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HEADER HYDROLASE 04-AUG-07 2QUA
TITLE CRYSTAL STRUCTURE OF LIPA FROM SERRATIA MARCESCENS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXTRACELLULAR LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SERRATIA MARCESCENS;
SOURCE 3 STRAIN: SM6;
SOURCE 4 GENE: LIPA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS BETA ROLL, ALPHA/BETA HYDROLASE, HELICAL HAIRPIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.MEIER,U.BAUMANN
REVDAT 1 28-AUG-07 2QUA 0
JRNL AUTH R.MEIER,T.DREPPER,V.SVENSSON,K.E.JAEGER,U.BAUMANN
JRNL TITL A CALCIUM-GATED LID AND A LARGE BETA-ROLL SANDWICH
JRNL TITL 2 ARE REVEALED BY THE CRYSTAL STRUCTURE OF
JRNL TITL 3 EXTRACELLULAR LIPASE FROM SERRATIA MARCESCENS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0036
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 51167
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1195
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3081
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2910
REMARK 3 BIN FREE R VALUE SET COUNT : 72
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 4942
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.45000
REMARK 3 B22 (A**2) : -1.45000
REMARK 3 B33 (A**2) : 2.17000
REMARK 3 B12 (A**2) : -0.72000
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): 0.128
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.116
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.499
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4751 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6389 ; 1.227 ; 1.935
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 614 ; 5.483 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 225 ;36.279 ;25.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 687 ;11.963 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;18.478 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 697 ; 0.060 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3694 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2055 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3209 ; 0.318 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 385 ; 0.163 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 35 ; 0.127 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 46 ; 0.245 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.148 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3122 ; 1.842 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4759 ; 2.558 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1854 ; 4.368 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1630 ; 5.933 ; 4.500
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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3377 -2.5135 23.8956
REMARK 3 T TENSOR
REMARK 3 T11: -0.0067 T22: -0.0816
REMARK 3 T33: 0.0477 T12: -0.0282
REMARK 3 T13: 0.1410 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 1.4055 L22: 3.1187
REMARK 3 L33: 1.2502 L12: -0.1628
REMARK 3 L13: -0.7619 L23: -0.1673
REMARK 3 S TENSOR
REMARK 3 S11: -0.0692 S12: -0.1537 S13: -0.3030
REMARK 3 S21: 0.5982 S22: 0.0104 S23: 0.5898
REMARK 3 S31: 0.1134 S32: 0.1050 S33: 0.0588
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 250 A 461
REMARK 3 ORIGIN FOR THE GROUP (A): 27.5487 24.6180 17.1063
REMARK 3 T TENSOR
REMARK 3 T11: -0.0875 T22: -0.1062
REMARK 3 T33: -0.1153 T12: -0.0225
REMARK 3 T13: 0.0787 T23: -0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 0.9499 L22: 3.2415
REMARK 3 L33: 0.5398 L12: -0.2055
REMARK 3 L13: -0.0105 L23: 0.5538
REMARK 3 S TENSOR
REMARK 3 S11: -0.0709 S12: -0.0129 S13: -0.1745
REMARK 3 S21: 0.0504 S22: -0.0443 S23: 0.3547
REMARK 3 S31: -0.0780 S32: 0.0119 S33: 0.1152
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): 25.3400 44.8144 36.3818
REMARK 3 T TENSOR
REMARK 3 T11: 0.0760 T22: -0.0469
REMARK 3 T33: -0.1739 T12: -0.0013
REMARK 3 T13: 0.0188 T23: -0.0532
REMARK 3 L TENSOR
REMARK 3 L11: 3.9273 L22: 2.6051
REMARK 3 L33: 3.5804 L12: -0.3396
REMARK 3 L13: -1.9964 L23: 0.8118
REMARK 3 S TENSOR
REMARK 3 S11: 0.0153 S12: -0.2262 S13: 0.2930
REMARK 3 S21: 0.3345 S22: -0.0229 S23: 0.1000
REMARK 3 S31: -0.1734 S32: -0.0103 S33: 0.0075
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: NULL
REMARK 4
REMARK 4 2QUA COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB044063.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-NOV-2006
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000, 0.780
REMARK 200 MONOCHROMATOR : SI(111) MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51634
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
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 (%) : 94.5
REMARK 200 DATA REDUNDANCY : 4.880
