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HEADER HYDROLASE 24-AUG-19 6KSI
TITLE STAPHYLOCOCCUS AUREUS LIPASE - NATIVE
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
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 6KSI 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 2
REMARK 2 RESOLUTION. 2.08 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) : 2.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 128855
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) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6444
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) : 2.08
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.14
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8840
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.75
REMARK 3 BIN R VALUE (WORKING SET) : 0.4120
REMARK 3 BIN FREE R VALUE SET COUNT : 466
REMARK 3 BIN FREE R VALUE : 0.4210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6048
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 126
REMARK 3 SOLVENT ATOMS : 76
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.84000
REMARK 3 B22 (A**2) : 0.84000
REMARK 3 B33 (A**2) : -1.67000
REMARK 3 B12 (A**2) : 0.00000
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): 0.124
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.120
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 : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6322 ; 0.029 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5702 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8534 ; 2.896 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13262 ; 4.054 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 762 ; 7.036 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 306 ;35.647 ;24.183
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 996 ;19.718 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;21.158 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 876 ; 0.323 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7080 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1326 ; 0.018 ; 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): 3058 ; 3.481 ; 4.520
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3053 ; 3.447 ; 4.514
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3816 ; 4.450 ; 6.742
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 : 11
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): 16.617 26.320 -11.849
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 : B 4 B 385
REMARK 3 ORIGIN FOR THE GROUP (A): 63.660 35.892 -24.215
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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 401 A 401
REMARK 3 RESIDUE RANGE : B 401 B 401
REMARK 3 ORIGIN FOR THE GROUP (A): 36.704 34.388 -28.265
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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 402 A 402
REMARK 3 RESIDUE RANGE : B 402 B 402
REMARK 3 ORIGIN FOR THE GROUP (A): 43.250 28.273 -8.441
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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 403 A 403
REMARK 3 RESIDUE RANGE : B 403 B 403
REMARK 3 ORIGIN FOR THE GROUP (A): 37.225 35.424 -16.631
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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 404 A 405
REMARK 3 RESIDUE RANGE : B 404 B 404
REMARK 3 ORIGIN FOR THE GROUP (A): 31.090 38.233 -34.263
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 559
REMARK 3 RESIDUE RANGE : B 501 B 517
REMARK 3 ORIGIN FOR THE GROUP (A): 24.683 31.896 -13.307
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 406 A 406
REMARK 3 RESIDUE RANGE : B 405 B 405
REMARK 3 ORIGIN FOR THE GROUP (A): 41.668 27.201 -20.461
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 407 A 407
REMARK 3 RESIDUE RANGE : B 406 B 406
REMARK 3 ORIGIN FOR THE GROUP (A): 36.687 34.750 -28.421
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 : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 408 A 408
REMARK 3 ORIGIN FOR THE GROUP (A): 35.000 40.464 -14.743
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 : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 409 A 409
REMARK 3 RESIDUE RANGE : B 407 B 407
REMARK 3 ORIGIN FOR THE GROUP (A): 40.277 31.120 -16.874
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 6KSI 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_1300013566.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
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 : 246153
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
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: 2HIH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 80.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M SODIUM FORMATE, 0.1M SODIUM
