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HEADER HYDROLASE 20-FEB-03 1ODT
TITLE CEPHALOSPORIN C DEACETYLASE MUTATED, IN COMPLEX WITH
TITLE 2 ACETATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CEPHALOSPORIN C DEACETYLASE;
COMPND 3 SYNONYM: MULTI-FUNCTIONAL ESTERASE, CAH;
COMPND 4 CHAIN: C, H;
COMPND 5 EC: 3.1.1.41;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: COMPLEX WITH ACETATE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 4 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_VECTOR: PET26B;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET26B
KEYWDS ALPHA/BETA HYDROLASE, ACETYLXYLAN, CARBOHYDRATE ESTERASE,
KEYWDS 2 CEPHALOSPORIN, X-RAY STRUCTURE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.VINCENT,S.J.CHARNOCK,K.H.G.VERSCHUEREN,J.P.TURKENBURG,
AUTHOR 2 D.J.SCOTT,W.A.OFFEN,S.ROBERTS,G.PELL,H.J.GILBERT,
AUTHOR 3 J.A.BRANNIGAN,G.J.DAVIES
REVDAT 1 10-JUL-03 1ODT 0
JRNL AUTH F.VINCENT,S.CHARNOCK,K.VERSCHUEREN,J.TURKENBURG,
JRNL AUTH 2 D.SCOTT,W.OFFEN,S.ROBERTS,G.PELL,H.GILBERT,G.DAVIES,
JRNL AUTH 3 J.BRANNIGAN
JRNL TITL MULTIFUNCTIONAL XYLOOLIGOSACCHARIDE/CEPHALOSPORIN C
JRNL TITL 2 DEACETYLASE REVEALED BY THE HEXAMERIC STRUCTURE OF
JRNL TITL 3 THE BACILLUS SUBTILIS ENZYME AT 1.9A RESOLUTION
JRNL REF J.MOL.BIOL. V. 330 593 2003
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 1.7 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.19
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 95.35
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.53
REMARK 3 NUMBER OF REFLECTIONS : 63610
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) : 0.15752
REMARK 3 R VALUE (WORKING SET) : 0.15569
REMARK 3 FREE R VALUE : 0.19120
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 3376
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.699
REMARK 3 BIN RESOLUTION RANGE LOW : 1.743
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4548
REMARK 3 BIN R VALUE (WORKING SET) : 0.224
REMARK 3 BIN FREE R VALUE SET COUNT : 241
REMARK 3 BIN FREE R VALUE : 0.284
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5065
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 563
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.564
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.94
REMARK 3 B22 (A**2) : -0.94
REMARK 3 B33 (A**2) : 1.41
REMARK 3 B12 (A**2) : -0.47
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.101
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.099
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.004
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 5211 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4618 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED (DEGREES): 7074 ; 1.589 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10775 ; 1.075 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 632 ; 5.869 ; 5.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 755 ; 0.131 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 5800 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1078 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED (A): 1109 ; 0.227 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5575 ; 0.246 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2835 ; 0.089 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED (A): 445 ; 0.188 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 24 ; 0.218 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 60 ; 0.330 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED (A): 37 ; 0.208 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 3164 ; 0.783 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 5096 ; 1.352 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 2047 ; 2.413 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 1978 ; 3.793 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 317
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3370 77.9850 43.4120
REMARK 3 T TENSOR
REMARK 3 T11: 0.0892 T22: 0.1150
REMARK 3 T33: 0.0072 T12: 0.0058
REMARK 3 T13: 0.0150 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 0.3932 L22: 0.6111
REMARK 3 L33: 0.3823 L12: -0.0330
REMARK 3 L13: 0.0887 L23: -0.0952
REMARK 3 S TENSOR
REMARK 3 S11: -0.0036 S12: 0.0493 S13: -0.0175
REMARK 3 S21: -0.0398 S22: -0.0017 S23: -0.0373
REMARK 3 S31: 0.0179 S32: 0.0377 S33: 0.0054
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 317
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4900 106.8960 66.7690
REMARK 3 T TENSOR
REMARK 3 T11: 0.0837 T22: 0.0979
REMARK 3 T33: 0.0154 T12: -0.0108
REMARK 3 T13: -0.0122 T23: -0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 0.4109 L22: 0.6824
REMARK 3 L33: 0.3956 L12: -0.0219
REMARK 3 L13: -0.0522 L23: -0.1084
REMARK 3 S TENSOR
REMARK 3 S11: -0.0033 S12: -0.0236 S13: 0.0227
REMARK 3 S21: 0.0347 S22: -0.0118 S23: -0.0481
REMARK 3 S31: -0.0368 S32: 0.0492 S33: 0.0150
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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
REMARK 3 THE RIDING POSITIONS
REMARK 4
REMARK 4 1ODT COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 21-FEB-2003.
