HEADER OXIDOREDUCTASE 30-MAY-08 3DAT
TITLE CRYSTAL STRUCTURE OF THE TERNARY MTX NADPH COMPLEX OF BACILLUS
TITLE 2 ANTHRACIS DIHYDROFOLATE REDUCTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.5.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS STR.;
SOURCE 3 ORGANISM_TAXID: 260799;
SOURCE 4 STRAIN: STERNE;
SOURCE 5 GENE: DFRA, BAS2083, BA_2237, GBAA2237;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: CHAMPION PET-SUMO
KEYWDS DUAL-SITE INHIBITION, OXIDOREDUCTASE, PSEUDO-ROSSMANN FOLD, ADENINE
KEYWDS 2 NUCLEOTIDE BINDING DOMAIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.C.BENNETT,C.G.DEALWIS
REVDAT 6 30-AUG-23 3DAT 1 REMARK
REVDAT 5 25-OCT-17 3DAT 1 REMARK
REVDAT 4 20-NOV-13 3DAT 1 HET HETATM
REVDAT 3 13-JUL-11 3DAT 1 VERSN
REVDAT 2 19-MAY-09 3DAT 1 JRNL
REVDAT 1 14-APR-09 3DAT 0
JRNL AUTH B.C.BENNETT,Q.WAN,M.F.AHMAD,P.LANGAN,C.G.DEALWIS
JRNL TITL X-RAY STRUCTURE OF THE TERNARY MTX.NADPH COMPLEX OF THE
JRNL TITL 2 ANTHRAX DIHYDROFOLATE REDUCTASE: A PHARMACOPHORE FOR
JRNL TITL 3 DUAL-SITE INHIBITOR DESIGN.
JRNL REF J.STRUCT.BIOL. V. 166 162 2009
JRNL REFN ISSN 1047-8477
JRNL PMID 19374017
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.9
REMARK 3 NUMBER OF REFLECTIONS : 8170
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) : 0.239
REMARK 3 R VALUE (WORKING SET) : 0.237
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 404
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 505
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.26
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE SET COUNT : 17
REMARK 3 BIN FREE R VALUE : 0.3980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1280
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 81
REMARK 3 SOLVENT ATOMS : 34
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) : 44.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : 0.14000
REMARK 3 B33 (A**2) : -0.31000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.21000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.420
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.275
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.235
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.885
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.889
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1403 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1915 ; 1.892 ; 2.011
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 160 ; 8.102 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 65 ;38.816 ;23.692
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 205 ;21.993 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;17.853 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 196 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1083 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 603 ; 0.240 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 919 ; 0.323 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 53 ; 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): 12 ; 0.165 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.201 ; 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): 821 ; 0.759 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1291 ; 1.234 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 689 ; 1.856 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 624 ; 2.870 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 36
REMARK 3 RESIDUE RANGE : A 37 A 108
REMARK 3 RESIDUE RANGE : A 109 A 160
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3642 -9.1675 14.2230
REMARK 3 T TENSOR
REMARK 3 T11: -0.2626 T22: -0.0700
REMARK 3 T33: -0.1338 T12: 0.0234
REMARK 3 T13: 0.0542 T23: -0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 3.8092 L22: 1.5648
REMARK 3 L33: 14.7699 L12: 0.2207
REMARK 3 L13: 0.3391 L23: 0.8785
REMARK 3 S TENSOR
REMARK 3 S11: 0.0444 S12: -0.3582 S13: -0.0033
REMARK 3 S21: 0.0613 S22: 0.1482 S23: 0.0339
REMARK 3 S31: 0.3106 S32: 1.7936 S33: -0.1926
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: NULL
REMARK 4
REMARK 4 3DAT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-08.
