HEADER TRANSFERASE 09-NOV-09 2WXK
TITLE THE CRYSTAL STRUCTURE OF THE MURINE CLASS IA PI 3-KINASE P110DELTA IN
TITLE 2 COMPLEX WITH INK666.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE 3-KINASE CATALYTIC
COMPND 3 SUBUNIT DELTA ISOFORM;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: RESIDUES 106-1044;
COMPND 6 SYNONYM: PI3-KINASE P110 SUBUNIT DELTA, PTDINS-3-KINASE P110,
COMPND 7 P110DELTA, PI3K;
COMPND 8 EC: 2.7.1.153;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: SF21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFASTBAC HTA
KEYWDS TRANSFERASE, PHOSPHOPROTEIN, ISOFORM-SPECIFIC INHIBITORS, CANCER
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BERNDT,S.MILLER,O.WILLIAMS,D.D.LEE,B.T.HOUSEMAN,J.I.PACOLD,
AUTHOR 2 F.GORREC,W.-C.HON,Y.LIU,C.ROMMEL,P.GAILLARD,T.RUCKLE,M.K.SCHWARZ,
AUTHOR 3 K.M.SHOKAT,J.P.SHAW,R.L.WILLIAMS
REVDAT 5 20-DEC-23 2WXK 1 REMARK SHEET
REVDAT 4 24-APR-19 2WXK 1 SOURCE
REVDAT 3 13-JUL-11 2WXK 1 VERSN
REVDAT 2 26-JAN-10 2WXK 1 JRNL REMARK
REVDAT 1 12-JAN-10 2WXK 0
JRNL AUTH A.BERNDT,S.MILLER,O.WILLIAMS,D.D.LEE,B.T.HOUSEMAN,
JRNL AUTH 2 J.I.PACOLD,F.GORREC,W.-C.HON,Y.LIU,C.ROMMEL,P.GAILLARD,
JRNL AUTH 3 T.RUCKLE,M.K.SCHWARZ,K.M.SHOKAT,J.P.SHAW,R.L.WILLIAMS
JRNL TITL THE P110D STRUCTURE: MECHANISMS FOR SELECTIVITY AND POTENCY
JRNL TITL 2 OF NEW PI(3)K INHIBITORS
JRNL REF NAT.CHEM.BIOL. V. 6 117 2010
JRNL REFN ISSN 1552-4450
JRNL PMID 20081827
JRNL DOI 10.1038/NCHEMBIO.293
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0046
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 68.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 22700
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT : 733
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1628
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE SET COUNT : 53
REMARK 3 BIN FREE R VALUE : 0.3800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6739
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 71.32
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.88000
REMARK 3 B22 (A**2) : -1.97000
REMARK 3 B33 (A**2) : 0.09000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.460
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.358
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 40.304
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.918
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.844
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6926 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 5 ; 0.107 ; 0.022
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9346 ; 1.693 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9 ; 7.480 ; 3.849
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 823 ; 6.771 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 324 ;36.818 ;24.043
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1252 ;21.415 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;22.929 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1023 ; 0.109 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5166 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 4 ; 0.008 ; 0.030
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3428 ; 0.264 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3 ; 0.337 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4753 ; 0.329 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1 ; 0.063 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 233 ; 0.185 ; 0.200
