HEADER TRANSFERASE 18-JUN-14 4UPU
TITLE CRYSTAL STRUCTURE OF IP3 3-K CALMODULIN BINDING REGION IN COMPLEX WITH
TITLE 2 CALMODULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 2-149;
COMPND 5 SYNONYM: CAM;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: INOSITOL-TRISPHOSPHATE 3-KINASE A;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: CALMODULIN BINDING REGION, RESIDUES 158-183;
COMPND 11 SYNONYM: INOSITOL 1\,4\,5-TRISPHOSPHATE 3-KINASE A, IP3 3-KINASE A,
COMPND 12 IP3K A, INSP 3-KINASE A;
COMPND 13 EC: 2.7.1.127;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET14B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VARIANT: ROSETTA PLYSS;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PKLSLT
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.FRANCO-ECHEVARRIA,J.I.BANOS-SANZ,B.MONTERROSO,A.ROUND,J.SANZ-
AUTHOR 2 APARICIO,B.GONZALEZ
REVDAT 4 10-JAN-24 4UPU 1 REMARK LINK
REVDAT 3 22-OCT-14 4UPU 1 JRNL
REVDAT 2 10-SEP-14 4UPU 1 TITLE MASTER
REVDAT 1 20-AUG-14 4UPU 0
JRNL AUTH E.FRANCO-ECHEVARRIA,J.I.BANOS-SANZ,B.MONTERROSO,A.ROUND,
JRNL AUTH 2 J.SANZ-APARICIO,B.GONZALEZ
JRNL TITL A NEW CALMODULIN BINDING MOTIF FOR INOSITOL
JRNL TITL 2 1,4,5-TRISPHOSPHATE 3-KINASE REGULATION.
JRNL REF BIOCHEM.J. V. 463 319 2014
JRNL REFN ISSN 0264-6021
JRNL PMID 25101901
JRNL DOI 10.1042/BJ20140757
REMARK 2
REMARK 2 RESOLUTION. 2.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 2.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 79.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 14144
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 752
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) : 2.34
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.40
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1031
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE SET COUNT : 54
REMARK 3 BIN FREE R VALUE : 0.2380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1305
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 81
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.77000
REMARK 3 B22 (A**2) : -11.33000
REMARK 3 B33 (A**2) : 5.56000
REMARK 3 B12 (A**2) : -1.80000
REMARK 3 B13 (A**2) : -18.88000
REMARK 3 B23 (A**2) : -2.03000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.039
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.034
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.581
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1342 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1806 ; 1.451 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 166 ; 5.608 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 74 ;34.239 ;26.216
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 251 ;17.038 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;16.743 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 199 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1024 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 661 ; 2.104 ; 3.285
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 825 ; 3.286 ; 4.903
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 680 ; 3.478 ; 3.663
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 : 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. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U
REMARK 3 VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4UPU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1290060902.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALBA
REMARK 200 BEAMLINE : XALOC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : KB FOCUSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14994
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.340
REMARK 200 RESOLUTION RANGE LOW (A) : 79.740
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.90
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.9100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.66
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.060
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2VAY
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 29% W/V POLYETHYLENE GLYCOL 4000, 0.2