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : 0.09300
REMARK 200 FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.23
REMARK 200 R MERGE FOR SHELL (I) : 0.73000
REMARK 200 R SYM FOR SHELL (I) : 0.73000
REMARK 200 FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% MPD, 0.1 M NA-ACETATE, PH 4.6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 281K, PH 4.60
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 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
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-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 -0.500000 -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 0.00000
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 0.00000
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 0.00000
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 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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: MONOMER
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 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
REMARK 500 O HOH A 772 O HOH A 799 2.03
REMARK 500 OE1 GLN A 420 O HOH A 919 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 7 -123.70 42.88
REMARK 500 SER A 60 -163.71 -161.67
REMARK 500 SER A 144 173.68 118.18
REMARK 500 SER A 207 -119.22 72.70
REMARK 500 SER A 304 142.18 -176.06
REMARK 500 ASN A 345 41.43 -141.10
REMARK 500 ARG A 393 -161.01 57.15
REMARK 500 ASN A 433 -40.55 -140.68
REMARK 500 ASN A 509 -153.12 63.03
REMARK 500 ASN A 583 -130.64 54.44
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 621 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 118 O
REMARK 620 2 GLN A 120 OE1 77.1
REMARK 620 3 SER A 144 O 160.5 84.4
REMARK 620 4 ASP A 153 OD1 91.7 91.1 82.6
REMARK 620 5 ASP A 157 OD1 71.7 146.4 127.6 102.0
REMARK 620 6 ASP A 157 OD2 124.2 158.7 74.5 88.7 53.8
REMARK 620 7 HOH A 662 O 99.5 85.6 85.0 167.4 87.3 90.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 620 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 254 OE1
REMARK 620 2 ASP A 276 OD1 98.2
REMARK 620 3 ASP A 276 OD2 95.2 54.6
REMARK 620 4 ASN A 284 O 85.5 82.7 137.0
REMARK 620 5 ASN A 285 OD1 98.6 154.0 142.5 79.0
REMARK 620 6 HOH A 671 O 95.8 130.6 77.2 145.7 66.9
REMARK 620 7 HOH A 669 O 172.4 74.5 82.0 91.7 87.8 90.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 619 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 375 O
REMARK 620 2 GLY A 377 O 88.6
REMARK 620 3 ASP A 379 OD2 76.6 86.3
REMARK 620 4 GLY A 392 O 79.8 168.3 89.1
REMARK 620 5 ASP A 394 O 88.1 83.0 161.5 98.4
REMARK 620 6 ASP A 397 OD1 155.5 80.9 80.7 109.0 112.2
REMARK 620 7 ASP A 397 OD2 148.3 120.6 114.5 71.1 83.9 52.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 617 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 384 O
REMARK 620 2 GLY A 386 O 95.5
REMARK 620 3 ASP A 388 OD2 83.3 80.8
REMARK 620 4 ASP A 401 OD1 95.1 158.8 82.4
REMARK 620 5 ASP A 401 OD2 87.6 144.8 134.3 54.0
REMARK 620 6 GLY A 403 O 92.1 76.1 155.9 121.7 68.7
REMARK 620 7 ASN A 406 OD1 177.6 86.9 96.8 82.5 90.6 88.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 618 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 393 O
REMARK 620 2 GLY A 395 O 108.8
REMARK 620 3 ASP A 397 OD2 81.0 84.0
REMARK 620 4 GLY A 410 O 84.6 166.1 102.0
REMARK 620 5 LYS A 412 O 94.9 77.3 158.4 98.6
REMARK 620 6 ASN A 415 OD1 167.4 83.8 101.2 82.8 87.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 614 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 491 O
REMARK 620 2 GLY A 493 O 94.2
REMARK 620 3 ASP A 495 OD2 83.1 81.7
REMARK 620 4 GLY A 508 O 91.3 171.6 92.8
REMARK 620 5 ALA A 510 O 81.4 84.1 158.1 102.9
REMARK 620 6 ASP A 513 OD1 168.0 80.8 85.5 92.6 108.6
REMARK 620 7 ASP A 513 OD2 143.5 113.9 122.2 63.9 78.9 47.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 616 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 509 O
REMARK 620 2 GLY A 511 O 108.3
REMARK 620 3 ASP A 513 OD2 81.4 86.3
REMARK 620 4 GLY A 527 O 82.1 169.5 93.9
REMARK 620 5 SER A 529 O 82.2 83.1 156.5 100.4
REMARK 620 6 ASP A 532 OD1 161.5 81.0 83.4 88.6 115.3
REMARK 620 7 ASP A 532 OD2 138.4 106.7 122.9 64.5 80.3 46.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 615 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 528 O
REMARK 620 2 GLY A 530 O 103.6
REMARK 620 3 ASP A 532 OD2 84.7 83.2
REMARK 620 4 PHE A 549 O 90.1 89.6 169.8
REMARK 620 5 ASP A 552 OD1 158.9 97.3 94.9 93.0
REMARK 620 6 HOH A 635 O 79.5 176.6 95.8 91.8 79.5
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QUB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF EXTRACELLULAR LIPASE LIPA FROM
REMARK 900 SERRATIA MARCESCENS. SPACE GROUP H3.