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): 39 ; 0.312 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.267 ; 0.200
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): 4155 ; 0.585 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6675 ; 1.175 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2771 ; 1.811 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2671 ; 3.002 ; 4.500
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 : 5
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 109 A 189
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0212 -14.0049 20.0826
REMARK 3 T TENSOR
REMARK 3 T11: 0.1117 T22: 0.4121
REMARK 3 T33: 0.4267 T12: -0.1018
REMARK 3 T13: -0.0660 T23: 0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.1550 L22: 5.0440
REMARK 3 L33: 7.1199 L12: -0.8144
REMARK 3 L13: -0.1212 L23: 2.0631
REMARK 3 S TENSOR
REMARK 3 S11: 0.0908 S12: -0.0103 S13: 0.0243
REMARK 3 S21: -0.6175 S22: 0.0331 S23: 0.2633
REMARK 3 S31: -0.0905 S32: -0.8173 S33: -0.1239
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 190 A 290
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7228 9.7573 37.7044
REMARK 3 T TENSOR
REMARK 3 T11: 0.3573 T22: 0.2091
REMARK 3 T33: 0.3648 T12: 0.0140
REMARK 3 T13: 0.1105 T23: -0.0730
REMARK 3 L TENSOR
REMARK 3 L11: 5.5236 L22: 7.5587
REMARK 3 L33: 4.5699 L12: 0.6506
REMARK 3 L13: 2.1648 L23: 1.2950
REMARK 3 S TENSOR
REMARK 3 S11: -0.3801 S12: -0.3458 S13: 0.4005
REMARK 3 S21: 0.2021 S22: 0.3997 S23: -0.2682
REMARK 3 S31: -1.0841 S32: -0.2353 S33: -0.0196
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 317 A 494
REMARK 3 ORIGIN FOR THE GROUP (A): -13.0367 -48.8324 15.2611
REMARK 3 T TENSOR
REMARK 3 T11: 1.2608 T22: 0.1422
REMARK 3 T33: 0.2569 T12: -0.3831
REMARK 3 T13: -0.0728 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 2.5191 L22: 2.4610
REMARK 3 L33: 4.8225 L12: 0.1739
REMARK 3 L13: -1.1548 L23: -1.4644
REMARK 3 S TENSOR
REMARK 3 S11: -0.3189 S12: 0.0692 S13: -0.3048
REMARK 3 S21: -0.9077 S22: 0.2470 S23: 0.1517
REMARK 3 S31: 2.0385 S32: -0.4865 S33: 0.0719
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 505 A 677
REMARK 3 ORIGIN FOR THE GROUP (A): -15.4784 -32.3856 34.1981
REMARK 3 T TENSOR
REMARK 3 T11: 0.3179 T22: 0.3292
REMARK 3 T33: 0.2091 T12: -0.2161
REMARK 3 T13: 0.0565 T23: 0.0557
REMARK 3 L TENSOR
REMARK 3 L11: 0.6254 L22: 3.8872
REMARK 3 L33: 4.9119 L12: 0.5249
REMARK 3 L13: -0.4840 L23: -2.5327
REMARK 3 S TENSOR
REMARK 3 S11: -0.0417 S12: -0.2281 S13: -0.1716
REMARK 3 S21: 0.1783 S22: 0.0801 S23: 0.2280
REMARK 3 S31: 0.7408 S32: -0.5484 S33: -0.0384
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 678 A 1027
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1429 -11.5210 31.1654
REMARK 3 T TENSOR
REMARK 3 T11: 0.0535 T22: 0.2589
REMARK 3 T33: 0.2121 T12: 0.0032
REMARK 3 T13: 0.0386 T23: -0.0640
REMARK 3 L TENSOR
REMARK 3 L11: 2.3824 L22: 1.6235
REMARK 3 L33: 2.8900 L12: -0.1235
REMARK 3 L13: 0.7674 L23: -0.4858
REMARK 3 S TENSOR
REMARK 3 S11: 0.0240 S12: -0.3689 S13: 0.1534
REMARK 3 S21: -0.0904 S22: -0.0623 S23: -0.3309
REMARK 3 S31: 0.2756 S32: 0.4170 S33: 0.0383
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 2WXK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-NOV-09.
