HEADER TRANSFERASE/TRANSFERASE INHIBITOR 08-JUN-11 3SD5
TITLE CRYSTAL STRUCTURE OF PI3K GAMMA WITH 5-(2,4-DIMORPHOLINOPYRIMIDIN-6-
TITLE 2 YL)-4-(TRIFLUOROMETHYL)PYRIDIN-2-AMINE
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: 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
KEYWDS LIPID KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.S.KNAPP,R.A.ELLING
REVDAT 3 13-SEP-23 3SD5 1 REMARK SEQADV
REVDAT 2 29-FEB-12 3SD5 1 JRNL
REVDAT 1 04-JAN-12 3SD5 0
JRNL AUTH S.M.MAIRA,S.PECCHI,A.HUANG,M.BURGER,M.KNAPP,D.STERKER,
JRNL AUTH 2 C.SCHNELL,D.GUTHY,T.NAGEL,M.WIESMANN,S.BRACHMANN,C.FRITSCH,
JRNL AUTH 3 M.DORSCH,P.CHENE,K.SHOEMAKER,A.DE POVER,D.MENEZES,
JRNL AUTH 4 G.MARTINY-BARON,D.FABBRO,C.J.WILSON,R.SCHLEGEL,F.HOFMANN,
JRNL AUTH 5 C.GARCIA-ECHEVERRIA,W.R.SELLERS,C.F.VOLIVA
JRNL TITL IDENTIFICATION AND CHARACTERIZATION OF NVP-BKM120, AN ORALLY
JRNL TITL 2 AVAILABLE PAN-CLASS I PI3-KINASE INHIBITOR.
JRNL REF MOL.CANCER THER. V. 11 317 2012
JRNL REFN ISSN 1535-7163
JRNL PMID 22188813
JRNL DOI 10.1158/1535-7163.MCT-11-0474
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 17166
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1629
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 54.1747 - 7.3210 0.96 2529 127 0.2058 0.2489
REMARK 3 2 7.3210 - 5.8130 0.97 2550 143 0.2185 0.2414
REMARK 3 3 5.8130 - 5.0789 0.97 2540 143 0.1947 0.2655
REMARK 3 4 5.0789 - 4.6148 0.97 2535 158 0.1740 0.2172
REMARK 3 5 4.6148 - 4.2841 0.98 2569 140 0.1680 0.2157
REMARK 3 6 4.2841 - 4.0316 0.97 2544 148 0.1792 0.2721
REMARK 3 7 4.0316 - 3.8298 0.97 2540 127 0.2171 0.2531
REMARK 3 8 3.8298 - 3.6631 0.97 2539 133 0.2165 0.2800
REMARK 3 9 3.6631 - 3.5221 0.97 2558 129 0.2405 0.2642
REMARK 3 10 3.5221 - 3.4006 0.96 2537 129 0.2762 0.3602
REMARK 3 11 3.4006 - 3.2943 0.97 2554 123 0.2804 0.3123
REMARK 3 12 3.2943 - 3.2000 0.97 2540 129 0.2897 0.3462
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 51.16
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.990
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.720
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 59.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.61180
REMARK 3 B22 (A**2) : 6.20170
REMARK 3 B33 (A**2) : -1.58990
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.56200
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 6543
REMARK 3 ANGLE : 0.596 8895
REMARK 3 CHIRALITY : 0.045 1029
REMARK 3 PLANARITY : 0.002 1145
REMARK 3 DIHEDRAL : 14.493 2344
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 144:208)
REMARK 3 ORIGIN FOR THE GROUP (A): 31.9409 -18.5703 17.9994
REMARK 3 T TENSOR
REMARK 3 T11: 0.3597 T22: 0.1925
REMARK 3 T33: 0.4062 T12: 0.0456
REMARK 3 T13: -0.1229 T23: -0.1140
REMARK 3 L TENSOR
REMARK 3 L11: 2.8283 L22: 1.7056
REMARK 3 L33: 1.7271 L12: -0.3034
REMARK 3 L13: 0.2645 L23: -0.0381
REMARK 3 S TENSOR
REMARK 3 S11: 0.1600 S12: 0.4669 S13: -0.7750
REMARK 3 S21: -0.2787 S22: 0.1403 S23: 0.0798
REMARK 3 S31: 0.2706 S32: 0.0748 S33: 0.0707
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 209:308)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4575 -11.1017 37.9121
REMARK 3 T TENSOR
REMARK 3 T11: 0.1192 T22: 0.5265
