HEADER TRANSFERASE 04-OCT-07 2RGP
TITLE STRUCTURE OF EGFR IN COMPLEX WITH HYDRAZONE, A POTENT DUAL INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 702-1016;
COMPND 5 SYNONYM: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-1;
COMPND 6 EC: 2.7.10.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 STRAIN: HUMAN STRAINS UNDEFINED;
SOURCE 5 GENE: EGFR, ERBB1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: MODIFIED PDEST8
KEYWDS KINASE DOMAIN, ALTERNATIVE SPLICING, ANTI-ONCOGENE, ATP-BINDING, CELL
KEYWDS 2 CYCLE, DISEASE MUTATION, GLYCOPROTEIN, MEMBRANE, NUCLEOTIDE-BINDING,
KEYWDS 3 PHOSPHOPROTEIN, POLYMORPHISM, RECEPTOR, SECRETED, TRANSFERASE,
KEYWDS 4 TRANSMEMBRANE, TYROSINE-PROTEIN KINASE, UBL CONJUGATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.C.ABAD
REVDAT 4 30-AUG-23 2RGP 1 REMARK
REVDAT 3 25-OCT-17 2RGP 1 REMARK
REVDAT 2 24-FEB-09 2RGP 1 VERSN
REVDAT 1 26-AUG-08 2RGP 0
JRNL AUTH G.XU,M.C.ABAD,P.J.CONNOLLY,M.P.NEEPER,G.T.STRUBLE,
JRNL AUTH 2 B.A.SPRINGER,S.L.EMANUEL,N.PANDEY,R.H.GRUNINGER,M.ADAMS,
JRNL AUTH 3 S.MORENO-MAZZA,A.R.FUENTES-PESQUERA,S.A.MIDDLETON
JRNL TITL 4-AMINO-6-ARYLAMINO-PYRIMIDINE-5-CARBALDEHYDE HYDRAZONES AS
JRNL TITL 2 POTENT ERBB-2/EGFR DUAL KINASE INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 18 4615 2008
JRNL REFN ISSN 0960-894X
JRNL PMID 18653333
JRNL DOI 10.1016/J.BMCL.2008.07.020
REMARK 2
REMARK 2 RESOLUTION. 2.00 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 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 22479
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 SET) : 0.228
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2248
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2289
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 85
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -13.32700
REMARK 3 B22 (A**2) : 5.60600
REMARK 3 B33 (A**2) : 7.72100
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.559 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.599 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.112 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.255 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
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 : MSI_CNX_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : INH.PAR
REMARK 3 PARAMETER FILE 3 : MSI_CNX_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : MSI_CNX_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2RGP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-07.
REMARK 100 THE DEPOSITION ID IS D_1000044837.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26482
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.20800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.280
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1XKK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M NA/K3PO4, 0.1M CAPS PH 9.0 AND 0.2M
REMARK 280 LI2SO4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 22.92500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.93000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.01500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.93000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.92500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.01500
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 GLU A 734
REMARK 465 GLY A 735
REMARK 465 GLU A 736
REMARK 465 LYS A 737
REMARK 465 GLU A 749
REMARK 465 ALA A 750
REMARK 465 THR A 751
REMARK 465 SER A 752
REMARK 465 PRO A 753
REMARK 465 GLU A 868
REMARK 465 TYR A 869
REMARK 465 HIS A 870
REMARK 465 ALA A 871
REMARK 465 GLU A 872
REMARK 465 GLY A 873
REMARK 465 GLY A 874
REMARK 465 LYS A 875
REMARK 465 HIS A 988
REMARK 465 LEU A 989
REMARK 465 PRO A 990
REMARK 465 SER A 991
REMARK 465 PRO A 992
REMARK 465 THR A 993
REMARK 465 ASP A 994
REMARK 465 SER A 995
REMARK 465 GLU A 1004
REMARK 465 GLU A 1005
REMARK 465 ASP A 1006
REMARK 465 MET A 1007
REMARK 465 ASP A 1008
REMARK 465 ASP A 1009
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 A1015 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ILE A 715 -60.52 -97.49