REMARK 280 M (NH4)2SO4, 0.1 M SODIUM ACETATE TRIHYDRATE PH 4.0 AND 10 MM
REMARK 280 SPERMIDINE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 3 2
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 Y,X,-Z
REMARK 290 14555 -Y,-X,-Z
REMARK 290 15555 Y,-X,Z
REMARK 290 16555 -Y,X,Z
REMARK 290 17555 X,Z,-Y
REMARK 290 18555 -X,Z,Y
REMARK 290 19555 -X,-Z,-Y
REMARK 290 20555 X,-Z,Y
REMARK 290 21555 Z,Y,-X
REMARK 290 22555 Z,-Y,X
REMARK 290 23555 -Z,Y,X
REMARK 290 24555 -Z,-Y,-X
REMARK 290 25555 X+1/2,Y+1/2,Z+1/2
REMARK 290 26555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 27555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 28555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 29555 Z+1/2,X+1/2,Y+1/2
REMARK 290 30555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 31555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 32555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 33555 Y+1/2,Z+1/2,X+1/2
REMARK 290 34555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 35555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 36555 -Y+1/2,-Z+1/2,X+1/2
REMARK 290 37555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 38555 -Y+1/2,-X+1/2,-Z+1/2
REMARK 290 39555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 40555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 41555 X+1/2,Z+1/2,-Y+1/2
REMARK 290 42555 -X+1/2,Z+1/2,Y+1/2
REMARK 290 43555 -X+1/2,-Z+1/2,-Y+1/2
REMARK 290 44555 X+1/2,-Z+1/2,Y+1/2
REMARK 290 45555 Z+1/2,Y+1/2,-X+1/2
REMARK 290 46555 Z+1/2,-Y+1/2,X+1/2
REMARK 290 47555 -Z+1/2,Y+1/2,X+1/2
REMARK 290 48555 -Z+1/2,-Y+1/2,-X+1/2
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 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 25 1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY2 25 0.000000 1.000000 0.000000 79.74000
REMARK 290 SMTRY3 25 0.000000 0.000000 1.000000 79.74000
REMARK 290 SMTRY1 26 -1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY2 26 0.000000 -1.000000 0.000000 79.74000
REMARK 290 SMTRY3 26 0.000000 0.000000 1.000000 79.74000
REMARK 290 SMTRY1 27 -1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY2 27 0.000000 1.000000 0.000000 79.74000
REMARK 290 SMTRY3 27 0.000000 0.000000 -1.000000 79.74000
REMARK 290 SMTRY1 28 1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY2 28 0.000000 -1.000000 0.000000 79.74000
REMARK 290 SMTRY3 28 0.000000 0.000000 -1.000000 79.74000
REMARK 290 SMTRY1 29 0.000000 0.000000 1.000000 79.74000
REMARK 290 SMTRY2 29 1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY3 29 0.000000 1.000000 0.000000 79.74000
REMARK 290 SMTRY1 30 0.000000 0.000000 1.000000 79.74000
REMARK 290 SMTRY2 30 -1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY3 30 0.000000 -1.000000 0.000000 79.74000
REMARK 290 SMTRY1 31 0.000000 0.000000 -1.000000 79.74000
REMARK 290 SMTRY2 31 -1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY3 31 0.000000 1.000000 0.000000 79.74000
REMARK 290 SMTRY1 32 0.000000 0.000000 -1.000000 79.74000
REMARK 290 SMTRY2 32 1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY3 32 0.000000 -1.000000 0.000000 79.74000
REMARK 290 SMTRY1 33 0.000000 1.000000 0.000000 79.74000
REMARK 290 SMTRY2 33 0.000000 0.000000 1.000000 79.74000
REMARK 290 SMTRY3 33 1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY1 34 0.000000 -1.000000 0.000000 79.74000
REMARK 290 SMTRY2 34 0.000000 0.000000 1.000000 79.74000
REMARK 290 SMTRY3 34 -1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY1 35 0.000000 1.000000 0.000000 79.74000
REMARK 290 SMTRY2 35 0.000000 0.000000 -1.000000 79.74000
REMARK 290 SMTRY3 35 -1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY1 36 0.000000 -1.000000 0.000000 79.74000
REMARK 290 SMTRY2 36 0.000000 0.000000 -1.000000 79.74000
REMARK 290 SMTRY3 36 1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY1 37 0.000000 1.000000 0.000000 79.74000
REMARK 290 SMTRY2 37 1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY3 37 0.000000 0.000000 -1.000000 79.74000
REMARK 290 SMTRY1 38 0.000000 -1.000000 0.000000 79.74000
