HEADER TRANSFERASE/INHIBITOR 16-MAR-06 2CHW
TITLE A PHARMACOLOGICAL MAP OF THE PI3-K FAMILY DEFINES A ROLE FOR P110
TITLE 2 ALPHA IN SIGNALING: THE STRUCTURE OF COMPLEX OF PHOSPHOINOSITIDE 3-
TITLE 3 KINASE GAMMA WITH INHIBITOR PIK-39
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: HUMAN PI-3K GAMMA CATALYTIC SUBUNIT, RESIDUES 144-1102;
COMPND 6 SYNONYM: PHOSPHOINOSITIDE 3-KINASE, PI3-KINASE P110 SUBUNIT GAMMA,
COMPND 7 PTDINS-3-KINASE P110, PI3K, PI3KGAMMA;
COMPND 8 EC: 2.7.1.137, 2.7.1.153;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PVL1393
KEYWDS TRANSFERASE/INHIBITOR, COMPLEX TRANSFERASE-INHIBITOR,
KEYWDS 2 PHOSPHOINOSITIDE, KINASE, LIPID, INHIBITOR, 3-KINASE, SIGNALING,
KEYWDS 3 QUINAZOLINONE, TRANSFERASE, TRANSFERASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.A.KNIGHT,B.GONZALEZ,M.E.FELDMAN,E.R.ZUNDER,D.D.GOLDENBERG,
AUTHOR 2 O.WILLIAMS,R.LOEWITH,D.STOKOE,A.BALLA,B.TOTH,T.BALLA,W.A.WEISS,
AUTHOR 3 R.L.WILLIAMS,K.M.SHOKAT
REVDAT 4 13-DEC-23 2CHW 1 REMARK
REVDAT 3 16-OCT-19 2CHW 1 REMARK
REVDAT 2 24-FEB-09 2CHW 1 VERSN
REVDAT 1 22-MAY-06 2CHW 0
JRNL AUTH Z.A.KNIGHT,B.GONZALEZ,M.E.FELDMAN,E.R.ZUNDER,D.D.GOLDENBERG,
JRNL AUTH 2 O.WILLIAMS,R.LOEWITH,D.STOKOE,A.BALLA,B.TOTH,T.BALLA,
JRNL AUTH 3 W.A.WEISS,R.L.WILLIAMS,K.M.SHOKAT
JRNL TITL A PHARMACOLOGICAL MAP OF THE PI3-K FAMILY DEFINES A ROLE FOR
JRNL TITL 2 P110ALPHA IN SIGNALING
JRNL REF CELL(CAMBRIDGE,MASS.) V. 125 733 2006
JRNL REFN ISSN 0092-8674
JRNL PMID 16647110
JRNL DOI 10.1016/J.CELL.2006.03.035
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 30150
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) : 0.240
REMARK 3 R VALUE (WORKING SET) : 0.237
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1295
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2191
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3410
REMARK 3 BIN FREE R VALUE SET COUNT : 94
REMARK 3 BIN FREE R VALUE : 0.4060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6807
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 8
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.28000
REMARK 3 B22 (A**2) : 1.87000
REMARK 3 B33 (A**2) : -0.68000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.52000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.983
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.376
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.355
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.088
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.889
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6988 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9455 ; 1.419 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 832 ; 6.724 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 326 ;40.485 ;24.233
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1268 ;20.775 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;17.625 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1059 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5205 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3371 ; 0.242 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4770 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 235 ; 0.172 ; 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): 27 ; 0.212 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.188 ; 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): 4288 ; 0.562 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6799 ; 0.984 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3076 ; 1.286 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2656 ; 2.015 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2CHW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1290028178.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JAN-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : TORROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, TRUNCATE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31445
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 62.140
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.680
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.45000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.150
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1E8Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOUR DIFFUSION 1 MICROLITER PROTEIN
