HEADER LIPID DEGRADATION 24-AUG-96 1DJX
TITLE PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED
TITLE 2 WITH INOSITOL-1,4,5-TRISPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PLC-D1;
COMPND 5 EC: 3.1.4.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: CATALYTICALLY-ACTIVE DELETION VARIANT THAT LACKS AN N-
COMPND 9 TERMINAL PH DOMAIN, COMPLEXED WITH INOSITOL-1,4,5-TRISPHOSPHATE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: CDNA FRAGMENT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX (PHARMACIA);
SOURCE 9 EXPRESSION_SYSTEM_GENE: CDNA FRAGMENT
KEYWDS PHOSPHORIC DIESTER HYDROLASE, HYDROLASE, LIPID DEGRADATION,
KEYWDS 2 TRANSDUCER, CALCIUM-BINDING, PHOSPHOLIPASE C, PHOSPHOINOSITIDE-
KEYWDS 3 SPECIFIC
EXPDTA X-RAY DIFFRACTION
AUTHOR L.-O.ESSEN,O.PERISIC,R.L.WILLIAMS
REVDAT 3 07-FEB-24 1DJX 1 REMARK LINK
REVDAT 2 24-FEB-09 1DJX 1 VERSN
REVDAT 1 07-JUL-97 1DJX 0
JRNL AUTH L.O.ESSEN,O.PERISIC,M.KATAN,Y.WU,M.F.ROBERTS,R.L.WILLIAMS
JRNL TITL STRUCTURAL MAPPING OF THE CATALYTIC MECHANISM FOR A
JRNL TITL 2 MAMMALIAN PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C.
JRNL REF BIOCHEMISTRY V. 36 1704 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9048554
JRNL DOI 10.1021/BI962512P
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.O.ESSEN,O.PERISIC,R.CHEUNG,M.KATAN,R.L.WILLIAMS
REMARK 1 TITL CRYSTAL STRUCTURE OF A MAMMALIAN PHOSPHOINOSITIDE-SPECIFIC
REMARK 1 TITL 2 PHOSPHOLIPASE C DELTA
REMARK 1 REF NATURE V. 380 595 1996
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT 5E
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 111796
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : SHELLS
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4609
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2200
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 4.00
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 4609
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 111796
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8535
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 779
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.014 ; 1.000 ; 8784
REMARK 3 BOND ANGLES (DEGREES) : 1.305 ; 1.200 ; 11845
REMARK 3 TORSION ANGLES (DEGREES) : 18.470; 0.000 ; 5195
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.013 ; 1.000 ; 231
REMARK 3 GENERAL PLANES (A) : 0.013 ; 5.000 ; 1265
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : 2.412 ; 5.000 ; 8736
REMARK 3 NON-BONDED CONTACTS (A) : 0.029 ; 20.000; 250
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DJX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172817.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-95
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.89
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 113379
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: DATA COLLECTED AT 100 K FROM SINGLE FROZEN CRYSTAL.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 41 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y+1/2,Z+1/2
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y,-Z+1/2
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X,-Y+1/2
REMARK 290 7555 -Z,-X+1/2,Y+1/2
REMARK 290 8555 -Z+1/2,X+1/2,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y+1/2,Z+1/2,-X
REMARK 290 11555 Y+1/2,-Z,-X+1/2
REMARK 290 12555 -Y,-Z+1/2,X+1/2
REMARK 290 13555 Y+3/4,X+1/4,-Z+3/4
REMARK 290 14555 -Y+1/4,-X+1/4,-Z+1/4
REMARK 290 15555 Y+1/4,-X+3/4,Z+3/4
REMARK 290 16555 -Y+3/4,X+3/4,Z+1/4
REMARK 290 17555 X+3/4,Z+1/4,-Y+3/4
REMARK 290 18555 -X+3/4,Z+3/4,Y+1/4
REMARK 290 19555 -X+1/4,-Z+1/4,-Y+1/4
REMARK 290 20555 X+1/4,-Z+3/4,Y+3/4
REMARK 290 21555 Z+3/4,Y+1/4,-X+3/4
REMARK 290 22555 Z+1/4,-Y+3/4,X+3/4
REMARK 290 23555 -Z+3/4,Y+3/4,X+1/4
REMARK 290 24555 -Z+1/4,-Y+1/4,-X+1/4
REMARK 290 25555 X,Y+1/2,Z+1/2
REMARK 290 26555 -X,-Y,Z
REMARK 290 27555 -X+1/2,Y,-Z+1/2
REMARK 290 28555 X+1/2,-Y+1/2,-Z
REMARK 290 29555 Z,X+1/2,Y+1/2
REMARK 290 30555 Z+1/2,-X+1/2,-Y
REMARK 290 31555 -Z,-X,Y
REMARK 290 32555 -Z+1/2,X,-Y+1/2
REMARK 290 33555 Y,Z+1/2,X+1/2
REMARK 290 34555 -Y+1/2,Z,-X+1/2
REMARK 290 35555 Y+1/2,-Z+1/2,-X
REMARK 290 36555 -Y,-Z,X
REMARK 290 37555 Y+3/4,X+3/4,-Z+1/4
REMARK 290 38555 -Y+1/4,-X+3/4,-Z+3/4
REMARK 290 39555 Y+1/4,-X+1/4,Z+1/4
REMARK 290 40555 -Y+3/4,X+1/4,Z+3/4
REMARK 290 41555 X+3/4,Z+3/4,-Y+1/4
REMARK 290 42555 -X+3/4,Z+1/4,Y+3/4
REMARK 290 43555 -X+1/4,-Z+3/4,-Y+3/4
REMARK 290 44555 X+1/4,-Z+1/4,Y+1/4
REMARK 290 45555 Z+3/4,Y+3/4,-X+1/4
REMARK 290 46555 Z+1/4,-Y+1/4,X+1/4
REMARK 290 47555 -Z+3/4,Y+1/4,X+3/4
REMARK 290 48555 -Z+1/4,-Y+3/4,-X+3/4
REMARK 290 49555 X+1/2,Y,Z+1/2
REMARK 290 50555 -X+1/2,-Y+1/2,Z
REMARK 290 51555 -X,Y+1/2,-Z+1/2
REMARK 290 52555 X,-Y,-Z
REMARK 290 53555 Z+1/2,X,Y+1/2
REMARK 290 54555 Z,-X,-Y
REMARK 290 55555 -Z+1/2,-X+1/2,Y
REMARK 290 56555 -Z,X+1/2,-Y+1/2
REMARK 290 57555 Y+1/2,Z,X+1/2
REMARK 290 58555 -Y,Z+1/2,-X+1/2
REMARK 290 59555 Y,-Z,-X
REMARK 290 60555 -Y+1/2,-Z+1/2,X
REMARK 290 61555 Y+1/4,X+1/4,-Z+1/4
REMARK 290 62555 -Y+3/4,-X+1/4,-Z+3/4
REMARK 290 63555 Y+3/4,-X+3/4,Z+1/4
REMARK 290 64555 -Y+1/4,X+3/4,Z+3/4
REMARK 290 65555 X+1/4,Z+1/4,-Y+1/4
REMARK 290 66555 -X+1/4,Z+3/4,Y+3/4
REMARK 290 67555 -X+3/4,-Z+1/4,-Y+3/4
REMARK 290 68555 X+3/4,-Z+3/4,Y+1/4
REMARK 290 69555 Z+1/4,Y+1/4,-X+1/4
