HEADER TRANSFERASE 29-AUG-12 4GU9
TITLE FOCAL ADHESION KINASE CATALYTIC DOMAIN IN COMPLEX WITH (2-FLUORO-
TITLE 2 PHENYL)-(1H-PYRAZOLO[3,4-D]PYRIMIDIN-4-YL)-AMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FOCAL ADHESION KINASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC PROTEIN KINASE DOMAIN RESIDES 410-686;
COMPND 5 SYNONYM: FADK 1, FOCAL ADHESION KINASE-RELATED NONKINASE, FRNK,
COMPND 6 PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 71, PPP1R71, PROTEIN-
COMPND 7 TYROSINE KINASE 2, P125FAK, PP125FAK;
COMPND 8 EC: 2.7.10.2;
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 GENE: PTK2, FAK, FAK1;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS PROTEIN TYROSINE KINASE, TRANSFERASE, ATP BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR D.MUSIL
REVDAT 2 13-SEP-23 4GU9 1 REMARK SEQADV
REVDAT 1 04-SEP-13 4GU9 0
JRNL AUTH T.HEINRICH,J.SEENISAMY,L.EMMANUVEL,S.S.KULKARNI,J.BOMKE,
JRNL AUTH 2 F.ROHDICH,H.GREINER,C.ESDAR,M.KRIER,U.GRADLER,D.MUSIL
JRNL TITL FRAGMENT-BASED DISCOVERY OF NEW HIGHLY SUBSTITUTED
JRNL TITL 2 1H-PYRROLO[2,3-B]- AND 3H-IMIDAZOLO[4,5-B]-PYRIDINES AS
JRNL TITL 3 FOCAL ADHESION KINASE INHIBITORS.
JRNL REF J.MED.CHEM. V. 56 1160 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23294348
JRNL DOI 10.1021/JM3016014
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.1
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 22727
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1165
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.52
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.75
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2954
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1879
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2788
REMARK 3 BIN R VALUE (WORKING SET) : 0.1839
REMARK 3 BIN FREE R VALUE : 0.2528
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.62
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 166
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4079
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 133
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.41
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.24290
REMARK 3 B22 (A**2) : -0.01180
REMARK 3 B33 (A**2) : -1.23110
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.286
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.366
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 : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4210 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5691 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1476 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 93 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 601 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4210 ; 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 : 538 ; 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 : 4721 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.10
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.09
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.19
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: A 414 A 685
REMARK 3 ORIGIN FOR THE GROUP (A): 8.6635 19.6507 -34.3308
REMARK 3 T TENSOR
REMARK 3 T11: -0.1176 T22: -0.0803
REMARK 3 T33: -0.1039 T12: 0.0381
REMARK 3 T13: 0.0064 T23: 0.0639
REMARK 3 L TENSOR
REMARK 3 L11: 1.4325 L22: 1.3436
REMARK 3 L33: 2.4225 L12: 0.8389
REMARK 3 L13: -0.8602 L23: -1.0858
REMARK 3 S TENSOR
REMARK 3 S11: -0.0127 S12: 0.2050 S13: 0.1485
REMARK 3 S21: -0.0690 S22: 0.0998 S23: 0.0611
REMARK 3 S31: -0.0317 S32: -0.3103 S33: -0.0870
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: B 415 B 683
REMARK 3 ORIGIN FOR THE GROUP (A): 17.8154 -0.2868 -2.8902
REMARK 3 T TENSOR
REMARK 3 T11: -0.0595 T22: -0.0772
REMARK 3 T33: -0.0890 T12: 0.0136
REMARK 3 T13: -0.0154 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 1.1928 L22: 1.9300
REMARK 3 L33: 0.8576 L12: 0.3994
REMARK 3 L13: -0.1531 L23: -0.5008
REMARK 3 S TENSOR
REMARK 3 S11: -0.0207 S12: -0.1197 S13: -0.0246
REMARK 3 S21: 0.0039 S22: 0.0576 S23: -0.0104
REMARK 3 S31: 0.0865 S32: -0.0059 S33: -0.0369
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4GU9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-12.