REMARK 100 THE DEPOSITION ID IS D_1290041560.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-AUG-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97620
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23471
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 74.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.08
REMARK 200 R MERGE (I) : 0.17000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.1400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.36
REMARK 200 R MERGE FOR SHELL (I) : 0.74000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2RD0
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (V/V) GLYCEROL, 10% (W/V) PEG 4K,
REMARK 280 30 MM NANO3, 30 MM NA2HPO4, 30 MM (NH4)2SO4, 100 MM IMIDAZOLE PH
REMARK 280 6.8
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
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 111.56050
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 111.56050
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 1.000000 0.000000 0.000000 32.18100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 71.83450
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.18100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 71.83450
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 111.56050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.18100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 71.83450
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 111.56050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.18100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 71.83450
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 105
REMARK 465 GLY A 106
REMARK 465 ASP A 107
REMARK 465 ARG A 108
REMARK 465 SER A 174
REMARK 465 ALA A 175
REMARK 465 ARG A 176
REMARK 465 GLY A 177
REMARK 465 TRP A 178
REMARK 465 ARG A 179
REMARK 465 ALA A 180
REMARK 465 GLY A 181
REMARK 465 LEU A 182
REMARK 465 LEU A 183
REMARK 465 ARG A 184
REMARK 465 VAL A 185
REMARK 465 SER A 186
REMARK 465 VAL A 233
REMARK 465 PRO A 292
REMARK 465 ALA A 293
REMARK 465 PRO A 294
REMARK 465 GLN A 295
REMARK 465 VAL A 296
REMARK 465 GLN A 297
REMARK 465 LYS A 298
REMARK 465 PRO A 299
REMARK 465 ARG A 300
REMARK 465 ALA A 301
REMARK 465 LYS A 302
REMARK 465 PRO A 303
REMARK 465 PRO A 304
REMARK 465 PRO A 305
REMARK 465 ILE A 306
REMARK 465 PRO A 307
REMARK 465 ALA A 308
REMARK 465 LYS A 309
REMARK 465 LYS A 310
REMARK 465 PRO A 311
REMARK 465 SER A 312
REMARK 465 SER A 313
REMARK 465 VAL A 314
REMARK 465 SER A 315
REMARK 465 ASP A 336
REMARK 465 GLU A 337
REMARK 465 ARG A 338
REMARK 465 GLU A 399
REMARK 465 LYS A 400
REMARK 465 ALA A 401
REMARK 465 LYS A 402
REMARK 465 LYS A 403
REMARK 465 ALA A 404
REMARK 465 ARG A 405
REMARK 465 SER A 406
REMARK 465 THR A 407
REMARK 465 LYS A 408
REMARK 465 LYS A 409
REMARK 465 LYS A 410
REMARK 465 SER A 411
REMARK 465 LYS A 412
REMARK 465 LYS A 413
REMARK 465 ALA A 414
REMARK 465 PRO A 446
REMARK 465 ASP A 447
REMARK 465 GLU A 448
REMARK 465 LYS A 449
REMARK 465 GLY A 450
REMARK 465 PRO A 480
REMARK 465 HIS A 481
REMARK 465 GLY A 495
REMARK 465 ARG A 496
REMARK 465 HIS A 497
REMARK 465 GLY A 498
REMARK 465 GLU A 499
REMARK 465 ARG A 500
REMARK 465 GLY A 501
REMARK 465 ARG A 502
REMARK 465 ILE A 503
REMARK 465 THR A 504
REMARK 465 GLN A 508
REMARK 465 LEU A 509
REMARK 465 GLN A 510
REMARK 465 ARG A 518
REMARK 465 GLY A 519
REMARK 465 THR A 921
REMARK 465 LYS A 922
REMARK 465 PHE A 923
REMARK 465 GLY A 924
REMARK 465 ILE A 925
REMARK 465 LYS A 1028
REMARK 465 THR A 1029
REMARK 465 LYS A 1030
REMARK 465 VAL A 1031
REMARK 465 ASN A 1032
REMARK 465 TRP A 1033
