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HEADER HYDROLASE/HYDROLASE INHIBITOR 04-SEP-12 4GXN
TITLE DIETHYLPHOSPHONATE INHIBITED STRUCTURE OF THE PROTEUS MIRABILIS LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PROTEUS MIRABILIS;
SOURCE 3 ORGANISM_TAXID: 584;
SOURCE 4 STRAIN: ATCC;
SOURCE 5 GENE: LIPA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21GOLD(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS LIPASE, HYDROLASE, A/B HYDROLASE FOLD, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.P.KORMAN,J.U.BOWIE
REVDAT 1 06-FEB-13 4GXN 0
JRNL AUTH T.P.KORMAN,J.U.BOWIE
JRNL TITL CRYSTAL STRUCTURE OF PROTEUS MIRABILIS LIPASE, A NOVEL
JRNL TITL 2 LIPASE FROM THE PROTEUS/PSYCHROPHILIC SUBFAMILY OF LIPASE
JRNL TITL 3 FAMILY I.1.
JRNL REF PLOS ONE V. 7 52890 2012
JRNL REFN ESSN 1932-6203
JRNL PMID 23300806
JRNL DOI 10.1371/JOURNAL.PONE.0052890
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.5
REMARK 3 NUMBER OF REFLECTIONS : 13875
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 715
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) : 863
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.08
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 53
REMARK 3 BIN FREE R VALUE : 0.3500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2211
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 175
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06000
REMARK 3 B22 (A**2) : -0.06000
REMARK 3 B33 (A**2) : 0.19000
REMARK 3 B12 (A**2) : -0.06000
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): 0.373
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.247
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.175
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.854
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2273 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2144 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3066 ; 0.872 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4914 ; 0.703 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 282 ; 5.101 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 108 ;35.826 ;24.815
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 365 ;12.073 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;15.574 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 337 ; 0.053 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2617 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 542 ; 0.001 ; 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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 10
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 2 A 33
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3650 14.1550 -0.3730
REMARK 3 T TENSOR
REMARK 3 T11: 0.0472 T22: 0.0990
REMARK 3 T33: 0.1889 T12: -0.0435
REMARK 3 T13: -0.0377 T23: -0.0463
REMARK 3 L TENSOR
REMARK 3 L11: 2.8512 L22: 1.3992
REMARK 3 L33: 3.0733 L12: -0.6006
REMARK 3 L13: -1.0058 L23: 0.4167
REMARK 3 S TENSOR
REMARK 3 S11: -0.0511 S12: -0.1358 S13: 0.0032
REMARK 3 S21: -0.0671 S22: -0.1226 S23: 0.4764
REMARK 3 S31: 0.1680 S32: -0.2018 S33: 0.1736
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 34 A 55
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5710 8.2230 -3.4940
REMARK 3 T TENSOR
REMARK 3 T11: 0.1213 T22: 0.0984
REMARK 3 T33: 0.0541 T12: -0.0077
REMARK 3 T13: -0.0055 T23: -0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 4.8764 L22: 3.4195
REMARK 3 L33: 2.2552 L12: -1.4645
REMARK 3 L13: 2.3597 L23: -1.3114
REMARK 3 S TENSOR
REMARK 3 S11: -0.0140 S12: 0.1685 S13: -0.0383
REMARK 3 S21: 0.0568 S22: -0.1670 S23: 0.1004
REMARK 3 S31: 0.0339 S32: -0.0503 S33: 0.1810
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 56 A 114
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5750 10.3980 -7.2780
REMARK 3 T TENSOR
REMARK 3 T11: 0.0986 T22: 0.1058
REMARK 3 T33: 0.0366 T12: -0.0149
REMARK 3 T13: 0.0345 T23: 0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 2.5543 L22: 1.3764
REMARK 3 L33: 2.3853 L12: -0.0810
REMARK 3 L13: 1.9684 L23: 0.4836
REMARK 3 S TENSOR
