HEADER TRANSFERASE/TRANSFERASE INHIBITOR 11-JAN-11 3QAR
TITLE CRYSTAL STRUCTURE OF PI3K-GAMMA IN COMPLEX WITH TRIAZINE-BENZIMIDAZOLE
TITLE 2 32
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_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS INHIBITOR, P110, KINASE, TRANSFERASE, ATP-BINDING, P84, P101,
KEYWDS 2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.WHITTINGTON,J.TANG,P.YAKOWEC
REVDAT 2 13-SEP-23 3QAR 1 REMARK SEQADV
REVDAT 1 30-MAR-11 3QAR 0
JRNL AUTH E.A.PETERSON,P.S.ANDREWS,X.BE,A.A.BOEZIO,T.L.BUSH,A.C.CHENG,
JRNL AUTH 2 J.R.COATS,A.E.COLLETTI,K.W.COPELAND,M.DUPONT,R.GRACEFFA,
JRNL AUTH 3 B.GRUBINSKA,J.C.HARMANGE,J.L.KIM,E.L.MULLADY,P.OLIVIERI,
JRNL AUTH 4 L.B.SCHENKEL,M.K.STANTON,Y.TEFFERA,D.A.WHITTINGTON,T.CAI,
JRNL AUTH 5 D.S.LA
JRNL TITL DISCOVERY OF TRIAZINE-BENZIMIDAZOLES AS SELECTIVE INHIBITORS
JRNL TITL 2 OF MTOR.
JRNL REF BIOORG.MED.CHEM.LETT. V. 21 2064 2011
JRNL REFN ISSN 0960-894X
JRNL PMID 21376583
JRNL DOI 10.1016/J.BMCL.2011.02.007
REMARK 2
REMARK 2 RESOLUTION. 2.65 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) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 27988
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 : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1754
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) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1937
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.3090
REMARK 3 BIN FREE R VALUE SET COUNT : 130
REMARK 3 BIN FREE R VALUE : 0.3560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6750
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 21
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.80000
REMARK 3 B22 (A**2) : 4.79000
REMARK 3 B33 (A**2) : -1.18000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.99000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.905
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.392
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.316
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 32.030
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6932 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9382 ; 0.987 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 824 ; 5.230 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 322 ;37.883 ;24.317
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1251 ;15.865 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 40 ;15.737 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1055 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5140 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3066 ; 0.185 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4690 ; 0.298 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 190 ; 0.129 ; 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 ; 0.106 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.035 ; 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): 4296 ; 0.340 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6744 ; 0.603 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3016 ; 0.640 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2638 ; 1.049 ; 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 147 A 248