REMARK 3 T33: 0.3164 T12: -0.0507
REMARK 3 T13: 0.0979 T23: 0.2351
REMARK 3 L TENSOR
REMARK 3 L11: 1.0681 L22: 0.8350
REMARK 3 L33: 2.0844 L12: -0.8638
REMARK 3 L13: -0.5373 L23: 0.2443
REMARK 3 S TENSOR
REMARK 3 S11: -0.0925 S12: -0.6236 S13: -0.5508
REMARK 3 S21: 0.1691 S22: 0.0225 S23: 0.2844
REMARK 3 S31: 0.2990 S32: -0.6548 S33: -0.3784
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 309:477)
REMARK 3 ORIGIN FOR THE GROUP (A): 59.0951 -8.4677 15.1969
REMARK 3 T TENSOR
REMARK 3 T11: 0.3789 T22: 0.8220
REMARK 3 T33: 0.1900 T12: 0.0528
REMARK 3 T13: 0.1202 T23: -0.0758
REMARK 3 L TENSOR
REMARK 3 L11: 1.7957 L22: 1.0085
REMARK 3 L33: 1.4267 L12: -0.4841
REMARK 3 L13: 0.1146 L23: 0.0340
REMARK 3 S TENSOR
REMARK 3 S11: 0.1201 S12: 0.7052 S13: 0.0170
REMARK 3 S21: -0.2364 S22: 0.0033 S23: -0.1942
REMARK 3 S31: -0.1659 S32: 0.8478 S33: -0.0050
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 478:688)
REMARK 3 ORIGIN FOR THE GROUP (A): 49.9758 -9.9251 32.4928
REMARK 3 T TENSOR
REMARK 3 T11: -0.0485 T22: 0.0039
REMARK 3 T33: -0.1270 T12: 0.1111
REMARK 3 T13: 0.1280 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 2.3917 L22: 0.7249
REMARK 3 L33: 2.1150 L12: -0.1826
REMARK 3 L13: 1.2464 L23: 0.0547
REMARK 3 S TENSOR
REMARK 3 S11: 0.0850 S12: 0.1518 S13: -0.1601
REMARK 3 S21: -0.0827 S22: 0.0633 S23: -0.1279
REMARK 3 S31: 0.1581 S32: 0.4847 S33: 0.3065
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 689:941)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7086 5.9759 21.6031
REMARK 3 T TENSOR
REMARK 3 T11: 0.0253 T22: -0.0004
REMARK 3 T33: -0.1351 T12: 0.1744
REMARK 3 T13: 0.0501 T23: -0.0681
REMARK 3 L TENSOR
REMARK 3 L11: 2.0482 L22: 1.4838
REMARK 3 L33: 1.8563 L12: 0.0568
REMARK 3 L13: 0.1944 L23: 0.2120
REMARK 3 S TENSOR
REMARK 3 S11: -0.0801 S12: 0.2426 S13: 0.4443
REMARK 3 S21: -0.0681 S22: 0.0521 S23: 0.3446
REMARK 3 S31: -0.5008 S32: -0.3635 S33: 0.0773
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 942:1037)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.4793 15.3774 37.4579
REMARK 3 T TENSOR
REMARK 3 T11: 0.5336 T22: 0.1296
REMARK 3 T33: 0.3387 T12: 0.1509
REMARK 3 T13: -0.0482 T23: -0.0707
REMARK 3 L TENSOR
REMARK 3 L11: 2.6653 L22: 1.0663
REMARK 3 L33: 0.8474 L12: -0.5601
REMARK 3 L13: 1.3843 L23: -0.1611
REMARK 3 S TENSOR
REMARK 3 S11: -0.3176 S12: -0.3949 S13: 0.8465
REMARK 3 S21: 0.2018 S22: 0.0154 S23: 0.0414
REMARK 3 S31: -0.7698 S32: -0.3623 S33: -0.3530
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 1038:1092)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.1566 19.6320 37.9671
REMARK 3 T TENSOR
REMARK 3 T11: 0.6419 T22: 0.3855
REMARK 3 T33: 0.7865 T12: -0.0557
REMARK 3 T13: -0.1488 T23: -0.2244
REMARK 3 L TENSOR
REMARK 3 L11: 3.1620 L22: 2.3253
REMARK 3 L33: 2.5396 L12: -1.2606
REMARK 3 L13: 1.0863 L23: -0.2531
REMARK 3 S TENSOR
REMARK 3 S11: -0.3553 S12: -0.4047 S13: 1.0376
REMARK 3 S21: 0.0576 S22: 0.0491 S23: -0.1780
REMARK 3 S31: -0.7677 S32: -0.2296 S33: 0.1836
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE FRIEDEL PAIRS WERE USED FOR PHASING
REMARK 4
REMARK 4 3SD5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-11.
