HEADER TRANSFERASE 23-AUG-16 5T27
TITLE MPI3KD IN COMPLEX WITH 5D
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 SYNONYM: PTDINS-3-KINASE SUBUNIT DELTA,PHOSPHATIDYLINOSITOL 4,5-
COMPND 6 BISPHOSPHATE 3-KINASE 110 KDA CATALYTIC SUBUNIT DELTA,P110DELTA;
COMPND 7 EC: 2.7.1.153;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PIK3CD;
SOURCE 6 EXPRESSION_SYSTEM: INSECT CELL EXPRESSION VECTOR PTIE1;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 266783
KEYWDS MI3KD, INHIBITOR, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.PETERSEN,I.TERSTIGE,M.PERRY,T.SVENSSON,C.TYRCHAN,H.LINDMARK,L.OSTER
REVDAT 1 19-APR-17 5T27 0
JRNL AUTH I.TERSTIEGE,M.PERRY,J.PETERSEN,C.TYRCHAN,T.SVENSSON,
JRNL AUTH 2 H.LINDMARK,L.OSTER
JRNL TITL DISCOVERY OF TRIAZOLE AMINOPYRAZINES AS A HIGHLY POTENT AND
JRNL TITL 2 SELECTIVE SERIES OF PI3K DELTA INHIBITORS.
JRNL REF BIOORG. MED. CHEM. LETT. V. 27 679 2017
JRNL REFN ESSN 1464-3405
JRNL PMID 28017532
JRNL DOI 10.1016/J.BMCL.2016.11.004
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.6
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 31107
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) : 0.254
REMARK 3 R VALUE (WORKING SET) : 0.252
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1575
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 16
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.69
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.86
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2841
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2810
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2685
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.49
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 156
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6628
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 18
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 68.84
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.03770
REMARK 3 B22 (A**2) : -0.64150
REMARK 3 B33 (A**2) : 2.67910
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.450
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.763
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.349
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.813
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.357
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.897
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.862
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6815 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 9193 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2406 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 168 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 971 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6815 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 848 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 7556 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.05
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.31
