HEADER TRANSFERASE 05-AUG-09 3IJZ
TITLE LACTOBACILLUS CASEI THYMIDYLATE SYNTHASE TERNARY COMPLEX WITH DUMP AND
TITLE 2 PTHALIMIDIC DERIVATIVE 15C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TS, TSASE;
COMPND 5 EC: 2.1.1.45;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS CASEI;
SOURCE 3 ORGANISM_TAXID: 1582;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS TRANSFERASE, NUCLEOTIDE SYNTHASE, METHYLTRANSFERASE, NUCLEOTIDE
KEYWDS 2 BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR C.POZZI,L.CANCIAN,R.LEONE,R.LUCIANI,S.FERRARI,S.MANGANI,M.P.COSTI
REVDAT 3 01-NOV-23 3IJZ 1 REMARK
REVDAT 2 24-JUL-13 3IJZ 1 JRNL VERSN
REVDAT 1 11-AUG-10 3IJZ 0
JRNL AUTH S.MANGANI,L.CANCIAN,R.LEONE,C.POZZI,S.LAZZARI,R.LUCIANI,
JRNL AUTH 2 S.FERRARI,M.P.COSTI
JRNL TITL IDENTIFICATION OF THE BINDING MODES OF N-PHENYLPHTHALIMIDES
JRNL TITL 2 INHIBITING BACTERIAL THYMIDYLATE SYNTHASE THROUGH X-RAY
JRNL TITL 3 CRYSTALLOGRAPHY SCREENING
JRNL REF J.MED.CHEM. V. 54 5454 2011
JRNL REFN ISSN 0022-2623
JRNL PMID 21696158
JRNL DOI 10.1021/JM2005018
REMARK 2
REMARK 2 RESOLUTION. 2.21 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 2.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.25
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 19575
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1056
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) : 2.21
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.27
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1336
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.04
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 83
REMARK 3 BIN FREE R VALUE : 0.3160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2566
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 147
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.03
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.266
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.215
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.143
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.500
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2693 ; 0.018 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3664 ; 1.921 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 311 ; 6.832 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 136 ;36.610 ;23.897
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 431 ;18.408 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;18.110 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 377 ; 0.127 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2099 ; 0.009 ; 0.021
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): 1559 ; 1.047 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2519 ; 1.934 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1134 ; 2.626 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1145 ; 4.067 ; 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 : 1.40
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 3IJZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054506.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.983
REMARK 200 MONOCHROMATOR : SILICON (111) CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20713
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.210
REMARK 200 RESOLUTION RANGE LOW (A) : 74.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 16.50
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : 0.09300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 16.40
REMARK 200 R MERGE FOR SHELL (I) : 0.35600
REMARK 200 R SYM FOR SHELL (I) : 0.35600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.100
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 2TDM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% SATURATED AMMONIUM SULFATE, 1MM
REMARK 280 DTT, 20MM POTASSIUM PHOSPHATE, PH 6.8, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 74.98967
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 149.97933
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 112.48450
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 187.47417
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 37.49483
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 74.98967
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 149.97933
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 187.47417
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 112.48450
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 37.49483
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 0.500000 0.866025 0.000000 38.82800
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -67.25207
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 37.49483
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 PRO A 313
REMARK 465 VAL A 314
REMARK 465 ALA A 315
REMARK 465 VAL A 316