REMARK 100 THE DEPOSITION ID IS D_1000066058.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54055
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 106.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : 0.10000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.31900
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3P2B
REMARK 200
REMARK 200 REMARK: THE STRUCTURE FACTOR FILE CONTAIN FRIEDEL PAIRS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM ACETATE, 0.1M SODIUM
REMARK 280 CITRATE, 0.1M TRIS PH8.5, 16-19% (W/V)PEG 4000, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, 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 72.13200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.92400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 72.13200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.92400
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 MET A 143
REMARK 465 LYS A 214
REMARK 465 ILE A 215
REMARK 465 ALA A 216
REMARK 465 ASN A 217
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 GLU A 321
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 SER A 353
REMARK 465 LEU A 354
REMARK 465 TRP A 355
REMARK 465 ASP A 356
REMARK 465 LEU A 373
REMARK 465 PRO A 374
REMARK 465 ARG A 375
REMARK 465 ASN A 376
REMARK 465 THR A 377
REMARK 465 ASP A 378
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 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 PHE A 497
REMARK 465 TYR A 523
REMARK 465 CYS A 524
REMARK 465 HIS A 525
REMARK 465 PRO A 526
REMARK 465 ILE A 527
REMARK 465 ALA A 528
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 ARG A 544
REMARK 465 ALA A 545
REMARK 465 GLU A 546
REMARK 465 LEU A 823
REMARK 465 SER A 824
REMARK 465 GLY A 897
REMARK 465 ASN A 898
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 GLU A 981
REMARK 465 GLY A 999
REMARK 465 LYS A 1000
REMARK 465 PRO A 1040
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 145 CG CD OE1 OE2
REMARK 470 GLU A 146 CG CD OE1 OE2
REMARK 470 GLN A 148 CG CD OE1 NE2
REMARK 470 ARG A 152 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 194 CG CD CE NZ
REMARK 470 LEU A 211 CG CD1 CD2
REMARK 470 LYS A 213 CG CD CE NZ
REMARK 470 PHE A 221 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 226 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 234 CG CD CE NZ
REMARK 470 ASP A 239 CG OD1 OD2
REMARK 470 LYS A 251 CG CD CE NZ
REMARK 470 MET A 252 CG SD CE
REMARK 470 LYS A 288 CG CD CE NZ
REMARK 470 LYS A 298 CG CD CE NZ
REMARK 470 LYS A 320 CG CD CE NZ
REMARK 470 ARG A 359 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 362 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 379 CG CD1 CD2
REMARK 470 GLN A 392 CG CD OE1 NE2
REMARK 470 ARG A 398 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 404 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 406 CG CD OE1 OE2
REMARK 470 LYS A 421 CG CD CE NZ
REMARK 470 LYS A 425 CG CD CE NZ
REMARK 470 LYS A 587 CG CD CE NZ
REMARK 470 GLU A 615 CG CD OE1 OE2
REMARK 470 HIS A 730 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 740 CG CD OE1 OE2
