HEADER TRANSFERASE/TRANSFERASE INHIBITOR 14-APR-09 3H2E
TITLE STRUCTURAL STUDIES OF PTERIN-BASED INHIBITORS OF DIHYDROPTEROATE
TITLE 2 SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROPTEROATE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.5.1.15;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS STR. A2012;
SOURCE 3 ORGANISM_TAXID: 191218;
SOURCE 4 GENE: FOLP, BAO_0074;
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: PET-28A
KEYWDS ANTHRACIS, FOLATE BIOSYNTHESIS, DIHYDROPTEROATE, PTERINE,
KEYWDS 2 TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.-K.YUN,S.W.WHITE
REVDAT 5 06-SEP-23 3H2E 1 REMARK SEQADV LINK
REVDAT 4 01-NOV-17 3H2E 1 REMARK
REVDAT 3 13-JUL-11 3H2E 1 VERSN
REVDAT 2 26-JAN-10 3H2E 1 JRNL
REVDAT 1 08-DEC-09 3H2E 0
JRNL AUTH K.E.HEVENER,M.K.YUN,J.QI,I.D.KERR,K.BABAOGLU,J.G.HURDLE,
JRNL AUTH 2 K.BALAKRISHNA,S.W.WHITE,R.E.LEE
JRNL TITL STRUCTURAL STUDIES OF PTERIN-BASED INHIBITORS OF
JRNL TITL 2 DIHYDROPTEROATE SYNTHASE.
JRNL REF J.MED.CHEM. V. 53 166 2010
JRNL REFN ISSN 0022-2623
JRNL PMID 19899766
JRNL DOI 10.1021/JM900861D
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) : 48.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 48547
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2447
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) : 2050
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 58.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE SET COUNT : 101
REMARK 3 BIN FREE R VALUE : 0.2650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4131
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 73
REMARK 3 SOLVENT ATOMS : 256
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) : 40.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.43000
REMARK 3 B22 (A**2) : 1.43000
REMARK 3 B33 (A**2) : -2.15000
REMARK 3 B12 (A**2) : 0.72000
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): 0.167
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.153
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.111
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.966
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
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): 4267 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5765 ; 1.317 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 533 ; 5.240 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 187 ;30.220 ;25.080
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 785 ;15.785 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;18.807 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 643 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3141 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1780 ; 0.202 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2915 ; 0.298 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 228 ; 0.137 ; 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): 72 ; 0.194 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.350 ; 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): 2743 ; 1.007 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4255 ; 1.482 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1810 ; 2.340 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1508 ; 3.786 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 274
REMARK 3 ORIGIN FOR THE GROUP (A): -78.4390 80.8340 91.3390
REMARK 3 T TENSOR
REMARK 3 T11: -0.0782 T22: -0.0335
REMARK 3 T33: -0.2085 T12: 0.1137
REMARK 3 T13: 0.0103 T23: 0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 1.3800 L22: 0.8962
REMARK 3 L33: 2.0022 L12: -0.0702
REMARK 3 L13: 0.5303 L23: 0.0871
REMARK 3 S TENSOR
REMARK 3 S11: -0.0288 S12: 0.0071 S13: -0.0025
REMARK 3 S21: 0.0645 S22: 0.0322 S23: 0.0277
REMARK 3 S31: 0.0236 S32: 0.1465 S33: -0.0035
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 274
REMARK 3 ORIGIN FOR THE GROUP (A): -68.2670 61.3510 138.4260
REMARK 3 T TENSOR
REMARK 3 T11: 0.0559 T22: -0.1046
REMARK 3 T33: -0.1959 T12: -0.0151
REMARK 3 T13: -0.0453 T23: 0.0352
REMARK 3 L TENSOR
REMARK 3 L11: 0.7923 L22: 1.1985
REMARK 3 L33: 1.5735 L12: 0.0247
REMARK 3 L13: -0.2446 L23: -0.2525
REMARK 3 S TENSOR
REMARK 3 S11: -0.0089 S12: 0.0538 S13: -0.0109