REMARK 290 70555 Z+3/4,-Y+3/4,X+1/4
REMARK 290 71555 -Z+1/4,Y+3/4,X+3/4
REMARK 290 72555 -Z+3/4,-Y+1/4,-X+3/4
REMARK 290 73555 X+1/2,Y+1/2,Z
REMARK 290 74555 -X+1/2,-Y,Z+1/2
REMARK 290 75555 -X,Y,-Z
REMARK 290 76555 X,-Y+1/2,-Z+1/2
REMARK 290 77555 Z+1/2,X+1/2,Y
REMARK 290 78555 Z,-X+1/2,-Y+1/2
REMARK 290 79555 -Z+1/2,-X,Y+1/2
REMARK 290 80555 -Z,X,-Y
REMARK 290 81555 Y+1/2,Z+1/2,X
REMARK 290 82555 -Y,Z,-X
REMARK 290 83555 Y,-Z+1/2,-X+1/2
REMARK 290 84555 -Y+1/2,-Z,X+1/2
REMARK 290 85555 Y+1/4,X+3/4,-Z+3/4
REMARK 290 86555 -Y+3/4,-X+3/4,-Z+1/4
REMARK 290 87555 Y+3/4,-X+1/4,Z+3/4
REMARK 290 88555 -Y+1/4,X+1/4,Z+1/4
REMARK 290 89555 X+1/4,Z+3/4,-Y+3/4
REMARK 290 90555 -X+1/4,Z+1/4,Y+1/4
REMARK 290 91555 -X+3/4,-Z+3/4,-Y+1/4
REMARK 290 92555 X+3/4,-Z+1/4,Y+3/4
REMARK 290 93555 Z+1/4,Y+3/4,-X+3/4
REMARK 290 94555 Z+3/4,-Y+1/4,X+3/4
REMARK 290 95555 -Z+1/4,Y+1/4,X+1/4
REMARK 290 96555 -Z+3/4,-Y+3/4,-X+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 198.77000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 198.77000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 198.77000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 198.77000
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 198.77000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 198.77000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 198.77000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 198.77000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 198.77000
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 198.77000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 198.77000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 198.77000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 198.77000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 298.15500
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 298.15500
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 99.38500
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 99.38500
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 99.38500
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 298.15500
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 298.15500
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 99.38500
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 99.38500
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 298.15500
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 298.15500
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 99.38500
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 99.38500
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 99.38500
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 298.15500
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 298.15500
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 298.15500
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 99.38500
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 99.38500
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 298.15500
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 298.15500
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 298.15500
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 99.38500
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 99.38500
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 198.77000
REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 198.77000
REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 198.77000
REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 198.77000
REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 198.77000
REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 198.77000
REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 198.77000
REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 198.77000
REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 198.77000
REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 198.77000
REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 198.77000
REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 198.77000
REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 37 0.000000 1.000000 0.000000 298.15500
REMARK 290 SMTRY2 37 1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY3 37 0.000000 0.000000 -1.000000 99.38500
REMARK 290 SMTRY1 38 0.000000 -1.000000 0.000000 99.38500
REMARK 290 SMTRY2 38 -1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY3 38 0.000000 0.000000 -1.000000 298.15500
REMARK 290 SMTRY1 39 0.000000 1.000000 0.000000 99.38500
REMARK 290 SMTRY2 39 -1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY3 39 0.000000 0.000000 1.000000 99.38500
REMARK 290 SMTRY1 40 0.000000 -1.000000 0.000000 298.15500
REMARK 290 SMTRY2 40 1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY3 40 0.000000 0.000000 1.000000 298.15500
REMARK 290 SMTRY1 41 1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY2 41 0.000000 0.000000 1.000000 298.15500
REMARK 290 SMTRY3 41 0.000000 -1.000000 0.000000 99.38500
REMARK 290 SMTRY1 42 -1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY2 42 0.000000 0.000000 1.000000 99.38500
REMARK 290 SMTRY3 42 0.000000 1.000000 0.000000 298.15500
REMARK 290 SMTRY1 43 -1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY2 43 0.000000 0.000000 -1.000000 298.15500
