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HEADER HYDROLASE 29-OCT-13 4CCW
TITLE CRYSTAL STRUCTURE OF NAPROXEN ESTERASE (CARBOXYLESTERASE NP)
TITLE 2 FROM BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYL ESTERASE NP;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 2-300;
COMPND 5 SYNONYM: CARBOXYLESTERASE NP;
COMPND 6 EC: 3.1.1.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 STRAIN: THAI I-8;
SOURCE 5 ATCC: CBS 679.85;
SOURCE 6 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 1423;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: I-85
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.J.ROZEBOOM,L.F.GODINHO,M.NARDINI,W.J.QUAX,B.W.DIJKSTRA
REVDAT 1 22-JAN-14 4CCW 0
JRNL AUTH H.J.ROZEBOOM,L.F.GODINHO,M.NARDINI,W.J.QUAX,B.W.DIJKSTRA
JRNL TITL CRYSTL STRUCTURES OF TWO BACILLUS CARBOXYLESTERASES WITH
JRNL TITL 2 DIFFERENT ENATIOSELECTIVITIES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.40
REMARK 3 NUMBER OF REFLECTIONS : 26175
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) : 0.22895
REMARK 3 R VALUE (WORKING SET) : 0.22695
REMARK 3 FREE R VALUE : 0.26678
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1413
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) : 1.750
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.795
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1582
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.247
REMARK 3 BIN FREE R VALUE SET COUNT : 76
REMARK 3 BIN FREE R VALUE : 0.306
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2290
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.473
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.65
REMARK 3 B22 (A**2) : 0.65
REMARK 3 B33 (A**2) : -0.97
REMARK 3 B12 (A**2) : 0.32
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): 0.162
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.149
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.935
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2366 ; 0.008 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3216 ; 1.173 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 284 ; 5.207 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 113 ;33.981 ;23.628
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 375 ;13.193 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;21.249 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 342 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1831 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 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 : 9
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 : A 9 A 25
REMARK 3 ORIGIN FOR THE GROUP (A): 32.3386 1.1237 31.1793
REMARK 3 T TENSOR
REMARK 3 T11: 0.3435 T22: 0.2601
REMARK 3 T33: 0.0669 T12: 0.0578
REMARK 3 T13: 0.0100 T23: 0.0566
REMARK 3 L TENSOR
REMARK 3 L11: 3.1747 L22: 11.5865
REMARK 3 L33: 7.0661 L12: 5.2267
REMARK 3 L13: -0.7407 L23: -0.3129
REMARK 3 S TENSOR
REMARK 3 S11: -0.0084 S12: -0.3417 S13: 0.0119
REMARK 3 S21: 0.1091 S22: 0.0616 S23: 0.1458
REMARK 3 S31: 0.3000 S32: -0.4384 S33: -0.0531
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 : A 26 A 39
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3366 16.9683 33.2839
REMARK 3 T TENSOR
REMARK 3 T11: 0.7068 T22: 0.4683
REMARK 3 T33: 0.0999 T12: 0.2861
REMARK 3 T13: 0.0077 T23: -0.0576
REMARK 3 L TENSOR
REMARK 3 L11: 14.7339 L22: 4.5753
REMARK 3 L33: 3.5080 L12: 2.2497
REMARK 3 L13: 2.0786 L23: 2.5816
REMARK 3 S TENSOR
REMARK 3 S11: -1.5470 S12: -0.7322 S13: 0.4690
REMARK 3 S21: 0.9774 S22: 0.9670 S23: 0.2972
REMARK 3 S31: 0.2258 S32: 0.0974 S33: 0.5800
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 40 A 100
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5347 17.4777 25.3904
