HEADER LYASE 22-OCT-04 1WA3
TITLE MECHANISM OF THE CLASS I KDPG ALDOLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-KETO-3-DEOXY-6-PHOSPHOGLUCONATE ALDOLASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, 2-DEHYDRO-3-
COMPND 5 DEOXYPHOSPHOGLUCONATE ALDOLASE, 4-HYDROXY-2-OXOGLUTARATE ALDOLASE;
COMPND 6 EC: 4.1.2.14;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: SCHIFF BASE FORMED WITH PYRUVATE IN THE ACTIVE SITE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 ATCC: 43589;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28B;
SOURCE 9 OTHER_DETAILS: DSM 3109
KEYWDS KDPG, PYRUVATE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.W.B.FULLERTON,J.S.GRIFFITHS,A.B.MERKEL,N.J.WYMER,M.J.HUTCHINS,
AUTHOR 2 C.A.FIERKE,E.J.TOONE,J.H.NAISMITH
REVDAT 8 13-DEC-23 1WA3 1 REMARK
REVDAT 7 15-NOV-23 1WA3 1 REMARK LINK ATOM
REVDAT 6 23-OCT-13 1WA3 1 HEADER KEYWDS REMARK
REVDAT 5 13-JUL-11 1WA3 1 VERSN
REVDAT 4 24-FEB-09 1WA3 1 VERSN
REVDAT 3 22-MAR-06 1WA3 1 JRNL
REVDAT 2 18-JAN-06 1WA3 1 JRNL
REVDAT 1 26-JAN-05 1WA3 0
JRNL AUTH S.W.B.FULLERTON,J.S.GRIFFITHS,A.B.MERKEL,M.CHERIYAN,
JRNL AUTH 2 N.J.WYMER,M.J.HUTCHINS,C.A.FIERKE,E.J.TOONE,J.H.NAISMITH
JRNL TITL MECHANISM OF THE CLASS I KDPG ALDOLASE.
JRNL REF BIOORG.MED.CHEM. V. 14 3002 2006
JRNL REFN ISSN 0968-0896
JRNL PMID 16403639
JRNL DOI 10.1016/J.BMC.2005.12.022
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0007
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 3 NUMBER OF REFLECTIONS : 73594
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3900
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 25
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.94
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4320
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.10
REMARK 3 BIN R VALUE (WORKING SET) : 0.2140
REMARK 3 BIN FREE R VALUE SET COUNT : 201
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9203
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 306
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.04000
REMARK 3 B33 (A**2) : -0.06000
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): 0.198
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.170
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.116
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.840
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9437 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12705 ; 1.606 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1205 ; 5.244 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 336 ;37.805 ;25.179