REMARK 3 S21: -0.1512 S22: -0.0733 S23: -0.0245
REMARK 3 S31: -0.2367 S32: 0.0908 S33: 0.0822
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 3H2E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000052605.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48615
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 48.210
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 11.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.3000
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) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.34600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1TX0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULFATE, PROPANE, BIS-TRIS, PH
REMARK 280 9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 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
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
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+2/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+1/3
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 175.96333
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 87.98167
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 0.00000
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 175.96333
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 87.98167
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 175.96333
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 87.98167
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 175.96333
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 0.00000
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 87.98167
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -108.0 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 -1.000000 0.000000 0.000000 -196.12600
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 169.85010
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 3670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -147.09450
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 84.92505
REMARK 350 BIOMT3 2 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLY A 275
REMARK 465 VAL A 276
REMARK 465 LYS A 277
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 PRO B 30
REMARK 465 ASP B 31
REMARK 465 SER B 32
REMARK 465 PHE B 33
REMARK 465 GLU B 65
REMARK 465 SER B 66
REMARK 465 THR B 67
REMARK 465 ARG B 68
REMARK 465 PRO B 69
REMARK 465 GLY B 70
REMARK 465 PHE B 71
REMARK 465 ALA B 72
REMARK 465 LYS B 73
REMARK 465 GLY B 275
REMARK 465 VAL B 276
REMARK 465 LYS B 277
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 ASN B 27 100.84 -59.38
REMARK 500
REMARK 500 REMARK: NULL
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 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 280
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B59 B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B59 B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 280
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 281
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TWW RELATED DB: PDB
REMARK 900 RELATED ID: 1TWZ RELATED DB: PDB
REMARK 900 RELATED ID: 1TX0 RELATED DB: PDB
REMARK 900 RELATED ID: 1TX2 RELATED DB: PDB
REMARK 900 RELATED ID: 1TWS RELATED DB: PDB
REMARK 900 RELATED ID: 3H21 RELATED DB: PDB
REMARK 900 RELATED ID: 3H22 RELATED DB: PDB
REMARK 900 RELATED ID: 3H23 RELATED DB: PDB
REMARK 900 RELATED ID: 3H24 RELATED DB: PDB
REMARK 900 RELATED ID: 3H26 RELATED DB: PDB
REMARK 900 RELATED ID: 3H2A RELATED DB: PDB
REMARK 900 RELATED ID: 3H2C RELATED DB: PDB
REMARK 900 RELATED ID: 3H2F RELATED DB: PDB
REMARK 900 RELATED ID: 3H2M RELATED DB: PDB
REMARK 900 RELATED ID: 3H2N RELATED DB: PDB
REMARK 900 RELATED ID: 3H2O RELATED DB: PDB
DBREF 3H2E A 1 277 UNP B1UXN2 B1UXN2_BACAN 1 277
DBREF 3H2E B 1 277 UNP B1UXN2 B1UXN2_BACAN 1 277
