HEADER TRANSFERASE 12-JUN-17 5O83
TITLE DISCOVERY OF CDZ173 (LENIOLISIB), REPRESENTING A STRUCTURALLY NOVEL
TITLE 2 CLASS OF PI3K DELTA-SELECTIVE INHIBITORS
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: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9-DE
KEYWDS KINASE, TRANSFERASE, PI3K DELTA, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GUTMANN,G.RUMMEL,B.SHRESTHA
REVDAT 3 16-OCT-19 5O83 1 REMARK
REVDAT 2 11-OCT-17 5O83 1 JRNL
REVDAT 1 20-SEP-17 5O83 0
JRNL AUTH K.HOEGENAUER,N.SOLDERMANN,F.ZECRI,R.S.STRANG,N.GRAVELEAU,
JRNL AUTH 2 R.M.WOLF,N.G.COOKE,A.B.SMITH,G.J.HOLLINGWORTH,J.BLANZ,
JRNL AUTH 3 S.GUTMANN,G.RUMMEL,A.LITTLEWOOD-EVANS,C.BURKHART
JRNL TITL DISCOVERY OF CDZ173 (LENIOLISIB), REPRESENTING A
JRNL TITL 2 STRUCTURALLY NOVEL CLASS OF PI3K DELTA-SELECTIVE INHIBITORS.
JRNL REF ACS MED CHEM LETT V. 8 975 2017
JRNL REFN ISSN 1948-5875
JRNL PMID 28947947
JRNL DOI 10.1021/ACSMEDCHEMLETT.7B00293
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 22803
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) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1141
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 : 11
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.04
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.23
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2980
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.3040
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2831
REMARK 3 BIN R VALUE (WORKING SET) : 0.3010
REMARK 3 BIN FREE R VALUE : 0.3640
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 149
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 : 5672
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 55
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 84.96
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.43830
REMARK 3 B22 (A**2) : -15.08370
REMARK 3 B33 (A**2) : 14.64540
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.10130
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.440
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 2.822
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.387
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.882
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.853
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5828 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7927 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1810 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 94 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 920 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5828 ; 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 : 796 ; 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 : 6471 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.00
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.21
