HEADER TRANSFERASE 30-JUN-05 2A4Z
TITLE CRYSTAL STRUCTURE OF HUMAN PI3KGAMMA COMPLEXED WITH AS604850
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: P110 SUBUNIT GAMMA, RESIDUES 143-1101;
COMPND 6 SYNONYM: PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT, PI3-KINASE
COMPND 7 P110 SUBUNIT GAMMA, PTDINS- 3-KINASE P110, PI3K, PI3KGAMMA;
COMPND 8 EC: 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 CELL_LINE: SF9;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PVL1393
KEYWDS PROTEIN-INHIBITOR COMPLEX, PI3KG, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.CAMPS,T.RUCKLE,H.JI,V.ARDISSONE,F.RINTELEN,J.SHAW,C.FERRANDI,
AUTHOR 2 C.CHABERT,C.GILLIERON,B.FRANCON,T.MARTIN,D.GRETENER,D.PERRIN,
AUTHOR 3 D.LEROY,P.-A.VITTE,E.HIRSCH,M.P.WYMANN,R.CIRILLO,M.K.SCHWARZ,
AUTHOR 4 C.ROMMEL
REVDAT 4 25-OCT-23 2A4Z 1 REMARK SEQADV
REVDAT 3 11-OCT-17 2A4Z 1 REMARK
REVDAT 2 24-FEB-09 2A4Z 1 VERSN
REVDAT 1 20-SEP-05 2A4Z 0
JRNL AUTH M.CAMPS,T.RUCKLE,H.JI,V.ARDISSONE,F.RINTELEN,J.SHAW,
JRNL AUTH 2 C.FERRANDI,C.CHABERT,C.GILLIERON,B.FRANCON,T.MARTIN,
JRNL AUTH 3 D.GRETENER,D.PERRIN,D.LEROY,P.-A.VITTE,E.HIRSCH,M.P.WYMANN,
JRNL AUTH 4 R.CIRILLO,M.K.SCHWARZ,C.ROMMEL
JRNL TITL BLOCKADE OF PI3KGAMMA SUPPRESSES JOINT INFLAMMATION AND
JRNL TITL 2 DAMAGE IN MOUSE MODELS OF RHEUMATOID ARTHRITIS
JRNL REF NAT.MED. (N.Y.) V. 11 936 2005
JRNL REFN ISSN 1078-8956
JRNL PMID 16127437
JRNL DOI 10.1038/NM1284
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1219204.625
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 21669
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) : 0.264
REMARK 3 R VALUE (WORKING SET) : 0.257
REMARK 3 FREE R VALUE : 0.352
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2156
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 25981
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3159
REMARK 3 BIN R VALUE (WORKING SET) : 0.3520
REMARK 3 BIN FREE R VALUE : 0.4490
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 346
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.024
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6247
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 7
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 127.4
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.84000
REMARK 3 B22 (A**2) : 6.62000
REMARK 3 B33 (A**2) : -3.77000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 6.45000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM SIGMAA (A) : 0.33
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.58
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.63
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.820
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 6.030 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 8.960 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 8.660 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 11.120; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : BABINET
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 280.0
REMARK 3
REMARK 3 NCS MODEL : RESTRAINTS
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : INH.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : INH.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 2A4Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033494.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAY-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0716
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21670
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
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 (%) : 96.1
