HEADER SIGNALING PROTEIN/INHIBITOR 24-OCT-06 2NO3
TITLE NOVEL 4-ANILINOPYRIMIDINES AS POTENT JNK1 INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: JNK1 RESIDUES 1-364;
COMPND 5 SYNONYM: STRESS-ACTIVATED PROTEIN KINASE JNK1, C-JUN N-TERMINAL
COMPND 6 KINASE 1, JNK-46;
COMPND 7 EC: 2.7.11.24;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: C-JUN-AMINO-TERMINAL KINASE-INTERACTING PROTEIN 1;
COMPND 12 CHAIN: F, G;
COMPND 13 FRAGMENT: PEPJIP1 PEPTIDE;
COMPND 14 SYNONYM: JNK-INTERACTING PROTEIN 1, JIP-1, JNK MAP KINASE SCAFFOLD
COMPND 15 PROTEIN 1, ISLET-BRAIN 1, IB-1, MITOGEN-ACTIVATED PROTEIN KINASE 8-
COMPND 16 INTERACTING PROTEIN 1;
COMPND 17 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: MAPK8, JNK1, PRKM8;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: THE SEQUENCE IS FOUND NATURALLY IN HOMO SAPIENS
KEYWDS JNK1, C-JUN N-TERMINAL KINASE, JNK1 INHIBITORS, ANILINOPYRIMIDINES
KEYWDS 2 JNK1 INHIBITORS, SIGNALING PROTEIN-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.ABAD-ZAPATERO
REVDAT 5 30-AUG-23 2NO3 1 REMARK
REVDAT 4 20-OCT-21 2NO3 1 REMARK SEQADV
REVDAT 3 18-OCT-17 2NO3 1 REMARK
REVDAT 2 24-FEB-09 2NO3 1 VERSN
REVDAT 1 17-APR-07 2NO3 0
JRNL AUTH M.LIU,S.WANG,J.E.CLAMPIT,R.J.GUM,D.L.HAASCH,C.M.RONDINONE,
JRNL AUTH 2 J.M.TREVILLYAN,C.ABAD-ZAPATERO,E.H.FRY,H.L.SHAM,G.LIU
JRNL TITL DISCOVERY OF A NEW CLASS OF 4-ANILINOPYRIMIDINES AS POTENT
JRNL TITL 2 C-JUN N-TERMINAL KINASE INHIBITORS: SYNTHESIS AND SAR
JRNL TITL 3 STUDIES.
JRNL REF BIOORG.MED.CHEM.LETT. V. 17 668 2007
JRNL REFN ISSN 0960-894X
JRNL PMID 17107797
JRNL DOI 10.1016/J.BMCL.2006.10.093
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.LIU,Z.XIN,J.E.CLAMPIT,S.WANG,R.J.GUM,D.L.HAASCH,
REMARK 1 AUTH 2 J.M.TREVILLYAN,C.ABAD-ZAPATERO,E.H.FRY,H.L.SHAM
REMARK 1 TITL SYNTHESIS AND SAR OF
REMARK 1 TITL 2 1,9-DIHYDRO-9-HYDROXYPYRAZOLO[3,4-B]QUINOLIN-4-ONES AS
REMARK 1 TITL 3 NOVEL, SELECTIVE C-JUN N-TERMINAL KINASE INHIBITORS.