SEQADV 3H2E MET A -19 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E GLY A -18 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E SER A -17 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E SER A -16 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E HIS A -15 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E HIS A -14 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E HIS A -13 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E HIS A -12 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E HIS A -11 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E HIS A -10 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E SER A -9 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E SER A -8 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E GLY A -7 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E LEU A -6 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E VAL A -5 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E PRO A -4 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E ARG A -3 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E GLY A -2 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E SER A -1 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E HIS A 0 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E MET B -19 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E GLY B -18 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E SER B -17 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E SER B -16 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E HIS B -15 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E HIS B -14 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E HIS B -13 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E HIS B -12 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E HIS B -11 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E HIS B -10 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E SER B -9 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E SER B -8 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E GLY B -7 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E LEU B -6 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E VAL B -5 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E PRO B -4 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E ARG B -3 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E GLY B -2 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E SER B -1 UNP B1UXN2 EXPRESSION TAG
SEQADV 3H2E HIS B 0 UNP B1UXN2 EXPRESSION TAG
SEQRES 1 A 297 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 297 LEU VAL PRO ARG GLY SER HIS MET LYS TRP ASP TYR ASP
SEQRES 3 A 297 LEU ARG CYS GLY GLU TYR THR LEU ASN LEU ASN GLU LYS
SEQRES 4 A 297 THR LEU ILE MET GLY ILE LEU ASN VAL THR PRO ASP SER
SEQRES 5 A 297 PHE SER ASP GLY GLY SER TYR ASN GLU VAL ASP ALA ALA
SEQRES 6 A 297 VAL ARG HIS ALA LYS GLU MET ARG ASP GLU GLY ALA HIS
SEQRES 7 A 297 ILE ILE ASP ILE GLY GLY GLU SER THR ARG PRO GLY PHE
SEQRES 8 A 297 ALA LYS VAL SER VAL GLU GLU GLU ILE LYS ARG VAL VAL
SEQRES 9 A 297 PRO MET ILE GLN ALA VAL SER LYS GLU VAL LYS LEU PRO
SEQRES 10 A 297 ILE SER ILE ASP THR TYR LYS ALA GLU VAL ALA LYS GLN
SEQRES 11 A 297 ALA ILE GLU ALA GLY ALA HIS ILE ILE ASN ASP ILE TRP
SEQRES 12 A 297 GLY ALA LYS ALA GLU PRO LYS ILE ALA GLU VAL ALA ALA
SEQRES 13 A 297 HIS TYR ASP VAL PRO ILE ILE LEU MET HIS ASN ARG ASP
SEQRES 14 A 297 ASN MET ASN TYR ARG ASN LEU MET ALA ASP MET ILE ALA
SEQRES 15 A 297 ASP LEU TYR ASP SER ILE LYS ILE ALA LYS ASP ALA GLY
SEQRES 16 A 297 VAL ARG ASP GLU ASN ILE ILE LEU ASP PRO GLY ILE GLY
SEQRES 17 A 297 PHE ALA LYS THR PRO GLU GLN ASN LEU GLU ALA MET ARG
SEQRES 18 A 297 ASN LEU GLU GLN LEU ASN VAL LEU GLY TYR PRO VAL LEU
SEQRES 19 A 297 LEU GLY THR SER ARG LYS SER PHE ILE GLY HIS VAL LEU
SEQRES 20 A 297 ASP LEU PRO VAL GLU GLU ARG LEU GLU GLY THR GLY ALA
SEQRES 21 A 297 THR VAL CYS LEU GLY ILE GLU LYS GLY CYS GLU PHE VAL
SEQRES 22 A 297 ARG VAL HIS ASP VAL LYS GLU MET SER ARG MET ALA LYS
SEQRES 23 A 297 MET MET ASP ALA MET ILE GLY LYS GLY VAL LYS
SEQRES 1 B 297 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 297 LEU VAL PRO ARG GLY SER HIS MET LYS TRP ASP TYR ASP
SEQRES 3 B 297 LEU ARG CYS GLY GLU TYR THR LEU ASN LEU ASN GLU LYS
SEQRES 4 B 297 THR LEU ILE MET GLY ILE LEU ASN VAL THR PRO ASP SER
SEQRES 5 B 297 PHE SER ASP GLY GLY SER TYR ASN GLU VAL ASP ALA ALA
SEQRES 6 B 297 VAL ARG HIS ALA LYS GLU MET ARG ASP GLU GLY ALA HIS
SEQRES 7 B 297 ILE ILE ASP ILE GLY GLY GLU SER THR ARG PRO GLY PHE
SEQRES 8 B 297 ALA LYS VAL SER VAL GLU GLU GLU ILE LYS ARG VAL VAL
