HEADER HYDROLASE 23-JAN-13 4IVK
TITLE CRYSTAL STRUCTURE OF A FAMMILY VIII CARBOXYLESTERASE IN A COMPLEX WITH
TITLE 2 CEPHALOTHIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASES;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 OTHER_DETAILS: DEEP SEA SEDIMENT
KEYWDS HELICAL DOMAIN AND A ALPHA/BETA DOMAIN, DEEP SEA SEDIMENT, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.J.AN,M.-K.KIM,C.-S.JEONG,S.-S.CHA
REVDAT 3 20-SEP-23 4IVK 1 REMARK SEQADV LINK
REVDAT 2 30-OCT-13 4IVK 1 JRNL
REVDAT 1 19-JUN-13 4IVK 0
JRNL AUTH S.S.CHA,Y.J.AN,C.S.JEONG,M.K.KIM,J.H.JEON,C.M.LEE,H.S.LEE,
JRNL AUTH 2 S.G.KANG,J.H.LEE
JRNL TITL STRUCTURAL BASIS FOR THE BETA-LACTAMASE ACTIVITY OF ESTU1, A
JRNL TITL 2 FAMILY VIII CARBOXYLESTERASE.
JRNL REF PROTEINS V. 81 2045 2013
JRNL REFN ISSN 0887-3585
JRNL PMID 23737193
JRNL DOI 10.1002/PROT.24334
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 84680
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4471
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6197
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE SET COUNT : 327
REMARK 3 BIN FREE R VALUE : 0.2380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3086
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 338
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.18000
REMARK 3 B22 (A**2) : -1.18000
REMARK 3 B33 (A**2) : 2.36000
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): 0.075
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.068
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.039
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.725
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3197 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3037 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4329 ; 1.139 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7009 ; 0.749 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 403 ; 5.566 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 126 ;29.294 ;23.651
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 529 ;12.004 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;13.039 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 472 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3594 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 698 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 6234 ; 1.564 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 93 ;27.141 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 6410 ; 8.950 ; 5.000
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 : 1.20
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 4IVK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1000077263.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NE3A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89398
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 4IVI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2 M AMMONIUM SULFATE AND 0.1 M TRIS
REMARK 280 -HCL (PH 8.5), MICROBATCH, TEMPERATURE 295KK
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 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 0.00000
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 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 74.55100
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 74.55100
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 86.28550
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 74.55100
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 74.55100
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 86.28550
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 74.55100
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 74.55100
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 86.28550
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 74.55100