REMARK 290 SMTRY3 43 0.000000 -1.000000 0.000000 298.15500
REMARK 290 SMTRY1 44 1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY2 44 0.000000 0.000000 -1.000000 99.38500
REMARK 290 SMTRY3 44 0.000000 1.000000 0.000000 99.38500
REMARK 290 SMTRY1 45 0.000000 0.000000 1.000000 298.15500
REMARK 290 SMTRY2 45 0.000000 1.000000 0.000000 298.15500
REMARK 290 SMTRY3 45 -1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY1 46 0.000000 0.000000 1.000000 99.38500
REMARK 290 SMTRY2 46 0.000000 -1.000000 0.000000 99.38500
REMARK 290 SMTRY3 46 1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY1 47 0.000000 0.000000 -1.000000 298.15500
REMARK 290 SMTRY2 47 0.000000 1.000000 0.000000 99.38500
REMARK 290 SMTRY3 47 1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY1 48 0.000000 0.000000 -1.000000 99.38500
REMARK 290 SMTRY2 48 0.000000 -1.000000 0.000000 298.15500
REMARK 290 SMTRY3 48 -1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY1 49 1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY2 49 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 49 0.000000 0.000000 1.000000 198.77000
REMARK 290 SMTRY1 50 -1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY2 50 0.000000 -1.000000 0.000000 198.77000
REMARK 290 SMTRY3 50 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 51 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 51 0.000000 1.000000 0.000000 198.77000
REMARK 290 SMTRY3 51 0.000000 0.000000 -1.000000 198.77000
REMARK 290 SMTRY1 52 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 52 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 52 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 53 0.000000 0.000000 1.000000 198.77000
REMARK 290 SMTRY2 53 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 53 0.000000 1.000000 0.000000 198.77000
REMARK 290 SMTRY1 54 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 54 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 54 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 55 0.000000 0.000000 -1.000000 198.77000
REMARK 290 SMTRY2 55 -1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY3 55 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 56 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 56 1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY3 56 0.000000 -1.000000 0.000000 198.77000
REMARK 290 SMTRY1 57 0.000000 1.000000 0.000000 198.77000
REMARK 290 SMTRY2 57 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 57 1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY1 58 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 58 0.000000 0.000000 1.000000 198.77000
REMARK 290 SMTRY3 58 -1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY1 59 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 59 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 59 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 60 0.000000 -1.000000 0.000000 198.77000
REMARK 290 SMTRY2 60 0.000000 0.000000 -1.000000 198.77000
REMARK 290 SMTRY3 60 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 61 0.000000 1.000000 0.000000 99.38500
REMARK 290 SMTRY2 61 1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY3 61 0.000000 0.000000 -1.000000 99.38500
REMARK 290 SMTRY1 62 0.000000 -1.000000 0.000000 298.15500
REMARK 290 SMTRY2 62 -1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY3 62 0.000000 0.000000 -1.000000 298.15500
REMARK 290 SMTRY1 63 0.000000 1.000000 0.000000 298.15500
REMARK 290 SMTRY2 63 -1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY3 63 0.000000 0.000000 1.000000 99.38500
REMARK 290 SMTRY1 64 0.000000 -1.000000 0.000000 99.38500
REMARK 290 SMTRY2 64 1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY3 64 0.000000 0.000000 1.000000 298.15500
REMARK 290 SMTRY1 65 1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY2 65 0.000000 0.000000 1.000000 99.38500
REMARK 290 SMTRY3 65 0.000000 -1.000000 0.000000 99.38500
REMARK 290 SMTRY1 66 -1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY2 66 0.000000 0.000000 1.000000 298.15500
REMARK 290 SMTRY3 66 0.000000 1.000000 0.000000 298.15500
REMARK 290 SMTRY1 67 -1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY2 67 0.000000 0.000000 -1.000000 99.38500
REMARK 290 SMTRY3 67 0.000000 -1.000000 0.000000 298.15500
REMARK 290 SMTRY1 68 1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY2 68 0.000000 0.000000 -1.000000 298.15500
REMARK 290 SMTRY3 68 0.000000 1.000000 0.000000 99.38500
REMARK 290 SMTRY1 69 0.000000 0.000000 1.000000 99.38500
REMARK 290 SMTRY2 69 0.000000 1.000000 0.000000 99.38500
REMARK 290 SMTRY3 69 -1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY1 70 0.000000 0.000000 1.000000 298.15500
REMARK 290 SMTRY2 70 0.000000 -1.000000 0.000000 298.15500
REMARK 290 SMTRY3 70 1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY1 71 0.000000 0.000000 -1.000000 99.38500
REMARK 290 SMTRY2 71 0.000000 1.000000 0.000000 298.15500
REMARK 290 SMTRY3 71 1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY1 72 0.000000 0.000000 -1.000000 298.15500
REMARK 290 SMTRY2 72 0.000000 -1.000000 0.000000 99.38500
REMARK 290 SMTRY3 72 -1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY1 73 1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY2 73 0.000000 1.000000 0.000000 198.77000
