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HEADER HYDROLASE 24-AUG-19 6KSL
TITLE STAPHYLOCOCCUS AUREUS LIPASE - S116A INACTIVE MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 GENE: LIP, BN1321_80040;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FATTY ACID BINDING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.KITADOKORO,M.TANAKA,S.KAMITANI
REVDAT 1 08-APR-20 6KSL 0
JRNL AUTH K.KITADOKORO,M.TANAKA,T.HIKIMA,Y.OKUNO,M.YAMAMOTO,S.KAMITANI
JRNL TITL CRYSTAL STRUCTURE OF PATHOGENIC STAPHYLOCOCCUS AUREUS LIPASE
JRNL TITL 2 COMPLEX WITH THE ANTI-OBESITY DRUG ORLISTAT.
JRNL REF SCI REP V. 10 5469 2020
JRNL REFN ESSN 2045-2322
JRNL PMID 32214208
JRNL DOI 10.1038/S41598-020-62427-8
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.KITADOKORO,M.TANAKA,T.HIKIMA,Y.OKUNO,M.YAMAMOTO,S.KAMITANI
REMARK 1 TITL CRYSTAL STRUCTURE OF PATHOGENIC STAPHYLOCOCCUS AUREUS LIPASE
REMARK 1 TITL 2 COMPLEX WITH THE ANTI-OBESITY DRUG ORLISTAT.
REMARK 1 REF SCI REP V. 10 5469 2020
REMARK 1 REFN ESSN 2045-2322
REMARK 1 PMID 32214208
REMARK 1 DOI 10.1038/S41598-020-62427-8.
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.KITADOKORO,M.TANAKA,S.KAMITANI
REMARK 1 TITL ANTI-OBESITY DRUG OF HUMAN GASTRIC LIPASE INHIBITS
REMARK 1 TITL 2 PATHOGENIC STAPHYLOCOCCUS AUREUS LIPASE.
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 2.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 58006
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) : 0.250
REMARK 3 R VALUE (WORKING SET) : 0.249
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2901
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) : 2.59
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3902
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.4090
REMARK 3 BIN FREE R VALUE SET COUNT : 206
REMARK 3 BIN FREE R VALUE : 0.3660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6046
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 12
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 65.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.60000
REMARK 3 B22 (A**2) : -0.60000
REMARK 3 B33 (A**2) : 1.94000
REMARK 3 B12 (A**2) : -0.30000
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): 0.294
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.235
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6259 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5603 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8471 ; 2.122 ; 1.936
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13022 ; 3.930 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 762 ; 6.474 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 306 ;35.799 ;24.183
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 994 ;22.649 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;24.951 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 876 ; 0.175 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7052 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1326 ; 0.010 ; 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): 3054 ; 4.314 ; 6.393
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3053 ; 4.312 ; 6.392
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3814 ; 6.200 ; 9.585
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 4 A 385
REMARK 3 ORIGIN FOR THE GROUP (A): -58.002 51.691 -1.969
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: 0.0000
REMARK 3 T33: 0.0000 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
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 401 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): -64.445 63.904 -7.812
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: 0.0000
REMARK 3 T33: 0.0000 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
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 402 A 402
REMARK 3 ORIGIN FOR THE GROUP (A): -61.984 34.139 5.925
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: 0.0000
REMARK 3 T33: 0.0000 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
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 : B 4 B 385
REMARK 3 ORIGIN FOR THE GROUP (A): -25.542 83.759 -11.925
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: 0.0000
REMARK 3 T33: 0.0000 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
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 : B 401 B 401
REMARK 3 ORIGIN FOR THE GROUP (A): -24.197 88.328 2.310
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: 0.0000
REMARK 3 T33: 0.0000 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
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 : B 402 B 402
REMARK 3 ORIGIN FOR THE GROUP (A): -15.816 74.959 -26.640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: 0.0000
REMARK 3 T33: 0.0000 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 501 A 507
REMARK 3 RESIDUE RANGE : B 501 B 505
REMARK 3 ORIGIN FOR THE GROUP (A): -47.343 71.284 -4.324
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: 0.0000
REMARK 3 T33: 0.0000 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 403 A 403
REMARK 3 RESIDUE RANGE : B 403 B 404
REMARK 3 ORIGIN FOR THE GROUP (A): -29.122 66.105 -8.884
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: 0.0000
REMARK 3 T33: 0.0000 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 404 A 404
REMARK 3 RESIDUE RANGE : B 405 B 405
REMARK 3 ORIGIN FOR THE GROUP (A): -45.521 62.935 -8.569
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: 0.0000
REMARK 3 T33: 0.0000 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
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 : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6KSL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-AUG-19.