REMARK 100 THE EBI ID CODE IS EBI-12218.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-2002
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63610
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.69
REMARK 200 RESOLUTION RANGE LOW (A) : 95
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 3.1
REMARK 200 R MERGE (I) : 0.048
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.9
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.8
REMARK 200 R MERGE FOR SHELL (I) : 0.393
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.7
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: PDB ENTRY 1ODS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.1
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MOPS PH 6.5
REMARK 280 0.2 M NA ACETATE 30% MPD , 0.1M MGCL2,
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 Y-X,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,Y-X,-Z
REMARK 290 7555 2/3+X,1/3+Y,1/3+Z
REMARK 290 8555 2/3-Y,1/3+X-Y,1/3+Z
REMARK 290 9555 2/3+Y-X,1/3-X,1/3+Z
REMARK 290 10555 2/3+Y,1/3+X,1/3-Z
REMARK 290 11555 2/3+X-Y,1/3-Y,1/3-Z
REMARK 290 12555 2/3-X,1/3+Y-X,1/3-Z
REMARK 290 13555 1/3+X,2/3+Y,2/3+Z
REMARK 290 14555 1/3-Y,2/3+X-Y,2/3+Z
REMARK 290 15555 1/3+Y-X,2/3-X,2/3+Z
REMARK 290 16555 1/3+Y,2/3+X,2/3-Z
REMARK 290 17555 1/3+X-Y,2/3-Y,2/3-Z
REMARK 290 18555 1/3-X,2/3+Y-X,2/3-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 -0.500010 -0.866009 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866042 -0.499990 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.499990 0.866009 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866042 -0.500010 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500010 0.865998 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866042 0.500010 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000022 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 -0.499990 -0.866020 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866042 0.499990 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 78.58300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.37107
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 44.03267
REMARK 290 SMTRY1 8 -0.500010 -0.866009 0.000000 78.58300
REMARK 290 SMTRY2 8 0.866042 -0.499990 0.000000 45.37107
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 44.03267
REMARK 290 SMTRY1 9 -0.499990 0.866009 0.000000 78.58300
REMARK 290 SMTRY2 9 -0.866042 -0.500010 0.000000 45.37107
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 44.03267
REMARK 290 SMTRY1 10 -0.500010 0.865998 0.000000 78.58300
REMARK 290 SMTRY2 10 0.866042 0.500010 0.000000 45.37107
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 44.03267
REMARK 290 SMTRY1 11 1.000000 0.000022 0.000000 78.58300
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 45.37107
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 44.03267
REMARK 290 SMTRY1 12 -0.499990 -0.866020 0.000000 78.58300
REMARK 290 SMTRY2 12 -0.866042 0.499990 0.000000 45.37107
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 44.03267
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 -0.00100
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 90.74214
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 88.06533
REMARK 290 SMTRY1 14 -0.500010 -0.866009 0.000000 -0.00100
REMARK 290 SMTRY2 14 0.866042 -0.499990 0.000000 90.74214
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 88.06533
REMARK 290 SMTRY1 15 -0.499990 0.866009 0.000000 -0.00100
REMARK 290 SMTRY2 15 -0.866042 -0.500010 0.000000 90.74214
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 88.06533
REMARK 290 SMTRY1 16 -0.500010 0.865998 0.000000 -0.00100
REMARK 290 SMTRY2 16 0.866042 0.500010 0.000000 90.74214
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 88.06533
REMARK 290 SMTRY1 17 1.000000 0.000022 0.000000 -0.00100
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 90.74214
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 88.06533
REMARK 290 SMTRY1 18 -0.499990 -0.866020 0.000000 -0.00100
REMARK 290 SMTRY2 18 -0.866042 0.499990 0.000000 90.74214
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 88.06533
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 C 1 .. 317 H 1 .. 317 0.153
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 3 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: HEXAMERIC
REMARK 300
REMARK 300 FOR THE HOMO-ASSEMBLY DESCRIBED BY REMARK 350
REMARK 300 THE DIFFERENCE IN ACCESSIBLE SURFACE AREA PER
REMARK 300 CHAIN BETWEEN THE ISOLATED CHAIN AND THAT FOR
REMARK 300 THE CHAIN IN THE COMPLEX IS 2821.8 ANGSTROM**2
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: C, H
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 -0.500010 -0.866009 0.000000 78.58200
REMARK 350 BIOMT2 2 0.866042 -0.499990 0.000000 136.11321
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.499990 0.866009 0.000000 -78.58500
REMARK 350 BIOMT2 3 -0.866042 -0.500010 0.000000 136.11321
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 HOH S 59 LIES ON A SPECIAL POSITION.