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : 0.08700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.31400
REMARK 200 R SYM FOR SHELL (I) : 0.31400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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 1E8Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 4K, 100MM TRIS-HCL, 200MM
REMARK 280 (NH4)2SO4, PH 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 300K
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 71.17600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.82400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 71.17600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.82400
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 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 ARG A 226
REMARK 465 SER A 227
REMARK 465 THR A 228
REMARK 465 THR A 229
REMARK 465 LYS A 251
REMARK 465 MET A 252
REMARK 465 ALA A 253
REMARK 465 LYS A 254
REMARK 465 LYS A 255
REMARK 465 LYS A 256
REMARK 465 SER A 257
REMARK 465 LEU A 258
REMARK 465 MET A 259
REMARK 465 ASP A 260
REMARK 465 ILE A 261
REMARK 465 PRO A 262
REMARK 465 GLU A 263
REMARK 465 SER A 264
REMARK 465 GLN A 265
REMARK 465 SER A 266
REMARK 465 GLU A 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 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 VAL A 458
REMARK 465 ARG A 459
REMARK 465 GLY A 489
REMARK 465 LYS A 490
REMARK 465 GLY A 491
REMARK 465 GLU A 492
REMARK 465 ASP A 493
REMARK 465 GLN A 494
REMARK 465 GLY A 495
REMARK 465 SER A 496
REMARK 465 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 SER A 753
REMARK 465 ALA A 754
REMARK 465 GLU A 755
REMARK 465 LYS A 756
REMARK 465 TYR A 757
REMARK 465 ASP A 758
REMARK 465 VAL A 759
REMARK 465 SER A 760
REMARK 465 SER A 761
REMARK 465 GLN A 762
REMARK 465 GLY A 966
REMARK 465 HIS A 967
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 LEU A 1088
REMARK 465 HIS A 1089
REMARK 465 LEU A 1090
REMARK 465 VAL A 1091
REMARK 465 LEU A 1092
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 151 CG CD OE1 NE2
REMARK 470 ARG A 152 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 153 CG CD OE1 NE2
REMARK 470 ASP A 164 CG OD1 OD2
REMARK 470 ARG A 178 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 191 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 205 CG CD CE NZ
REMARK 470 GLU A 209 CG CD OE1 OE2
REMARK 470 LYS A 214 CG CD CE NZ
REMARK 470 GLN A 231 CG CD OE1 NE2
REMARK 470 LYS A 234 CG CD CE NZ
REMARK 470 ASP A 239 CG OD1 OD2
REMARK 470 GLN A 268 CG CD OE1 NE2
REMARK 470 ASP A 269 CG OD1 OD2
REMARK 470 LYS A 288 CG CD CE NZ
REMARK 470 LYS A 298 CG CD CE NZ
REMARK 470 ASN A 299 CG OD1 ND2
REMARK 470 GLU A 301 CG CD OE1 OE2
REMARK 470 LEU A 307 CG CD1 CD2
REMARK 470 GLU A 317 CG CD OE1 OE2
REMARK 470 ARG A 319 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 320 CG CD CE NZ
REMARK 470 ARG A 359 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 360 CG CD CE NZ
REMARK 470 ARG A 362 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 364 CG CD CE NZ
REMARK 470 LEU A 373 CG CD1 CD2
REMARK 470 LYS A 402 CG CD CE NZ
REMARK 470 GLU A 406 CG CD OE1 OE2
REMARK 470 LYS A 419 CG CD CE NZ
REMARK 470 LYS A 421 CG CD CE NZ
REMARK 470 ASP A 422 CG OD1 OD2
REMARK 470 ARG A 477 CG CD NE CZ NH1 NH2
REMARK 470 SER A 504 OG
REMARK 470 ASP A 521 CG OD1 OD2
REMARK 470 ASN A 522 CG OD1 ND2
REMARK 470 ARG A 544 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 546 CG CD OE1 OE2
REMARK 470 ARG A 552 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 601 CG CD OE1 NE2
REMARK 470 GLU A 602 CG CD OE1 OE2
REMARK 470 LYS A 606 CG CD CE NZ