REMARK 465 LEU A 1034
REMARK 465 ALA A 1035
REMARK 465 HIS A 1036
REMARK 465 ASN A 1037
REMARK 465 VAL A 1038
REMARK 465 SER A 1039
REMARK 465 LYS A 1040
REMARK 465 ASP A 1041
REMARK 465 ASN A 1042
REMARK 465 ARG A 1043
REMARK 465 GLN A 1044
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 THR A 434 CG2
REMARK 470 LEU A 452 CG CD1 CD2
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 OE2 GLU A 234 OH TYR A 239 1.97
REMARK 500 O VAL A 699 OG SER A 703 2.03
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 CYS A 745 CB CYS A 745 SG -0.130
REMARK 500 GLU A 866 CD GLU A 866 OE1 0.073
REMARK 500 CYS A 879 CB CYS A 879 SG -0.099
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 PRO A 443 C - N - CA ANGL. DEV. = 9.6 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 GLN A 156 18.16 -142.47
REMARK 500 VAL A 227 -70.03 -49.38
REMARK 500 PRO A 231 -81.68 -49.32
REMARK 500 GLU A 237 13.13 -67.92
REMARK 500 TYR A 251 -177.14 -174.10
REMARK 500 LEU A 270 158.51 -32.32
REMARK 500 ARG A 331 87.68 -156.35
REMARK 500 LYS A 332 -178.03 -170.65
REMARK 500 CYS A 355 172.91 173.13
REMARK 500 VAL A 365 28.97 -72.59
REMARK 500 CYS A 366 -168.07 -63.75
REMARK 500 ASP A 378 39.77 -85.64
REMARK 500 LEU A 384 128.12 -38.17
REMARK 500 ALA A 421 132.64 -173.93
REMARK 500 ASP A 427 173.81 -57.61
REMARK 500 SER A 467 -20.35 -150.63
REMARK 500 GLU A 573 157.12 -48.90
REMARK 500 LYS A 602 4.68 -68.51
REMARK 500 LYS A 705 11.50 -141.41
REMARK 500 HIS A 730 71.94 62.38
REMARK 500 ASP A 736 109.06 -163.35
REMARK 500 GLU A 742 -91.68 -84.69
REMARK 500 THR A 750 -169.27 -163.42
REMARK 500 SER A 754 135.55 -177.17
REMARK 500 LYS A 755 -125.04 80.45
REMARK 500 ARG A 821 56.49 32.65
REMARK 500 THR A 847 89.46 -58.46
REMARK 500 ASP A 911 70.74 46.12
REMARK 500 ASN A 918 66.26 -69.08
REMARK 500 GLU A 928 -157.04 -102.33
REMARK 500 VAL A 930 130.36 -38.58
REMARK 500 ASN A 949 62.16 -152.61
REMARK 500 ALA A1003 63.13 38.48
REMARK 500 GLU A1008 -39.92 -31.91
REMARK 500 GLU A1009 -73.92 -77.68
REMARK 500 SER A1026 91.56 -55.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 230 PRO A 231 142.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RW4 A 1500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WXM RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE MURINE CLASS IA PI 3-KINASE P110DELTA
REMARK 900 IN COMPLEX WITH DL06.
REMARK 900 RELATED ID: 2WXH RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE MURINE CLASS IA PI 3-KINASE P110DELTA
REMARK 900 IN COMPLEX WITH SW14.
REMARK 900 RELATED ID: 2WXL RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE MURINE CLASS IA PI 3-KINASE P110DELTA
REMARK 900 IN COMPLEX WITH ZSTK474.
REMARK 900 RELATED ID: 2WXG RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE MURINE CLASS IA PI 3-KINASE P110DELTA
REMARK 900 IN COMPLEX WITH SW13.
REMARK 900 RELATED ID: 2WXI RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE MURINE CLASS IA PI 3-KINASE P110DELTA
REMARK 900 IN COMPLEX WITH SW30.
REMARK 900 RELATED ID: 2WXP RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE MURINE CLASS IA PI 3-KINASE P110DELTA
REMARK 900 IN COMPLEX WITH GDC-0941.
REMARK 900 RELATED ID: 2WXO RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE MURINE CLASS IA PI 3-KINASE P110DELTA
REMARK 900 IN COMPLEX WITH AS5.
REMARK 900 RELATED ID: 2WXF RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE MURINE CLASS IA PI 3-KINASE P110DELTA
REMARK 900 IN COMPLEX WITH PIK-39.
REMARK 900 RELATED ID: 2WXQ RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE MURINE CLASS IA PI 3-KINASE P110DELTA
REMARK 900 IN COMPLEX WITH AS15.
