HEADER LYASE 13-APR-15 4ZAF
TITLE STRUCTURE OF UBIX IN COMPLEX WITH OXIDISED FMN AND DIMETHYLALLYL
TITLE 2 MONOPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE AROMATIC ACID DECARBOXYLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: PA4019;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PRENYL TRANSFERASE, FLAVIN BINDING, UBIX, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.WHITE,D.LEYS
REVDAT 3 30-AUG-17 4ZAF 1 LINK
REVDAT 2 01-JUL-15 4ZAF 1 JRNL
REVDAT 1 17-JUN-15 4ZAF 0
JRNL AUTH M.D.WHITE,K.A.PAYNE,K.FISHER,S.A.MARSHALL,D.PARKER,
JRNL AUTH 2 N.J.RATTRAY,D.K.TRIVEDI,R.GOODACRE,S.E.RIGBY,N.S.SCRUTTON,
JRNL AUTH 3 S.HAY,D.LEYS
JRNL TITL UBIX IS A FLAVIN PRENYLTRANSFERASE REQUIRED FOR BACTERIAL
JRNL TITL 2 UBIQUINONE BIOSYNTHESIS.
JRNL REF NATURE V. 522 497 2015
JRNL REFN ESSN 1476-4687
JRNL PMID 26083743
JRNL DOI 10.1038/NATURE14559
REMARK 2
REMARK 2 RESOLUTION. 1.71 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 1.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 24314
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) : 0.139
REMARK 3 R VALUE (WORKING SET) : 0.137
REMARK 3 FREE R VALUE : 0.172
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1295
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.71
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.76
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1773
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.2110
REMARK 3 BIN FREE R VALUE SET COUNT : 88
REMARK 3 BIN FREE R VALUE : 0.2380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1546
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 139
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.078
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.082
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.057
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.770
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1712 ; 0.025 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1652 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2342 ; 2.119 ; 2.001
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3795 ; 0.996 ; 3.006
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 225 ; 6.202 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 67 ;38.353 ;23.881
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 270 ;11.893 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;18.205 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 268 ; 0.285 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1967 ; 0.016 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 375 ; 0.002 ; 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): 871 ; 2.257 ; 2.093
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 872 ; 2.256 ; 2.094
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1094 ; 3.054 ; 3.117
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1095 ; 3.053 ; 3.118
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 841 ; 3.472 ; 2.460
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 836 ; 3.461 ; 2.454
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1242 ; 5.161 ; 3.540
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2075 ; 6.489 ;18.551
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2076 ; 6.488 ;18.559
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 : NULL
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
REMARK 4
REMARK 4 4ZAF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208934.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24314
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.710
REMARK 200 RESOLUTION RANGE LOW (A) : 70.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.02700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.29800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: THIS STRUCTURE WAS SOLVED USING DIFFERENCE FOURIER
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 3350, 150MM SODIUM
REMARK 280 THIOCYANATE, AND 100MM TRIS PH 7.2, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X,Y+1/2,Z+1/2
REMARK 290 14555 -X,-Y+1/2,Z+1/2
REMARK 290 15555 -X,Y+1/2,-Z+1/2
REMARK 290 16555 X,-Y+1/2,-Z+1/2
REMARK 290 17555 Z,X+1/2,Y+1/2
REMARK 290 18555 Z,-X+1/2,-Y+1/2
REMARK 290 19555 -Z,-X+1/2,Y+1/2
REMARK 290 20555 -Z,X+1/2,-Y+1/2
REMARK 290 21555 Y,Z+1/2,X+1/2
REMARK 290 22555 -Y,Z+1/2,-X+1/2
REMARK 290 23555 Y,-Z+1/2,-X+1/2
REMARK 290 24555 -Y,-Z+1/2,X+1/2
REMARK 290 25555 X+1/2,Y,Z+1/2
REMARK 290 26555 -X+1/2,-Y,Z+1/2
REMARK 290 27555 -X+1/2,Y,-Z+1/2
REMARK 290 28555 X+1/2,-Y,-Z+1/2
REMARK 290 29555 Z+1/2,X,Y+1/2
REMARK 290 30555 Z+1/2,-X,-Y+1/2
REMARK 290 31555 -Z+1/2,-X,Y+1/2
REMARK 290 32555 -Z+1/2,X,-Y+1/2
REMARK 290 33555 Y+1/2,Z,X+1/2
REMARK 290 34555 -Y+1/2,Z,-X+1/2
REMARK 290 35555 Y+1/2,-Z,-X+1/2
REMARK 290 36555 -Y+1/2,-Z,X+1/2
REMARK 290 37555 X+1/2,Y+1/2,Z
REMARK 290 38555 -X+1/2,-Y+1/2,Z
REMARK 290 39555 -X+1/2,Y+1/2,-Z
REMARK 290 40555 X+1/2,-Y+1/2,-Z
REMARK 290 41555 Z+1/2,X+1/2,Y
REMARK 290 42555 Z+1/2,-X+1/2,-Y