REMARK 500 LEU A 782 74.60 -103.22
REMARK 500 THR A 783 -134.37 -93.32
REMARK 500 LYS A 806 -18.34 -49.77
REMARK 500 ARG A 836 -10.72 78.42
REMARK 500 ASP A 837 41.73 -148.25
REMARK 500 ARG A 986 75.20 -119.73
REMARK 500 PHE A 997 115.27 98.99
REMARK 500 TYR A 998 4.65 -50.77
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 PO4 A 81
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 82
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HYZ A 1
DBREF 2RGP A 702 1016 UNP P00533 EGFR_HUMAN 702 1016
SEQRES 1 A 315 ALA LEU LEU ARG ILE LEU LYS GLU THR GLU PHE LYS LYS
SEQRES 2 A 315 ILE LYS VAL LEU GLY SER GLY ALA PHE GLY THR VAL TYR
SEQRES 3 A 315 LYS GLY LEU TRP ILE PRO GLU GLY GLU LYS VAL LYS ILE
SEQRES 4 A 315 PRO VAL ALA ILE LYS GLU LEU ARG GLU ALA THR SER PRO
SEQRES 5 A 315 LYS ALA ASN LYS GLU ILE LEU ASP GLU ALA TYR VAL MET
SEQRES 6 A 315 ALA SER VAL ASP ASN PRO HIS VAL CYS ARG LEU LEU GLY
SEQRES 7 A 315 ILE CYS LEU THR SER THR VAL GLN LEU ILE THR GLN LEU
SEQRES 8 A 315 MET PRO PHE GLY CYS LEU LEU ASP TYR VAL ARG GLU HIS
SEQRES 9 A 315 LYS ASP ASN ILE GLY SER GLN TYR LEU LEU ASN TRP CYS
SEQRES 10 A 315 VAL GLN ILE ALA LYS GLY MET ASN TYR LEU GLU ASP ARG
SEQRES 11 A 315 ARG LEU VAL HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU
SEQRES 12 A 315 VAL LYS THR PRO GLN HIS VAL LYS ILE THR ASP PHE GLY
SEQRES 13 A 315 LEU ALA LYS LEU LEU GLY ALA GLU GLU LYS GLU TYR HIS
SEQRES 14 A 315 ALA GLU GLY GLY LYS VAL PRO ILE LYS TRP MET ALA LEU
SEQRES 15 A 315 GLU SER ILE LEU HIS ARG ILE TYR THR HIS GLN SER ASP
SEQRES 16 A 315 VAL TRP SER TYR GLY VAL THR VAL TRP GLU LEU MET THR
SEQRES 17 A 315 PHE GLY SER LYS PRO TYR ASP GLY ILE PRO ALA SER GLU
SEQRES 18 A 315 ILE SER SER ILE LEU GLU LYS GLY GLU ARG LEU PRO GLN
SEQRES 19 A 315 PRO PRO ILE CYS THR ILE ASP VAL TYR MET ILE MET VAL
SEQRES 20 A 315 LYS CYS TRP MET ILE ASP ALA ASP SER ARG PRO LYS PHE
SEQRES 21 A 315 ARG GLU LEU ILE ILE GLU PHE SER LYS MET ALA ARG ASP
SEQRES 22 A 315 PRO GLN ARG TYR LEU VAL ILE GLN GLY ASP GLU ARG MET
SEQRES 23 A 315 HIS LEU PRO SER PRO THR ASP SER ASN PHE TYR ARG ALA
SEQRES 24 A 315 LEU MET ASP GLU GLU ASP MET ASP ASP VAL VAL ASP ALA
SEQRES 25 A 315 ASP GLU TYR
HET PO4 A 81 5
HET PO4 A 82 5
HET HYZ A 1 33
HETNAM PO4 PHOSPHATE ION
HETNAM HYZ N-[1-(3-FLUOROBENZYL)-1H-INDAZOL-5-YL]-5-[(PIPERIDIN-1-
HETNAM 2 HYZ YLAMINO)METHYL]PYRIMIDINE-4,6-DIAMINE
FORMUL 2 PO4 2(O4 P 3-)
FORMUL 4 HYZ C24 H27 F N8
FORMUL 5 HOH *85(H2 O)
HELIX 1 1 ALA A 755 SER A 768 1 14
HELIX 2 2 CYS A 797 HIS A 805 1 9
HELIX 3 3 GLY A 810 ARG A 831 1 22
HELIX 4 4 ALA A 839 ARG A 841 5 3
HELIX 5 5 GLY A 857 LEU A 862 1 6
HELIX 6 6 PRO A 877 MET A 881 5 5
HELIX 7 7 ALA A 882 ARG A 889 1 8
HELIX 8 8 THR A 892 THR A 909 1 18
HELIX 9 9 PRO A 919 SER A 921 5 3
HELIX 10 10 GLU A 922 LYS A 929 1 8
HELIX 11 11 THR A 940 TRP A 951 1 12
HELIX 12 12 ASP A 954 ARG A 958 5 5
HELIX 13 13 LYS A 960 ASP A 974 1 15
HELIX 14 14 ASP A 974 LEU A 979 1 6
HELIX 15 15 PHE A 997 ASP A 1003 1 7
SHEET 1 A 6 ARG A 705 ILE A 706 0
SHEET 2 A 6 LEU A 777 LEU A 782 1 O ILE A 780 N ARG A 705
SHEET 3 A 6 VAL A 786 GLN A 791 -1 O ILE A 789 N LEU A 778
SHEET 4 A 6 ILE A 740 LEU A 747 -1 N ALA A 743 O THR A 790
SHEET 5 A 6 GLY A 724 TRP A 731 -1 N TYR A 727 O ILE A 744
SHEET 6 A 6 PHE A 712 SER A 720 -1 N LYS A 716 O LYS A 728
SHEET 1 B 2 VAL A 843 THR A 847 0
SHEET 2 B 2 HIS A 850 ILE A 853 -1 O LYS A 852 N LEU A 844
SITE 1 AC1 7 ARG A 803 LYS A 913 LYS A 970 ARG A 977
SITE 2 AC1 7 HOH A1074 HOH A1075 HOH A1093
SITE 1 AC2 5 ARG A 832 LEU A 833 ARG A 836 LYS A 860
SITE 2 AC2 5 HIS A 888
SITE 1 AC3 16 LEU A 718 GLY A 719 ALA A 743 LYS A 745
SITE 2 AC3 16 CYS A 775 ARG A 776 LEU A 777 LEU A 788
SITE 3 AC3 16 THR A 790 GLN A 791 MET A 793 ASP A 800
SITE 4 AC3 16 LEU A 844 THR A 854 ASP A 855 PHE A 856
CRYST1 45.850 68.030 103.860 90.00 90.00 90.00 P 21 21 21 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 0.021810 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014699 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009628 0.00000
(ATOM LINES ARE NOT SHOWN.)
END