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.09
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8717 -15.4765 -28.1273
REMARK 3 T TENSOR
REMARK 3 T11: -0.1270 T22: -0.1761
REMARK 3 T33: -0.1586 T12: -0.0674
REMARK 3 T13: 0.0260 T23: 0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 0.9457 L22: 0.6548
REMARK 3 L33: 1.7357 L12: 0.1785
REMARK 3 L13: -0.0148 L23: -0.2258
REMARK 3 S TENSOR
REMARK 3 S11: -0.0523 S12: -0.0412 S13: 0.1010
REMARK 3 S21: -0.0253 S22: -0.0510 S23: 0.0333
REMARK 3 S31: -0.0821 S32: 0.3318 S33: 0.1033
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5O83 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1200005346.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22803
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 58.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: EQUAL VOLUMES OF RESERVOIR SOLUTION
REMARK 280 (43.3 MM NANO4, 43.3 MM AS, 43.3 MM NA2HPO4, 20%GLYCEROL, 12%
REMARK 280 PEG4000, 0.1M IMIDAZOLE PH6.8) WERE MIXED WITH PROTEIN, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 290K
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 71.06000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.99500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 71.06000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.99500
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34240 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 GLN A 104
REMARK 465 GLY A 105
REMARK 465 GLY A 106
REMARK 465 ASP A 107
REMARK 465 ARG A 108
REMARK 465 SER A 174
REMARK 465 ALA A 175
REMARK 465 ARG A 176
REMARK 465 GLY A 177
REMARK 465 TRP A 178
REMARK 465 ARG A 179
REMARK 465 ALA A 180
REMARK 465 GLY A 181
REMARK 465 LEU A 182
REMARK 465 LEU A 183
REMARK 465 ARG A 184
REMARK 465 VAL A 185
REMARK 465 SER A 186
REMARK 465 PRO A 231
REMARK 465 LEU A 232
REMARK 465 VAL A 233
REMARK 465 GLU A 234
REMARK 465 GLY A 269
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 LEU A 316
REMARK 465 GLU A 326
REMARK 465 GLU A 337
REMARK 465 ARG A 338
REMARK 465 VAL A 363
REMARK 465 ASN A 364
REMARK 465 VAL A 365
REMARK 465 LYS A 372
REMARK 465 GLN A 373
REMARK 465 ARG A 374
REMARK 465 LEU A 375
REMARK 465 VAL A 398
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 LEU A 452
REMARK 465 PRO A 480
REMARK 465 HIS A 481
REMARK 465 GLY A 495
REMARK 465 ARG A 496
REMARK 465 HIS A 497
REMARK 465 GLY A 498
REMARK 465 GLU A 499
REMARK 465 ARG A 500
REMARK 465 GLY A 501
REMARK 465 ARG A 502
REMARK 465 ILE A 503
REMARK 465 THR A 504
REMARK 465 GLU A 505
REMARK 465 GLU A 506
REMARK 465 GLU A 507
REMARK 465 GLN A 508
REMARK 465 LEU A 509
REMARK 465 GLN A 510
REMARK 465 LEU A 511
REMARK 465 ARG A 512
REMARK 465 GLU A 513
REMARK 465 ILE A 514
REMARK 465 LEU A 515
REMARK 465 GLU A 516
REMARK 465 ARG A 517
REMARK 465 ARG A 518
REMARK 465 GLY A 519