REMARK 280 ACETATE, PH 4.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 125.61200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 62.80600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 188.41800
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 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 125.61200
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 188.41800
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 62.80600
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 OD2 ASP A 236 ZN ZN A 401 1.47
REMARK 500 OD2 ASP B 236 ZN ZN B 401 1.56
REMARK 500 OD1 ASP A 64 ZN ZN A 401 1.63
REMARK 500 O PHE B 17 CA LEU B 18 1.70
REMARK 500 O PHE B 178 CA GLY B 179 1.74
REMARK 500 O PHE A 17 CA LEU A 18 1.75
REMARK 500 O ALA A 174 O PHE A 178 2.02
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 O HOH A 537 O HOH A 537 7554 1.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 PHE A 17 C PHE A 17 O 0.160
REMARK 500 LEU A 18 N LEU A 18 CA 0.345
REMARK 500 TYR A 32 CB TYR A 32 CG 0.098
REMARK 500 SER A 55 CA SER A 55 CB 0.104
REMARK 500 TYR A 63 CG TYR A 63 CD1 0.106
REMARK 500 ARG A 65 CZ ARG A 65 NH1 0.083
REMARK 500 TYR A 72 CG TYR A 72 CD1 0.111
REMARK 500 TYR A 80 CE1 TYR A 80 CZ 0.098
REMARK 500 GLU A 127 CG GLU A 127 CD 0.093
REMARK 500 ASP A 236 CG ASP A 236 OD2 0.211
REMARK 500 ARG A 300 CD ARG A 300 NE 0.110
REMARK 500 LEU B 18 N LEU B 18 CA 0.302
REMARK 500 GLU B 127 CD GLU B 127 OE1 0.066
REMARK 500 TYR B 139 CE1 TYR B 139 CZ 0.106
REMARK 500 HIS B 143 CG HIS B 143 CD2 0.059
REMARK 500 GLY B 179 N GLY B 179 CA 0.118
REMARK 500 ARG B 225 CD ARG B 225 NE -0.129
REMARK 500 ASN B 328 CG ASN B 328 ND2 0.204
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. = -38.3 DEGREES
REMARK 500 LEU A 18 CA - CB - CG ANGL. DEV. = 22.6 DEGREES
REMARK 500 ASP A 23 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 GLN A 53 N - CA - CB ANGL. DEV. = -10.8 DEGREES
REMARK 500 ASP A 64 CB - CG - OD1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 ASP A 64 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 77 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 VAL A 113 CG1 - CB - CG2 ANGL. DEV. = 11.3 DEGREES
REMARK 500 LEU A 124 CB - CG - CD2 ANGL. DEV. = 12.7 DEGREES
REMARK 500 MET A 125 CG - SD - CE ANGL. DEV. = 11.0 DEGREES
REMARK 500 GLU A 127 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 VAL A 159 CG1 - CB - CG2 ANGL. DEV. = 11.7 DEGREES
REMARK 500 VAL A 184 CG1 - CB - CG2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG A 185 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 LYS A 212 CD - CE - NZ ANGL. DEV. = 16.1 DEGREES
REMARK 500 VAL A 226 CG1 - CB - CG2 ANGL. DEV. = 15.3 DEGREES
REMARK 500 ASP A 236 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP A 236 CB - CG - OD2 ANGL. DEV. = 11.9 DEGREES
REMARK 500 LEU A 244 CB - CG - CD2 ANGL. DEV. = 12.0 DEGREES
REMARK 500 VAL A 268 CB - CA - C ANGL. DEV. = -15.6 DEGREES
REMARK 500 LEU A 282 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500 ARG A 293 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 LYS A 305 CD - CE - NZ ANGL. DEV. = 18.3 DEGREES
REMARK 500 VAL A 310 CA - CB - CG1 ANGL. DEV. = 9.4 DEGREES
REMARK 500 ILE A 313 CG1 - CB - CG2 ANGL. DEV. = 19.0 DEGREES
REMARK 500 ILE A 313 CB - CG1 - CD1 ANGL. DEV. = 22.9 DEGREES
REMARK 500 LEU A 316 CB - CG - CD2 ANGL. DEV. = 13.6 DEGREES
REMARK 500 VAL A 326 CG1 - CB - CG2 ANGL. DEV. = 15.1 DEGREES
REMARK 500 ARG A 335 CD - NE - CZ ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG A 335 NE - CZ - NH1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG A 335 NE - CZ - NH2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 VAL A 340 CG1 - CB - CG2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 ASP A 356 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP A 356 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 LEU A 358 CB - CG - CD1 ANGL. DEV. = 11.0 DEGREES
REMARK 500 PHE B 17 O - C - N ANGL. DEV. = -11.6 DEGREES
REMARK 500 LEU B 18 C - N - CA ANGL. DEV. = -36.1 DEGREES
REMARK 500 LEU B 18 CA - CB - CG ANGL. DEV. = 19.4 DEGREES
REMARK 500 ARG B 77 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG B 130 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 130 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 LYS B 134 CA - CB - CG ANGL. DEV. = 13.6 DEGREES
REMARK 500 ASP B 176 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 PHE B 178 O - C - N ANGL. DEV. = -13.7 DEGREES
REMARK 500 GLY B 179 C - N - CA ANGL. DEV. = -31.9 DEGREES
REMARK 500 VAL B 184 CG1 - CB - CG2 ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG B 185 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 MET B 188 CG - SD - CE ANGL. DEV. = 10.5 DEGREES
REMARK 500 LEU B 191 CB - CG - CD2 ANGL. DEV. = 12.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 68 ANGLE DEVIATIONS.