REMARK 1 REF BIOORG.MED.CHEM.LETT. V. 16 2590 2006
REMARK 1 REFN ISSN 0960-894X
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.G.SZCZEPANKIEWICZ,C.KOSOGOF,L.T.J.NELSON,G.LIU,H.ZHAO,
REMARK 1 AUTH 2 M.D.SERBY,Z.XIN,B.LIU,R.J.GUM,D.HAASCH
REMARK 1 TITL SELECTIVE AMINOPYRIDINE-BASED C-JUN N-TERMINAL KINASE
REMARK 1 TITL 2 INHIBITORS WITH CELLULAR ACTIVIY
REMARK 1 REF J.MED.CHEM. V. 49 3563 2006
REMARK 1 REFN ISSN 0022-2623
REMARK 1 REFERENCE 3
REMARK 1 AUTH H.ZHAO,M.D.SERBY,Z.XIN,B.G.SZCZEPANKIEWICZ,M.LIU,C.KOSOGOF,
REMARK 1 AUTH 2 B.LIU,R.J.GUM,J.E.CLAMPIT,D.L.HAASCH
REMARK 1 TITL DISCOVERY OF POTENT, HIGHLY SELECTIVE AND ORALLY
REMARK 1 TITL 2 BIOAVAILABLE PYRIDINE CARBOXAMIDE C-JUN NH2-TERMINAL KINASE
REMARK 1 TITL 3 INHIBITORS
REMARK 1 REF J.MED.CHEM. V. 49 4455 2006
REMARK 1 REFN ISSN 0022-2623
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2002
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) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 162862.680
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 75.2
REMARK 3 NUMBER OF REFLECTIONS : 22039
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) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2180
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.31
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 45.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1163
REMARK 3 BIN R VALUE (WORKING SET) : 0.2780
REMARK 3 BIN FREE R VALUE : 0.3350
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 11.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 153
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.027
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5897
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 68
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.93000
REMARK 3 B22 (A**2) : 7.93000
REMARK 3 B33 (A**2) : -15.87000
REMARK 3 B12 (A**2) : 22.73000
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) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.34
REMARK 3 LOW RESOLUTION CUTOFF (A) : 8.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.48
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.44
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.30
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.830
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.22
REMARK 3 BSOL : 24.18
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 : ACCELRYS_CNX_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : GCR.PAR
REMARK 3 PARAMETER FILE 3 : ACCELRYS_CNX_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 4 : 859.PAR
REMARK 3 PARAMETER FILE 5 : SO4.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : GCR.TOP
REMARK 3 TOPOLOGY FILE 3 : ACCELRYS_CNX_TOPPAR:ION.PARAM
REMARK 3 TOPOLOGY FILE 4 : 859.TOP
REMARK 3 TOPOLOGY FILE 5 : SO4.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2NO3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1000040098.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JAN-05
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27814
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : 0.08300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.45400
REMARK 200 R SYM FOR SHELL (I) : 0.81200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
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: ENTRY 2H96
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS PREINCUBATED WITH THE JIP1
REMARK 280 PEPTIDE AT A 5X MOLAR EXCESS. PROTEIN CONCENTRATION 9- 12.6 MG/
REMARK 280 ML. HANGING DROPS CONSISTED OF 2UL PROTEIN PLUS 2 UL WELL
REMARK 280 SOLUTION. WELL SOLUTION:2.8-3.1 M AMMONIUM SULFATE, 10- 14%
REMARK 280 GLYCEROL. FOR CO-CRYSTALLIZATION EXPERIMENT WITH THE COMPOUND,
REMARK 280 THE COMPOUND WAS DISSOLVED IN DMSO AT 100 MM CONCENTRATION.
REMARK 280 ALLOW TO INCUBATE FOR AT LEAST AN HOUR ON ICE. SOLUTION WAS SPUN
REMARK 280 FOR 5 MINUTES AT 2000G PRIOR TO SETTING UP FOR CRYSTALLIZATION.,
REMARK 280 PH 6.20, VAPOR DIFFUSION, TEMPERATURE 277.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.24133
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 41.12067