REMARK 465 SER A 520
REMARK 465 GLY A 521
REMARK 465 GLU A 522
REMARK 465 LYS A 841
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 THR A 847
REMARK 465 PHE A 919
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 ARG A 929
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 VAL A 109 CG1 CG2
REMARK 470 LYS A 110 CG CD CE NZ
REMARK 470 LYS A 111 CG CD CE NZ
REMARK 470 LEU A 112 CG CD1 CD2
REMARK 470 ILE A 113 CG1 CG2 CD1
REMARK 470 SER A 115 OG
REMARK 470 ARG A 132 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 136 CG1 CG2
REMARK 470 ASP A 138 CG OD1 OD2
REMARK 470 LYS A 142 CG CD CE NZ
REMARK 470 ARG A 144 NE CZ NH1 NH2
REMARK 470 GLN A 145 CG CD OE1 NE2
REMARK 470 VAL A 160 CG1 CG2
REMARK 470 LEU A 163 CG CD1 CD2
REMARK 470 ASN A 187 CG OD1 ND2
REMARK 470 ARG A 188 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 190 CG CD1 CD2
REMARK 470 LEU A 191 CG CD1 CD2
REMARK 470 VAL A 192 CG1 CG2
REMARK 470 ASN A 193 CG OD1 ND2
REMARK 470 VAL A 194 CG1 CG2
REMARK 470 LYS A 195 CG CD CE NZ
REMARK 470 PHE A 196 CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 197 CG CD OE1 OE2
REMARK 470 SER A 199 OG
REMARK 470 GLU A 200 CG CD OE1 OE2
REMARK 470 GLU A 201 CG CD OE1 OE2
REMARK 470 SER A 202 OG
REMARK 470 PHE A 203 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 THR A 204 OG1 CG2
REMARK 470 PHE A 205 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 206 CG CD OE1 NE2
REMARK 470 VAL A 207 CG1 CG2
REMARK 470 SER A 208 OG
REMARK 470 LYS A 210 CG CD CE NZ
REMARK 470 ASP A 211 CG OD1 OD2
REMARK 470 LEU A 214 CD1 CD2
REMARK 470 LEU A 216 CG CD1 CD2
REMARK 470 LEU A 221 CG CD1 CD2
REMARK 470 ARG A 222 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 223 CG CD CE NZ
REMARK 470 LYS A 224 CG CD CE NZ
REMARK 470 THR A 226 OG1 CG2
REMARK 470 VAL A 227 CG1 CG2
REMARK 470 PHE A 228 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 229 NE CZ NH1 NH2
REMARK 470 GLN A 230 C O CB CG CD OE1 NE2
REMARK 470 GLN A 235 CG CD OE1 NE2
REMARK 470 GLU A 238 CG CD OE1 OE2
REMARK 470 ASN A 244 CG OD1 ND2
REMARK 470 ASN A 253 CG OD1 ND2
REMARK 470 LEU A 256 CG CD1 CD2
REMARK 470 CYS A 257 SG
REMARK 470 ILE A 262 CG1 CG2 CD1
REMARK 470 SER A 264 OG
REMARK 470 LEU A 266 CG CD1 CD2
REMARK 470 HIS A 267 CG ND1 CD2 CE1 NE2
REMARK 470 SER A 268 OG
REMARK 470 LEU A 270 CG CD1 CD2
REMARK 470 THR A 271 OG1 CG2
REMARK 470 VAL A 277 CG1 CG2
REMARK 470 SER A 279 OG
REMARK 470 SER A 281 OG
REMARK 470 ILE A 282 CD1
REMARK 470 LEU A 283 CD1 CD2
REMARK 470 GLU A 288 CG CD OE1 OE2
REMARK 470 GLN A 289 CG CD OE1 NE2
REMARK 470 SER A 290 OG
REMARK 470 TRP A 317 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 317 CZ3 CH2
REMARK 470 SER A 318 OG
REMARK 470 LEU A 319 CG CD1 CD2
REMARK 470 GLU A 320 CG CD OE1 OE2
REMARK 470 GLN A 321 CG CD OE1 NE2
REMARK 470 PRO A 322 CG CD
REMARK 470 SER A 324 OG
