HEADER TRANSFERASE/TRANSFERASE INHIBITOR 16-MAY-11 3S2A
TITLE CRYSTAL STRUCTURE OF PI3K-GAMMA IN COMPLEX WITH A QUINOLINE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE 3-KINASE CATALYTIC
COMPND 3 SUBUNIT GAMMA ISOFORM;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: CATALYTIC DOMAIN (UNP RESIDUES 144-1102);
COMPND 6 SYNONYM: PI3-KINASE SUBUNIT GAMMA, PI3K-GAMMA, PTDINS-3-KINASE
COMPND 7 SUBUNIT GAMMA, PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE 3-KINASE 110 KDA
COMPND 8 CATALYTIC SUBUNIT GAMMA, PTDINS-3-KINASE SUBUNIT P110-GAMMA, P120-
COMPND 9 PI3K;
COMPND 10 EC: 2.7.1.153;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PIK3CG;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS P110-GAMMA, KINASE, PHOSPHOTRANSFER, P101, P84, LEUKOCYTES,
KEYWDS 2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.WHITTINGTON,J.TANG,P.YAKOWEC
REVDAT 3 13-SEP-23 3S2A 1 REMARK SEQADV
REVDAT 2 20-JUL-11 3S2A 1 JRNL
REVDAT 1 08-JUN-11 3S2A 0
JRNL AUTH N.NISHIMURA,A.SIEGMUND,L.LIU,K.YANG,M.C.BRYAN,K.L.ANDREWS,
JRNL AUTH 2 Y.BO,S.K.BOOKER,S.CAENEPEEL,D.FREEMAN,H.LIAO,J.MCCARTER,
JRNL AUTH 3 E.L.MULLADY,T.SAN MIGUEL,R.SUBRAMANIAN,N.TAMAYO,L.WANG,
JRNL AUTH 4 D.A.WHITTINGTON,L.ZALAMEDA,N.ZHANG,P.E.HUGHES,M.H.NORMAN
JRNL TITL PHOSPSHOINOSITIDE 3-KINASE (PI3K)/MAMMALIAN TARGET OF
JRNL TITL 2 RAPAMYCIN (MTOR) DUAL INHIBITORS: DISCOVERY AND
JRNL TITL 3 STRUCTURE-ACTIVITY RELATIONSHIPS OF A SERIES OF QUINOLINE
JRNL TITL 4 AND QUINOXALINE DERIVATIVES.
JRNL REF J.MED.CHEM. V. 54 4735 2011
JRNL REFN ISSN 0022-2623
JRNL PMID 21612232
JRNL DOI 10.1021/JM200386S
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 31959
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) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.301
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1623
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) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1263
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 52.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.3700
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.3450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6744
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 49
REMARK 3 SOLVENT ATOMS : 29
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 80.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 85.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.60000
REMARK 3 B22 (A**2) : 2.42000
REMARK 3 B33 (A**2) : -0.73000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.54000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.927
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.379
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.286
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.978
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6936 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9390 ; 1.034 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 824 ; 5.438 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 322 ;38.031 ;24.379
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1251 ;16.685 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;16.597 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1055 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5146 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2941 ; 0.194 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4691 ; 0.300 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 197 ; 0.141 ; 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): 24 ; 0.200 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.141 ; 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): 4291 ; 0.346 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6746 ; 0.612 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3033 ; 0.812 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2644 ; 1.318 ; 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 : 7
