 1 O TRP A 85 N ALA A 63
SHEET 5 A 9 GLU A 113 GLU A 117 1 O GLU A 117 N CYS A 88
SHEET 6 A 9 GLN A 137 HIS A 141 1 O ILE A 139 N VAL A 116
SHEET 7 A 9 ARG A 170 THR A 174 1 O SER A 172 N TYR A 140
SHEET 8 A 9 THR A 192 ALA A 195 1 O ILE A 194 N VAL A 173
SHEET 9 A 9 ASN A 7 LEU A 12 1 N GLN A 9 O ALA A 195
LINK OE2 GLU A 35 MG MG A 222 1555 1555 2.12
LINK OD2 ASP A 64 MG MG A 222 1555 1555 1.93
LINK MG MG A 222 O HOH A 301 1555 1555 2.31
LINK MG MG A 222 O HOH A 302 1555 1555 2.34
LINK MG MG A 222 O HOH A 303 1555 1555 1.91
LINK MG MG A 222 O HOH A 304 1555 1555 2.14
SITE 1 AC1 6 GLU A 35 ASP A 64 HOH A 301 HOH A 302
SITE 2 AC1 6 HOH A 303 HOH A 304
CRYST1 83.780 83.780 171.620 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 0.011936 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011936 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005827 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