REMARK 470 ILE A 325 CG1 CG2 CD1
REMARK 470 ILE A 328 CG1 CG2 CD1
REMARK 470 GLU A 329 CG CD OE1 OE2
REMARK 470 LYS A 340 CG CD CE NZ
REMARK 470 LEU A 341 CG CD1 CD2
REMARK 470 VAL A 342 CG1 CG2
REMARK 470 VAL A 343 CG1 CG2
REMARK 470 GLN A 344 CD OE1 NE2
REMARK 470 LEU A 347 CG CD1 CD2
REMARK 470 GLU A 352 CG CD OE1 OE2
REMARK 470 LYS A 356 CG CD CE NZ
REMARK 470 THR A 357 OG1 CG2
REMARK 470 VAL A 358 CG1 CG2
REMARK 470 SER A 359 OG
REMARK 470 SER A 360 OG
REMARK 470 SER A 361 OG
REMARK 470 GLU A 362 CG CD OE1 OE2
REMARK 470 CYS A 366 SG
REMARK 470 SER A 367 OG
REMARK 470 VAL A 370 CG1 CG2
REMARK 470 GLU A 376 CG CD OE1 OE2
REMARK 470 PHE A 377 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A 378 CG OD1 OD2
REMARK 470 ILE A 379 CG1 CG2 CD1
REMARK 470 SER A 380 OG
REMARK 470 VAL A 381 CG1 CG2
REMARK 470 LEU A 390 CG CD1 CD2
REMARK 470 LEU A 394 CG CD1 CD2
REMARK 470 VAL A 397 CG1 CG2
REMARK 470 ASP A 415 CG OD1 OD2
REMARK 470 CYS A 416 SG
REMARK 470 LEU A 423 CG CD1 CD2
REMARK 470 LYS A 429 CG CD CE NZ
REMARK 470 ASP A 430 CG OD1 OD2
REMARK 470 LYS A 433 CG CD CE NZ
REMARK 470 THR A 434 OG1 CG2
REMARK 470 GLU A 436 CG CD OE1 OE2
REMARK 470 SER A 444 OG
REMARK 470 VAL A 445 CG1 CG2
REMARK 470 LEU A 453 CG CD1 CD2
REMARK 470 ARG A 460 CG CD NE CZ NH1 NH2
REMARK 470 THR A 465 OG1 CG2
REMARK 470 GLU A 466 CG CD OE1 OE2
REMARK 470 SER A 467 OG
REMARK 470 LEU A 471 CG CD1 CD2
REMARK 470 TYR A 474 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 475 CG CD1 CD2
REMARK 470 PRO A 476 CG CD
REMARK 470 GLU A 477 CG CD OE1 OE2
REMARK 470 VAL A 478 CG1 CG2
REMARK 470 PRO A 482 CG CD
REMARK 470 VAL A 483 CG1 CG2
REMARK 470 TYR A 484 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 488 CG CD1 CD2
REMARK 470 GLU A 489 CG CD OE1 OE2
REMARK 470 LYS A 490 CG CD CE NZ
REMARK 470 ILE A 491 CG1 CG2 CD1
REMARK 470 LEU A 492 CG CD1 CD2
REMARK 470 GLU A 493 CG CD OE1 OE2
REMARK 470 LEU A 523 CG CD1 CD2
REMARK 470 GLU A 525 CG CD OE1 OE2
REMARK 470 GLU A 527 CD OE1 OE2
REMARK 470 LYS A 528 CG CD CE NZ
REMARK 470 ASP A 529 CG OD1 OD2
REMARK 470 LEU A 530 CG CD1 CD2
REMARK 470 VAL A 531 CG1 CG2
REMARK 470 LYS A 533 CG CD CE NZ
REMARK 470 MET A 534 CG SD CE
REMARK 470 HIS A 536 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 537 CG CD OE1 OE2
REMARK 470 VAL A 538 CG1 CG2
REMARK 470 GLN A 539 CG CD OE1 NE2
REMARK 470 GLU A 540 CG CD OE1 OE2
REMARK 470 HIS A 541 CG ND1 CD2 CE1 NE2
REMARK 470 PHE A 542 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 548 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 549 CG CD1 CD2
REMARK 470 LEU A 551 CG CD1 CD2
REMARK 470 VAL A 552 CG1 CG2
REMARK 470 LYS A 557 CG CD CE NZ
REMARK 470 GLU A 559 CG CD OE1 OE2
REMARK 470 ASP A 560 CG OD1 OD2
REMARK 470 VAL A 561 CG1 CG2
REMARK 470 GLN A 563 OE1 NE2
REMARK 470 LEU A 565 CG CD1 CD2