REMARK 290 SMTRY3 73 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 74 -1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY2 74 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 74 0.000000 0.000000 1.000000 198.77000
REMARK 290 SMTRY1 75 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 75 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 75 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 76 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 76 0.000000 -1.000000 0.000000 198.77000
REMARK 290 SMTRY3 76 0.000000 0.000000 -1.000000 198.77000
REMARK 290 SMTRY1 77 0.000000 0.000000 1.000000 198.77000
REMARK 290 SMTRY2 77 1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY3 77 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 78 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 78 -1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY3 78 0.000000 -1.000000 0.000000 198.77000
REMARK 290 SMTRY1 79 0.000000 0.000000 -1.000000 198.77000
REMARK 290 SMTRY2 79 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 79 0.000000 1.000000 0.000000 198.77000
REMARK 290 SMTRY1 80 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 80 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 80 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 81 0.000000 1.000000 0.000000 198.77000
REMARK 290 SMTRY2 81 0.000000 0.000000 1.000000 198.77000
REMARK 290 SMTRY3 81 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 82 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 82 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 82 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 83 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 83 0.000000 0.000000 -1.000000 198.77000
REMARK 290 SMTRY3 83 -1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY1 84 0.000000 -1.000000 0.000000 198.77000
REMARK 290 SMTRY2 84 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 84 1.000000 0.000000 0.000000 198.77000
REMARK 290 SMTRY1 85 0.000000 1.000000 0.000000 99.38500
REMARK 290 SMTRY2 85 1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY3 85 0.000000 0.000000 -1.000000 298.15500
REMARK 290 SMTRY1 86 0.000000 -1.000000 0.000000 298.15500
REMARK 290 SMTRY2 86 -1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY3 86 0.000000 0.000000 -1.000000 99.38500
REMARK 290 SMTRY1 87 0.000000 1.000000 0.000000 298.15500
REMARK 290 SMTRY2 87 -1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY3 87 0.000000 0.000000 1.000000 298.15500
REMARK 290 SMTRY1 88 0.000000 -1.000000 0.000000 99.38500
REMARK 290 SMTRY2 88 1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY3 88 0.000000 0.000000 1.000000 99.38500
REMARK 290 SMTRY1 89 1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY2 89 0.000000 0.000000 1.000000 298.15500
REMARK 290 SMTRY3 89 0.000000 -1.000000 0.000000 298.15500
REMARK 290 SMTRY1 90 -1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY2 90 0.000000 0.000000 1.000000 99.38500
REMARK 290 SMTRY3 90 0.000000 1.000000 0.000000 99.38500
REMARK 290 SMTRY1 91 -1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY2 91 0.000000 0.000000 -1.000000 298.15500
REMARK 290 SMTRY3 91 0.000000 -1.000000 0.000000 99.38500
REMARK 290 SMTRY1 92 1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY2 92 0.000000 0.000000 -1.000000 99.38500
REMARK 290 SMTRY3 92 0.000000 1.000000 0.000000 298.15500
REMARK 290 SMTRY1 93 0.000000 0.000000 1.000000 99.38500
REMARK 290 SMTRY2 93 0.000000 1.000000 0.000000 298.15500
REMARK 290 SMTRY3 93 -1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY1 94 0.000000 0.000000 1.000000 298.15500
REMARK 290 SMTRY2 94 0.000000 -1.000000 0.000000 99.38500
REMARK 290 SMTRY3 94 1.000000 0.000000 0.000000 298.15500
REMARK 290 SMTRY1 95 0.000000 0.000000 -1.000000 99.38500
REMARK 290 SMTRY2 95 0.000000 1.000000 0.000000 99.38500
REMARK 290 SMTRY3 95 1.000000 0.000000 0.000000 99.38500
REMARK 290 SMTRY1 96 0.000000 0.000000 -1.000000 298.15500
REMARK 290 SMTRY2 96 0.000000 -1.000000 0.000000 298.15500
REMARK 290 SMTRY3 96 -1.000000 0.000000 0.000000 99.38500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLY A 133
REMARK 465 SER A 134
REMARK 465 MET A 135
REMARK 465 ASP A 136
REMARK 465 GLN A 137
REMARK 465 ARG A 138
REMARK 465 GLN A 139
REMARK 465 LYS A 140
REMARK 465 LEU A 141
REMARK 465 GLN A 142
REMARK 465 HIS A 143
REMARK 465 TRP A 144
REMARK 465 ILE A 145
REMARK 465 HIS A 146
REMARK 465 SER A 147
REMARK 465 CYS A 148
REMARK 465 LEU A 149
REMARK 465 ARG A 150
REMARK 465 LYS A 151
REMARK 465 ALA A 152
REMARK 465 ASP A 153
REMARK 465 LYS A 154
REMARK 465 ASN A 155
REMARK 465 LYS A 156
REMARK 465 ASP A 157
REMARK 465 ASN A 158
REMARK 465 LYS A 159
REMARK 465 MET A 160
REMARK 465 ASN A 161
REMARK 465 PHE A 162
REMARK 465 LYS A 163
REMARK 465 GLU A 164
REMARK 465 LEU A 165
REMARK 465 LYS A 166
REMARK 465 ASP A 167
REMARK 465 PHE A 168
REMARK 465 LEU A 169
REMARK 465 LYS A 170
REMARK 465 GLU A 171
REMARK 465 LEU A 172
REMARK 465 ASN A 173
REMARK 465 ILE A 174
REMARK 465 GLN A 175
REMARK 465 VAL A 176
REMARK 465 ASP A 177
REMARK 465 ASP A 178
REMARK 465 GLY A 179
REMARK 465 TYR A 180
REMARK 465 ALA A 181
REMARK 465 ARG A 182
REMARK 465 LYS A 183
REMARK 465 ILE A 184
REMARK 465 PHE A 185
REMARK 465 ARG A 186
REMARK 465 GLU A 187