REMARK 100 THE DEPOSITION ID IS D_1300013569.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 109044
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.590
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 10.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: 6KSI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 76.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M AMMONIUM PHOSPHATE DIBASIC, 0.1M
REMARK 280 TRIS PH8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 77.68433
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 155.36867
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 116.52650
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 194.21083
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 38.84217
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 77.68433
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 155.36867
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 194.21083
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 116.52650
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 38.84217
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 -13
REMARK 465 ASN A -12
REMARK 465 HIS A -11
REMARK 465 LYS A -10
REMARK 465 VAL A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 MET A -2
REMARK 465 LYS A -1
REMARK 465 ALA A 0
REMARK 465 ASN A 1
REMARK 465 GLN A 2
REMARK 465 VAL A 3
REMARK 465 GLY A 386
REMARK 465 LYS A 387
REMARK 465 GLY A 388
REMARK 465 THR A 389
REMARK 465 GLN A 390
REMARK 465 LEU A 391
REMARK 465 LYS A 392
REMARK 465 ALA A 393
REMARK 465 SER A 394
REMARK 465 MET B -13
REMARK 465 ASN B -12
REMARK 465 HIS B -11
REMARK 465 LYS B -10
REMARK 465 VAL B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 MET B -2
REMARK 465 LYS B -1
REMARK 465 ALA B 0
REMARK 465 ASN B 1
REMARK 465 GLN B 2
REMARK 465 VAL B 3
REMARK 465 GLY B 386
REMARK 465 LYS B 387
REMARK 465 GLY B 388
REMARK 465 THR B 389
REMARK 465 GLN B 390
REMARK 465 LEU B 391
REMARK 465 LYS B 392
REMARK 465 ALA B 393
REMARK 465 SER B 394
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 OD1 ASP A 289 NH2 ARG A 293 1.62
REMARK 500 OD2 ASP B 289 NH2 ARG B 293 2.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP A 289 CZ PHE B 360 6555 2.05
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 18 C - N - CA ANGL. DEV. = -17.6 DEGREES
REMARK 500 GLY A 179 C - N - CA ANGL. DEV. = -22.4 DEGREES
REMARK 500 ASP A 203 CB - CG - OD1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 VAL A 268 CB - CA - C ANGL. DEV. = -12.0 DEGREES
REMARK 500 LEU A 275 CB - CG - CD2 ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG A 293 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 LEU B 18 C - N - CA ANGL. DEV. = -18.7 DEGREES