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 NZ LYS A 297 O HOH A 356 2.15
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 LEU A 201 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 LEU A 201 CB - CG - CD2 ANGL. DEV. = -15.2 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 ASP A 22 -93.04 -163.15
REMARK 500 HIS A 25 174.11 79.78
REMARK 500 ASP A 103 76.16 -154.75
REMARK 500 LYS A 110 -78.46 -60.27
REMARK 500 GLU A 113 -12.30 -140.62
REMARK 500 ALA A 152 54.11 -146.32
REMARK 500 ASN A 285 108.48 -46.81
REMARK 500 HIS A 289 -32.52 -131.00
REMARK 500 ASN A 303 37.23 71.36
REMARK 500 LYS A 311 96.56 -61.49
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 15C A 468
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMP A 469
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BNZ RELATED DB: PDB
REMARK 900 RELATED ID: 3BYX RELATED DB: PDB
REMARK 900 RELATED ID: 3C06 RELATED DB: PDB
REMARK 900 RELATED ID: 3C0A RELATED DB: PDB
REMARK 900 RELATED ID: 3BZ0 RELATED DB: PDB
REMARK 900 RELATED ID: 3IK0 RELATED DB: PDB
REMARK 900 RELATED ID: 3IK1 RELATED DB: PDB
DBREF 3IJZ A 1 316 UNP P00469 TYSY_LACCA 1 316
SEQRES 1 A 316 MET LEU GLU GLN PRO TYR LEU ASP LEU ALA LYS LYS VAL
SEQRES 2 A 316 LEU ASP GLU GLY HIS PHE LYS PRO ASP ARG THR HIS THR
SEQRES 3 A 316 GLY THR TYR SER ILE PHE GLY HIS GLN MET ARG PHE ASP
SEQRES 4 A 316 LEU SER LYS GLY PHE PRO LEU LEU THR THR LYS LYS VAL
SEQRES 5 A 316 PRO PHE GLY LEU ILE LYS SER GLU LEU LEU TRP PHE LEU
SEQRES 6 A 316 HIS GLY ASP THR ASN ILE ARG PHE LEU LEU GLN HIS ARG
SEQRES 7 A 316 ASN HIS ILE TRP ASP GLU TRP ALA PHE GLU LYS TRP VAL
SEQRES 8 A 316 LYS SER ASP GLU TYR HIS GLY PRO ASP MET THR ASP PHE
SEQRES 9 A 316 GLY HIS ARG SER GLN LYS ASP PRO GLU PHE ALA ALA VAL
SEQRES 10 A 316 TYR HIS GLU GLU MET ALA LYS PHE ASP ASP ARG VAL LEU
SEQRES 11 A 316 HIS ASP ASP ALA PHE ALA ALA LYS TYR GLY ASP LEU GLY
SEQRES 12 A 316 LEU VAL TYR GLY SER GLN TRP ARG ALA TRP HIS THR SER
SEQRES 13 A 316 LYS GLY ASP THR ILE ASP GLN LEU GLY ASP VAL ILE GLU
SEQRES 14 A 316 GLN ILE LYS THR HIS PRO TYR SER ARG ARG LEU ILE VAL
SEQRES 15 A 316 SER ALA TRP ASN PRO GLU ASP VAL PRO THR MET ALA LEU
SEQRES 16 A 316 PRO PRO CYS HIS THR LEU TYR GLN PHE TYR VAL ASN ASP
SEQRES 17 A 316 GLY LYS LEU SER LEU GLN LEU TYR GLN ARG SER ALA ASP
SEQRES 18 A 316 ILE PHE LEU GLY VAL PRO PHE ASN ILE ALA SER TYR ALA
SEQRES 19 A 316 LEU LEU THR HIS LEU VAL ALA HIS GLU CYS GLY LEU GLU
SEQRES 20 A 316 VAL GLY GLU PHE ILE HIS THR PHE GLY ASP ALA HIS LEU
SEQRES 21 A 316 TYR VAL ASN HIS LEU ASP GLN ILE LYS GLU GLN LEU SER
SEQRES 22 A 316 ARG THR PRO ARG PRO ALA PRO THR LEU GLN LEU ASN PRO
SEQRES 23 A 316 ASP LYS HIS ASP ILE PHE ASP PHE ASP MET LYS ASP ILE
SEQRES 24 A 316 LYS LEU LEU ASN TYR ASP PRO TYR PRO ALA ILE LYS ALA
SEQRES 25 A 316 PRO VAL ALA VAL
HET 15C A 468 21
HET UMP A 469 20
HETNAM 15C 2-(4-ACETYLPHENYL)-4-METHYL-1H-ISOINDOLE-1,3(2H)-DIONE
HETNAM UMP 2'-DEOXYURIDINE 5'-MONOPHOSPHATE
HETSYN UMP DUMP
FORMUL 2 15C C17 H13 N O3
FORMUL 3 UMP C9 H13 N2 O8 P
FORMUL 4 HOH *147(H2 O)
HELIX 1 1 GLU A 3 GLY A 17 1 15
HELIX 2 2 SER A 41 GLY A 43 5 3
HELIX 3 3 PRO A 53 HIS A 66 1 14
HELIX 4 4 ILE A 71 GLN A 76 1 6
HELIX 5 5 TRP A 82 LYS A 92 1 11
HELIX 6 6 GLY A 105 ASP A 111 1 7
HELIX 7 7 GLU A 113 ASP A 132 1 20
HELIX 8 8 ASP A 132 GLY A 140 1 9
HELIX 9 9 VAL A 145 ALA A 152 1 8
HELIX 10 10 ASP A 162 HIS A 174 1 13
HELIX 11 11 GLY A 225 CYS A 244 1 20
HELIX 12 12 HIS A 264 SER A 273 1 10
HELIX 13 13 ASP A 290 PHE A 294 5 5
HELIX 14 14 ASP A 295 LYS A 297 5 3
SHEET 1 A 4 HIS A 18 PRO A 21 0
SHEET 2 A 4 GLY A 27 PHE A 32 -1 O THR A 28 N LYS A 20
SHEET 3 A 4 GLU A 247 TYR A 261 -1 O LEU A 260 N TYR A 29
SHEET 4 A 4 GLN A 35 ASP A 39 -1 N MET A 36 O HIS A 253
SHEET 1 B 6 HIS A 18 PRO A 21 0
SHEET 2 B 6 GLY A 27 PHE A 32 -1 O THR A 28 N LYS A 20
SHEET 3 B 6 GLU A 247 TYR A 261 -1 O LEU A 260 N TYR A 29
SHEET 4 B 6 LYS A 210 ASP A 221 1 N LEU A 211 O GLY A 249
SHEET 5 B 6 HIS A 199 ASN A 207 -1 N TYR A 205 O SER A 212
SHEET 6 B 6 ILE A 181 SER A 183 -1 N VAL A 182 O TYR A 202
SHEET 1 C 2 TRP A 153 HIS A 154 0
SHEET 2 C 2 THR A 160 ILE A 161 -1 O ILE A 161 N TRP A 153
SHEET 1 D 2 THR A 281 LEU A 284 0
SHEET 2 D 2 ILE A 299 LEU A 302 -1 O LYS A 300 N GLN A 283
SITE 1 AC1 8 GLU A 60 ILE A 81 TRP A 82 TRP A 85
SITE 2 AC1 8 LEU A 195 HOH A 461 HOH A 462 UMP A 469
SITE 1 AC2 15 ARG A 178 ARG A 179 CYS A 198 HIS A 199
SITE 2 AC2 15 GLN A 217 ARG A 218 SER A 219 ALA A 220
SITE 3 AC2 15 ASP A 221 GLY A 225 ASN A 229 HIS A 259
SITE 4 AC2 15 TYR A 261 HOH A 345 15C A 468
CRYST1 77.656 77.656 224.969 90.00 90.00 120.00 P 61 2 2 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 0.012877 0.007435 0.000000 0.00000
SCALE2 0.000000 0.014869 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004445 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
