HEADER TRANSFERASE 14-MAY-07 2V0J
TITLE CHARACTERIZATION OF SUBSTRATE BINDING AND CATALYSIS OF THE POTENTIAL
TITLE 2 ANTIBACTERIAL TARGET N-ACETYLGLUCOSAMINE-1-PHOSPHATE
TITLE 3 URIDYLTRANSFERASE (GLMU)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL PROTEIN GLMU;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GLMU FROM HAEMOPHILIS INFLUENZAE;
COMPND 5 EC: 2.-.-.-
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE 3 ORGANISM_TAXID: 727
KEYWDS GLMU, CELL WALL, MAGNESIUM, CELL SHAPE, TRANSFERASE, PEPTIDOGLYCAN
KEYWDS 2 SYNTHESIS, ASSOCIATIVE MECHANISM, MULTIFUNCTIONAL ENZYME,
KEYWDS 3 NUCLEOTIDYLTRANSFERASE, URIDYLATION, METAL-BINDING, ACYLTRANSFERASE,
KEYWDS 4 CATALYTIC MECHANISM
EXPDTA X-RAY DIFFRACTION
AUTHOR I.MOCHALKIN,S.LIGHTLE,J.F.OHREN,N.Y.CHIRGADZE
REVDAT 3 13-DEC-23 2V0J 1 LINK
REVDAT 2 24-FEB-09 2V0J 1 VERSN
REVDAT 1 15-JAN-08 2V0J 0
JRNL AUTH I.MOCHALKIN,S.LIGHTLE,Y.ZHU,J.F.OHREN,C.SPESSARD,
JRNL AUTH 2 N.Y.CHIRGADZE,C.BANOTAI,M.MELNICK,L.MCDOWELL
JRNL TITL CHARACTERIZATION OF SUBSTRATE BINDING AND CATALYSIS IN THE
JRNL TITL 2 POTENTIAL ANTIBACTERIAL TARGET
JRNL TITL 3 N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE (GLMU).
JRNL REF PROTEIN SCI. V. 16 2657 2007
JRNL REFN ISSN 0961-8368
JRNL PMID 18029420
JRNL DOI 10.1110/PS.073135107
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.5
REMARK 3 NUMBER OF REFLECTIONS : 42985
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2307
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) : 3163
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1980
REMARK 3 BIN FREE R VALUE SET COUNT : 163
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3406
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 361
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.63000
REMARK 3 B22 (A**2) : 0.63000
REMARK 3 B33 (A**2) : -0.94000
REMARK 3 B12 (A**2) : 0.31000
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): 0.156
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.141
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.084
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.482
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3548 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3246 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4802 ; 1.234 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7574 ; 1.065 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 448 ; 5.914 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 159 ;33.908 ;25.849
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 609 ;13.016 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;17.427 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 554 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3920 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 628 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 590 ; 0.203 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3069 ; 0.177 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1703 ; 0.161 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1970 ; 0.081 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 246 ; 0.143 ; 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): 21 ; 0.194 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 127 ; 0.238 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 39 ; 0.158 ; 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): 2883 ; 0.916 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3564 ; 1.104 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1507 ; 0.986 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1238 ; 1.408 ; 3.000
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2V0J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1290032565.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45786
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.1000
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 (%) : 91.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.30000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: HKL-2000
REMARK 200 STARTING MODEL: PDB ENTRY 2VOI
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 54.36000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 31.38476
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 108.91800
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 54.36000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 31.38476
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 108.91800
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 54.36000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 31.38476
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 108.91800
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 54.36000
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 31.38476
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 108.91800
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 54.36000
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 31.38476
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 108.91800
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 54.36000
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 31.38476
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 108.91800
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 62.76952
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 217.83600
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 62.76952
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 217.83600
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 62.76952
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 217.83600
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 62.76952
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 217.83600
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 62.76952
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 217.83600
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 62.76952
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 217.83600
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 15820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 64970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.6 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 108.72000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 54.36000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 94.15428
REMARK 350 BIOMT3 3 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 MG MG A1454 LIES ON A SPECIAL POSITION.