REMARK 3 T TENSOR
REMARK 3 T11: 0.2668 T22: 0.1397
REMARK 3 T33: 0.1238 T12: -0.0064
REMARK 3 T13: 0.0661 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 1.6561 L22: 1.6346
REMARK 3 L33: 1.8563 L12: 0.2984
REMARK 3 L13: -0.1173 L23: 0.6772
REMARK 3 S TENSOR
REMARK 3 S11: 0.0621 S12: -0.2927 S13: 0.0759
REMARK 3 S21: 0.3774 S22: 0.0032 S23: 0.1295
REMARK 3 S31: 0.1460 S32: -0.0229 S33: -0.0653
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 101 A 162
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2919 19.6300 15.0083
REMARK 3 T TENSOR
REMARK 3 T11: 0.1993 T22: 0.1498
REMARK 3 T33: 0.2407 T12: 0.0177
REMARK 3 T13: 0.0758 T23: 0.0175
REMARK 3 L TENSOR
REMARK 3 L11: 0.9940 L22: 1.1910
REMARK 3 L33: 1.5033 L12: -0.0405
REMARK 3 L13: -0.2282 L23: 0.7218
REMARK 3 S TENSOR
REMARK 3 S11: 0.0023 S12: -0.0925 S13: 0.0991
REMARK 3 S21: 0.2311 S22: 0.0209 S23: 0.2033
REMARK 3 S31: 0.0130 S32: -0.2614 S33: -0.0232
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 163 A 189
REMARK 3 ORIGIN FOR THE GROUP (A): 41.1586 3.1668 9.7569
REMARK 3 T TENSOR
REMARK 3 T11: 0.1553 T22: 0.1318
REMARK 3 T33: 0.2406 T12: 0.0385
REMARK 3 T13: -0.0330 T23: -0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 2.2883 L22: 2.9580
REMARK 3 L33: 3.7751 L12: -1.4566
REMARK 3 L13: 0.1274 L23: -1.2262
REMARK 3 S TENSOR
REMARK 3 S11: -0.0974 S12: -0.1566 S13: 0.0141
REMARK 3 S21: 0.1816 S22: 0.1005 S23: -0.1797
REMARK 3 S31: 0.3832 S32: 0.3332 S33: -0.0031
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 190 A 206
REMARK 3 ORIGIN FOR THE GROUP (A): 42.7038 6.1185 23.1675
REMARK 3 T TENSOR
REMARK 3 T11: 0.3867 T22: 0.1927
REMARK 3 T33: 0.1271 T12: 0.1369
REMARK 3 T13: -0.0446 T23: -0.0408
REMARK 3 L TENSOR
REMARK 3 L11: 9.0501 L22: 6.5890
REMARK 3 L33: 5.0446 L12: 6.2390
REMARK 3 L13: 3.0776 L23: -0.7201
REMARK 3 S TENSOR
REMARK 3 S11: -0.0987 S12: 0.3725 S13: -0.4231
REMARK 3 S21: 0.2067 S22: 0.1099 S23: -0.4659
REMARK 3 S31: 0.0220 S32: 0.5259 S33: -0.0113
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 207 A 217
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6134 -1.0042 16.6762
REMARK 3 T TENSOR
REMARK 3 T11: 0.7261 T22: 0.5688
REMARK 3 T33: 0.3154 T12: 0.1804
REMARK 3 T13: 0.0351 T23: 0.2267
REMARK 3 L TENSOR
REMARK 3 L11: 18.9776 L22: 3.8790
REMARK 3 L33: 47.4057 L12: -8.4866
REMARK 3 L13: 29.9167 L23: -13.5213
REMARK 3 S TENSOR
REMARK 3 S11: 1.3893 S12: -1.5776 S13: -1.2677
REMARK 3 S21: -0.4790 S22: 0.8290 S23: 0.6883
REMARK 3 S31: 1.9575 S32: -2.7458 S33: -2.2183
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 218 A 260
REMARK 3 ORIGIN FOR THE GROUP (A): 29.4549 20.6192 3.2451
REMARK 3 T TENSOR
REMARK 3 T11: 0.1471 T22: 0.0962
REMARK 3 T33: 0.2176 T12: -0.0192
REMARK 3 T13: 0.0192 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 1.2634 L22: 2.2228
REMARK 3 L33: 1.1442 L12: -0.1178
REMARK 3 L13: 0.3798 L23: -0.0595
REMARK 3 S TENSOR
REMARK 3 S11: -0.0746 S12: 0.0404 S13: 0.0338
REMARK 3 S21: 0.0539 S22: 0.0938 S23: 0.0505
REMARK 3 S31: -0.1362 S32: -0.0719 S33: -0.0192
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 261 A 293
REMARK 3 ORIGIN FOR THE GROUP (A): 38.8478 26.6282 13.0224
REMARK 3 T TENSOR
REMARK 3 T11: 0.2162 T22: 0.0636
REMARK 3 T33: 0.2522 T12: -0.0553
REMARK 3 T13: -0.0088 T23: -0.0394
REMARK 3 L TENSOR
REMARK 3 L11: 1.9649 L22: 2.8125
REMARK 3 L33: 3.2545 L12: -0.3690
REMARK 3 L13: 0.7636 L23: 0.5323
REMARK 3 S TENSOR
REMARK 3 S11: -0.0425 S12: -0.0922 S13: 0.3102
REMARK 3 S21: 0.3908 S22: 0.0055 S23: -0.2858
REMARK 3 S31: -0.4275 S32: 0.1325 S33: 0.0369
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 4CCW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-OCT-13.
