HEADER LIGASE 31-JAN-00 1EEH
TITLE UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 6.3.2.9;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: JM83 (PMLD58)
KEYWDS LIGASE, PEPTIDOGLYCAN SYNTHESIS, MURD, ADP-FORMING ENZYME
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.BERTRAND,E.FANCHON,L.MARTIN,L.CHANTALAT,G.AUGER,D.BLANOT,J.VAN
AUTHOR 2 HEIJENOORT,O.DIDEBERG
REVDAT 6 07-FEB-24 1EEH 1 REMARK
REVDAT 5 11-APR-18 1EEH 1 REMARK
REVDAT 4 04-APR-18 1EEH 1 REMARK
REVDAT 3 24-FEB-09 1EEH 1 VERSN
REVDAT 2 01-APR-03 1EEH 1 JRNL
REVDAT 1 17-JAN-01 1EEH 0
JRNL AUTH J.A.BERTRAND,E.FANCHON,L.MARTIN,L.CHANTALAT,G.AUGER,
JRNL AUTH 2 D.BLANOT,J.VAN HEIJENOORT,O.DIDEBERG
JRNL TITL "OPEN" STRUCTURES OF MURD: DOMAIN MOVEMENTS AND STRUCTURAL
JRNL TITL 2 SIMILARITIES WITH FOLYLPOLYGLUTAMATE SYNTHETASE.
JRNL REF J.MOL.BIOL. V. 301 1257 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10966819
JRNL DOI 10.1006/JMBI.2000.3994
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.A.BERTRAND,G.AUGER,E.FANCHON,L.MARTIN,D.BLANOT,
REMARK 1 AUTH 2 J.VAN HEIJENOORT,O.DIDEBERG
REMARK 1 TITL CRYSTAL STRUCTURE OF UDP-N-ACETYLMURAMOYL-L-ALANINE:
REMARK 1 TITL 2 D-GLUTAMATE LIGASE FROM ESCHERICHIA COLI
REMARK 1 REF EMBO J. V. 16 3416 1997
REMARK 1 REFN ISSN 0261-4189
REMARK 1 DOI 10.1093/EMBOJ/16.12.3416
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.A.BERTRAND,G.AUGER,L.MARTIN,E.FANCHON,D.BLANOT,
REMARK 1 AUTH 2 D.LE BELLER,J.VAN HEIJENOORT,O.DIDEBERG
REMARK 1 TITL DETERMINATION OF THE MURD MECHANISM THROUGH CRYSTALLOGRAPHIC
REMARK 1 TITL 2 ANALYSIS OF ENZYME COMPLEXES
REMARK 1 REF J.MOL.BIOL. V. 289 579 1999
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1999.2800
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 13.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 26411
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 SET) : 0.219
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.200
REMARK 3 FREE R VALUE TEST SET COUNT : 2034
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 60.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3131
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE : 0.2860
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 274
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3237
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 186
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.02000
REMARK 3 B22 (A**2) : -4.17000
REMARK 3 B33 (A**2) : 1.15000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.12
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.470
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.860
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.200 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.810 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.730 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.510 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.46
REMARK 3 BSOL : 53.14
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 ELECTRON DENSITY WAS WEAK FOR RESIDUES 111-116 AND RESIDUES
REMARK 3 220-226. IN ADDITION, RESIDUES 240-245 WERE NOT VISIBLE IN
REMARK 3 THE ELECTRON DENSITY AND THEIR COORDINATES ARE NOT INCLUDED
REMARK 3 IN THIS ENTRY.