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.02
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5T27 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1000223532.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31300
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 56.350
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8000
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) : 2.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.52000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50% ETHYLENE GLYCOL/PEG 8000, 0.1 M
REMARK 280 CARBOXYLIC ACIDS MIX, 0.1 M BUFFER SYSTEM 2 PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 109.92200
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 109.92200
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 31.89500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 71.83250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 31.89500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 71.83250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 109.92200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 31.89500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 71.83250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 109.92200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 31.89500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 71.83250
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 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 PRO A 231
REMARK 465 LEU A 232
REMARK 465 VAL A 233
REMARK 465 GLU A 234
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 CYS A 366
REMARK 465 SER A 367
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 GLU A 451
REMARK 465 PRO A 480
REMARK 465 HIS A 481
REMARK 465 HIS A 500
REMARK 465 GLY A 501
REMARK 465 GLU A 502
REMARK 465 ARG A 503
REMARK 465 GLY A 504
REMARK 465 ARG A 505
REMARK 465 ILE A 506
REMARK 465 GLN A 510A
REMARK 465 LEU A 510B
REMARK 465 GLN A 510C
REMARK 465 ARG A 518
REMARK 465 GLY A 519
REMARK 465 SER A 520
REMARK 465 GLY A 521
REMARK 465 SER A 842
REMARK 465 ASN A 843
REMARK 465 MET A 844
REMARK 465 ALA A 845
REMARK 465 ALA A 846
REMARK 465 LYS A 920
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 ASN A 926
REMARK 465 ARG A 927
REMARK 465 GLU A 928
REMARK 465 LEU A 1004
REMARK 465 GLY A 1005
REMARK 465 LYS A 1006
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 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 O MET A 424 NZ LYS A 433 2.06
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 ARG A 229 102.23 60.49
REMARK 500 HIS A 247 52.28 -96.13
REMARK 500 LEU A 270 153.65 -47.75
REMARK 500 ILE A 328 -83.11 -73.19
REMARK 500 LYS A 332 165.29 58.69
REMARK 500 VAL A 333 179.53 -45.31
REMARK 500 ASN A 334 141.50 105.45
REMARK 500 MET A 387 30.40 -98.73
REMARK 500 VAL A 459 32.53 -95.16
REMARK 500 GLU A 508 -59.85 73.11
REMARK 500 SER A 675 86.45 -162.28
REMARK 500 HIS A 730 62.20 65.20
REMARK 500 ASP A 736 113.00 -166.43