REMARK 500 GLY B 179 C - N - CA ANGL. DEV. = -23.5 DEGREES
REMARK 500 ARG B 193 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ILE B 220 CG1 - CB - CG2 ANGL. DEV. = -13.2 DEGREES
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 LEU A 18 43.89 -108.85
REMARK 500 PHE A 38 99.22 -169.03
REMARK 500 LYS A 39 92.19 -68.64
REMARK 500 ALA A 116 -128.54 52.98
REMARK 500 SER A 269 27.89 -152.28
REMARK 500 LEU A 275 -36.67 -36.07
REMARK 500 PHE A 286 -19.65 -39.54
REMARK 500 VAL A 309 -19.73 -144.36
REMARK 500 ALA A 332 74.27 -112.22
REMARK 500 LEU B 18 40.25 -107.34
REMARK 500 PHE B 38 101.52 -168.39
REMARK 500 LYS B 39 92.48 -68.21
REMARK 500 ALA B 116 -127.50 51.86
REMARK 500 SER B 269 27.37 -153.90
REMARK 500 LEU B 275 -38.27 -33.36
REMARK 500 VAL B 309 -16.78 -145.67
REMARK 500 ALA B 332 75.04 -107.07
REMARK 500 THR B 384 -160.42 -124.03
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 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 64 OD1
REMARK 620 2 ASP A 64 OD2 54.4
REMARK 620 3 HIS A 84 NE2 110.1 155.4
REMARK 620 4 HIS A 90 NE2 132.4 107.6 96.8
REMARK 620 5 ASP A 236 OD2 134.0 97.3 80.6 87.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 283 O
REMARK 620 2 ASP A 348 OD2 89.1
REMARK 620 3 ASP A 351 OD1 151.1 104.5
REMARK 620 4 ASP A 351 OD2 152.5 93.8 53.4
REMARK 620 5 ASP A 356 OD2 78.7 83.9 77.7 128.8
REMARK 620 6 ASP A 359 OD2 79.8 168.9 85.4 96.2 93.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 64 OD1
REMARK 620 2 HIS B 84 NE2 114.4
REMARK 620 3 HIS B 90 NE2 111.1 99.6
REMARK 620 4 ASP B 236 OD2 144.7 92.5 84.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 283 O
REMARK 620 2 ASP B 348 OD2 87.8
REMARK 620 3 ASP B 351 OD1 158.5 100.8
REMARK 620 4 ASP B 351 OD2 148.9 91.0 51.5
REMARK 620 5 ASP B 356 OD2 84.3 83.3 77.3 126.4
REMARK 620 6 ASP B 359 OD2 86.1 173.8 84.5 94.9 94.8
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 ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DAO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BUA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DAO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DAO B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BUA B 405
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 E68Q WAS GENETIC VARIANT.
DBREF1 6KSL A -1 394 UNP A0A0U1MWF9_STAAU
DBREF2 6KSL A A0A0U1MWF9 295 690
DBREF1 6KSL B -1 394 UNP A0A0U1MWF9_STAAU
DBREF2 6KSL B A0A0U1MWF9 295 690
