HEADER OXIDOREDUCTASE 28-NOV-95 1MBT
TITLE OXIDOREDUCTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MURB;
COMPND 5 EC: 1.1.1.158;
COMPND 6 OTHER_DETAILS: BOUND FLAVIN-ADENINE DINUCLEOTIDE, PH 8.0
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: AB1157 (ATCC)
KEYWDS FLAVOENZYME, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.E.BENSON,C.T.WALSH,J.M.HOGLE
REVDAT 3 14-FEB-24 1MBT 1 REMARK
REVDAT 2 24-FEB-09 1MBT 1 VERSN
REVDAT 1 14-OCT-96 1MBT 0
JRNL AUTH T.E.BENSON,C.T.WALSH,J.M.HOGLE
JRNL TITL THE STRUCTURE OF THE SUBSTRATE-FREE FORM OF MURB, AN
JRNL TITL 2 ESSENTIAL ENZYME FOR THE SYNTHESIS OF BACTERIAL CELL WALLS.
JRNL REF STRUCTURE V. 4 47 1996
JRNL REFN ISSN 0969-2126
JRNL PMID 8805513
JRNL DOI 10.1016/S0969-2126(96)00008-1
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.E.BENSON,D.J.FILMAN,C.T.WALSH,J.M.HOGLE
REMARK 1 TITL AN ENZYME-SUBSTRATE COMPLEX INVOLVED IN BACTERIAL CELL WALL
REMARK 1 TITL 2 BIOSYNTHESIS
REMARK 1 REF NAT.STRUCT.BIOL. V. 2 644 1995
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH T.E.BENSON,C.T.WALSH,J.M.HOGLE
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY CRYSTALLOGRAPHIC
REMARK 1 TITL 2 STUDIES OF UDP-N-ACETYL ENOLPYRUVYLGLUCOSAMINE REDUCTASE
REMARK 1 REF PROTEIN SCI. V. 3 1125 1994
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.E.BENSON,J.L.MARQUARDT,A.C.MARQUARDT,F.A.ETZKORN,C.T.WALSH
REMARK 1 TITL OVEREXPRESSION, PURIFICATION, AND MECHANISTIC STUDY OF
REMARK 1 TITL 2 UDP-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE
REMARK 1 REF BIOCHEMISTRY V. 32 2024 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00
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) (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 7271
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.322
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2654
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 4
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 2.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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: NULL
REMARK 4
REMARK 4 1MBT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174933.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7297
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 12.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 25.20000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.40000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.55000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.40000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.20000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.55000
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 400
REMARK 400 COMPOUND
REMARK 400 DENSITY.
REMARK 400
REMARK 400 THE SECONDARY STRUCTURE ASSIGNMENT IN THIS PDB ENTRY
REMARK 400 REFLECTS THE RESULTS OF AN AUTOMATED PROCEDURE. FOR
REMARK 400 SECONDARY STRUCTURE ASSIGNMENTS MADE BY THE AUTHORS BASED
REMARK 400 ON INSPECTION OF HYDROGEN BONDING PATTERNS, SEE THE
REMARK 400 ORIGINAL REFERENCE.
