HEADER HYDROLASE 30-AUG-06 2I72
TITLE AMPC BETA-LACTAMASE IN COMPLEX WITH 5-DIFORMYLAMINOMETHYL-
TITLE 2 BENZO[B]THIOPHEN-2-BORONIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTAMASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 20-377;
COMPND 5 SYNONYM: CEPHALOSPORINASE;
COMPND 6 EC: 3.5.2.6;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: AMPC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI K12;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: K12;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: POGO295
KEYWDS AMPC, BETA-LACTAMASE, CEPHALOSPORINASE, SERINE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.VENTURELLI,L.CANCIAN,D.TONDI,F.MORANDI,G.CANNAZZA,B.SEGATORE,
AUTHOR 2 F.PRATI,G.AMICOSANTE,B.K.SHOICHET,M.P.COSTI
REVDAT 5 30-AUG-23 2I72 1 REMARK LINK
REVDAT 4 18-OCT-17 2I72 1 REMARK
REVDAT 3 24-FEB-09 2I72 1 VERSN
REVDAT 2 27-NOV-07 2I72 1 JRNL
REVDAT 1 11-SEP-07 2I72 0
JRNL AUTH A.VENTURELLI,D.TONDI,L.CANCIAN,F.MORANDI,G.CANNAZZA,
JRNL AUTH 2 B.SEGATORE,F.PRATI,G.AMICOSANTE,B.K.SHOICHET,M.P.COSTI
JRNL TITL OPTIMIZING CELL PERMEATION OF AN ANTIBIOTIC RESISTANCE
JRNL TITL 2 INHIBITOR FOR IMPROVED EFFICACY
JRNL REF J.MED.CHEM. V. 50 5644 2007
JRNL REFN ISSN 0022-2623
JRNL PMID 17956081
JRNL DOI 10.1021/JM070643Q
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 39056
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3524
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2545
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1830
REMARK 3 BIN FREE R VALUE SET COUNT : 269
REMARK 3 BIN FREE R VALUE : 0.2460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5476
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 384
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.77000
REMARK 3 B22 (A**2) : -0.39000
REMARK 3 B33 (A**2) : 0.65000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.15000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.255
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.190
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.116
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.492
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5673 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7765 ; 1.566 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 702 ; 6.399 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 241 ;36.931 ;24.689