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1738 ;18.334 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;18.371 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1463 ; 0.143 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6818 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4506 ; 0.214 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6487 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 450 ; 0.131 ; 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): 134 ; 0.256 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.395 ; 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): 6172 ; 1.112 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9687 ; 1.599 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3608 ; 2.775 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3018 ; 4.493 ; 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 : 6
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 2 A 203
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5560 33.7470 36.6010
REMARK 3 T TENSOR
REMARK 3 T11: 0.0036 T22: 0.0234
REMARK 3 T33: 0.0176 T12: 0.0077
REMARK 3 T13: 0.0065 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.0632 L22: 0.1482
REMARK 3 L33: 0.6474 L12: 0.0529
REMARK 3 L13: 0.0496 L23: 0.2882
REMARK 3 S TENSOR
REMARK 3 S11: -0.0031 S12: -0.0344 S13: -0.0010
REMARK 3 S21: -0.0791 S22: -0.0041 S23: 0.0192
REMARK 3 S31: -0.1652 S32: 0.0131 S33: 0.0072
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 2 B 203
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5560 33.7470 36.6010
REMARK 3 T TENSOR
REMARK 3 T11: 0.0036 T22: 0.0234
REMARK 3 T33: 0.0176 T12: 0.0077
REMARK 3 T13: 0.0065 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.0677 L22: 0.5472
REMARK 3 L33: 0.6993 L12: 0.0991
REMARK 3 L13: 0.0509 L23: 0.5790
REMARK 3 S TENSOR
REMARK 3 S11: 0.0118 S12: -0.0125 S13: -0.0333
REMARK 3 S21: 0.0345 S22: 0.0571 S23: -0.0237
REMARK 3 S31: 0.0139 S32: 0.1052 S33: -0.0689
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 : C 3 C 203
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5560 33.7470 36.6010
REMARK 3 T TENSOR
REMARK 3 T11: 0.0036 T22: 0.0234
REMARK 3 T33: 0.0176 T12: 0.0077
REMARK 3 T13: 0.0063 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.1059 L22: 2.5720
REMARK 3 L33: 0.0820 L12: 0.2136
REMARK 3 L13: -0.0012 L23: 0.4166
REMARK 3 S TENSOR
REMARK 3 S11: 0.2247 S12: -0.0699 S13: -0.0254
REMARK 3 S21: 0.8109 S22: -0.0905 S23: -0.2205
REMARK 3 S31: 0.5003 S32: -0.0246 S33: -0.1342
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 : D 2 D 204
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5560 33.7470 36.6010
REMARK 3 T TENSOR
REMARK 3 T11: 0.0036 T22: 0.0235
REMARK 3 T33: 0.0176 T12: 0.0074
REMARK 3 T13: 0.0065 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.2261 L22: 0.8971
REMARK 3 L33: 1.6082 L12: 0.4486
REMARK 3 L13: 0.5303 L23: 1.0017
REMARK 3 S TENSOR
REMARK 3 S11: 0.0857 S12: 0.0066 S13: -0.0692
REMARK 3 S21: 0.2523 S22: 0.2294 S23: -0.3473
REMARK 3 S31: 0.4178 S32: 0.0943 S33: -0.3151
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 2 E 203
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5560 33.7470 36.6010
REMARK 3 T TENSOR
REMARK 3 T11: 0.0036 T22: 0.0234
REMARK 3 T33: 0.0176 T12: 0.0076
REMARK 3 T13: 0.0065 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.1105 L22: 0.2055
REMARK 3 L33: 0.6692 L12: 0.0354
REMARK 3 L13: 0.1982 L23: 0.3103
REMARK 3 S TENSOR