REMARK 4
REMARK 4 1EEH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1000010494.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-SEP-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.073
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : XRII-CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31255
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.878
REMARK 200 RESOLUTION RANGE LOW (A) : 13.392
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.7
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 49.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.27900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 9.8 MG/ML MURD, 1 MM
REMARK 280 UMA, 1 MM SODIUM AZIDE, 1 MM DTT, 20 MM HEPES PH 7.5 RESEVOIR: 5-
REMARK 280 9 % PEG 3350 MONODISPERSE, 100 MM SODIUM ACETATE PH 5.2, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 29.42000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.45500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.64000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.45500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.42000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.64000
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 ASN A 240
REMARK 465 HIS A 241
REMARK 465 GLN A 242
REMARK 465 GLN A 243
REMARK 465 GLY A 244
REMARK 465 GLU A 245
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 PRO A 411 C - N - CA ANGL. DEV. = 13.3 DEGREES
REMARK 500 PRO A 411 C - N - CD ANGL. DEV. = -13.1 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 SER A 56 176.18 178.86
REMARK 500 ASN A 113 135.24 68.71
REMARK 500 ASP A 149 1.89 -66.12
REMARK 500 ARG A 221 37.23 80.43
REMARK 500 ASP A 224 -167.91 -107.84
REMARK 500 VAL A 258 -9.11 -49.41
REMARK 500 ARG A 380 77.76 -158.95
REMARK 500 GLN A 418 -10.03 -140.10
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 UMA A 450
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UAG RELATED DB: PDB
REMARK 900 RELATED ID: 2UAG RELATED DB: PDB
REMARK 900 RELATED ID: 3UAG RELATED DB: PDB
REMARK 900 RELATED ID: 4UAG RELATED DB: PDB
DBREF 1EEH A 1 437 UNP P14900 MURD_ECOLI 1 437
SEQRES 1 A 437 ALA ASP TYR GLN GLY LYS ASN VAL VAL ILE ILE GLY LEU
SEQRES 2 A 437 GLY LEU THR GLY LEU SER CYS VAL ASP PHE PHE LEU ALA
SEQRES 3 A 437 ARG GLY VAL THR PRO ARG VAL MET ASP THR ARG MET THR
SEQRES 4 A 437 PRO PRO GLY LEU ASP LYS LEU PRO GLU ALA VAL GLU ARG
SEQRES 5 A 437 HIS THR GLY SER LEU ASN ASP GLU TRP LEU MET ALA ALA
SEQRES 6 A 437 ASP LEU ILE VAL ALA SER PRO GLY ILE ALA LEU ALA HIS
SEQRES 7 A 437 PRO SER LEU SER ALA ALA ALA ASP ALA GLY ILE GLU ILE
SEQRES 8 A 437 VAL GLY ASP ILE GLU LEU PHE CYS ARG GLU ALA GLN ALA
SEQRES 9 A 437 PRO ILE VAL ALA ILE THR GLY SER ASN GLY LYS SER THR
SEQRES 10 A 437 VAL THR THR LEU VAL GLY GLU MET ALA LYS ALA ALA GLY
SEQRES 11 A 437 VAL ASN VAL GLY VAL GLY GLY ASN ILE GLY LEU PRO ALA
SEQRES 12 A 437 LEU MET LEU LEU ASP ASP GLU CYS GLU LEU TYR VAL LEU
SEQRES 13 A 437 GLU LEU SER SER PHE GLN LEU GLU THR THR SER SER LEU
SEQRES 14 A 437 GLN ALA VAL ALA ALA THR ILE LEU ASN VAL THR GLU ASP
SEQRES 15 A 437 HIS MET ASP ARG TYR PRO PHE GLY LEU GLN GLN TYR ARG
SEQRES 16 A 437 ALA ALA LYS LEU ARG ILE TYR GLU ASN ALA LYS VAL CYS
SEQRES 17 A 437 VAL VAL ASN ALA ASP ASP ALA LEU THR MET PRO ILE ARG
SEQRES 18 A 437 GLY ALA ASP GLU ARG CYS VAL SER PHE GLY VAL ASN MET
SEQRES 19 A 437 GLY ASP TYR HIS LEU ASN HIS GLN GLN GLY GLU THR TRP
SEQRES 20 A 437 LEU ARG VAL LYS GLY GLU LYS VAL LEU ASN VAL LYS GLU