REMARK 3 ORIGIN FOR THE GROUP (A): 21.3206 -13.9653 27.8279
REMARK 3 T TENSOR
REMARK 3 T11: -0.2365 T22: -0.2075
REMARK 3 T33: 0.1679 T12: -0.0102
REMARK 3 T13: -0.0196 T23: 0.0574
REMARK 3 L TENSOR
REMARK 3 L11: 4.4075 L22: 0.7701
REMARK 3 L33: 2.3007 L12: -0.4327
REMARK 3 L13: 0.4148 L23: -0.3772
REMARK 3 S TENSOR
REMARK 3 S11: 0.1475 S12: -0.0890 S13: -1.1456
REMARK 3 S21: -0.0791 S22: 0.1571 S23: 0.4659
REMARK 3 S31: 0.2400 S32: -0.4121 S33: -0.3046
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): 12.1527 -12.6488 30.8796
REMARK 3 T TENSOR
REMARK 3 T11: -0.3541 T22: -0.0053
REMARK 3 T33: 0.1793 T12: -0.1016
REMARK 3 T13: 0.0444 T23: 0.2447
REMARK 3 L TENSOR
REMARK 3 L11: 5.2863 L22: 3.1151
REMARK 3 L33: 6.0561 L12: -1.2852
REMARK 3 L13: 0.1031 L23: 2.0361
REMARK 3 S TENSOR
REMARK 3 S11: 0.2262 S12: -0.6031 S13: -0.8658
REMARK 3 S21: 0.0660 S22: 0.2489 S23: 0.4607
REMARK 3 S31: 0.1174 S32: -0.8829 S33: -0.4751
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 353 A 436
REMARK 3 ORIGIN FOR THE GROUP (A): 66.3791 -4.7813 14.6264
REMARK 3 T TENSOR
REMARK 3 T11: -0.2520 T22: 0.5435
REMARK 3 T33: -0.2428 T12: 0.0304
REMARK 3 T13: 0.0601 T23: -0.1008
REMARK 3 L TENSOR
REMARK 3 L11: 2.2728 L22: 3.1835
REMARK 3 L33: 4.3394 L12: 1.2656
REMARK 3 L13: -0.0444 L23: -1.4219
REMARK 3 S TENSOR
REMARK 3 S11: 0.1498 S12: 0.6713 S13: -0.0613
REMARK 3 S21: 0.0006 S22: -0.0907 S23: 0.0829
REMARK 3 S31: -0.2226 S32: 1.0049 S33: -0.0591
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): 56.7912 -8.0377 13.4640
REMARK 3 T TENSOR
REMARK 3 T11: -0.1677 T22: 0.4280
REMARK 3 T33: -0.2339 T12: 0.0872
REMARK 3 T13: 0.0901 T23: -0.2240
REMARK 3 L TENSOR
REMARK 3 L11: 4.0167 L22: 2.6779
REMARK 3 L33: 3.3910 L12: -0.6685
REMARK 3 L13: 1.7956 L23: -1.6374
REMARK 3 S TENSOR
REMARK 3 S11: 0.1091 S12: 0.9737 S13: -0.1517
REMARK 3 S21: -0.0391 S22: -0.0148 S23: -0.0337
REMARK 3 S31: -0.0350 S32: 0.8303 S33: -0.0943
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): 45.7779 -9.9919 33.8835
REMARK 3 T TENSOR
REMARK 3 T11: -0.0542 T22: -0.1159
REMARK 3 T33: 0.0061 T12: 0.0201
REMARK 3 T13: 0.0168 T23: -0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 3.6558 L22: 0.3906
REMARK 3 L33: 2.0267 L12: -0.3857
REMARK 3 L13: 1.8761 L23: 0.0134
REMARK 3 S TENSOR
REMARK 3 S11: 0.1318 S12: -0.0216 S13: -0.5108
REMARK 3 S21: 0.0434 S22: 0.0491 S23: 0.1430
REMARK 3 S31: 0.0087 S32: 0.1458 S33: -0.1809
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): 19.9768 5.2230 17.2371
REMARK 3 T TENSOR
REMARK 3 T11: -0.0472 T22: -0.0096
REMARK 3 T33: -0.0807 T12: 0.1034
REMARK 3 T13: 0.0170 T23: -0.0308
REMARK 3 L TENSOR
REMARK 3 L11: 2.7159 L22: 2.2156
REMARK 3 L33: 1.6305 L12: -1.1570
REMARK 3 L13: 1.0204 L23: -0.6745
REMARK 3 S TENSOR
REMARK 3 S11: 0.0618 S12: 0.3619 S13: -0.1574
REMARK 3 S21: -0.0699 S22: 0.0070 S23: 0.2923
REMARK 3 S31: -0.3624 S32: -0.1054 S33: -0.0688
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 1092
REMARK 3 ORIGIN FOR THE GROUP (A): 29.0442 19.4945 36.9226
REMARK 3 T TENSOR
REMARK 3 T11: 0.2232 T22: -0.1207
REMARK 3 T33: -0.0483 T12: 0.1692
REMARK 3 T13: -0.1613 T23: -0.1872
REMARK 3 L TENSOR
REMARK 3 L11: 3.3719 L22: 2.9599