REMARK 375 MG MG A1455 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 MET A 1
REMARK 465 THR A 2
REMARK 465 LYS A 3
REMARK 465 ILE A 453
REMARK 465 LYS A 454
REMARK 465 LYS A 455
REMARK 465 LYS A 456
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 2182 O HOH A 2201 2.17
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 ALA A 12 20.72 -140.90
REMARK 500 ASN A 124 18.62 55.65
REMARK 500 ASN A 391 141.74 36.27
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 A2061 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH A2109 DISTANCE = 6.10 ANGSTROMS
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 A1454 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 406 OD2
REMARK 620 2 ASP A 406 OD2 97.1
REMARK 620 3 ASP A 406 OD2 97.0 97.0
REMARK 620 4 HOH A2310 O 85.7 174.7 87.2
REMARK 620 5 HOH A2310 O 87.3 85.7 174.6 89.8
REMARK 620 6 HOH A2310 O 174.6 87.3 85.6 89.8 89.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1455 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 406 OD1
REMARK 620 2 ASP A 406 OD1 97.1
REMARK 620 3 ASP A 406 OD1 96.9 97.0
REMARK 620 4 HOH A2309 O 171.2 91.7 83.2
REMARK 620 5 HOH A2309 O 83.2 171.5 91.4 87.9
REMARK 620 6 HOH A2309 O 91.7 83.5 171.3 88.1 88.1
REMARK 620 N 1 2 3 4 5
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2U A1453
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1454
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1455
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A1456
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A1457
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A1458
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1459
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1462
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1463
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1464
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2V0H RELATED DB: PDB
REMARK 900 CHARACTERIZATION OF SUBSTRATE BINDING AND CATALYSIS OF THE
REMARK 900 POTENTIAL ANTIBACTERIAL TARGET N-ACETYLGLUCOSAMINE-1-PHOSPHATE
REMARK 900 URIDYLTRANSFERASE (GLMU)
REMARK 900 RELATED ID: 2V0I RELATED DB: PDB
REMARK 900 CHARACTERIZATION OF SUBSTRATE BINDING AND CATALYSIS OF THE
REMARK 900 POTENTIAL ANTIBACTERIAL TARGET N-ACETYLGLUCOSAMINE-1-PHOSPHATE
REMARK 900 URIDYLTRANSFERASE (GLMU)
REMARK 900 RELATED ID: 2V0K RELATED DB: PDB
REMARK 900 CHARACTERIZATION OF SUBSTRATE BINDING AND CATALYSIS OF THE
