HEADER TRANSFERASE/TRANSFERASE INHIBITOR 03-FEB-15 4XZ4
TITLE STRUCTURE OF PI3K GAMMA IN COMPLEX WITH AN INHIBITOR
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: UNP RESIDUES 144-1102;
COMPND 6 SYNONYM: PTDINS-3-KINASE SUBUNIT GAMMA,PHOSPHATIDYLINOSITOL 4,5-
COMPND 7 BISPHOSPHATE 3-KINASE 110 KDA CATALYTIC SUBUNIT GAMMA,P110GAMMA,
COMPND 8 PHOSPHOINOSITIDE-3-KINASE CATALYTIC GAMMA POLYPEPTIDE,
COMPND 9 SERINE/THREONINE PROTEIN KINASE PIK3CG,P120-PI3K;
COMPND 10 EC: 2.7.1.153,2.7.11.1;
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_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS TRANSFERASE, INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.N.COLLIER,D.MESSERSMITH,A.LE TIRAN,U.K.BANDARAGE,C.BOUCHER,J.COME,
AUTHOR 2 K.M.COTTRELL,V.DAMAGNEZ,J.D.DORAN,J.P.GRIFFITH,S.KHARE-PANDIT,
AUTHOR 3 E.B.KRUEGER,M.W.LEDEBOER,B.LEDFORD,Y.LIAO,S.MAHAJAN,C.S.MOODY,
AUTHOR 4 T.WANG,J.XU,A.M.ARONOV
REVDAT 2 28-FEB-24 4XZ4 1 REMARK
REVDAT 1 03-FEB-16 4XZ4 0
JRNL AUTH P.N.COLLIER,D.MESSERSMITH,A.LE TIRAN,U.K.BANDARAGE,
JRNL AUTH 2 C.BOUCHER,J.COME,K.M.COTTRELL,V.DAMAGNEZ,J.D.DORAN,
JRNL AUTH 3 J.P.GRIFFITH,S.KHARE-PANDIT,E.B.KRUEGER,M.W.LEDEBOER,
JRNL AUTH 4 B.LEDFORD,Y.LIAO,S.MAHAJAN,C.S.MOODY,T.WANG,J.XU,A.M.ARONOV
JRNL TITL STRUCTURE OF PI3K GAMMA IN COMPLEX WITH AN INHIBITOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 73.1
REMARK 3 NUMBER OF REFLECTIONS : 21666
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1170
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 68
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 3.06
REMARK 3 BIN R VALUE (WORKING SET) : 0.4390
REMARK 3 BIN FREE R VALUE SET COUNT : 2
REMARK 3 BIN FREE R VALUE : 0.1290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6844
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 6
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.71000
REMARK 3 B22 (A**2) : 2.03000
REMARK 3 B33 (A**2) : -3.28000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.434
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.323
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 36.894
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7015 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6791 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9489 ; 1.569 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15618 ; 0.840 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 835 ; 7.623 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 330 ;37.987 ;24.212
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1275 ;20.985 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;17.743 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1062 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7775 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1615 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3363 ; 2.983 ; 4.450
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3362 ; 2.982 ; 4.449
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4190 ; 5.070 ; 6.656
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4191 ; 5.070 ; 6.656
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3652 ; 2.972 ; 4.816
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3630 ; 2.922 ; 4.795
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5268 ; 4.976 ; 7.059
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8100 ; 8.241 ;35.400