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 41.12067
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 82.24133
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F, B, G
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 1
REMARK 465 SER A 2
REMARK 465 ARG A 3
REMARK 465 SER A 4
REMARK 465 LYS A 5
REMARK 465 ARG A 6
REMARK 465 ASP A 7
REMARK 465 HIS A 365
REMARK 465 HIS A 366
REMARK 465 HIS A 367
REMARK 465 HIS A 368
REMARK 465 HIS A 369
REMARK 465 HIS A 370
REMARK 465 ARG F 553
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ARG B 3
REMARK 465 SER B 4
REMARK 465 LYS B 5
REMARK 465 ARG B 6
REMARK 465 GLU B 364
REMARK 465 HIS B 365
REMARK 465 HIS B 366
REMARK 465 HIS B 367
REMARK 465 HIS B 368
REMARK 465 HIS B 369
REMARK 465 HIS B 370
REMARK 465 ARG G 553
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 LYS A 24 CG CD CE NZ
REMARK 470 LYS A 68 CG CD CE NZ
REMARK 470 GLU A 185 CG CD OE1 OE2
REMARK 470 GLU A 346 CG CD OE1 OE2
REMARK 470 LYS A 358 CG CD CE NZ
REMARK 470 LYS B 24 CG CD CE NZ
REMARK 470 ARG B 69 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 174 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 183 CG CD OE1 OE2
REMARK 470 GLU B 185 CG CD OE1 OE2
REMARK 470 LYS B 358 CG CD CE NZ
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 319 C - N - CA ANGL. DEV. = 10.3 DEGREES
REMARK 500 PRO B 333 C - N - CA ANGL. DEV. = 9.8 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 PHE A 10 -172.58 -65.30
REMARK 500 TYR A 11 -155.19 -165.43
REMARK 500 ILE A 15 74.13 -109.26
REMARK 500 ASP A 17 25.04 -70.16
REMARK 500 LYS A 24 -18.53 -49.20
REMARK 500 ASN A 28 81.73 48.07
REMARK 500 LYS A 30 136.07 -170.73
REMARK 500 ILE A 32 -6.50 -149.69
REMARK 500 SER A 34 77.05 -105.73
REMARK 500 GLU A 49 46.12 70.08
REMARK 500 ARG A 59 78.16 36.57
REMARK 500 PRO A 60 -19.52 -45.54
REMARK 500 PHE A 61 27.41 -156.38
REMARK 500 GLN A 62 -84.82 -44.04
REMARK 500 GLN A 64 -6.98 -57.08
REMARK 500 ALA A 67 -72.90 -68.00
REMARK 500 LYS A 68 -35.90 -31.85
REMARK 500 LEU A 74 -74.91 -47.01
REMARK 500 CYS A 79 -0.96 -59.34
REMARK 500 ILE A 86 112.64 -21.77
REMARK 500 PHE A 92 -153.30 -166.66
REMARK 500 THR A 93 125.51 -175.85
REMARK 500 LEU A 98 -74.88 -29.65
REMARK 500 GLN A 102 7.65 179.59
REMARK 500 GLU A 109 -173.89 -55.57
REMARK 500 ARG A 127 -71.89 -56.18
REMARK 500 SER A 144 -6.96 -59.03
REMARK 500 ARG A 150 -24.17 61.32
REMARK 500 LYS A 153 161.25 175.67
REMARK 500 SER A 155 -28.67 -38.09
REMARK 500 ASP A 169 137.69 75.82
REMARK 500 ALA A 176 -87.11 19.82
REMARK 500 THR A 178 -40.44 -23.92
REMARK 500 SER A 179 -132.92 -167.15
REMARK 500 PHE A 180 42.37 -103.23
REMARK 500 MET A 181 -156.62 45.79
REMARK 500 ARG A 189 -87.31 -32.85
REMARK 500 TYR A 190 -22.20 -29.44
REMARK 500 ASN A 205 -2.88 -55.22
REMARK 500 HIS A 221 11.35 80.99
REMARK 500 LEU A 224 -71.34 -65.70
REMARK 500 PHE A 225 75.86 -106.24
REMARK 500 PRO A 226 -129.94 -43.55
REMARK 500 ASP A 277 -41.35 -27.63
REMARK 500 SER A 284 -112.87 -106.26
REMARK 500 GLU A 285 -16.71 -141.93
REMARK 500 ILE A 310 119.23 -28.32
REMARK 500 PRO A 319 -20.77 -36.87
REMARK 500 VAL A 323 -1.30 -56.45
REMARK 500 ASP A 326 111.56 -160.43
REMARK 500
REMARK 500 THIS ENTRY HAS 122 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 SO4 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 859 A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 859 B 902
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2G01 RELATED DB: PDB
REMARK 900 PYRAZOLOQUINOLONES AS NOVEL, SELECTIVE JNK1 INHIBITORS
REMARK 900 RELATED ID: 2GMX RELATED DB: PDB
REMARK 900 SELECTIVE AMINOPYRIDINE-BASED C-JUN N-TERMINAL KINASE INHIBITORS
REMARK 900 WITH CELLULAR ACTIVITY
REMARK 900 RELATED ID: 2H96 RELATED DB: PDB
REMARK 900 HIGHLY SELECTIVE AND ORALLY BIOAVAILABLE PYRIDINE CARBOXAMIDE JNK1
REMARK 900 INHIHIBITORS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE NATIVE, UNMUTATED SEQUENCE IS THE SAME AS
REMARK 999 THE P45983-2 ISOFORM. THE INTRODUCED MUTATIONS
REMARK 999 (THR183>GLU, TYR185>GLU) ARE INTENDED TO MIMIC
REMARK 999 THE ACTIVATED FORM OF THE KINASE UPON
REMARK 999 PHOSPHORYLATION OF THOSE TWO RESIDUES.