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 TYR A 29 142.30 -177.86
REMARK 500 SER A 116 -126.82 48.96
REMARK 500 THR A 181 153.96 -48.84
REMARK 500 SER A 269 25.90 -151.19
REMARK 500 VAL A 309 -13.30 -142.69
REMARK 500 ALA A 332 68.02 -106.54
REMARK 500 TYR B 29 141.28 -173.86
REMARK 500 SER B 116 -122.41 57.66
REMARK 500 SER B 269 23.20 -147.18
REMARK 500 VAL B 309 -13.58 -145.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 18 GLY A 19 -147.11
REMARK 500 GLN B 4 PRO B 5 146.48
REMARK 500 LEU B 18 GLY B 19 -145.95
REMARK 500 GLY B 179 ASN B 180 144.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG B 225 0.07 SIDE CHAIN
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 HIS A 84 NE2
REMARK 620 2 HIS A 90 NE2 106.5
REMARK 620 N 1
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 90.2
REMARK 620 3 ASP A 351 OD1 161.5 99.5
REMARK 620 4 ASP A 351 OD2 149.2 89.0 47.6
REMARK 620 5 ASP A 356 OD2 85.3 82.3 80.5 125.0
REMARK 620 6 ASP A 359 OD2 80.4 168.7 91.2 95.8 103.0
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 111.9
REMARK 620 3 HIS B 90 NE2 113.1 109.6
REMARK 620 N 1 2
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 85.8
REMARK 620 3 ASP B 351 OD1 158.2 102.4
REMARK 620 4 ASP B 351 OD2 151.3 87.4 50.3
REMARK 620 5 ASP B 356 OD2 77.4 80.0 84.1 128.6
REMARK 620 6 ASP B 359 OD2 84.0 169.1 88.5 99.8 101.4
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 6NA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DAO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DAO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LEA A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OCA A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BUA A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NA B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DAO B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LEA B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OCA B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BUA B 407
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 E68Q WAS GENETIC VARIANT.
DBREF1 6KSI A -1 394 UNP A0A0U1MWF9_STAAU
DBREF2 6KSI A A0A0U1MWF9 295 690
DBREF1 6KSI B -1 394 UNP A0A0U1MWF9_STAAU
DBREF2 6KSI B A0A0U1MWF9 295 690
SEQADV 6KSI MET A -13 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI ASN A -12 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI HIS A -11 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI LYS A -10 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI VAL A -9 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI HIS A -8 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI HIS A -7 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI HIS A -6 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI HIS A -5 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI HIS A -4 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI HIS A -3 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI MET A -2 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI GLN A 68 UNP A0A0U1MWF GLU 364 VARIANT
SEQADV 6KSI MET B -13 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI ASN B -12 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI HIS B -11 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI LYS B -10 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI VAL B -9 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI HIS B -8 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI HIS B -7 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI HIS B -6 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI HIS B -5 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI HIS B -4 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI HIS B -3 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI MET B -2 UNP A0A0U1MWF EXPRESSION TAG
SEQADV 6KSI GLN B 68 UNP A0A0U1MWF GLU 364 VARIANT
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 SER
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 SER
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 6NA A 403 8
HET DAO A 404 14
HET DAO A 405 14
HET LEA A 406 7
HET OCA A 407 10
HET PLM A 408 18
HET BUA A 409 6
HET ZN B 401 1
HET CA B 402 1
HET 6NA B 403 8
HET DAO B 404 14