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 144 A 244
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9101 -13.7786 27.3212
REMARK 3 T TENSOR
REMARK 3 T11: -0.0693 T22: -0.0963
REMARK 3 T33: 0.2256 T12: 0.0284
REMARK 3 T13: -0.0420 T23: 0.1932
REMARK 3 L TENSOR
REMARK 3 L11: 5.5272 L22: 2.0708
REMARK 3 L33: 1.9266 L12: 0.2349
REMARK 3 L13: 0.5853 L23: -0.4776
REMARK 3 S TENSOR
REMARK 3 S11: 0.1295 S12: -0.0664 S13: -1.1912
REMARK 3 S21: 0.1580 S22: 0.1860 S23: 0.6420
REMARK 3 S31: 0.0572 S32: -0.7496 S33: -0.3155
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 269 A 321
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6481 -12.1901 31.8021
REMARK 3 T TENSOR
REMARK 3 T11: -0.1376 T22: 0.2893
REMARK 3 T33: 0.5051 T12: -0.0306
REMARK 3 T13: 0.0403 T23: 0.4744
REMARK 3 L TENSOR
REMARK 3 L11: 6.6275 L22: 3.7115
REMARK 3 L33: 8.0180 L12: -1.2453
REMARK 3 L13: 0.0739 L23: 2.0373
REMARK 3 S TENSOR
REMARK 3 S11: 0.3039 S12: -0.7089 S13: -1.2502
REMARK 3 S21: 0.0750 S22: 0.2193 S23: 0.8068
REMARK 3 S31: 0.0889 S32: -1.0327 S33: -0.5233
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 351 A 436
REMARK 3 ORIGIN FOR THE GROUP (A): 66.8394 -5.6882 15.0009
REMARK 3 T TENSOR
REMARK 3 T11: -0.2250 T22: 0.1615
REMARK 3 T33: -0.2023 T12: 0.0212
REMARK 3 T13: 0.0434 T23: -0.1366
REMARK 3 L TENSOR
REMARK 3 L11: 3.3953 L22: 6.3833
REMARK 3 L33: 6.4844 L12: 1.0814
REMARK 3 L13: -1.7165 L23: -3.4341
REMARK 3 S TENSOR
REMARK 3 S11: 0.0824 S12: 0.2027 S13: 0.0671
REMARK 3 S21: -0.1184 S22: -0.0599 S23: -0.3314
REMARK 3 S31: -0.0715 S32: 0.6416 S33: -0.0225
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 457 A 533
REMARK 3 ORIGIN FOR THE GROUP (A): 57.3206 -8.5581 14.0169
REMARK 3 T TENSOR
REMARK 3 T11: -0.1961 T22: 0.0894
REMARK 3 T33: -0.3134 T12: 0.0110
REMARK 3 T13: 0.0790 T23: -0.1801
REMARK 3 L TENSOR
REMARK 3 L11: 6.6205 L22: 6.1340
REMARK 3 L33: 5.2534 L12: -0.0658
REMARK 3 L13: -0.3017 L23: -1.5582
REMARK 3 S TENSOR
REMARK 3 S11: 0.0585 S12: 0.6650 S13: -0.3518
REMARK 3 S21: -0.1071 S22: -0.1588 S23: -0.2567
REMARK 3 S31: 0.1959 S32: 0.3702 S33: 0.1003
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 546 A 725
REMARK 3 ORIGIN FOR THE GROUP (A): 46.3608 -9.8808 34.5007
REMARK 3 T TENSOR
REMARK 3 T11: -0.1969 T22: -0.3105
REMARK 3 T33: -0.1907 T12: 0.0196
REMARK 3 T13: 0.0480 T23: 0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 5.8160 L22: 0.6932
REMARK 3 L33: 3.1917 L12: -0.7137
REMARK 3 L13: 2.8730 L23: -0.2424
REMARK 3 S TENSOR
REMARK 3 S11: 0.0991 S12: -0.4144 S13: -0.6045
REMARK 3 S21: 0.1640 S22: 0.0906 S23: 0.1209
REMARK 3 S31: 0.0558 S32: 0.1041 S33: -0.1897
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 726 A 885
REMARK 3 ORIGIN FOR THE GROUP (A): 20.3138 5.2022 17.3220
REMARK 3 T TENSOR
REMARK 3 T11: -0.0226 T22: -0.0709
REMARK 3 T33: -0.0844 T12: 0.1394
REMARK 3 T13: 0.0246 T23: 0.0693
REMARK 3 L TENSOR
REMARK 3 L11: 6.1186 L22: 3.2033
REMARK 3 L33: 3.2057 L12: -0.7817
REMARK 3 L13: 2.0168 L23: 0.5688
REMARK 3 S TENSOR
REMARK 3 S11: 0.0205 S12: 0.8652 S13: 0.0854
REMARK 3 S21: -0.4863 S22: 0.0292 S23: 0.4755
REMARK 3 S31: -0.6118 S32: -0.4049 S33: -0.0497
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 886 A 1088
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0613 19.6487 37.3821
REMARK 3 T TENSOR
REMARK 3 T11: 0.4298 T22: -0.1036
REMARK 3 T33: 0.1635 T12: 0.2412
REMARK 3 T13: -0.1158 T23: -0.1990
REMARK 3 L TENSOR
REMARK 3 L11: 7.6771 L22: 4.3927
REMARK 3 L33: 3.2542 L12: -2.4232
REMARK 3 L13: 2.8606 L23: -0.5664
REMARK 3 S TENSOR
REMARK 3 S11: -0.9177 S12: -0.9457 S13: 1.8128
REMARK 3 S21: 0.4378 S22: 0.3569 S23: -0.2237
REMARK 3 S31: -1.2137 S32: -0.4763 S33: 0.5608
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3S2A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-11.