REMARK 470 LYS A 744 CG CD CE NZ
REMARK 470 LYS A 750 CG CD CE NZ
REMARK 470 GLU A 755 CG CD OE1 OE2
REMARK 470 LYS A 756 CG CD CE NZ
REMARK 470 TYR A 757 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A 762 CG CD OE1 NE2
REMARK 470 GLN A 766 CG CD OE1 NE2
REMARK 470 LEU A 767 CG CD1 CD2
REMARK 470 LYS A 768 CG CD CE NZ
REMARK 470 GLN A 769 CG CD OE1 NE2
REMARK 470 LYS A 770 CG CD CE NZ
REMARK 470 GLU A 772 CG CD OE1 OE2
REMARK 470 LEU A 774 CG CD1 CD2
REMARK 470 GLN A 775 CG CD OE1 NE2
REMARK 470 ASN A 776 CG OD1 ND2
REMARK 470 GLN A 778 CG CD OE1 NE2
REMARK 470 LEU A 779 CG CD1 CD2
REMARK 470 LYS A 792 CG CD CE NZ
REMARK 470 LYS A 800 CG CD CE NZ
REMARK 470 LYS A 807 CG CD CE NZ
REMARK 470 LYS A 809 CG CD CE NZ
REMARK 470 LYS A 816 CG CD CE NZ
REMARK 470 LYS A 833 CG CD CE NZ
REMARK 470 LYS A 890 CG CD CE NZ
REMARK 470 LEU A 907 CG CD1 CD2
REMARK 470 LEU A 911 CG CD1 CD2
REMARK 470 LYS A1015 CG CD CE NZ
REMARK 470 GLN A1041 CG CD OE1 NE2
REMARK 470 LYS A1045 CG CD CE NZ
REMARK 470 GLU A1046 CG CD OE1 OE2
REMARK 470 LYS A1066 CG CD CE NZ
REMARK 470 PHE A1087 CG CD1 CD2 CE1 CE2 CZ
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 LEU A 157 NH1 ARG A 700 2.12
REMARK 500 OH TYR A 196 O CYS A 724 2.15
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 HIS A 199 69.35 33.37
REMARK 500 CYS A 219 137.92 68.97
REMARK 500 SER A 227 -69.89 67.32
REMARK 500 SER A 230 67.09 -157.69
REMARK 500 LYS A 251 55.68 -90.67
REMARK 500 ASN A 289 39.82 -94.76
REMARK 500 GLN A 391 -26.70 57.31
REMARK 500 PHE A 578 50.36 -101.17
REMARK 500 ARG A 613 49.24 -101.08
REMARK 500 ASP A 632 -155.33 -76.21
REMARK 500 ASP A 653 -32.18 -38.52
REMARK 500 HIS A 673 -70.15 -67.37
REMARK 500 GLN A 705 4.40 -158.67
REMARK 500 GLU A 755 44.20 -88.15
REMARK 500 GLN A 778 -71.99 -179.31
REMARK 500 ALA A 805 44.98 -83.44
REMARK 500 LYS A 809 75.30 46.30
REMARK 500 ASP A 837 98.48 -68.10
REMARK 500 SER A 859 45.22 71.98
REMARK 500 LYS A 875 52.14 28.39
REMARK 500 ALA A 901 84.33 -66.47
REMARK 500 ILE A 944 44.39 -100.90
REMARK 500 ASP A 964 89.92 57.94
REMARK 500 HIS A1023 51.80 -112.27
REMARK 500 LYS A1078 77.53 -103.80
REMARK 500 LEU A1090 42.85 -74.80
REMARK 500 VAL A1091 -30.58 -153.26
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 SD5 A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3P2B RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 Q459R CONFLICT IN UNP ENTRY P48736
DBREF 3SD5 A 144 1102 UNP P48736 PK3CG_HUMAN 144 1102
SEQADV 3SD5 MET A 143 UNP P48736 EXPRESSION TAG
SEQADV 3SD5 ARG A 459 UNP P48736 GLN 459 SEE REMARK 999
SEQADV 3SD5 HIS A 1103 UNP P48736 EXPRESSION TAG
SEQADV 3SD5 HIS A 1104 UNP P48736 EXPRESSION TAG
SEQADV 3SD5 HIS A 1105 UNP P48736 EXPRESSION TAG
SEQADV 3SD5 HIS A 1106 UNP P48736 EXPRESSION TAG
SEQADV 3SD5 HIS A 1107 UNP P48736 EXPRESSION TAG
SEQADV 3SD5 HIS A 1108 UNP P48736 EXPRESSION TAG
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 SD5 A 1 29
HETNAM SD5 5-[2,6-DI(MORPHOLIN-4-YL)PYRIMIDIN-4-YL]-4-
HETNAM 2 SD5 (TRIFLUOROMETHYL)PYRIDIN-2-AMINE
FORMUL 2 SD5 C18 H21 F3 N6 O2