REMARK 900 POTENTIAL ANTIBACTERIAL TARGET N-ACETYLGLUCOSAMINE-1-PHOSPHATE
REMARK 900 URIDYLTRANSFERASE (GLMU)
REMARK 900 RELATED ID: 2V0L RELATED DB: PDB
REMARK 900 CHARACTERIZATION OF SUBSTRATE BINDING AND CATALYSIS OF THE
REMARK 900 POTENTIAL ANTIBACTERIAL TARGET N-ACETYLGLUCOSAMINE-1-PHOSPHATE
REMARK 900 URIDYLTRANSFERASE (GLMU)
DBREF 2V0J A 1 456 UNP P43889 GLMU_HAEIN 1 456
SEQRES 1 A 456 MET THR LYS LYS ALA LEU SER ALA VAL ILE LEU ALA ALA
SEQRES 2 A 456 GLY LYS GLY THR ARG MET TYR SER ASP LEU PRO LYS VAL
SEQRES 3 A 456 LEU HIS THR ILE ALA GLY LYS PRO MET VAL LYS HIS VAL
SEQRES 4 A 456 ILE ASP THR ALA HIS GLN LEU GLY SER GLU ASN ILE HIS
SEQRES 5 A 456 LEU ILE TYR GLY HIS GLY GLY ASP LEU MET ARG THR HIS
SEQRES 6 A 456 LEU ALA ASN GLU GLN VAL ASN TRP VAL LEU GLN THR GLU
SEQRES 7 A 456 GLN LEU GLY THR ALA HIS ALA VAL GLN GLN ALA ALA PRO
SEQRES 8 A 456 PHE PHE LYS ASP ASN GLU ASN ILE VAL VAL LEU TYR GLY
SEQRES 9 A 456 ASP ALA PRO LEU ILE THR LYS GLU THR LEU GLU LYS LEU
SEQRES 10 A 456 ILE GLU ALA LYS PRO GLU ASN GLY ILE ALA LEU LEU THR
SEQRES 11 A 456 VAL ASN LEU ASP ASN PRO THR GLY TYR GLY ARG ILE ILE
SEQRES 12 A 456 ARG GLU ASN GLY ASN VAL VAL ALA ILE VAL GLU GLN LYS
SEQRES 13 A 456 ASP ALA ASN ALA GLU GLN LEU ASN ILE LYS GLU VAL ASN
SEQRES 14 A 456 THR GLY VAL MET VAL SER ASP GLY ALA SER PHE LYS LYS
SEQRES 15 A 456 TRP LEU ALA ARG VAL GLY ASN ASN ASN ALA GLN GLY GLU
SEQRES 16 A 456 TYR TYR LEU THR ASP LEU ILE ALA LEU ALA ASN GLN ASP
SEQRES 17 A 456 ASN CYS GLN VAL VAL ALA VAL GLN ALA THR ASP VAL MET
SEQRES 18 A 456 GLU VAL GLU GLY ALA ASN ASN ARG LEU GLN LEU ALA ALA
SEQRES 19 A 456 LEU GLU ARG TYR PHE GLN ASN LYS GLN ALA SER LYS LEU
SEQRES 20 A 456 LEU LEU GLU GLY VAL MET ILE TYR ASP PRO ALA ARG PHE
SEQRES 21 A 456 ASP LEU ARG GLY THR LEU GLU HIS GLY LYS ASP VAL GLU
SEQRES 22 A 456 ILE ASP VAL ASN VAL ILE ILE GLU GLY ASN VAL LYS LEU
SEQRES 23 A 456 GLY ASP ARG VAL LYS ILE GLY THR GLY CYS VAL LEU LYS
SEQRES 24 A 456 ASN VAL VAL ILE GLY ASN ASP VAL GLU ILE LYS PRO TYR
SEQRES 25 A 456 SER VAL LEU GLU ASP SER ILE VAL GLY GLU LYS ALA ALA
SEQRES 26 A 456 ILE GLY PRO PHE SER ARG LEU ARG PRO GLY ALA GLU LEU
SEQRES 27 A 456 ALA ALA GLU THR HIS VAL GLY ASN PHE VAL GLU ILE LYS
SEQRES 28 A 456 LYS SER THR VAL GLY LYS GLY SER LYS VAL ASN HIS LEU
SEQRES 29 A 456 THR TYR VAL GLY ASP SER GLU ILE GLY SER ASN CYS ASN
SEQRES 30 A 456 ILE GLY ALA GLY VAL ILE THR CYS ASN TYR ASP GLY ALA
SEQRES 31 A 456 ASN LYS PHE LYS THR ILE ILE GLY ASP ASP VAL PHE VAL