REMARK 100 THE PDBE ID CODE IS EBI-58836.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUL-98
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : 28534
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.75
REMARK 200 RESOLUTION RANGE LOW (A) : 40.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.7
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.40
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.20
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRIES 1ZOI, 1IUN, 1C4X
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LIQUID-LIQUID DIFFUSION WITH
REMARK 280 80% PEG6000, 0.1 M TRIS PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 141.64067
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 70.82033
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 70.82033
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 141.64067
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 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 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 A2075 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 SER A 2
REMARK 465 ASN A 3
REMARK 465 HIS A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 SER A 7
REMARK 465 ILE A 8
REMARK 465 ALA A 294
REMARK 465 GLU A 295
REMARK 465 THR A 296
REMARK 465 GLY A 297
REMARK 465 ILE A 298
REMARK 465 SER A 299
REMARK 465 ARG A 300
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 10 76.49 -168.09
REMARK 500 LEU A 65 -3.01 73.49
REMARK 500 SER A 67 174.44 65.49
REMARK 500 ASN A 94 -160.60 -173.35
REMARK 500 GLU A 122 -78.77 -89.84
REMARK 500 SER A 130 -126.27 54.70
REMARK 500 GLU A 157 -114.20 44.40
REMARK 500 THR A 158 -64.82 74.89
REMARK 500 SER A 176 -112.28 27.89
REMARK 500 VAL A 275 58.29 -91.95
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 VKC A1294
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CCY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CARBOXYLESTERASE CESB (YBFK) FROM
REMARK 900 BACILLUS SUBTILIS
DBREF 4CCW A 2 300 UNP Q59248 Q59248_BACIU 2 300
SEQRES 1 A 299 SER ASN HIS SER SER SER ILE PRO GLU LEU SER ASP ASN
SEQRES 2 A 299 GLY ILE ARG TYR TYR GLN THR TYR ASN GLU SER LEU SER
SEQRES 3 A 299 LEU TRP PRO VAL ARG CYS LYS SER PHE TYR ILE SER THR
SEQRES 4 A 299 ARG PHE GLY GLN THR HIS VAL ILE ALA SER GLY PRO GLU
SEQRES 5 A 299 ASP ALA PRO PRO LEU VAL LEU LEU HIS GLY ALA LEU PHE
SEQRES 6 A 299 SER SER THR MET TRP TYR PRO ASN ILE ALA ASP TRP SER
SEQRES 7 A 299 SER LYS TYR ARG THR TYR ALA VAL ASP ILE ILE GLY ASP
SEQRES 8 A 299 LYS ASN LYS SER ILE PRO GLU ASN LEU SER GLY THR ARG
SEQRES 9 A 299 THR ASP TYR ALA ASN TRP LEU LEU ASP VAL PHE ASP ASN
SEQRES 10 A 299 LEU GLY ILE GLU LYS SER HIS MET ILE GLY LEU SER LEU
SEQRES 11 A 299 GLY GLY LEU HIS THR MET ASN PHE LEU LEU ARG MET PRO
SEQRES 12 A 299 GLU ARG VAL LYS SER ALA ALA ILE LEU SER PRO ALA GLU