REMARK 470 LEU A 568 CG CD1 CD2
REMARK 470 SER A 570 OG
REMARK 470 VAL A 576 CG1 CG2
REMARK 470 LEU A 580 CD1 CD2
REMARK 470 LEU A 583 CD1 CD2
REMARK 470 ASP A 584 CG OD1 OD2
REMARK 470 SER A 586 OG
REMARK 470 CYS A 590 SG
REMARK 470 VAL A 592 CG1 CG2
REMARK 470 SER A 594 OG
REMARK 470 ILE A 597 CG1 CG2 CD1
REMARK 470 LYS A 598 CG CD CE NZ
REMARK 470 ARG A 601 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 602 CG CD CE NZ
REMARK 470 ASP A 606 CG OD1 OD2
REMARK 470 GLU A 628 CG CD OE1 OE2
REMARK 470 LYS A 631 CG CD CE NZ
REMARK 470 ARG A 641 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 643 CG1 CG2 CD1
REMARK 470 GLU A 654 CD OE1 OE2
REMARK 470 VAL A 660 CG1 CG2
REMARK 470 SER A 675 OG
REMARK 470 THR A 676 OG1 CG2
REMARK 470 VAL A 701 CG1 CG2
REMARK 470 GLN A 704 CG CD OE1 NE2
REMARK 470 LYS A 705 CG CD CE NZ
REMARK 470 GLN A 710 CG CD OE1 NE2
REMARK 470 LYS A 712 CE NZ
REMARK 470 GLU A 713 CG CD OE1 OE2
REMARK 470 GLU A 722 CG CD OE1 OE2
REMARK 470 THR A 723 OG1 CG2
REMARK 470 GLU A 726 CD OE1 OE2
REMARK 470 GLU A 747 CG CD OE1 OE2
REMARK 470 GLN A 748 CG CD OE1 NE2
REMARK 470 SER A 754 OG
REMARK 470 LYS A 755 CG CD CE NZ
REMARK 470 LYS A 757 CD CE NZ
REMARK 470 SER A 764 OG
REMARK 470 GLU A 766 CG CD OE1 OE2
REMARK 470 GLU A 767 CG CD OE1 OE2
REMARK 470 SER A 770 OG
REMARK 470 GLN A 795 CG CD OE1 NE2
REMARK 470 LEU A 839 CG CD1 CD2
REMARK 470 ASN A 840 CG OD1 ND2
REMARK 470 LEU A 856 CG CD1 CD2
REMARK 470 SER A 861 OG
REMARK 470 GLU A 866 CG CD OE1 OE2
REMARK 470 ASP A 869 CG OD1 OD2
REMARK 470 ARG A 870 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 893 CG OD1 OD2
REMARK 470 SER A 896 OG
REMARK 470 ASP A 897 CG OD1 OD2
REMARK 470 ILE A 933 CG1 CG2 CD1
REMARK 470 LEU A 934 CG CD1 CD2
REMARK 470 THR A 935 OG1 CG2
REMARK 470 TYR A 936 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A 937 CG OD1 OD2
REMARK 470 VAL A 939 CG1 CG2
REMARK 470 THR A 947 OG1 CG2
REMARK 470 ASN A 948 CG OD1 ND2
REMARK 470 GLU A 951 CG CD OE1 OE2
REMARK 470 ARG A 955 NE CZ NH1 NH2
REMARK 470 LEU A 972 CG CD1 CD2
REMARK 470 GLU A 988 CG CD OE1 OE2
REMARK 470 SER A 990 OG
REMARK 470 LYS A 993 CG CD CE NZ
REMARK 470 ILE A 995 CG1 CG2 CD1
REMARK 470 LEU A1004 CG CD1 CD2
REMARK 470 GLU A1009 CG CD OE1 OE2
REMARK 470 LEU A1012 CG CD1 CD2
REMARK 470 LYS A1013 CG CD CE NZ
REMARK 470 VAL A1017 CG1 CG2
REMARK 470 LYS A1018 CG CD CE NZ
REMARK 470 ASN A1020 CG OD1 ND2
REMARK 470 ARG A1024 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1025 CG CD OE1 OE2
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 LYS A 123 118.12 -166.19
REMARK 500 ASN A 244 127.05 -36.51
REMARK 500 HIS A 247 49.00 -88.14
REMARK 500 ILE A 328 -111.39 -79.12
REMARK 500 MET A 387 48.36 -99.77
REMARK 500 MET A 534 37.24 -90.57
REMARK 500 SER A 675 67.04 -151.18
REMARK 500 GLU A 742 -98.80 -86.19
REMARK 500 THR A 750 -165.22 -168.28