SEQRES 32 A 456 GLY SER ASP THR GLN LEU VAL ALA PRO VAL LYS VAL ALA
SEQRES 33 A 456 ASN GLY ALA THR ILE GLY ALA GLY THR THR ILE THR ARG
SEQRES 34 A 456 ASP VAL GLY GLU ASN GLU LEU VAL ILE THR ARG VAL ALA
SEQRES 35 A 456 GLN ARG HIS ILE GLN GLY TRP GLN ARG PRO ILE LYS LYS
SEQRES 36 A 456 LYS
HET H2U A1453 21
HET MG A1454 1
HET MG A1455 1
HET PG4 A1456 13
HET PGE A1457 10
HET PGE A1458 10
HET SO4 A1459 5
HET SO4 A1460 5
HET SO4 A1461 5
HET SO4 A1462 5
HET SO4 A1463 5
HET SO4 A1464 5
HETNAM H2U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM SO4 SULFATE ION
FORMUL 2 H2U C9 H15 N2 O9 P
FORMUL 3 MG 2(MG 2+)
FORMUL 5 PG4 C8 H18 O5
FORMUL 6 PGE 2(C6 H14 O4)
FORMUL 8 SO4 6(O4 S 2-)
FORMUL 14 HOH *361(H2 O)
HELIX 1 1 GLY A 16 TYR A 20 5 5
HELIX 2 2 PRO A 24 LEU A 27 5 4
HELIX 3 3 MET A 35 LEU A 46 1 12
HELIX 4 4 GLY A 58 LEU A 66 1 9
HELIX 5 5 GLY A 81 ALA A 90 1 10
HELIX 6 6 PRO A 91 PHE A 93 5 3
HELIX 7 7 THR A 110 LYS A 121 1 12
HELIX 8 8 ASN A 159 ASN A 164 1 6
HELIX 9 9 GLY A 177 ALA A 185 1 9
HELIX 10 10 TYR A 197 THR A 199 5 3
HELIX 11 11 ASP A 200 ASP A 208 1 9
HELIX 12 12 ASP A 219 GLU A 224 5 6
HELIX 13 13 ASN A 228 GLU A 250 1 23
HELIX 14 14 ASP A 256 ALA A 258 5 3
SHEET 1 AA 7 ASN A 72 LEU A 75 0
SHEET 2 AA 7 ILE A 51 TYR A 55 1 O ILE A 51 N ASN A 72
SHEET 3 AA 7 LEU A 6 LEU A 11 1 O ALA A 8 N HIS A 52
SHEET 4 AA 7 ASN A 98 TYR A 103 1 O ASN A 98 N SER A 7
SHEET 5 AA 7 GLU A 167 ASP A 176 -1 O MET A 173 N VAL A 101
SHEET 6 AA 7 ILE A 126 ASN A 132 -1 O ALA A 127 N VAL A 174
SHEET 7 AA 7 VAL A 212 GLN A 216 1 O VAL A 213 N LEU A 128
SHEET 1 AB 2 THR A 29 ILE A 30 0
SHEET 2 AB 2 LYS A 33 PRO A 34 -1 O LYS A 33 N ILE A 30
SHEET 1 AC 2 ARG A 141 GLU A 145 0
SHEET 2 AC 2 ASN A 148 VAL A 153 -1 O ASN A 148 N GLU A 145
SHEET 1 AD 8 MET A 253 ILE A 254 0
SHEET 2 AD 8 GLU A 273 ILE A 274 1 N ILE A 274 O MET A 253
SHEET 3 AD 8 LYS A 291 ILE A 292 1 N ILE A 292 O GLU A 273
SHEET 4 AD 8 GLU A 308 ILE A 309 1 N ILE A 309 O LYS A 291
SHEET 5 AD 8 ALA A 325 ILE A 326 1 N ILE A 326 O GLU A 308
SHEET 6 AD 8 HIS A 343 LYS A 351 1 N VAL A 344 O ALA A 325
SHEET 7 AD 8 SER A 330 LEU A 332 1 O ARG A 331 N ILE A 350
SHEET 8 AD 8 VAL A 314 VAL A 320 1 O VAL A 314 N LEU A 332
SHEET 1 AE11 MET A 253 ILE A 254 0
SHEET 2 AE11 GLU A 273 ILE A 274 1 N ILE A 274 O MET A 253
SHEET 3 AE11 LYS A 291 ILE A 292 1 N ILE A 292 O GLU A 273
SHEET 4 AE11 GLU A 308 ILE A 309 1 N ILE A 309 O LYS A 291