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 856 ;15.357 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;18.300 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 840 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4390 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2623 ; 0.206 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3885 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 378 ; 0.159 ; 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): 48 ; 0.222 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.094 ; 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): 3615 ; 1.259 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5667 ; 1.493 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2483 ; 2.802 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2098 ; 4.059 ; 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2I72 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-SEP-06.
REMARK 100 THE DEPOSITION ID IS D_1000039218.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.115869
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39060
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 45.314
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : 0.08700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000
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 (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.34500
REMARK 200 R SYM FOR SHELL (I) : 0.34500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1CB3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM PHOSPHATE BUFFER, PH 8.7,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
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 58.81600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.61800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 58.81600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 38.61800
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 ILE B 283
REMARK 465 ILE B 284
REMARK 465 ASN B 285
REMARK 465 GLY B 286
REMARK 465 SER B 287
REMARK 465 ASP B 288
REMARK 465 ASN B 289
REMARK 465 LYS B 290
REMARK 465 ILE B 291
REMARK 465 ALA B 292
REMARK 465 LEU B 293
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 LYS A 50 CG CD CE NZ
REMARK 470 LYS A 126 CG CD CE NZ
REMARK 470 GLU A 205 CG CD OE1 OE2
REMARK 470 LYS A 207 CG CD CE NZ
REMARK 470 LYS A 246 CG CD CE NZ
REMARK 470 LYS A 290 CG CD CE NZ
REMARK 470 LYS B 50 CG CD CE NZ
REMARK 470 LYS B 126 CG CD CE NZ
REMARK 470 GLU B 205 CG CD OE1 OE2
REMARK 470 LYS B 207 CG CD CE NZ
REMARK 470 LYS B 246 CG CD CE NZ
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 OD1 ASP A 87 OH TYR A 92 2.18
REMARK 500 OG SER B 64 O21 VA1 B 964 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 GLU B 21 CD GLU B 21 OE1 -0.092
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 GLU B 21 OE1 - CD - OE2 ANGL. DEV. = 7.6 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 VAL A 178 -60.20 -122.14
REMARK 500 TYR A 221 22.71 -158.29
REMARK 500 ALA A 307 111.49 -33.75
REMARK 500 ASN A 341 42.13 -95.20
REMARK 500 ASN B 102 -75.62 -37.31
REMARK 500 VAL B 178 -57.49 -121.60