REMARK 3 S11: 0.1058 S12: -0.0530 S13: -0.0274
REMARK 3 S21: 0.0002 S22: -0.0560 S23: -0.0034
REMARK 3 S31: -0.0317 S32: -0.0255 S33: -0.0499
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 3 F 203
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5560 33.7470 36.6010
REMARK 3 T TENSOR
REMARK 3 T11: 0.0036 T22: 0.0234
REMARK 3 T33: 0.0176 T12: 0.0077
REMARK 3 T13: 0.0065 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.4098 L22: 0.6612
REMARK 3 L33: 0.2825 L12: 0.1015
REMARK 3 L13: 0.1694 L23: 0.4096
REMARK 3 S TENSOR
REMARK 3 S11: 0.0402 S12: 0.0173 S13: -0.1752
REMARK 3 S21: 0.0131 S22: -0.0055 S23: -0.0701
REMARK 3 S31: -0.0302 S32: 0.0226 S33: -0.0347
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WA3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1290021345.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAR-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.932
REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220)
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 309752
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 32.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.07000
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) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.30000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 1EUA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.075M SODIUM ACETATE, 0.1M AMMONIUM
REMARK 280 SULPHATE, 28%W/V PEG4000, PH 4.60
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
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 50.55000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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
REMARK 350 BIOMOLECULE: 2
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: 5180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 THR A 204
REMARK 465 GLU A 205
REMARK 465 MET B 1
REMARK 465 THR B 204
REMARK 465 GLU B 205
REMARK 465 MET C 1
REMARK 465 LYS C 2
REMARK 465 THR C 204
REMARK 465 GLU C 205
REMARK 465 MET D 1
REMARK 465 GLU D 205
REMARK 465 MET E 1
REMARK 465 THR E 204
REMARK 465 GLU E 205
REMARK 465 MET F 1
REMARK 465 LYS F 2
REMARK 465 THR F 204
REMARK 465 GLU F 205
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 THR D 204 OG1 CG2
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 OD2 ASP B 187 O HOH B 2066 1.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG A 77 OE2 GLU A 198 1455 1.82
REMARK 500 NH1 ARG B 77 OD2 ASP B 162 1455 2.08
REMARK 500 OD1 ASN A 19 OD1 ASP C 187 2655 2.16
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 VAL A 13 CB - CA - C ANGL. DEV. = -11.7 DEGREES
REMARK 500 VAL A 172 CG1 - CB - CG2 ANGL. DEV. = 12.5 DEGREES
REMARK 500 VAL B 31 CG1 - CB - CG2 ANGL. DEV. = 10.7 DEGREES
REMARK 500 VAL B 172 CG1 - CB - CG2 ANGL. DEV. = 13.7 DEGREES
REMARK 500 LEU B 173 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 VAL C 111 CG1 - CB - CG2 ANGL. DEV. = 13.2 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 LYS B 11 -9.31 65.03
REMARK 500 LYS C 11 -7.15 70.65
REMARK 500 LYS D 11 -14.33 68.33