REMARK 100 THE DEPOSITION ID IS D_1000065670.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31971
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.03700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 57.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.35100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.030
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 3QK0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% W/V PEG3350, 245 MM AMMONIUM
REMARK 280 SULFATE, 100 MM TRIS, PH 7.3, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 72.23250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.08450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 72.23250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.08450
REMARK 290 SMTRY3 4 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 143
REMARK 465 LEU A 245
REMARK 465 GLN A 246
REMARK 465 SER A 247
REMARK 465 PHE A 248
REMARK 465 PHE A 249
REMARK 465 THR A 250
REMARK 465 LYS A 251
REMARK 465 MET A 252
REMARK 465 ALA A 253
REMARK 465 LYS A 254
REMARK 465 LYS A 255
REMARK 465 LYS A 256
REMARK 465 SER A 257
REMARK 465 LEU A 258
REMARK 465 MET A 259
REMARK 465 ASP A 260
REMARK 465 ILE A 261
REMARK 465 PRO A 262
REMARK 465 GLU A 263
REMARK 465 SER A 264
REMARK 465 GLN A 265
REMARK 465 SER A 266
REMARK 465 GLU A 267
REMARK 465 GLN A 268
REMARK 465 GLU A 322
REMARK 465 TRP A 323
REMARK 465 PRO A 324
REMARK 465 LEU A 325
REMARK 465 VAL A 326
REMARK 465 ASP A 327
REMARK 465 ASP A 328
REMARK 465 CYS A 329
REMARK 465 THR A 330
REMARK 465 GLY A 331
REMARK 465 VAL A 332
REMARK 465 THR A 333
REMARK 465 GLY A 334
REMARK 465 TYR A 335
REMARK 465 HIS A 336
REMARK 465 GLU A 337
REMARK 465 GLN A 338
REMARK 465 LEU A 339
REMARK 465 THR A 340
REMARK 465 ILE A 341
REMARK 465 HIS A 342
REMARK 465 GLY A 343
REMARK 465 LYS A 344
REMARK 465 ASP A 345
REMARK 465 HIS A 346
REMARK 465 GLU A 347
REMARK 465 SER A 348
REMARK 465 VAL A 349
REMARK 465 PHE A 350
REMARK 465 PRO A 374
REMARK 465 ARG A 375
REMARK 465 ASN A 376
REMARK 465 THR A 377
REMARK 465 LYS A 437
REMARK 465 ALA A 438
REMARK 465 PRO A 439
REMARK 465 ALA A 440
REMARK 465 LEU A 441
REMARK 465 SER A 442
REMARK 465 SER A 443
REMARK 465 LYS A 444
REMARK 465 ALA A 445
REMARK 465 SER A 446
REMARK 465 ALA A 447
REMARK 465 GLU A 448
REMARK 465 SER A 449
REMARK 465 PRO A 450