REMARK 3 S11: -0.0012 S12: 0.1909 S13: 0.0414
REMARK 3 S21: -0.0979 S22: -0.0320 S23: 0.0021
REMARK 3 S31: -0.0227 S32: 0.0114 S33: 0.0331
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 115 A 123
REMARK 3 ORIGIN FOR THE GROUP (A): 25.8950 1.8880 17.6730
REMARK 3 T TENSOR
REMARK 3 T11: 0.2634 T22: 0.1035
REMARK 3 T33: 0.1304 T12: -0.0873
REMARK 3 T13: -0.0251 T23: 0.0912
REMARK 3 L TENSOR
REMARK 3 L11: 12.2233 L22: 19.0885
REMARK 3 L33: 33.0055 L12: -6.8090
REMARK 3 L13: 3.4983 L23: -1.9791
REMARK 3 S TENSOR
REMARK 3 S11: 0.8868 S12: -0.1509 S13: -0.3760
REMARK 3 S21: 0.1461 S22: -0.8485 S23: -0.7340
REMARK 3 S31: 1.4524 S32: -0.3263 S33: -0.0383
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 124 A 154
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6000 7.4200 21.5310
REMARK 3 T TENSOR
REMARK 3 T11: 0.9212 T22: 0.5525
REMARK 3 T33: 0.1227 T12: -0.7009
REMARK 3 T13: -0.1528 T23: 0.1128
REMARK 3 L TENSOR
REMARK 3 L11: 7.0624 L22: 6.5217
REMARK 3 L33: 7.4462 L12: -6.7069
REMARK 3 L13: 3.4005 L23: -3.2019
REMARK 3 S TENSOR
REMARK 3 S11: 0.8078 S12: -0.4254 S13: -0.6170
REMARK 3 S21: -0.4518 S22: 0.1324 S23: 0.5881
REMARK 3 S31: 1.2602 S32: -0.9710 S33: -0.9402
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 155 A 175
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1480 6.3420 -0.4840
REMARK 3 T TENSOR
REMARK 3 T11: 0.1039 T22: 0.0991
REMARK 3 T33: 0.1410 T12: -0.0008
REMARK 3 T13: -0.0025 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 4.1833 L22: 1.9884
REMARK 3 L33: 8.9710 L12: 0.5614
REMARK 3 L13: -2.8831 L23: -1.8988
REMARK 3 S TENSOR
REMARK 3 S11: -0.1259 S12: 0.0056 S13: -0.3030
REMARK 3 S21: -0.0645 S22: -0.0621 S23: -0.2346
REMARK 3 S31: 0.3657 S32: 0.2177 S33: 0.1880
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 176 A 195
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9510 20.6400 -9.0130
REMARK 3 T TENSOR
REMARK 3 T11: 0.1193 T22: 0.1671
REMARK 3 T33: 0.1851 T12: -0.0661
REMARK 3 T13: -0.0083 T23: 0.1127
REMARK 3 L TENSOR
REMARK 3 L11: 4.5658 L22: 7.0889
REMARK 3 L33: 4.2772 L12: 1.7991
REMARK 3 L13: -0.1610 L23: 0.9633
REMARK 3 S TENSOR
REMARK 3 S11: -0.2187 S12: 0.3419 S13: 0.5230
REMARK 3 S21: -0.2290 S22: -0.0249 S23: -0.5026
REMARK 3 S31: -0.3089 S32: 0.4752 S33: 0.2436
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 196 A 223
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9390 23.7230 16.9140
REMARK 3 T TENSOR
REMARK 3 T11: 0.1259 T22: 0.1455
REMARK 3 T33: 0.1016 T12: -0.0425
REMARK 3 T13: 0.0159 T23: -0.1185
REMARK 3 L TENSOR
REMARK 3 L11: 4.3480 L22: 1.9540
REMARK 3 L33: 2.8306 L12: 0.4043
REMARK 3 L13: 0.7903 L23: -0.9284
REMARK 3 S TENSOR
REMARK 3 S11: -0.0222 S12: -0.5571 S13: 0.4801
REMARK 3 S21: 0.2591 S22: -0.2217 S23: 0.1464
REMARK 3 S31: -0.1653 S32: -0.1843 S33: 0.2439
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 224 A 259
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6210 21.8740 7.3680
REMARK 3 T TENSOR
REMARK 3 T11: 0.0904 T22: 0.0709
REMARK 3 T33: 0.0908 T12: -0.0512
REMARK 3 T13: -0.0317 T23: -0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 2.0860 L22: 2.0873
REMARK 3 L33: 2.9014 L12: -0.6256
REMARK 3 L13: 0.5193 L23: 0.3008
REMARK 3 S TENSOR
REMARK 3 S11: -0.1036 S12: -0.0823 S13: 0.2821
REMARK 3 S21: 0.1091 S22: -0.0160 S23: -0.2177
REMARK 3 S31: -0.2268 S32: 0.0751 S33: 0.1196
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 260 A 287
REMARK 3 ORIGIN FOR THE GROUP (A): 6.1550 26.2480 -0.4220
REMARK 3 T TENSOR
REMARK 3 T11: 0.0927 T22: 0.0751
REMARK 3 T33: 0.3033 T12: 0.0103
REMARK 3 T13: -0.0899 T23: -0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 2.6107 L22: 1.5400
REMARK 3 L33: 7.6056 L12: -0.1715
REMARK 3 L13: 0.5339 L23: -0.3415
REMARK 3 S TENSOR
REMARK 3 S11: -0.1428 S12: -0.0474 S13: 0.8004
REMARK 3 S21: -0.1434 S22: -0.0991 S23: 0.2300
REMARK 3 S31: -0.5034 S32: -0.1240 S33: 0.2419
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 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 4GXN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-12.
