HEADER LIGASE 06-MAR-07 2UUO
TITLE CRYSTAL STRUCTURE OF MURD LIGASE IN COMPLEX WITH D-GLU CONTAINING
TITLE 2 SULFONAMIDE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE LIGASE, UDP-N-
COMPND 5 ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE SYNTHETASE, D-GLUTAMIC ACID-
COMPND 6 ADDING ENZYME;
COMPND 7 EC: 6.3.2.9;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: INHIBITOR N-(6-PENTOXY-NAPHTHALENE-2-SULFONYL)-D-
COMPND 10 GLUTAMIC ACID BOUND
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI DH5[ALPHA];
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 668369;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PABD16
KEYWDS MURD-INHIBITOR COMPLEX, PEPTIDOGLYCAN SYNTHESIS, LIGASE, CELL WALL,
KEYWDS 2 CELL SHAPE, CELL CYCLE, NUCLEOTIDE-BINDING, SULFONAMIDE INHIBITOR,
KEYWDS 3 MURD LIGASE, ATP-BINDING, CELL DIVISION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HUMLJAN,M.KOTNIK,C.CONTRERAS-MARTEL,D.BLANOT,U.URLEB,A.DESSEN,
AUTHOR 2 T.SOLMAJER,S.GOBEC
REVDAT 5 13-DEC-23 2UUO 1 LINK
REVDAT 4 31-JAN-18 2UUO 1 SOURCE JRNL
REVDAT 3 24-MAR-09 2UUO 1 JRNL
REVDAT 2 24-FEB-09 2UUO 1 VERSN
REVDAT 1 25-MAR-08 2UUO 0
JRNL AUTH J.HUMLJAN,M.KOTNIK,C.CONTRERAS-MARTEL,D.BLANOT,U.URLEB,
JRNL AUTH 2 A.DESSEN,T.SOLMAJER,S.GOBEC
JRNL TITL NOVEL NAPHTHALENE-N-SULFONYL-D-GLUTAMIC ACID DERIVATIVES AS
JRNL TITL 2 INHIBITORS OF MURD, A KEY PEPTIDOGLYCAN BIOSYNTHESIS ENZYME.
JRNL REF J. MED. CHEM. V. 51 7486 2008
JRNL REFN ISSN 1520-4804
JRNL PMID 19007109
JRNL DOI 10.1021/JM800762U
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 18383
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 939
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1252
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.59
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.3200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3228
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 233
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.04000
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): 0.437
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.290
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.829
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3315 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4499 ; 1.415 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 426 ; 3.101 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 141 ;39.244 ;24.539
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 542 ;12.629 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;17.326 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 520 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2495 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1705 ; 0.234 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2292 ; 0.320 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 231 ; 0.166 ; 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): 37 ; 0.217 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.209 ; 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): 2128 ; 1.163 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3393 ; 2.058 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1187 ; 3.501 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1106 ; 5.457 ; 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 2UUO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1290031762.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-SEP-06
REMARK 200 TEMPERATURE (KELVIN) : 288
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18900
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.28000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.800
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 3UAG
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 1.7 M
REMARK 280 (NH4)2SO4, 7% PEG 400, 100 MM HEPES, PH 7.5; THEN SOAKED IN 2 MM
