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Chemical substance (3) PDB-CCD (3) Chemical reaction (1) KEGG ENZYME (1) Gene (1) KEGG GENES (1) Protein sequence (3) UniProt (1) SWISS-PROT (1) PDBSTR (1) Protein domain (10) InterPro (7) PROSITE (3) Literature (1) PubMed (1) All databases (19)
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HEADER TRANSFERASE/TRANSFERASE INHIBITOR 07-JAN-17 5UGA
TITLE CRYSTAL STRUCTURE OF THE EGFR KINASE DOMAIN (L858R, T790M, V948R) IN
TITLE 2 COMPLEX WITH 4-(4-{[2-{[(3S)-1-ACETYLPYRROLIDIN-3-YL]AMINO}-9-
TITLE 3 (PROPAN-2-YL)-9H-PURIN-6-YL]AMINO}PHENYL)-1-METHYLPIPERAZIN-1-IUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 695-1022;
COMPND 5 SYNONYM: PROTO-ONCOGENE C-ERBB-1,RECEPTOR TYROSINE-PROTEIN KINASE
COMPND 6 ERBB-1;
COMPND 7 EC: 2.7.10.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: EGFR, ERBB, ERBB1, HER1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA AFF. FRUGIPERDA 2 RZ-2014;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 1491790
KEYWDS KINASE, COVALENT INHIBITOR, LUNG CANCER, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.S.GAJIWALA,R.A.FERRE
REVDAT 3 06-MAR-24 5UGA 1 REMARK
REVDAT 2 26-APR-17 5UGA 1 JRNL
REVDAT 1 22-MAR-17 5UGA 0
JRNL AUTH S.PLANKEN,D.C.BEHENNA,S.K.NAIR,T.O.JOHNSON,A.NAGATA,
JRNL AUTH 2 C.ALMADEN,S.BAILEY,T.E.BALLARD,L.BERNIER,H.CHENG,
JRNL AUTH 3 S.CHO-SCHULTZ,D.DALVIE,J.G.DEAL,D.M.DINH,M.P.EDWARDS,
JRNL AUTH 4 R.A.FERRE,K.S.GAJIWALA,M.HEMKENS,R.S.KANIA,J.C.KATH,
JRNL AUTH 5 J.MATTHEWS,B.W.MURRAY,S.NIESSEN,S.T.ORR,M.PAIRISH,N.W.SACH,
JRNL AUTH 6 H.SHEN,M.SHI,J.SOLOWIEJ,K.TRAN,E.TSENG,P.VICINI,Y.WANG,
JRNL AUTH 7 S.L.WEINRICH,R.ZHOU,M.ZIENTEK,L.LIU,Y.LUO,S.XIN,C.ZHANG,
JRNL AUTH 8 J.LAFONTAINE
JRNL TITL DISCOVERY OF
JRNL TITL 2 N-((3R,4R)-4-FLUORO-1-(6-((3-METHOXY-1-METHYL-1H-PYRAZOL-4-Y
JRNL TITL 3 L)AMINO)-9-METHYL-9H-PURIN-2-YL)PYRROLIDINE-3-YL)ACRYLAMIDE
JRNL TITL 4 (PF-06747775) THROUGH STRUCTURE-BASED DRUG DESIGN: A HIGH
JRNL TITL 5 AFFINITY IRREVERSIBLE INHIBITOR TARGETING ONCOGENIC EGFR
JRNL TITL 6 MUTANTS WITH SELECTIVITY OVER WILD-TYPE EGFR.
JRNL REF J. MED. CHEM. V. 60 3002 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28287730
JRNL DOI 10.1021/ACS.JMEDCHEM.6B01894
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2005
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1412291.730
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 28809
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) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1431
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.2350
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2330
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1437
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0070
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
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) : 1.82
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.93
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4357
REMARK 3 BIN R VALUE (WORKING SET) : 0.4480
REMARK 3 BIN FREE R VALUE : 0.4610
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 231
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2276
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 63
REMARK 3 SOLVENT ATOMS : 160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 22.75000
REMARK 3 B22 (A**2) : -12.29000
REMARK 3 B33 (A**2) : -10.46000
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) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.54
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) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.50
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 0.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.630
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.290 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.990 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.190 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.170 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 42.77
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5UGA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-17.