REMARK 465 CYS A 188
REMARK 465 ASP A 189
REMARK 465 HIS A 190
REMARK 465 SER A 191
REMARK 465 GLN A 192
REMARK 465 THR A 193
REMARK 465 ASP A 194
REMARK 465 SER A 195
REMARK 465 LEU A 196
REMARK 465 GLU A 197
REMARK 465 ASP A 198
REMARK 465 GLU A 199
REMARK 465 GLY A 443
REMARK 465 GLY A 444
REMARK 465 LEU A 445
REMARK 465 LEU A 446
REMARK 465 PRO A 447
REMARK 465 ALA A 448
REMARK 465 GLY A 449
REMARK 465 GLY A 450
REMARK 465 GLU A 451
REMARK 465 ASN A 452
REMARK 465 GLY A 453
REMARK 465 SER A 454
REMARK 465 GLU A 455
REMARK 465 ALA A 456
REMARK 465 THR A 457
REMARK 465 ASP A 458
REMARK 465 VAL A 459
REMARK 465 SER A 460
REMARK 465 ASP A 461
REMARK 465 GLU A 462
REMARK 465 VAL A 463
REMARK 465 GLU A 464
REMARK 465 ALA A 465
REMARK 465 ALA A 466
REMARK 465 GLU A 467
REMARK 465 MET A 468
REMARK 465 GLU A 469
REMARK 465 ASP A 470
REMARK 465 GLU A 471
REMARK 465 ALA A 472
REMARK 465 VAL A 473
REMARK 465 ARG A 474
REMARK 465 SER A 475
REMARK 465 GLN A 476
REMARK 465 VAL A 477
REMARK 465 GLN A 478
REMARK 465 HIS A 479
REMARK 465 LYS A 480
REMARK 465 PRO A 481
REMARK 465 LYS A 482
REMARK 465 GLU A 483
REMARK 465 ASP A 484
REMARK 465 LYS A 485
REMARK 465 LEU A 486
REMARK 465 GLY B 133
REMARK 465 SER B 134
REMARK 465 MET B 135
REMARK 465 ASP B 136
REMARK 465 GLN B 137
REMARK 465 ARG B 138
REMARK 465 GLN B 139
REMARK 465 LYS B 140
REMARK 465 LEU B 141
REMARK 465 GLN B 142
REMARK 465 HIS B 143
REMARK 465 TRP B 144
REMARK 465 ILE B 145
REMARK 465 HIS B 146
REMARK 465 SER B 147
REMARK 465 CYS B 148
REMARK 465 LEU B 149
REMARK 465 ARG B 150
REMARK 465 LYS B 151
REMARK 465 ALA B 152
REMARK 465 ASP B 153
REMARK 465 LYS B 154
REMARK 465 ASN B 155
REMARK 465 LYS B 156
REMARK 465 ASP B 157
REMARK 465 LEU B 446
REMARK 465 PRO B 447
REMARK 465 ALA B 448
REMARK 465 GLY B 449
REMARK 465 GLY B 450
REMARK 465 GLU B 451
REMARK 465 ASN B 452
REMARK 465 GLY B 453
REMARK 465 SER B 454
REMARK 465 GLU B 455
REMARK 465 ALA B 456
REMARK 465 THR B 457
REMARK 465 ASP B 458
REMARK 465 VAL B 459
REMARK 465 SER B 460
REMARK 465 ASP B 461
REMARK 465 GLU B 462
REMARK 465 VAL B 463
REMARK 465 GLU B 464
REMARK 465 ALA B 465
REMARK 465 ALA B 466
REMARK 465 GLU B 467
REMARK 465 MET B 468
REMARK 465 GLU B 469
REMARK 465 ASP B 470
REMARK 465 GLU B 471
REMARK 465 ALA B 472
REMARK 465 VAL B 473
REMARK 465 ARG B 474
REMARK 465 SER B 475
REMARK 465 GLN B 476
REMARK 465 VAL B 477
REMARK 465 GLN B 478
REMARK 465 HIS B 479
REMARK 465 LYS B 480
REMARK 465 PRO B 481
REMARK 465 LYS B 482
REMARK 465 GLU B 483
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 SER A 509
REMARK 475 PRO A 510
REMARK 475 GLY A 511
REMARK 475 THR A 512
REMARK 475 SER A 513
REMARK 475 GLY A 514
REMARK 475 SER B 509
REMARK 475 PRO B 510
REMARK 475 GLY B 511
REMARK 475 THR B 512
REMARK 475 SER B 513
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 200 CG CD OE1 OE2
REMARK 480 GLU A 202 CB CG CD OE1 OE2
REMARK 480 TYR A 205 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 480 LYS A 206 CB CG CD CE NZ
REMARK 480 MET A 207 CB CG SD CE
REMARK 480 LEU A 208 CG CD1 CD2
REMARK 480 GLU A 226 CG CD OE1 OE2
REMARK 480 LYS A 487 CD CE NZ
REMARK 480 ARG A 627 CG CD NE CZ NH1 NH2
REMARK 480 ASN A 647 CG OD1 ND2
REMARK 480 LYS A 648 CG CD CE NZ
REMARK 480 ASN A 649 CB CG OD1 ND2
REMARK 480 ILE A 651 CD1
REMARK 480 ASN B 158 CG OD1 ND2
REMARK 480 LYS B 159 CB CG CD CE NZ
REMARK 480 MET B 160 CG SD CE
REMARK 480 ASN B 161 CG OD1 ND2
REMARK 480 LYS B 163 CG CD CE NZ
REMARK 480 LYS B 166 CG CD CE NZ
REMARK 480 PHE B 168 CD1 CD2 CE1 CE2 CZ
REMARK 480 LYS B 170 CG CD CE NZ
REMARK 480 GLU B 171 CG CD OE1 OE2
REMARK 480 ASN B 173 OD1 ND2
REMARK 480 LYS B 206 CG CD CE NZ
REMARK 480 LYS B 485 CG CD CE NZ
REMARK 480 LYS B 487 CG CD CE NZ
REMARK 480 ARG B 627 CG CD NE CZ NH1 NH2
REMARK 480 LYS B 643 CG CD CE NZ
REMARK 480 ASN B 645 CB CG OD1 ND2
REMARK 480 ASN B 647 CB CG OD1 ND2
REMARK 480 LYS B 648 CB CG CD CE NZ
REMARK 480 ASN B 649 CB CG OD1 ND2
REMARK 480 ASP B 708 CG OD1 OD2
REMARK 480 LYS B 712 CG CD CE NZ
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 O HOH A 858 O HOH A 859 2.07
REMARK 500 O HOH B 946 O HOH B 947 2.14
REMARK 500 O ARG B 541 O HOH B 1094 2.19
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 TYR A 358 CE1 TYR A 358 CZ -0.093
REMARK 500 TYR A 601 CG TYR A 601 CD2 -0.091
REMARK 500 TYR A 601 CG TYR A 601 CD1 -0.091
REMARK 500 TYR A 601 CE1 TYR A 601 CZ -0.098
REMARK 500 TYR A 601 CZ TYR A 601 CE2 -0.099
REMARK 500 PHE A 715 CG PHE A 715 CD2 -0.109
REMARK 500 PHE A 715 CG PHE A 715 CD1 -0.105
REMARK 500 PHE A 715 CE1 PHE A 715 CZ -0.153
REMARK 500 PHE A 715 CZ PHE A 715 CE2 -0.135
REMARK 500 TYR B 601 CG TYR B 601 CD2 -0.091
REMARK 500 TYR B 601 CG TYR B 601 CD1 -0.091
REMARK 500 TYR B 601 CE1 TYR B 601 CZ -0.107
REMARK 500 TYR B 601 CZ TYR B 601 CE2 -0.096
REMARK 500 PHE B 715 CG PHE B 715 CD2 -0.103
REMARK 500 PHE B 715 CG PHE B 715 CD1 -0.092
REMARK 500 PHE B 715 CE1 PHE B 715 CZ -0.136
REMARK 500 PHE B 715 CZ PHE B 715 CE2 -0.143
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 GLY A 514 N - CA - C ANGL. DEV. = -18.5 DEGREES
REMARK 500 MET A 686 CG - SD - CE ANGL. DEV. = 10.4 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 THR A 203 -77.09 -30.23
REMARK 500 THR A 209 40.16 -94.08
REMARK 500 ALA A 225 157.13 -49.78