SEQRES 13 A 299 THR PHE LEU PRO PHE HIS HIS ASP PHE TYR LYS TYR ALA
SEQRES 14 A 299 LEU GLY LEU THR ALA SER ASN GLY VAL GLU LYS PHE LEU
SEQRES 15 A 299 ASN TRP MET MET THR ASP GLN ASN VAL LEU HIS PRO ILE
SEQRES 16 A 299 PHE VAL LYS GLN PHE GLN ALA GLY VAL MET TRP GLN ASP
SEQRES 17 A 299 GLY SER ARG ASN PRO ASN PRO LYS ALA ASP GLY PHE PRO
SEQRES 18 A 299 TYR VAL PHE THR ASP GLU GLU LEU ARG SER ALA ARG VAL
SEQRES 19 A 299 PRO ILE LEU LEU LEU LEU GLY GLU HIS GLU VAL ILE TYR
SEQRES 20 A 299 ASP PRO HIS SER ALA LEU HIS ARG ALA SER SER PHE VAL
SEQRES 21 A 299 PRO ASP ILE GLU ALA GLU VAL ILE LYS ASN ALA GLY HIS
SEQRES 22 A 299 VAL LEU SER MET GLU GLN PRO ALA TYR VAL ASN GLU ARG
SEQRES 23 A 299 VAL MET ARG PHE PHE ASN ALA GLU THR GLY ILE SER ARG
HET VKC A1294 8
HETNAM VKC (2-HYDROXYETHOXY)ACETIC ACID
FORMUL 2 VKC C4 H8 O4
FORMUL 3 HOH *220(H2 O)
HELIX 1 1 SER A 12 LEU A 26 1 15
HELIX 2 2 SER A 27 TRP A 29 5 3
HELIX 3 3 SER A 67 TYR A 72 5 6
HELIX 4 4 ASN A 74 TYR A 82 1 9
HELIX 5 5 THR A 104 LEU A 119 1 16
HELIX 6 6 SER A 130 MET A 143 1 14
HELIX 7 7 HIS A 163 LEU A 173 1 11
HELIX 8 8 ASN A 177 MET A 187 1 11
HELIX 9 9 ASP A 189 LEU A 193 5 5
HELIX 10 10 HIS A 194 TRP A 207 1 14
HELIX 11 11 THR A 226 SER A 232 1 7
HELIX 12 12 ASP A 249 VAL A 261 1 13
HELIX 13 13 VAL A 275 GLN A 280 1 6
HELIX 14 14 GLN A 280 ASN A 293 1 14
SHEET 1 AA 2 CYS A 33 THR A 40 0
SHEET 2 AA 2 GLY A 43 SER A 50 -1 O GLY A 43 N THR A 40
SHEET 1 AB 2 ILE A 97 PRO A 98 0
SHEET 2 AB 2 GLY A 43 SER A 50 1 O GLN A 44 N ILE A 97
SHEET 1 AC 8 ILE A 264 ILE A 269 0
SHEET 2 AC 8 ILE A 237 GLY A 242 1 O ILE A 237 N GLU A 265
SHEET 3 AC 8 VAL A 147 LEU A 153 1 O ALA A 150 N LEU A 238
SHEET 4 AC 8 SER A 124 LEU A 129 1 O SER A 124 N LYS A 148
SHEET 5 AC 8 PRO A 57 LEU A 61 1 O PRO A 57 N HIS A 125
SHEET 6 AC 8 ARG A 83 VAL A 87 1 O ARG A 83 N LEU A 58
SHEET 7 AC 8 GLY A 43 SER A 50 -1 O ILE A 48 N ALA A 86
SHEET 8 AC 8 ILE A 97 PRO A 98 1 O ILE A 97 N GLN A 44
SHEET 1 AD 8 ILE A 264 ILE A 269 0
SHEET 2 AD 8 ILE A 237 GLY A 242 1 O ILE A 237 N GLU A 265
SHEET 3 AD 8 VAL A 147 LEU A 153 1 O ALA A 150 N LEU A 238
SHEET 4 AD 8 SER A 124 LEU A 129 1 O SER A 124 N LYS A 148
SHEET 5 AD 8 PRO A 57 LEU A 61 1 O PRO A 57 N HIS A 125
SHEET 6 AD 8 ARG A 83 VAL A 87 1 O ARG A 83 N LEU A 58
SHEET 7 AD 8 GLY A 43 SER A 50 -1 O ILE A 48 N ALA A 86
SHEET 8 AD 8 CYS A 33 THR A 40 -1 O LYS A 34 N ALA A 49
CISPEP 1 PHE A 221 PRO A 222 0 2.93
SITE 1 AC1 6 ALA A 64 LEU A 65 PHE A 166 ALA A 170
SITE 2 AC1 6 PHE A 182 HOH A2220
CRYST1 46.987 46.987 212.461 90.00 90.00 120.00 P 32 2 1 6
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 0.021282 0.012287 0.000000 0.00000
SCALE2 0.000000 0.024575 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004707 0.00000
TER 2291 ASN A 293
MASTER 470 0 1 14 20 0 2 6 2518 1 8 23
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