REMARK 500 LYS A 757 63.81 36.57
REMARK 500 LEU A 808 41.34 -92.54
REMARK 500 ARG A 809 66.43 23.29
REMARK 500 ILE A 910 -72.57 -116.47
REMARK 500 PHE A 912 41.60 -102.23
REMARK 500 ASN A 949 82.44 -150.59
REMARK 500 LEU A 989 78.56 -154.55
REMARK 500 ALA A1003 58.67 37.14
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 9NQ A 1101
DBREF 5O83 A 106 1044 UNP O35904 PK3CD_MOUSE 106 1043
SEQADV 5O83 GLN A 104 UNP O35904 EXPRESSION TAG
SEQADV 5O83 GLY A 105 UNP O35904 EXPRESSION TAG
SEQADV 5O83 GLN A 508 UNP O35904 INSERTION
SEQRES 1 A 941 GLN GLY GLY ASP ARG VAL LYS LYS LEU ILE ASN SER GLN
SEQRES 2 A 941 ILE SER LEU LEU ILE GLY LYS GLY LEU HIS GLU PHE ASP
SEQRES 3 A 941 SER LEU ARG ASP PRO GLU VAL ASN ASP PHE ARG THR LYS
SEQRES 4 A 941 MET ARG GLN PHE CYS GLU GLU ALA ALA ALA HIS ARG GLN
SEQRES 5 A 941 GLN LEU GLY TRP VAL GLU TRP LEU GLN TYR SER PHE PRO
SEQRES 6 A 941 LEU GLN LEU GLU PRO SER ALA ARG GLY TRP ARG ALA GLY
SEQRES 7 A 941 LEU LEU ARG VAL SER ASN ARG ALA LEU LEU VAL ASN VAL
SEQRES 8 A 941 LYS PHE GLU GLY SER GLU GLU SER PHE THR PHE GLN VAL
SEQRES 9 A 941 SER THR LYS ASP MET PRO LEU ALA LEU MET ALA CYS ALA
SEQRES 10 A 941 LEU ARG LYS LYS ALA THR VAL PHE ARG GLN PRO LEU VAL
SEQRES 11 A 941 GLU GLN PRO GLU GLU TYR ALA LEU GLN VAL ASN GLY ARG
SEQRES 12 A 941 HIS GLU TYR LEU TYR GLY ASN TYR PRO LEU CYS HIS PHE
SEQRES 13 A 941 GLN TYR ILE CYS SER CYS LEU HIS SER GLY LEU THR PRO
SEQRES 14 A 941 HIS LEU THR MET VAL HIS SER SER SER ILE LEU ALA MET
SEQRES 15 A 941 ARG ASP GLU GLN SER ASN PRO ALA PRO GLN VAL GLN LYS
SEQRES 16 A 941 PRO ARG ALA LYS PRO PRO PRO ILE PRO ALA LYS LYS PRO
SEQRES 17 A 941 SER SER VAL SER LEU TRP SER LEU GLU GLN PRO PHE SER
SEQRES 18 A 941 ILE GLU LEU ILE GLU GLY ARG LYS VAL ASN ALA ASP GLU
SEQRES 19 A 941 ARG MET LYS LEU VAL VAL GLN ALA GLY LEU PHE HIS GLY
SEQRES 20 A 941 ASN GLU MET LEU CYS LYS THR VAL SER SER SER GLU VAL
SEQRES 21 A 941 ASN VAL CYS SER GLU PRO VAL TRP LYS GLN ARG LEU GLU
SEQRES 22 A 941 PHE ASP ILE SER VAL CYS ASP LEU PRO ARG MET ALA ARG
SEQRES 23 A 941 LEU CYS PHE ALA LEU TYR ALA VAL VAL GLU LYS ALA LYS
SEQRES 24 A 941 LYS ALA ARG SER THR LYS LYS LYS SER LYS LYS ALA ASP
SEQRES 25 A 941 CYS PRO ILE ALA TRP ALA ASN LEU MET LEU PHE ASP TYR
SEQRES 26 A 941 LYS ASP GLN LEU LYS THR GLY GLU ARG CYS LEU TYR MET
SEQRES 27 A 941 TRP PRO SER VAL PRO ASP GLU LYS GLY GLU LEU LEU ASN
SEQRES 28 A 941 PRO ALA GLY THR VAL ARG GLY ASN PRO ASN THR GLU SER
SEQRES 29 A 941 ALA ALA ALA LEU VAL ILE TYR LEU PRO GLU VAL ALA PRO
SEQRES 30 A 941 HIS PRO VAL TYR PHE PRO ALA LEU GLU LYS ILE LEU GLU
SEQRES 31 A 941 LEU GLY ARG HIS GLY GLU ARG GLY ARG ILE THR GLU GLU
SEQRES 32 A 941 GLU GLN LEU GLN LEU ARG GLU ILE LEU GLU ARG ARG GLY
SEQRES 33 A 941 SER GLY GLU LEU TYR GLU HIS GLU LYS ASP LEU VAL TRP
SEQRES 34 A 941 LYS MET ARG HIS GLU VAL GLN GLU HIS PHE PRO GLU ALA