REMARK 280 PLUS 1 MICROLITER RESERVOIR RESERVOIR: 17% PEG 4000, 250 MM
REMARK 280 AMMONIUM SULFATE AND 100 MM TRIS PH 7.5 PROTEIN: 4 MG/ML IN 0.5
REMARK 280 MM AMMONIUM SULFATE, 20 MM TRIS PH 7.2, 1% ETHYLENE GLYCOL, 0.02%
REMARK 280 CHAPS AND 5 MM DTT, PH 7.50, VAPOR DIFFUSION
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 71.90200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.76150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 71.90200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.76150
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: PQS
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 MET A 143
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 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 SER A 353
REMARK 465 LEU A 354
REMARK 465 TRP A 355
REMARK 465 ASP A 356
REMARK 465 GLY A 436
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 LYS A 457
REMARK 465 VAL A 458
REMARK 465 ARG A 459
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 LEU A 529
REMARK 465 PRO A 530
REMARK 465 LYS A 531
REMARK 465 HIS A 532
REMARK 465 GLN A 533
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 ILE A 968
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 LYS A 980
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 465 HIS A 1103
REMARK 465 HIS A 1104
REMARK 465 HIS A 1105
REMARK 465 HIS A 1106
REMARK 465 HIS A 1107
REMARK 465 HIS A 1108
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 GLU A 322 CB CG CD OE1 OE2
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 LYS A 364 CE LYS A 364 NZ 0.309
REMARK 500 LYS A 364 C LYS A 364 O 0.123
REMARK 500 LYS A 364 C ILE A 365 N 0.167
REMARK 500 ARG A 366 CG ARG A 366 CD 0.256
REMARK 500 ARG A 366 NE ARG A 366 CZ 0.141
REMARK 500 ARG A 366 CZ ARG A 366 NH1 0.229
REMARK 500 ARG A 366 C ARG A 366 O 0.136
REMARK 500 GLY A 367 C GLY A 367 O 0.097
REMARK 500 THR A 405 CB THR A 405 OG1 0.177
REMARK 500 GLU A 407 CD GLU A 407 OE1 0.086
REMARK 500 GLU A 407 CD GLU A 407 OE2 0.073
REMARK 500 TRP A 410 NE1 TRP A 410 CE2 0.090
REMARK 500 GLU A 918 CG GLU A 918 CD 0.142
REMARK 500 GLU A 918 CD GLU A 918 OE1 0.102
REMARK 500 LYS A1008 CB LYS A1008 CG 0.175
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 ARG A 366 NE - CZ - NH1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG A 366 NE - CZ - NH2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 LEU A 575 CA - CB - CG ANGL. DEV. = 14.9 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 153 -70.29 -59.94
REMARK 500 LEU A 154 -38.72 -38.24
REMARK 500 ASN A 167 49.57 -97.65
REMARK 500 HIS A 199 56.78 39.65
REMARK 500 LYS A 213 1.51 -59.67
REMARK 500 ILE A 215 69.27 -107.89
REMARK 500 ALA A 216 41.27 -76.64
REMARK 500 ASN A 217 13.59 -174.67
REMARK 500 ARG A 226 -100.50 -106.28
REMARK 500 SER A 227 -90.04 -77.92
REMARK 500 PRO A 237 -36.24 -39.30
REMARK 500 ILE A 244 -29.98 -158.56
REMARK 500 ALA A 253 -98.13 -77.53
REMARK 500 ILE A 287 -19.23 -45.56
REMARK 500 LYS A 298 -33.47 -38.58
REMARK 500 ASP A 312 105.94 -43.12
REMARK 500 PRO A 313 -1.97 -57.18
REMARK 500 ASP A 316 40.84 -100.82
REMARK 500 LEU A 379 -123.46 -111.52
REMARK 500 GLU A 406 -8.32 -58.08
REMARK 500 TRP A 410 -48.49 -134.69
REMARK 500 LYS A 501 -3.99 -47.17
REMARK 500 ASP A 509 78.08 -65.11
REMARK 500 PRO A 526 -124.15 -105.50
REMARK 500 PHE A 578 44.96 -108.17
REMARK 500 LEU A 611 -0.92 -56.51
REMARK 500 ARG A 613 42.34 -107.74
REMARK 500 ALA A 754 -168.35 -74.80
REMARK 500 LYS A 756 99.08 -47.42
REMARK 500 ASP A 758 -39.85 -140.84
REMARK 500 VAL A 759 63.03 66.59
REMARK 500 SER A 761 -34.08 -38.29
REMARK 500 ASN A 776 -103.71 -77.39
REMARK 500 GLN A 778 -56.56 -120.25
REMARK 500 PRO A 780 150.29 -45.11
REMARK 500 ASP A 788 80.07 -152.65
REMARK 500 ILE A 798 -37.13 -36.10
REMARK 500 LEU A 838 -7.16 -57.31
REMARK 500 CYS A 863 29.37 45.59
REMARK 500 LYS A 875 34.70 39.53
REMARK 500 ASN A 898 77.68 -150.24
REMARK 500 THR A 899 43.87 -145.16
REMARK 500 GLU A 918 0.18 -55.50
REMARK 500 PHE A 965 42.44 -80.01
REMARK 500 LYS A1001 171.80 -57.44
REMARK 500 PRO A1040 -84.72 -39.74
REMARK 500 SER A1044 35.38 -60.60
REMARK 500 LYS A1045 -90.02 -167.59
REMARK 500 GLU A1046 -38.64 -38.08
REMARK 500 GLU A1049 24.51 -71.12
REMARK 500
REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS.