REMARK 500 GLU A 317 -126.21 -127.82
REMARK 500 VAL A 421 82.82 -64.37
REMARK 500 THR A 422 -66.03 -102.36
REMARK 500 SER A 508 138.95 -171.64
REMARK 500 PRO A 510 -153.16 -76.18
REMARK 500 SER A 513 70.01 -157.48
REMARK 500 GLN A 515 169.55 -20.44
REMARK 500 SER A 535 48.47 -142.25
REMARK 500 ARG A 556 49.42 -81.27
REMARK 500 ILE A 574 70.87 -101.37
REMARK 500 ARG A 627 68.96 -155.95
REMARK 500 VAL A 644 33.06 -59.27
REMARK 500 ASN A 645 86.37 67.96
REMARK 500 LYS A 646 -86.32 -136.32
REMARK 500 ASN A 647 -106.37 -155.57
REMARK 500 LYS A 648 11.15 -153.50
REMARK 500 ASN A 681 52.14 -155.74
REMARK 500 PHE B 162 -28.36 -33.74
REMARK 500 ASP B 167 -82.90 -62.42
REMARK 500 ASN B 173 -1.84 75.35
REMARK 500 ILE B 174 97.39 -60.52
REMARK 500 GLN B 175 97.16 -59.10
REMARK 500 TYR B 180 -50.48 -136.45
REMARK 500 ASP B 198 -83.21 -19.24
REMARK 500 GLU B 317 -125.10 -136.98
REMARK 500 ASN B 349 18.02 52.64
REMARK 500 TYR B 358 33.40 71.64
REMARK 500 THR B 422 -34.97 -136.88
REMARK 500 SER B 509 132.69 158.46
REMARK 500 GLN B 515 168.59 -21.12
REMARK 500 SER B 535 50.41 -141.86
REMARK 500 ILE B 574 68.83 -101.76
REMARK 500 ILE B 636 -65.74 -90.42
REMARK 500 VAL B 644 -153.51 -64.02
REMARK 500 LYS B 646 141.16 -38.99
REMARK 500 LYS B 648 -129.23 65.47
REMARK 500 SER B 650 95.87 -33.82
REMARK 500 ASP B 653 75.29 -119.97
REMARK 500 ASN B 681 49.37 -156.77
REMARK 500 ASN B 724 4.17 -69.02
REMARK 500 PRO B 744 -38.75 -35.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 2 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 I3P A 1 O2
REMARK 620 2 ASN A 312 OD1 92.1
REMARK 620 3 GLU A 341 OE2 77.3 81.5
REMARK 620 4 ASP A 343 OD2 138.6 91.7 144.0
REMARK 620 5 ASP A 343 OD1 160.8 103.2 93.5 53.5
REMARK 620 6 GLU A 390 OE1 78.2 169.9 93.5 97.5 85.8
REMARK 620 7 HOH A1070 O 78.1 101.6 155.2 60.8 109.3 79.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 3 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 650 OG
REMARK 620 2 ILE A 651 O 75.7
REMARK 620 3 ASP A 653 OD1 158.0 88.1
REMARK 620 4 ASP A 653 OD2 126.5 111.0 46.1
REMARK 620 5 ASN A 677 OD1 125.2 91.5 69.1 108.0
REMARK 620 6 HOH A1002 O 121.1 161.8 77.2 66.1 73.3
REMARK 620 7 HOH A1003 O 62.1 98.9 136.6 150.0 68.0 84.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 2 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 I3P B 1 O2
REMARK 620 2 ASN B 312 OD1 85.8
REMARK 620 3 GLU B 341 OE2 74.7 78.3
REMARK 620 4 ASP B 343 OD2 138.6 88.2 143.5
REMARK 620 5 ASP B 343 OD1 165.8 101.4 94.6 54.6
REMARK 620 6 GLU B 390 OE1 81.5 167.1 96.2 102.7 90.6
REMARK 620 7 HOH B1176 O 62.9 100.4 137.5 78.1 126.6 75.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 3 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE B 651 O
REMARK 620 2 ASP B 653 OD1 83.1
REMARK 620 3 ASP B 653 OD2 124.0 40.9
REMARK 620 4 ASN B 677 OD1 96.5 89.3 86.6
REMARK 620 5 HOH B 791 O 73.4 97.7 105.9 166.8
REMARK 620 6 HOH B 793 O 168.5 108.0 67.1 87.0 101.3
REMARK 620 7 HOH B 794 O 77.9 150.9 151.4 71.4 97.7 92.9
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I3P A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I3P B 1
DBREF 1DJX A 133 756 UNP P10688 PLCD1_RAT 133 756
DBREF 1DJX B 133 756 UNP P10688 PLCD1_RAT 133 756
SEQRES 1 A 624 GLY SER MET ASP GLN ARG GLN LYS LEU GLN HIS TRP ILE
SEQRES 2 A 624 HIS SER CYS LEU ARG LYS ALA ASP LYS ASN LYS ASP ASN
SEQRES 3 A 624 LYS MET ASN PHE LYS GLU LEU LYS ASP PHE LEU LYS GLU
SEQRES 4 A 624 LEU ASN ILE GLN VAL ASP ASP GLY TYR ALA ARG LYS ILE
SEQRES 5 A 624 PHE ARG GLU CYS ASP HIS SER GLN THR ASP SER LEU GLU
SEQRES 6 A 624 ASP GLU GLU ILE GLU THR PHE TYR LYS MET LEU THR GLN
SEQRES 7 A 624 ARG ALA GLU ILE ASP ARG ALA PHE GLU GLU ALA ALA GLY
SEQRES 8 A 624 SER ALA GLU THR LEU SER VAL GLU ARG LEU VAL THR PHE
SEQRES 9 A 624 LEU GLN HIS GLN GLN ARG GLU GLU GLU ALA GLY PRO ALA
SEQRES 10 A 624 LEU ALA LEU SER LEU ILE GLU ARG TYR GLU PRO SER GLU
SEQRES 11 A 624 THR ALA LYS ALA GLN ARG GLN MET THR LYS ASP GLY PHE
SEQRES 12 A 624 LEU MET TYR LEU LEU SER ALA ASP GLY ASN ALA PHE SER
SEQRES 13 A 624 LEU ALA HIS ARG ARG VAL TYR GLN ASP MET ASP GLN PRO
SEQRES 14 A 624 LEU SER HIS TYR LEU VAL SER SER SER HIS ASN THR TYR
SEQRES 15 A 624 LEU LEU GLU ASP GLN LEU THR GLY PRO SER SER THR GLU
SEQRES 16 A 624 ALA TYR ILE ARG ALA LEU CYS LYS GLY CYS ARG CYS LEU
SEQRES 17 A 624 GLU LEU ASP CYS TRP ASP GLY PRO ASN GLN GLU PRO ILE
SEQRES 18 A 624 ILE TYR HIS GLY TYR THR PHE THR SER LYS ILE LEU PHE
SEQRES 19 A 624 CYS ASP VAL LEU ARG ALA ILE ARG ASP TYR ALA PHE LYS
SEQRES 20 A 624 ALA SER PRO TYR PRO VAL ILE LEU SER LEU GLU ASN HIS
SEQRES 21 A 624 CYS SER LEU GLU GLN GLN ARG VAL MET ALA ARG HIS LEU
SEQRES 22 A 624 ARG ALA ILE LEU GLY PRO ILE LEU LEU ASP GLN PRO LEU
SEQRES 23 A 624 ASP GLY VAL THR THR SER LEU PRO SER PRO GLU GLN LEU
SEQRES 24 A 624 LYS GLY LYS ILE LEU LEU LYS GLY LYS LYS LEU GLY GLY
SEQRES 25 A 624 LEU LEU PRO ALA GLY GLY GLU ASN GLY SER GLU ALA THR
SEQRES 26 A 624 ASP VAL SER ASP GLU VAL GLU ALA ALA GLU MET GLU ASP
SEQRES 27 A 624 GLU ALA VAL ARG SER GLN VAL GLN HIS LYS PRO LYS GLU
SEQRES 28 A 624 ASP LYS LEU LYS LEU VAL PRO GLU LEU SER ASP MET ILE
SEQRES 29 A 624 ILE TYR CYS LYS SER VAL HIS PHE GLY GLY PHE SER SER
SEQRES 30 A 624 PRO GLY THR SER GLY GLN ALA PHE TYR GLU MET ALA SER