REMARK 100 THE DEPOSITION ID IS D_1000074639.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.6
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) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22728
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 44.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.45600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3PXK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, 16% PEG3350, PH 8.6, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 23.27050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.38050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.14400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.38050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.27050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.14400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 408
REMARK 465 SER A 409
REMARK 465 PRO A 410
REMARK 465 SER A 411
REMARK 465 THR A 412
REMARK 465 ARG A 413
REMARK 465 GLU A 445
REMARK 465 ASN A 446
REMARK 465 GLY A 566
REMARK 465 LEU A 567
REMARK 465 SER A 568
REMARK 465 ARG A 569
REMARK 465 TYR A 570
REMARK 465 MET A 571
REMARK 465 GLU A 572
REMARK 465 ASP A 573
REMARK 465 SER A 574
REMARK 465 THR A 575
REMARK 465 TYR A 576
REMARK 465 TYR A 577
REMARK 465 LYS A 578
REMARK 465 ALA A 579
REMARK 465 SER A 580
REMARK 465 LYS A 581
REMARK 465 GLY A 582
REMARK 465 LYS A 583
REMARK 465 GLN A 686
REMARK 465 GLY B 408
REMARK 465 SER B 409
REMARK 465 PRO B 410
REMARK 465 SER B 411
REMARK 465 THR B 412
REMARK 465 ARG B 413
REMARK 465 ASP B 414
REMARK 465 GLU B 445
REMARK 465 ASN B 446
REMARK 465 GLU B 572
REMARK 465 ASP B 573
REMARK 465 SER B 574
REMARK 465 THR B 575
REMARK 465 TYR B 576
REMARK 465 TYR B 577
REMARK 465 LYS B 578
REMARK 465 ALA B 579
REMARK 465 SER B 580
REMARK 465 LYS B 581
REMARK 465 GLY B 582
REMARK 465 LYS B 583
REMARK 465 LYS B 684
REMARK 465 ALA B 685
REMARK 465 GLN B 686
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 ALA A 448 94.25 -28.69
REMARK 500 ARG A 545 -11.95 76.10
REMARK 500 ASP A 546 58.30 -144.78
REMARK 500 ALA B 448 73.08 -107.79
REMARK 500 ARG B 545 -13.81 78.11
REMARK 500 ASP B 546 59.96 -144.36
REMARK 500 GLU B 682 -10.43 -142.61
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 4GU A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4GU B 701
DBREF 4GU9 A 410 686 UNP Q05397 FAK1_HUMAN 410 686
DBREF 4GU9 B 410 686 UNP Q05397 FAK1_HUMAN 410 686
SEQADV 4GU9 GLY A 408 UNP Q05397 EXPRESSION TAG
SEQADV 4GU9 SER A 409 UNP Q05397 EXPRESSION TAG
SEQADV 4GU9 GLY B 408 UNP Q05397 EXPRESSION TAG
SEQADV 4GU9 SER B 409 UNP Q05397 EXPRESSION TAG
SEQRES 1 A 279 GLY SER PRO SER THR ARG ASP TYR GLU ILE GLN ARG GLU