DBREF 2QUA A 1 613 UNP Q59933 Q59933_SERMA 1 613
SEQADV 2QUA SER A -1 UNP Q59933 EXPRESSION TAG
SEQADV 2QUA HIS A 0 UNP Q59933 EXPRESSION TAG
SEQRES 1 A 615 SER HIS MET GLY ILE PHE SER TYR LYS ASP LEU ASP GLU
SEQRES 2 A 615 ASN ALA SER LYS ALA LEU PHE SER ASP ALA LEU ALA ILE
SEQRES 3 A 615 SER THR TYR ALA TYR HIS ASN ILE ASP ASN GLY PHE ASP
SEQRES 4 A 615 GLU GLY TYR HIS GLN THR GLY PHE GLY LEU GLY LEU PRO
SEQRES 5 A 615 LEU THR LEU ILE THR ALA LEU ILE GLY SER THR GLN SER
SEQRES 6 A 615 GLN GLY GLY LEU PRO GLY LEU PRO TRP ASN PRO ASP SER
SEQRES 7 A 615 GLU GLN ALA ALA GLN GLU ALA VAL ASN ASN ALA GLY TRP
SEQRES 8 A 615 SER VAL ILE SER ALA THR GLN LEU GLY TYR ALA GLY LYS
SEQRES 9 A 615 THR ASP ALA ARG GLY THR TYR TYR GLY GLU THR ALA GLY
SEQRES 10 A 615 TYR THR THR ALA GLN ALA GLU VAL LEU GLY LYS TYR ASP
SEQRES 11 A 615 SER GLU GLY ASN LEU THR ALA ILE GLY ILE SER PHE ARG
SEQRES 12 A 615 GLY THR SER GLY PRO ARG GLU SER LEU ILE GLY ASP THR
SEQRES 13 A 615 ILE GLY ASP VAL ILE ASN ASP LEU LEU ALA GLY PHE GLY
SEQRES 14 A 615 PRO LYS GLY TYR ALA ASP GLY TYR THR LEU LYS ALA PHE
SEQRES 15 A 615 GLY ASN LEU LEU GLY ASP VAL ALA LYS PHE ALA GLN ALA
SEQRES 16 A 615 HIS GLY LEU SER GLY GLU ASP VAL VAL VAL SER GLY HIS
SEQRES 17 A 615 SER LEU GLY GLY LEU ALA VAL ASN SER MET ALA ALA GLN
SEQRES 18 A 615 SER ASP ALA ASN TRP GLY GLY PHE TYR ALA GLN SER ASN
SEQRES 19 A 615 TYR VAL ALA PHE ALA SER PRO THR GLN TYR GLU ALA GLY
SEQRES 20 A 615 GLY LYS VAL ILE ASN ILE GLY TYR GLU ASN ASP PRO VAL
SEQRES 21 A 615 PHE ARG ALA LEU ASP GLY THR SER LEU THR LEU PRO SER
SEQRES 22 A 615 LEU GLY VAL HIS ASP ALA PRO HIS THR SER ALA THR ASN
SEQRES 23 A 615 ASN ILE VAL ASN PHE ASN ASP HIS TYR ALA SER ASP ALA
SEQRES 24 A 615 TRP ASN LEU LEU PRO PHE SER ILE LEU ASN ILE PRO THR
SEQRES 25 A 615 TRP LEU SER HIS LEU PRO PHE PHE TYR GLN ASP GLY LEU
SEQRES 26 A 615 MET ARG VAL LEU ASN SER GLU PHE TYR SER LEU THR ASP
SEQRES 27 A 615 LYS ASP SER THR ILE ILE VAL SER ASN LEU SER ASN VAL
SEQRES 28 A 615 THR ARG GLY ASN THR TRP VAL GLU ASP LEU ASN ARG ASN
SEQRES 29 A 615 ALA GLU THR HIS SER GLY PRO THR PHE ILE ILE GLY SER
SEQRES 30 A 615 ASP GLY ASN ASP LEU ILE LYS GLY GLY LYS GLY ASN ASP
SEQRES 31 A 615 TYR LEU GLU GLY ARG ASP GLY ASP ASP ILE PHE ARG ASP
