HEADER HYDROLASE 21-NOV-07 3BFC
TITLE CLASS A BETA-LACTAMASE SED-G238C COMPLEXED WITH IMIPENEM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CLASS A BETA-LACTAMASE SED1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: SED-G238C, UNP RESIDUES 34-295;
COMPND 5 EC: 3.5.2.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CITROBACTER SEDLAKII;
SOURCE 3 ORGANISM_TAXID: 67826;
SOURCE 4 STRAIN: 2596;
SOURCE 5 GENE: BLA-SED-1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET29A
KEYWDS HYDROLASE, BETA-LACTAMASE, CLASS A, SED-G238C, IMIPENEM, ACYL-ENZYME
EXPDTA X-RAY DIFFRACTION
AUTHOR L.PERNOT,S.PETRELLA,W.SOUGAKOFF
REVDAT 4 01-NOV-23 3BFC 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK
REVDAT 3 24-AUG-11 3BFC 1 HETNAM HETSYN VERSN
REVDAT 2 24-FEB-09 3BFC 1 VERSN
REVDAT 1 18-DEC-07 3BFC 0
JRNL AUTH L.PERNOT,S.PETRELLA,W.SOUGAKOFF
JRNL TITL ACYL-INTERMEDIATE STRUCTURES OF THE CLASS A BETA-LACTAMASE
JRNL TITL 2 SED-G238C
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.PETRELLA,L.PERNOT,W.SOUGAKOFF
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDY OF
REMARK 1 TITL 2 THE CLASS A BETA-LACTAMASE SED-1 AND ITS MUTANT SED-G238C
REMARK 1 TITL 3 FROM CITROBACTER SEDLAKII
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 60 125 2004
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 14684905
REMARK 1 DOI 10.1107/S0907444903022765
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 57592
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) : 0.206
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3061
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9238
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE : 0.2820
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 473
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7948
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 80
REMARK 3 SOLVENT ATOMS : 620
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.21000
REMARK 3 B22 (A**2) : -3.28000
REMARK 3 B33 (A**2) : 7.49000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.44000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.26
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) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.30
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.820
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 3BFC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000045449.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-NOV-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.984
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60669
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.29100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.870
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 3BFD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% PEG MME 2000, 200MM KSCN, 100MM
REMARK 280 SODIUM CACODYLATE PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 94.21800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.69950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 94.21800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.69950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 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 CYS A 69 CA - CB - SG ANGL. DEV. = 12.2 DEGREES
REMARK 500 CYS A 238 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 CYS B 69 CA - CB - SG ANGL. DEV. = 10.0 DEGREES
REMARK 500 CYS B 238 CA - CB - SG ANGL. DEV. = 8.9 DEGREES
REMARK 500 CYS C 69 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 CYS C 238 CA - CB - SG ANGL. DEV. = 9.4 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 CYS A 69 -126.12 34.37
REMARK 500 THR A 103 -144.77 -115.42
REMARK 500 SER A 220 -129.02 -105.35
REMARK 500 ASP A 246 130.82 -176.32
REMARK 500 GLU A 254 -130.17 52.11
REMARK 500 ARG A 275 65.88 -118.45
REMARK 500 CYS B 69 -137.80 55.60
REMARK 500 THR B 103 -144.27 -129.55
REMARK 500 TRP B 105 103.39 -167.60
REMARK 500 SER B 220 -129.67 -102.04
REMARK 500 ASP B 246 134.14 -171.12
REMARK 500 GLU B 254 -124.16 51.52
REMARK 500 CYS C 69 -137.35 52.99
REMARK 500 THR C 103 -151.05 -122.79
REMARK 500 ASN C 115 -157.48 -132.82
REMARK 500 ASP C 131 107.70 -59.28
REMARK 500 SER C 220 -127.89 -104.24
REMARK 500 ASP C 240 162.99 -48.95
REMARK 500 GLU C 254 -126.83 48.59
REMARK 500 CYS D 69 -136.84 52.57
REMARK 500 HIS D 87 78.96 -102.70
REMARK 500 THR D 103 -144.06 -111.45
REMARK 500 SER D 220 -123.49 -108.52
REMARK 500 GLU D 254 -124.48 54.34
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 IM2 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IM2 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IM2 C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IM2 D 304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BFD RELATED DB: PDB
REMARK 900 CLASS A BETA-LACTAMASE SED-G238C
REMARK 900 RELATED ID: 3BFE RELATED DB: PDB
REMARK 900 CLASS A BETA-LACTAMASE SED-1
REMARK 900 RELATED ID: 3BFF RELATED DB: PDB
REMARK 900 CLASS A BETA-LACTAMASE SED-G238C COMPLEXED WITH FAROPENEM
REMARK 900 RELATED ID: 3BFG RELATED DB: PDB
REMARK 900 CLASS A BETA-LACTAMASE SED-G238C COMPLEXED WITH MEROPENEM
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS COORDINATES IS USED NON-SEQUENTIAL RESIDUE NUMBERING.