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 039 A2093
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E8Y RELATED DB: PDB
REMARK 900 STRUCTURE DETERMINANTS OF PHOSPHOINOSITIDE 3- KINASE INHIBITION BY
REMARK 900 WORTMANNIN, LY294002, QUERCETIN, MYRICETIN AND STAUROSPORINE
REMARK 900 RELATED ID: 1E8Z RELATED DB: PDB
REMARK 900 STRUCTURE DETERMINANTS OF PHOSPHOINOSITIDE 3- KINASE INHIBITION BY
REMARK 900 WORTMANNIN, LY294002, QUERCETIN, MYRICETIN AND STAUROSPORINE
REMARK 900 RELATED ID: 1HE8 RELATED DB: PDB
REMARK 900 RAS G12V - PI 3-KINASE GAMMA COMPLEX
REMARK 900 RELATED ID: 2A4Z RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PI3KGAMMA COMPLEXED WITH AS604850
REMARK 900 RELATED ID: 2A5U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PI3KGAMMA COMPLEXED WITH AS605240
REMARK 900 RELATED ID: 2CHX RELATED DB: PDB
REMARK 900 A PHARMACOLOGICAL MAP OF THE PI3-K FAMILY DEFINES A ROLE FOR
REMARK 900 P110ALPHA IN SIGNALING : THE STRUCTURE OF COMPLEX OF
REMARK 900 PHOSPHOINOSITIDE 3-KINASE GAMMA WITH INHIBITOR PIK-90
REMARK 900 RELATED ID: 2CHZ RELATED DB: PDB
REMARK 900 A PHARMACOLOGICAL MAP OF THE PI3-K FAMILY DEFINES A ROLE FOR
REMARK 900 P110ALPHA IN SIGNALING : THE STRUCTURE OF COMPLEX OF
REMARK 900 PHOSPHOINOSITIDE 3-KINASE GAMMA WITH INHIBITOR PIK-93.
DBREF 2CHW A 143 143 PDB 2CHW 2CHW 143 143
DBREF 2CHW A 144 1102 UNP P48736 PK3CG_HUMAN 143 1101
DBREF 2CHW A 1103 1108 PDB 2CHW 2CHW 1103 1108
SEQRES 1 A 966 MET SER GLU GLU SER GLN ALA PHE GLN ARG GLN LEU THR
SEQRES 2 A 966 ALA LEU ILE GLY TYR ASP VAL THR ASP VAL SER ASN VAL
SEQRES 3 A 966 HIS ASP ASP GLU LEU GLU PHE THR ARG ARG GLY LEU VAL
SEQRES 4 A 966 THR PRO ARG MET ALA GLU VAL ALA SER ARG ASP PRO LYS
SEQRES 5 A 966 LEU TYR ALA MET HIS PRO TRP VAL THR SER LYS PRO LEU
SEQRES 6 A 966 PRO GLU TYR LEU TRP LYS LYS ILE ALA ASN ASN CYS ILE
SEQRES 7 A 966 PHE ILE VAL ILE HIS ARG SER THR THR SER GLN THR ILE
SEQRES 8 A 966 LYS VAL SER PRO ASP ASP THR PRO GLY ALA ILE LEU GLN
SEQRES 9 A 966 SER PHE PHE THR LYS MET ALA LYS LYS LYS SER LEU MET
SEQRES 10 A 966 ASP ILE PRO GLU SER GLN SER GLU GLN ASP PHE VAL LEU
SEQRES 11 A 966 ARG VAL CYS GLY ARG ASP GLU TYR LEU VAL GLY GLU THR
SEQRES 12 A 966 PRO ILE LYS ASN PHE GLN TRP VAL ARG HIS CYS LEU LYS
SEQRES 13 A 966 ASN GLY GLU GLU ILE HIS VAL VAL LEU ASP THR PRO PRO
SEQRES 14 A 966 ASP PRO ALA LEU ASP GLU VAL ARG LYS GLU GLU TRP PRO
SEQRES 15 A 966 LEU VAL ASP ASP CYS THR GLY VAL THR GLY TYR HIS GLU