SEQRES 31 A 624 PHE SER GLU SER ARG ALA LEU ARG LEU LEU GLN GLU SER
SEQRES 32 A 624 GLY ASN GLY PHE VAL ARG HIS ASN VAL SER CYS LEU SER
SEQRES 33 A 624 ARG ILE TYR PRO ALA GLY TRP ARG THR ASP SER SER ASN
SEQRES 34 A 624 TYR SER PRO VAL GLU MET TRP ASN GLY GLY CYS GLN ILE
SEQRES 35 A 624 VAL ALA LEU ASN PHE GLN THR PRO GLY PRO GLU MET ASP
SEQRES 36 A 624 VAL TYR LEU GLY CYS PHE GLN ASP ASN GLY GLY CYS GLY
SEQRES 37 A 624 TYR VAL LEU LYS PRO ALA PHE LEU ARG ASP PRO ASN THR
SEQRES 38 A 624 THR PHE ASN SER ARG ALA LEU THR GLN GLY PRO TRP TRP
SEQRES 39 A 624 ARG PRO GLU ARG LEU ARG VAL ARG ILE ILE SER GLY GLN
SEQRES 40 A 624 GLN LEU PRO LYS VAL ASN LYS ASN LYS ASN SER ILE VAL
SEQRES 41 A 624 ASP PRO LYS VAL ILE VAL GLU ILE HIS GLY VAL GLY ARG
SEQRES 42 A 624 ASP THR GLY SER ARG GLN THR ALA VAL ILE THR ASN ASN
SEQRES 43 A 624 GLY PHE ASN PRO ARG TRP ASP MET GLU PHE GLU PHE GLU
SEQRES 44 A 624 VAL THR VAL PRO ASP LEU ALA LEU VAL ARG PHE MET VAL
SEQRES 45 A 624 GLU ASP TYR ASP SER SER SER LYS ASN ASP PHE ILE GLY
SEQRES 46 A 624 GLN SER THR ILE PRO TRP ASN SER LEU LYS GLN GLY TYR
SEQRES 47 A 624 ARG HIS VAL HIS LEU LEU SER LYS ASN GLY ASP GLN HIS
SEQRES 48 A 624 PRO SER ALA THR LEU PHE VAL LYS ILE SER ILE GLN ASP
SEQRES 1 B 624 GLY SER MET ASP GLN ARG GLN LYS LEU GLN HIS TRP ILE
SEQRES 2 B 624 HIS SER CYS LEU ARG LYS ALA ASP LYS ASN LYS ASP ASN
SEQRES 3 B 624 LYS MET ASN PHE LYS GLU LEU LYS ASP PHE LEU LYS GLU
SEQRES 4 B 624 LEU ASN ILE GLN VAL ASP ASP GLY TYR ALA ARG LYS ILE
SEQRES 5 B 624 PHE ARG GLU CYS ASP HIS SER GLN THR ASP SER LEU GLU
SEQRES 6 B 624 ASP GLU GLU ILE GLU THR PHE TYR LYS MET LEU THR GLN
SEQRES 7 B 624 ARG ALA GLU ILE ASP ARG ALA PHE GLU GLU ALA ALA GLY
SEQRES 8 B 624 SER ALA GLU THR LEU SER VAL GLU ARG LEU VAL THR PHE
SEQRES 9 B 624 LEU GLN HIS GLN GLN ARG GLU GLU GLU ALA GLY PRO ALA
SEQRES 10 B 624 LEU ALA LEU SER LEU ILE GLU ARG TYR GLU PRO SER GLU
SEQRES 11 B 624 THR ALA LYS ALA GLN ARG GLN MET THR LYS ASP GLY PHE
SEQRES 12 B 624 LEU MET TYR LEU LEU SER ALA ASP GLY ASN ALA PHE SER
SEQRES 13 B 624 LEU ALA HIS ARG ARG VAL TYR GLN ASP MET ASP GLN PRO
SEQRES 14 B 624 LEU SER HIS TYR LEU VAL SER SER SER HIS ASN THR TYR
SEQRES 15 B 624 LEU LEU GLU ASP GLN LEU THR GLY PRO SER SER THR GLU
SEQRES 16 B 624 ALA TYR ILE ARG ALA LEU CYS LYS GLY CYS ARG CYS LEU
SEQRES 17 B 624 GLU LEU ASP CYS TRP ASP GLY PRO ASN GLN GLU PRO ILE
SEQRES 18 B 624 ILE TYR HIS GLY TYR THR PHE THR SER LYS ILE LEU PHE
SEQRES 19 B 624 CYS ASP VAL LEU ARG ALA ILE ARG ASP TYR ALA PHE LYS
SEQRES 20 B 624 ALA SER PRO TYR PRO VAL ILE LEU SER LEU GLU ASN HIS
SEQRES 21 B 624 CYS SER LEU GLU GLN GLN ARG VAL MET ALA ARG HIS LEU
SEQRES 22 B 624 ARG ALA ILE LEU GLY PRO ILE LEU LEU ASP GLN PRO LEU
SEQRES 23 B 624 ASP GLY VAL THR THR SER LEU PRO SER PRO GLU GLN LEU
SEQRES 24 B 624 LYS GLY LYS ILE LEU LEU LYS GLY LYS LYS LEU GLY GLY
SEQRES 25 B 624 LEU LEU PRO ALA GLY GLY GLU ASN GLY SER GLU ALA THR
SEQRES 26 B 624 ASP VAL SER ASP GLU VAL GLU ALA ALA GLU MET GLU ASP
SEQRES 27 B 624 GLU ALA VAL ARG SER GLN VAL GLN HIS LYS PRO LYS GLU
SEQRES 28 B 624 ASP LYS LEU LYS LEU VAL PRO GLU LEU SER ASP MET ILE
SEQRES 29 B 624 ILE TYR CYS LYS SER VAL HIS PHE GLY GLY PHE SER SER
SEQRES 30 B 624 PRO GLY THR SER GLY GLN ALA PHE TYR GLU MET ALA SER
SEQRES 31 B 624 PHE SER GLU SER ARG ALA LEU ARG LEU LEU GLN GLU SER
SEQRES 32 B 624 GLY ASN GLY PHE VAL ARG HIS ASN VAL SER CYS LEU SER
SEQRES 33 B 624 ARG ILE TYR PRO ALA GLY TRP ARG THR ASP SER SER ASN
SEQRES 34 B 624 TYR SER PRO VAL GLU MET TRP ASN GLY GLY CYS GLN ILE
SEQRES 35 B 624 VAL ALA LEU ASN PHE GLN THR PRO GLY PRO GLU MET ASP
SEQRES 36 B 624 VAL TYR LEU GLY CYS PHE GLN ASP ASN GLY GLY CYS GLY
SEQRES 37 B 624 TYR VAL LEU LYS PRO ALA PHE LEU ARG ASP PRO ASN THR
SEQRES 38 B 624 THR PHE ASN SER ARG ALA LEU THR GLN GLY PRO TRP TRP
SEQRES 39 B 624 ARG PRO GLU ARG LEU ARG VAL ARG ILE ILE SER GLY GLN
SEQRES 40 B 624 GLN LEU PRO LYS VAL ASN LYS ASN LYS ASN SER ILE VAL
SEQRES 41 B 624 ASP PRO LYS VAL ILE VAL GLU ILE HIS GLY VAL GLY ARG
SEQRES 42 B 624 ASP THR GLY SER ARG GLN THR ALA VAL ILE THR ASN ASN
SEQRES 43 B 624 GLY PHE ASN PRO ARG TRP ASP MET GLU PHE GLU PHE GLU
SEQRES 44 B 624 VAL THR VAL PRO ASP LEU ALA LEU VAL ARG PHE MET VAL
SEQRES 45 B 624 GLU ASP TYR ASP SER SER SER LYS ASN ASP PHE ILE GLY
SEQRES 46 B 624 GLN SER THR ILE PRO TRP ASN SER LEU LYS GLN GLY TYR
SEQRES 47 B 624 ARG HIS VAL HIS LEU LEU SER LYS ASN GLY ASP GLN HIS
SEQRES 48 B 624 PRO SER ALA THR LEU PHE VAL LYS ILE SER ILE GLN ASP
HET CA A 2 1
HET CA A 3 1
HET ACT A 5 4
HET I3P A 1 24
HET CA B 2 1
HET CA B 3 1
HET ACT B 5 4
HET I3P B 1 24
HETNAM CA CALCIUM ION
HETNAM ACT ACETATE ION
HETNAM I3P D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE
FORMUL 3 CA 4(CA 2+)
FORMUL 5 ACT 2(C2 H3 O2 1-)
FORMUL 6 I3P 2(C6 H15 O15 P3)
FORMUL 11 HOH *779(H2 O)
HELIX 1 1 THR A 203 LEU A 208 1 6
HELIX 2 2 ALA A 212 ALA A 222 1 11
HELIX 3 3 VAL A 230 HIS A 239 1 10
HELIX 4 4 PRO A 248 TYR A 258 1 11
HELIX 5 5 GLU A 262 ALA A 266 1 5
HELIX 6 6 LYS A 272 LEU A 279 1 8
HELIX 7 7 LEU A 289 ARG A 292 5 4
HELIX 8 8 LEU A 302 HIS A 304 5 3
HELIX 9 9 THR A 326 CYS A 334 1 9
HELIX 10 10 PRO A 348 GLN A 350 5 3
HELIX 11 11 PHE A 366 TYR A 376 1 11
HELIX 12 12 LEU A 395 ILE A 412 1 18
HELIX 13 13 PRO A 490 MET A 495 1 6
HELIX 14 14 GLU A 525 SER A 545 1 21