HET LEA B 405 7
HET OCA B 406 10
HET BUA B 407 6
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM 6NA HEXANOIC ACID
HETNAM DAO LAURIC ACID
HETNAM LEA PENTANOIC ACID
HETNAM OCA OCTANOIC ACID (CAPRYLIC ACID)
HETNAM PLM PALMITIC ACID
HETNAM BUA BUTANOIC ACID
HETSYN LEA VALERIC ACID
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 CA 2(CA 2+)
FORMUL 5 6NA 2(C6 H12 O2)
FORMUL 6 DAO 3(C12 H24 O2)
FORMUL 8 LEA 2(C5 H10 O2)
FORMUL 9 OCA 2(C8 H16 O2)
FORMUL 10 PLM C16 H32 O2
FORMUL 11 BUA 2(C4 H8 O2)
FORMUL 19 HOH *76(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 SER 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 MET A 195 1 15
HELIX 10 AB1 LEU A 206 GLY A 210 5 5
HELIX 11 AB2 SER A 218 LYS A 228 1 11
HELIX 12 AB3 SER A 229 THR A 233 5 5
HELIX 13 AB4 ASN A 237 LEU A 242 1 6
HELIX 14 AB5 THR A 243 THR A 254 1 12
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 THR A 384 1 22
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 SER B 116 GLY B 132 1 17
HELIX 26 AC8 ASN B 133 GLY B 144 1 12
HELIX 27 AC9 SER B 172 LYS B 177 1 6
HELIX 28 AD1 THR B 181 GLY B 196 1 16
HELIX 29 AD2 LEU B 206 GLY B 210 5 5
HELIX 30 AD3 SER B 218 SER B 227 1 10
HELIX 31 AD4 LYS B 228 SER B 234 5 7
HELIX 32 AD5 ASN B 237 LEU B 242 1 6
HELIX 33 AD6 THR B 243 MET B 253 1 11
HELIX 34 AD7 PHE B 285 LEU B 287 5 3
HELIX 35 AD8 MET B 288 HIS B 297 1 10
HELIX 36 AD9 ARG B 300 ARG B 304 5 5
HELIX 37 AE1 PRO B 311 LEU B 316 1 6
HELIX 38 AE2 VAL B 350 GLY B 354 5 5
HELIX 39 AE3 LYS B 363 THR B 384 1 22
SHEET 1 AA1 7 VAL A 51 GLN A 53 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 VAL A 113 N VAL A 14
SHEET 4 AA1 7 VAL A 159 LEU A 165 1 O THR A 163 N GLY A 114
SHEET 5 AA1 7 THR A 261 TYR A 265 1 O THR A 261 N ILE A 162
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 VAL A 340
SHEET 1 AA2 2 GLY A 76 ASP A 79 0
SHEET 2 AA2 2 TYR A 93 TYR A 97 -1 O TYR A 97 N GLY A 76
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 GLN B 53 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 VAL B 113 N VAL B 14
SHEET 4 AA5 7 VAL B 159 LEU B 165 1 O LEU B 165 N GLY B 114
SHEET 5 AA5 7 THR B 261 TYR B 265 1 O THR B 261 N ILE B 162
SHEET 6 AA5 7 TRP B 338 VAL B 340 1 O GLN B 339 N THR B 264
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 TYR B 97 N GLY B 76
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 NE2 HIS A 84 ZN ZN A 401 1555 1555 2.01
LINK NE2 HIS A 90 ZN ZN A 401 1555 1555 2.19
LINK O GLY A 283 CA CA A 402 1555 1555 2.30
LINK OD2 ASP A 348 CA CA A 402 1555 1555 2.32
LINK OD1 ASP A 351 CA CA A 402 1555 1555 2.81
LINK OD2 ASP A 351 CA CA A 402 1555 1555 2.55
LINK OD2 ASP A 356 CA CA A 402 1555 1555 2.59
LINK OD2 ASP A 359 CA CA A 402 1555 1555 2.31
LINK OD1 ASP B 64 ZN ZN B 401 1555 1555 1.97
LINK NE2 HIS B 84 ZN ZN B 401 1555 1555 2.04
LINK NE2 HIS B 90 ZN ZN B 401 1555 1555 2.17
LINK O GLY B 283 CA CA B 402 1555 1555 2.49
LINK OD2 ASP B 348 CA CA B 402 1555 1555 2.50
LINK OD1 ASP B 351 CA CA B 402 1555 1555 2.74
LINK OD2 ASP B 351 CA CA B 402 1555 1555 2.50
LINK OD2 ASP B 356 CA CA B 402 1555 1555 2.58
LINK OD2 ASP B 359 CA CA B 402 1555 1555 2.52
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 1 BUA A 409
SITE 1 AC4 5 ARG A 193 TYR A 219 ILE B 187 PHE B 194
SITE 2 AC4 5 DAO B 404
SITE 1 AC5 4 GLN A 213 SER A 218 TYR A 219 THR B 290
SITE 1 AC6 5 LEU A 18 TYR A 29 TYR A 32 HIS A 115
SITE 2 AC6 5 BUA A 409
SITE 1 AC7 3 LEU A 18 TYR A 29 PHE A 59
SITE 1 AC8 8 LEU A 287 THR A 290 ASN B 197 LYS B 198
SITE 2 AC8 8 TYR B 199 GLN B 213 SER B 218 TYR B 219
SITE 1 AC9 2 6NA A 403 LEA A 406
SITE 1 AD1 4 ASP B 64 HIS B 84 HIS B 90 ASP B 236
SITE 1 AD2 5 GLY B 283 ASP B 348 ASP B 351 ASP B 356
SITE 2 AD2 5 ASP B 359
SITE 1 AD3 1 BUA B 407
SITE 1 AD4 4 ILE A 187 DAO A 404 ARG B 193 TYR B 219
SITE 1 AD5 2 ALA B 175 PHE B 178
SITE 1 AD6 3 LEU B 18 TYR B 29 PHE B 59
SITE 1 AD7 1 6NA B 403
CRYST1 129.913 129.913 251.224 90.00 90.00 90.00 P 41 2 2 16
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 0.007697 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007697 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003981 0.00000
TER 3025 GLU A 385
TER 6050 GLU B 385
MASTER 823 0 16 39 26 0 21 6 6250 2 145 64
END |