SEQRES 16 A 966 GLN LEU THR ILE HIS GLY LYS ASP HIS GLU SER VAL PHE
SEQRES 17 A 966 THR VAL SER LEU TRP ASP CYS ASP ARG LYS PHE ARG VAL
SEQRES 18 A 966 LYS ILE ARG GLY ILE ASP ILE PRO VAL LEU PRO ARG ASN
SEQRES 19 A 966 THR ASP LEU THR VAL PHE VAL GLU ALA ASN ILE GLN HIS
SEQRES 20 A 966 GLY GLN GLN VAL LEU CYS GLN ARG ARG THR SER PRO LYS
SEQRES 21 A 966 PRO PHE THR GLU GLU VAL LEU TRP ASN VAL TRP LEU GLU
SEQRES 22 A 966 PHE SER ILE LYS ILE LYS ASP LEU PRO LYS GLY ALA LEU
SEQRES 23 A 966 LEU ASN LEU GLN ILE TYR CYS GLY LYS ALA PRO ALA LEU
SEQRES 24 A 966 SER SER LYS ALA SER ALA GLU SER PRO SER SER GLU SER
SEQRES 25 A 966 LYS GLY LYS VAL ARG LEU LEU TYR TYR VAL ASN LEU LEU
SEQRES 26 A 966 LEU ILE ASP HIS ARG PHE LEU LEU ARG ARG GLY GLU TYR
SEQRES 27 A 966 VAL LEU HIS MET TRP GLN ILE SER GLY LYS GLY GLU ASP
SEQRES 28 A 966 GLN GLY SER PHE ASN ALA ASP LYS LEU THR SER ALA THR
SEQRES 29 A 966 ASN PRO ASP LYS GLU ASN SER MET SER ILE SER ILE LEU
SEQRES 30 A 966 LEU ASP ASN TYR CYS HIS PRO ILE ALA LEU PRO LYS HIS
SEQRES 31 A 966 GLN PRO THR PRO ASP PRO GLU GLY ASP ARG VAL ARG ALA
SEQRES 32 A 966 GLU MET PRO ASN GLN LEU ARG LYS GLN LEU GLU ALA ILE
SEQRES 33 A 966 ILE ALA THR ASP PRO LEU ASN PRO LEU THR ALA GLU ASP
SEQRES 34 A 966 LYS GLU LEU LEU TRP HIS PHE ARG TYR GLU SER LEU LYS
SEQRES 35 A 966 HIS PRO LYS ALA TYR PRO LYS LEU PHE SER SER VAL LYS
SEQRES 36 A 966 TRP GLY GLN GLN GLU ILE VAL ALA LYS THR TYR GLN LEU
SEQRES 37 A 966 LEU ALA ARG ARG GLU VAL TRP ASP GLN SER ALA LEU ASP
SEQRES 38 A 966 VAL GLY LEU THR MET GLN LEU LEU ASP CYS ASN PHE SER
SEQRES 39 A 966 ASP GLU ASN VAL ARG ALA ILE ALA VAL GLN LYS LEU GLU
SEQRES 40 A 966 SER LEU GLU ASP ASP ASP VAL LEU HIS TYR LEU LEU GLN
SEQRES 41 A 966 LEU VAL GLN ALA VAL LYS PHE GLU PRO TYR HIS ASP SER
SEQRES 42 A 966 ALA LEU ALA ARG PHE LEU LEU LYS ARG GLY LEU ARG ASN
SEQRES 43 A 966 LYS ARG ILE GLY HIS PHE LEU PHE TRP PHE LEU ARG SER
SEQRES 44 A 966 GLU ILE ALA GLN SER ARG HIS TYR GLN GLN ARG PHE ALA
SEQRES 45 A 966 VAL ILE LEU GLU ALA TYR LEU ARG GLY CYS GLY THR ALA
SEQRES 46 A 966 MET LEU HIS ASP PHE THR GLN GLN VAL GLN VAL ILE GLU
SEQRES 47 A 966 MET LEU GLN LYS VAL THR LEU ASP ILE LYS SER LEU SER
SEQRES 48 A 966 ALA GLU LYS TYR ASP VAL SER SER GLN VAL ILE SER GLN
SEQRES 49 A 966 LEU LYS GLN LYS LEU GLU ASN LEU GLN ASN SER GLN LEU
SEQRES 50 A 966 PRO GLU SER PHE ARG VAL PRO TYR ASP PRO GLY LEU LYS
SEQRES 51 A 966 ALA GLY ALA LEU ALA ILE GLU LYS CYS LYS VAL MET ALA