REMARK 375 HOH X 52 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED MUTATION IN CHAIN C, SER 181 TO ALA 181
REMARK 400 ENGINEERED MUTATION IN CHAIN H, SER 181 TO ALA 181
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 GLY C 318
REMARK 465 GLY H 318
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 LEU C 316 O
REMARK 470 LEU H 316 O
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU C 3 CB - CG - CD1 ANGL. DEV. = 10.8 DEGREES
REMARK 500 LEU C 30 CA - CB - CG ANGL. DEV. = 10.8 DEGREES
REMARK 500 LEU C 290 CB - CG - CD2 ANGL. DEV. = 12.1 DEGREES
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 AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 500 NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUESS: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET H 102 SD MET H 102 CE -0.249
REMARK 500
REMARK 500 REMARK: NULL
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
REMARK 500 O ASP C 195 O HOH X 185 2.18
REMARK 500 OE2 GLU H 26 O HOH S 42 1.97
REMARK 500 O HOH S 138 O HOH X 140 2.16
REMARK 500 O HOH S 190 O HOH S 192 2.09
REMARK 500 O HOH X 104 O HOH X 186 2.10
REMARK 500 O HOH X 162 O HOH X 169 2.19
REMARK 500 O HOH X 251 O HOH X 271 2.16
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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500
REMARK 500 SER C 122 -51.67 65.84
REMARK 500 ALA C 181 -118.69 62.96
REMARK 500 SER H 122 -53.62 62.85
REMARK 500 ALA H 181 -115.22 61.37
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 C X
REMARK 525 H S
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: ACT BINDING SITE FOR CHAIN H
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1L7A RELATED DB: PDB
REMARK 900 STRUCTURAL GENOMICS, CRYSTAL STRUCTURE OF
REMARK 900 CEPHALOSPORIN CDEACETYLASE
REMARK 900 RELATED ID: 1ODS RELATED DB: PDB
REMARK 900 CEPHALOSPORIN C DEACETYLASE FROM BACILLUS
REMARK 900 SUBTILIS
DBREF 1ODT C 1 318 SWS P94388 P94388 1 318
DBREF 1ODT H 1 318 SWS P94388 P94388 1 318
SEQADV 1ODT ALA C 181 SWS P94388 SER 181 ENGINEERED MUTATION
SEQADV 1ODT ALA H 181 SWS P94388 SER 181 ENGINEERED MUTATION
SEQADV 1ODT GLU C 220 SWS P94388 GLN 220 CONFLICT
SEQADV 1ODT GLU H 220 SWS P94388 GLN 220 CONFLICT
SEQRES 1 C 318 MET GLN LEU PHE ASP LEU PRO LEU ASP GLN LEU GLN THR
SEQRES 2 C 318 TYR LYS PRO GLU LYS THR ALA PRO LYS ASP PHE SER GLU
SEQRES 3 C 318 PHE TRP LYS LEU SER LEU GLU GLU LEU ALA LYS VAL GLN
SEQRES 4 C 318 ALA GLU PRO ASP LEU GLN PRO VAL ASP TYR PRO ALA ASP
SEQRES 5 C 318 GLY VAL LYS VAL TYR ARG LEU THR TYR LYS SER PHE GLY
SEQRES 6 C 318 ASN ALA ARG ILE THR GLY TRP TYR ALA VAL PRO ASP LYS
SEQRES 7 C 318 GLU GLY PRO HIS PRO ALA ILE VAL LYS TYR HIS GLY TYR
SEQRES 8 C 318 ASN ALA SER TYR ASP GLY GLU ILE HIS GLU MET VAL ASN
SEQRES 9 C 318 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 C 318 ARG GLY GLN GLN SER SER GLU ASP THR SER ILE SER PRO