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 ASN A 2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 3 NE2 HIS A 3 CD2 -0.066
REMARK 500 HIS A 15 NE2 HIS A 15 CD2 -0.076
REMARK 500 HIS A 73 NE2 HIS A 73 CD2 -0.070
REMARK 500 HIS A 82 NE2 HIS A 82 CD2 -0.069
REMARK 500 HIS A 90 NE2 HIS A 90 CD2 -0.071
REMARK 500 HIS A 165 NE2 HIS A 165 CD2 -0.069
REMARK 500 HIS A 212 NE2 HIS A 212 CD2 -0.070
REMARK 500 HIS A 285 NE2 HIS A 285 CD2 -0.066
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 TRP A 8 CD1 - CG - CD2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 TRP A 8 CE2 - CD2 - CG ANGL. DEV. = -6.9 DEGREES
REMARK 500 TRP A 33 CD1 - CG - CD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TRP A 33 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 TRP A 79 CD1 - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP A 79 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP A 89 CD1 - CG - CD2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 TRP A 89 CE2 - CD2 - CG ANGL. DEV. = -6.9 DEGREES
REMARK 500 TRP A 89 CG - CD2 - CE3 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TYR A 158 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 170 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 170 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 TRP A 184 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP A 184 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 195 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 TRP A 267 CD1 - CG - CD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TRP A 267 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 286 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 GLU A 316 CA - CB - CG ANGL. DEV. = 13.7 DEGREES
REMARK 500 TRP A 321 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP A 321 CE2 - CD2 - CG ANGL. DEV. = -5.9 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 50 2.99 -61.22
REMARK 500 ASN A 51 24.17 -142.03
REMARK 500 GLU A 56 -167.49 -117.06
REMARK 500 ARG A 59 31.43 -71.68
REMARK 500 ALA A 124 140.07 -173.01
REMARK 500 GLN A 130 -38.66 -32.72
REMARK 500 THR A 143 -9.53 -142.04
REMARK 500 LYS A 145 107.11 -36.50
REMARK 500 ALA A 151 -26.87 -38.60
REMARK 500 HIS A 165 -45.94 -140.13
REMARK 500 ARG A 170 -47.43 -160.05
REMARK 500 LEU A 188 40.63 -98.76
REMARK 500 PRO A 249 1.24 -54.09
REMARK 500 PRO A 252 84.64 -68.24
REMARK 500 ALA A 257 -35.58 -39.82
REMARK 500 ALA A 289 -1.04 -59.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE A 248 PRO A 249 -149.54
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 A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 401
DBREF 1MBT A 1 342 UNP P08373 MURB_ECOLI 1 342
SEQRES 1 A 342 MET ASN HIS SER LEU LYS PRO TRP ASN THR PHE GLY ILE
SEQRES 2 A 342 ASP HIS ASN ALA GLN HIS ILE VAL CYS ALA GLU ASP GLU
SEQRES 3 A 342 GLN GLN LEU LEU ASN ALA TRP GLN TYR ALA THR ALA GLU
SEQRES 4 A 342 GLY GLN PRO VAL LEU ILE LEU GLY GLU GLY SER ASN VAL
SEQRES 5 A 342 LEU PHE LEU GLU ASP TYR ARG GLY THR VAL ILE ILE ASN
SEQRES 6 A 342 ARG ILE LYS GLY ILE GLU ILE HIS ASP GLU PRO ASP ALA
SEQRES 7 A 342 TRP TYR LEU HIS VAL GLY ALA GLY GLU ASN TRP HIS ARG
SEQRES 8 A 342 LEU VAL LYS TYR THR LEU GLN GLU GLY MET PRO GLY LEU