REMARK 900 RELATED ID: 2WXN RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE MURINE CLASS IA PI 3-KINASE P110DELTA
REMARK 900 IN COMPLEX WITH DL06.
REMARK 900 RELATED ID: 2WXE RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE MURINE CLASS IA PI 3-KINASE P110DELTA
REMARK 900 IN COMPLEX WITH IC87114.
REMARK 900 RELATED ID: 2WXJ RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE MURINE CLASS IA PI 3-KINASE P110DELTA
REMARK 900 IN COMPLEX WITH INK654.
REMARK 900 RELATED ID: 2WXR RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE MURINE CLASS IA PI 3-KINASE P110DELTA.
DBREF 2WXK A 106 1044 UNP Q3UDT3 Q3UDT3_MOUSE 106 1044
SEQADV 2WXK GLY A 105 UNP Q3UDT3 EXPRESSION TAG
SEQRES 1 A 940 GLY GLY ASP ARG VAL LYS LYS LEU ILE ASN SER GLN ILE
SEQRES 2 A 940 SER LEU LEU ILE GLY LYS GLY LEU HIS GLU PHE ASP SER
SEQRES 3 A 940 LEU ARG ASP PRO GLU VAL ASN ASP PHE ARG THR LYS MET
SEQRES 4 A 940 ARG GLN PHE CYS GLU GLU ALA ALA ALA HIS ARG GLN GLN
SEQRES 5 A 940 LEU GLY TRP VAL GLU TRP LEU GLN TYR SER PHE PRO LEU
SEQRES 6 A 940 GLN LEU GLU PRO SER ALA ARG GLY TRP ARG ALA GLY LEU
SEQRES 7 A 940 LEU ARG VAL SER ASN ARG ALA LEU LEU VAL ASN VAL LYS
SEQRES 8 A 940 PHE GLU GLY SER GLU GLU SER PHE THR PHE GLN VAL SER
SEQRES 9 A 940 THR LYS ASP MET PRO LEU ALA LEU MET ALA CYS ALA LEU
SEQRES 10 A 940 ARG LYS LYS ALA THR VAL PHE ARG GLN PRO LEU VAL GLU
SEQRES 11 A 940 GLN PRO GLU GLU TYR ALA LEU GLN VAL ASN GLY ARG HIS
SEQRES 12 A 940 GLU TYR LEU TYR GLY ASN TYR PRO LEU CYS HIS PHE GLN
SEQRES 13 A 940 TYR ILE CYS SER CYS LEU HIS SER GLY LEU THR PRO HIS
SEQRES 14 A 940 LEU THR MET VAL HIS SER SER SER ILE LEU ALA MET ARG
SEQRES 15 A 940 ASP GLU GLN SER ASN PRO ALA PRO GLN VAL GLN LYS PRO
SEQRES 16 A 940 ARG ALA LYS PRO PRO PRO ILE PRO ALA LYS LYS PRO SER
SEQRES 17 A 940 SER VAL SER LEU TRP SER LEU GLU GLN PRO PHE SER ILE
SEQRES 18 A 940 GLU LEU ILE GLU GLY ARG LYS VAL ASN ALA ASP GLU ARG
SEQRES 19 A 940 MET LYS LEU VAL VAL GLN ALA GLY LEU PHE HIS GLY ASN
SEQRES 20 A 940 GLU MET LEU CYS LYS THR VAL SER SER SER GLU VAL ASN
SEQRES 21 A 940 VAL CYS SER GLU PRO VAL TRP LYS GLN ARG LEU GLU PHE
SEQRES 22 A 940 ASP ILE SER VAL CYS ASP LEU PRO ARG MET ALA ARG LEU
SEQRES 23 A 940 CYS PHE ALA LEU TYR ALA VAL VAL GLU LYS ALA LYS LYS