REMARK 500 LEU B 184 77.42 -102.52
REMARK 500 TYR B 221 27.35 -156.75
REMARK 500 PRO B 280 9.70 -56.05
REMARK 500 ALA B 307 121.19 -37.99
REMARK 500 ASN B 341 44.43 -94.96
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 VA1 A 964
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VA1 B 964
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CB3 RELATED DB: PDB
REMARK 900 AMPC BETA-LACTAMASE FROM E. COLI COMPLEXED WITH INHIBITOR, BENZO(B)
REMARK 900 THIOPHENE-2-BORONIC ACID (BZB)
REMARK 900 RELATED ID: 1KE4 RELATED DB: PDB
REMARK 900 AMPC BETA-LACTAMASE FROM E. COLI
DBREF 2I72 A 4 361 UNP P00811 AMPC_ECOLI 20 377
DBREF 2I72 B 4 361 UNP P00811 AMPC_ECOLI 20 377
SEQRES 1 A 358 ALA PRO GLN GLN ILE ASN ASP ILE VAL HIS ARG THR ILE
SEQRES 2 A 358 THR PRO LEU ILE GLU GLN GLN LYS ILE PRO GLY MET ALA
SEQRES 3 A 358 VAL ALA VAL ILE TYR GLN GLY LYS PRO TYR TYR PHE THR
SEQRES 4 A 358 TRP GLY TYR ALA ASP ILE ALA LYS LYS GLN PRO VAL THR
SEQRES 5 A 358 GLN GLN THR LEU PHE GLU LEU GLY SER VAL SER LYS THR
SEQRES 6 A 358 PHE THR GLY VAL LEU GLY GLY ASP ALA ILE ALA ARG GLY
SEQRES 7 A 358 GLU ILE LYS LEU SER ASP PRO THR THR LYS TYR TRP PRO
SEQRES 8 A 358 GLU LEU THR ALA LYS GLN TRP ASN GLY ILE THR LEU LEU
SEQRES 9 A 358 HIS LEU ALA THR TYR THR ALA GLY GLY LEU PRO LEU GLN
SEQRES 10 A 358 VAL PRO ASP GLU VAL LYS SER SER SER ASP LEU LEU ARG
SEQRES 11 A 358 PHE TYR GLN ASN TRP GLN PRO ALA TRP ALA PRO GLY THR
SEQRES 12 A 358 GLN ARG LEU TYR ALA ASN SER SER ILE GLY LEU PHE GLY
SEQRES 13 A 358 ALA LEU ALA VAL LYS PRO SER GLY LEU SER PHE GLU GLN
SEQRES 14 A 358 ALA MET GLN THR ARG VAL PHE GLN PRO LEU LYS LEU ASN
SEQRES 15 A 358 HIS THR TRP ILE ASN VAL PRO PRO ALA GLU GLU LYS ASN
SEQRES 16 A 358 TYR ALA TRP GLY TYR ARG GLU GLY LYS ALA VAL HIS VAL
SEQRES 17 A 358 SER PRO GLY ALA LEU ASP ALA GLU ALA TYR GLY VAL LYS
SEQRES 18 A 358 SER THR ILE GLU ASP MET ALA ARG TRP VAL GLN SER ASN
SEQRES 19 A 358 LEU LYS PRO LEU ASP ILE ASN GLU LYS THR LEU GLN GLN
SEQRES 20 A 358 GLY ILE GLN LEU ALA GLN SER ARG TYR TRP GLN THR GLY
SEQRES 21 A 358 ASP MET TYR GLN GLY LEU GLY TRP GLU MET LEU ASP TRP
SEQRES 22 A 358 PRO VAL ASN PRO ASP SER ILE ILE ASN GLY SER ASP ASN
SEQRES 23 A 358 LYS ILE ALA LEU ALA ALA ARG PRO VAL LYS ALA ILE THR
SEQRES 24 A 358 PRO PRO THR PRO ALA VAL ARG ALA SER TRP VAL HIS LYS
SEQRES 25 A 358 THR GLY ALA THR GLY GLY PHE GLY SER TYR VAL ALA PHE
SEQRES 26 A 358 ILE PRO GLU LYS GLU LEU GLY ILE VAL MET LEU ALA ASN
SEQRES 27 A 358 LYS ASN TYR PRO ASN PRO ALA ARG VAL ASP ALA ALA TRP
SEQRES 28 A 358 GLN ILE LEU ASN ALA LEU GLN
SEQRES 1 B 358 ALA PRO GLN GLN ILE ASN ASP ILE VAL HIS ARG THR ILE
SEQRES 2 B 358 THR PRO LEU ILE GLU GLN GLN LYS ILE PRO GLY MET ALA
SEQRES 3 B 358 VAL ALA VAL ILE TYR GLN GLY LYS PRO TYR TYR PHE THR