SEQRES 11 C 318 HIS GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 C 318 ASP LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 C 318 ALA VAL ARG ALA LEU GLU VAL ILE SER SER PHE ASP GLU
SEQRES 14 C 318 VAL ASP GLU THR ARG ILE GLY VAL THR GLY GLY ALA GLN
SEQRES 15 C 318 GLY GLY GLY LEU THR ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 C 318 ILE PRO LYS ALA ALA VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 C 318 ASN PHE GLU ARG ALA ILE ASP VAL ALA LEU GLU GLU PRO
SEQRES 18 C 318 TYR LEU GLU ILE ASN SER PHE PHE ARG ARG ASN GLY SER
SEQRES 19 C 318 PRO GLU THR GLU VAL GLN ALA MET LYS THR LEU SER TYR
SEQRES 20 C 318 PHE ASP ILE MET ASN LEU ALA ASP ARG VAL LYS VAL PRO
SEQRES 21 C 318 VAL LEU MET SER ILE GLY LEU ILE ASP LYS VAL THR PRO
SEQRES 22 C 318 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 C 318 LYS LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 C 318 TYR ILE PRO ALA PHE GLN THR GLU LYS LEU ALA PHE PHE
SEQRES 25 C 318 LYS GLN HIS LEU LYS GLY
SEQRES 1 H 318 MET GLN LEU PHE ASP LEU PRO LEU ASP GLN LEU GLN THR
SEQRES 2 H 318 TYR LYS PRO GLU LYS THR ALA PRO LYS ASP PHE SER GLU
SEQRES 3 H 318 PHE TRP LYS LEU SER LEU GLU GLU LEU ALA LYS VAL GLN
SEQRES 4 H 318 ALA GLU PRO ASP LEU GLN PRO VAL ASP TYR PRO ALA ASP
SEQRES 5 H 318 GLY VAL LYS VAL TYR ARG LEU THR TYR LYS SER PHE GLY
SEQRES 6 H 318 ASN ALA ARG ILE THR GLY TRP TYR ALA VAL PRO ASP LYS
SEQRES 7 H 318 GLU GLY PRO HIS PRO ALA ILE VAL LYS TYR HIS GLY TYR
SEQRES 8 H 318 ASN ALA SER TYR ASP GLY GLU ILE HIS GLU MET VAL ASN
SEQRES 9 H 318 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 H 318 ARG GLY GLN GLN SER SER GLU ASP THR SER ILE SER PRO
SEQRES 11 H 318 HIS GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 H 318 ASP LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 H 318 ALA VAL ARG ALA LEU GLU VAL ILE SER SER PHE ASP GLU
SEQRES 14 H 318 VAL ASP GLU THR ARG ILE GLY VAL THR GLY GLY ALA GLN
SEQRES 15 H 318 GLY GLY GLY LEU THR ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 H 318 ILE PRO LYS ALA ALA VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 H 318 ASN PHE GLU ARG ALA ILE ASP VAL ALA LEU GLU GLU PRO
SEQRES 18 H 318 TYR LEU GLU ILE ASN SER PHE PHE ARG ARG ASN GLY SER
SEQRES 19 H 318 PRO GLU THR GLU VAL GLN ALA MET LYS THR LEU SER TYR
SEQRES 20 H 318 PHE ASP ILE MET ASN LEU ALA ASP ARG VAL LYS VAL PRO
SEQRES 21 H 318 VAL LEU MET SER ILE GLY LEU ILE ASP LYS VAL THR PRO
SEQRES 22 H 318 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 H 318 LYS LYS GLU LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 H 318 TYR ILE PRO ALA PHE GLN THR GLU LYS LEU ALA PHE PHE
SEQRES 25 H 318 LYS GLN HIS LEU LYS GLY
HET ACT C1318 4
HET ACT H1318 4
HETNAM ACT ACETATE ION
FORMUL 3 ACT 2(C2 H3 O2 1-)
FORMUL 4 HOH *563(H2 O1)