REMARK 500 GLU A 742 -103.11 -87.38
REMARK 500 LYS A 757 61.97 33.35
REMARK 500 LEU A 808 26.56 -79.98
REMARK 500 GLN A 838 5.12 -68.04
REMARK 500 ASP A 911 62.23 36.66
REMARK 500 LEU A 989 59.20 -144.34
REMARK 500 SER A1026 82.52 -66.04
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 74F A 1101
DBREF 5T27 A 106 1044 UNP O35904 PK3CD_MOUSE 106 1043
SEQADV 5T27 GLN A 510A UNP O35904 INSERTION
SEQRES 1 A 939 GLY ASP ARG VAL LYS LYS LEU ILE ASN SER GLN ILE SER
SEQRES 2 A 939 LEU LEU ILE GLY LYS GLY LEU HIS GLU PHE ASP SER LEU
SEQRES 3 A 939 ARG ASP PRO GLU VAL ASN ASP PHE ARG THR LYS MET ARG
SEQRES 4 A 939 GLN PHE CYS GLU GLU ALA ALA ALA HIS ARG GLN GLN LEU
SEQRES 5 A 939 GLY TRP VAL GLU TRP LEU GLN TYR SER PHE PRO LEU GLN
SEQRES 6 A 939 LEU GLU PRO SER ALA ARG GLY TRP ARG ALA GLY LEU LEU
SEQRES 7 A 939 ARG VAL SER ASN ARG ALA LEU LEU VAL ASN VAL LYS PHE
SEQRES 8 A 939 GLU GLY SER GLU GLU SER PHE THR PHE GLN VAL SER THR
SEQRES 9 A 939 LYS ASP MET PRO LEU ALA LEU MET ALA CYS ALA LEU ARG
SEQRES 10 A 939 LYS LYS ALA THR VAL PHE ARG GLN PRO LEU VAL GLU GLN
SEQRES 11 A 939 PRO GLU GLU TYR ALA LEU GLN VAL ASN GLY ARG HIS GLU
SEQRES 12 A 939 TYR LEU TYR GLY ASN TYR PRO LEU CYS HIS PHE GLN TYR
SEQRES 13 A 939 ILE CYS SER CYS LEU HIS SER GLY LEU THR PRO HIS LEU
SEQRES 14 A 939 THR MET VAL HIS SER SER SER ILE LEU ALA MET ARG ASP
SEQRES 15 A 939 GLU GLN SER ASN PRO ALA PRO GLN VAL GLN LYS PRO ARG
SEQRES 16 A 939 ALA LYS PRO PRO PRO ILE PRO ALA LYS LYS PRO SER SER
SEQRES 17 A 939 VAL SER LEU TRP SER LEU GLU GLN PRO PHE SER ILE GLU
SEQRES 18 A 939 LEU ILE GLU GLY ARG LYS VAL ASN ALA ASP GLU ARG MET
SEQRES 19 A 939 LYS LEU VAL VAL GLN ALA GLY LEU PHE HIS GLY ASN GLU
SEQRES 20 A 939 MET LEU CYS LYS THR VAL SER SER SER GLU VAL ASN VAL
SEQRES 21 A 939 CYS SER GLU PRO VAL TRP LYS GLN ARG LEU GLU PHE ASP
SEQRES 22 A 939 ILE SER VAL CYS ASP LEU PRO ARG MET ALA ARG LEU CYS
SEQRES 23 A 939 PHE ALA LEU TYR ALA VAL VAL GLU LYS ALA LYS LYS ALA
SEQRES 24 A 939 ARG SER THR LYS LYS LYS SER LYS LYS ALA ASP CYS PRO
SEQRES 25 A 939 ILE ALA TRP ALA ASN LEU MET LEU PHE ASP TYR LYS ASP
SEQRES 26 A 939 GLN LEU LYS THR GLY GLU ARG CYS LEU TYR MET TRP PRO
SEQRES 27 A 939 SER VAL PRO ASP GLU LYS GLY GLU LEU LEU ASN PRO ALA
SEQRES 28 A 939 GLY THR VAL ARG GLY ASN PRO ASN THR GLU SER ALA ALA
SEQRES 29 A 939 ALA LEU VAL ILE TYR LEU PRO GLU VAL ALA PRO HIS PRO
SEQRES 30 A 939 VAL TYR PHE PRO ALA LEU GLU LYS ILE LEU GLU LEU GLY
SEQRES 31 A 939 ARG HIS GLY GLU ARG GLY ARG ILE THR GLU GLU GLU GLN
SEQRES 32 A 939 LEU GLN LEU ARG GLU ILE LEU GLU ARG ARG GLY SER GLY
SEQRES 33 A 939 GLU LEU TYR GLU HIS GLU LYS ASP LEU VAL TRP LYS MET
SEQRES 34 A 939 ARG HIS GLU VAL GLN GLU HIS PHE PRO GLU ALA LEU ALA
SEQRES 35 A 939 ARG LEU LEU LEU VAL THR LYS TRP ASN LYS HIS GLU ASP
SEQRES 36 A 939 VAL ALA GLN MET LEU TYR LEU LEU CYS SER TRP PRO GLU
SEQRES 37 A 939 LEU PRO VAL LEU SER ALA LEU GLU LEU LEU ASP PHE SER
SEQRES 38 A 939 PHE PRO ASP CYS TYR VAL GLY SER PHE ALA ILE LYS SER