SEQRES 4 B 358 TRP GLY TYR ALA ASP ILE ALA LYS LYS GLN PRO VAL THR
SEQRES 5 B 358 GLN GLN THR LEU PHE GLU LEU GLY SER VAL SER LYS THR
SEQRES 6 B 358 PHE THR GLY VAL LEU GLY GLY ASP ALA ILE ALA ARG GLY
SEQRES 7 B 358 GLU ILE LYS LEU SER ASP PRO THR THR LYS TYR TRP PRO
SEQRES 8 B 358 GLU LEU THR ALA LYS GLN TRP ASN GLY ILE THR LEU LEU
SEQRES 9 B 358 HIS LEU ALA THR TYR THR ALA GLY GLY LEU PRO LEU GLN
SEQRES 10 B 358 VAL PRO ASP GLU VAL LYS SER SER SER ASP LEU LEU ARG
SEQRES 11 B 358 PHE TYR GLN ASN TRP GLN PRO ALA TRP ALA PRO GLY THR
SEQRES 12 B 358 GLN ARG LEU TYR ALA ASN SER SER ILE GLY LEU PHE GLY
SEQRES 13 B 358 ALA LEU ALA VAL LYS PRO SER GLY LEU SER PHE GLU GLN
SEQRES 14 B 358 ALA MET GLN THR ARG VAL PHE GLN PRO LEU LYS LEU ASN
SEQRES 15 B 358 HIS THR TRP ILE ASN VAL PRO PRO ALA GLU GLU LYS ASN
SEQRES 16 B 358 TYR ALA TRP GLY TYR ARG GLU GLY LYS ALA VAL HIS VAL
SEQRES 17 B 358 SER PRO GLY ALA LEU ASP ALA GLU ALA TYR GLY VAL LYS
SEQRES 18 B 358 SER THR ILE GLU ASP MET ALA ARG TRP VAL GLN SER ASN
SEQRES 19 B 358 LEU LYS PRO LEU ASP ILE ASN GLU LYS THR LEU GLN GLN
SEQRES 20 B 358 GLY ILE GLN LEU ALA GLN SER ARG TYR TRP GLN THR GLY
SEQRES 21 B 358 ASP MET TYR GLN GLY LEU GLY TRP GLU MET LEU ASP TRP
SEQRES 22 B 358 PRO VAL ASN PRO ASP SER ILE ILE ASN GLY SER ASP ASN
SEQRES 23 B 358 LYS ILE ALA LEU ALA ALA ARG PRO VAL LYS ALA ILE THR
SEQRES 24 B 358 PRO PRO THR PRO ALA VAL ARG ALA SER TRP VAL HIS LYS
SEQRES 25 B 358 THR GLY ALA THR GLY GLY PHE GLY SER TYR VAL ALA PHE
SEQRES 26 B 358 ILE PRO GLU LYS GLU LEU GLY ILE VAL MET LEU ALA ASN
SEQRES 27 B 358 LYS ASN TYR PRO ASN PRO ALA ARG VAL ASP ALA ALA TRP
SEQRES 28 B 358 GLN ILE LEU ASN ALA LEU GLN
HET VA1 A 964 18
HET VA1 B 964 18
HETNAM VA1 {5-[(DIFORMYLAMINO)METHYL]-1-BENZOTHIEN-2-YL}BORONIC
HETNAM 2 VA1 ACID
HETSYN VA1 5-DIFORMYLAMINOMETHYL-BENZO[B]THIOPHEN-2-BORONIC ACID
FORMUL 3 VA1 2(C11 H10 B N O4 S)
FORMUL 5 HOH *384(H2 O)
HELIX 1 1 PRO A 5 LYS A 24 1 20
HELIX 2 2 VAL A 65 ARG A 80 1 16
HELIX 3 3 PRO A 88 TYR A 92 5 5
HELIX 4 4 ALA A 98 ASN A 102 5 5
HELIX 5 5 THR A 105 THR A 111 1 7
HELIX 6 6 SER A 127 TRP A 138 1 12
HELIX 7 7 ALA A 151 VAL A 163 1 13
HELIX 8 8 SER A 169 VAL A 178 1 10
HELIX 9 9 PRO A 192 TYR A 199 5 8
HELIX 10 10 LEU A 216 GLY A 222 1 7
HELIX 11 11 ILE A 227 LYS A 239 1 13
HELIX 12 12 PRO A 240 ILE A 243 5 4
HELIX 13 13 GLU A 245 GLN A 256 1 12
HELIX 14 14 ASN A 279 SER A 287 1 9
HELIX 15 15 ASP A 288 LEU A 293 1 6
HELIX 16 16 PRO A 330 GLU A 333 5 4
HELIX 17 17 PRO A 345 GLN A 361 1 17
HELIX 18 18 PRO B 5 LYS B 24 1 20
HELIX 19 19 VAL B 65 ARG B 80 1 16
HELIX 20 20 PRO B 88 TYR B 92 5 5
HELIX 21 21 ALA B 98 ASN B 102 5 5
HELIX 22 22 THR B 105 THR B 111 1 7
HELIX 23 23 SER B 127 TRP B 138 1 12
HELIX 24 24 ALA B 151 VAL B 163 1 13