REMARK 3 L33: 1.1615 L12: -1.3395
REMARK 3 L13: 1.0239 L23: -0.2999
REMARK 3 S TENSOR
REMARK 3 S11: -0.6696 S12: -0.3837 S13: 0.7332
REMARK 3 S21: 0.5220 S22: 0.2035 S23: -0.2247
REMARK 3 S31: -0.4246 S32: -0.1101 S33: 0.4661
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 3QAR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1000063408.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-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 : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97740
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29742
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.41400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: PDB ENTRY 1E8Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 21% PEG 3350, 0.1 M TRIS PH 7.3, 245
REMARK 280 MM AMMONIUM SULFATE, 5 MM EDTA, VAPOR DIFFUSION, TEMPERATURE 298K
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 71.91900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.00750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 71.91900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.00750
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 SER A 144
REMARK 465 GLU A 145
REMARK 465 GLU A 146
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 THR A 351
REMARK 465 VAL A 352
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 SER A 496
REMARK 465 TYR A 523
REMARK 465 CYS A 524
REMARK 465 HIS A 525
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 GLU A 755
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 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 LEU A 529 CG CD1 CD2
REMARK 470 LYS A 980 CG CD CE NZ
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 HIS A 199 54.34 39.00
REMARK 500 ARG A 226 -67.59 -103.03
REMARK 500 SER A 227 -83.44 -143.47
REMARK 500 LEU A 379 -159.62 -150.90
REMARK 500 ARG A 579 -59.62 -17.34
REMARK 500 ARG A 613 50.55 -110.78
REMARK 500 ARG A 614 50.74 -109.51
REMARK 500 ASN A 776 -76.46 -93.25
REMARK 500 SER A 782 113.24 -162.21
REMARK 500 ASP A 788 77.42 -153.17
REMARK 500 GLU A 956 4.13 -68.48
REMARK 500 ASP A 964 73.07 49.37
REMARK 500 HIS A 967 62.38 62.29
REMARK 500 ARG A 982 -161.11 -120.23
REMARK 500 LEU A1042 -109.22 -130.33
REMARK 500 THR A1043 73.95 49.33
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 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QAR A 1103
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QAQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PI3K-GAMMA IN COMPLEX WITH TRIAZINE-
REMARK 900 BENZIMIDAZOLE 1
DBREF 3QAR A 144 1102 UNP P48736 PK3CG_HUMAN 144 1102
SEQADV 3QAR 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 3 5
HET SO4 A 4 5
HET QAR A1103 23
HETNAM SO4 SULFATE ION
HETNAM QAR 1-(4-AMINO-6-METHYL-1,3,5-TRIAZIN-2-YL)-N-(1H-PYRAZOL-
HETNAM 2 QAR 3-YL)-1H-BENZIMIDAZOL-2-AMINE
HETSYN QAR 1-(4-AMINO-6-METHYL-1,3,5-TRIAZIN-2-YL)-N-(1H-PYRAZOL-
HETSYN 2 QAR 3-YL)-1H-BENZO[D]IMIDAZOL-2-AMINE
FORMUL 2 SO4 3(O4 S 2-)
FORMUL 5 QAR C14 H13 N9
FORMUL 6 HOH *21(H2 O)
HELIX 1 1 GLN A 148 GLY A 159 1 12
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 PRO A 286 ASN A 289 5 4
HELIX 7 7 PHE A 290 ASN A 299 1 10
HELIX 8 8 ASP A 312 GLU A 317 5 6