SEQADV 6KSL MET A -13 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL ASN A -12 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL HIS A -11 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL LYS A -10 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL VAL A -9 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL HIS A -8 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL HIS A -7 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL HIS A -6 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL HIS A -5 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL HIS A -4 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL HIS A -3 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL MET A -2 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL GLN A 68 UNP A0A0U1MWF GLU 364 VARIANT
SEQADV 6KSL ALA A 116 UNP A0A0U1MWF SER 412 ENGINEERED MUTATION
SEQADV 6KSL MET B -13 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL ASN B -12 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL HIS B -11 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL LYS B -10 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL VAL B -9 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL HIS B -8 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL HIS B -7 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL HIS B -6 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL HIS B -5 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL HIS B -4 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL HIS B -3 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL MET B -2 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSL GLN B 68 UNP A0A0U1MWF GLU 364 VARIANT
SEQADV 6KSL ALA B 116 UNP A0A0U1MWF SER 412 ENGINEERED MUTATION
SEQRES 1 A 408 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET LYS
SEQRES 2 A 408 ALA ASN GLN VAL GLN PRO LEU ASN LYS TYR PRO VAL VAL
SEQRES 3 A 408 PHE VAL HIS GLY PHE LEU GLY LEU VAL GLY ASP ASN ALA
SEQRES 4 A 408 PRO ALA LEU TYR PRO ASN TYR TRP GLY GLY ASN LYS PHE
SEQRES 5 A 408 LYS VAL ILE GLU GLU LEU ARG LYS GLN GLY TYR ASN VAL
SEQRES 6 A 408 HIS GLN ALA SER VAL SER ALA PHE GLY SER ASN TYR ASP
SEQRES 7 A 408 ARG ALA VAL GLN LEU TYR TYR TYR ILE LYS GLY GLY ARG
SEQRES 8 A 408 VAL ASP TYR GLY ALA ALA HIS ALA ALA LYS TYR GLY HIS
SEQRES 9 A 408 GLU ARG TYR GLY LYS THR TYR LYS GLY ILE MET PRO ASN
SEQRES 10 A 408 TRP GLU PRO GLY LYS LYS VAL HIS LEU VAL GLY HIS ALA
SEQRES 11 A 408 MET GLY GLY GLN THR ILE ARG LEU MET GLU GLU PHE LEU
SEQRES 12 A 408 ARG ASN GLY ASN LYS GLU GLU ILE ALA TYR HIS GLN ALA
SEQRES 13 A 408 HIS GLY GLY GLU ILE SER PRO LEU PHE THR GLY GLY HIS
SEQRES 14 A 408 ASN ASN MET VAL ALA SER ILE THR THR LEU ALA THR PRO
SEQRES 15 A 408 HIS ASN GLY SER GLN ALA ALA ASP LYS PHE GLY ASN THR
SEQRES 16 A 408 GLU ALA VAL ARG LYS ILE MET PHE ALA LEU ASN ARG PHE
SEQRES 17 A 408 MET GLY ASN LYS TYR SER ASN ILE ASP LEU GLY LEU THR