HELIX 1 1 PRO C 7 GLN C 12 1 6
HELIX 2 2 ASP C 23 LYS C 37 1 15
HELIX 3 3 PHE C 64 ASN C 66 5 3
HELIX 4 4 TYR C 95 GLY C 97 5 3
HELIX 5 5 GLU C 98 HIS C 108 1 11
HELIX 6 6 TYR C 148 SER C 166 1 19
HELIX 7 7 ALA C 181 SER C 194 1 14
HELIX 8 8 ASN C 209 ALA C 217 1 9
HELIX 9 9 TYR C 222 ASN C 232 1 11
HELIX 10 10 SER C 234 TYR C 247 1 14
HELIX 11 11 ASP C 249 ALA C 254 1 6
HELIX 12 12 ASP C 255 VAL C 257 5 3
HELIX 13 13 PRO C 273 LEU C 284 1 12
HELIX 14 14 ILE C 301 HIS C 315 1 15
HELIX 15 15 PRO H 7 THR H 13 1 7
HELIX 16 16 ASP H 23 LYS H 37 1 15
HELIX 17 17 PHE H 64 ASN H 66 5 3
HELIX 18 18 TYR H 95 GLY H 97 5 3
HELIX 19 19 GLU H 98 HIS H 108 1 11
HELIX 20 20 TYR H 148 SER H 166 1 19
HELIX 21 21 ALA H 181 SER H 194 1 14
HELIX 22 22 ASN H 209 ALA H 217 1 9
HELIX 23 23 TYR H 222 ASN H 232 1 11
HELIX 24 24 SER H 234 TYR H 247 1 14
HELIX 25 25 ASP H 249 ALA H 254 1 6
HELIX 26 26 ASP H 255 VAL H 257 5 3
HELIX 27 27 PRO H 273 LEU H 284 1 12
HELIX 28 28 ILE H 301 HIS H 315 1 15
SHEET 1 CA 9 ASP C 43 VAL C 47 0
SHEET 2 CA 9 VAL C 54 LYS C 62 -1 O VAL C 56 N VAL C 47
SHEET 3 CA 9 ARG C 68 PRO C 76 -1 O ILE C 69 N TYR C 61
SHEET 4 CA 9 ALA C 111 MET C 115 -1 O THR C 112 N ALA C 74
SHEET 5 CA 9 HIS C 82 TYR C 88 1 O PRO C 83 N ALA C 111
SHEET 6 CA 9 VAL C 170 GLY C 180 1 N ASP C 171 O HIS C 82
SHEET 7 CA 9 ALA C 199 ASP C 203 1 O ALA C 199 N VAL C 177
SHEET 8 CA 9 VAL C 261 GLY C 266 1 O LEU C 262 N ALA C 202
SHEET 9 CA 9 LYS C 288 TYR C 293 1 O GLU C 289 N MET C 263
SHEET 1 HA 9 ASP H 43 VAL H 47 0
SHEET 2 HA 9 VAL H 54 SER H 63 -1 O VAL H 56 N VAL H 47
SHEET 3 HA 9 ALA H 67 PRO H 76 -1 O ALA H 67 N SER H 63
SHEET 4 HA 9 ALA H 111 MET H 115 -1 O THR H 112 N ALA H 74
SHEET 5 HA 9 HIS H 82 TYR H 88 1 O PRO H 83 N ALA H 111
SHEET 6 HA 9 VAL H 170 GLY H 180 1 N ASP H 171 O HIS H 82
SHEET 7 HA 9 ALA H 199 ASP H 203 1 O ALA H 199 N VAL H 177
SHEET 8 HA 9 VAL H 261 GLY H 266 1 O LEU H 262 N ALA H 202
SHEET 9 HA 9 LYS H 288 TYR H 293 1 O GLU H 289 N MET H 263
CISPEP 1 GLY C 80 PRO C 81 0 1.84
CISPEP 2 GLU C 220 PRO C 221 0 2.05
CISPEP 3 GLY H 80 PRO H 81 0 -4.37
CISPEP 4 GLU H 220 PRO H 221 0 3.25
SITE 1 AC1 7 GLY C 90 TYR C 91 ALA C 181 GLN C 182
SITE 2 AC1 7 TYR C 206 PRO C 221 HIS C 298
SITE 1 AC2 6 GLY H 90 TYR H 91 ALA H 181 GLN H 182
SITE 2 AC2 6 HIS H 298 HOH S 274
CRYST1 157.167 157.170 132.098 90.00 90.00 120.00 H 3 2 36
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 0.006363 0.003673 0.000000 0.00000
SCALE2 0.000000 0.007347 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007570 0.00000
MTRIX1 1 0.991000 0.133000 0.000000 -11.98389 1
MTRIX2 1 0.133000 -0.991000 0.003000 180.54744 1
MTRIX3 1 0.001000 -0.003000 -1.000000 110.41402 1
TER 2531 LYS C 317
TER 5067 LYS H 317
MASTER 450 0 2 28 18 0 4 9 5636 2 8 50
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