REMARK 100 THE DEPOSITION ID IS D_1000225823.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 98
REMARK 200 PH : NULL
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
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28868
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 58.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.46200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SALT: 0.2 M AMMONIUM SULFATE
REMARK 280 PRECIPITANT: 20.0 %W/V PEG 8000 BUFFER: 0.1 M HEPES (PH 7.50)
REMARK 280 PRECIPITANT: 13.6 %V/V ISO-PROPANOL, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 296K
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 20.45200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.10900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.79750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.10900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.45200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.79750
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 GLY A 694
REMARK 465 SER A 695
REMARK 465 GLY A 696
REMARK 465 GLU A 697
REMARK 465 ALA A 698
REMARK 465 PRO A 699
REMARK 465 ASN A 700
REMARK 465 GLN A 701
REMARK 465 ALA A 702
REMARK 465 ARG A 986
REMARK 465 MET A 987
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 ASN A 996
REMARK 465 PHE A 997
REMARK 465 TYR A 998
REMARK 465 ARG A 999
REMARK 465 ALA A 1000
REMARK 465 LEU A 1001
REMARK 465 MET A 1002
REMARK 465 ASP A 1003
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 465 VAL A 1010
REMARK 465 VAL A 1011
REMARK 465 ASP A 1012
REMARK 465 ALA A 1013
REMARK 465 ASP A 1014
REMARK 465 GLU A 1015
REMARK 465 TYR A 1016
REMARK 465 LEU A 1017
REMARK 465 ILE A 1018
REMARK 465 PRO A 1019
REMARK 465 GLN A 1020
REMARK 465 GLN A 1021
REMARK 465 GLY A 1022
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 THR A 783 -118.78 -122.18
REMARK 500 ASP A 837 34.19 -149.78
REMARK 500 GLU A 872 -154.87 -105.20
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 8BM A 9001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 9002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 9003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 9004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 9005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 9006
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5UG8 RELATED DB: PDB
REMARK 900 RELATED ID: 5UG9 RELATED DB: PDB
REMARK 900 RELATED ID: 5UGB RELATED DB: PDB
REMARK 900 RELATED ID: 5UGC RELATED DB: PDB
DBREF 5UGA A 695 1022 UNP P00533 EGFR_HUMAN 695 1022
SEQADV 5UGA GLY A 694 UNP P00533 EXPRESSION TAG
SEQADV 5UGA MET A 790 UNP P00533 THR 790 ENGINEERED MUTATION
SEQADV 5UGA ARG A 858 UNP P00533 LEU 858 ENGINEERED MUTATION
SEQADV 5UGA ARG A 948 UNP P00533 VAL 948 ENGINEERED MUTATION
SEQRES 1 A 329 GLY SER GLY GLU ALA PRO ASN GLN ALA LEU LEU ARG ILE
SEQRES 2 A 329 LEU LYS GLU THR GLU PHE LYS LYS ILE LYS VAL LEU GLY
SEQRES 3 A 329 SER GLY ALA PHE GLY THR VAL TYR LYS GLY LEU TRP ILE
SEQRES 4 A 329 PRO GLU GLY GLU LYS VAL LYS ILE PRO VAL ALA ILE LYS
SEQRES 5 A 329 GLU LEU ARG GLU ALA THR SER PRO LYS ALA ASN LYS GLU
SEQRES 6 A 329 ILE LEU ASP GLU ALA TYR VAL MET ALA SER VAL ASP ASN
SEQRES 7 A 329 PRO HIS VAL CYS ARG LEU LEU GLY ILE CYS LEU THR SER
SEQRES 8 A 329 THR VAL GLN LEU ILE MET GLN LEU MET PRO PHE GLY CYS
SEQRES 9 A 329 LEU LEU ASP TYR VAL ARG GLU HIS LYS ASP ASN ILE GLY
SEQRES 10 A 329 SER GLN TYR LEU LEU ASN TRP CYS VAL GLN ILE ALA LYS
SEQRES 11 A 329 GLY MET ASN TYR LEU GLU ASP ARG ARG LEU VAL HIS ARG