REMARK 100 THE DEPOSITION ID IS D_1000047806.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90000
REMARK 200 MONOCHROMATOR : SILICON (111) DOUBLE-CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10216
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.13100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.28600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC 5.2.0019
REMARK 200 STARTING MODEL: PDB ENTRY 2QK8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 5.5, 0.2 M CACL2,
REMARK 280 20% W/V PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 40.95000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.57800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 40.95000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 21.57800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 215 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 GLN A 162
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 17 CG CD CE NZ
REMARK 470 ASP A 18 CB CG OD1 OD2
REMARK 470 LYS A 34 CG CD CE NZ
REMARK 470 LYS A 88 CB CG CD CE NZ
REMARK 470 GLU A 91 CG CD OE1 OE2
REMARK 470 GLU A 92 CG CD OE1 OE2
REMARK 470 GLU A 122 CB CG CD OE1 OE2
REMARK 470 ASN A 134 CG OD1 ND2
REMARK 470 LYS A 136 CB CG CD CE NZ
REMARK 470 LYS A 142 CG CD CE NZ
REMARK 470 GLU A 147 CG CD OE1 OE2
REMARK 470 LYS A 148 CB CG CD CE NZ
REMARK 470 TYR A 154 CG CD1 CD2 CE1 CE2 CZ OH
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 A 17 -63.14 -123.58
REMARK 500 ASP A 18 -92.51 -79.43
REMARK 500 ASN A 19 47.89 -143.72
REMARK 500 CYS A 87 31.45 -93.37
REMARK 500 ASP A 131 104.48 -21.20
REMARK 500 THR A 133 -138.01 51.80
REMARK 500 ASN A 134 -106.35 62.24
REMARK 500 TRP A 135 111.39 -39.72
REMARK 500 LYS A 148 -33.78 110.66
REMARK 500 PRO A 150 38.98 -82.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 97 GLY A 98 -131.52
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 MTX A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QK8 RELATED DB: PDB
REMARK 900 MTX BINARY COMPLEX OF BACILLUS ANTHRACIS DIHYDROFOLATE REDUCTASE
DBREF 3DAT A 1 162 UNP Q81R22 Q81R22_BACAN 1 162
SEQRES 1 A 162 MET ILE VAL SER PHE MET VAL ALA MET ASP GLU ASN ARG
SEQRES 2 A 162 VAL ILE GLY LYS ASP ASN ASN LEU PRO TRP ARG LEU PRO
SEQRES 3 A 162 SER GLU LEU GLN TYR VAL LYS LYS THR THR MET GLY HIS
SEQRES 4 A 162 PRO LEU ILE MET GLY ARG LYS ASN TYR GLU ALA ILE GLY
SEQRES 5 A 162 ARG PRO LEU PRO GLY ARG ARG ASN ILE ILE VAL THR ARG
SEQRES 6 A 162 ASN GLU GLY TYR HIS VAL GLU GLY CYS GLU VAL ALA HIS
SEQRES 7 A 162 SER VAL GLU GLU VAL PHE GLU LEU CYS LYS ASN GLU GLU
SEQRES 8 A 162 GLU ILE PHE ILE PHE GLY GLY ALA GLN ILE TYR ASP LEU
SEQRES 9 A 162 PHE LEU PRO TYR VAL ASP LYS LEU TYR ILE THR LYS ILE
SEQRES 10 A 162 HIS HIS ALA PHE GLU GLY ASP THR PHE PHE PRO GLU MET
SEQRES 11 A 162 ASP MET THR ASN TRP LYS GLU VAL PHE VAL GLU LYS GLY
SEQRES 12 A 162 LEU THR ASP GLU LYS ASN PRO TYR THR TYR TYR TYR HIS
SEQRES 13 A 162 VAL TYR GLU LYS GLN GLN
HET MTX A 201 33
HET NDP A 202 48
HETNAM MTX METHOTREXATE
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
FORMUL 2 MTX C20 H22 N8 O5
FORMUL 3 NDP C21 H30 N7 O17 P3
FORMUL 4 HOH *34(H2 O)
HELIX 1 1 SER A 27 MET A 37 1 11
HELIX 2 2 ARG A 45 ALA A 50 1 6
HELIX 3 3 SER A 79 CYS A 87 1 9
HELIX 4 4 GLY A 98 LEU A 106 1 9
SHEET 1 A 8 GLU A 75 ALA A 77 0
SHEET 2 A 8 ASN A 60 VAL A 63 1 N ASN A 60 O GLU A 75
SHEET 3 A 8 LEU A 41 GLY A 44 1 N LEU A 41 O ILE A 61
SHEET 4 A 8 GLU A 92 ILE A 95 1 O PHE A 94 N ILE A 42
SHEET 5 A 8 ILE A 2 ASP A 10 1 N SER A 4 O ILE A 95
SHEET 6 A 8 LYS A 111 ILE A 117 1 O ILE A 117 N MET A 9
SHEET 7 A 8 TYR A 153 GLU A 159 -1 O TYR A 154 N LYS A 116
SHEET 8 A 8 LYS A 136 LYS A 142 -1 N VAL A 138 O VAL A 157
SHEET 1 B 2 VAL A 14 GLY A 16 0
SHEET 2 B 2 THR A 125 PHE A 126 -1 O THR A 125 N ILE A 15
SITE 1 AC1 16 MET A 6 VAL A 7 ALA A 8 LEU A 21
SITE 2 AC1 16 GLU A 28 LEU A 29 VAL A 32 ILE A 51
SITE 3 AC1 16 ARG A 53 LEU A 55 ARG A 58 PHE A 96
SITE 4 AC1 16 TYR A 102 THR A 115 NDP A 202 HOH A 229
SITE 1 AC2 27 VAL A 7 ALA A 8 ILE A 15 ASN A 19
SITE 2 AC2 27 ASN A 20 LEU A 21 TRP A 23 GLY A 44
SITE 3 AC2 27 ARG A 45 LYS A 46 ASN A 47 VAL A 63
SITE 4 AC2 27 THR A 64 ARG A 65 HIS A 78 PHE A 96
SITE 5 AC2 27 GLY A 97 GLY A 98 ALA A 99 GLN A 100
SITE 6 AC2 27 ILE A 101 TYR A 102 LEU A 104 THR A 125
SITE 7 AC2 27 MTX A 201 HOH A 212 HOH A 224
CRYST1 81.900 43.156 67.870 90.00 119.31 90.00 C 1 2 1 4
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 0.012210 0.000000 0.006854 0.00000
SCALE2 0.000000 0.023172 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016897 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