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 8071 ; 8.202 ;35.234
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 144 A 1092
REMARK 3 ORIGIN FOR THE GROUP (A): 34.2647 47.0845 26.8148
REMARK 3 T TENSOR
REMARK 3 T11: 0.3166 T22: 0.0423
REMARK 3 T33: 0.2556 T12: 0.0044
REMARK 3 T13: -0.0306 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 4.5356 L22: 1.7018
REMARK 3 L33: 2.8380 L12: -0.7006
REMARK 3 L13: 0.8021 L23: -0.1235
REMARK 3 S TENSOR
REMARK 3 S11: -0.0938 S12: 0.0908 S13: 0.0987
REMARK 3 S21: 0.1694 S22: 0.1066 S23: 0.2331
REMARK 3 S31: -0.3896 S32: -0.0929 S33: -0.0128
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4XZ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206447.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 98
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) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21666
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 44.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 73.1
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 200MM LITHIUM SULFATE, 10
REMARK 280 MM DTT, 10 MM EDTA, 100 MM TRIS, PH 8.5, 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 71.85100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.58850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 71.85100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.58850
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 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 PRO A 324
REMARK 465 LEU A 325
REMARK 465 VAL A 326
REMARK 465 ASP A 327
REMARK 465 ASP A 328
REMARK 465 CYS A 329
REMARK 465 THR A 330
REMARK 465 GLY A 331
REMARK 465 VAL A 332
REMARK 465 THR A 333
REMARK 465 GLY A 334
REMARK 465 TYR A 335
REMARK 465 HIS A 336
REMARK 465 GLU A 337
REMARK 465 GLN A 338
REMARK 465 LEU A 339
REMARK 465 THR A 340
REMARK 465 ILE A 341
REMARK 465 HIS A 342
REMARK 465 GLY A 343
REMARK 465 LYS A 344
REMARK 465 ASP A 345
REMARK 465 HIS A 346
REMARK 465 GLU A 347
REMARK 465 SER A 348
REMARK 465 VAL A 349
REMARK 465 PHE A 350
REMARK 465 THR A 351
REMARK 465 VAL A 352
REMARK 465 SER A 353
REMARK 465 LEU A 354
REMARK 465 TRP A 355
REMARK 465 ASP A 356
REMARK 465 GLY A 436
REMARK 465 LYS A 437
REMARK 465 ALA A 438
REMARK 465 PRO A 439
REMARK 465 ALA A 440
REMARK 465 LEU A 441
REMARK 465 SER A 442
REMARK 465 SER A 443
REMARK 465 LYS A 444
REMARK 465 ALA A 445
REMARK 465 SER A 446
REMARK 465 ALA A 447
REMARK 465 GLU A 448
REMARK 465 SER A 449
REMARK 465 PRO A 450
REMARK 465 SER A 451
REMARK 465 SER A 452
REMARK 465 GLU A 453
REMARK 465 SER A 454
REMARK 465 LYS A 455
REMARK 465 GLY A 456
REMARK 465 LYS A 457
REMARK 465 VAL A 458
REMARK 465 LYS A 490
REMARK 465 GLY A 491
REMARK 465 GLU A 492
REMARK 465 ASP A 493
REMARK 465 GLN A 494
REMARK 465 GLY A 495
REMARK 465 SER A 496
REMARK 465 TYR A 523
REMARK 465 CYS A 524
REMARK 465 LEU A 529
REMARK 465 PRO A 530
REMARK 465 LYS A 531
REMARK 465 HIS A 532
REMARK 465 GLN A 533
REMARK 465 PRO A 534
REMARK 465 THR A 535
REMARK 465 PRO A 536
REMARK 465 ASP A 537
REMARK 465 PRO A 538
REMARK 465 GLU A 539
REMARK 465 GLY A 540
REMARK 465 ASP A 541
REMARK 465 ARG A 542
REMARK 465 VAL A 543
REMARK 465 ILE A 968
REMARK 465 LEU A 969
REMARK 465 GLY A 970
REMARK 465 ASN A 971
REMARK 465 TYR A 972
REMARK 465 LYS A 973
REMARK 465 SER A 974
REMARK 465 PHE A 975
REMARK 465 LEU A 976
REMARK 465 GLY A 977
REMARK 465 ILE A 978
REMARK 465 ASN A 979
REMARK 465 LYS A 980