REMARK 290 43555 -Z+1/2,-X+1/2,Y
REMARK 290 44555 -Z+1/2,X+1/2,-Y
REMARK 290 45555 Y+1/2,Z+1/2,X
REMARK 290 46555 -Y+1/2,Z+1/2,-X
REMARK 290 47555 Y+1/2,-Z+1/2,-X
REMARK 290 48555 -Y+1/2,-Z+1/2,X
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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 70.95000
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 70.95000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 70.95000
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 70.95000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 70.95000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 70.95000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 70.95000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 70.95000
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 70.95000
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 70.95000
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 70.95000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 70.95000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 70.95000
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 70.95000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 70.95000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 70.95000
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 70.95000
REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 70.95000
REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 70.95000
REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 70.95000
REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 70.95000
REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 70.95000
REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 70.95000
REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 70.95000
REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 70.95000
REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 70.95000
REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 70.95000
REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 70.95000
REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 70.95000
REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 70.95000
REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 70.95000
REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 70.95000
REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY1 37 1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY2 37 0.000000 1.000000 0.000000 70.95000
REMARK 290 SMTRY3 37 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 38 -1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY2 38 0.000000 -1.000000 0.000000 70.95000
REMARK 290 SMTRY3 38 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 39 -1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY2 39 0.000000 1.000000 0.000000 70.95000
REMARK 290 SMTRY3 39 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 40 1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY2 40 0.000000 -1.000000 0.000000 70.95000
REMARK 290 SMTRY3 40 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 41 0.000000 0.000000 1.000000 70.95000
REMARK 290 SMTRY2 41 1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY3 41 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 42 0.000000 0.000000 1.000000 70.95000
REMARK 290 SMTRY2 42 -1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY3 42 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 43 0.000000 0.000000 -1.000000 70.95000
REMARK 290 SMTRY2 43 -1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY3 43 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 44 0.000000 0.000000 -1.000000 70.95000
REMARK 290 SMTRY2 44 1.000000 0.000000 0.000000 70.95000
REMARK 290 SMTRY3 44 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 45 0.000000 1.000000 0.000000 70.95000
REMARK 290 SMTRY2 45 0.000000 0.000000 1.000000 70.95000
REMARK 290 SMTRY3 45 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 46 0.000000 -1.000000 0.000000 70.95000
REMARK 290 SMTRY2 46 0.000000 0.000000 1.000000 70.95000
REMARK 290 SMTRY3 46 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 47 0.000000 1.000000 0.000000 70.95000
REMARK 290 SMTRY2 47 0.000000 0.000000 -1.000000 70.95000
REMARK 290 SMTRY3 47 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 48 0.000000 -1.000000 0.000000 70.95000
REMARK 290 SMTRY2 48 0.000000 0.000000 -1.000000 70.95000
REMARK 290 SMTRY3 48 1.000000 0.000000 0.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 71860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 68830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -413.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 6 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 8 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT1 9 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 9 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 9 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 10 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 11 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT3 12 1.000000 0.000000 0.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 501 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 518 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 521 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 532 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A 208