SEQRES 24 A 940 ALA ARG SER THR LYS LYS LYS SER LYS LYS ALA ASP CYS
SEQRES 25 A 940 PRO ILE ALA TRP ALA ASN LEU MET LEU PHE ASP TYR LYS
SEQRES 26 A 940 ASP GLN LEU LYS THR GLY GLU ARG CYS LEU TYR MET TRP
SEQRES 27 A 940 PRO SER VAL PRO ASP GLU LYS GLY GLU LEU LEU ASN PRO
SEQRES 28 A 940 ALA GLY THR VAL ARG GLY ASN PRO ASN THR GLU SER ALA
SEQRES 29 A 940 ALA ALA LEU VAL ILE TYR LEU PRO GLU VAL ALA PRO HIS
SEQRES 30 A 940 PRO VAL TYR PHE PRO ALA LEU GLU LYS ILE LEU GLU LEU
SEQRES 31 A 940 GLY ARG HIS GLY GLU ARG GLY ARG ILE THR GLU GLU GLU
SEQRES 32 A 940 GLN LEU GLN LEU ARG GLU ILE LEU GLU ARG ARG GLY SER
SEQRES 33 A 940 GLY GLU LEU TYR GLU HIS GLU LYS ASP LEU VAL TRP LYS
SEQRES 34 A 940 MET ARG HIS GLU VAL GLN GLU HIS PHE PRO GLU ALA LEU
SEQRES 35 A 940 ALA ARG LEU LEU LEU VAL THR LYS TRP ASN LYS HIS GLU
SEQRES 36 A 940 ASP VAL ALA GLN MET LEU TYR LEU LEU CYS SER TRP PRO
SEQRES 37 A 940 GLU LEU PRO VAL LEU SER ALA LEU GLU LEU LEU ASP PHE
SEQRES 38 A 940 SER PHE PRO ASP CYS TYR VAL GLY SER PHE ALA ILE LYS
SEQRES 39 A 940 SER LEU ARG LYS LEU THR ASP ASP GLU LEU PHE GLN TYR
SEQRES 40 A 940 LEU LEU GLN LEU VAL GLN VAL LEU LYS TYR GLU SER TYR
SEQRES 41 A 940 LEU ASP CYS GLU LEU THR LYS PHE LEU LEU GLY ARG ALA
SEQRES 42 A 940 LEU ALA ASN ARG LYS ILE GLY HIS PHE LEU PHE TRP HIS
SEQRES 43 A 940 LEU ARG SER GLU MET HIS VAL PRO SER VAL ALA LEU ARG
SEQRES 44 A 940 PHE GLY LEU ILE MET GLU ALA TYR CYS ARG GLY SER THR
SEQRES 45 A 940 HIS HIS MET LYS VAL LEU MET LYS GLN GLY GLU ALA LEU
SEQRES 46 A 940 SER LYS LEU LYS ALA LEU ASN ASP PHE VAL LYS VAL SER
SEQRES 47 A 940 SER GLN LYS THR THR LYS PRO GLN THR LYS GLU MET MET
SEQRES 48 A 940 HIS MET CYS MET ARG GLN GLU THR TYR MET GLU ALA LEU
SEQRES 49 A 940 SER HIS LEU GLN SER PRO LEU ASP PRO SER THR LEU LEU
SEQRES 50 A 940 GLU GLU VAL CYS VAL GLU GLN CYS THR PHE MET ASP SER
SEQRES 51 A 940 LYS MET LYS PRO LEU TRP ILE MET TYR SER SER GLU GLU
SEQRES 52 A 940 ALA GLY SER ALA GLY ASN VAL GLY ILE ILE PHE LYS ASN
SEQRES 53 A 940 GLY ASP ASP LEU ARG GLN ASP MET LEU THR LEU GLN MET
SEQRES 54 A 940 ILE GLN LEU MET ASP VAL LEU TRP LYS GLN GLU GLY LEU
SEQRES 55 A 940 ASP LEU ARG MET THR PRO TYR GLY CYS LEU PRO THR GLY
SEQRES 56 A 940 ASP ARG THR GLY LEU ILE GLU VAL VAL LEU HIS SER ASP
