HEADER TRANSFERASE 03-JUN-08 3DCJ
TITLE CRYSTAL STRUCTURE OF GLYCINAMIDE FORMYLTRANSFERASE (PURN) FROM
TITLE 2 MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH 5-METHYL-5,6,7,8-
TITLE 3 TETRAHYDROFOLIC ACID DERIVATIVE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE 5'-PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE
COMPND 3 PURN;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: GART, GAR TRANSFORMYLASE, 5'-PHOSPHORIBOSYLGLYCINAMIDE
COMPND 6 TRANSFORMYLASE, PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE;
COMPND 7 EC: 2.1.2.2;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: PURN, MT0983, RV0956;
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: PDEST17
KEYWDS GLYCINAMIDE FORMYLTRANSFERASE, PURN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.ZHANG,C.J.SQUIRE,E.N.BAKER
REVDAT 5 30-AUG-23 3DCJ 1 REMARK SEQADV LINK
REVDAT 4 24-JUL-19 3DCJ 1 REMARK
REVDAT 3 04-AUG-09 3DCJ 1 REMARK
REVDAT 2 16-JUN-09 3DCJ 1 JRNL
REVDAT 1 12-MAY-09 3DCJ 0
JRNL AUTH Z.ZHANG,T.T.CARADOC-DAVIES,J.M.DICKSON,E.N.BAKER,C.J.SQUIRE
JRNL TITL STRUCTURES OF GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE
JRNL TITL 2 (PURN) FROM MYCOBACTERIUM TUBERCULOSIS REVEAL A NOVEL DIMER
JRNL TITL 3 WITH RELEVANCE TO DRUG DISCOVERY.
JRNL REF J.MOL.BIOL. V. 389 722 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19394344
JRNL DOI 10.1016/J.JMB.2009.04.044
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0078
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 22471
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1138
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1339
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 62
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3004
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 286
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.59
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.272
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.218
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.141
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.596
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3142 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4316 ; 1.859 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 413 ; 6.405 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 113 ;27.821 ;21.858
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 436 ;15.470 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;20.327 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 527 ; 0.118 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2393 ; 0.009 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 2068 ; 0.934 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3329 ; 1.639 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1074 ; 2.955 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 985 ; 4.712 ; 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 : NULL
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. U VALUES HAVE BEEN REFINED INDIVIDUALLY.
REMARK 4
REMARK 4 3DCJ 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_1000047867.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAR-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) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : OSMIC MIRROR FOCUSING OPTICS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22471
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 32.580
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1MEO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2 M MG NITRATE, PH
REMARK 280 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 30.83000