REMARK 100 THE RCSB ID CODE IS RCSB074761.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
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 FR-E+ DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : VARIMAX CONFOCAL OPTICS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20659
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.12500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.53200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PROPANE PH 6.5, 16% W/V
REMARK 280 PEG 2000 MME, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
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
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 42.31000
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 21.15500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ASP A 149
REMARK 465 PRO A 150
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 LEU A 13 75.41 87.97
REMARK 500 PHE A 47 51.41 -96.28
REMARK 500 SER A 79 -117.14 61.17
REMARK 500 LYS A 208 -114.90 52.02
REMARK 500 ILE A 246 -64.68 -95.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 256 OD1
REMARK 620 2 LEU A 264 O 97.7
REMARK 620 3 ASP A 213 OD2 168.1 93.8
REMARK 620 4 ASN A 210 OD1 86.9 89.7 96.0
REMARK 620 5 GLN A 260 O 88.6 77.1 91.2 165.3
REMARK 620 6 HOH A 411 O 91.8 170.4 76.6 91.4 102.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DEP A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GW3 RELATED DB: PDB
REMARK 900 UNINHIBITED WILD-TYPE PROTEUS MIRABILIS LIPASE
DBREF 4GXN A 1 287 UNP B4EVM3 B4EVM3_PROMH 1 287
SEQADV 4GXN MET A -19 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN GLY A -18 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN SER A -17 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN SER A -16 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN HIS A -15 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN HIS A -14 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN HIS A -13 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN HIS A -12 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN HIS A -11 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN HIS A -10 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN SER A -9 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN SER A -8 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN GLY A -7 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN LEU A -6 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN VAL A -5 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN PRO A -4 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN ARG A -3 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN GLY A -2 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN SER A -1 UNP B4EVM3 EXPRESSION TAG
SEQADV 4GXN HIS A 0 UNP B4EVM3 EXPRESSION TAG
SEQRES 1 A 307 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 307 LEU VAL PRO ARG GLY SER HIS MET SER THR LYS TYR PRO
SEQRES 3 A 307 ILE VAL LEU VAL HIS GLY LEU ALA GLY PHE ASN GLU ILE
SEQRES 4 A 307 VAL GLY PHE PRO TYR PHE TYR GLY ILE ALA ASP ALA LEU
SEQRES 5 A 307 ARG GLN ASP GLY HIS GLN VAL PHE THR ALA SER LEU SER
SEQRES 6 A 307 ALA PHE ASN SER ASN GLU VAL ARG GLY LYS GLN LEU TRP
SEQRES 7 A 307 GLN PHE VAL GLN THR LEU LEU GLN GLU THR GLN ALA LYS
SEQRES 8 A 307 LYS VAL ASN PHE ILE GLY HIS SER GLN GLY PRO LEU ALA