REMARK 999 THREE NUMBERS, 58, 239, AND 253 WERE SIMPLY SKIPPED IN THE
REMARK 999 NUMBERING AND HAVE NOTHING TO DO WITH LACK OF ELECTRON
REMARK 999 DENSITY.
DBREF 3BFC A 26 290 UNP Q93PQ0 Q93PQ0_9ENTR 34 295
DBREF 3BFC B 26 290 UNP Q93PQ0 Q93PQ0_9ENTR 34 295
DBREF 3BFC C 26 290 UNP Q93PQ0 Q93PQ0_9ENTR 34 295
DBREF 3BFC D 26 290 UNP Q93PQ0 Q93PQ0_9ENTR 34 295
SEQADV 3BFC CYS A 238 UNP Q93PQ0 GLY 245 ENGINEERED MUTATION
SEQADV 3BFC CYS B 238 UNP Q93PQ0 GLY 245 ENGINEERED MUTATION
SEQADV 3BFC CYS C 238 UNP Q93PQ0 GLY 245 ENGINEERED MUTATION
SEQADV 3BFC CYS D 238 UNP Q93PQ0 GLY 245 ENGINEERED MUTATION
SEQRES 1 A 262 VAL GLN GLN VAL GLN LYS LYS LEU ALA ALA LEU GLU LYS
SEQRES 2 A 262 GLN SER GLY GLY ARG LEU GLY VAL ALA LEU ILE ASN THR
SEQRES 3 A 262 ALA ASP ASN SER GLN VAL LEU TYR ARG ALA ASP GLU ARG
SEQRES 4 A 262 PHE ALA MET CYS SER THR SER LYS VAL MET THR ALA ALA
SEQRES 5 A 262 ALA VAL LEU LYS GLN SER GLU THR HIS ASP GLY ILE LEU
SEQRES 6 A 262 GLN GLN LYS MET THR ILE LYS LYS ALA ASP LEU THR ASN
SEQRES 7 A 262 TRP ASN PRO VAL THR GLU LYS TYR VAL GLY ASN THR MET
SEQRES 8 A 262 THR LEU ALA GLU LEU SER ALA ALA THR LEU GLN TYR SER
SEQRES 9 A 262 ASP ASN THR ALA MET ASN LYS LEU LEU ALA HIS LEU GLY
SEQRES 10 A 262 GLY PRO GLY ASN VAL THR ALA PHE ALA ARG SER ILE GLY
SEQRES 11 A 262 ASP THR THR PHE ARG LEU ASP ARG LYS GLU PRO GLU LEU
SEQRES 12 A 262 ASN THR ALA ILE PRO GLY ASP GLU ARG ASP THR THR SER
SEQRES 13 A 262 PRO LEU ALA MET ALA LYS SER LEU ARG LYS LEU THR LEU
SEQRES 14 A 262 GLY ASP ALA LEU ALA GLY PRO GLN ARG ALA GLN LEU VAL
SEQRES 15 A 262 ASP TRP LEU LYS GLY ASN THR THR GLY GLY GLN SER ILE
SEQRES 16 A 262 ARG ALA GLY LEU PRO ALA HIS TRP VAL VAL GLY ASP LYS
SEQRES 17 A 262 THR GLY ALA CYS ASP TYR GLY THR THR ASN ASP ILE ALA
SEQRES 18 A 262 VAL ILE TRP PRO GLU ASP ARG ALA PRO LEU VAL LEU VAL
SEQRES 19 A 262 THR TYR PHE THR GLN PRO GLN GLN ASP ALA LYS TRP ARG
SEQRES 20 A 262 LYS ASP VAL LEU ALA ALA ALA ALA LYS ILE VAL THR GLU
SEQRES 21 A 262 GLY LYS
SEQRES 1 B 262 VAL GLN GLN VAL GLN LYS LYS LEU ALA ALA LEU GLU LYS
SEQRES 2 B 262 GLN SER GLY GLY ARG LEU GLY VAL ALA LEU ILE ASN THR
SEQRES 3 B 262 ALA ASP ASN SER GLN VAL LEU TYR ARG ALA ASP GLU ARG
SEQRES 4 B 262 PHE ALA MET CYS SER THR SER LYS VAL MET THR ALA ALA
SEQRES 5 B 262 ALA VAL LEU LYS GLN SER GLU THR HIS ASP GLY ILE LEU