SEQRES 18 A 408 GLN TRP GLY PHE LYS GLN LEU PRO ASN GLU SER TYR ILE
SEQRES 19 A 408 ASP TYR ILE LYS ARG VAL SER LYS SER LYS ILE TRP THR
SEQRES 20 A 408 SER ASP ASP ASN ALA ALA TYR ASP LEU THR LEU ASP GLY
SEQRES 21 A 408 SER ALA LYS LEU ASN ASN MET THR SER MET ASN PRO ASN
SEQRES 22 A 408 ILE THR TYR THR THR TYR THR GLY VAL SER SER HIS THR
SEQRES 23 A 408 GLY PRO LEU GLY TYR GLU ASN PRO ASP LEU GLY THR PHE
SEQRES 24 A 408 PHE LEU MET ASP THR THR SER ARG ILE ILE GLY HIS ASP
SEQRES 25 A 408 ALA ARG GLU GLU TRP ARG LYS ASN ASP GLY VAL VAL PRO
SEQRES 26 A 408 VAL ILE SER SER LEU HIS PRO SER ASN GLN PRO PHE VAL
SEQRES 27 A 408 ASN VAL THR ASN ASN GLU PRO ALA THR ARG ARG GLY ILE
SEQRES 28 A 408 TRP GLN VAL LYS PRO ILE LEU GLN GLY TRP ASP HIS VAL
SEQRES 29 A 408 ASP PHE ILE GLY VAL ASP PHE LEU ASP PHE LYS ARG LYS
SEQRES 30 A 408 GLY SER GLU LEU ALA ASN PHE TYR ILE GLY ILE ILE ASN
SEQRES 31 A 408 ASP LEU LEU SER VAL GLU ALA THR GLU GLY LYS GLY THR
SEQRES 32 A 408 GLN LEU LYS ALA SER
SEQRES 1 B 408 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS MET LYS
SEQRES 2 B 408 ALA ASN GLN VAL GLN PRO LEU ASN LYS TYR PRO VAL VAL
SEQRES 3 B 408 PHE VAL HIS GLY PHE LEU GLY LEU VAL GLY ASP ASN ALA
SEQRES 4 B 408 PRO ALA LEU TYR PRO ASN TYR TRP GLY GLY ASN LYS PHE
SEQRES 5 B 408 LYS VAL ILE GLU GLU LEU ARG LYS GLN GLY TYR ASN VAL
SEQRES 6 B 408 HIS GLN ALA SER VAL SER ALA PHE GLY SER ASN TYR ASP
SEQRES 7 B 408 ARG ALA VAL GLN LEU TYR TYR TYR ILE LYS GLY GLY ARG
SEQRES 8 B 408 VAL ASP TYR GLY ALA ALA HIS ALA ALA LYS TYR GLY HIS
SEQRES 9 B 408 GLU ARG TYR GLY LYS THR TYR LYS GLY ILE MET PRO ASN
SEQRES 10 B 408 TRP GLU PRO GLY LYS LYS VAL HIS LEU VAL GLY HIS ALA
SEQRES 11 B 408 MET GLY GLY GLN THR ILE ARG LEU MET GLU GLU PHE LEU
SEQRES 12 B 408 ARG ASN GLY ASN LYS GLU GLU ILE ALA TYR HIS GLN ALA
SEQRES 13 B 408 HIS GLY GLY GLU ILE SER PRO LEU PHE THR GLY GLY HIS
SEQRES 14 B 408 ASN ASN MET VAL ALA SER ILE THR THR LEU ALA THR PRO
SEQRES 15 B 408 HIS ASN GLY SER GLN ALA ALA ASP LYS PHE GLY ASN THR
SEQRES 16 B 408 GLU ALA VAL ARG LYS ILE MET PHE ALA LEU ASN ARG PHE
SEQRES 17 B 408 MET GLY ASN LYS TYR SER ASN ILE ASP LEU GLY LEU THR
SEQRES 18 B 408 GLN TRP GLY PHE LYS GLN LEU PRO ASN GLU SER TYR ILE
SEQRES 19 B 408 ASP TYR ILE LYS ARG VAL SER LYS SER LYS ILE TRP THR
SEQRES 20 B 408 SER ASP ASP ASN ALA ALA TYR ASP LEU THR LEU ASP GLY
SEQRES 21 B 408 SER ALA LYS LEU ASN ASN MET THR SER MET ASN PRO ASN
SEQRES 22 B 408 ILE THR TYR THR THR TYR THR GLY VAL SER SER HIS THR
SEQRES 23 B 408 GLY PRO LEU GLY TYR GLU ASN PRO ASP LEU GLY THR PHE
SEQRES 24 B 408 PHE LEU MET ASP THR THR SER ARG ILE ILE GLY HIS ASP
SEQRES 25 B 408 ALA ARG GLU GLU TRP ARG LYS ASN ASP GLY VAL VAL PRO