REMARK 290 SMTRY2 38 -1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY3 38 0.000000 0.000000 -1.000000 79.74000
REMARK 290 SMTRY1 39 0.000000 1.000000 0.000000 79.74000
REMARK 290 SMTRY2 39 -1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY3 39 0.000000 0.000000 1.000000 79.74000
REMARK 290 SMTRY1 40 0.000000 -1.000000 0.000000 79.74000
REMARK 290 SMTRY2 40 1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY3 40 0.000000 0.000000 1.000000 79.74000
REMARK 290 SMTRY1 41 1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY2 41 0.000000 0.000000 1.000000 79.74000
REMARK 290 SMTRY3 41 0.000000 -1.000000 0.000000 79.74000
REMARK 290 SMTRY1 42 -1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY2 42 0.000000 0.000000 1.000000 79.74000
REMARK 290 SMTRY3 42 0.000000 1.000000 0.000000 79.74000
REMARK 290 SMTRY1 43 -1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY2 43 0.000000 0.000000 -1.000000 79.74000
REMARK 290 SMTRY3 43 0.000000 -1.000000 0.000000 79.74000
REMARK 290 SMTRY1 44 1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY2 44 0.000000 0.000000 -1.000000 79.74000
REMARK 290 SMTRY3 44 0.000000 1.000000 0.000000 79.74000
REMARK 290 SMTRY1 45 0.000000 0.000000 1.000000 79.74000
REMARK 290 SMTRY2 45 0.000000 1.000000 0.000000 79.74000
REMARK 290 SMTRY3 45 -1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY1 46 0.000000 0.000000 1.000000 79.74000
REMARK 290 SMTRY2 46 0.000000 -1.000000 0.000000 79.74000
REMARK 290 SMTRY3 46 1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY1 47 0.000000 0.000000 -1.000000 79.74000
REMARK 290 SMTRY2 47 0.000000 1.000000 0.000000 79.74000
REMARK 290 SMTRY3 47 1.000000 0.000000 0.000000 79.74000
REMARK 290 SMTRY1 48 0.000000 0.000000 -1.000000 79.74000
REMARK 290 SMTRY2 48 0.000000 -1.000000 0.000000 79.74000
REMARK 290 SMTRY3 48 -1.000000 0.000000 0.000000 79.74000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 48-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 119950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 165820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2468.9 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 0.000000 1.000000 159.48000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 -159.48000
REMARK 350 BIOMT1 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 3 -1.000000 0.000000 0.000000 159.48000
REMARK 350 BIOMT3 3 0.000000 1.000000 0.000000 -159.48000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 0.000000 -1.000000 159.48000
REMARK 350 BIOMT3 4 0.000000 1.000000 0.000000 -159.48000
REMARK 350 BIOMT1 5 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 5 1.000000 0.000000 0.000000 159.48000
REMARK 350 BIOMT3 5 0.000000 -1.000000 0.000000 159.48000
REMARK 350 BIOMT1 6 0.000000 -1.000000 0.000000 159.48000
REMARK 350 BIOMT2 6 0.000000 0.000000 -1.000000 159.48000
REMARK 350 BIOMT3 6 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 7 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 7 0.000000 0.000000 1.000000 159.48000
REMARK 350 BIOMT3 7 0.000000 -1.000000 0.000000 159.48000
REMARK 350 BIOMT1 8 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 8 0.000000 -1.000000 0.000000 318.96000
REMARK 350 BIOMT3 8 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 9 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 9 0.000000 0.000000 -1.000000 159.48000
REMARK 350 BIOMT3 9 0.000000 -1.000000 0.000000 159.48000
REMARK 350 BIOMT1 10 0.000000 -1.000000 0.000000 159.48000
REMARK 350 BIOMT2 10 0.000000 0.000000 1.000000 159.48000
REMARK 350 BIOMT3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 11 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 12 0.000000 1.000000 0.000000 -159.48000
REMARK 350 BIOMT2 12 1.000000 0.000000 0.000000 159.48000
REMARK 350 BIOMT3 12 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 13 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 13 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 13 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 14 0.000000 1.000000 0.000000 -159.48000