SEQRES 2 A 279 ARG ILE GLU LEU GLY ARG CYS ILE GLY GLU GLY GLN PHE
SEQRES 3 A 279 GLY ASP VAL HIS GLN GLY ILE TYR MET SER PRO GLU ASN
SEQRES 4 A 279 PRO ALA LEU ALA VAL ALA ILE LYS THR CYS LYS ASN CYS
SEQRES 5 A 279 THR SER ASP SER VAL ARG GLU LYS PHE LEU GLN GLU ALA
SEQRES 6 A 279 LEU THR MET ARG GLN PHE ASP HIS PRO HIS ILE VAL LYS
SEQRES 7 A 279 LEU ILE GLY VAL ILE THR GLU ASN PRO VAL TRP ILE ILE
SEQRES 8 A 279 MET GLU LEU CYS THR LEU GLY GLU LEU ARG SER PHE LEU
SEQRES 9 A 279 GLN VAL ARG LYS TYR SER LEU ASP LEU ALA SER LEU ILE
SEQRES 10 A 279 LEU TYR ALA TYR GLN LEU SER THR ALA LEU ALA TYR LEU
SEQRES 11 A 279 GLU SER LYS ARG PHE VAL HIS ARG ASP ILE ALA ALA ARG
SEQRES 12 A 279 ASN VAL LEU VAL SER SER ASN ASP CYS VAL LYS LEU GLY
SEQRES 13 A 279 ASP PHE GLY LEU SER ARG TYR MET GLU ASP SER THR TYR
SEQRES 14 A 279 TYR LYS ALA SER LYS GLY LYS LEU PRO ILE LYS TRP MET
SEQRES 15 A 279 ALA PRO GLU SER ILE ASN PHE ARG ARG PHE THR SER ALA
SEQRES 16 A 279 SER ASP VAL TRP MET PHE GLY VAL CYS MET TRP GLU ILE
SEQRES 17 A 279 LEU MET HIS GLY VAL LYS PRO PHE GLN GLY VAL LYS ASN
SEQRES 18 A 279 ASN ASP VAL ILE GLY ARG ILE GLU ASN GLY GLU ARG LEU
SEQRES 19 A 279 PRO MET PRO PRO ASN CYS PRO PRO THR LEU TYR SER LEU
SEQRES 20 A 279 MET THR LYS CYS TRP ALA TYR ASP PRO SER ARG ARG PRO
SEQRES 21 A 279 ARG PHE THR GLU LEU LYS ALA GLN LEU SER THR ILE LEU
SEQRES 22 A 279 GLU GLU GLU LYS ALA GLN
SEQRES 1 B 279 GLY SER PRO SER THR ARG ASP TYR GLU ILE GLN ARG GLU
SEQRES 2 B 279 ARG ILE GLU LEU GLY ARG CYS ILE GLY GLU GLY GLN PHE
SEQRES 3 B 279 GLY ASP VAL HIS GLN GLY ILE TYR MET SER PRO GLU ASN
SEQRES 4 B 279 PRO ALA LEU ALA VAL ALA ILE LYS THR CYS LYS ASN CYS
SEQRES 5 B 279 THR SER ASP SER VAL ARG GLU LYS PHE LEU GLN GLU ALA
SEQRES 6 B 279 LEU THR MET ARG GLN PHE ASP HIS PRO HIS ILE VAL LYS
SEQRES 7 B 279 LEU ILE GLY VAL ILE THR GLU ASN PRO VAL TRP ILE ILE
SEQRES 8 B 279 MET GLU LEU CYS THR LEU GLY GLU LEU ARG SER PHE LEU
SEQRES 9 B 279 GLN VAL ARG LYS TYR SER LEU ASP LEU ALA SER LEU ILE
SEQRES 10 B 279 LEU TYR ALA TYR GLN LEU SER THR ALA LEU ALA TYR LEU
SEQRES 11 B 279 GLU SER LYS ARG PHE VAL HIS ARG ASP ILE ALA ALA ARG
SEQRES 12 B 279 ASN VAL LEU VAL SER SER ASN ASP CYS VAL LYS LEU GLY
SEQRES 13 B 279 ASP PHE GLY LEU SER ARG TYR MET GLU ASP SER THR TYR
SEQRES 14 B 279 TYR LYS ALA SER LYS GLY LYS LEU PRO ILE LYS TRP MET
SEQRES 15 B 279 ALA PRO GLU SER ILE ASN PHE ARG ARG PHE THR SER ALA
SEQRES 16 B 279 SER ASP VAL TRP MET PHE GLY VAL CYS MET TRP GLU ILE
SEQRES 17 B 279 LEU MET HIS GLY VAL LYS PRO PHE GLN GLY VAL LYS ASN
SEQRES 18 B 279 ASN ASP VAL ILE GLY ARG ILE GLU ASN GLY GLU ARG LEU
SEQRES 19 B 279 PRO MET PRO PRO ASN CYS PRO PRO THR LEU TYR SER LEU
SEQRES 20 B 279 MET THR LYS CYS TRP ALA TYR ASP PRO SER ARG ARG PRO