REMARK 280 INHIBITOR SOLUTION.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 67.38950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.69475
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 101.08425
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 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 0
REMARK 465 ILE A 220
REMARK 465 ARG A 221
REMARK 465 GLY A 222
REMARK 465 ALA A 223
REMARK 465 ASP A 224
REMARK 465 GLU A 225
REMARK 465 GLN A 242
REMARK 465 GLN A 243
REMARK 465 GLY A 244
REMARK 465 HIS A 440
REMARK 465 HIS A 441
REMARK 465 HIS A 442
REMARK 465 HIS A 443
REMARK 465 HIS A 444
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 HIS A 439 CA C O CB CG ND1 CD2
REMARK 470 HIS A 439 CE1 NE2
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 2095 O HOH A 2120 2.04
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 LEU A 13 -131.17 -97.40
REMARK 500 SER A 56 174.16 173.19
REMARK 500 LEU A 147 109.53 -47.77
REMARK 500 SER A 167 -17.78 -141.48
REMARK 500 HIS A 301 -2.97 75.47
REMARK 500 ARG A 380 81.30 -176.09
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 A1440
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LK3 A1441
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E0D RELATED DB: PDB
REMARK 900 UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
REMARK 900 RELATED ID: 1EEH RELATED DB: PDB
REMARK 900 UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
REMARK 900 RELATED ID: 1UAG RELATED DB: PDB
REMARK 900 UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
REMARK 900 RELATED ID: 2JFF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MURD LIGASE IN COMPLEX WITH D-GLU CONTAINING
REMARK 900 SULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 2JFG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MURD LIGASE IN COMPLEX WITH UMA AND ADP
REMARK 900 RELATED ID: 2JFH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MURD LIGASE IN COMPLEX WITH L-GLU CONTAINING
REMARK 900 SULFONAMIDE INHIBITOR
REMARK 900 RELATED ID: 2UAG RELATED DB: PDB
REMARK 900 UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
REMARK 900 RELATED ID: 3UAG RELATED DB: PDB
REMARK 900 UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
REMARK 900 RELATED ID: 4UAG RELATED DB: PDB
REMARK 900 UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
REMARK 900 RELATED ID: 2UUP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MURD LIGASE IN COMPLEX WITH D-GLU CONTAINING
REMARK 900 SULFONAMIDE INHIBITOR
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 C-TERMINAL HIS-TAG (SHHHHHH)
DBREF 2UUO A 0 0 PDB 2UUO 2UUO 0 0
DBREF 2UUO A 1 437 UNP P14900 MURD_ECOLI 1 437
DBREF 2UUO A 438 444 PDB 2UUO 2UUO 438 444
SEQRES 1 A 445 MET ALA ASP TYR GLN GLY LYS ASN VAL VAL ILE ILE GLY
SEQRES 2 A 445 LEU GLY LEU THR GLY LEU SER CYS VAL ASP PHE PHE LEU
SEQRES 3 A 445 ALA ARG GLY VAL THR PRO ARG VAL MET ASP THR ARG MET
SEQRES 4 A 445 THR PRO PRO GLY LEU ASP LYS LEU PRO GLU ALA VAL GLU
SEQRES 5 A 445 ARG HIS THR GLY SER LEU ASN ASP GLU TRP LEU MET ALA
SEQRES 6 A 445 ALA ASP LEU ILE VAL ALA SER PRO GLY ILE ALA LEU ALA
SEQRES 7 A 445 HIS PRO SER LEU SER ALA ALA ALA ASP ALA GLY ILE GLU
SEQRES 8 A 445 ILE VAL GLY ASP ILE GLU LEU PHE CYS ARG GLU ALA GLN
SEQRES 9 A 445 ALA PRO ILE VAL ALA ILE THR GLY SER ASN GLY LYS SER
SEQRES 10 A 445 THR VAL THR THR LEU VAL GLY GLU MET ALA LYS ALA ALA
SEQRES 11 A 445 GLY VAL ASN VAL GLY VAL GLY GLY ASN ILE GLY LEU PRO
SEQRES 12 A 445 ALA LEU MET LEU LEU ASP ASP GLU CYS GLU LEU TYR VAL
SEQRES 13 A 445 LEU GLU LEU SER SER PHE GLN LEU GLU THR THR SER SER
SEQRES 14 A 445 LEU GLN ALA VAL ALA ALA THR ILE LEU ASN VAL THR GLU
SEQRES 15 A 445 ASP HIS MET ASP ARG TYR PRO PHE GLY LEU GLN GLN TYR
SEQRES 16 A 445 ARG ALA ALA KCX LEU ARG ILE TYR GLU ASN ALA LYS VAL
SEQRES 17 A 445 CYS VAL VAL ASN ALA ASP ASP ALA LEU THR MET PRO ILE
SEQRES 18 A 445 ARG GLY ALA ASP GLU ARG CYS VAL SER PHE GLY VAL ASN
SEQRES 19 A 445 MET GLY ASP TYR HIS LEU ASN HIS GLN GLN GLY GLU THR