REMARK 465 GLY A 1093
REMARK 465 ILE A 1094
REMARK 465 LYS A 1095
REMARK 465 GLN A 1096
REMARK 465 GLY A 1097
REMARK 465 GLU A 1098
REMARK 465 LYS A 1099
REMARK 465 HIS A 1100
REMARK 465 SER A 1101
REMARK 465 ALA A 1102
REMARK 465 HIS A 1103
REMARK 465 HIS A 1104
REMARK 465 HIS A 1105
REMARK 465 HIS A 1106
REMARK 465 HIS A 1107
REMARK 465 HIS A 1108
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 144 N
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 995 OG SER A 1003 2.10
REMARK 500 OG SER A 204 OE2 GLU A 652 2.14
REMARK 500 OG1 THR A 988 OD1 ASP A 990 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A1086 CB TRP A1086 CG 0.109
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 904 CB - CG - OD1 ANGL. DEV. = 6.5 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 ASN A 167 59.48 -117.43
REMARK 500 ASP A 170 -172.73 -174.16
REMARK 500 CYS A 219 145.31 -177.18
REMARK 500 SER A 227 74.81 -165.68
REMARK 500 PRO A 237 -16.74 -47.76
REMARK 500 PHE A 249 -6.34 -53.86
REMARK 500 LYS A 251 -71.98 -117.50
REMARK 500 ALA A 314 -9.73 -59.06
REMARK 500 GLU A 317 140.58 -31.35
REMARK 500 GLU A 322 67.16 -150.26
REMARK 500 PRO A 374 -70.61 -50.31
REMARK 500 ASN A 376 -34.16 79.12
REMARK 500 ASP A 378 95.11 -45.97
REMARK 500 HIS A 389 87.02 -163.14
REMARK 500 GLN A 391 -14.68 59.81
REMARK 500 GLU A 406 -32.18 -37.78
REMARK 500 HIS A 471 1.48 -68.48
REMARK 500 ASN A 498 127.62 -176.26
REMARK 500 PRO A 526 -165.26 -107.52
REMARK 500 ILE A 527 138.21 123.67
REMARK 500 THR A 561 138.14 -12.62
REMARK 500 PHE A 578 49.42 -103.95
REMARK 500 THR A 726 -43.96 -4.35
REMARK 500 ALA A 754 -81.18 -63.91
REMARK 500 GLU A 755 -66.05 -123.00
REMARK 500 LYS A 756 91.92 14.99
REMARK 500 ASN A 776 -50.32 -14.54
REMARK 500 SER A 777 13.89 -171.33
REMARK 500 GLN A 778 -55.36 -128.12
REMARK 500 PHE A 783 149.38 -179.73
REMARK 500 LEU A 865 76.66 -112.34
REMARK 500 TYR A 867 160.55 -44.63
REMARK 500 LYS A 875 45.17 37.90
REMARK 500 SER A 894 -76.37 -73.84
REMARK 500 VAL A 896 -86.60 -114.76
REMARK 500 ASN A 898 -168.11 -64.89
REMARK 500 THR A 899 24.95 -64.13
REMARK 500 GLU A 926 -71.71 -51.45
REMARK 500 LYS A1000 53.65 88.86
REMARK 500 PRO A1040 -149.13 -50.41
REMARK 500 SER A1044 15.00 -66.36
REMARK 500 LYS A1045 -81.93 -116.95
REMARK 500 GLU A1062 -77.34 -62.70
REMARK 500 GLU A1073 24.27 -72.65
REMARK 500 PHE A1084 -54.48 -25.26
REMARK 500 LEU A1090 -28.97 -35.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TRP A 201 VAL A 202 -146.92
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 456 A 1201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4XX5 RELATED DB: PDB
DBREF 4XZ4 A 144 1102 UNP P48736 PK3CG_HUMAN 144 1102
SEQADV 4XZ4 MET A 143 UNP P48736 INITIATING METHIONINE
SEQADV 4XZ4 ARG A 459 UNP P48736 GLN 459 CONFLICT
SEQADV 4XZ4 HIS A 1103 UNP P48736 EXPRESSION TAG
SEQADV 4XZ4 HIS A 1104 UNP P48736 EXPRESSION TAG
SEQADV 4XZ4 HIS A 1105 UNP P48736 EXPRESSION TAG
SEQADV 4XZ4 HIS A 1106 UNP P48736 EXPRESSION TAG
SEQADV 4XZ4 HIS A 1107 UNP P48736 EXPRESSION TAG
SEQADV 4XZ4 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 456 A1201 21
HETNAM 456 N-[5-(6-METHOXYPYRAZIN-2-YL)-4,5,6,7-TETRAHYDRO[1,
HETNAM 2 456 3]THIAZOLO[5,4-C]PYRIDIN-2-YL]ACETAMIDE
FORMUL 2 456 C13 H15 N5 O2 S
FORMUL 3 HOH *6(H2 O)
HELIX 1 AA1 GLU A 146 GLY A 159 1 14
HELIX 2 AA2 ASP A 171 LEU A 180 1 10
HELIX 3 AA3 LEU A 180 SER A 190 1 11
HELIX 4 AA4 ASP A 192 HIS A 199 1 8
HELIX 5 AA5 PRO A 208 LYS A 214 1 7