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 47.98874
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 30.83000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 59.87236
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 VAL A 1
REMARK 465 GLN A 2
REMARK 465 GLY A 209
REMARK 465 ARG A 210
REMARK 465 LYS A 211
REMARK 465 VAL A 212
REMARK 465 THR A 213
REMARK 465 ILE A 214
REMARK 465 GLY A 215
REMARK 465 VAL B 1
REMARK 465 GLN B 2
REMARK 465 GLU B 3
REMARK 465 GLY B 209
REMARK 465 ARG B 210
REMARK 465 LYS B 211
REMARK 465 VAL B 212
REMARK 465 THR B 213
REMARK 465 ILE B 214
REMARK 465 GLY B 215
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 GLU A 3 CB CG CD OE1 OE2
REMARK 470 GLU A 177 CG CD OE1 OE2
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 O HOH A 518 O HOH A 537 2.19
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 ARG A 40 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 LEU A 115 CA - CB - CG ANGL. DEV. = 17.4 DEGREES
REMARK 500 ARG B 178 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 184 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 184 NE - CZ - NH2 ANGL. DEV. = -3.3 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 PRO A 38 39.35 -87.55
REMARK 500 PRO A 119 55.41 -90.86
REMARK 500 THR A 142 -153.39 -122.92
REMARK 500 ASP A 150 -157.53 -120.64
REMARK 500 THR B 142 -152.58 -116.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 THH B 401
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 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 423 O
REMARK 620 2 HOH A 491 O 92.3
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THH A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THH B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DA8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PURN FROM MYCOBACTERIUM TUBERCULOSIS
DBREF 3DCJ A 2 215 UNP P71554 P71554_MYCTU 2 215
DBREF 3DCJ B 2 215 UNP P71554 P71554_MYCTU 2 215
SEQADV 3DCJ VAL A 1 UNP P71554 EXPRESSION TAG
SEQADV 3DCJ VAL B 1 UNP P71554 EXPRESSION TAG
SEQRES 1 A 215 VAL GLN GLU PRO LEU ARG VAL PRO PRO SER ALA PRO ALA
SEQRES 2 A 215 ARG LEU VAL VAL LEU ALA SER GLY THR GLY SER LEU LEU
SEQRES 3 A 215 ARG SER LEU LEU ASP ALA ALA VAL GLY ASP TYR PRO ALA
SEQRES 4 A 215 ARG VAL VAL ALA VAL GLY VAL ASP ARG GLU CYS ARG ALA
SEQRES 5 A 215 ALA GLU ILE ALA ALA GLU ALA SER VAL PRO VAL PHE THR
SEQRES 6 A 215 VAL ARG LEU ALA ASP HIS PRO SER ARG ASP ALA TRP ASP
SEQRES 7 A 215 VAL ALA ILE THR ALA ALA THR ALA ALA HIS GLU PRO ASP
SEQRES 8 A 215 LEU VAL VAL SER ALA GLY PHE MET ARG ILE LEU GLY PRO
SEQRES 9 A 215 GLN PHE LEU SER ARG PHE TYR GLY ARG THR LEU ASN THR
SEQRES 10 A 215 HIS PRO ALA LEU LEU PRO ALA PHE PRO GLY THR HIS GLY
SEQRES 11 A 215 VAL ALA ASP ALA LEU ALA TYR GLY VAL LYS VAL THR GLY
SEQRES 12 A 215 ALA THR VAL HIS LEU VAL ASP ALA GLY THR ASP THR GLY
SEQRES 13 A 215 PRO ILE LEU ALA GLN GLN PRO VAL PRO VAL LEU ASP GLY
SEQRES 14 A 215 ASP ASP GLU GLU THR LEU HIS GLU ARG ILE LYS VAL THR
SEQRES 15 A 215 GLU ARG ARG LEU LEU VAL ALA ALA VAL ALA ALA LEU ALA
SEQRES 16 A 215 THR HIS GLY VAL THR VAL VAL GLY ARG THR ALA THR MET
SEQRES 17 A 215 GLY ARG LYS VAL THR ILE GLY
SEQRES 1 B 215 VAL GLN GLU PRO LEU ARG VAL PRO PRO SER ALA PRO ALA
SEQRES 2 B 215 ARG LEU VAL VAL LEU ALA SER GLY THR GLY SER LEU LEU
SEQRES 3 B 215 ARG SER LEU LEU ASP ALA ALA VAL GLY ASP TYR PRO ALA
SEQRES 4 B 215 ARG VAL VAL ALA VAL GLY VAL ASP ARG GLU CYS ARG ALA
SEQRES 5 B 215 ALA GLU ILE ALA ALA GLU ALA SER VAL PRO VAL PHE THR
SEQRES 6 B 215 VAL ARG LEU ALA ASP HIS PRO SER ARG ASP ALA TRP ASP
SEQRES 7 B 215 VAL ALA ILE THR ALA ALA THR ALA ALA HIS GLU PRO ASP
SEQRES 8 B 215 LEU VAL VAL SER ALA GLY PHE MET ARG ILE LEU GLY PRO