SEQRES 39 A 939 LEU ARG LYS LEU THR ASP ASP GLU LEU PHE GLN TYR LEU
SEQRES 40 A 939 LEU GLN LEU VAL GLN VAL LEU LYS TYR GLU SER TYR LEU
SEQRES 41 A 939 ASP CYS GLU LEU THR LYS PHE LEU LEU GLY ARG ALA LEU
SEQRES 42 A 939 ALA ASN ARG LYS ILE GLY HIS PHE LEU PHE TRP HIS LEU
SEQRES 43 A 939 ARG SER GLU MET HIS VAL PRO SER VAL ALA LEU ARG PHE
SEQRES 44 A 939 GLY LEU ILE MET GLU ALA TYR CYS ARG GLY SER THR HIS
SEQRES 45 A 939 HIS MET LYS VAL LEU MET LYS GLN GLY GLU ALA LEU SER
SEQRES 46 A 939 LYS LEU LYS ALA LEU ASN ASP PHE VAL LYS VAL SER SER
SEQRES 47 A 939 GLN LYS THR THR LYS PRO GLN THR LYS GLU MET MET HIS
SEQRES 48 A 939 MET CYS MET ARG GLN GLU THR TYR MET GLU ALA LEU SER
SEQRES 49 A 939 HIS LEU GLN SER PRO LEU ASP PRO SER THR LEU LEU GLU
SEQRES 50 A 939 GLU VAL CYS VAL GLU GLN CYS THR PHE MET ASP SER LYS
SEQRES 51 A 939 MET LYS PRO LEU TRP ILE MET TYR SER SER GLU GLU ALA
SEQRES 52 A 939 GLY SER ALA GLY ASN VAL GLY ILE ILE PHE LYS ASN GLY
SEQRES 53 A 939 ASP ASP LEU ARG GLN ASP MET LEU THR LEU GLN MET ILE
SEQRES 54 A 939 GLN LEU MET ASP VAL LEU TRP LYS GLN GLU GLY LEU ASP
SEQRES 55 A 939 LEU ARG MET THR PRO TYR GLY CYS LEU PRO THR GLY ASP
SEQRES 56 A 939 ARG THR GLY LEU ILE GLU VAL VAL LEU HIS SER ASP THR
SEQRES 57 A 939 ILE ALA ASN ILE GLN LEU ASN LYS SER ASN MET ALA ALA
SEQRES 58 A 939 THR ALA ALA PHE ASN LYS ASP ALA LEU LEU ASN TRP LEU
SEQRES 59 A 939 LYS SER LYS ASN PRO GLY GLU ALA LEU ASP ARG ALA ILE
SEQRES 60 A 939 GLU GLU PHE THR LEU SER CYS ALA GLY TYR CYS VAL ALA
SEQRES 61 A 939 THR TYR VAL LEU GLY ILE GLY ASP ARG HIS SER ASP ASN
SEQRES 62 A 939 ILE MET ILE ARG GLU SER GLY GLN LEU PHE HIS ILE ASP
SEQRES 63 A 939 PHE GLY HIS PHE LEU GLY ASN PHE LYS THR LYS PHE GLY
SEQRES 64 A 939 ILE ASN ARG GLU ARG VAL PRO PHE ILE LEU THR TYR ASP
SEQRES 65 A 939 PHE VAL HIS VAL ILE GLN GLN GLY LYS THR ASN ASN SER
SEQRES 66 A 939 GLU LYS PHE GLU ARG PHE ARG GLY TYR CYS GLU ARG ALA
SEQRES 67 A 939 TYR THR ILE LEU ARG ARG HIS GLY LEU LEU PHE LEU HIS
SEQRES 68 A 939 LEU PHE ALA LEU MET ARG ALA ALA GLY LEU PRO GLU LEU
SEQRES 69 A 939 SER CYS SER LYS ASP ILE GLN TYR LEU LYS ASP SER LEU
SEQRES 70 A 939 ALA LEU GLY LYS THR GLU GLU GLU ALA LEU LYS HIS PHE
SEQRES 71 A 939 ARG VAL LYS PHE ASN GLU ALA LEU ARG GLU SER TRP LYS
SEQRES 72 A 939 THR LYS VAL ASN TRP LEU ALA HIS ASN VAL SER LYS ASP
SEQRES 73 A 939 ASN ARG GLN
HET 74F A1101 30
HETNAM 74F 3-(BENZOTRIAZOL-1-YL)-5-[1-METHYL-5-[(1~{S})-1-
HETNAM 2 74F MORPHOLIN-4-YLETHYL]-1,2,4-TRIAZOL-3-YL]PYRAZIN-2-
HETNAM 3 74F AMINE
FORMUL 2 74F C19 H22 N10 O
FORMUL 3 HOH *18(H2 O)
HELIX 1 AA1 VAL A 109 GLY A 122 1 14
HELIX 2 AA2 LEU A 125 LEU A 131 1 7
HELIX 3 AA3 ASP A 133 GLN A 156 1 24
HELIX 4 AA4 GLY A 158 PHE A 167 1 10
HELIX 5 AA5 MET A 212 PHE A 228 1 17
HELIX 6 AA6 GLN A 235 GLU A 237 5 3
HELIX 7 AA7 PRO A 255 HIS A 258 5 4
HELIX 8 AA8 PHE A 259 GLY A 269 1 11
HELIX 9 AA9 SER A 279 GLN A 289 1 11
HELIX 10 AB1 CYS A 382 LEU A 384 5 3
HELIX 11 AB2 ALA A 487 ARG A 496 1 10
HELIX 12 AB3 GLU A 508 LEU A 515 1 8