SHEET 5 AE11 ALA A 325 ILE A 326 1 N ILE A 326 O GLU A 308
SHEET 6 AE11 HIS A 343 LYS A 351 1 N VAL A 344 O ALA A 325
SHEET 7 AE11 LYS A 360 GLY A 368 1 O VAL A 361 N GLY A 345
SHEET 8 AE11 ASN A 377 ILE A 378 1 O ILE A 378 N ASN A 362
SHEET 9 AE11 PHE A 402 VAL A 403 1 N VAL A 403 O ASN A 377
SHEET 10 AE11 THR A 420 ILE A 421 1 N ILE A 421 O PHE A 402
SHEET 11 AE11 LEU A 436 VAL A 437 1 N VAL A 437 O THR A 420
SHEET 1 AF 3 ILE A 383 ASN A 386 0
SHEET 2 AF 3 GLN A 408 ALA A 411 1 O LEU A 409 N CYS A 385
SHEET 3 AF 3 THR A 426 ILE A 427 1 O ILE A 427 N VAL A 410
LINK OD2 ASP A 406 MG MG A1454 1555 1555 2.11
LINK OD2 ASP A 406 MG MG A1454 2655 1555 2.11
LINK OD2 ASP A 406 MG MG A1454 3665 1555 2.11
LINK OD1 ASP A 406 MG MG A1455 2655 1555 2.10
LINK OD1 ASP A 406 MG MG A1455 3665 1555 2.10
LINK OD1 ASP A 406 MG MG A1455 1555 1555 2.10
LINK MG MG A1454 O HOH A2310 1555 1555 2.17
LINK MG MG A1454 O HOH A2310 1555 2655 2.17
LINK MG MG A1454 O HOH A2310 1555 3665 2.17
LINK MG MG A1455 O HOH A2309 1555 1555 2.08
LINK MG MG A1455 O HOH A2309 1555 2655 2.08
LINK MG MG A1455 O HOH A2309 1555 3665 2.07
CISPEP 1 GLY A 327 PRO A 328 0 -0.74
CISPEP 2 ALA A 411 PRO A 412 0 -2.16
SITE 1 AC1 14 LEU A 11 ALA A 13 GLY A 14 LYS A 25
SITE 2 AC1 14 GLN A 76 GLN A 79 LEU A 80 GLY A 81
SITE 3 AC1 14 THR A 82 TYR A 103 ASP A 105 HOH A2348
SITE 4 AC1 14 HOH A2349 HOH A2350
SITE 1 AC2 2 ASP A 406 HOH A2310
SITE 1 AC3 2 ASP A 406 HOH A2309
SITE 1 AC4 9 ASN A 72 PHE A 92 ASN A 386 ASP A 388
SITE 2 AC4 9 PHE A 402 ALA A 423 HOH A2318 HOH A2351
SITE 3 AC4 9 HOH A2352
SITE 1 AC5 7 ASP A 157 ASN A 159 GLN A 162 ASN A 189
SITE 2 AC5 7 ASN A 191 ALA A 192 GLY A 194
SITE 1 AC6 8 GLU A 49 GLN A 70 VAL A 71 ASN A 72
SITE 2 AC6 8 TYR A 387 PRO A 412 HOH A2041 HOH A2353
SITE 1 AC7 7 LYS A 360 ASN A 362 HIS A 363 LYS A 392
SITE 2 AC7 7 HOH A2256 HOH A2286 HOH A2354
SITE 1 AC8 7 ASN A 377 ARG A 451 HOH A2284 HOH A2285
SITE 2 AC8 7 HOH A2296 HOH A2355 HOH A2356
SITE 1 AC9 4 ARG A 331 ARG A 333 PRO A 334 HOH A2357
SITE 1 BC1 5 GLY A 14 LYS A 15 GLY A 16 THR A 17
SITE 2 BC1 5 HOH A2358
SITE 1 BC2 2 HIS A 57 GLN A 79
SITE 1 BC3 4 HIS A 57 GLY A 58 HOH A2360 HOH A2361
CRYST1 108.720 108.720 326.754 90.00 90.00 120.00 H 3 2 18
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 0.009198 0.005310 0.000000 0.00000
SCALE2 0.000000 0.010621 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003060 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