REMARK 500 LYS F 11 -4.99 72.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D2003 DISTANCE = 6.98 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR A 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR B 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR C 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR D 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR E 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR F 1204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VLW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 2-DEHYDRO-3- DEOXYPHOSPHOGLUCONATEALDOLASE/4-
REMARK 900 HYDROXY-2- OXOGLUTARATE ALDOLASE (TM0066) FROMTHERMOTOGA MARITIMA
REMARK 900 AT 2.30 A RESOLUTION
DBREF 1WA3 A 1 205 UNP Q9WXS1 Q9WXS1 1 205
DBREF 1WA3 B 1 205 UNP Q9WXS1 Q9WXS1 1 205
DBREF 1WA3 C 1 205 UNP Q9WXS1 Q9WXS1 1 205
DBREF 1WA3 D 1 205 UNP Q9WXS1 Q9WXS1 1 205
DBREF 1WA3 E 1 205 UNP Q9WXS1 Q9WXS1 1 205
DBREF 1WA3 F 1 205 UNP Q9WXS1 Q9WXS1 1 205
SEQRES 1 A 205 MET LYS MET GLU GLU LEU PHE LYS LYS HIS LYS ILE VAL
SEQRES 2 A 205 ALA VAL LEU ARG ALA ASN SER VAL GLU GLU ALA LYS GLU
SEQRES 3 A 205 LYS ALA LEU ALA VAL PHE GLU GLY GLY VAL HIS LEU ILE
SEQRES 4 A 205 GLU ILE THR PHE THR VAL PRO ASP ALA ASP THR VAL ILE
SEQRES 5 A 205 LYS GLU LEU SER PHE LEU LYS GLU LYS GLY ALA ILE ILE
SEQRES 6 A 205 GLY ALA GLY THR VAL THR SER VAL GLU GLN CYS ARG LYS
SEQRES 7 A 205 ALA VAL GLU SER GLY ALA GLU PHE ILE VAL SER PRO HIS
SEQRES 8 A 205 LEU ASP GLU GLU ILE SER GLN PHE CYS LYS GLU LYS GLY
SEQRES 9 A 205 VAL PHE TYR MET PRO GLY VAL MET THR PRO THR GLU LEU
SEQRES 10 A 205 VAL LYS ALA MET LYS LEU GLY HIS THR ILE LEU LYS LEU
SEQRES 11 A 205 PHE PRO GLY GLU VAL VAL GLY PRO GLN PHE VAL LYS ALA
SEQRES 12 A 205 MET LYS GLY PRO PHE PRO ASN VAL LYS PHE VAL PRO THR
SEQRES 13 A 205 GLY GLY VAL ASN LEU ASP ASN VAL CYS GLU TRP PHE LYS
SEQRES 14 A 205 ALA GLY VAL LEU ALA VAL GLY VAL GLY SER ALA LEU VAL
SEQRES 15 A 205 LYS GLY THR PRO ASP GLU VAL ARG GLU LYS ALA LYS ALA
SEQRES 16 A 205 PHE VAL GLU LYS ILE ARG GLY CYS THR GLU
SEQRES 1 B 205 MET LYS MET GLU GLU LEU PHE LYS LYS HIS LYS ILE VAL
SEQRES 2 B 205 ALA VAL LEU ARG ALA ASN SER VAL GLU GLU ALA LYS GLU
SEQRES 3 B 205 LYS ALA LEU ALA VAL PHE GLU GLY GLY VAL HIS LEU ILE
SEQRES 4 B 205 GLU ILE THR PHE THR VAL PRO ASP ALA ASP THR VAL ILE
SEQRES 5 B 205 LYS GLU LEU SER PHE LEU LYS GLU LYS GLY ALA ILE ILE
SEQRES 6 B 205 GLY ALA GLY THR VAL THR SER VAL GLU GLN CYS ARG LYS
SEQRES 7 B 205 ALA VAL GLU SER GLY ALA GLU PHE ILE VAL SER PRO HIS
SEQRES 8 B 205 LEU ASP GLU GLU ILE SER GLN PHE CYS LYS GLU LYS GLY
SEQRES 9 B 205 VAL PHE TYR MET PRO GLY VAL MET THR PRO THR GLU LEU
SEQRES 10 B 205 VAL LYS ALA MET LYS LEU GLY HIS THR ILE LEU LYS LEU
SEQRES 11 B 205 PHE PRO GLY GLU VAL VAL GLY PRO GLN PHE VAL LYS ALA
SEQRES 12 B 205 MET LYS GLY PRO PHE PRO ASN VAL LYS PHE VAL PRO THR
SEQRES 13 B 205 GLY GLY VAL ASN LEU ASP ASN VAL CYS GLU TRP PHE LYS
SEQRES 14 B 205 ALA GLY VAL LEU ALA VAL GLY VAL GLY SER ALA LEU VAL