REMARK 465 SER A 451
REMARK 465 SER A 452
REMARK 465 GLU A 453
REMARK 465 SER A 454
REMARK 465 LYS A 455
REMARK 465 GLY A 456
REMARK 465 GLY A 489
REMARK 465 LYS A 490
REMARK 465 GLY A 491
REMARK 465 GLU A 492
REMARK 465 ASP A 493
REMARK 465 GLN A 494
REMARK 465 GLY A 495
REMARK 465 TYR A 523
REMARK 465 CYS A 524
REMARK 465 PRO A 534
REMARK 465 THR A 535
REMARK 465 PRO A 536
REMARK 465 ASP A 537
REMARK 465 PRO A 538
REMARK 465 GLU A 539
REMARK 465 GLY A 540
REMARK 465 ASP A 541
REMARK 465 ARG A 542
REMARK 465 VAL A 543
REMARK 465 ARG A 544
REMARK 465 ALA A 545
REMARK 465 LYS A 756
REMARK 465 TYR A 757
REMARK 465 LEU A 969
REMARK 465 GLY A 970
REMARK 465 ASN A 971
REMARK 465 TYR A 972
REMARK 465 LYS A 973
REMARK 465 SER A 974
REMARK 465 PHE A 975
REMARK 465 LEU A 976
REMARK 465 GLY A 977
REMARK 465 ILE A 978
REMARK 465 ASN A 979
REMARK 465 HIS A 1089
REMARK 465 LEU A 1090
REMARK 465 VAL A 1091
REMARK 465 LEU A 1092
REMARK 465 GLY A 1093
REMARK 465 ILE A 1094
REMARK 465 LYS A 1095
REMARK 465 GLN A 1096
REMARK 465 GLY A 1097
REMARK 465 GLU A 1098
REMARK 465 LYS A 1099
REMARK 465 HIS A 1100
REMARK 465 SER A 1101
REMARK 465 ALA A 1102
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 LYS A 457 CG CD CE NZ
REMARK 470 HIS A 525 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 980 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 918 CD GLU A 918 OE2 0.081
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 SER A 147 40.90 -90.84
REMARK 500 GLN A 148 -53.98 -139.76
REMARK 500 HIS A 169 -0.32 -147.58
REMARK 500 HIS A 199 58.68 35.70
REMARK 500 LYS A 213 5.72 -65.92
REMARK 500 ASN A 217 82.24 36.92
REMARK 500 ARG A 226 -111.73 -88.99
REMARK 500 SER A 227 -72.79 -111.59
REMARK 500 ASP A 239 91.54 -66.49
REMARK 500 LEU A 281 77.48 -103.35
REMARK 500 LEU A 379 -140.13 -125.14
REMARK 500 ASP A 470 -172.47 -69.23
REMARK 500 PHE A 578 31.93 -97.77
REMARK 500 ARG A 579 -67.03 -20.44
REMARK 500 ARG A 613 56.77 -112.08
REMARK 500 ARG A 614 63.32 -116.56
REMARK 500 THR A 726 -35.05 -39.45
REMARK 500 SER A 777 -81.42 -26.80
REMARK 500 GLN A 778 6.66 -158.22
REMARK 500 LEU A 823 33.42 -98.93
REMARK 500 SER A 824 -145.79 -121.69
REMARK 500 ASN A 825 -22.56 -171.63
REMARK 500 VAL A 896 -62.64 -92.65
REMARK 500 ASN A 898 -77.92 -71.43
REMARK 500 GLU A1049 23.78 -78.86
REMARK 500 TRP A1080 11.89 -140.07