SEQRES 9 A 307 CYS ARG TYR VAL ALA ALA ASN TYR PRO ASP SER VAL ALA
SEQRES 10 A 307 SER VAL THR SER ILE ASN GLY VAL ASN HIS GLY SER GLU
SEQRES 11 A 307 ILE ALA ASP LEU TYR ARG ARG ILE MET ARG LYS ASP SER
SEQRES 12 A 307 ILE PRO GLU TYR ILE VAL GLU LYS VAL LEU ASN ALA PHE
SEQRES 13 A 307 GLY THR ILE ILE SER THR PHE SER GLY HIS ARG GLY ASP
SEQRES 14 A 307 PRO GLN ASP ALA ILE ALA ALA LEU GLU SER LEU THR THR
SEQRES 15 A 307 GLU GLN VAL THR GLU PHE ASN ASN LYS TYR PRO GLN ALA
SEQRES 16 A 307 LEU PRO LYS THR PRO GLY GLY GLU GLY ASP GLU ILE VAL
SEQRES 17 A 307 ASN GLY VAL HIS TYR TYR CYS PHE GLY SER TYR ILE GLN
SEQRES 18 A 307 GLY LEU ILE ALA GLY GLU LYS GLY ASN LEU LEU ASP PRO
SEQRES 19 A 307 THR HIS ALA ALA MET ARG VAL LEU ASN THR PHE PHE THR
SEQRES 20 A 307 GLU LYS GLN ASN ASP GLY LEU VAL GLY ARG SER SER MET
SEQRES 21 A 307 ARG LEU GLY LYS LEU ILE LYS ASP ASP TYR ALA GLN ASP
SEQRES 22 A 307 HIS ILE ASP MET VAL ASN GLN VAL ALA GLY LEU VAL GLY
SEQRES 23 A 307 TYR ASN GLU ASP ILE VAL ALA ILE TYR THR GLN HIS ALA
SEQRES 24 A 307 LYS TYR LEU ALA SER LYS GLN LEU
HET CA A 301 1
HET DEP A 302 8
HET PGE A 303 10
HETNAM CA CALCIUM ION
HETNAM DEP DIETHYL PHOSPHONATE
HETNAM PGE TRIETHYLENE GLYCOL
FORMUL 2 CA CA 2+
FORMUL 3 DEP C4 H11 O3 P
FORMUL 4 PGE C6 H14 O4
FORMUL 5 HOH *175(H2 O)
HELIX 1 1 GLY A 15 GLY A 21 1 7
HELIX 2 2 GLY A 27 ASP A 35 1 9
HELIX 3 3 SER A 49 GLN A 69 1 21
HELIX 4 4 GLN A 80 TYR A 92 1 13
HELIX 5 5 SER A 109 ARG A 120 1 12
HELIX 6 6 PRO A 125 GLY A 145 1 21
HELIX 7 7 ALA A 153 GLU A 158 1 6
HELIX 8 8 THR A 161 TYR A 172 1 12
HELIX 9 9 LEU A 203 LEU A 212 5 10
HELIX 10 10 ASP A 213 THR A 224 1 12
HELIX 11 11 GLY A 236 ARG A 241 5 6
HELIX 12 12 ILE A 255 ASN A 259 5 5
HELIX 13 13 ASP A 270 LYS A 285 1 16
SHEET 1 A 6 VAL A 39 LEU A 44 0
SHEET 2 A 6 ILE A 7 GLY A 12 1 N LEU A 9 O ALA A 42
SHEET 3 A 6 VAL A 73 SER A 79 1 O ASN A 74 N VAL A 8
SHEET 4 A 6 VAL A 96 GLY A 104 1 O SER A 98 N PHE A 75
SHEET 5 A 6 VAL A 191 SER A 198 1 O TYR A 194 N SER A 101
SHEET 6 A 6 ILE A 187 VAL A 188 -1 N VAL A 188 O VAL A 191
SHEET 1 B 6 VAL A 39 LEU A 44 0
SHEET 2 B 6 ILE A 7 GLY A 12 1 N LEU A 9 O ALA A 42
SHEET 3 B 6 VAL A 73 SER A 79 1 O ASN A 74 N VAL A 8
SHEET 4 B 6 VAL A 96 GLY A 104 1 O SER A 98 N PHE A 75
SHEET 5 B 6 VAL A 191 SER A 198 1 O TYR A 194 N SER A 101
SHEET 6 B 6 LYS A 244 TYR A 250 1 O ILE A 246 N CYS A 195
LINK OD1 ASP A 256 CA CA A 301 1555 1555 2.31
LINK O LEU A 264 CA CA A 301 1555 1555 2.31
LINK OD2 ASP A 213 CA CA A 301 1555 1555 2.32
LINK OD1 ASN A 210 CA CA A 301 1555 1555 2.33
LINK O GLN A 260 CA CA A 301 1555 1555 2.33
LINK OG SER A 79 P DEP A 302 1555 1555 1.61
LINK CA CA A 301 O HOH A 411 1555 1555 2.40
CISPEP 1 GLN A 260 VAL A 261 0 2.18
SITE 1 AC1 7 ASN A 210 ASP A 213 ASP A 256 GLN A 260
SITE 2 AC1 7 VAL A 261 LEU A 264 HOH A 411
SITE 1 AC2 6 TYR A 24 SER A 79 GLN A 80 LEU A 160
SITE 2 AC2 6 HIS A 254 HOH A 553
SITE 1 AC3 5 ILE A 19 PHE A 47 GLU A 67 HOH A 462
SITE 2 AC3 5 HOH A 520
CRYST1 65.574 65.574 63.465 90.00 90.00 120.00 P 32 3
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 0.015250 0.008805 0.000000 0.00000
SCALE2 0.000000 0.017609 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015757 0.00000
TER 2212 LEU A 287
MASTER 490 0 3 13 12 0 6 6 2405 1 27 24
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