SEQRES 57 A 940 THR ILE ALA ASN ILE GLN LEU ASN LYS SER ASN MET ALA
SEQRES 58 A 940 ALA THR ALA ALA PHE ASN LYS ASP ALA LEU LEU ASN TRP
SEQRES 59 A 940 LEU LYS SER LYS ASN PRO GLY GLU ALA LEU ASP ARG ALA
SEQRES 60 A 940 ILE GLU GLU PHE THR LEU SER CYS ALA GLY TYR CYS VAL
SEQRES 61 A 940 ALA THR TYR VAL LEU GLY ILE GLY ASP ARG HIS SER ASP
SEQRES 62 A 940 ASN ILE MET ILE ARG GLU SER GLY GLN LEU PHE HIS ILE
SEQRES 63 A 940 ASP PHE GLY HIS PHE LEU GLY ASN PHE LYS THR LYS PHE
SEQRES 64 A 940 GLY ILE ASN ARG GLU ARG VAL PRO PHE ILE LEU THR TYR
SEQRES 65 A 940 ASP PHE VAL HIS VAL ILE GLN GLN GLY LYS THR ASN ASN
SEQRES 66 A 940 SER GLU LYS PHE GLU ARG PHE ARG GLY TYR CYS GLU ARG
SEQRES 67 A 940 ALA TYR THR ILE LEU ARG ARG HIS GLY LEU LEU PHE LEU
SEQRES 68 A 940 HIS LEU PHE ALA LEU MET ARG ALA ALA GLY LEU PRO GLU
SEQRES 69 A 940 LEU SER CYS SER LYS ASP ILE GLN TYR LEU LYS ASP SER
SEQRES 70 A 940 LEU ALA LEU GLY LYS THR GLU GLU GLU ALA LEU LYS HIS
SEQRES 71 A 940 PHE ARG VAL LYS PHE ASN GLU ALA LEU ARG GLU SER TRP
SEQRES 72 A 940 LYS THR LYS VAL ASN TRP LEU ALA HIS ASN VAL SER LYS
SEQRES 73 A 940 ASP ASN ARG GLN
HET RW4 A1500 38
HETNAM RW4 3-(2-AMINO-1,3-BENZOTHIAZOL-6-YL)-1-{[2-(4-
HETNAM 2 RW4 METHYLPIPERAZIN-1-YL)QUINOLIN-3-YL]METHYL}-1H-
HETNAM 3 RW4 PYRAZOLO[3,4-D]PYRIMIDIN-4-AMINE
FORMUL 2 RW4 C27 H26 N10 S
HELIX 1 1 VAL A 109 GLY A 122 1 14
HELIX 2 2 LEU A 125 SER A 130 1 6
HELIX 3 3 ASP A 133 GLN A 155 1 23
HELIX 4 4 GLY A 158 PHE A 167 1 10
HELIX 5 5 MET A 212 PHE A 228 1 17
HELIX 6 6 GLN A 235 GLU A 237 5 3
HELIX 7 7 PRO A 255 HIS A 258 5 4
HELIX 8 8 PHE A 259 SER A 268 1 10
HELIX 9 9 SER A 279 GLN A 289 1 11
HELIX 10 10 ALA A 487 LEU A 494 1 8
HELIX 11 11 TYR A 524 MET A 534 1 11
HELIX 12 12 MET A 534 PHE A 542 1 9
HELIX 13 13 ALA A 545 THR A 553 1 9
HELIX 14 14 LYS A 557 CYS A 569 1 13
HELIX 15 15 PRO A 575 LEU A 583 1 9
HELIX 16 16 ASP A 589 ARG A 601 1 13
HELIX 17 17 THR A 604 LYS A 620 1 17
HELIX 18 18 CYS A 627 ASN A 640 1 14
HELIX 19 19 ASN A 640 SER A 653 1 14
HELIX 20 20 VAL A 657 SER A 675 1 19
HELIX 21 21 SER A 675 SER A 703 1 29
HELIX 22 22 THR A 707 GLN A 721 1 15
HELIX 23 23 GLN A 721 LEU A 728 1 8
HELIX 24 24 VAL A 746 CYS A 749 5 4
HELIX 25 25 ALA A 768 ASN A 773 5 6
HELIX 26 26 LEU A 784 GLU A 804 1 21