HELIX 25 25 SER B 169 VAL B 178 1 10
HELIX 26 26 PRO B 192 TYR B 199 5 8
HELIX 27 27 LEU B 216 GLY B 222 1 7
HELIX 28 28 THR B 226 LYS B 239 1 14
HELIX 29 29 PRO B 240 ILE B 243 5 4
HELIX 30 30 GLU B 245 GLN B 256 1 12
HELIX 31 31 PRO B 330 GLU B 333 5 4
HELIX 32 32 PRO B 345 GLN B 361 1 17
SHEET 1 A10 GLN A 52 PRO A 53 0
SHEET 2 A10 LYS A 37 ASP A 47 -1 N ALA A 46 O GLN A 52
SHEET 3 A10 GLY A 27 TYR A 34 -1 N VAL A 32 O TYR A 39
SHEET 4 A10 LEU A 334 ALA A 340 -1 O LEU A 339 N ALA A 29
SHEET 5 A10 GLY A 323 ILE A 329 -1 N ILE A 329 O LEU A 334
SHEET 6 A10 SER A 311 ALA A 318 -1 N GLY A 317 O SER A 324
SHEET 7 A10 GLU A 272 ASP A 275 -1 N LEU A 274 O TRP A 312
SHEET 8 A10 MET A 265 GLN A 267 -1 N TYR A 266 O MET A 273
SHEET 9 A10 ARG A 258 THR A 262 -1 N THR A 262 O MET A 265
SHEET 10 A10 LYS A 299 THR A 305 -1 O THR A 305 N ARG A 258
SHEET 1 B 2 LEU A 59 GLU A 61 0
SHEET 2 B 2 LYS A 224 THR A 226 -1 O SER A 225 N PHE A 60
SHEET 1 C 2 GLN A 147 ARG A 148 0
SHEET 2 C 2 ARG A 296 PRO A 297 -1 O ARG A 296 N ARG A 148
SHEET 1 D 2 GLY A 202 ARG A 204 0
SHEET 2 D 2 LYS A 207 VAL A 209 -1 O VAL A 209 N GLY A 202
SHEET 1 E10 GLN B 52 PRO B 53 0
SHEET 2 E10 LYS B 37 ASP B 47 -1 N ALA B 46 O GLN B 52
SHEET 3 E10 GLY B 27 TYR B 34 -1 N TYR B 34 O LYS B 37
SHEET 4 E10 LEU B 334 ALA B 340 -1 O GLY B 335 N ILE B 33
SHEET 5 E10 PHE B 322 ILE B 329 -1 N ILE B 329 O LEU B 334
SHEET 6 E10 SER B 311 THR B 319 -1 N GLY B 317 O SER B 324
SHEET 7 E10 GLU B 272 ASP B 275 -1 N GLU B 272 O HIS B 314
SHEET 8 E10 MET B 265 GLN B 267 -1 N TYR B 266 O MET B 273
SHEET 9 E10 ARG B 258 THR B 262 -1 N TYR B 259 O GLN B 267
SHEET 10 E10 LYS B 299 THR B 305 -1 O THR B 305 N ARG B 258
SHEET 1 F 2 PHE B 60 GLU B 61 0
SHEET 2 F 2 LYS B 224 SER B 225 -1 O SER B 225 N PHE B 60
SHEET 1 G 2 GLN B 147 ARG B 148 0
SHEET 2 G 2 ARG B 296 PRO B 297 -1 O ARG B 296 N ARG B 148
SHEET 1 H 2 GLY B 202 ARG B 204 0
SHEET 2 H 2 LYS B 207 VAL B 209 -1 O VAL B 209 N GLY B 202
LINK OG SER A 64 B7 VA1 A 964 1555 1555 1.68
LINK OG SER B 64 B7 VA1 B 964 1555 1555 1.54
CISPEP 1 TRP A 276 PRO A 277 0 1.14
CISPEP 2 THR A 302 PRO A 303 0 -1.67
CISPEP 3 TRP B 276 PRO B 277 0 -3.08
CISPEP 4 THR B 302 PRO B 303 0 -2.67
SITE 1 AC1 10 SER A 64 GLN A 120 ASP A 123 TYR A 150
SITE 2 AC1 10 ASN A 152 TYR A 221 GLY A 317 ALA A 318
SITE 3 AC1 10 HOH A1158 HOH A1163
SITE 1 AC2 11 SER B 64 GLN B 120 VAL B 121 ASP B 123
SITE 2 AC2 11 TYR B 150 ASN B 152 TYR B 221 GLY B 317
SITE 3 AC2 11 ALA B 318 HOH B 975 HOH B1142
CRYST1 117.632 77.236 97.825 90.00 116.73 90.00 C 1 2 1 8
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 0.008501 0.000000 0.004281 0.00000
SCALE2 0.000000 0.012947 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011445 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