SEQRES 32 A 615 ALA GLY GLY TYR ASN LEU ILE ALA GLY GLY LYS GLY HIS
SEQRES 33 A 615 ASN ILE PHE ASP THR GLN GLN ALA LEU LYS ASN THR GLU
SEQRES 34 A 615 VAL ALA TYR ASP GLY ASN THR LEU TYR LEU ARG ASP ALA
SEQRES 35 A 615 LYS GLY GLY ILE THR LEU ALA ASP ASP ILE SER THR LEU
SEQRES 36 A 615 ARG SER LYS GLU THR SER TRP LEU ILE PHE ASN LYS GLU
SEQRES 37 A 615 VAL ASP HIS GLN VAL THR ALA ALA GLY LEU LYS SER ASP
SEQRES 38 A 615 SER GLY LEU LYS ALA TYR ALA ALA ALA THR GLY GLY ASP
SEQRES 39 A 615 GLY ASP ASP VAL LEU GLN ALA ARG SER HIS ASP ALA TRP
SEQRES 40 A 615 LEU PHE GLY ASN ALA GLY ASN ASP THR LEU ILE GLY HIS
SEQRES 41 A 615 ALA GLY GLY ASN LEU THR PHE VAL GLY GLY SER GLY ASP
SEQRES 42 A 615 ASP ILE LEU LYS GLY VAL GLY ASN GLY ASN THR PHE LEU
SEQRES 43 A 615 PHE SER GLY ASP PHE GLY ARG ASP GLN LEU TYR GLY PHE
SEQRES 44 A 615 ASN ALA SER ASP LYS LEU VAL PHE ILE GLY THR GLU GLY
SEQRES 45 A 615 ALA SER GLY ASN ILE ARG ASP TYR ALA THR GLN GLN ASN
SEQRES 46 A 615 ASP ASP LEU VAL LEU ALA PHE GLY HIS SER GLN VAL THR
SEQRES 47 A 615 LEU ILE GLY VAL SER LEU ASP HIS ILE SER THR ASP GLN
SEQRES 48 A 615 VAL VAL LEU ALA
HET CA A 614 1
HET CA A 615 1
HET CA A 616 1
HET CA A 617 1
HET CA A 618 1
HET CA A 619 1
HET CA A 620 1
HET CA A 621 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 8(CA 2+)
FORMUL 10 HOH *333(H2 O)
HELIX 1 1 ASP A 10 ALA A 28 1 19
HELIX 2 2 ASP A 33 GLY A 44 1 12
HELIX 3 3 GLY A 48 GLY A 59 1 12
HELIX 4 4 ASP A 75 ALA A 87 1 13
HELIX 5 5 SER A 93 GLY A 98 1 6
HELIX 6 6 PRO A 146 GLU A 148 5 3
HELIX 7 7 SER A 149 GLY A 167 1 19
HELIX 8 8 GLY A 170 HIS A 194 1 25
HELIX 9 9 SER A 197 GLU A 199 5 3
HELIX 10 10 SER A 207 SER A 220 1 14
HELIX 11 11 ASN A 223 PHE A 227 5 5
HELIX 12 12 THR A 268 GLY A 273 5 6
HELIX 13 13 ASP A 291 SER A 295 1 5
HELIX 14 14 ALA A 297 LEU A 301 5 5
HELIX 15 15 ASN A 307 HIS A 314 5 8
HELIX 16 16 LEU A 315 ASN A 328 1 14
HELIX 17 17 PHE A 331 THR A 335 5 5
HELIX 18 18 ALA A 422 THR A 426 5 5
HELIX 19 19 ASN A 574 ASP A 577 5 4
HELIX 20 20 SER A 601 ILE A 605 5 5
HELIX 21 21 SER A 606 ASP A 608 5 3
SHEET 1 A 3 SER A 90 VAL A 91 0
SHEET 2 A 3 GLN A 120 TYR A 127 -1 O GLY A 125 N SER A 90
SHEET 3 A 3 TYR A 109 TYR A 110 -1 N TYR A 109 O ALA A 121
SHEET 1 B 6 SER A 90 VAL A 91 0
SHEET 2 B 6 GLN A 120 TYR A 127 -1 O GLY A 125 N SER A 90