SEQRES 6 B 262 GLN GLN LYS MET THR ILE LYS LYS ALA ASP LEU THR ASN
SEQRES 7 B 262 TRP ASN PRO VAL THR GLU LYS TYR VAL GLY ASN THR MET
SEQRES 8 B 262 THR LEU ALA GLU LEU SER ALA ALA THR LEU GLN TYR SER
SEQRES 9 B 262 ASP ASN THR ALA MET ASN LYS LEU LEU ALA HIS LEU GLY
SEQRES 10 B 262 GLY PRO GLY ASN VAL THR ALA PHE ALA ARG SER ILE GLY
SEQRES 11 B 262 ASP THR THR PHE ARG LEU ASP ARG LYS GLU PRO GLU LEU
SEQRES 12 B 262 ASN THR ALA ILE PRO GLY ASP GLU ARG ASP THR THR SER
SEQRES 13 B 262 PRO LEU ALA MET ALA LYS SER LEU ARG LYS LEU THR LEU
SEQRES 14 B 262 GLY ASP ALA LEU ALA GLY PRO GLN ARG ALA GLN LEU VAL
SEQRES 15 B 262 ASP TRP LEU LYS GLY ASN THR THR GLY GLY GLN SER ILE
SEQRES 16 B 262 ARG ALA GLY LEU PRO ALA HIS TRP VAL VAL GLY ASP LYS
SEQRES 17 B 262 THR GLY ALA CYS ASP TYR GLY THR THR ASN ASP ILE ALA
SEQRES 18 B 262 VAL ILE TRP PRO GLU ASP ARG ALA PRO LEU VAL LEU VAL
SEQRES 19 B 262 THR TYR PHE THR GLN PRO GLN GLN ASP ALA LYS TRP ARG
SEQRES 20 B 262 LYS ASP VAL LEU ALA ALA ALA ALA LYS ILE VAL THR GLU
SEQRES 21 B 262 GLY LYS
SEQRES 1 C 262 VAL GLN GLN VAL GLN LYS LYS LEU ALA ALA LEU GLU LYS
SEQRES 2 C 262 GLN SER GLY GLY ARG LEU GLY VAL ALA LEU ILE ASN THR
SEQRES 3 C 262 ALA ASP ASN SER GLN VAL LEU TYR ARG ALA ASP GLU ARG
SEQRES 4 C 262 PHE ALA MET CYS SER THR SER LYS VAL MET THR ALA ALA
SEQRES 5 C 262 ALA VAL LEU LYS GLN SER GLU THR HIS ASP GLY ILE LEU
SEQRES 6 C 262 GLN GLN LYS MET THR ILE LYS LYS ALA ASP LEU THR ASN
SEQRES 7 C 262 TRP ASN PRO VAL THR GLU LYS TYR VAL GLY ASN THR MET
SEQRES 8 C 262 THR LEU ALA GLU LEU SER ALA ALA THR LEU GLN TYR SER
SEQRES 9 C 262 ASP ASN THR ALA MET ASN LYS LEU LEU ALA HIS LEU GLY
SEQRES 10 C 262 GLY PRO GLY ASN VAL THR ALA PHE ALA ARG SER ILE GLY
SEQRES 11 C 262 ASP THR THR PHE ARG LEU ASP ARG LYS GLU PRO GLU LEU
SEQRES 12 C 262 ASN THR ALA ILE PRO GLY ASP GLU ARG ASP THR THR SER
SEQRES 13 C 262 PRO LEU ALA MET ALA LYS SER LEU ARG LYS LEU THR LEU
SEQRES 14 C 262 GLY ASP ALA LEU ALA GLY PRO GLN ARG ALA GLN LEU VAL
SEQRES 15 C 262 ASP TRP LEU LYS GLY ASN THR THR GLY GLY GLN SER ILE
SEQRES 16 C 262 ARG ALA GLY LEU PRO ALA HIS TRP VAL VAL GLY ASP LYS
SEQRES 17 C 262 THR GLY ALA CYS ASP TYR GLY THR THR ASN ASP ILE ALA
SEQRES 18 C 262 VAL ILE TRP PRO GLU ASP ARG ALA PRO LEU VAL LEU VAL
SEQRES 19 C 262 THR TYR PHE THR GLN PRO GLN GLN ASP ALA LYS TRP ARG
SEQRES 20 C 262 LYS ASP VAL LEU ALA ALA ALA ALA LYS ILE VAL THR GLU