HELIX 13 AB4 TYR A 524 MET A 534 1 11
HELIX 14 AB5 MET A 534 PHE A 542 1 9
HELIX 15 AB6 ALA A 545 LEU A 551 1 7
HELIX 16 AB7 LYS A 557 CYS A 569 1 13
HELIX 17 AB8 PRO A 575 LEU A 582 1 8
HELIX 18 AB9 ASP A 589 ARG A 601 1 13
HELIX 19 AC1 THR A 604 VAL A 618 1 15
HELIX 20 AC2 CYS A 627 ASN A 640 1 14
HELIX 21 AC3 ASN A 640 SER A 653 1 14
HELIX 22 AC4 VAL A 657 GLY A 674 1 18
HELIX 23 AC5 SER A 675 THR A 706 1 32
HELIX 24 AC6 THR A 707 ARG A 720 1 14
HELIX 25 AC7 GLN A 721 LEU A 728 1 8
HELIX 26 AC8 VAL A 746 CYS A 749 5 4
HELIX 27 AC9 LEU A 784 GLN A 803 1 20
HELIX 28 AD1 ILE A 834 GLN A 838 1 5
HELIX 29 AD2 PHE A 850 ASN A 863 1 14
HELIX 30 AD3 ALA A 867 GLY A 890 1 24
HELIX 31 AD4 THR A 935 GLN A 943 1 9
HELIX 32 AD5 ASN A 949 HIS A 970 1 22
HELIX 33 AD6 HIS A 970 ARG A 982 1 13
HELIX 34 AD7 ALA A 983 GLY A 985 5 3
HELIX 35 AD8 CYS A 991 ALA A 1003 1 13
HELIX 36 AD9 GLU A 1008 SER A 1026 1 19
SHEET 1 AA1 5 SER A 202 SER A 208 0
SHEET 2 AA1 5 ALA A 189 PHE A 196 -1 N LEU A 190 O VAL A 207
SHEET 3 AA1 5 HIS A 273 HIS A 278 1 O LEU A 274 N ASN A 193
SHEET 4 AA1 5 TYR A 239 VAL A 243 -1 N ALA A 240 O VAL A 277
SHEET 5 AA1 5 TYR A 249 LEU A 250 -1 O LEU A 250 N LEU A 241
SHEET 1 AA2 4 VAL A 370 SER A 380 0
SHEET 2 AA2 4 PRO A 322 GLU A 329 -1 N PHE A 323 O PHE A 377
SHEET 3 AA2 4 ALA A 470 LEU A 475 -1 O VAL A 472 N GLU A 329
SHEET 4 AA2 4 GLY A 435 TYR A 440 -1 N ARG A 437 O ILE A 473
SHEET 1 AA3 3 GLU A 352 MET A 353 0
SHEET 2 AA3 3 LYS A 340 HIS A 349 -1 N HIS A 349 O GLU A 352
SHEET 3 AA3 3 VAL A 363 ASN A 364 -1 O VAL A 363 N LEU A 341
SHEET 1 AA4 5 VAL A 358 SER A 359 0
SHEET 2 AA4 5 LYS A 340 HIS A 349 -1 N ALA A 345 O VAL A 358
SHEET 3 AA4 5 ARG A 389 VAL A 397 -1 O ARG A 389 N PHE A 348
SHEET 4 AA4 5 CYS A 416 MET A 424 -1 O LEU A 423 N LEU A 390
SHEET 5 AA4 5 TRP A 442 PRO A 443 -1 O TRP A 442 N TRP A 420
SHEET 1 AA5 2 LEU A 731 SER A 733 0
SHEET 2 AA5 2 ASP A 736 LEU A 741 -1 O LEU A 741 N LEU A 731
SHEET 1 AA6 3 GLU A 743 VAL A 744 0
SHEET 2 AA6 3 LEU A 759 SER A 764 -1 O SER A 764 N GLU A 743
SHEET 3 AA6 3 THR A 750 PHE A 751 -1 N THR A 750 O TRP A 760
SHEET 1 AA7 5 GLU A 743 VAL A 744 0
SHEET 2 AA7 5 LEU A 759 SER A 764 -1 O SER A 764 N GLU A 743
SHEET 3 AA7 5 GLY A 775 ASN A 780 -1 O ILE A 776 N ILE A 761
SHEET 4 AA7 5 THR A 822 GLU A 826 -1 O ILE A 825 N ILE A 777
SHEET 5 AA7 5 CYS A 815 GLY A 819 -1 N LEU A 816 O LEU A 824
SHEET 1 AA8 3 SER A 831 THR A 833 0
SHEET 2 AA8 3 ILE A 899 ARG A 902 -1 O ILE A 901 N ASP A 832
SHEET 3 AA8 3 LEU A 907 HIS A 909 -1 O PHE A 908 N MET A 900
CISPEP 1 THR A 507 GLU A 508 0 4.22
SITE 1 AC1 12 MET A 752 TRP A 760 ILE A 777 LYS A 779
SITE 2 AC1 12 GLU A 826 VAL A 827 VAL A 828 SER A 831
SITE 3 AC1 12 ASP A 832 ASN A 836 MET A 900 ILE A 910
CRYST1 63.790 143.665 219.844 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 0.015676 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006961 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004549 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