SEQRES 21 B 279 ARG PHE THR GLU LEU LYS ALA GLN LEU SER THR ILE LEU
SEQRES 22 B 279 GLU GLU GLU LYS ALA GLN
HET 4GU A 701 17
HET 4GU B 701 17
HETNAM 4GU N-(2-FLUOROPHENYL)-1H-PYRAZOLO[3,4-D]PYRIMIDIN-4-AMINE
FORMUL 3 4GU 2(C11 H8 F N5)
FORMUL 5 HOH *133(H2 O)
HELIX 1 1 GLN A 418 GLU A 420 5 3
HELIX 2 2 SER A 461 ARG A 476 1 16
HELIX 3 3 LEU A 507 ARG A 514 1 8
HELIX 4 4 ASP A 519 LYS A 540 1 22
HELIX 5 5 ALA A 548 ARG A 550 5 3
HELIX 6 6 PRO A 585 MET A 589 5 5
HELIX 7 7 ALA A 590 ARG A 597 1 8
HELIX 8 8 THR A 600 MET A 617 1 18
HELIX 9 9 LYS A 627 ASN A 629 5 3
HELIX 10 10 ASP A 630 ASN A 637 1 8
HELIX 11 11 PRO A 648 TRP A 659 1 12
HELIX 12 12 ASP A 662 ARG A 666 5 5
HELIX 13 13 ARG A 668 ALA A 685 1 18
HELIX 14 14 GLN B 418 GLU B 420 5 3
HELIX 15 15 SER B 461 ARG B 476 1 16
HELIX 16 16 LEU B 507 ARG B 514 1 8
HELIX 17 17 ASP B 519 LYS B 540 1 22
HELIX 18 18 ALA B 548 ARG B 550 5 3
HELIX 19 19 LEU B 567 MET B 571 5 5
HELIX 20 20 PRO B 585 MET B 589 5 5
HELIX 21 21 ALA B 590 ARG B 597 1 8
HELIX 22 22 THR B 600 MET B 617 1 18
HELIX 23 23 LYS B 627 ASN B 637 1 11
HELIX 24 24 PRO B 648 TRP B 659 1 12
HELIX 25 25 ASP B 662 ARG B 666 5 5
HELIX 26 26 ARG B 668 GLU B 681 1 14
SHEET 1 A 5 ILE A 422 GLU A 430 0
SHEET 2 A 5 ASP A 435 TYR A 441 -1 O GLN A 438 N ARG A 426
SHEET 3 A 5 LEU A 449 THR A 455 -1 O ILE A 453 N HIS A 437
SHEET 4 A 5 TRP A 496 GLU A 500 -1 O MET A 499 N ALA A 452
SHEET 5 A 5 LEU A 486 ILE A 490 -1 N GLY A 488 O ILE A 498
SHEET 1 B 3 GLY A 505 GLU A 506 0
SHEET 2 B 3 VAL A 552 SER A 556 -1 O VAL A 554 N GLY A 505
SHEET 3 B 3 CYS A 559 LEU A 562 -1 O LYS A 561 N LEU A 553
SHEET 1 C 5 ILE B 422 GLU B 430 0
SHEET 2 C 5 ASP B 435 MET B 442 -1 O GLN B 438 N ARG B 426
SHEET 3 C 5 ALA B 448 THR B 455 -1 O ILE B 453 N HIS B 437
SHEET 4 C 5 TRP B 496 GLU B 500 -1 O ILE B 497 N LYS B 454
SHEET 5 C 5 LEU B 486 ILE B 490 -1 N GLY B 488 O ILE B 498
SHEET 1 D 3 GLY B 505 GLU B 506 0
SHEET 2 D 3 VAL B 552 SER B 556 -1 O VAL B 554 N GLY B 505
SHEET 3 D 3 CYS B 559 LEU B 562 -1 O LYS B 561 N LEU B 553
SSBOND 1 CYS A 456 CYS A 459 1555 1555 2.04
SSBOND 2 CYS B 456 CYS B 459 1555 1555 2.04
CISPEP 1 ASN A 493 PRO A 494 0 -3.09
CISPEP 2 ASN B 493 PRO B 494 0 -2.14
SITE 1 AC1 8 ILE A 428 VAL A 436 ALA A 452 VAL A 484
SITE 2 AC1 8 MET A 499 GLU A 500 CYS A 502 LEU A 553
SITE 1 AC2 9 ILE B 428 GLY B 429 VAL B 436 ALA B 452
SITE 2 AC2 9 VAL B 484 MET B 499 GLU B 500 CYS B 502
SITE 3 AC2 9 LEU B 553
CRYST1 46.541 88.288 136.761 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.021486 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011327 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007312 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