SEQRES 20 A 445 TRP LEU ARG VAL LYS GLY GLU LYS VAL LEU ASN VAL LYS
SEQRES 21 A 445 GLU MET LYS LEU SER GLY GLN HIS ASN TYR THR ASN ALA
SEQRES 22 A 445 LEU ALA ALA LEU ALA LEU ALA ASP ALA ALA GLY LEU PRO
SEQRES 23 A 445 ARG ALA SER SER LEU LYS ALA LEU THR THR PHE THR GLY
SEQRES 24 A 445 LEU PRO HIS ARG PHE GLU VAL VAL LEU GLU HIS ASN GLY
SEQRES 25 A 445 VAL ARG TRP ILE ASN ASP SER LYS ALA THR ASN VAL GLY
SEQRES 26 A 445 SER THR GLU ALA ALA LEU ASN GLY LEU HIS VAL ASP GLY
SEQRES 27 A 445 THR LEU HIS LEU LEU LEU GLY GLY ASP GLY LYS SER ALA
SEQRES 28 A 445 ASP PHE SER PRO LEU ALA ARG TYR LEU ASN GLY ASP ASN
SEQRES 29 A 445 VAL ARG LEU TYR CYS PHE GLY ARG ASP GLY ALA GLN LEU
SEQRES 30 A 445 ALA ALA LEU ARG PRO GLU VAL ALA GLU GLN THR GLU THR
SEQRES 31 A 445 MET GLU GLN ALA MET ARG LEU LEU ALA PRO ARG VAL GLN
SEQRES 32 A 445 PRO GLY ASP MET VAL LEU LEU SER PRO ALA CYS ALA SER
SEQRES 33 A 445 LEU ASP GLN PHE LYS ASN PHE GLU GLN ARG GLY ASN GLU
SEQRES 34 A 445 PHE ALA ARG LEU ALA LYS GLU LEU GLY SER HIS HIS HIS
SEQRES 35 A 445 HIS HIS HIS
MODRES 2UUO KCX A 198 LYS LYSINE NZ-CARBOXYLIC ACID
HET KCX A 198 12
HET SO4 A1440 5
HET LK3 A1441 29
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM SO4 SULFATE ION
HETNAM LK3 N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC
HETNAM 2 LK3 ACID
FORMUL 1 KCX C7 H14 N2 O4
FORMUL 2 SO4 O4 S 2-
FORMUL 3 LK3 C20 H25 N O7 S
FORMUL 4 HOH *233(H2 O)
HELIX 1 1 LEU A 13 ARG A 27 1 15
HELIX 2 2 GLY A 42 LEU A 46 5 5
HELIX 3 3 ASN A 58 MET A 63 1 6
HELIX 4 4 HIS A 78 ALA A 87 1 10
HELIX 5 5 GLY A 93 ALA A 102 1 10
HELIX 6 6 GLY A 114 ALA A 129 1 16
HELIX 7 7 PRO A 142 LEU A 146 5 5
HELIX 8 8 SER A 159 THR A 165 1 7
HELIX 9 9 PHE A 189 ARG A 200 1 12
HELIX 10 10 ILE A 201 GLU A 203 5 3
HELIX 11 11 ASP A 214 MET A 218 5 5
HELIX 12 12 LYS A 259 MET A 261 5 3
HELIX 13 13 GLY A 265 ALA A 282 1 18
HELIX 14 14 PRO A 285 PHE A 296 1 12
HELIX 15 15 ASN A 322 ASN A 331 1 10
HELIX 16 16 PHE A 352 ARG A 357 1 6
HELIX 17 17 ASP A 372 ALA A 378 1 7
HELIX 18 18 LEU A 379 GLU A 382 5 4
HELIX 19 19 THR A 389 ALA A 398 1 10
HELIX 20 20 PRO A 399 VAL A 401 5 3
HELIX 21 21 ASN A 421 GLY A 437 1 17
SHEET 1 AA 5 ARG A 52 THR A 54 0
SHEET 2 AA 5 ARG A 32 ASP A 35 1 O VAL A 33 N HIS A 53
SHEET 3 AA 5 VAL A 8 ILE A 11 1 O VAL A 8 N ARG A 32
SHEET 4 AA 5 LEU A 67 ALA A 70 1 O LEU A 67 N VAL A 9
SHEET 5 AA 5 GLU A 90 VAL A 92 1 O GLU A 90 N ILE A 68
SHEET 1 AB 6 VAL A 133 GLY A 137 0
SHEET 2 AB 6 LEU A 153 GLU A 157 1 O LEU A 153 N GLY A 134
SHEET 3 AB 6 ILE A 106 THR A 110 1 O VAL A 107 N LEU A 156
SHEET 4 AB 6 ALA A 173 ILE A 176 1 O ALA A 173 N ALA A 108
SHEET 5 AB 6 CYS A 208 ASN A 211 1 O VAL A 209 N ILE A 176
SHEET 6 AB 6 VAL A 228 PHE A 230 1 O VAL A 228 N VAL A 210
SHEET 1 AC 3 TYR A 237 ASN A 240 0
SHEET 2 AC 3 TRP A 247 VAL A 250 -1 O TRP A 247 N ASN A 240
SHEET 3 AC 3 GLU A 253 ASN A 257 -1 O GLU A 253 N VAL A 250
SHEET 1 AD 6 GLU A 304 HIS A 309 0
SHEET 2 AD 6 VAL A 312 ASN A 316 -1 O VAL A 312 N HIS A 309
SHEET 3 AD 6 MET A 406 LEU A 409 1 O VAL A 407 N ILE A 315
SHEET 4 AD 6 LEU A 339 GLY A 344 1 O HIS A 340 N LEU A 408
SHEET 5 AD 6 VAL A 364 PHE A 369 1 O ARG A 365 N LEU A 341
SHEET 6 AD 6 ALA A 384 GLN A 386 1 O GLU A 385 N CYS A 368
SSBOND 1 CYS A 208 CYS A 227 1555 1555 1.54
LINK C ALA A 197 N KCX A 198 1555 1555 1.33
LINK C KCX A 198 N LEU A 199 1555 1555 1.33
SITE 1 AC1 8 ASN A 113 GLY A 114 LYS A 115 SER A 116
SITE 2 AC1 8 THR A 117 ARG A 302 LYS A 319 HOH A2231
SITE 1 AC2 15 ILE A 11 GLY A 12 ARG A 37 GLY A 73
SITE 2 AC2 15 PHE A 161 HIS A 183 LYS A 348 ALA A 414
SITE 3 AC2 15 SER A 415 LEU A 416 ASN A 421 PHE A 422
SITE 4 AC2 15 HOH A2105 HOH A2232 HOH A2233
CRYST1 65.297 65.297 134.779 90.00 90.00 90.00 P 41 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 0.015315 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015315 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007420 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