HELIX 15 15 VAL A 565 GLY A 570 1 6
HELIX 16 16 PRO A 584 GLN A 594 1 11
HELIX 17 17 ASN A 596 GLY A 598 5 3
HELIX 18 18 ALA A 606 ARG A 609 5 4
HELIX 19 19 GLY A 664 ASP A 666 5 3
HELIX 20 20 PRO A 695 LEU A 697 5 3
HELIX 21 21 TRP A 723 SER A 725 5 3
HELIX 22 22 PHE B 162 LEU B 172 1 11
HELIX 23 23 TYR B 180 CYS B 188 1 9
HELIX 24 24 ASP B 198 THR B 209 1 12
HELIX 25 25 ALA B 212 ALA B 222 1 11
HELIX 26 26 VAL B 230 HIS B 239 1 10
HELIX 27 27 PRO B 248 TYR B 258 1 11
HELIX 28 28 GLU B 262 ALA B 266 1 5
HELIX 29 29 LYS B 272 LEU B 280 1 9
HELIX 30 30 LEU B 289 HIS B 291 5 3
HELIX 31 31 LEU B 302 HIS B 304 5 3
HELIX 32 32 THR B 326 CYS B 334 1 9
HELIX 33 33 PRO B 348 GLN B 350 5 3
HELIX 34 34 PHE B 366 TYR B 376 1 11
HELIX 35 35 LEU B 395 ILE B 412 1 18
HELIX 36 36 PRO B 490 MET B 495 1 6
HELIX 37 37 GLU B 525 SER B 545 1 21
HELIX 38 38 VAL B 565 GLY B 570 1 6
HELIX 39 39 PRO B 584 GLY B 598 1 15
HELIX 40 40 ALA B 606 ARG B 609 5 4
HELIX 41 41 GLY B 664 ASP B 666 5 3
HELIX 42 42 PRO B 695 LEU B 697 5 3
HELIX 43 43 TRP B 723 SER B 725 5 3
SHEET 1 A 3 TYR A 601 LEU A 603 0
SHEET 2 A 3 TYR A 305 SER A 310 -1 N LEU A 306 O VAL A 602
SHEET 3 A 3 ILE A 574 LEU A 577 1 N VAL A 575 O VAL A 307
SHEET 1 B 3 CYS A 339 TRP A 345 0
SHEET 2 B 3 VAL A 385 HIS A 392 1 N ILE A 386 O LEU A 340
SHEET 3 B 3 ILE A 435 LYS A 438 1 N LEU A 436 O VAL A 385
SHEET 1 C 3 LYS A 500 VAL A 502 0
SHEET 2 C 3 GLU A 519 SER A 524 1 N MET A 520 O LYS A 500
SHEET 3 C 3 SER A 548 TYR A 551 1 N ARG A 549 O ALA A 521
SHEET 1 D 4 MET A 686 VAL A 692 0
SHEET 2 D 4 GLU A 629 GLN A 639 -1 N ILE A 635 O MET A 686
SHEET 3 D 4 THR A 747 GLN A 755 -1 N GLN A 755 O ARG A 630
SHEET 4 D 4 GLY A 729 HIS A 734 -1 N VAL A 733 O LEU A 748
SHEET 1 E 4 GLY A 668 GLN A 671 0
SHEET 2 E 4 PRO A 654 HIS A 661 -1 N ILE A 660 O GLY A 668
SHEET 3 E 4 LEU A 699 ASP A 706 -1 N GLU A 705 O LYS A 655
SHEET 4 E 4 ASP A 714 PRO A 722 -1 N ILE A 721 O VAL A 700
SHEET 1 F 2 LYS B 159 ASN B 161 0
SHEET 2 F 2 SER B 195 GLU B 197 -1 N LEU B 196 O MET B 160
SHEET 1 G 2 TYR B 305 VAL B 307 0
SHEET 2 G 2 TYR B 601 LEU B 603 -1 N VAL B 602 O LEU B 306
SHEET 1 H 3 CYS B 339 TRP B 345 0
SHEET 2 H 3 VAL B 385 HIS B 392 1 N ILE B 386 O LEU B 340
SHEET 3 H 3 ILE B 435 LYS B 438 1 N LEU B 436 O VAL B 385
SHEET 1 I 3 LYS B 500 VAL B 502 0
SHEET 2 I 3 GLU B 519 SER B 524 1 N MET B 520 O LYS B 500
SHEET 3 I 3 SER B 548 TYR B 551 1 N ARG B 549 O ALA B 521
SHEET 1 J 4 MET B 686 VAL B 692 0
SHEET 2 J 4 GLU B 629 GLN B 639 -1 N ILE B 635 O MET B 686
SHEET 3 J 4 THR B 747 GLN B 755 -1 N GLN B 755 O ARG B 630
SHEET 4 J 4 GLY B 729 HIS B 734 -1 N VAL B 733 O LEU B 748
SHEET 1 K 4 GLY B 668 GLN B 671 0
SHEET 2 K 4 PRO B 654 HIS B 661 -1 N ILE B 660 O GLY B 668
SHEET 3 K 4 LEU B 699 ASP B 706 -1 N GLU B 705 O LYS B 655
SHEET 4 K 4 ASP B 714 PRO B 722 -1 N ILE B 721 O VAL B 700
LINK O2 I3P A 1 CA CA A 2 1555 1555 2.36
LINK CA CA A 2 OD1 ASN A 312 1555 1555 2.36
LINK CA CA A 2 OE2 GLU A 341 1555 1555 2.45
LINK CA CA A 2 OD2 ASP A 343 1555 1555 2.44
LINK CA CA A 2 OD1 ASP A 343 1555 1555 2.47
LINK CA CA A 2 OE1 GLU A 390 1555 1555 2.28
LINK CA CA A 2 O HOH A1070 1555 1555 3.10
LINK CA CA A 3 OG SER A 650 1555 1555 3.37
LINK CA CA A 3 O ILE A 651 1555 1555 2.06
LINK CA CA A 3 OD1 ASP A 653 1555 1555 2.78
LINK CA CA A 3 OD2 ASP A 653 1555 1555 2.80
LINK CA CA A 3 OD1 ASN A 677 1555 1555 2.75
LINK CA CA A 3 O HOH A1002 1555 1555 2.74
LINK CA CA A 3 O HOH A1003 1555 1555 2.92
LINK O2 I3P B 1 CA CA B 2 1555 1555 2.14
LINK CA CA B 2 OD1 ASN B 312 1555 1555 2.50
LINK CA CA B 2 OE2 GLU B 341 1555 1555 2.59
LINK CA CA B 2 OD2 ASP B 343 1555 1555 2.32
LINK CA CA B 2 OD1 ASP B 343 1555 1555 2.42
LINK CA CA B 2 OE1 GLU B 390 1555 1555 2.30
LINK CA CA B 2 O HOH B1176 1555 1555 2.66
LINK CA CA B 3 O ILE B 651 1555 1555 2.33
LINK CA CA B 3 OD1 ASP B 653 1555 1555 2.20
LINK CA CA B 3 OD2 ASP B 653 1555 1555 3.31
LINK CA CA B 3 OD1 ASN B 677 1555 1555 2.82
LINK CA CA B 3 O HOH B 791 1555 1555 2.80
LINK CA CA B 3 O HOH B 793 1555 1555 2.44
LINK CA CA B 3 O HOH B 794 1555 1555 2.83
CISPEP 1 SER B 509 PRO B 510 0 -4.66
SITE 1 AC1 5 I3P A 1 ASN A 312 GLU A 341 ASP A 343
SITE 2 AC1 5 GLU A 390
SITE 1 AC2 6 SER A 650 ILE A 651 ASP A 653 ASN A 677
SITE 2 AC2 6 HOH A1002 HOH A1003
SITE 1 AC3 7 GLY A 583 PRO A 584 ASP A 587 ARG A 701
SITE 2 AC3 7 PHE A 715 LYS A 738 HOH A 994
SITE 1 AC4 6 I3P B 1 ASN B 312 GLU B 341 ASP B 343
SITE 2 AC4 6 GLU B 390 HOH B1176
SITE 1 AC5 6 ILE B 651 ASP B 653 ASN B 677 HOH B 791
SITE 2 AC5 6 HOH B 793 HOH B 794
SITE 1 AC6 7 GLY B 583 PRO B 584 ASP B 587 ARG B 701
SITE 2 AC6 7 PHE B 715 LYS B 738 HOH B 930
SITE 1 AC7 12 CA A 2 HIS A 311 ASN A 312 GLU A 341
SITE 2 AC7 12 HIS A 356 GLU A 390 LYS A 438 SER A 522
SITE 3 AC7 12 ARG A 549 TYR A 551 HOH A1034 HOH A1070
SITE 1 AC8 16 CA B 2 HIS B 311 ASN B 312 GLU B 341
SITE 2 AC8 16 HIS B 356 GLU B 390 LYS B 438 SER B 522
SITE 3 AC8 16 ARG B 549 TYR B 551 HOH B1028 HOH B1031
SITE 4 AC8 16 HOH B1148 HOH B1149 HOH B1150 HOH B1176
CRYST1 397.540 397.540 397.540 90.00 90.00 90.00 F 41 3 2 192
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 0.002515 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002515 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002515 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