SEQRES 9 B 297 PRO MET ILE GLN ALA VAL SER LYS GLU VAL LYS LEU PRO
SEQRES 10 B 297 ILE SER ILE ASP THR TYR LYS ALA GLU VAL ALA LYS GLN
SEQRES 11 B 297 ALA ILE GLU ALA GLY ALA HIS ILE ILE ASN ASP ILE TRP
SEQRES 12 B 297 GLY ALA LYS ALA GLU PRO LYS ILE ALA GLU VAL ALA ALA
SEQRES 13 B 297 HIS TYR ASP VAL PRO ILE ILE LEU MET HIS ASN ARG ASP
SEQRES 14 B 297 ASN MET ASN TYR ARG ASN LEU MET ALA ASP MET ILE ALA
SEQRES 15 B 297 ASP LEU TYR ASP SER ILE LYS ILE ALA LYS ASP ALA GLY
SEQRES 16 B 297 VAL ARG ASP GLU ASN ILE ILE LEU ASP PRO GLY ILE GLY
SEQRES 17 B 297 PHE ALA LYS THR PRO GLU GLN ASN LEU GLU ALA MET ARG
SEQRES 18 B 297 ASN LEU GLU GLN LEU ASN VAL LEU GLY TYR PRO VAL LEU
SEQRES 19 B 297 LEU GLY THR SER ARG LYS SER PHE ILE GLY HIS VAL LEU
SEQRES 20 B 297 ASP LEU PRO VAL GLU GLU ARG LEU GLU GLY THR GLY ALA
SEQRES 21 B 297 THR VAL CYS LEU GLY ILE GLU LYS GLY CYS GLU PHE VAL
SEQRES 22 B 297 ARG VAL HIS ASP VAL LYS GLU MET SER ARG MET ALA LYS
SEQRES 23 B 297 MET MET ASP ALA MET ILE GLY LYS GLY VAL LYS
MODRES 3H2E LYS B 109 LYS COVALENT
HET SO4 A 278 5
HET SO4 A 279 5
HET SO4 A 280 5
HET SO4 A 281 5
HET B59 B 901 17
HET B59 B 902 16
HET SO4 B 278 5
HET SO4 B 279 5
HET SO4 B 280 5
HET SO4 B 281 5
HETNAM SO4 SULFATE ION
HETNAM B59 1,3-DIMETHYL-2,4,7-TRIOXO-1,2,3,4,7,8-
HETNAM 2 B59 HEXAHYDROPTERIDINE-6-CARBALDEHYDE
FORMUL 3 SO4 8(O4 S 2-)
FORMUL 7 B59 2(C9 H8 N4 O4)
FORMUL 13 HOH *256(H2 O)
HELIX 1 1 SER A 38 GLU A 55 1 18
HELIX 2 2 SER A 75 VAL A 94 1 20
HELIX 3 3 LYS A 104 GLY A 115 1 12
HELIX 4 4 PRO A 129 ASP A 139 1 11
HELIX 5 5 ASN A 155 ALA A 174 1 20
HELIX 6 6 ARG A 177 GLU A 179 5 3
HELIX 7 7 THR A 192 ASN A 202 1 11
HELIX 8 8 LEU A 203 GLY A 210 5 8
HELIX 9 9 LYS A 220 ASP A 228 1 9
HELIX 10 10 PRO A 230 GLU A 233 5 4
HELIX 11 11 ARG A 234 LYS A 248 1 15
HELIX 12 12 ASP A 257 GLY A 273 1 17
HELIX 13 13 SER B 38 GLU B 55 1 18
HELIX 14 14 SER B 75 VAL B 94 1 20
HELIX 15 15 LYS B 104 GLY B 115 1 12
HELIX 16 16 PRO B 129 ASP B 139 1 11
HELIX 17 17 ASN B 155 ALA B 174 1 20
HELIX 18 18 ARG B 177 GLU B 179 5 3
HELIX 19 19 THR B 192 ASN B 202 1 11
HELIX 20 20 LEU B 203 GLY B 210 5 8
HELIX 21 21 LYS B 220 ASP B 228 1 9
HELIX 22 22 PRO B 230 GLU B 233 5 4
HELIX 23 23 ARG B 234 LYS B 248 1 15
HELIX 24 24 ASP B 257 GLY B 273 1 17
SHEET 1 A 2 LEU A 7 CYS A 9 0
SHEET 2 A 2 TYR A 12 LEU A 14 -1 O LEU A 14 N LEU A 7
SHEET 1 B 8 ILE A 181 ASP A 184 0
SHEET 2 B 8 ILE A 142 MET A 145 1 N LEU A 144 O ILE A 182
SHEET 3 B 8 ILE A 118 ASP A 121 1 N ILE A 119 O ILE A 143
SHEET 4 B 8 ILE A 98 ASP A 101 1 N ILE A 100 O ASN A 120
SHEET 5 B 8 ILE A 59 GLY A 63 1 N ILE A 62 O SER A 99
SHEET 6 B 8 LEU A 21 ASN A 27 1 N LEU A 26 O ASP A 61
SHEET 7 B 8 PHE A 252 VAL A 255 1 O VAL A 253 N MET A 23
SHEET 8 B 8 LEU A 214 LEU A 215 1 N LEU A 215 O ARG A 254
SHEET 1 C 2 LEU B 7 CYS B 9 0
SHEET 2 C 2 TYR B 12 LEU B 14 -1 O LEU B 14 N LEU B 7
SHEET 1 D 8 ILE B 181 ASP B 184 0
SHEET 2 D 8 ILE B 142 MET B 145 1 N LEU B 144 O ILE B 182
SHEET 3 D 8 ILE B 118 ASP B 121 1 N ILE B 119 O ILE B 143
SHEET 4 D 8 ILE B 98 ASP B 101 1 N ILE B 100 O ASN B 120
SHEET 5 D 8 ILE B 59 GLY B 63 1 N ILE B 62 O SER B 99
SHEET 6 D 8 LEU B 21 ILE B 25 1 N GLY B 24 O ASP B 61
SHEET 7 D 8 PHE B 252 VAL B 255 1 O VAL B 253 N MET B 23
SHEET 8 D 8 LEU B 214 LEU B 215 1 N LEU B 215 O ARG B 254
LINK NZ LYS B 109 C11 B59 B 902 1555 1555 1.28
CISPEP 1 ARG A 68 PRO A 69 0 3.90
SITE 1 AC1 7 ASN A 27 ARG A 68 PRO A 69 ARG A 254
SITE 2 AC1 7 HIS A 256 HOH A 295 HOH A 395
SITE 1 AC2 3 LYS A 50 ARG A 53 HOH A 331
SITE 1 AC3 1 ARG A 219
SITE 1 AC4 2 SER A 221 ARG A 234
SITE 1 AC5 6 PHE A 33 LYS B 81 LYS B 109 HIS B 137
SITE 2 AC5 6 TYR B 138 B59 B 902
SITE 1 AC6 6 LYS B 81 GLN B 88 LYS B 109 GLN B 110
SITE 2 AC6 6 HOH B 391 B59 B 901
SITE 1 AC7 4 ARG B 254 HIS B 256 HOH B 360 HOH B 368
SITE 1 AC8 2 ASN B 27 ARG B 219
SITE 1 AC9 2 LYS B 50 ARG B 53
SITE 1 BC1 3 SER B 221 ARG B 234 HOH B 400
CRYST1 98.063 98.063 263.945 90.00 90.00 120.00 P 62 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 0.010198 0.005888 0.000000 0.00000
SCALE2 0.000000 0.011775 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003789 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