SEQRES 35 A 941 LEU ALA ARG LEU LEU LEU VAL THR LYS TRP ASN LYS HIS
SEQRES 36 A 941 GLU ASP VAL ALA GLN MET LEU TYR LEU LEU CYS SER TRP
SEQRES 37 A 941 PRO GLU LEU PRO VAL LEU SER ALA LEU GLU LEU LEU ASP
SEQRES 38 A 941 PHE SER PHE PRO ASP CYS TYR VAL GLY SER PHE ALA ILE
SEQRES 39 A 941 LYS SER LEU ARG LYS LEU THR ASP ASP GLU LEU PHE GLN
SEQRES 40 A 941 TYR LEU LEU GLN LEU VAL GLN VAL LEU LYS TYR GLU SER
SEQRES 41 A 941 TYR LEU ASP CYS GLU LEU THR LYS PHE LEU LEU GLY ARG
SEQRES 42 A 941 ALA LEU ALA ASN ARG LYS ILE GLY HIS PHE LEU PHE TRP
SEQRES 43 A 941 HIS LEU ARG SER GLU MET HIS VAL PRO SER VAL ALA LEU
SEQRES 44 A 941 ARG PHE GLY LEU ILE MET GLU ALA TYR CYS ARG GLY SER
SEQRES 45 A 941 THR HIS HIS MET LYS VAL LEU MET LYS GLN GLY GLU ALA
SEQRES 46 A 941 LEU SER LYS LEU LYS ALA LEU ASN ASP PHE VAL LYS VAL
SEQRES 47 A 941 SER SER GLN LYS THR THR LYS PRO GLN THR LYS GLU MET
SEQRES 48 A 941 MET HIS MET CYS MET ARG GLN GLU THR TYR MET GLU ALA
SEQRES 49 A 941 LEU SER HIS LEU GLN SER PRO LEU ASP PRO SER THR LEU
SEQRES 50 A 941 LEU GLU GLU VAL CYS VAL GLU GLN CYS THR PHE MET ASP
SEQRES 51 A 941 SER LYS MET LYS PRO LEU TRP ILE MET TYR SER SER GLU
SEQRES 52 A 941 GLU ALA GLY SER ALA GLY ASN VAL GLY ILE ILE PHE LYS
SEQRES 53 A 941 ASN GLY ASP ASP LEU ARG GLN ASP MET LEU THR LEU GLN
SEQRES 54 A 941 MET ILE GLN LEU MET ASP VAL LEU TRP LYS GLN GLU GLY
SEQRES 55 A 941 LEU ASP LEU ARG MET THR PRO TYR GLY CYS LEU PRO THR
SEQRES 56 A 941 GLY ASP ARG THR GLY LEU ILE GLU VAL VAL LEU HIS SER
SEQRES 57 A 941 ASP THR ILE ALA ASN ILE GLN LEU ASN LYS SER ASN MET
SEQRES 58 A 941 ALA ALA THR ALA ALA PHE ASN LYS ASP ALA LEU LEU ASN
SEQRES 59 A 941 TRP LEU LYS SER LYS ASN PRO GLY GLU ALA LEU ASP ARG
SEQRES 60 A 941 ALA ILE GLU GLU PHE THR LEU SER CYS ALA GLY TYR CYS
SEQRES 61 A 941 VAL ALA THR TYR VAL LEU GLY ILE GLY ASP ARG HIS SER
SEQRES 62 A 941 ASP ASN ILE MET ILE ARG GLU SER GLY GLN LEU PHE HIS
SEQRES 63 A 941 ILE ASP PHE GLY HIS PHE LEU GLY ASN PHE LYS THR LYS
SEQRES 64 A 941 PHE GLY ILE ASN ARG GLU ARG VAL PRO PHE ILE LEU THR
SEQRES 65 A 941 TYR ASP PHE VAL HIS VAL ILE GLN GLN GLY LYS THR ASN
SEQRES 66 A 941 ASN SER GLU LYS PHE GLU ARG PHE ARG GLY TYR CYS GLU
SEQRES 67 A 941 ARG ALA TYR THR ILE LEU ARG ARG HIS GLY LEU LEU PHE
SEQRES 68 A 941 LEU HIS LEU PHE ALA LEU MET ARG ALA ALA GLY LEU PRO
SEQRES 69 A 941 GLU LEU SER CYS SER LYS ASP ILE GLN TYR LEU LYS ASP
SEQRES 70 A 941 SER LEU ALA LEU GLY LYS THR GLU GLU GLU ALA LEU LYS
SEQRES 71 A 941 HIS PHE ARG VAL LYS PHE ASN GLU ALA LEU ARG GLU SER
SEQRES 72 A 941 TRP LYS THR LYS VAL ASN TRP LEU ALA HIS ASN VAL SER
SEQRES 73 A 941 LYS ASP ASN ARG GLN
HET 9NQ A1101 32
HETNAM 9NQ LENIOLISIB
FORMUL 2 9NQ C21 H25 F3 N6 O2
FORMUL 3 HOH *55(H2 O)
HELIX 1 AA1 VAL A 109 GLY A 122 1 14
HELIX 2 AA2 LEU A 125 SER A 130 1 6
HELIX 3 AA3 ASP A 133 GLN A 155 1 23