SEQRES 21 C 262 GLY LYS
SEQRES 1 D 262 VAL GLN GLN VAL GLN LYS LYS LEU ALA ALA LEU GLU LYS
SEQRES 2 D 262 GLN SER GLY GLY ARG LEU GLY VAL ALA LEU ILE ASN THR
SEQRES 3 D 262 ALA ASP ASN SER GLN VAL LEU TYR ARG ALA ASP GLU ARG
SEQRES 4 D 262 PHE ALA MET CYS SER THR SER LYS VAL MET THR ALA ALA
SEQRES 5 D 262 ALA VAL LEU LYS GLN SER GLU THR HIS ASP GLY ILE LEU
SEQRES 6 D 262 GLN GLN LYS MET THR ILE LYS LYS ALA ASP LEU THR ASN
SEQRES 7 D 262 TRP ASN PRO VAL THR GLU LYS TYR VAL GLY ASN THR MET
SEQRES 8 D 262 THR LEU ALA GLU LEU SER ALA ALA THR LEU GLN TYR SER
SEQRES 9 D 262 ASP ASN THR ALA MET ASN LYS LEU LEU ALA HIS LEU GLY
SEQRES 10 D 262 GLY PRO GLY ASN VAL THR ALA PHE ALA ARG SER ILE GLY
SEQRES 11 D 262 ASP THR THR PHE ARG LEU ASP ARG LYS GLU PRO GLU LEU
SEQRES 12 D 262 ASN THR ALA ILE PRO GLY ASP GLU ARG ASP THR THR SER
SEQRES 13 D 262 PRO LEU ALA MET ALA LYS SER LEU ARG LYS LEU THR LEU
SEQRES 14 D 262 GLY ASP ALA LEU ALA GLY PRO GLN ARG ALA GLN LEU VAL
SEQRES 15 D 262 ASP TRP LEU LYS GLY ASN THR THR GLY GLY GLN SER ILE
SEQRES 16 D 262 ARG ALA GLY LEU PRO ALA HIS TRP VAL VAL GLY ASP LYS
SEQRES 17 D 262 THR GLY ALA CYS ASP TYR GLY THR THR ASN ASP ILE ALA
SEQRES 18 D 262 VAL ILE TRP PRO GLU ASP ARG ALA PRO LEU VAL LEU VAL
SEQRES 19 D 262 THR TYR PHE THR GLN PRO GLN GLN ASP ALA LYS TRP ARG
SEQRES 20 D 262 LYS ASP VAL LEU ALA ALA ALA ALA LYS ILE VAL THR GLU
SEQRES 21 D 262 GLY LYS
HET IM2 A 301 20
HET IM2 B 302 20
HET IM2 C 303 20
HET IM2 D 304 20
HETNAM IM2 (5R)-5-[(1S,2R)-1-FORMYL-2-HYDROXYPROPYL]-3-[(2-{[(E)-
HETNAM 2 IM2 IMINOMETHYL]AMINO}ETHYL)SULFANYL]-4,5-DIHYDRO-1H-
HETNAM 3 IM2 PYRROLE-2-CARBOX YLIC ACID
HETSYN IM2 IMIPENEM, OPEN FORM; N-FORMIMIDOYL-THIENAMYCINE, OPEN
HETSYN 2 IM2 FORM
FORMUL 5 IM2 4(C12 H19 N3 O4 S)
FORMUL 9 HOH *620(H2 O)
HELIX 1 1 VAL A 26 GLY A 41 1 16
HELIX 2 2 CYS A 69 THR A 71 5 3
HELIX 3 3 SER A 72 SER A 84 1 13
HELIX 4 4 GLY A 89 GLN A 92 5 4
HELIX 5 5 VAL A 108 VAL A 113 5 6
HELIX 6 6 LEU A 119 TYR A 129 1 11
HELIX 7 7 ASP A 131 GLY A 143 1 13
HELIX 8 8 GLY A 144 ILE A 155 1 12
HELIX 9 9 PRO A 167 THR A 171 5 5
HELIX 10 10 SER A 182 LEU A 195 1 14
HELIX 11 11 ALA A 200 GLY A 213 1 14
HELIX 12 12 SER A 220 LEU A 225 5 6
HELIX 13 13 ARG A 275 GLU A 288 1 14
HELIX 14 14 VAL B 26 GLY B 41 1 16
HELIX 15 15 CYS B 69 THR B 71 5 3
HELIX 16 16 SER B 72 GLU B 85 1 14