HELIX 9 9 SER A 353 CYS A 357 5 5
HELIX 10 10 LYS A 421 LEU A 423 5 3
HELIX 11 11 ASN A 498 THR A 503 5 6
HELIX 12 12 PRO A 548 THR A 561 1 14
HELIX 13 13 THR A 568 PHE A 578 1 11
HELIX 14 14 PHE A 578 LEU A 583 1 6
HELIX 15 15 LYS A 584 LYS A 587 5 4
HELIX 16 16 ALA A 588 SER A 594 1 7
HELIX 17 17 GLN A 600 ALA A 612 1 13
HELIX 18 18 ARG A 614 SER A 620 1 7
HELIX 19 19 ASP A 623 LEU A 630 1 8
HELIX 20 20 ASP A 637 GLU A 649 1 13
HELIX 21 21 GLU A 652 ALA A 666 1 15
HELIX 22 22 VAL A 667 GLU A 670 5 4
HELIX 23 23 SER A 675 ASN A 688 1 14
HELIX 24 24 ASN A 688 ALA A 704 1 17
HELIX 25 25 TYR A 709 ARG A 722 1 14
HELIX 26 26 GLY A 725 LEU A 752 1 28
HELIX 27 27 SER A 760 SER A 777 1 18
HELIX 28 28 ASP A 837 THR A 857 1 21
HELIX 29 29 ILE A 888 SER A 894 1 7
HELIX 30 30 GLU A 905 SER A 915 1 11
HELIX 31 31 THR A 917 GLY A 943 1 27
HELIX 32 32 THR A 988 MET A 995 1 8
HELIX 33 33 HIS A 1005 HIS A 1022 1 18
HELIX 34 34 HIS A 1023 MET A 1039 1 17
HELIX 35 35 SER A 1044 GLU A 1049 1 6
HELIX 36 36 GLU A 1049 LEU A 1055 1 7
HELIX 37 37 ASN A 1060 GLY A 1079 1 20
HELIX 38 38 TRP A 1080 LEU A 1090 1 11
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 220 O VAL A 235
SHEET 3 A 4 ILE A 303 ASP A 308 1 O VAL A 305 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 4 GLU A 407 LYS A 419 0
SHEET 2 B 4 LYS A 360 ASP A 369 -1 N PHE A 361 O PHE A 416
SHEET 3 B 4 SER A 515 LEU A 520 -1 O SER A 517 N GLY A 367
SHEET 4 B 4 GLY A 478 HIS A 483 -1 N GLY A 478 O LEU A 520
SHEET 1 C 3 GLN A 392 ARG A 398 0
SHEET 2 C 3 THR A 380 HIS A 389 -1 N ALA A 385 O ARG A 397
SHEET 3 C 3 LYS A 402 PRO A 403 -1 O LYS A 402 N VAL A 381
SHEET 1 D 4 GLN A 392 ARG A 398 0
SHEET 2 D 4 THR A 380 HIS A 389 -1 N ALA A 385 O ARG A 397
SHEET 3 D 4 LEU A 428 GLY A 436 -1 O LEU A 428 N GLN A 388
SHEET 4 D 4 GLN A 459 LEU A 467 -1 O LEU A 466 N LEU A 429
SHEET 1 E 4 PHE A 783 VAL A 785 0
SHEET 2 E 4 ASP A 788 LEU A 796 -1 O ALA A 793 N PHE A 783
SHEET 3 E 4 LEU A 811 CYS A 817 -1 O LYS A 816 N GLY A 794
SHEET 4 E 4 LYS A 802 VAL A 803 -1 N LYS A 802 O TRP A 812
SHEET 1 F 6 PHE A 783 VAL A 785 0
SHEET 2 F 6 ASP A 788 LEU A 796 -1 O ALA A 793 N PHE A 783
SHEET 3 F 6 LEU A 811 CYS A 817 -1 O LYS A 816 N GLY A 794
SHEET 4 F 6 ILE A 828 HIS A 834 -1 O PHE A 832 N LEU A 811
SHEET 5 F 6 ILE A 876 GLU A 880 -1 O ILE A 879 N ILE A 831
SHEET 6 F 6 CYS A 869 GLY A 873 -1 N ILE A 870 O MET A 878
SHEET 1 G 3 ALA A 885 THR A 887 0
SHEET 2 G 3 ILE A 952 THR A 955 -1 O ILE A 954 N THR A 886
SHEET 3 G 3 LEU A 960 HIS A 962 -1 O PHE A 961 N MET A 953
CISPEP 1 SER A 777 GLN A 778 0 1.84
SITE 1 AC1 4 PRO A 206 LEU A 207 TRP A 212 LYS A 288
SITE 1 AC2 3 TRP A 576 ARG A 579 LYS A 606
SITE 1 AC3 5 ARG A 947 HIS A 948 ASN A 951 TRP A1086
SITE 2 AC3 5 LEU A1090
SITE 1 AC4 12 ILE A 831 ASP A 836 ASP A 841 TYR A 867
SITE 2 AC4 12 ILE A 879 GLU A 880 ILE A 881 VAL A 882
SITE 3 AC4 12 LYS A 890 MET A 953 ILE A 963 ASP A 964
CRYST1 143.838 68.015 106.046 90.00 95.45 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 0.006952 0.000000 0.000663 0.00000
SCALE2 0.000000 0.014703 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009473 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