SEQRES 12 A 329 ASP LEU ALA ALA ARG ASN VAL LEU VAL LYS THR PRO GLN
SEQRES 13 A 329 HIS VAL LYS ILE THR ASP PHE GLY ARG ALA LYS LEU LEU
SEQRES 14 A 329 GLY ALA GLU GLU LYS GLU TYR HIS ALA GLU GLY GLY LYS
SEQRES 15 A 329 VAL PRO ILE LYS TRP MET ALA LEU GLU SER ILE LEU HIS
SEQRES 16 A 329 ARG ILE TYR THR HIS GLN SER ASP VAL TRP SER TYR GLY
SEQRES 17 A 329 VAL THR VAL TRP GLU LEU MET THR PHE GLY SER LYS PRO
SEQRES 18 A 329 TYR ASP GLY ILE PRO ALA SER GLU ILE SER SER ILE LEU
SEQRES 19 A 329 GLU LYS GLY GLU ARG LEU PRO GLN PRO PRO ILE CYS THR
SEQRES 20 A 329 ILE ASP VAL TYR MET ILE MET ARG LYS CYS TRP MET ILE
SEQRES 21 A 329 ASP ALA ASP SER ARG PRO LYS PHE ARG GLU LEU ILE ILE
SEQRES 22 A 329 GLU PHE SER LYS MET ALA ARG ASP PRO GLN ARG TYR LEU
SEQRES 23 A 329 VAL ILE GLN GLY ASP GLU ARG MET HIS LEU PRO SER PRO
SEQRES 24 A 329 THR ASP SER ASN PHE TYR ARG ALA LEU MET ASP GLU GLU
SEQRES 25 A 329 ASP MET ASP ASP VAL VAL ASP ALA ASP GLU TYR LEU ILE
SEQRES 26 A 329 PRO GLN GLN GLY
HET 8BM A9001 35
HET SO4 A9002 5
HET SO4 A9003 5
HET GOL A9004 6
HET GOL A9005 6
HET GOL A9006 6
HETNAM 8BM 4-(4-{[2-{[(3S)-1-ACETYLPYRROLIDIN-3-YL]AMINO}-9-
HETNAM 2 8BM (PROPAN-2-YL)-9H-PURIN-6-YL]AMINO}PHENYL)-1-
HETNAM 3 8BM METHYLPIPERAZIN-1-IUM
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN 8BM 1-[(3S)-3-{[6-{[4-(4-METHYLPIPERAZIN-1-YL)
HETSYN 2 8BM PHENYL]AMINO}-9-(PROPAN-2-YL)-9H-PURIN-2-
HETSYN 3 8BM YL]AMINO}PYRROLIDIN-1-YL]ETHAN-1-ONE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 8BM C25 H35 N9 O
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 GOL 3(C3 H8 O3)
FORMUL 8 HOH *160(H2 O)
HELIX 1 AA1 ALA A 755 SER A 768 1 14
HELIX 2 AA2 CYS A 797 HIS A 805 1 9
HELIX 3 AA3 LYS A 806 ILE A 809 5 4
HELIX 4 AA4 GLY A 810 ARG A 831 1 22
HELIX 5 AA5 ALA A 839 ARG A 841 5 3
HELIX 6 AA6 PRO A 877 MET A 881 5 5
HELIX 7 AA7 ALA A 882 ARG A 889 1 8
HELIX 8 AA8 THR A 892 THR A 909 1 18
HELIX 9 AA9 PRO A 919 SER A 921 5 3
HELIX 10 AB1 GLU A 922 LYS A 929 1 8
HELIX 11 AB2 THR A 940 CYS A 950 1 11
HELIX 12 AB3 ASP A 954 ARG A 958 5 5
HELIX 13 AB4 LYS A 960 ARG A 973 1 14
HELIX 14 AB5 ASP A 974 LEU A 979 1 6
SHEET 1 AA1 6 ARG A 705 ILE A 706 0
SHEET 2 AA1 6 LEU A 777 LEU A 782 1 O ILE A 780 N ARG A 705
SHEET 3 AA1 6 VAL A 786 GLN A 791 -1 O ILE A 789 N GLY A 779
SHEET 4 AA1 6 ILE A 740 LEU A 747 -1 N ALA A 743 O MET A 790
SHEET 5 AA1 6 GLY A 724 TRP A 731 -1 N TRP A 731 O ILE A 740
SHEET 6 AA1 6 PHE A 712 GLY A 721 -1 N LEU A 718 O VAL A 726
SHEET 1 AA2 2 LEU A 833 VAL A 834 0
SHEET 2 AA2 2 LYS A 860 LEU A 861 -1 O LYS A 860 N VAL A 834
SHEET 1 AA3 2 VAL A 843 THR A 847 0
SHEET 2 AA3 2 HIS A 850 ILE A 853 -1 O LYS A 852 N LEU A 844
SHEET 1 AA4 2 TYR A 869 HIS A 870 0
SHEET 2 AA4 2 ILE A 890 TYR A 891 -1 O TYR A 891 N TYR A 869
SITE 1 AC1 12 LEU A 718 GLY A 719 SER A 720 VAL A 726
SITE 2 AC1 12 ALA A 743 GLN A 791 MET A 793 PRO A 794
SITE 3 AC1 12 GLY A 796 ASN A 842 LEU A 844 THR A 854
SITE 1 AC2 7 ARG A 836 TYR A 869 ALA A 871 GLU A 872
SITE 2 AC2 7 GLY A 873 HOH A9113 HOH A9182
SITE 1 AC3 3 ARG A 803 LYS A 913 HOH A9131
SITE 1 AC4 5 SER A 752 ASN A 816 GLN A 820 LYS A 823
SITE 2 AC4 5 HOH A9102
SITE 1 AC5 8 THR A 940 ILE A 941 ASP A 942 ARG A 977
SITE 2 AC5 8 TYR A 978 HOH A9121 HOH A9162 HOH A9188
SITE 1 AC6 4 LEU A 747 ALA A 750 PRO A 753 LYS A 754
CRYST1 40.904 69.595 110.218 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 0.024447 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014369 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009073 0.00000
(ATOM LINES ARE NOT SHOWN.)
END