SEQRES 15 B 205 LYS GLY THR PRO ASP GLU VAL ARG GLU LYS ALA LYS ALA
SEQRES 16 B 205 PHE VAL GLU LYS ILE ARG GLY CYS THR GLU
SEQRES 1 C 205 MET LYS MET GLU GLU LEU PHE LYS LYS HIS LYS ILE VAL
SEQRES 2 C 205 ALA VAL LEU ARG ALA ASN SER VAL GLU GLU ALA LYS GLU
SEQRES 3 C 205 LYS ALA LEU ALA VAL PHE GLU GLY GLY VAL HIS LEU ILE
SEQRES 4 C 205 GLU ILE THR PHE THR VAL PRO ASP ALA ASP THR VAL ILE
SEQRES 5 C 205 LYS GLU LEU SER PHE LEU LYS GLU LYS GLY ALA ILE ILE
SEQRES 6 C 205 GLY ALA GLY THR VAL THR SER VAL GLU GLN CYS ARG LYS
SEQRES 7 C 205 ALA VAL GLU SER GLY ALA GLU PHE ILE VAL SER PRO HIS
SEQRES 8 C 205 LEU ASP GLU GLU ILE SER GLN PHE CYS LYS GLU LYS GLY
SEQRES 9 C 205 VAL PHE TYR MET PRO GLY VAL MET THR PRO THR GLU LEU
SEQRES 10 C 205 VAL LYS ALA MET LYS LEU GLY HIS THR ILE LEU LYS LEU
SEQRES 11 C 205 PHE PRO GLY GLU VAL VAL GLY PRO GLN PHE VAL LYS ALA
SEQRES 12 C 205 MET LYS GLY PRO PHE PRO ASN VAL LYS PHE VAL PRO THR
SEQRES 13 C 205 GLY GLY VAL ASN LEU ASP ASN VAL CYS GLU TRP PHE LYS
SEQRES 14 C 205 ALA GLY VAL LEU ALA VAL GLY VAL GLY SER ALA LEU VAL
SEQRES 15 C 205 LYS GLY THR PRO ASP GLU VAL ARG GLU LYS ALA LYS ALA
SEQRES 16 C 205 PHE VAL GLU LYS ILE ARG GLY CYS THR GLU
SEQRES 1 D 205 MET LYS MET GLU GLU LEU PHE LYS LYS HIS LYS ILE VAL
SEQRES 2 D 205 ALA VAL LEU ARG ALA ASN SER VAL GLU GLU ALA LYS GLU
SEQRES 3 D 205 LYS ALA LEU ALA VAL PHE GLU GLY GLY VAL HIS LEU ILE
SEQRES 4 D 205 GLU ILE THR PHE THR VAL PRO ASP ALA ASP THR VAL ILE
SEQRES 5 D 205 LYS GLU LEU SER PHE LEU LYS GLU LYS GLY ALA ILE ILE
SEQRES 6 D 205 GLY ALA GLY THR VAL THR SER VAL GLU GLN CYS ARG LYS
SEQRES 7 D 205 ALA VAL GLU SER GLY ALA GLU PHE ILE VAL SER PRO HIS
SEQRES 8 D 205 LEU ASP GLU GLU ILE SER GLN PHE CYS LYS GLU LYS GLY
SEQRES 9 D 205 VAL PHE TYR MET PRO GLY VAL MET THR PRO THR GLU LEU
SEQRES 10 D 205 VAL LYS ALA MET LYS LEU GLY HIS THR ILE LEU LYS LEU
SEQRES 11 D 205 PHE PRO GLY GLU VAL VAL GLY PRO GLN PHE VAL LYS ALA
SEQRES 12 D 205 MET LYS GLY PRO PHE PRO ASN VAL LYS PHE VAL PRO THR
SEQRES 13 D 205 GLY GLY VAL ASN LEU ASP ASN VAL CYS GLU TRP PHE LYS
SEQRES 14 D 205 ALA GLY VAL LEU ALA VAL GLY VAL GLY SER ALA LEU VAL
SEQRES 15 D 205 LYS GLY THR PRO ASP GLU VAL ARG GLU LYS ALA LYS ALA
SEQRES 16 D 205 PHE VAL GLU LYS ILE ARG GLY CYS THR GLU
SEQRES 1 E 205 MET LYS MET GLU GLU LEU PHE LYS LYS HIS LYS ILE VAL
SEQRES 2 E 205 ALA VAL LEU ARG ALA ASN SER VAL GLU GLU ALA LYS GLU
SEQRES 3 E 205 LYS ALA LEU ALA VAL PHE GLU GLY GLY VAL HIS LEU ILE
SEQRES 4 E 205 GLU ILE THR PHE THR VAL PRO ASP ALA ASP THR VAL ILE
SEQRES 5 E 205 LYS GLU LEU SER PHE LEU LYS GLU LYS GLY ALA ILE ILE
SEQRES 6 E 205 GLY ALA GLY THR VAL THR SER VAL GLU GLN CYS ARG LYS
SEQRES 7 E 205 ALA VAL GLU SER GLY ALA GLU PHE ILE VAL SER PRO HIS
SEQRES 8 E 205 LEU ASP GLU GLU ILE SER GLN PHE CYS LYS GLU LYS GLY
SEQRES 9 E 205 VAL PHE TYR MET PRO GLY VAL MET THR PRO THR GLU LEU
SEQRES 10 E 205 VAL LYS ALA MET LYS LEU GLY HIS THR ILE LEU LYS LEU
SEQRES 11 E 205 PHE PRO GLY GLU VAL VAL GLY PRO GLN PHE VAL LYS ALA
SEQRES 12 E 205 MET LYS GLY PRO PHE PRO ASN VAL LYS PHE VAL PRO THR