SEQRES 26 B 408 VAL ILE SER SER LEU HIS PRO SER ASN GLN PRO PHE VAL
SEQRES 27 B 408 ASN VAL THR ASN ASN GLU PRO ALA THR ARG ARG GLY ILE
SEQRES 28 B 408 TRP GLN VAL LYS PRO ILE LEU GLN GLY TRP ASP HIS VAL
SEQRES 29 B 408 ASP PHE ILE GLY VAL ASP PHE LEU ASP PHE LYS ARG LYS
SEQRES 30 B 408 GLY SER GLU LEU ALA ASN PHE TYR ILE GLY ILE ILE ASN
SEQRES 31 B 408 ASP LEU LEU SER VAL GLU ALA THR GLU GLY LYS GLY THR
SEQRES 32 B 408 GLN LEU LYS ALA SER
HET ZN A 401 1
HET CA A 402 1
HET DAO A 403 14
HET BUA A 404 6
HET ZN B 401 1
HET CA B 402 1
HET DAO B 403 14
HET DAO B 404 14
HET BUA B 405 6
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM DAO LAURIC ACID
HETNAM BUA BUTANOIC ACID
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 CA 2(CA 2+)
FORMUL 5 DAO 3(C12 H24 O2)
FORMUL 6 BUA 2(C4 H8 O2)
FORMUL 12 HOH *12(H2 O)
HELIX 1 AA1 VAL A 21 ALA A 25 5 5
HELIX 2 AA2 LYS A 39 GLN A 47 1 9
HELIX 3 AA3 SER A 61 GLY A 75 1 15
HELIX 4 AA4 GLY A 81 GLY A 89 1 9
HELIX 5 AA5 ALA A 116 GLY A 132 1 17
HELIX 6 AA6 ASN A 133 GLY A 144 1 12
HELIX 7 AA7 SER A 148 THR A 152 5 5
HELIX 8 AA8 SER A 172 LYS A 177 1 6
HELIX 9 AA9 THR A 181 GLY A 196 1 16
HELIX 10 AB1 LEU A 206 GLY A 210 5 5
HELIX 11 AB2 SER A 218 SER A 227 1 10
HELIX 12 AB3 LYS A 228 THR A 233 5 6
HELIX 13 AB4 ASN A 237 LEU A 242 1 6
HELIX 14 AB5 THR A 243 ASN A 252 1 10
HELIX 15 AB6 PHE A 285 LEU A 287 5 3
HELIX 16 AB7 MET A 288 HIS A 297 1 10
HELIX 17 AB8 ARG A 300 ARG A 304 5 5
HELIX 18 AB9 PRO A 311 LEU A 316 1 6
HELIX 19 AC1 VAL A 350 GLY A 354 5 5
HELIX 20 AC2 LYS A 363 ALA A 383 1 21
HELIX 21 AC3 VAL B 21 ALA B 25 5 5
HELIX 22 AC4 LYS B 39 GLN B 47 1 9
HELIX 23 AC5 SER B 61 GLY B 75 1 15
HELIX 24 AC6 GLY B 81 GLY B 89 1 9
HELIX 25 AC7 ALA B 116 GLY B 132 1 17
HELIX 26 AC8 ASN B 133 GLY B 144 1 12
HELIX 27 AC9 SER B 148 THR B 152 5 5
HELIX 28 AD1 SER B 172 LYS B 177 1 6
HELIX 29 AD2 THR B 181 GLY B 196 1 16
HELIX 30 AD3 LEU B 206 GLY B 210 5 5
HELIX 31 AD4 SER B 218 SER B 227 1 10
HELIX 32 AD5 LYS B 228 THR B 233 5 6
HELIX 33 AD6 ASN B 237 LEU B 242 1 6
HELIX 34 AD7 THR B 243 ASN B 252 1 10
HELIX 35 AD8 PHE B 285 LEU B 287 5 3
HELIX 36 AD9 MET B 288 HIS B 297 1 10
HELIX 37 AE1 ARG B 300 ARG B 304 5 5
HELIX 38 AE2 PRO B 311 LEU B 316 1 6
HELIX 39 AE3 VAL B 350 GLY B 354 5 5
HELIX 40 AE4 LYS B 363 ALA B 383 1 21
SHEET 1 AA1 7 VAL A 51 ALA A 54 0
SHEET 2 AA1 7 VAL A 11 VAL A 14 1 N PHE A 13 O HIS A 52
SHEET 3 AA1 7 VAL A 110 HIS A 115 1 O HIS A 111 N VAL A 12
SHEET 4 AA1 7 VAL A 159 LEU A 165 1 O THR A 163 N LEU A 112
SHEET 5 AA1 7 THR A 261 TYR A 265 1 O TYR A 265 N THR A 164
SHEET 6 AA1 7 TRP A 338 VAL A 340 1 O GLN A 339 N THR A 264
SHEET 7 AA1 7 PHE A 323 ASN A 325 1 N VAL A 324 O TRP A 338
SHEET 1 AA2 2 GLY A 76 ASP A 79 0