SEQRES 52 A 966 SER LYS LYS LYS PRO LEU TRP LEU GLU PHE LYS CYS ALA
SEQRES 53 A 966 ASP PRO THR ALA LEU SER ASN GLU THR ILE GLY ILE ILE
SEQRES 54 A 966 PHE LYS HIS GLY ASP ASP LEU ARG GLN ASP MET LEU ILE
SEQRES 55 A 966 LEU GLN ILE LEU ARG ILE MET GLU SER ILE TRP GLU THR
SEQRES 56 A 966 GLU SER LEU ASP LEU CYS LEU LEU PRO TYR GLY CYS ILE
SEQRES 57 A 966 SER THR GLY ASP LYS ILE GLY MET ILE GLU ILE VAL LYS
SEQRES 58 A 966 ASP ALA THR THR ILE ALA LYS ILE GLN GLN SER THR VAL
SEQRES 59 A 966 GLY ASN THR GLY ALA PHE LYS ASP GLU VAL LEU ASN HIS
SEQRES 60 A 966 TRP LEU LYS GLU LYS SER PRO THR GLU GLU LYS PHE GLN
SEQRES 61 A 966 ALA ALA VAL GLU ARG PHE VAL TYR SER CYS ALA GLY TYR
SEQRES 62 A 966 CYS VAL ALA THR PHE VAL LEU GLY ILE GLY ASP ARG HIS
SEQRES 63 A 966 ASN ASP ASN ILE MET ILE THR GLU THR GLY ASN LEU PHE
SEQRES 64 A 966 HIS ILE ASP PHE GLY HIS ILE LEU GLY ASN TYR LYS SER
SEQRES 65 A 966 PHE LEU GLY ILE ASN LYS GLU ARG VAL PRO PHE VAL LEU
SEQRES 66 A 966 THR PRO ASP PHE LEU PHE VAL MET GLY THR SER GLY LYS
SEQRES 67 A 966 LYS THR SER PRO HIS PHE GLN LYS PHE GLN ASP ILE CYS
SEQRES 68 A 966 VAL LYS ALA TYR LEU ALA LEU ARG HIS HIS THR ASN LEU
SEQRES 69 A 966 LEU ILE ILE LEU PHE SER MET MET LEU MET THR GLY MET
SEQRES 70 A 966 PRO GLN LEU THR SER LYS GLU ASP ILE GLU TYR ILE ARG
SEQRES 71 A 966 ASP ALA LEU THR VAL GLY LYS ASN GLU GLU ASP ALA LYS
SEQRES 72 A 966 LYS TYR PHE LEU ASP GLN ILE GLU VAL CYS ARG ASP LYS
SEQRES 73 A 966 GLY TRP THR VAL GLN PHE ASN TRP PHE LEU HIS LEU VAL
SEQRES 74 A 966 LEU GLY ILE LYS GLN GLY GLU LYS HIS SER ALA HIS HIS
SEQRES 75 A 966 HIS HIS HIS HIS
HET 039 A2093 31
HETNAM 039 2-((9H-PURIN-6-YLTHIO)METHYL)-5-CHLORO-3-(2-
HETNAM 2 039 METHOXYPHENYL)QUINAZOLIN-4(3H)-ONE
HETSYN 039 PIK-39
FORMUL 2 039 C21 H15 CL N6 O2 S
FORMUL 3 HOH *8(H2 O)
HELIX 1 1 SER A 144 GLY A 159 1 16
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 241 PHE A 249 1 9
HELIX 7 7 PRO A 286 ASN A 289 5 4
HELIX 8 8 PHE A 290 ASN A 299 1 10
HELIX 9 9 ASN A 498 THR A 503 5 6
HELIX 10 10 PRO A 548 THR A 561 1 14
HELIX 11 11 THR A 568 PHE A 578 1 11
HELIX 12 12 PHE A 578 LYS A 584 1 7
HELIX 13 13 HIS A 585 LYS A 587 5 3
HELIX 14 14 ALA A 588 SER A 594 1 7
HELIX 15 15 GLN A 600 LEU A 611 1 12
HELIX 16 16 ARG A 614 SER A 620 1 7
HELIX 17 17 ASP A 623 LEU A 631 1 9
HELIX 18 18 ASP A 637 GLU A 649 1 13
HELIX 19 19 GLU A 652 ALA A 666 1 15
HELIX 20 20 VAL A 667 GLU A 670 5 4
HELIX 21 21 SER A 675 ASN A 688 1 14