REMARK 350 BIOMT2 14 -1.000000 0.000000 0.000000 159.48000
REMARK 350 BIOMT3 14 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 15 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 15 0.000000 -1.000000 0.000000 318.96000
REMARK 350 BIOMT3 15 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 16 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 16 1.000000 0.000000 0.000000 159.48000
REMARK 350 BIOMT3 16 0.000000 1.000000 0.000000 -159.48000
REMARK 350 BIOMT1 17 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 17 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 17 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 18 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 18 -1.000000 0.000000 0.000000 159.48000
REMARK 350 BIOMT3 18 0.000000 -1.000000 0.000000 159.48000
REMARK 350 BIOMT1 19 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 19 0.000000 -1.000000 0.000000 318.96000
REMARK 350 BIOMT3 19 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 20 0.000000 1.000000 0.000000 -159.48000
REMARK 350 BIOMT2 20 0.000000 0.000000 1.000000 159.48000
REMARK 350 BIOMT3 20 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 21 0.000000 1.000000 0.000000 -159.48000
REMARK 350 BIOMT2 21 0.000000 0.000000 -1.000000 159.48000
REMARK 350 BIOMT3 21 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 22 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT2 22 0.000000 -1.000000 0.000000 318.96000
REMARK 350 BIOMT3 22 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 23 0.000000 -1.000000 0.000000 159.48000
REMARK 350 BIOMT2 23 -1.000000 0.000000 0.000000 159.48000
REMARK 350 BIOMT3 23 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 24 0.000000 -1.000000 0.000000 159.48000
REMARK 350 BIOMT2 24 1.000000 0.000000 0.000000 159.48000
REMARK 350 BIOMT3 24 0.000000 0.000000 1.000000 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 CA CA A1153 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2018 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2019 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 ALA A 2
REMARK 465 ASP A 3
REMARK 465 LYS A 149
REMARK 465 GLY B 158
REMARK 465 GLU B 159
REMARK 465 ASP B 160
REMARK 465 VAL B 161
REMARK 465 GLY B 162
REMARK 465 GLN B 163
REMARK 465 LYS B 164
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 VAL B 178 -62.74 73.64
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 A1149 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 21 OD1
REMARK 620 2 ASP A 23 OD1 76.6
REMARK 620 3 ASP A 25 OD1 83.1 79.5
REMARK 620 4 THR A 27 O 81.3 152.5 81.8
REMARK 620 5 GLU A 32 OE1 110.4 128.2 150.6 75.0
REMARK 620 6 GLU A 32 OE2 101.8 77.2 154.2 123.8 51.0
REMARK 620 7 HOH A2011 O 162.2 87.2 86.8 111.7 85.3 81.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1150 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 57 OD1
REMARK 620 2 ASP A 59 OD1 70.2
REMARK 620 3 ASN A 61 OD1 83.8 72.1
REMARK 620 4 THR A 63 O 80.2 145.3 87.4
REMARK 620 5 GLU A 68 OE1 98.2 122.1 165.6 78.9
REMARK 620 6 GLU A 68 OE2 77.4 72.2 143.6 119.1 50.0
REMARK 620 7 HOH A2030 O 146.7 78.6 97.8 133.0 88.4 82.3
REMARK 620 8 HOH A2031 O 148.5 131.0 82.6 70.8 88.5 127.7 63.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1151 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 94 OD1
REMARK 620 2 ASP A 96 OD1 77.3
REMARK 620 3 ASN A 98 OD1 87.5 78.7
REMARK 620 4 TYR A 100 O 85.2 154.7 82.5
REMARK 620 5 GLU A 105 OE1 110.6 129.1 148.7 74.2
REMARK 620 6 GLU A 105 OE2 95.5 77.9 155.0 122.5 51.7
REMARK 620 7 HOH A2049 O 166.8 89.5 88.2 106.6 79.1 83.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1153 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 119 OD2
REMARK 620 2 ASP A 119 OD2 91.2
REMARK 620 3 ASP A 119 OD2 95.1 93.9
REMARK 620 4 HOH A2060 O 165.0 102.9 79.1
REMARK 620 5 HOH A2060 O 75.9 155.0 108.3 92.7
REMARK 620 6 HOH A2060 O 100.3 72.8 159.7 88.9 88.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1152 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 130 OD1
REMARK 620 2 ASP A 132 OD1 82.6