REMARK 465 GLU A 209
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 207 OG
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 NH2 ARG A 185 O HOH A 401 1.62
REMARK 500 OD1 ASP A 125 O HOH A 402 1.71
REMARK 500 OD1 ASN A 117 O HOH A 403 1.96
REMARK 500 NE2 GLN A 81 O HOH A 404 2.13
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 413 O HOH A 466 3555 1.70
REMARK 500 O HOH A 403 O HOH A 474 11555 2.15
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 GLU A 49 CD GLU A 49 OE1 0.069
REMARK 500 LEU A 205 C LEU A 205 O 0.133
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 MET A 61 CG - SD - CE ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG A 122 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 139 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG A 139 NE - CZ - NH2 ANGL. DEV. = -4.6 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 CYS A 116 51.50 38.54
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 K A 307 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 539 O
REMARK 620 2 HOH A 404 O 113.9
REMARK 620 3 HOH A 469 O 140.2 105.8
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4LR A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 307
DBREF 4ZAF A 1 209 UNP Q9HX08 PAAD_PSEAE 1 209
SEQRES 1 A 209 MET SER GLY PRO GLU ARG ILE THR LEU ALA MET THR GLY
SEQRES 2 A 209 ALA SER GLY ALA GLN TYR GLY LEU ARG LEU LEU ASP CYS
SEQRES 3 A 209 LEU VAL GLN GLU GLU ARG GLU VAL HIS PHE LEU ILE SER
SEQRES 4 A 209 LYS ALA ALA GLN LEU VAL MET ALA THR GLU THR ASP VAL
SEQRES 5 A 209 ALA LEU PRO ALA LYS PRO GLN ALA MET GLN ALA PHE LEU
SEQRES 6 A 209 THR GLU TYR CYS GLY ALA ALA ALA GLY GLN ILE ARG VAL
SEQRES 7 A 209 PHE GLY GLN ASN ASP TRP MET ALA PRO PRO ALA SER GLY
SEQRES 8 A 209 SER SER ALA PRO ASN ALA MET VAL ILE CYS PRO CYS SER
SEQRES 9 A 209 THR GLY THR LEU SER ALA VAL ALA THR GLY ALA CYS ASN
SEQRES 10 A 209 ASN LEU ILE GLU ARG ALA ALA ASP VAL ALA LEU LYS GLU
SEQRES 11 A 209 ARG ARG PRO LEU VAL LEU VAL PRO ARG GLU ALA PRO PHE
SEQRES 12 A 209 SER SER ILE HIS LEU GLU ASN MET LEU LYS LEU SER ASN
SEQRES 13 A 209 LEU GLY ALA VAL ILE LEU PRO ALA ALA PRO GLY PHE TYR
SEQRES 14 A 209 HIS GLN PRO GLN SER VAL GLU ASP LEU VAL ASP PHE VAL
SEQRES 15 A 209 VAL ALA ARG ILE LEU ASN THR LEU GLY ILE PRO GLN ASP
SEQRES 16 A 209 MET LEU PRO ARG TRP GLY GLU GLN HIS LEU VAL SER ASP
SEQRES 17 A 209 GLU
HET 4LR A 301 10
HET FMN A 302 31
HET SCN A 303 3
HET SCN A 304 3
HET SCN A 305 3
HET SCN A 306 3
HET K A 307 1
HETNAM 4LR DIMETHYLALLYL MONOPHOSPHATE
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETNAM SCN THIOCYANATE ION
HETNAM K POTASSIUM ION
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 2 4LR C5 H11 O4 P
FORMUL 3 FMN C17 H21 N4 O9 P
FORMUL 4 SCN 4(C N S 1-)
FORMUL 8 K K 1+
FORMUL 9 HOH *139(H2 O)
HELIX 1 AA1 GLY A 16 GLU A 30 1 15
HELIX 2 AA2 SER A 39 THR A 50 1 12
HELIX 3 AA3 LYS A 57 GLY A 70 1 14
HELIX 4 AA4 ALA A 86 SER A 90 5 5
HELIX 5 AA5 SER A 104 GLY A 114 1 11
HELIX 6 AA6 ASN A 118 ARG A 131 1 14
HELIX 7 AA7 SER A 144 LEU A 157 1 14
HELIX 8 AA8 SER A 174 GLY A 191 1 18
SHEET 1 AA1 6 ILE A 76 VAL A 78 0
SHEET 2 AA1 6 GLU A 33 ILE A 38 1 N VAL A 34 O ARG A 77
SHEET 3 AA1 6 ARG A 6 MET A 11 1 N ILE A 7 O HIS A 35
SHEET 4 AA1 6 ALA A 97 CYS A 103 1 O ALA A 97 N THR A 8
SHEET 5 AA1 6 LEU A 134 PRO A 138 1 O VAL A 135 N ILE A 100
SHEET 6 AA1 6 VAL A 160 ILE A 161 1 O VAL A 160 N LEU A 136
LINK K K A 307 O HOH A 539 1555 1555 2.38
LINK K K A 307 O HOH A 404 1555 1555 2.70
LINK S SCN A 303 S SCN A 304 1555 9555 2.04
LINK K K A 307 O HOH A 469 1555 3555 3.48
CISPEP 1 CYS A 101 PRO A 102 0 -4.91
CISPEP 2 ALA A 141 PRO A 142 0 -13.43
SITE 1 AC1 13 TRP A 84 ALA A 89 SER A 90 GLY A 91
SITE 2 AC1 13 ARG A 122 LYS A 129 ARG A 139 GLU A 140
SITE 3 AC1 13 TYR A 169 ARG A 185 TRP A 200 FMN A 302
SITE 4 AC1 13 HOH A 435
SITE 1 AC2 20 THR A 12 GLY A 13 ALA A 14 SER A 15
SITE 2 AC2 20 SER A 39 ALA A 41 TRP A 84 SER A 104
SITE 3 AC2 20 THR A 105 THR A 107 CYS A 116 ARG A 122
SITE 4 AC2 20 ARG A 139 GLU A 140 4LR A 301 HOH A 434
SITE 5 AC2 20 HOH A 450 HOH A 463 HOH A 466 HOH A 469
SITE 1 AC3 1 SCN A 304
SITE 1 AC4 4 ASN A 96 ALA A 97 PRO A 133 SCN A 303
SITE 1 AC5 5 THR A 66 GLU A 67 ALA A 71 GLN A 203
SITE 2 AC5 5 HOH A 485
SITE 1 AC6 3 ARG A 131 HOH A 428 HOH A 530
SITE 1 AC7 3 LYS A 40 HOH A 404 HOH A 539
CRYST1 141.900 141.900 141.900 90.00 90.00 90.00 F 2 3 48
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 0.007047 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007047 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007047 0.00000
(ATOM LINES ARE NOT SHOWN.)
END