SEQRES 13 E 205 GLY GLY VAL ASN LEU ASP ASN VAL CYS GLU TRP PHE LYS
SEQRES 14 E 205 ALA GLY VAL LEU ALA VAL GLY VAL GLY SER ALA LEU VAL
SEQRES 15 E 205 LYS GLY THR PRO ASP GLU VAL ARG GLU LYS ALA LYS ALA
SEQRES 16 E 205 PHE VAL GLU LYS ILE ARG GLY CYS THR GLU
SEQRES 1 F 205 MET LYS MET GLU GLU LEU PHE LYS LYS HIS LYS ILE VAL
SEQRES 2 F 205 ALA VAL LEU ARG ALA ASN SER VAL GLU GLU ALA LYS GLU
SEQRES 3 F 205 LYS ALA LEU ALA VAL PHE GLU GLY GLY VAL HIS LEU ILE
SEQRES 4 F 205 GLU ILE THR PHE THR VAL PRO ASP ALA ASP THR VAL ILE
SEQRES 5 F 205 LYS GLU LEU SER PHE LEU LYS GLU LYS GLY ALA ILE ILE
SEQRES 6 F 205 GLY ALA GLY THR VAL THR SER VAL GLU GLN CYS ARG LYS
SEQRES 7 F 205 ALA VAL GLU SER GLY ALA GLU PHE ILE VAL SER PRO HIS
SEQRES 8 F 205 LEU ASP GLU GLU ILE SER GLN PHE CYS LYS GLU LYS GLY
SEQRES 9 F 205 VAL PHE TYR MET PRO GLY VAL MET THR PRO THR GLU LEU
SEQRES 10 F 205 VAL LYS ALA MET LYS LEU GLY HIS THR ILE LEU LYS LEU
SEQRES 11 F 205 PHE PRO GLY GLU VAL VAL GLY PRO GLN PHE VAL LYS ALA
SEQRES 12 F 205 MET LYS GLY PRO PHE PRO ASN VAL LYS PHE VAL PRO THR
SEQRES 13 F 205 GLY GLY VAL ASN LEU ASP ASN VAL CYS GLU TRP PHE LYS
SEQRES 14 F 205 ALA GLY VAL LEU ALA VAL GLY VAL GLY SER ALA LEU VAL
SEQRES 15 F 205 LYS GLY THR PRO ASP GLU VAL ARG GLU LYS ALA LYS ALA
SEQRES 16 F 205 PHE VAL GLU LYS ILE ARG GLY CYS THR GLU
HET PYR A1204 5
HET SO4 A1205 5
HET PYR B1204 5
HET SO4 B1205 5
HET PYR C1204 5
HET SO4 C1205 5
HET PYR D1205 5
HET SO4 D1206 5
HET PYR E1204 5
HET SO4 E1205 5
HET PYR F1204 5
HET SO4 F1205 5
HETNAM PYR PYRUVIC ACID
HETNAM SO4 SULFATE ION
FORMUL 7 PYR 6(C3 H4 O3)
FORMUL 8 SO4 6(O4 S 2-)
FORMUL 19 HOH *306(H2 O)
HELIX 1 1 LYS A 2 LYS A 11 1 10
HELIX 2 2 SER A 20 GLY A 34 1 15
HELIX 3 3 ASP A 47 LEU A 55 1 9
HELIX 4 4 LEU A 55 LYS A 61 1 7
HELIX 5 5 SER A 72 GLY A 83 1 12
HELIX 6 6 ASP A 93 GLY A 104 1 12
HELIX 7 7 THR A 113 LEU A 123 1 11
HELIX 8 8 PRO A 132 GLY A 146 1 15
HELIX 9 9 ASN A 163 GLY A 171 1 9
HELIX 10 10 GLY A 178 LYS A 183 1 6
HELIX 11 11 THR A 185 CYS A 203 1 19
HELIX 12 12 LYS B 2 LYS B 11 1 10
HELIX 13 13 SER B 20 GLY B 34 1 15
HELIX 14 14 ASP B 47 LEU B 55 1 9
HELIX 15 15 SER B 56 GLY B 62 5 7
HELIX 16 16 SER B 72 SER B 82 1 11
HELIX 17 17 ASP B 93 GLY B 104 1 12
HELIX 18 18 THR B 113 LEU B 123 1 11
HELIX 19 19 PRO B 132 GLY B 146 1 15
HELIX 20 20 ASN B 163 GLY B 171 1 9
HELIX 21 21 GLY B 178 LYS B 183 1 6
HELIX 22 22 THR B 185 CYS B 203 1 19
HELIX 23 23 MET C 3 LYS C 11 1 9
HELIX 24 24 SER C 20 GLY C 34 1 15
HELIX 25 25 ASP C 47 SER C 56 1 10
HELIX 26 26 PHE C 57 GLY C 62 5 6
HELIX 27 27 SER C 72 SER C 82 1 11
HELIX 28 28 ASP C 93 GLY C 104 1 12
HELIX 29 29 THR C 113 LEU C 123 1 11
HELIX 30 30 PRO C 132 GLY C 146 1 15
HELIX 31 31 ASN C 163 GLY C 171 1 9
HELIX 32 32 GLY C 178 LYS C 183 1 6
HELIX 33 33 THR C 185 GLY C 202 1 18
HELIX 34 34 LYS D 2 LYS D 11 1 10
HELIX 35 35 SER D 20 GLY D 34 1 15
HELIX 36 36 ASP D 47 LEU D 55 1 9
HELIX 37 37 LEU D 55 LYS D 61 1 7
HELIX 38 38 SER D 72 SER D 82 1 11
HELIX 39 39 ASP D 93 GLY D 104 1 12