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 SER A 268 1 10
HELIX 9 AA9 SER A 279 GLN A 289 1 11
HELIX 10 AB1 ALA A 487 LEU A 492 1 6
HELIX 11 AB2 TYR A 524 MET A 534 1 11
HELIX 12 AB3 MET A 534 HIS A 541 1 8
HELIX 13 AB4 PHE A 542 GLU A 544 5 3
HELIX 14 AB5 ALA A 545 THR A 553 1 9
HELIX 15 AB6 LYS A 557 CYS A 569 1 13
HELIX 16 AB7 PRO A 575 LEU A 583 1 9
HELIX 17 AB8 ASP A 589 ARG A 601 1 13
HELIX 18 AB9 THR A 604 LEU A 619 1 16
HELIX 19 AC1 CYS A 627 LEU A 638 1 12
HELIX 20 AC2 ASN A 640 SER A 653 1 14
HELIX 21 AC3 VAL A 660 GLY A 674 1 15
HELIX 22 AC4 SER A 675 GLN A 704 1 30
HELIX 23 AC5 THR A 707 ARG A 720 1 14
HELIX 24 AC6 GLN A 721 SER A 729 1 9
HELIX 25 AC7 CYS A 745 CYS A 749 5 5
HELIX 26 AC8 ALA A 768 ASN A 773 5 6
HELIX 27 AC9 LEU A 784 GLU A 804 1 21
HELIX 28 AD1 ILE A 834 ASN A 840 1 7
HELIX 29 AD2 PHE A 850 LYS A 852 5 3
HELIX 30 AD3 ASP A 853 ASN A 863 1 11
HELIX 31 AD4 PRO A 864 GLU A 866 5 3
HELIX 32 AD5 ALA A 867 LEU A 889 1 23
HELIX 33 AD6 THR A 935 GLN A 943 1 9
HELIX 34 AD7 ASN A 949 HIS A 970 1 22
HELIX 35 AD8 HIS A 970 MET A 981 1 12
HELIX 36 AD9 ARG A 982 GLY A 985 5 4
HELIX 37 AE1 CYS A 991 LEU A 1002 1 12
HELIX 38 AE2 THR A 1007 SER A 1026 1 20
SHEET 1 AA1 5 PHE A 203 SER A 208 0
SHEET 2 AA1 5 ALA A 189 PHE A 196 -1 N VAL A 194 O PHE A 203
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 GLN A 242 O THR A 275
SHEET 5 AA1 5 GLU A 248 LEU A 250 -1 O GLU A 248 N VAL A 243
SHEET 1 AA2 5 GLU A 352 MET A 353 0
SHEET 2 AA2 5 LEU A 341 HIS A 349 -1 N HIS A 349 O GLU A 352
SHEET 3 AA2 5 ARG A 389 ALA A 396 -1 O ARG A 389 N PHE A 348
SHEET 4 AA2 5 CYS A 416 MET A 424 -1 O ALA A 421 N PHE A 392
SHEET 5 AA2 5 TRP A 442 PRO A 443 -1 O TRP A 442 N TRP A 420
SHEET 1 AA3 2 GLY A 435 TYR A 440 0
SHEET 2 AA3 2 ALA A 470 LEU A 475 -1 O LEU A 471 N LEU A 439
SHEET 1 AA4 2 LEU A 731 SER A 733 0
SHEET 2 AA4 2 ASP A 736 LEU A 741 -1 O LEU A 741 N LEU A 731
SHEET 1 AA5 5 THR A 750 PHE A 751 0
SHEET 2 AA5 5 LEU A 759 TYR A 763 -1 O TRP A 760 N THR A 750
SHEET 3 AA5 5 VAL A 774 ASN A 780 -1 O VAL A 774 N TYR A 763
SHEET 4 AA5 5 THR A 822 GLU A 826 -1 O GLY A 823 N LYS A 779
SHEET 5 AA5 5 CYS A 815 PRO A 817 -1 N LEU A 816 O LEU A 824
SHEET 1 AA6 3 SER A 831 THR A 833 0
SHEET 2 AA6 3 ILE A 899 ARG A 902 -1 O ILE A 901 N ASP A 832
SHEET 3 AA6 3 LEU A 907 HIS A 909 -1 O PHE A 908 N MET A 900
SITE 1 AC1 15 THR A 750 MET A 752 PRO A 758 TRP A 760
SITE 2 AC1 15 ILE A 777 LYS A 779 ASP A 787 TYR A 813
SITE 3 AC1 15 ILE A 825 GLU A 826 VAL A 828 SER A 831
SITE 4 AC1 15 MET A 900 ASP A 911 HOH A1206
CRYST1 142.120 63.990 116.540 90.00 102.89 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 0.007036 0.000000 0.001610 0.00000
SCALE2 0.000000 0.015627 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008803 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