REMARK 620 3 ASP A 134 OD1 89.7 75.7
REMARK 620 4 GLN A 136 O 88.5 150.6 76.4
REMARK 620 5 GLU A 141 OE1 109.4 127.0 151.0 82.3
REMARK 620 6 GLU A 141 OE2 90.6 77.0 152.3 131.3 52.4
REMARK 620 7 HOH A2071 O 162.0 80.6 80.0 103.2 86.0 91.8
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 1149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1153
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1154
DBREF 4UPU A 2 149 UNP P62158 CALM_HUMAN 2 149
DBREF 4UPU B 158 183 UNP P23677 IP3KA_HUMAN 158 183
SEQRES 1 A 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 A 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 A 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES 8 A 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU
SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES 11 A 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN
SEQRES 12 A 148 MET MET THR ALA LYS
SEQRES 1 B 26 GLY GLU ASP VAL GLY GLN LYS ASN HIS TRP GLN LYS ILE
SEQRES 2 B 26 ARG THR MET VAL ASN LEU PRO VAL ILE SER PRO PHE LYS
HET CA A1149 1
HET CA A1150 1
HET CA A1151 1
HET CA A1152 1
HET CA A1153 1
HET GOL A1154 6
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 CA 5(CA 2+)
FORMUL 8 GOL C3 H8 O3
FORMUL 9 HOH *81(H2 O)
HELIX 1 1 THR A 6 ASP A 21 1 16
HELIX 2 2 THR A 29 LEU A 40 1 12
HELIX 3 3 THR A 45 ASP A 57 1 13
HELIX 4 4 PHE A 66 MET A 77 1 12
HELIX 5 5 SER A 82 ASP A 94 1 13
HELIX 6 6 SER A 102 LEU A 113 1 12
HELIX 7 7 THR A 118 ASP A 130 1 13
HELIX 8 8 TYR A 139 ALA A 148 1 10
HELIX 9 9 ASN B 165 ASN B 175 1 11
SHEET 1 AA 2 THR A 27 ILE A 28 0
SHEET 2 AA 2 ILE A 64 ASP A 65 -1 O ILE A 64 N ILE A 28
SHEET 1 AB 2 TYR A 100 ILE A 101 0
SHEET 2 AB 2 VAL A 137 ASN A 138 -1 O VAL A 137 N ILE A 101
LINK OD1 ASP A 21 CA CA A1149 1555 1555 2.27
LINK OD1 ASP A 23 CA CA A1149 1555 1555 2.34
LINK OD1 ASP A 25 CA CA A1149 1555 1555 2.44
LINK O THR A 27 CA CA A1149 1555 1555 2.26
LINK OE1 GLU A 32 CA CA A1149 1555 1555 2.56
LINK OE2 GLU A 32 CA CA A1149 1555 1555 2.47
LINK OD1 ASP A 57 CA CA A1150 1555 1555 2.32
LINK OD1 ASP A 59 CA CA A1150 1555 1555 2.55
LINK OD1 ASN A 61 CA CA A1150 1555 1555 2.31
LINK O THR A 63 CA CA A1150 1555 1555 2.48
LINK OE1 GLU A 68 CA CA A1150 1555 1555 2.55
LINK OE2 GLU A 68 CA CA A1150 1555 1555 2.57
LINK OD1 ASP A 94 CA CA A1151 1555 1555 2.18
LINK OD1 ASP A 96 CA CA A1151 1555 1555 2.51
LINK OD1 ASN A 98 CA CA A1151 1555 1555 2.39
LINK O TYR A 100 CA CA A1151 1555 1555 2.24
LINK OE1 GLU A 105 CA CA A1151 1555 1555 2.52
LINK OE2 GLU A 105 CA CA A1151 1555 1555 2.49
LINK OD2 ASP A 119 CA CA A1153 6566 1555 3.04
LINK OD2 ASP A 119 CA CA A1153 12665 1555 3.09
LINK OD2 ASP A 119 CA CA A1153 1555 1555 2.90
LINK OD1 ASP A 130 CA CA A1152 1555 1555 2.28
LINK OD1 ASP A 132 CA CA A1152 1555 1555 2.40
LINK OD1 ASP A 134 CA CA A1152 1555 1555 2.30
LINK O GLN A 136 CA CA A1152 1555 1555 2.31
LINK OE1 GLU A 141 CA CA A1152 1555 1555 2.39
LINK OE2 GLU A 141 CA CA A1152 1555 1555 2.49
LINK CA CA A1149 O HOH A2011 1555 1555 2.23
LINK CA CA A1150 O HOH A2030 1555 1555 2.50
LINK CA CA A1150 O HOH A2031 1555 1555 2.35
LINK CA CA A1151 O HOH A2049 1555 1555 2.45
LINK CA CA A1152 O HOH A2071 1555 1555 2.45
LINK CA CA A1153 O HOH A2060 1555 1555 2.31
LINK CA CA A1153 O HOH A2060 1555 6566 2.33
LINK CA CA A1153 O HOH A2060 1555 12665 2.49
SITE 1 AC1 6 ASP A 21 ASP A 23 ASP A 25 THR A 27
SITE 2 AC1 6 GLU A 32 HOH A2011
SITE 1 AC2 7 ASP A 57 ASP A 59 ASN A 61 THR A 63
SITE 2 AC2 7 GLU A 68 HOH A2030 HOH A2031
SITE 1 AC3 6 ASP A 94 ASP A 96 ASN A 98 TYR A 100
SITE 2 AC3 6 GLU A 105 HOH A2049
SITE 1 AC4 6 ASP A 130 ASP A 132 ASP A 134 GLN A 136
SITE 2 AC4 6 GLU A 141 HOH A2071
SITE 1 AC5 2 ASP A 119 HOH A2060
SITE 1 AC6 7 SER A 102 GLU A 105 HIS A 108 HOH A2049
SITE 2 AC6 7 HOH A2052 HOH A2055 HOH A2074
CRYST1 159.480 159.480 159.480 90.00 90.00 90.00 I 4 3 2 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 0.006270 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006270 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006270 0.00000
(ATOM LINES ARE NOT SHOWN.)
END