HELIX 22 22 ASN A 688 ALA A 704 1 17
HELIX 23 23 SER A 706 GLY A 725 1 20
HELIX 24 24 GLY A 725 LEU A 752 1 28
HELIX 25 25 SER A 760 ASN A 776 1 17
HELIX 26 26 ASP A 837 THR A 857 1 21
HELIX 27 27 ILE A 888 GLY A 897 1 10
HELIX 28 28 GLU A 905 LYS A 914 1 10
HELIX 29 29 THR A 917 LEU A 942 1 26
HELIX 30 30 HIS A 948 ASP A 950 5 3
HELIX 31 31 THR A 988 GLY A 996 1 9
HELIX 32 32 SER A 1003 ARG A 1021 1 19
HELIX 33 33 HIS A 1023 MET A 1039 1 17
HELIX 34 34 ASP A 1047 GLU A 1049 5 3
HELIX 35 35 TYR A 1050 LEU A 1055 1 6
HELIX 36 36 ASN A 1060 GLY A 1079 1 20
HELIX 37 37 TRP A 1080 HIS A 1089 1 10
SHEET 1 AA 4 SER A 230 VAL A 235 0
SHEET 2 AA 4 ILE A 220 HIS A 225 -1 O ILE A 220 N VAL A 235
SHEET 3 AA 4 ILE A 303 ASP A 308 1 O ILE A 303 N VAL A 223
SHEET 4 AA 4 VAL A 271 VAL A 274 -1 O VAL A 271 N ASP A 308
SHEET 1 AB 4 GLU A 407 LYS A 419 0
SHEET 2 AB 4 LYS A 360 ASP A 369 -1 O PHE A 361 N PHE A 416
SHEET 3 AB 4 SER A 515 LEU A 520 -1 O SER A 515 N ASP A 369
SHEET 4 AB 4 GLY A 478 VAL A 481 -1 O GLY A 478 N LEU A 520
SHEET 1 AC 5 GLN A 392 ARG A 398 0
SHEET 2 AC 5 PHE A 382 HIS A 389 -1 O ALA A 385 N ARG A 397
SHEET 3 AC 5 LEU A 428 TYR A 434 -1 O LEU A 428 N GLN A 388
SHEET 4 AC 5 TYR A 462 LEU A 467 -1 O TYR A 462 N ILE A 433
SHEET 5 AC 5 TRP A 485 GLN A 486 -1 O TRP A 485 N TYR A 463
SHEET 1 AD 4 PHE A 783 VAL A 785 0
SHEET 2 AD 4 ASP A 788 LEU A 796 -1 N ASP A 788 O VAL A 785
SHEET 3 AD 4 LEU A 811 CYS A 817 -1 O LYS A 816 N GLY A 794
SHEET 4 AD 4 LYS A 802 VAL A 803 -1 O LYS A 802 N TRP A 812
SHEET 1 AE 6 PHE A 783 VAL A 785 0
SHEET 2 AE 6 ASP A 788 LEU A 796 -1 N ASP A 788 O VAL A 785
SHEET 3 AE 6 LEU A 811 CYS A 817 -1 O LYS A 816 N GLY A 794
SHEET 4 AE 6 ILE A 828 HIS A 834 -1 O ILE A 828 N PHE A 815
SHEET 5 AE 6 ILE A 876 GLU A 880 -1 O GLY A 877 N LYS A 833
SHEET 6 AE 6 CYS A 869 GLY A 873 -1 O ILE A 870 N MET A 878
SHEET 1 AF 3 ALA A 885 THR A 887 0
SHEET 2 AF 3 ILE A 952 THR A 955 -1 O ILE A 954 N THR A 886
SHEET 3 AF 3 LEU A 960 HIS A 962 -1 O PHE A 961 N MET A 953
SITE 1 AC1 13 MET A 804 PRO A 810 LEU A 811 TRP A 812
SITE 2 AC1 13 ILE A 831 ILE A 879 GLU A 880 ILE A 881
SITE 3 AC1 13 VAL A 882 ALA A 885 THR A 887 MET A 953
SITE 4 AC1 13 ILE A 963
CRYST1 143.804 67.523 106.311 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 0.006954 0.000000 0.000663 0.00000
SCALE2 0.000000 0.014810 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009449 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