REMARK 500 PHE A1087 22.35 -74.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2NQ A 1103
DBREF 3S2A A 144 1102 UNP P48736 PK3CG_HUMAN 144 1102
SEQADV 3S2A GLY A 143 UNP P48736 EXPRESSION TAG
SEQRES 1 A 960 GLY SER GLU GLU SER GLN ALA PHE GLN ARG GLN LEU THR
SEQRES 2 A 960 ALA LEU ILE GLY TYR ASP VAL THR ASP VAL SER ASN VAL
SEQRES 3 A 960 HIS ASP ASP GLU LEU GLU PHE THR ARG ARG GLY LEU VAL
SEQRES 4 A 960 THR PRO ARG MET ALA GLU VAL ALA SER ARG ASP PRO LYS
SEQRES 5 A 960 LEU TYR ALA MET HIS PRO TRP VAL THR SER LYS PRO LEU
SEQRES 6 A 960 PRO GLU TYR LEU TRP LYS LYS ILE ALA ASN ASN CYS ILE
SEQRES 7 A 960 PHE ILE VAL ILE HIS ARG SER THR THR SER GLN THR ILE
SEQRES 8 A 960 LYS VAL SER PRO ASP ASP THR PRO GLY ALA ILE LEU GLN
SEQRES 9 A 960 SER PHE PHE THR LYS MET ALA LYS LYS LYS SER LEU MET
SEQRES 10 A 960 ASP ILE PRO GLU SER GLN SER GLU GLN ASP PHE VAL LEU
SEQRES 11 A 960 ARG VAL CYS GLY ARG ASP GLU TYR LEU VAL GLY GLU THR
SEQRES 12 A 960 PRO ILE LYS ASN PHE GLN TRP VAL ARG HIS CYS LEU LYS
SEQRES 13 A 960 ASN GLY GLU GLU ILE HIS VAL VAL LEU ASP THR PRO PRO
SEQRES 14 A 960 ASP PRO ALA LEU ASP GLU VAL ARG LYS GLU GLU TRP PRO
SEQRES 15 A 960 LEU VAL ASP ASP CYS THR GLY VAL THR GLY TYR HIS GLU
SEQRES 16 A 960 GLN LEU THR ILE HIS GLY LYS ASP HIS GLU SER VAL PHE
SEQRES 17 A 960 THR VAL SER LEU TRP ASP CYS ASP ARG LYS PHE ARG VAL
SEQRES 18 A 960 LYS ILE ARG GLY ILE ASP ILE PRO VAL LEU PRO ARG ASN
SEQRES 19 A 960 THR ASP LEU THR VAL PHE VAL GLU ALA ASN ILE GLN HIS
SEQRES 20 A 960 GLY GLN GLN VAL LEU CYS GLN ARG ARG THR SER PRO LYS
SEQRES 21 A 960 PRO PHE THR GLU GLU VAL LEU TRP ASN VAL TRP LEU GLU
SEQRES 22 A 960 PHE SER ILE LYS ILE LYS ASP LEU PRO LYS GLY ALA LEU
SEQRES 23 A 960 LEU ASN LEU GLN ILE TYR CYS GLY LYS ALA PRO ALA LEU
SEQRES 24 A 960 SER SER LYS ALA SER ALA GLU SER PRO SER SER GLU SER
SEQRES 25 A 960 LYS GLY LYS VAL GLN LEU LEU TYR TYR VAL ASN LEU LEU
SEQRES 26 A 960 LEU ILE ASP HIS ARG PHE LEU LEU ARG ARG GLY GLU TYR
SEQRES 27 A 960 VAL LEU HIS MET TRP GLN ILE SER GLY LYS GLY GLU ASP
SEQRES 28 A 960 GLN GLY SER PHE ASN ALA ASP LYS LEU THR SER ALA THR
SEQRES 29 A 960 ASN PRO ASP LYS GLU ASN SER MET SER ILE SER ILE LEU
SEQRES 30 A 960 LEU ASP ASN TYR CYS HIS PRO ILE ALA LEU PRO LYS HIS
SEQRES 31 A 960 GLN PRO THR PRO ASP PRO GLU GLY ASP ARG VAL ARG ALA