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 74.55100
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 86.28550
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 74.55100
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 74.55100
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 86.28550
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 74.55100
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 74.55100
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 86.28550
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 74.55100
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 74.55100
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 86.28550
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 74.55100
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 74.55100
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 86.28550
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 109670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 6 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 7 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 914 LIES ON A SPECIAL POSITION.
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 LYS A 2
REMARK 465 THR A 3
REMARK 465 SER A 4
REMARK 465 ALA A 5
REMARK 465 LYS A 6
REMARK 465 PHE A 7
REMARK 465 LEU A 8
REMARK 465 SER A 9
REMARK 465 PHE A 10
REMARK 465 ALA A 11
REMARK 465 VAL A 12
REMARK 465 SER A 13
REMARK 465 PHE A 14
REMARK 465 VAL A 15
REMARK 465 LEU A 16
REMARK 465 LEU A 17
REMARK 465 ILE A 18
REMARK 465 ILE A 19
REMARK 465 ALA A 20
REMARK 465 SER A 21
REMARK 465 THR A 22
REMARK 465 SER A 23
REMARK 465 PHE A 24
REMARK 465 HIS A 429
REMARK 465 HIS A 430
REMARK 465 HIS A 431
REMARK 465 HIS A 432
REMARK 465 HIS A 433
REMARK 465 HIS A 434
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 GLU A 26 CG CD OE1 OE2
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 GLU A 26 -56.58 161.41
REMARK 500 TYR A 99 -119.05 43.24
REMARK 500 LEU A 245 -59.37 -131.69
REMARK 500 ASP A 274 45.25 -141.80
REMARK 500 GLN A 296 -8.63 -154.79
REMARK 500 VAL A 369 -68.15 70.52
REMARK 500 PRO A 371 32.37 -83.07
REMARK 500 VAL A 406 -70.12 -127.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 CEP A 501
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CEP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IVI RELATED DB: PDB
DBREF 4IVK A 1 426 UNP K4HQE7 K4HQE7_9BACT 1 426
SEQADV 4IVK LEU A 427 UNP K4HQE7 EXPRESSION TAG
SEQADV 4IVK GLU A 428 UNP K4HQE7 EXPRESSION TAG
SEQADV 4IVK HIS A 429 UNP K4HQE7 EXPRESSION TAG
SEQADV 4IVK HIS A 430 UNP K4HQE7 EXPRESSION TAG
SEQADV 4IVK HIS A 431 UNP K4HQE7 EXPRESSION TAG
SEQADV 4IVK HIS A 432 UNP K4HQE7 EXPRESSION TAG
SEQADV 4IVK HIS A 433 UNP K4HQE7 EXPRESSION TAG
SEQADV 4IVK HIS A 434 UNP K4HQE7 EXPRESSION TAG
SEQRES 1 A 434 MET LYS THR SER ALA LYS PHE LEU SER PHE ALA VAL SER
SEQRES 2 A 434 PHE VAL LEU LEU ILE ILE ALA SER THR SER PHE ALA GLU
SEQRES 3 A 434 GLY PRO VAL THR ALA THR LYS PRO LYS GLU ALA GLY PHE
SEQRES 4 A 434 THR SER GLU GLY LEU ALA ARG ILE ASP ALA TYR LEU LYS
SEQRES 5 A 434 ASN GLU ILE GLN ALA LYS THR MET PRO GLY ALA VAL MET
SEQRES 6 A 434 MET ILE LYS ARG ASN GLY GLU THR ALA TYR PHE SER SER
SEQRES 7 A 434 PHE GLY LEU ARG ASP PRO ASP THR LYS GLU PRO MET THR
SEQRES 8 A 434 ALA GLU THR ILE PHE ARG ILE TYR SER MET SER LYS PRO
SEQRES 9 A 434 ILE THR THR VAL ALA ALA MET MET LEU VAL GLU GLU GLY
SEQRES 10 A 434 LYS LEU GLN LEU ASP GLU PRO VAL SER LYS TYR ILE PRO
SEQRES 11 A 434 SER PHE ALA ASN VAL LYS VAL GLY VAL GLU THR LYS GLY
SEQRES 12 A 434 GLU ASN GLY MET ALA LEU GLU THR GLY PRO VAL LYS ARG
SEQRES 13 A 434 ALA ILE THR ILE GLN ASP LEU MET ARG HIS THR SER GLY
SEQRES 14 A 434 ILE THR TYR GLY PHE VAL GLY ASP GLY LEU VAL LYS LYS