HELIX 40 40 THR D 113 LEU D 123 1 11
HELIX 41 41 PRO D 132 GLY D 137 1 6
HELIX 42 42 GLY D 137 GLY D 146 1 10
HELIX 43 43 ASN D 163 ALA D 170 1 8
HELIX 44 44 GLY D 178 LYS D 183 1 6
HELIX 45 45 THR D 185 THR D 204 1 20
HELIX 46 46 LYS E 2 LYS E 11 1 10
HELIX 47 47 SER E 20 GLY E 34 1 15
HELIX 48 48 ASP E 47 LEU E 55 1 9
HELIX 49 49 LEU E 55 GLU E 60 1 6
HELIX 50 50 SER E 72 SER E 82 1 11
HELIX 51 51 ASP E 93 GLY E 104 1 12
HELIX 52 52 THR E 113 LEU E 123 1 11
HELIX 53 53 PRO E 132 GLY E 137 1 6
HELIX 54 54 GLY E 137 LYS E 145 1 9
HELIX 55 55 ASN E 163 ALA E 170 1 8
HELIX 56 56 GLY E 178 LYS E 183 1 6
HELIX 57 57 THR E 185 CYS E 203 1 19
HELIX 58 58 MET F 3 LYS F 11 1 9
HELIX 59 59 SER F 20 GLY F 35 1 16
HELIX 60 60 ASP F 47 LEU F 55 1 9
HELIX 61 61 SER F 56 LYS F 61 1 6
HELIX 62 62 SER F 72 SER F 82 1 11
HELIX 63 63 ASP F 93 GLY F 104 1 12
HELIX 64 64 THR F 113 LEU F 123 1 11
HELIX 65 65 PRO F 132 GLY F 146 1 15
HELIX 66 66 ASN F 163 GLY F 171 1 9
HELIX 67 67 GLY F 178 LYS F 183 1 6
HELIX 68 68 THR F 185 GLY F 202 1 18
SHEET 1 AA 4 ILE A 64 GLY A 68 0
SHEET 2 AA 4 LEU A 38 THR A 42 1 O ILE A 39 N GLY A 66
SHEET 3 AA 4 ILE A 12 LEU A 16 1 O ILE A 12 N LEU A 38
SHEET 4 AA 4 VAL A 175 VAL A 177 1 O VAL A 175 N VAL A 13
SHEET 1 AB 2 PHE A 86 VAL A 88 0
SHEET 2 AB 2 PHE A 106 MET A 108 1 O PHE A 106 N ILE A 87
SHEET 1 AC 3 GLY A 110 VAL A 111 0
SHEET 2 AC 3 ILE A 127 LEU A 130 1 O LYS A 129 N VAL A 111
SHEET 3 AC 3 LYS A 152 PRO A 155 1 O LYS A 152 N LEU A 128
SHEET 1 BA 4 ILE B 64 GLY B 68 0
SHEET 2 BA 4 LEU B 38 THR B 42 1 O ILE B 39 N GLY B 66
SHEET 3 BA 4 ILE B 12 LEU B 16 1 O ILE B 12 N LEU B 38
SHEET 4 BA 4 VAL B 175 VAL B 177 1 O VAL B 175 N VAL B 13
SHEET 1 BB 2 PHE B 86 VAL B 88 0
SHEET 2 BB 2 PHE B 106 MET B 108 1 O PHE B 106 N ILE B 87
SHEET 1 BC 3 GLY B 110 VAL B 111 0
SHEET 2 BC 3 ILE B 127 LEU B 130 1 O LYS B 129 N VAL B 111
SHEET 3 BC 3 LYS B 152 PRO B 155 1 O LYS B 152 N LEU B 128
SHEET 1 CA 4 ILE C 64 GLY C 68 0
SHEET 2 CA 4 LEU C 38 THR C 42 1 O ILE C 39 N GLY C 66
SHEET 3 CA 4 ILE C 12 LEU C 16 1 O ILE C 12 N LEU C 38
SHEET 4 CA 4 VAL C 175 VAL C 177 1 O VAL C 175 N VAL C 13
SHEET 1 CB 2 PHE C 86 VAL C 88 0
SHEET 2 CB 2 PHE C 106 MET C 108 1 O PHE C 106 N ILE C 87
SHEET 1 CC 3 GLY C 110 VAL C 111 0
SHEET 2 CC 3 ILE C 127 LEU C 130 1 O LYS C 129 N VAL C 111
SHEET 3 CC 3 LYS C 152 PRO C 155 1 O LYS C 152 N LEU C 128
SHEET 1 DA 4 ILE D 64 GLY D 68 0
SHEET 2 DA 4 LEU D 38 THR D 42 1 O ILE D 39 N GLY D 66
SHEET 3 DA 4 ILE D 12 LEU D 16 1 O ILE D 12 N LEU D 38
SHEET 4 DA 4 VAL D 175 VAL D 177 1 O VAL D 175 N VAL D 13
SHEET 1 DB 2 PHE D 86 VAL D 88 0
SHEET 2 DB 2 PHE D 106 MET D 108 1 O PHE D 106 N ILE D 87
SHEET 1 DC 3 GLY D 110 VAL D 111 0
SHEET 2 DC 3 ILE D 127 LEU D 130 1 O LYS D 129 N VAL D 111
SHEET 3 DC 3 LYS D 152 PRO D 155 1 O LYS D 152 N LEU D 128
SHEET 1 EA 4 ILE E 64 GLY E 68 0
SHEET 2 EA 4 LEU E 38 THR E 42 1 O ILE E 39 N GLY E 66
SHEET 3 EA 4 ILE E 12 LEU E 16 1 O ILE E 12 N LEU E 38
SHEET 4 EA 4 VAL E 175 VAL E 177 1 O VAL E 175 N VAL E 13