SHEET 3 B 6 LEU A 133 PHE A 140 -1 O THR A 134 N LYS A 126
SHEET 4 B 6 VAL A 201 HIS A 206 1 O SER A 204 N ILE A 138
SHEET 5 B 6 ASN A 232 PHE A 236 1 O PHE A 236 N GLY A 205
SHEET 6 B 6 VAL A 248 ILE A 251 1 O ILE A 251 N ALA A 235
SHEET 1 C 8 ILE A 286 ASN A 290 0
SHEET 2 C 8 THR A 340 ASN A 345 1 O ILE A 341 N VAL A 287
SHEET 3 C 8 THR A 370 ILE A 373 1 O PHE A 371 N ILE A 342
SHEET 4 C 8 ASP A 388 GLU A 391 1 O GLU A 391 N ILE A 372
SHEET 5 C 8 ASN A 406 ALA A 409 1 O ALA A 409 N LEU A 390
SHEET 6 C 8 ILE A 444 ASP A 448 1 O LEU A 446 N ILE A 408
SHEET 7 C 8 THR A 434 ARG A 438 -1 N LEU A 437 O THR A 445
SHEET 8 C 8 GLU A 427 TYR A 430 -1 N ALA A 429 O TYR A 436
SHEET 1 D 7 LEU A 380 GLY A 383 0
SHEET 2 D 7 ILE A 398 ASP A 401 1 O ARG A 400 N GLY A 383
SHEET 3 D 7 ILE A 416 ASP A 418 1 O ASP A 418 N PHE A 399
SHEET 4 D 7 THR A 452 GLU A 457 1 O ARG A 454 N PHE A 417
SHEET 5 D 7 LYS A 465 THR A 472 -1 O LYS A 465 N GLU A 457
SHEET 6 D 7 GLY A 475 SER A 478 -1 O LYS A 477 N GLN A 470
SHEET 7 D 7 GLY A 481 LYS A 483 -1 O LYS A 483 N LEU A 476
SHEET 1 E 6 ALA A 487 THR A 489 0
SHEET 2 E 6 TRP A 505 PHE A 507 1 O PHE A 507 N ALA A 488
SHEET 3 E 6 THR A 524 VAL A 526 1 O VAL A 526 N LEU A 506
SHEET 4 E 6 THR A 542 SER A 546 1 O THR A 542 N PHE A 525
SHEET 5 E 6 LYS A 562 ILE A 566 1 O LYS A 562 N PHE A 543
SHEET 6 E 6 VAL A 610 ALA A 613 1 O ALA A 613 N PHE A 565
SHEET 1 F 7 VAL A 496 GLN A 498 0
SHEET 2 F 7 THR A 514 ILE A 516 1 O THR A 514 N LEU A 497
SHEET 3 F 7 ILE A 533 LYS A 535 1 O LYS A 535 N LEU A 515
SHEET 4 F 7 ARG A 551 TYR A 555 1 O GLN A 553 N LEU A 534
SHEET 5 F 7 SER A 593 LEU A 597 1 O THR A 596 N LEU A 554
SHEET 6 F 7 ASP A 585 PHE A 590 -1 N LEU A 586 O LEU A 597
SHEET 7 F 7 ALA A 579 GLN A 582 -1 N GLN A 582 O ASP A 585
LINK O THR A 118 CA CA A 621 1555 1555 2.35
LINK OE1 GLN A 120 CA CA A 621 1555 1555 2.33
LINK O SER A 144 CA CA A 621 1555 1555 2.42
LINK OD1 ASP A 153 CA CA A 621 1555 1555 2.27
LINK OD1 ASP A 157 CA CA A 621 1555 1555 2.46
LINK OD2 ASP A 157 CA CA A 621 1555 1555 2.31
LINK OE1 GLU A 254 CA CA A 620 1555 1555 2.35
LINK OD1 ASP A 276 CA CA A 620 1555 1555 2.43
LINK OD2 ASP A 276 CA CA A 620 1555 1555 2.34
LINK O ASN A 284 CA CA A 620 1555 1555 2.34