SHEET 2 AA2 2 TYR A 93 TYR A 97 -1 O LYS A 95 N VAL A 78
SHEET 1 AA3 2 GLY A 267 VAL A 268 0
SHEET 2 AA3 2 LEU A 344 GLN A 345 1 O LEU A 344 N VAL A 268
SHEET 1 AA4 2 SER A 270 THR A 272 0
SHEET 2 AA4 2 GLU A 278 PRO A 280 -1 O ASN A 279 N HIS A 271
SHEET 1 AA5 7 VAL B 51 ALA B 54 0
SHEET 2 AA5 7 VAL B 11 VAL B 14 1 N PHE B 13 O HIS B 52
SHEET 3 AA5 7 VAL B 110 HIS B 115 1 O HIS B 111 N VAL B 12
SHEET 4 AA5 7 VAL B 159 LEU B 165 1 O THR B 163 N LEU B 112
SHEET 5 AA5 7 THR B 261 TYR B 265 1 O TYR B 265 N THR B 164
SHEET 6 AA5 7 TRP B 338 VAL B 340 1 O GLN B 339 N TYR B 262
SHEET 7 AA5 7 PHE B 323 ASN B 325 1 N VAL B 324 O TRP B 338
SHEET 1 AA6 2 GLY B 76 ASP B 79 0
SHEET 2 AA6 2 TYR B 93 TYR B 97 -1 O LYS B 95 N VAL B 78
SHEET 1 AA7 2 GLY B 267 VAL B 268 0
SHEET 2 AA7 2 LEU B 344 GLN B 345 1 O LEU B 344 N VAL B 268
SHEET 1 AA8 2 SER B 270 THR B 272 0
SHEET 2 AA8 2 GLU B 278 PRO B 280 -1 O ASN B 279 N HIS B 271
LINK OD1 ASP A 64 ZN ZN A 401 1555 1555 1.81
LINK OD2 ASP A 64 ZN ZN A 401 1555 1555 2.58
LINK NE2 HIS A 84 ZN ZN A 401 1555 1555 2.52
LINK NE2 HIS A 90 ZN ZN A 401 1555 1555 1.76
LINK OD2 ASP A 236 ZN ZN A 401 1555 1555 2.10
LINK O GLY A 283 CA CA A 402 1555 1555 2.52
LINK OD2 ASP A 348 CA CA A 402 1555 1555 2.36
LINK OD1 ASP A 351 CA CA A 402 1555 1555 2.52
LINK OD2 ASP A 351 CA CA A 402 1555 1555 2.34
LINK OD2 ASP A 356 CA CA A 402 1555 1555 2.57
LINK OD2 ASP A 359 CA CA A 402 1555 1555 2.68
LINK OD1 ASP B 64 ZN ZN B 401 1555 1555 1.95
LINK NE2 HIS B 84 ZN ZN B 401 1555 1555 2.24
LINK NE2 HIS B 90 ZN ZN B 401 1555 1555 2.03
LINK OD2 ASP B 236 ZN ZN B 401 1555 1555 1.98
LINK O GLY B 283 CA CA B 402 1555 1555 2.29
LINK OD2 ASP B 348 CA CA B 402 1555 1555 2.38
LINK OD1 ASP B 351 CA CA B 402 1555 1555 2.62
LINK OD2 ASP B 351 CA CA B 402 1555 1555 2.46
LINK OD2 ASP B 356 CA CA B 402 1555 1555 2.56
LINK OD2 ASP B 359 CA CA B 402 1555 1555 2.60
SITE 1 AC1 4 ASP A 64 HIS A 84 HIS A 90 ASP A 236
SITE 1 AC2 5 GLY A 283 ASP A 348 ASP A 351 ASP A 356
SITE 2 AC2 5 ASP A 359
SITE 1 AC3 4 PHE A 17 ALA A 116 MET A 117 HIS A 349
SITE 1 AC4 1 LEU A 287
SITE 1 AC5 4 ASP B 64 HIS B 84 HIS B 90 ASP B 236
SITE 1 AC6 5 GLY B 283 ASP B 348 ASP B 351 ASP B 356
SITE 2 AC6 5 ASP B 359
SITE 1 AC7 6 GLY B 16 PHE B 17 ALA B 116 MET B 117
SITE 2 AC7 6 VAL B 309 HIS B 349
SITE 1 AC8 4 TYR A 199 GLN A 213 HOH A 502 THR B 290
SITE 1 AC9 2 TYR B 29 ILE B 353
CRYST1 164.209 164.209 233.053 90.00 90.00 120.00 P 61 2 2 24
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 0.006090 0.003516 0.000000 0.00000
SCALE2 0.000000 0.007032 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004291 0.00000
TER 3024 GLU A 385
TER 6048 GLU B 385
MASTER 683 0 9 40 26 0 12 6 6116 2 82 64
END |