SHEET 1 EB 2 PHE E 86 VAL E 88 0
SHEET 2 EB 2 PHE E 106 MET E 108 1 O PHE E 106 N ILE E 87
SHEET 1 EC 3 GLY E 110 VAL E 111 0
SHEET 2 EC 3 ILE E 127 LEU E 130 1 O LYS E 129 N VAL E 111
SHEET 3 EC 3 LYS E 152 PRO E 155 1 O LYS E 152 N LEU E 128
SHEET 1 FA 4 ILE F 64 GLY F 68 0
SHEET 2 FA 4 LEU F 38 THR F 42 1 O ILE F 39 N GLY F 66
SHEET 3 FA 4 ILE F 12 LEU F 16 1 O ILE F 12 N LEU F 38
SHEET 4 FA 4 VAL F 175 VAL F 177 1 O VAL F 175 N VAL F 13
SHEET 1 FB 2 PHE F 86 VAL F 88 0
SHEET 2 FB 2 PHE F 106 MET F 108 1 O PHE F 106 N ILE F 87
SHEET 1 FC 3 GLY F 110 VAL F 111 0
SHEET 2 FC 3 ILE F 127 LEU F 130 1 O LYS F 129 N VAL F 111
SHEET 3 FC 3 LYS F 152 PRO F 155 1 O LYS F 152 N LEU F 128
SSBOND 1 CYS A 165 CYS A 203 1555 1555 2.07
SSBOND 2 CYS B 165 CYS B 203 1555 1555 2.13
SSBOND 3 CYS C 165 CYS C 203 1555 1555 2.06
SSBOND 4 CYS D 165 CYS D 203 1555 1555 2.08
SSBOND 5 CYS E 165 CYS E 203 1555 1555 2.08
SSBOND 6 CYS F 165 CYS F 203 1555 1555 2.05
LINK NZ LYS A 129 CA PYR A1204 1555 1555 1.34
LINK NZ LYS B 129 CA PYR B1204 1555 1555 1.34
LINK NZ LYS C 129 CA PYR C1204 1555 1555 1.33
LINK NZ LYS D 129 CA PYR D1205 1555 1555 1.34
LINK NZ LYS E 129 CA PYR E1204 1555 1555 1.34
LINK NZ LYS F 129 CA PYR F1204 1555 1555 1.34
CISPEP 1 PHE A 131 PRO A 132 0 -1.25
CISPEP 2 PHE B 131 PRO B 132 0 -2.54
CISPEP 3 PHE C 131 PRO C 132 0 1.02
CISPEP 4 PHE D 131 PRO D 132 0 -3.98
CISPEP 5 PHE E 131 PRO E 132 0 0.19
CISPEP 6 PHE F 131 PRO F 132 0 -4.73
SITE 1 AC1 9 GLY A 157 GLY A 158 GLY A 178 SER A 179
SITE 2 AC1 9 HOH A2008 HOH A2065 HOH A2073 HOH A2074
SITE 3 AC1 9 HOH B2050
SITE 1 AC2 11 THR B 156 GLY B 157 GLY B 158 GLY B 178
SITE 2 AC2 11 SER B 179 HOH B2047 HOH B2069 HOH B2070
SITE 3 AC2 11 HOH B2071 HOH B2072 HOH B2073
SITE 1 AC3 8 GLY C 157 GLY C 158 GLY C 178 SER C 179
SITE 2 AC3 8 HOH C2027 HOH C2038 HOH C2040 HOH C2041
SITE 1 AC4 7 GLY D 158 GLY D 178 SER D 179 HOH D2042
SITE 2 AC4 7 HOH D2045 HOH D2049 HOH E2032
SITE 1 AC5 7 GLY E 157 GLY E 158 GLY E 178 SER E 179
SITE 2 AC5 7 HOH E2004 HOH E2036 HOH E2046
SITE 1 AC6 9 GLY F 157 GLY F 158 GLY F 178 SER F 179
SITE 2 AC6 9 HOH F2015 HOH F2020 HOH F2021 HOH F2022
SITE 3 AC6 9 HOH F2023
SITE 1 AC7 7 ARG A 17 THR A 69 VAL A 88 SER A 89
SITE 2 AC7 7 PRO A 90 LYS A 129 PHE A 131
SITE 1 AC8 9 ARG B 17 GLY B 68 THR B 69 VAL B 88
SITE 2 AC8 9 SER B 89 PRO B 90 LYS B 129 PHE B 131
SITE 3 AC8 9 HOH B2045
SITE 1 AC9 6 ARG C 17 THR C 69 SER C 89 PRO C 90
SITE 2 AC9 6 LYS C 129 PHE C 131
SITE 1 BC1 6 ARG D 17 THR D 69 SER D 89 PRO D 90
SITE 2 BC1 6 LYS D 129 PHE D 131
SITE 1 BC2 7 ARG E 17 THR E 69 VAL E 88 SER E 89
SITE 2 BC2 7 PRO E 90 LYS E 129 PHE E 131
SITE 1 BC3 8 ARG F 17 GLU F 40 THR F 69 VAL F 88
SITE 2 BC3 8 SER F 89 PRO F 90 LYS F 129 PHE F 131
CRYST1 42.600 101.100 124.600 90.00 97.20 90.00 P 1 21 1 12
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 0.023474 0.000000 0.002965 0.00000
SCALE2 0.000000 0.009891 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008089 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