HELIX 17 17 GLY B 89 GLN B 92 5 4
HELIX 18 18 LYS B 98 LEU B 102 5 5
HELIX 19 19 VAL B 108 TYR B 112 5 5
HELIX 20 20 LEU B 119 TYR B 129 1 11
HELIX 21 21 ASP B 131 GLY B 143 1 13
HELIX 22 22 GLY B 144 ILE B 155 1 12
HELIX 23 23 PRO B 167 THR B 171 5 5
HELIX 24 24 SER B 182 LEU B 195 1 14
HELIX 25 25 ALA B 200 GLY B 213 1 14
HELIX 26 26 SER B 220 LEU B 225 5 6
HELIX 27 27 ARG B 275 GLU B 288 1 14
HELIX 28 28 VAL C 26 GLY C 41 1 16
HELIX 29 29 CYS C 69 THR C 71 5 3
HELIX 30 30 SER C 72 GLU C 85 1 14
HELIX 31 31 GLY C 89 GLN C 92 5 4
HELIX 32 32 VAL C 108 TYR C 112 5 5
HELIX 33 33 LEU C 119 TYR C 129 1 11
HELIX 34 34 ASP C 131 GLY C 143 1 13
HELIX 35 35 PRO C 145 ILE C 155 1 11
HELIX 36 36 PRO C 167 THR C 171 5 5
HELIX 37 37 SER C 182 LEU C 195 1 14
HELIX 38 38 ALA C 200 GLY C 213 1 14
HELIX 39 39 SER C 220 LEU C 225 5 6
HELIX 40 40 ARG C 275 THR C 287 1 13
HELIX 41 41 VAL D 26 GLY D 41 1 16
HELIX 42 42 CYS D 69 THR D 71 5 3
HELIX 43 43 SER D 72 SER D 84 1 13
HELIX 44 44 GLY D 89 GLN D 92 5 4
HELIX 45 45 LYS D 98 LEU D 102 5 5
HELIX 46 46 VAL D 108 VAL D 113 5 6
HELIX 47 47 LEU D 119 TYR D 129 1 11
HELIX 48 48 ASP D 131 GLY D 143 1 13
HELIX 49 49 GLY D 144 ILE D 155 1 12
HELIX 50 50 PRO D 167 THR D 171 5 5
HELIX 51 51 SER D 182 LEU D 195 1 14
HELIX 52 52 ALA D 200 GLY D 213 1 14
HELIX 53 53 SER D 220 LEU D 225 5 6
HELIX 54 54 ARG D 275 GLU D 288 1 14
SHEET 1 A 5 GLN A 56 TYR A 60 0
SHEET 2 A 5 ARG A 43 ASN A 50 -1 N VAL A 46 O TYR A 60
SHEET 3 A 5 LEU A 259 THR A 266 -1 O TYR A 264 N GLY A 45
SHEET 4 A 5 THR A 243 TRP A 251 -1 N ILE A 250 O LEU A 259
SHEET 5 A 5 VAL A 230 CYS A 238 -1 N VAL A 230 O TRP A 251
SHEET 1 B 2 PHE A 66 ALA A 67 0
SHEET 2 B 2 THR A 180 THR A 181 -1 O THR A 181 N PHE A 66
SHEET 1 C 2 LYS A 94 ILE A 97 0
SHEET 2 C 2 ASN A 115 THR A 118 -1 O ASN A 115 N ILE A 97
SHEET 1 D 5 GLN B 56 TYR B 60 0
SHEET 2 D 5 ARG B 43 ASN B 50 -1 N VAL B 46 O TYR B 60
SHEET 3 D 5 LEU B 259 THR B 266 -1 O TYR B 264 N GLY B 45
SHEET 4 D 5 THR B 243 TRP B 251 -1 N ILE B 250 O LEU B 259
SHEET 5 D 5 VAL B 230 CYS B 238 -1 N GLY B 236 O ASN B 245
SHEET 1 E 2 PHE B 66 ALA B 67 0
SHEET 2 E 2 THR B 180 THR B 181 -1 O THR B 181 N PHE B 66
SHEET 1 F 2 LYS B 94 ILE B 97 0
SHEET 2 F 2 ASN B 115 THR B 118 -1 O ASN B 115 N ILE B 97
SHEET 1 G 5 GLN C 56 TYR C 60 0
SHEET 2 G 5 ARG C 43 ASN C 50 -1 N VAL C 46 O TYR C 60