HELIX 6 AA6 THR A 240 PHE A 249 1 10
HELIX 7 AA7 PRO A 286 ASN A 289 5 4
HELIX 8 AA8 PHE A 290 GLY A 300 1 11
HELIX 9 AA9 ASP A 312 ASP A 316 5 5
HELIX 10 AB1 LYS A 421 LEU A 423 5 3
HELIX 11 AB2 ASN A 498 THR A 503 5 6
HELIX 12 AB3 PRO A 548 THR A 561 1 14
HELIX 13 AB4 THR A 568 PHE A 578 1 11
HELIX 14 AB5 PHE A 578 LEU A 583 1 6
HELIX 15 AB6 LYS A 584 LYS A 587 5 4
HELIX 16 AB7 ALA A 588 SER A 594 1 7
HELIX 17 AB8 GLN A 600 ARG A 613 1 14
HELIX 18 AB9 ARG A 614 GLN A 619 1 6
HELIX 19 AC1 ASP A 623 LEU A 630 1 8
HELIX 20 AC2 ASP A 637 GLU A 649 1 13
HELIX 21 AC3 GLU A 652 VAL A 667 1 16
HELIX 22 AC4 LYS A 668 GLU A 670 5 3
HELIX 23 AC5 SER A 675 ASN A 688 1 14
HELIX 24 AC6 ASN A 688 SER A 706 1 19
HELIX 25 AC7 TYR A 709 GLY A 725 1 17
HELIX 26 AC8 THR A 726 SER A 753 1 28
HELIX 27 AC9 SER A 760 ASN A 776 1 17
HELIX 28 AD1 ILE A 798 CYS A 801 5 4
HELIX 29 AD2 ASP A 837 THR A 857 1 21
HELIX 30 AD3 ILE A 888 VAL A 896 1 9
HELIX 31 AD4 GLU A 905 LYS A 914 1 10
HELIX 32 AD5 THR A 917 GLY A 943 1 27
HELIX 33 AD6 HIS A 948 ASP A 950 5 3
HELIX 34 AD7 THR A 988 PHE A 993 1 6
HELIX 35 AD8 SER A 1003 HIS A 1022 1 20
HELIX 36 AD9 HIS A 1023 MET A 1039 1 17
HELIX 37 AE1 GLU A 1049 LEU A 1055 1 7
HELIX 38 AE2 ASN A 1060 ARG A 1076 1 17
HELIX 39 AE3 TRP A 1080 HIS A 1089 1 10
HELIX 40 AE4 LEU A 1090 LEU A 1092 5 3
SHEET 1 AA1 5 SER A 230 VAL A 235 0
SHEET 2 AA1 5 ILE A 220 HIS A 225 -1 N ILE A 224 O GLN A 231
SHEET 3 AA1 5 HIS A 304 ASP A 308 1 O LEU A 307 N HIS A 225
SHEET 4 AA1 5 VAL A 271 VAL A 274 -1 N VAL A 271 O ASP A 308
SHEET 5 AA1 5 TYR A 280 LEU A 281 -1 O LEU A 281 N LEU A 272
SHEET 1 AA2 4 GLU A 407 LYS A 419 0
SHEET 2 AA2 4 LYS A 360 ASP A 369 -1 N PHE A 361 O PHE A 416
SHEET 3 AA2 4 SER A 515 LEU A 520 -1 O SER A 515 N ASP A 369
SHEET 4 AA2 4 GLY A 478 HIS A 483 -1 N GLY A 478 O LEU A 520
SHEET 1 AA3 3 GLN A 392 ARG A 398 0
SHEET 2 AA3 3 THR A 380 HIS A 389 -1 N ILE A 387 O LEU A 394
SHEET 3 AA3 3 LYS A 402 PRO A 403 -1 O LYS A 402 N VAL A 381
SHEET 1 AA4 5 GLN A 392 ARG A 398 0
SHEET 2 AA4 5 THR A 380 HIS A 389 -1 N ILE A 387 O LEU A 394
SHEET 3 AA4 5 LEU A 428 TYR A 434 -1 O GLN A 432 N GLU A 384
SHEET 4 AA4 5 TYR A 462 LEU A 467 -1 O LEU A 466 N LEU A 429
SHEET 5 AA4 5 TRP A 485 GLN A 486 -1 O TRP A 485 N TYR A 463
SHEET 1 AA5 4 PHE A 783 VAL A 785 0
SHEET 2 AA5 4 ASP A 788 LEU A 796 -1 O ALA A 793 N PHE A 783
SHEET 3 AA5 4 LEU A 811 CYS A 817 -1 O LYS A 816 N GLY A 794
SHEET 4 AA5 4 LYS A 802 VAL A 803 -1 N LYS A 802 O TRP A 812
SHEET 1 AA6 6 PHE A 783 VAL A 785 0
SHEET 2 AA6 6 ASP A 788 LEU A 796 -1 O ALA A 793 N PHE A 783
SHEET 3 AA6 6 LEU A 811 CYS A 817 -1 O LYS A 816 N GLY A 794
SHEET 4 AA6 6 ILE A 828 HIS A 834 -1 O ILE A 828 N PHE A 815
SHEET 5 AA6 6 ILE A 876 GLU A 880 -1 O ILE A 879 N ILE A 831
SHEET 6 AA6 6 CYS A 869 GLY A 873 -1 N ILE A 870 O MET A 878
SHEET 1 AA7 3 ALA A 885 THR A 887 0
SHEET 2 AA7 3 ILE A 952 THR A 955 -1 O ILE A 954 N THR A 886
SHEET 3 AA7 3 LEU A 960 HIS A 962 -1 O PHE A 961 N MET A 953
SITE 1 AC1 11 TRP A 812 ILE A 831 LYS A 833 TYR A 867
SITE 2 AC1 11 ILE A 879 GLU A 880 ILE A 881 VAL A 882
SITE 3 AC1 11 ALA A 885 ASP A 964 HOH A1305
CRYST1 143.702 67.177 106.345 90.00 95.89 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 0.006959 0.000000 0.000718 0.00000
SCALE2 0.000000 0.014886 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009453 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