REMARK 470 ARG A 613 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 615 CG CD OE1 OE2
REMARK 470 GLU A 638 CG CD OE1 OE2
REMARK 470 GLN A 646 CG CD OE1 NE2
REMARK 470 ASP A 654 CG OD1 OD2
REMARK 470 LYS A 689 CG CD CE NZ
REMARK 470 ARG A 707 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 730 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 737 CG CD OE1 NE2
REMARK 470 ILE A 739 CG1 CG2 CD1
REMARK 470 GLU A 740 CG CD OE1 OE2
REMARK 470 LEU A 767 CG CD1 CD2
REMARK 470 GLN A 769 CG CD OE1 NE2
REMARK 470 GLU A 772 CG CD OE1 OE2
REMARK 470 ASN A 776 CG OD1 ND2
REMARK 470 SER A 777 OG
REMARK 470 GLN A 778 CG CD OE1 NE2
REMARK 470 LEU A 779 CG CD1 CD2
REMARK 470 LYS A 800 CG CD CE NZ
REMARK 470 LYS A 807 CG CD CE NZ
REMARK 470 GLU A 814 CG CD OE1 OE2
REMARK 470 LYS A 816 CG CD CE NZ
REMARK 470 LEU A 823 CG CD1 CD2
REMARK 470 LYS A 875 CG CD CE NZ
REMARK 470 ASP A 884 CG OD1 OD2
REMARK 470 GLN A 893 CG CD OE1 NE2
REMARK 470 LYS A 903 CG CD CE NZ
REMARK 470 GLU A 905 CG CD OE1 OE2
REMARK 470 VAL A 906 CG1 CG2
REMARK 470 HIS A 909 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A 946 CG OD1 OD2
REMARK 470 HIS A 948 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A 950 CG OD1 OD2
REMARK 470 ASP A 964 CG OD1 OD2
REMARK 470 ASP A 990 CG OD1 OD2
REMARK 470 LYS A1000 CG CD CE NZ
REMARK 470 LYS A1001 CG CD CE NZ
REMARK 470 GLN A1007 CG CD OE1 NE2
REMARK 470 GLN A1010 CG CD OE1 NE2
REMARK 470 ARG A1052 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1062 CG CD OE1 OE2
REMARK 470 LYS A1065 CG CD CE NZ
REMARK 470 ASP A1070 CG OD1 OD2
REMARK 470 ARG A1076 CG CD NE CZ NH1 NH2
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 PRO A 311 C - N - CA ANGL. DEV. = 10.8 DEGREES
REMARK 500 PRO A 526 C - N - CA ANGL. DEV. = 10.3 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 VAL A 165 13.67 -159.93
REMARK 500 HIS A 169 24.22 -148.14
REMARK 500 SER A 190 26.58 -78.05
REMARK 500 LYS A 194 -86.66 -55.37
REMARK 500 TYR A 196 -76.53 -59.28
REMARK 500 ALA A 197 -17.63 -38.33
REMARK 500 HIS A 199 63.35 38.56
REMARK 500 TYR A 210 -27.68 -35.61
REMARK 500 LYS A 214 15.73 -68.83
REMARK 500 ILE A 215 47.28 -171.04
REMARK 500 ALA A 216 41.04 -78.84
REMARK 500 PRO A 237 15.18 -54.71
REMARK 500 ASP A 238 28.64 -143.64
REMARK 500 SER A 247 -96.99 -52.50
REMARK 500 PHE A 248 90.96 -52.98
REMARK 500 PHE A 249 -29.52 160.68
REMARK 500 ASP A 269 23.58 -66.18
REMARK 500 ASP A 278 69.97 -119.49
REMARK 500 LEU A 281 52.32 -97.07
REMARK 500 LYS A 288 -6.60 -57.65
REMARK 500 VAL A 305 -165.81 -109.27
REMARK 500 LEU A 307 94.51 -63.99
REMARK 500 ASP A 316 33.94 -88.58
REMARK 500 GLN A 391 18.65 58.33
REMARK 500 LEU A 394 -84.87 -122.30
REMARK 500 GLN A 396 109.33 -176.14
REMARK 500 ARG A 398 -162.36 -117.57
REMARK 500 PRO A 401 73.10 -58.31
REMARK 500 GLU A 406 -28.97 -20.68
REMARK 500 HIS A 471 -7.50 -49.95
REMARK 500 PHE A 473 -16.91 68.29
REMARK 500 ASN A 512 20.56 -143.09
REMARK 500 ASN A 522 -173.44 -178.39
REMARK 500 TYR A 523 58.28 -150.11
REMARK 500 HIS A 525 148.05 66.22
REMARK 500 PRO A 526 -165.32 -68.74
REMARK 500 ALA A 545 -153.99 65.39
REMARK 500 PRO A 548 -130.16 -42.65
REMARK 500 ASN A 549 -7.86 -151.72
REMARK 500 ILE A 559 66.82 -68.30
REMARK 500 ALA A 560 -6.24 -169.90
REMARK 500 ASN A 565 108.90 -28.97
REMARK 500 LYS A 587 0.55 -58.17
REMARK 500 TRP A 617 -71.57 -66.44
REMARK 500 ASP A 618 8.69 -63.92
REMARK 500 GLU A 649 -14.45 -47.17
REMARK 500 GLN A 705 1.11 -153.97
REMARK 500 ARG A 722 40.86 -105.63
REMARK 500 ILE A 749 -8.22 -47.38
REMARK 500 LEU A 767 -72.60 -58.95
REMARK 500
REMARK 500 THIS ENTRY HAS 94 RAMACHANDRAN OUTLIERS.