SHEET 3 G 5 LEU C 259 THR C 266 -1 O TYR C 264 N GLY C 45
SHEET 4 G 5 THR C 243 TRP C 251 -1 N ILE C 250 O LEU C 259
SHEET 5 G 5 VAL C 230 CYS C 238 -1 N GLY C 236 O ASN C 245
SHEET 1 H 2 PHE C 66 ALA C 67 0
SHEET 2 H 2 THR C 180 THR C 181 -1 O THR C 181 N PHE C 66
SHEET 1 I 2 LYS C 94 ILE C 97 0
SHEET 2 I 2 ASN C 115 THR C 118 -1 O ASN C 115 N ILE C 97
SHEET 1 J 5 GLN D 56 TYR D 60 0
SHEET 2 J 5 ARG D 43 ASN D 50 -1 N VAL D 46 O TYR D 60
SHEET 3 J 5 LEU D 259 THR D 266 -1 O TYR D 264 N GLY D 45
SHEET 4 J 5 THR D 243 TRP D 251 -1 N ILE D 250 O LEU D 259
SHEET 5 J 5 VAL D 230 CYS D 238 -1 N VAL D 230 O TRP D 251
SHEET 1 K 2 PHE D 66 ALA D 67 0
SHEET 2 K 2 THR D 180 THR D 181 -1 O THR D 181 N PHE D 66
SHEET 1 L 2 LYS D 94 ILE D 97 0
SHEET 2 L 2 ASN D 115 THR D 118 -1 O ASN D 115 N ILE D 97
SSBOND 1 CYS A 69 CYS A 238 1555 1555 2.03
SSBOND 2 CYS B 69 CYS B 238 1555 1555 2.03
SSBOND 3 CYS C 69 CYS C 238 1555 1555 2.03
SSBOND 4 CYS D 69 CYS D 238 1555 1555 2.02
LINK OG SER A 70 C7 IM2 A 301 1555 1555 1.38
LINK OG SER B 70 C7 IM2 B 302 1555 1555 1.38
LINK OG SER C 70 C7 IM2 C 303 1555 1555 1.37
LINK OG SER D 70 C7 IM2 D 304 1555 1555 1.37
CISPEP 1 GLU A 166 PRO A 167 0 0.21
CISPEP 2 GLU B 166 PRO B 167 0 1.02
CISPEP 3 GLU C 166 PRO C 167 0 0.23
CISPEP 4 GLU D 166 PRO D 167 0 0.06
SITE 1 AC1 15 CYS A 69 SER A 70 LYS A 73 SER A 130
SITE 2 AC1 15 ASN A 132 GLU A 166 ASN A 170 THR A 216
SITE 3 AC1 15 LYS A 234 THR A 235 GLY A 236 ALA A 237
SITE 4 AC1 15 LYS A 276 HOH A 414 HOH A 415
SITE 1 AC2 14 CYS B 69 SER B 70 LYS B 73 SER B 130
SITE 2 AC2 14 ASN B 132 GLU B 166 ASN B 170 THR B 216
SITE 3 AC2 14 THR B 235 GLY B 236 ALA B 237 TRP B 274
SITE 4 AC2 14 HOH B 510 HOH B 524
SITE 1 AC3 14 ASN A 115 CYS C 69 SER C 70 LYS C 73
SITE 2 AC3 14 SER C 130 ASN C 132 GLU C 166 ASN C 170
SITE 3 AC3 14 THR C 216 THR C 235 GLY C 236 ALA C 237
SITE 4 AC3 14 TRP C 274 HOH C 441
SITE 1 AC4 13 CYS D 69 SER D 70 LYS D 73 TRP D 105
SITE 2 AC4 13 SER D 130 ASN D 132 GLU D 166 ASN D 170
SITE 3 AC4 13 THR D 216 THR D 235 GLY D 236 ALA D 237
SITE 4 AC4 13 HOH D 554
CRYST1 188.436 73.399 105.050 90.00 122.36 90.00 C 1 2 1 16
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 0.005307 0.000000 0.003362 0.00000
SCALE2 0.000000 0.013624 -0.000001 0.00000
SCALE3 0.000000 0.000000 0.011269 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