SEQRES 32 A 960 GLU MET PRO ASN GLN LEU ARG LYS GLN LEU GLU ALA ILE
SEQRES 33 A 960 ILE ALA THR ASP PRO LEU ASN PRO LEU THR ALA GLU ASP
SEQRES 34 A 960 LYS GLU LEU LEU TRP HIS PHE ARG TYR GLU SER LEU LYS
SEQRES 35 A 960 HIS PRO LYS ALA TYR PRO LYS LEU PHE SER SER VAL LYS
SEQRES 36 A 960 TRP GLY GLN GLN GLU ILE VAL ALA LYS THR TYR GLN LEU
SEQRES 37 A 960 LEU ALA ARG ARG GLU VAL TRP ASP GLN SER ALA LEU ASP
SEQRES 38 A 960 VAL GLY LEU THR MET GLN LEU LEU ASP CYS ASN PHE SER
SEQRES 39 A 960 ASP GLU ASN VAL ARG ALA ILE ALA VAL GLN LYS LEU GLU
SEQRES 40 A 960 SER LEU GLU ASP ASP ASP VAL LEU HIS TYR LEU LEU GLN
SEQRES 41 A 960 LEU VAL GLN ALA VAL LYS PHE GLU PRO TYR HIS ASP SER
SEQRES 42 A 960 ALA LEU ALA ARG PHE LEU LEU LYS ARG GLY LEU ARG ASN
SEQRES 43 A 960 LYS ARG ILE GLY HIS PHE LEU PHE TRP PHE LEU ARG SER
SEQRES 44 A 960 GLU ILE ALA GLN SER ARG HIS TYR GLN GLN ARG PHE ALA
SEQRES 45 A 960 VAL ILE LEU GLU ALA TYR LEU ARG GLY CYS GLY THR ALA
SEQRES 46 A 960 MET LEU HIS ASP PHE THR GLN GLN VAL GLN VAL ILE GLU
SEQRES 47 A 960 MET LEU GLN LYS VAL THR LEU ASP ILE LYS SER LEU SER
SEQRES 48 A 960 ALA GLU LYS TYR ASP VAL SER SER GLN VAL ILE SER GLN
SEQRES 49 A 960 LEU LYS GLN LYS LEU GLU ASN LEU GLN ASN SER GLN LEU
SEQRES 50 A 960 PRO GLU SER PHE ARG VAL PRO TYR ASP PRO GLY LEU LYS
SEQRES 51 A 960 ALA GLY ALA LEU ALA ILE GLU LYS CYS LYS VAL MET ALA
SEQRES 52 A 960 SER LYS LYS LYS PRO LEU TRP LEU GLU PHE LYS CYS ALA
SEQRES 53 A 960 ASP PRO THR ALA LEU SER ASN GLU THR ILE GLY ILE ILE
SEQRES 54 A 960 PHE LYS HIS GLY ASP ASP LEU ARG GLN ASP MET LEU ILE
SEQRES 55 A 960 LEU GLN ILE LEU ARG ILE MET GLU SER ILE TRP GLU THR
SEQRES 56 A 960 GLU SER LEU ASP LEU CYS LEU LEU PRO TYR GLY CYS ILE
SEQRES 57 A 960 SER THR GLY ASP LYS ILE GLY MET ILE GLU ILE VAL LYS
SEQRES 58 A 960 ASP ALA THR THR ILE ALA LYS ILE GLN GLN SER THR VAL
SEQRES 59 A 960 GLY ASN THR GLY ALA PHE LYS ASP GLU VAL LEU ASN HIS
SEQRES 60 A 960 TRP LEU LYS GLU LYS SER PRO THR GLU GLU LYS PHE GLN
SEQRES 61 A 960 ALA ALA VAL GLU ARG PHE VAL TYR SER CYS ALA GLY TYR
SEQRES 62 A 960 CYS VAL ALA THR PHE VAL LEU GLY ILE GLY ASP ARG HIS
SEQRES 63 A 960 ASN ASP ASN ILE MET ILE THR GLU THR GLY ASN LEU PHE
SEQRES 64 A 960 HIS ILE ASP PHE GLY HIS ILE LEU GLY ASN TYR LYS SER
SEQRES 65 A 960 PHE LEU GLY ILE ASN LYS GLU ARG VAL PRO PHE VAL LEU