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 BYM A 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E7U RELATED DB: PDB
REMARK 900 RELATED ID: 1E7V RELATED DB: PDB
REMARK 900 RELATED ID: 1E8W RELATED DB: PDB
REMARK 900 RELATED ID: 1E8X RELATED DB: PDB
REMARK 900 RELATED ID: 1E8Y RELATED DB: PDB
REMARK 900 RELATED ID: 2A5U RELATED DB: PDB
DBREF 2A4Z A 144 1102 UNP P48736 PK3CG_HUMAN 143 1101
SEQADV 2A4Z MET A 143 UNP P48736 INITIATING METHIONINE
SEQADV 2A4Z HIS A 1103 UNP P48736 EXPRESSION TAG
SEQADV 2A4Z HIS A 1104 UNP P48736 EXPRESSION TAG
SEQADV 2A4Z HIS A 1105 UNP P48736 EXPRESSION TAG
SEQADV 2A4Z HIS A 1106 UNP P48736 EXPRESSION TAG
SEQADV 2A4Z HIS A 1107 UNP P48736 EXPRESSION TAG
SEQADV 2A4Z 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 BYM A 101 19
HETNAM BYM (5E)-5-[(2,2-DIFLUORO-1,3-BENZODIOXOL-5-YL)METHYLENE]-
HETNAM 2 BYM 1,3-THIAZOLIDINE-2,4-DIONE
FORMUL 2 BYM C11 H5 F2 N O4 S
FORMUL 3 HOH *7(H2 O)
HELIX 1 1 GLU A 146 GLY A 159 1 14
HELIX 2 2 ASP A 171 ALA A 189 1 19
HELIX 3 3 ASP A 192 HIS A 199 1 8
HELIX 4 4 PRO A 208 LYS A 214 1 7
HELIX 5 5 GLY A 242 PHE A 248 1 7
HELIX 6 6 PRO A 286 ASN A 289 5 4
HELIX 7 7 PHE A 290 ASN A 299 1 10
HELIX 8 8 ASP A 312 GLU A 317 5 6
HELIX 9 9 ASN A 498 THR A 503 5 6
HELIX 10 10 GLN A 550 ILE A 559 1 10
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 LYS A 584 LYS A 587 5 4
HELIX 14 14 ALA A 588 SER A 594 1 7
HELIX 15 15 GLN A 600 ALA A 612 1 13
HELIX 16 16 GLU A 615 SER A 620 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 TYR A 659 1 8
HELIX 20 20 TYR A 659 VAL A 667 1 9
HELIX 21 21 LYS A 668 GLU A 670 5 3
HELIX 22 22 SER A 675 ASN A 688 1 14
HELIX 23 23 ASN A 688 ALA A 704 1 17
HELIX 24 24 TYR A 709 ARG A 722 1 14
HELIX 25 25 GLY A 725 ILE A 749 1 25
HELIX 26 26 VAL A 763 ASN A 776 1 14
HELIX 27 27 ALA A 797 CYS A 801 5 5
HELIX 28 28 LEU A 838 GLU A 858 1 21
HELIX 29 29 ILE A 888 THR A 895 1 8
HELIX 30 30 GLU A 905 LYS A 914 1 10
HELIX 31 31 THR A 917 GLN A 922 1 6
HELIX 32 32 GLN A 922 LEU A 942 1 21
HELIX 33 33 THR A 988 GLY A 996 1 9
HELIX 34 34 SER A 1003 HIS A 1022 1 20