HELIX 27 27 ILE A 834 GLN A 838 1 5
HELIX 28 28 LYS A 852 ASN A 863 1 12
HELIX 29 29 GLU A 866 GLY A 890 1 25
HELIX 30 30 HIS A 895 ASP A 897 5 3
HELIX 31 31 THR A 935 GLN A 943 1 9
HELIX 32 32 ASN A 949 HIS A 970 1 22
HELIX 33 33 HIS A 970 ARG A 982 1 13
HELIX 34 34 ALA A 983 GLY A 985 5 3
HELIX 35 35 CYS A 991 LEU A 1002 1 12
HELIX 36 36 THR A 1007 SER A 1026 1 20
SHEET 1 AA 5 SER A 202 SER A 208 0
SHEET 2 AA 5 ALA A 189 PHE A 196 -1 O LEU A 190 N VAL A 207
SHEET 3 AA 5 HIS A 273 HIS A 278 1 O LEU A 274 N LYS A 195
SHEET 4 AA 5 TYR A 239 VAL A 243 -1 O ALA A 240 N VAL A 277
SHEET 5 AA 5 TYR A 249 LEU A 250 -1 O LEU A 250 N LEU A 241
SHEET 1 AB 4 VAL A 370 SER A 380 0
SHEET 2 AB 4 PRO A 322 GLY A 330 -1 O PHE A 323 N PHE A 377
SHEET 3 AB 4 ALA A 470 LEU A 475 -1 O VAL A 472 N ILE A 328
SHEET 4 AB 4 GLY A 435 TYR A 440 -1 O GLY A 435 N LEU A 475
SHEET 1 AC 5 GLU A 352 MET A 353 0
SHEET 2 AC 5 LYS A 340 HIS A 349 -1 O HIS A 349 N GLU A 352
SHEET 3 AC 5 ARG A 389 VAL A 397 -1 O ARG A 389 N PHE A 348
SHEET 4 AC 5 CYS A 416 MET A 424 -1 O CYS A 416 N ALA A 396
SHEET 5 AC 5 TRP A 442 PRO A 443 -1 O TRP A 442 N TRP A 420
SHEET 1 AD 2 GLU A 352 MET A 353 0
SHEET 2 AD 2 VAL A 363 ASN A 364 -1 O VAL A 363 N LEU A 341
SHEET 1 AE 2 LEU A 731 SER A 733 0
SHEET 2 AE 2 ASP A 736 LEU A 741 -1 N ASP A 736 O SER A 733
SHEET 1 AF 3 GLU A 743 VAL A 744 0
SHEET 2 AF 3 LEU A 759 SER A 764 -1 O SER A 764 N GLU A 743
SHEET 3 AF 3 THR A 750 PHE A 751 -1 O THR A 750 N TRP A 760
SHEET 1 AG 2 GLU A 743 VAL A 744 0
SHEET 2 AG 2 LEU A 759 SER A 764 -1 O SER A 764 N GLU A 743
SHEET 1 AH 3 SER A 831 THR A 833 0
SHEET 2 AH 3 ILE A 899 ARG A 902 -1 O ILE A 901 N ASP A 832
SHEET 3 AH 3 LEU A 907 HIS A 909 -1 O PHE A 908 N MET A 900
CISPEP 1 PRO A 231 LEU A 232 0 -12.55
CISPEP 2 THR A 434 GLY A 435 0 -12.72
SITE 1 AC1 12 PHE A 751 MET A 752 TRP A 760 LYS A 779
SITE 2 AC1 12 ASP A 787 TYR A 813 GLU A 826 VAL A 827
SITE 3 AC1 12 VAL A 828 ASP A 832 ILE A 910 ASP A 911
CRYST1 64.362 143.669 223.121 90.00 90.00 90.00 C 2 2 21 8
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 0.015537 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006960 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004482 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