LINK OD1 ASN A 285 CA CA A 620 1555 1555 2.34
LINK O SER A 375 CA CA A 619 1555 1555 2.37
LINK O GLY A 377 CA CA A 619 1555 1555 2.35
LINK OD2 ASP A 379 CA CA A 619 1555 1555 2.33
LINK O GLY A 384 CA CA A 617 1555 1555 2.34
LINK O GLY A 386 CA CA A 617 1555 1555 2.38
LINK OD2 ASP A 388 CA CA A 617 1555 1555 2.34
LINK O GLY A 392 CA CA A 619 1555 1555 2.33
LINK O ARG A 393 CA CA A 618 1555 1555 2.36
LINK O ASP A 394 CA CA A 619 1555 1555 2.30
LINK O GLY A 395 CA CA A 618 1555 1555 2.36
LINK OD1 ASP A 397 CA CA A 619 1555 1555 2.35
LINK OD2 ASP A 397 CA CA A 619 1555 1555 2.55
LINK OD2 ASP A 397 CA CA A 618 1555 1555 2.37
LINK OD1 ASP A 401 CA CA A 617 1555 1555 2.39
LINK OD2 ASP A 401 CA CA A 617 1555 1555 2.41
LINK O GLY A 403 CA CA A 617 1555 1555 2.36
LINK OD1 ASN A 406 CA CA A 617 1555 1555 2.35
LINK O GLY A 410 CA CA A 618 1555 1555 2.38
LINK O LYS A 412 CA CA A 618 1555 1555 2.31
LINK OD1 ASN A 415 CA CA A 618 1555 1555 2.41
LINK O GLY A 491 CA CA A 614 1555 1555 2.31
LINK O GLY A 493 CA CA A 614 1555 1555 2.35
LINK OD2 ASP A 495 CA CA A 614 1555 1555 2.31
LINK O GLY A 508 CA CA A 614 1555 1555 2.32
LINK O ASN A 509 CA CA A 616 1555 1555 2.32
LINK O ALA A 510 CA CA A 614 1555 1555 2.28
LINK O GLY A 511 CA CA A 616 1555 1555 2.41
LINK OD1 ASP A 513 CA CA A 614 1555 1555 2.29
LINK OD2 ASP A 513 CA CA A 616 1555 1555 2.30
LINK OD2 ASP A 513 CA CA A 614 1555 1555 2.94
LINK O GLY A 527 CA CA A 616 1555 1555 2.36
LINK O GLY A 528 CA CA A 615 1555 1555 2.35
LINK O SER A 529 CA CA A 616 1555 1555 2.33
LINK O GLY A 530 CA CA A 615 1555 1555 2.36
LINK OD1 ASP A 532 CA CA A 616 1555 1555 2.35
LINK OD2 ASP A 532 CA CA A 615 1555 1555 2.31
LINK OD2 ASP A 532 CA CA A 616 1555 1555 2.95
LINK O PHE A 549 CA CA A 615 1555 1555 2.30
LINK OD1 ASP A 552 CA CA A 615 1555 1555 2.37
LINK CA CA A 615 O HOH A 635 1555 1555 2.33
LINK CA CA A 620 O HOH A 671 1555 1555 2.38
LINK CA CA A 620 O HOH A 669 1555 1555 2.37
LINK CA CA A 621 O HOH A 662 1555 1555 2.34
CRYST1 115.070 115.070 104.434 90.00 90.00 120.00 P 3 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 0.008690 0.005017 0.000000 0.00000
SCALE2 0.000000 0.010035 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009575 0.00000
TER 4602 ALA A 613
MASTER 426 0 8 21 37 0 0 6 4942 1 0 48
END |