HELIX 35 35 HIS A 1023 MET A 1039 1 17
HELIX 36 36 ILE A 1048 THR A 1056 1 9
HELIX 37 37 GLU A 1062 LYS A 1078 1 17
HELIX 38 38 TRP A 1080 TRP A 1086 1 7
SHEET 1 A 4 GLN A 231 VAL A 235 0
SHEET 2 A 4 ILE A 220 HIS A 225 -1 N ILE A 220 O VAL A 235
SHEET 3 A 4 HIS A 304 ASP A 308 1 O VAL A 305 N VAL A 223
SHEET 4 A 4 VAL A 271 VAL A 274 -1 N VAL A 271 O ASP A 308
SHEET 1 B 4 GLU A 407 LYS A 419 0
SHEET 2 B 4 LYS A 360 ASP A 369 -1 N VAL A 363 O LEU A 414
SHEET 3 B 4 SER A 515 LEU A 520 -1 O SER A 517 N GLY A 367
SHEET 4 B 4 GLY A 478 HIS A 483 -1 N GLY A 478 O LEU A 520
SHEET 1 C 5 GLN A 392 VAL A 393 0
SHEET 2 C 5 ASN A 386 HIS A 389 -1 N HIS A 389 O GLN A 392
SHEET 3 C 5 LEU A 428 TYR A 434 -1 O ASN A 430 N ASN A 386
SHEET 4 C 5 THR A 380 VAL A 383 -1 N PHE A 382 O TYR A 434
SHEET 5 C 5 LYS A 402 PRO A 403 -1 O LYS A 402 N VAL A 381
SHEET 1 D 5 GLN A 392 VAL A 393 0
SHEET 2 D 5 ASN A 386 HIS A 389 -1 N HIS A 389 O GLN A 392
SHEET 3 D 5 LEU A 428 TYR A 434 -1 O ASN A 430 N ASN A 386
SHEET 4 D 5 TYR A 462 LEU A 467 -1 O VAL A 464 N LEU A 431
SHEET 5 D 5 TRP A 485 GLN A 486 -1 O TRP A 485 N TYR A 463
SHEET 1 E 2 PHE A 783 ARG A 784 0
SHEET 2 E 2 LYS A 792 ALA A 793 -1 O ALA A 793 N PHE A 783
SHEET 1 F 5 LYS A 802 VAL A 803 0
SHEET 2 F 5 LEU A 811 PHE A 815 -1 O TRP A 812 N LYS A 802
SHEET 3 F 5 ILE A 828 HIS A 834 -1 O PHE A 832 N LEU A 811
SHEET 4 F 5 ILE A 876 ILE A 879 -1 O ILE A 879 N ILE A 831
SHEET 5 F 5 CYS A 869 GLY A 873 -1 N ILE A 870 O MET A 878
SHEET 1 G 3 ALA A 885 THR A 887 0
SHEET 2 G 3 ILE A 952 THR A 955 -1 O ILE A 954 N THR A 886
SHEET 3 G 3 LEU A 960 HIS A 962 -1 O PHE A 961 N MET A 953
SITE 1 AC1 12 PRO A 810 TRP A 812 LYS A 833 TYR A 867
SITE 2 AC1 12 ILE A 879 GLU A 880 ILE A 881 VAL A 882
SITE 3 AC1 12 ALA A 885 MET A 953 ILE A 963 ASP A 964
CRYST1 142.352 67.648 106.390 90.00 95.77 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 0.007030 0.000000 0.000710 0.00000
SCALE2 0.000000 0.014780 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009450 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