SEQRES 9 A 342 GLU ASN LEU ALA LEU ILE PRO GLY CYS VAL GLY SER SER
SEQRES 10 A 342 PRO ILE GLN ASN ILE GLY ALA TYR GLY VAL GLU LEU GLN
SEQRES 11 A 342 ARG VAL CYS ALA TYR VAL ASP SER VAL GLU LEU ALA THR
SEQRES 12 A 342 GLY LYS GLN VAL ARG LEU THR ALA LYS GLU CYS ARG PHE
SEQRES 13 A 342 GLY TYR ARG ASP SER ILE PHE LYS HIS GLU TYR GLN ASP
SEQRES 14 A 342 ARG PHE ALA ILE VAL ALA VAL GLY LEU ARG LEU PRO LYS
SEQRES 15 A 342 GLU TRP GLN PRO VAL LEU THR TYR GLY ASP LEU THR ARG
SEQRES 16 A 342 LEU ASP PRO THR THR VAL THR PRO GLN GLN VAL PHE ASN
SEQRES 17 A 342 ALA VAL CYS HIS MET ARG THR THR LYS LEU PRO ASP PRO
SEQRES 18 A 342 LYS VAL ASN GLY ASN ALA GLY SER PHE PHE LYS ASN PRO
SEQRES 19 A 342 VAL VAL SER ALA GLU THR ALA LYS ALA LEU LEU SER GLN
SEQRES 20 A 342 PHE PRO THR ALA PRO ASN TYR PRO GLN ALA ASP GLY SER
SEQRES 21 A 342 VAL LYS LEU ALA ALA GLY TRP LEU ILE ASP GLN CYS GLN
SEQRES 22 A 342 LEU LYS GLY MET GLN ILE GLY GLY ALA ALA VAL HIS ARG
SEQRES 23 A 342 GLN GLN ALA LEU VAL LEU ILE ASN GLU ASP ASN ALA LYS
SEQRES 24 A 342 SER GLU ASP VAL VAL GLN LEU ALA HIS HIS VAL ARG GLN
SEQRES 25 A 342 LYS VAL GLY GLU LYS PHE ASN VAL TRP LEU GLU PRO GLU
SEQRES 26 A 342 VAL ARG PHE ILE GLY ALA SER GLY GLU VAL SER ALA VAL
SEQRES 27 A 342 GLU THR ILE SER
HET SO4 A 600 5
HET FAD A 401 53
HETNAM SO4 SULFATE ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 2 SO4 O4 S 2-
FORMUL 3 FAD C27 H33 N9 O15 P2
FORMUL 4 HOH *4(H2 O)
HELIX 1 1 LEU A 5 PRO A 7 5 3
HELIX 2 2 GLU A 26 GLU A 39 1 14
HELIX 3 3 TRP A 89 GLN A 98 1 10
HELIX 4 4 GLU A 105 LEU A 107 5 3
HELIX 5 5 VAL A 114 GLN A 120 1 7
HELIX 6 6 LEU A 129 VAL A 132 5 4
HELIX 7 7 ILE A 162 HIS A 165 1 4
HELIX 8 8 GLY A 191 ARG A 195 5 5
HELIX 9 9 PRO A 203 LYS A 217 1 15
HELIX 10 10 ALA A 238 LEU A 245 1 8
HELIX 11 11 ALA A 265 GLN A 271 1 7
HELIX 12 12 SER A 300 PHE A 318 1 19
HELIX 13 13 ALA A 337 THR A 340 1 4
SHEET 1 A 3 HIS A 19 ALA A 23 0
SHEET 2 A 3 THR A 61 ASN A 65 1 N VAL A 62 O HIS A 19
SHEET 3 A 3 VAL A 43 LEU A 46 1 N LEU A 44 O THR A 61
SHEET 1 B 2 VAL A 52 PHE A 54 0
SHEET 2 B 2 ARG A 327 ILE A 329 1 N ARG A 327 O LEU A 53
SHEET 1 C 5 ILE A 70 ASP A 74 0
SHEET 2 C 5 ALA A 78 GLY A 84 -1 N HIS A 82 O GLU A 71
SHEET 3 C 5 ALA A 175 PRO A 181 -1 N LEU A 180 O TRP A 79
SHEET 4 C 5 CYS A 133 VAL A 139 -1 N ASP A 137 O ALA A 175
SHEET 5 C 5 GLN A 146 THR A 150 -1 N LEU A 149 O VAL A 136
SHEET 1 D 2 SER A 138 GLU A 140 0
SHEET 2 D 2 PHE A 171 ILE A 173 -1 N ALA A 172 O VAL A 139
SHEET 1 E 2 ALA A 282 VAL A 284 0
SHEET 2 E 2 LEU A 292 ASN A 294 -1 N ILE A 293 O ALA A 283
SITE 1 AC1 3 TYR A 158 ASN A 233 LYS A 262
SITE 1 AC2 25 ILE A 45 LEU A 46 GLY A 47 GLU A 48
SITE 2 AC2 25 GLY A 49 SER A 50 ASN A 51 VAL A 52
SITE 3 AC2 25 ASN A 65 ILE A 110 PRO A 111 GLY A 112
SITE 4 AC2 25 CYS A 113 SER A 116 ILE A 119 GLN A 120
SITE 5 AC2 25 ILE A 122 GLY A 123 ARG A 159 ILE A 173
SITE 6 AC2 25 ARG A 214 ASN A 226 GLY A 228 GLU A 325
SITE 7 AC2 25 ARG A 327
CRYST1 50.400 79.100 90.800 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 0.019841 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012642 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011013 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