SEQRES 66 A 960 THR PRO ASP PHE LEU PHE VAL MET GLY THR SER GLY LYS
SEQRES 67 A 960 LYS THR SER PRO HIS PHE GLN LYS PHE GLN ASP ILE CYS
SEQRES 68 A 960 VAL LYS ALA TYR LEU ALA LEU ARG HIS HIS THR ASN LEU
SEQRES 69 A 960 LEU ILE ILE LEU PHE SER MET MET LEU MET THR GLY MET
SEQRES 70 A 960 PRO GLN LEU THR SER LYS GLU ASP ILE GLU TYR ILE ARG
SEQRES 71 A 960 ASP ALA LEU THR VAL GLY LYS ASN GLU GLU ASP ALA LYS
SEQRES 72 A 960 LYS TYR PHE LEU ASP GLN ILE GLU VAL CYS ARG ASP LYS
SEQRES 73 A 960 GLY TRP THR VAL GLN PHE ASN TRP PHE LEU HIS LEU VAL
SEQRES 74 A 960 LEU GLY ILE LYS GLN GLY GLU LYS HIS SER ALA
HET SO4 A 1 5
HET SO4 A 2 5
HET SO4 A 3 5
HET 2NQ A1103 34
HETNAM SO4 SULFATE ION
HETNAM 2NQ N-{2-CHLORO-5-[4-(MORPHOLIN-4-YL)QUINOLIN-6-YL]PYRIDIN-
HETNAM 2 2NQ 3-YL}-4-FLUOROBENZENESULFONAMIDE
FORMUL 2 SO4 3(O4 S 2-)
FORMUL 5 2NQ C24 H20 CL F N4 O3 S
FORMUL 6 HOH *29(H2 O)
HELIX 1 1 GLU A 145 GLY A 159 1 15
HELIX 2 2 ASP A 171 LEU A 180 1 10
HELIX 3 3 LEU A 180 ARG A 191 1 12
HELIX 4 4 ASP A 192 HIS A 199 1 8
HELIX 5 5 PRO A 208 LYS A 213 1 6
HELIX 6 6 THR A 240 ILE A 244 5 5
HELIX 7 7 PRO A 286 ASN A 289 5 4
HELIX 8 8 PHE A 290 GLY A 300 1 11
HELIX 9 9 ASP A 312 GLU A 317 5 6
HELIX 10 10 TRP A 355 CYS A 357 5 3
HELIX 11 11 LYS A 421 LEU A 423 5 3
HELIX 12 12 ASN A 498 THR A 503 5 6
HELIX 13 13 PRO A 548 THR A 561 1 14
HELIX 14 14 THR A 568 PHE A 578 1 11
HELIX 15 15 PHE A 578 LEU A 583 1 6
HELIX 16 16 LYS A 584 LYS A 587 5 4
HELIX 17 17 ALA A 588 SER A 594 1 7
HELIX 18 18 GLN A 600 ALA A 612 1 13
HELIX 19 19 ARG A 614 SER A 620 1 7
HELIX 20 20 ASP A 623 LEU A 630 1 8
HELIX 21 21 ASP A 637 GLU A 649 1 13
HELIX 22 22 GLU A 652 ALA A 666 1 15
HELIX 23 23 VAL A 667 GLU A 670 5 4
HELIX 24 24 SER A 675 ARG A 687 1 13
HELIX 25 25 ASN A 688 SER A 706 1 19
HELIX 26 26 TYR A 709 GLY A 725 1 17
HELIX 27 27 GLY A 725 LEU A 752 1 28
HELIX 28 28 SER A 760 GLN A 778 1 19
HELIX 29 29 ILE A 798 CYS A 801 5 4
HELIX 30 30 LEU A 838 GLU A 858 1 21
HELIX 31 31 ILE A 888 VAL A 896 1 9
HELIX 32 32 GLU A 905 LYS A 914 1 10
HELIX 33 33 THR A 917 GLY A 943 1 27
HELIX 34 34 HIS A 948 ASP A 950 5 3
HELIX 35 35 THR A 988 GLY A 996 1 9
HELIX 36 36 SER A 1003 HIS A 1022 1 20
HELIX 37 37 HIS A 1023 MET A 1039 1 17
HELIX 38 38 SER A 1044 GLU A 1049 1 6
HELIX 39 39 TYR A 1050 LEU A 1055 1 6
HELIX 40 40 ASN A 1060 GLY A 1079 1 20