SEQRES 15 A 434 ALA TYR ILE ALA SER ASN LEU PHE ASP GLY ASP PHE ASP
SEQRES 16 A 434 ASN ALA GLU PHE ALA GLU ARG ILE ALA LYS LEU PRO LEU
SEQRES 17 A 434 VAL TYR GLN PRO GLY THR THR TRP ASP TYR GLY HIS SER
SEQRES 18 A 434 THR ASP ILE LEU GLY ARG VAL VAL GLU VAL VAL SER GLY
SEQRES 19 A 434 LYS SER LEU TYR GLN PHE GLU LYS GLU ARG LEU LEU ASP
SEQRES 20 A 434 PRO LEU GLY MET LYS ASP THR GLY PHE TYR VAL THR ASP
SEQRES 21 A 434 PRO ALA LYS LYS SER LEU VAL ALA GLU ALA MET PRO ASN
SEQRES 22 A 434 ASP ARG LYS ILE GLY GLY SER GLU MET PHE ASP PRO ARG
SEQRES 23 A 434 VAL GLN LYS LYS TRP GLU PRO GLY GLY GLN GLY MET VAL
SEQRES 24 A 434 SER THR ILE GLY ASP TYR ALA ARG PHE THR GLN MET VAL
SEQRES 25 A 434 LEU ASN GLY GLY THR LEU ASP GLY LYS ARG TYR LEU SER
SEQRES 26 A 434 PRO LYS THR ILE ALA TYR MET GLY SER ASN HIS ILE PRO
SEQRES 27 A 434 GLN ALA SER GLY ILE VAL PRO GLY ALA TYR TYR LEU PRO
SEQRES 28 A 434 GLY PRO GLY VAL GLY PHE GLY LEU GLY PHE ALA VAL ARG
SEQRES 29 A 434 THR GLU ALA GLY VAL THR PRO VAL GLU GLY SER VAL GLY
SEQRES 30 A 434 ASP LEU SER TRP GLY GLY ALA GLY GLY THR VAL PHE TRP
SEQRES 31 A 434 ILE ASP PRO LYS GLU ASN LEU THR VAL VAL PHE MET ALA
SEQRES 32 A 434 PRO MET VAL SER PRO ARG ALA ARG VAL TRP ARG THR LEU
SEQRES 33 A 434 ARG ASN ILE VAL TYR GLY ALA PHE ASP ARG LEU GLU HIS
SEQRES 34 A 434 HIS HIS HIS HIS HIS
HET CEP A 501 22
HET SO4 A 502 5
HET SO4 A 503 5
HET SO4 A 504 5
HET SO4 A 505 5
HETNAM CEP CEPHALOTHIN GROUP
HETNAM SO4 SULFATE ION
FORMUL 2 CEP C16 H18 N2 O6 S2
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 7 HOH *338(H2 O)
HELIX 1 1 THR A 40 ALA A 57 1 18
HELIX 2 2 MET A 101 GLU A 116 1 16
HELIX 3 3 PRO A 124 TYR A 128 5 5
HELIX 4 4 ILE A 129 ALA A 133 5 5
HELIX 5 5 THR A 159 HIS A 166 1 8
HELIX 6 6 GLY A 178 SER A 187 1 10
HELIX 7 7 ASP A 195 LYS A 205 1 11
HELIX 8 8 HIS A 220 GLY A 234 1 15
HELIX 9 9 SER A 236 LEU A 245 1 10
HELIX 10 10 LEU A 245 GLY A 250 1 6
HELIX 11 11 LYS A 263 VAL A 267 5 5
HELIX 12 12 MET A 271 ASP A 274 5 4
HELIX 13 13 THR A 301 ASN A 314 1 14
HELIX 14 14 SER A 325 GLY A 333 1 9
HELIX 15 15 PRO A 338 GLY A 342 5 5
HELIX 16 16 PRO A 408 ALA A 423 1 16
SHEET 1 A 8 GLU A 26 PRO A 28 0
SHEET 2 A 8 GLU A 72 GLY A 80 -1 O SER A 78 N GLY A 27
SHEET 3 A 8 GLY A 62 ARG A 69 -1 N ILE A 67 O TYR A 75
SHEET 4 A 8 LEU A 397 MET A 402 -1 O THR A 398 N LYS A 68
SHEET 5 A 8 VAL A 388 ASP A 392 -1 N ASP A 392 O LEU A 397
SHEET 6 A 8 LEU A 379 GLY A 382 -1 N LEU A 379 O ILE A 391
SHEET 7 A 8 ALA A 362 ARG A 364 -1 N ALA A 362 O SER A 380
SHEET 8 A 8 VAL A 355 PHE A 357 -1 N GLY A 356 O VAL A 363
SHEET 1 B 2 PHE A 96 ARG A 97 0
SHEET 2 B 2 VAL A 299 SER A 300 -1 O SER A 300 N PHE A 96
SHEET 1 C 2 LYS A 136 GLY A 143 0
SHEET 2 C 2 GLY A 146 PRO A 153 -1 O GLU A 150 N VAL A 139
SHEET 1 D 2 THR A 215 TRP A 216 0
SHEET 2 D 2 VAL A 344 PRO A 345 1 O VAL A 344 N TRP A 216
SHEET 1 E 2 LYS A 276 ILE A 277 0
SHEET 2 E 2 SER A 280 GLU A 281 -1 O SER A 280 N ILE A 277
SHEET 1 F 2 THR A 317 LEU A 318 0
SHEET 2 F 2 LYS A 321 ARG A 322 -1 O LYS A 321 N LEU A 318
LINK OG SER A 100 C8 CEP A 501 1555 1555 1.37
SITE 1 AC1 11 TYR A 99 SER A 100 PHE A 174 VAL A 175
SITE 2 AC1 11 TYR A 218 ILE A 277 GLN A 296 GLY A 383
SITE 3 AC1 11 ALA A 384 ARG A 409 HOH A 865
SITE 1 AC2 4 LYS A 33 PRO A 34 LYS A 35 GLU A 36
SITE 1 AC3 7 VAL A 29 SER A 78 THR A 91 ALA A 92
SITE 2 AC3 7 GLU A 93 HOH A 869 HOH A 880
SITE 1 AC4 7 GLY A 250 GLY A 303 ASP A 304 ARG A 307
SITE 2 AC4 7 HOH A 667 HOH A 732 HOH A 772
SITE 1 AC5 3 GLY A 279 SER A 280 GLU A 281
CRYST1 149.102 149.102 172.571 90.00 90.00 90.00 I 4 2 2 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 0.006707 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006707 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005795 0.00000
(ATOM LINES ARE NOT SHOWN.)
END