FORMUL 3 HOH *11(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 THR A 240 LYS A 251 1 12
HELIX 6 6 PRO A 286 PHE A 290 5 5
HELIX 7 7 TRP A 292 GLY A 300 1 9
HELIX 8 8 ASP A 312 GLU A 317 5 6
HELIX 9 9 ASN A 498 LEU A 502 5 5
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 LEU A 583 1 6
HELIX 13 13 HIS A 585 LYS A 587 5 3
HELIX 14 14 ALA A 588 PHE A 593 1 6
HELIX 15 15 GLN A 600 ALA A 612 1 13
HELIX 16 16 ARG A 614 GLN A 619 1 6
HELIX 17 17 ASP A 623 LEU A 630 1 8
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 TYR A 709 ARG A 722 1 14
HELIX 24 24 GLY A 725 SER A 753 1 29
HELIX 25 25 SER A 761 SER A 777 1 17
HELIX 26 26 ILE A 798 CYS A 801 5 4
HELIX 27 27 ASP A 837 GLU A 858 1 22
HELIX 28 28 ILE A 888 VAL A 896 1 9
HELIX 29 29 GLU A 905 SER A 915 1 11
HELIX 30 30 THR A 917 LEU A 942 1 26
HELIX 31 31 HIS A 948 ASP A 950 5 3
HELIX 32 32 PHE A 965 GLY A 970 1 6
HELIX 33 33 THR A 988 GLY A 996 1 9
HELIX 34 34 HIS A 1005 HIS A 1022 1 18
HELIX 35 35 HIS A 1023 GLY A 1038 1 16
HELIX 36 36 THR A 1043 ILE A 1048 1 6
HELIX 37 37 GLU A 1049 LEU A 1055 1 7
HELIX 38 38 ASN A 1060 LYS A 1078 1 19
HELIX 39 39 TRP A 1080 LEU A 1090 1 11
SHEET 1 A 2 ILE A 220 VAL A 223 0
SHEET 2 A 2 THR A 232 VAL A 235 -1 O VAL A 235 N ILE A 220
SHEET 1 B 2 VAL A 271 VAL A 274 0
SHEET 2 B 2 VAL A 305 ASP A 308 -1 O VAL A 306 N ARG A 273
SHEET 1 C 4 GLU A 407 LYS A 419 0
SHEET 2 C 4 LYS A 360 ASP A 369 -1 N PHE A 361 O PHE A 416
SHEET 3 C 4 SER A 515 LEU A 520 -1 O SER A 515 N ASP A 369
SHEET 4 C 4 GLY A 478 HIS A 483 -1 N GLY A 478 O LEU A 520
SHEET 1 D 3 GLN A 392 ARG A 398 0
SHEET 2 D 3 THR A 380 HIS A 389 -1 N ILE A 387 O LEU A 394
SHEET 3 D 3 LYS A 402 PRO A 403 -1 O LYS A 402 N VAL A 381
SHEET 1 E 5 GLN A 392 ARG A 398 0
SHEET 2 E 5 THR A 380 HIS A 389 -1 N ILE A 387 O LEU A 394
SHEET 3 E 5 LEU A 428 TYR A 434 -1 O ASN A 430 N ASN A 386
SHEET 4 E 5 LEU A 460 LEU A 467 -1 O LEU A 461 N ILE A 433
SHEET 5 E 5 TRP A 485 GLN A 486 -1 O TRP A 485 N TYR A 463
SHEET 1 F 4 PHE A 783 ARG A 784 0
SHEET 2 F 4 LYS A 792 LEU A 796 -1 O ALA A 793 N PHE A 783
SHEET 3 F 4 LEU A 811 CYS A 817 -1 O LYS A 816 N GLY A 794
SHEET 4 F 4 LYS A 802 VAL A 803 -1 N LYS A 802 O TRP A 812
SHEET 1 G 6 PHE A 783 ARG A 784 0
SHEET 2 G 6 LYS A 792 LEU A 796 -1 O ALA A 793 N PHE A 783
SHEET 3 G 6 LEU A 811 CYS A 817 -1 O LYS A 816 N GLY A 794
SHEET 4 G 6 ILE A 828 HIS A 834 -1 O ILE A 830 N LEU A 813
SHEET 5 G 6 ILE A 876 GLU A 880 -1 O ILE A 879 N ILE A 831
SHEET 6 G 6 CYS A 869 GLY A 873 -1 N ILE A 870 O MET A 878
SHEET 1 H 3 ALA A 885 THR A 887 0
SHEET 2 H 3 ILE A 952 THR A 955 -1 O ILE A 954 N THR A 886
SHEET 3 H 3 LEU A 960 HIS A 962 -1 O PHE A 961 N MET A 953
SITE 1 AC1 10 MET A 804 PRO A 810 ILE A 831 LEU A 838
SITE 2 AC1 10 ASP A 841 ILE A 879 GLU A 880 VAL A 882
SITE 3 AC1 10 THR A 887 ASP A 964
CRYST1 144.264 67.848 106.633 90.00 96.09 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 0.006932 0.000000 0.000740 0.00000
SCALE2 0.000000 0.014739 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009431 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