SEQRES 9 B 215 GLN PHE LEU SER ARG PHE TYR GLY ARG THR LEU ASN THR
SEQRES 10 B 215 HIS PRO ALA LEU LEU PRO ALA PHE PRO GLY THR HIS GLY
SEQRES 11 B 215 VAL ALA ASP ALA LEU ALA TYR GLY VAL LYS VAL THR GLY
SEQRES 12 B 215 ALA THR VAL HIS LEU VAL ASP ALA GLY THR ASP THR GLY
SEQRES 13 B 215 PRO ILE LEU ALA GLN GLN PRO VAL PRO VAL LEU ASP GLY
SEQRES 14 B 215 ASP ASP GLU GLU THR LEU HIS GLU ARG ILE LYS VAL THR
SEQRES 15 B 215 GLU ARG ARG LEU LEU VAL ALA ALA VAL ALA ALA LEU ALA
SEQRES 16 B 215 THR HIS GLY VAL THR VAL VAL GLY ARG THR ALA THR MET
SEQRES 17 B 215 GLY ARG LYS VAL THR ILE GLY
HET THH A 401 33
HET MG A 301 1
HET CL A 302 1
HET THH B 401 24
HET NO3 B 301 4
HET CL B 302 1
HETNAM THH N-[4-({[(6S)-2-AMINO-4-HYDROXY-5-METHYL-5,6,7,8-
HETNAM 2 THH TETRAHYDROPTERIDIN-6-YL]METHYL}AMINO)BENZOYL]-L-
HETNAM 3 THH GLUTAMIC ACID
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM NO3 NITRATE ION
HETSYN THH 5-METHYLTETRAHYDROFOLATE
FORMUL 3 THH 2(C20 H25 N7 O6)
FORMUL 4 MG MG 2+
FORMUL 5 CL 2(CL 1-)
FORMUL 7 NO3 N O3 1-
FORMUL 9 HOH *286(H2 O)
HELIX 1 1 GLY A 23 ALA A 33 1 11
HELIX 2 2 CYS A 50 ALA A 59 1 10
HELIX 3 3 ARG A 67 HIS A 71 5 5
HELIX 4 4 SER A 73 ALA A 87 1 15
HELIX 5 5 GLY A 103 TYR A 111 1 9
HELIX 6 6 HIS A 129 GLY A 138 1 10
HELIX 7 7 ASP A 171 GLY A 198 1 28
HELIX 8 8 GLY B 23 ALA B 33 1 11
HELIX 9 9 CYS B 50 ALA B 59 1 10
HELIX 10 10 ARG B 67 HIS B 71 5 5
HELIX 11 11 SER B 73 ALA B 87 1 15
HELIX 12 12 GLY B 103 TYR B 111 1 9
HELIX 13 13 HIS B 129 GLY B 138 1 10
HELIX 14 14 ASP B 171 GLY B 198 1 28
SHEET 1 A 3 LEU A 5 VAL A 7 0
SHEET 2 A 3 VAL A 199 VAL A 202 -1 O VAL A 199 N VAL A 7
SHEET 3 A 3 THR A 205 THR A 207 -1 O THR A 205 N VAL A 202
SHEET 1 B 7 VAL A 63 THR A 65 0
SHEET 2 B 7 ALA A 39 VAL A 46 1 N VAL A 46 O PHE A 64
SHEET 3 B 7 ALA A 13 LEU A 18 1 N VAL A 17 O GLY A 45
SHEET 4 B 7 LEU A 92 SER A 95 1 O VAL A 94 N LEU A 18
SHEET 5 B 7 THR A 114 HIS A 118 1 O LEU A 115 N SER A 95
SHEET 6 B 7 VAL A 141 LEU A 148 -1 O HIS A 147 N ASN A 116
SHEET 7 B 7 ILE A 158 PRO A 165 -1 O ALA A 160 N VAL A 146
SHEET 1 C 3 ARG B 6 VAL B 7 0
SHEET 2 C 3 VAL B 199 VAL B 202 -1 O VAL B 199 N VAL B 7
SHEET 3 C 3 THR B 205 THR B 207 -1 O THR B 207 N THR B 200
SHEET 1 D 7 VAL B 63 THR B 65 0
SHEET 2 D 7 ALA B 39 VAL B 46 1 N VAL B 44 O PHE B 64
SHEET 3 D 7 ALA B 13 ALA B 19 1 N LEU B 15 O ARG B 40
SHEET 4 D 7 LEU B 92 SER B 95 1 O VAL B 94 N LEU B 18
SHEET 5 D 7 THR B 114 HIS B 118 1 O LEU B 115 N SER B 95
SHEET 6 D 7 VAL B 141 VAL B 149 -1 O THR B 145 N HIS B 118
SHEET 7 D 7 THR B 155 PRO B 165 -1 O VAL B 164 N THR B 142
LINK MG MG A 301 O HOH A 423 1555 1555 2.18
LINK MG MG A 301 O HOH A 491 1555 1555 2.03
CISPEP 1 ALA A 11 PRO A 12 0 -8.58
CISPEP 2 LEU A 122 PRO A 123 0 15.85
CISPEP 3 ALA B 11 PRO B 12 0 -4.24
CISPEP 4 LEU B 122 PRO B 123 0 7.79
SITE 1 AC1 15 PHE A 98 MET A 99 ARG A 100 ILE A 101
SITE 2 AC1 15 LEU A 102 ASN A 116 THR A 128 VAL A 149
SITE 3 AC1 15 ASP A 150 GLY A 152 THR A 153 ASP A 154
SITE 4 AC1 15 MG A 301 HOH A 468 HOH A 513
SITE 1 AC2 4 THR A 117 THH A 401 HOH A 423 HOH A 491
SITE 1 AC3 1 PRO A 165
SITE 1 AC4 10 PHE B 98 ARG B 100 ILE B 101 LEU B 102
SITE 2 AC4 10 ASN B 116 VAL B 149 ASP B 150 GLY B 152
SITE 3 AC4 10 HOH B 582 HOH B 649
SITE 1 AC5 8 LEU A 68 ALA A 69 ALA B 86 PRO B 90
SITE 2 AC5 8 ARG B 109 PHE B 110 ARG B 113 HOH B 647
SITE 1 AC6 1 PRO B 165
CRYST1 62.153 61.660 61.525 90.00 103.31 90.00 P 1 21 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 0.016089 0.000000 0.003806 0.00000
SCALE2 0.000000 0.016218 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016702 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