HELIX 41 41 TRP A 1080 PHE A 1087 1 8
SHEET 1 A 4 SER A 230 VAL A 235 0
SHEET 2 A 4 ILE A 220 HIS A 225 -1 N ILE A 222 O ILE A 233
SHEET 3 A 4 ILE A 303 ASP A 308 1 O ILE A 303 N VAL A 223
SHEET 4 A 4 VAL A 271 VAL A 274 -1 N VAL A 271 O ASP A 308
SHEET 1 B 2 VAL A 352 SER A 353 0
SHEET 2 B 2 ILE A 527 ALA A 528 1 O ALA A 528 N VAL A 352
SHEET 1 C 4 GLU A 407 LYS A 419 0
SHEET 2 C 4 LYS A 360 ASP A 369 -1 N PHE A 361 O ILE A 418
SHEET 3 C 4 SER A 515 LEU A 520 -1 O SER A 517 N GLY A 367
SHEET 4 C 4 GLY A 478 HIS A 483 -1 N GLY A 478 O LEU A 520
SHEET 1 D 3 GLN A 392 ARG A 398 0
SHEET 2 D 3 THR A 380 HIS A 389 -1 N ALA A 385 O ARG A 397
SHEET 3 D 3 LYS A 402 PRO A 403 -1 O LYS A 402 N VAL A 381
SHEET 1 E 5 GLN A 392 ARG A 398 0
SHEET 2 E 5 THR A 380 HIS A 389 -1 N ALA A 385 O ARG A 397
SHEET 3 E 5 LEU A 428 GLY A 436 -1 O LEU A 428 N GLN A 388
SHEET 4 E 5 GLN A 459 LEU A 467 -1 O LEU A 466 N LEU A 429
SHEET 5 E 5 TRP A 485 GLN A 486 -1 O TRP A 485 N TYR A 463
SHEET 1 F 4 PHE A 783 VAL A 785 0
SHEET 2 F 4 ASP A 788 LEU A 796 -1 O ALA A 793 N PHE A 783
SHEET 3 F 4 LEU A 811 CYS A 817 -1 O LYS A 816 N GLY A 794
SHEET 4 F 4 LYS A 802 VAL A 803 -1 N LYS A 802 O TRP A 812
SHEET 1 G 6 PHE A 783 VAL A 785 0
SHEET 2 G 6 ASP A 788 LEU A 796 -1 O ALA A 793 N PHE A 783
SHEET 3 G 6 LEU A 811 CYS A 817 -1 O LYS A 816 N GLY A 794
SHEET 4 G 6 ILE A 828 HIS A 834 -1 O ILE A 828 N PHE A 815
SHEET 5 G 6 ILE A 876 GLU A 880 -1 O ILE A 879 N ILE A 831
SHEET 6 G 6 CYS A 869 GLY A 873 -1 N THR A 872 O ILE A 876
SHEET 1 H 3 ALA A 885 THR A 887 0
SHEET 2 H 3 ILE A 952 THR A 955 -1 O ILE A 954 N THR A 886
SHEET 3 H 3 LEU A 960 HIS A 962 -1 O PHE A 961 N MET A 953
SITE 1 AC1 5 PRO A 206 LEU A 207 TRP A 212 LYS A 288
SITE 2 AC1 5 LYS A1066
SITE 1 AC2 4 HOH A 28 TRP A 576 ARG A 579 LYS A 606
SITE 1 AC3 5 LEU A 657 PHE A 694 PHE A 698 GLN A 846
SITE 2 AC3 5 ARG A 849
SITE 1 AC4 13 HOH A 24 PRO A 810 ILE A 831 LYS A 833
SITE 2 AC4 13 TYR A 867 ILE A 879 GLU A 880 VAL A 882
SITE 3 AC4 13 ASP A 950 ASN A 951 MET A 953 ILE A 963
SITE 4 AC4 13 ASP A 964
CRYST1 144.465 68.169 107.347 90.00 94.80 90.00 C 1 2 1 4
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 0.006922 0.000000 0.000581 0.00000
SCALE2 0.000000 0.014669 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009348 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