SEQRES 21 A 437 MET LYS LEU SER GLY GLN HIS ASN TYR THR ASN ALA LEU
SEQRES 22 A 437 ALA ALA LEU ALA LEU ALA ASP ALA ALA GLY LEU PRO ARG
SEQRES 23 A 437 ALA SER SER LEU LYS ALA LEU THR THR PHE THR GLY LEU
SEQRES 24 A 437 PRO HIS ARG PHE GLU VAL VAL LEU GLU HIS ASN GLY VAL
SEQRES 25 A 437 ARG TRP ILE ASN ASP SER LYS ALA THR ASN VAL GLY SER
SEQRES 26 A 437 THR GLU ALA ALA LEU ASN GLY LEU HIS VAL ASP GLY THR
SEQRES 27 A 437 LEU HIS LEU LEU LEU GLY GLY ASP GLY LYS SER ALA ASP
SEQRES 28 A 437 PHE SER PRO LEU ALA ARG TYR LEU ASN GLY ASP ASN VAL
SEQRES 29 A 437 ARG LEU TYR CYS PHE GLY ARG ASP GLY ALA GLN LEU ALA
SEQRES 30 A 437 ALA LEU ARG PRO GLU VAL ALA GLU GLN THR GLU THR MET
SEQRES 31 A 437 GLU GLN ALA MET ARG LEU LEU ALA PRO ARG VAL GLN PRO
SEQRES 32 A 437 GLY ASP MET VAL LEU LEU SER PRO ALA CYS ALA SER LEU
SEQRES 33 A 437 ASP GLN PHE LYS ASN PHE GLU GLN ARG GLY ASN GLU PHE
SEQRES 34 A 437 ALA ARG LEU ALA LYS GLU LEU GLY
HET UMA A 450 49
HETNAM UMA URIDINE-5'-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE
FORMUL 2 UMA C23 H36 N4 O20 P2
FORMUL 3 HOH *186(H2 O)
HELIX 1 1 GLY A 14 ALA A 26 1 13
HELIX 2 2 GLY A 42 LEU A 46 5 5
HELIX 3 3 ASN A 58 ALA A 64 1 7
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 147 5 6
HELIX 8 8 SER A 159 THR A 165 1 7
HELIX 9 9 HIS A 183 TYR A 187 5 5
HELIX 10 10 GLY A 190 ARG A 200 1 11
HELIX 11 11 ILE A 201 GLU A 203 5 3
HELIX 12 12 ASP A 214 MET A 218 5 5
HELIX 13 13 LYS A 259 MET A 261 5 3
HELIX 14 14 GLY A 265 ALA A 282 1 18
HELIX 15 15 PRO A 285 PHE A 296 1 12
HELIX 16 16 ASN A 322 ASN A 331 1 10
HELIX 17 17 LYS A 348 PHE A 352 5 5
HELIX 18 18 PHE A 352 LEU A 359 5 8
HELIX 19 19 ASP A 372 ALA A 378 1 7
HELIX 20 20 LEU A 379 GLU A 382 5 4
HELIX 21 21 THR A 389 ALA A 398 1 10
HELIX 22 22 PRO A 399 VAL A 401 5 3
HELIX 23 23 ASN A 421 GLY A 437 1 17
SHEET 1 A 5 ARG A 52 THR A 54 0
SHEET 2 A 5 ARG A 32 ASP A 35 1 O VAL A 33 N HIS A 53
SHEET 3 A 5 VAL A 8 ILE A 11 1 O VAL A 8 N ARG A 32
SHEET 4 A 5 LEU A 67 ALA A 70 1 O LEU A 67 N VAL A 9
SHEET 5 A 5 GLU A 90 VAL A 92 1 O GLU A 90 N ILE A 68
SHEET 1 B 6 VAL A 133 GLY A 137 0
SHEET 2 B 6 LEU A 153 GLU A 157 1 O LEU A 153 N GLY A 134
SHEET 3 B 6 ILE A 106 THR A 110 1 N VAL A 107 O TYR A 154
SHEET 4 B 6 ALA A 173 ILE A 176 1 O ALA A 173 N ALA A 108
SHEET 5 B 6 VAL A 207 ASN A 211 1 O VAL A 207 N ALA A 174
SHEET 6 B 6 CYS A 227 PHE A 230 1 O VAL A 228 N VAL A 210
SHEET 1 C 3 TYR A 237 HIS A 238 0
SHEET 2 C 3 TRP A 247 VAL A 250 -1 N ARG A 249 O HIS A 238
SHEET 3 C 3 GLU A 253 ASN A 257 -1 N GLU A 253 O VAL A 250
SHEET 1 D 6 GLU A 304 HIS A 309 0
SHEET 2 D 6 VAL A 312 ASN A 316 -1 N VAL A 312 O HIS A 309
SHEET 3 D 6 MET A 406 LEU A 409 1 O VAL A 407 N ILE A 315
SHEET 4 D 6 LEU A 339 GLY A 344 1 N HIS A 340 O MET A 406
SHEET 5 D 6 VAL A 364 PHE A 369 1 N ARG A 365 O LEU A 339
SHEET 6 D 6 ALA A 384 GLN A 386 1 O GLU A 385 N CYS A 368
SITE 1 AC1 20 GLY A 14 LEU A 15 THR A 16 ASP A 35
SITE 2 AC1 20 THR A 36 ARG A 37 SER A 71 PRO A 72
SITE 3 AC1 20 GLY A 73 GLY A 137 ASN A 138 GLY A 140
SITE 4 AC1 20 GLN A 162 HIS A 183 HOH A 502 HOH A 554
SITE 5 AC1 20 HOH A 565 HOH A 684 HOH A1130 HOH A1146
CRYST1 58.840 63.280 114.910 90.00 90.00 90.00 P 21 21 21 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 0.016995 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015803 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008702 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