DBREF 2NO3 A 1 364 UNP P45983 MK08_HUMAN 1 364
DBREF 2NO3 B 1 364 UNP P45983 MK08_HUMAN 1 364
DBREF 2NO3 F 553 563 PDB 2NO3 2NO3 553 563
DBREF 2NO3 G 553 563 PDB 2NO3 2NO3 553 563
SEQADV 2NO3 GLU A 183 UNP P45983 THR 183 ENGINEERED MUTATION
SEQADV 2NO3 GLU A 185 UNP P45983 TYR 185 ENGINEERED MUTATION
SEQADV 2NO3 HIS A 365 UNP P45983 EXPRESSION TAG
SEQADV 2NO3 HIS A 366 UNP P45983 EXPRESSION TAG
SEQADV 2NO3 HIS A 367 UNP P45983 EXPRESSION TAG
SEQADV 2NO3 HIS A 368 UNP P45983 EXPRESSION TAG
SEQADV 2NO3 HIS A 369 UNP P45983 EXPRESSION TAG
SEQADV 2NO3 HIS A 370 UNP P45983 EXPRESSION TAG
SEQADV 2NO3 GLU B 183 UNP P45983 THR 183 ENGINEERED MUTATION
SEQADV 2NO3 GLU B 185 UNP P45983 TYR 185 ENGINEERED MUTATION
SEQADV 2NO3 HIS B 365 UNP P45983 EXPRESSION TAG
SEQADV 2NO3 HIS B 366 UNP P45983 EXPRESSION TAG
SEQADV 2NO3 HIS B 367 UNP P45983 EXPRESSION TAG
SEQADV 2NO3 HIS B 368 UNP P45983 EXPRESSION TAG
SEQADV 2NO3 HIS B 369 UNP P45983 EXPRESSION TAG
SEQADV 2NO3 HIS B 370 UNP P45983 EXPRESSION TAG
SEQRES 1 A 370 MET SER ARG SER LYS ARG ASP ASN ASN PHE TYR SER VAL
SEQRES 2 A 370 GLU ILE GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR
SEQRES 3 A 370 GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE
SEQRES 4 A 370 VAL CYS ALA ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL
SEQRES 5 A 370 ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR
SEQRES 6 A 370 HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS
SEQRES 7 A 370 CYS VAL ASN HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL
SEQRES 8 A 370 PHE THR PRO GLN LYS SER LEU GLU GLU PHE GLN ASP VAL
SEQRES 9 A 370 TYR ILE VAL MET GLU LEU MET ASP ALA ASN LEU CYS GLN
SEQRES 10 A 370 VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR
SEQRES 11 A 370 LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU HIS
SEQRES 12 A 370 SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN
SEQRES 13 A 370 ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU ASP
SEQRES 14 A 370 PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET
SEQRES 15 A 370 GLU PRO GLU VAL VAL THR ARG TYR TYR ARG ALA PRO GLU
SEQRES 16 A 370 VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP LEU
SEQRES 17 A 370 TRP SER VAL GLY CYS ILE MET GLY GLU MET VAL CYS HIS
SEQRES 18 A 370 LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP
SEQRES 19 A 370 ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO GLU
SEQRES 20 A 370 PHE MET LYS LYS LEU GLN PRO THR VAL ARG THR TYR VAL
SEQRES 21 A 370 GLU ASN ARG PRO LYS TYR ALA GLY TYR SER PHE GLU LYS
SEQRES 22 A 370 LEU PHE PRO ASP VAL LEU PHE PRO ALA ASP SER GLU HIS
SEQRES 23 A 370 ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER
SEQRES 24 A 370 LYS MET LEU VAL ILE ASP ALA SER LYS ARG ILE SER VAL
SEQRES 25 A 370 ASP GLU ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR
SEQRES 26 A 370 ASP PRO SER GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO
SEQRES 27 A 370 ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU
SEQRES 28 A 370 TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASP LEU GLU
SEQRES 29 A 370 HIS HIS HIS HIS HIS HIS
SEQRES 1 F 11 ARG PRO LYS ARG PRO THR THR LEU ASN LEU PHE
SEQRES 1 B 370 MET SER ARG SER LYS ARG ASP ASN ASN PHE TYR SER VAL
SEQRES 2 B 370 GLU ILE GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR
SEQRES 3 B 370 GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE
SEQRES 4 B 370 VAL CYS ALA ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL
SEQRES 5 B 370 ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR
SEQRES 6 B 370 HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS
SEQRES 7 B 370 CYS VAL ASN HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL
SEQRES 8 B 370 PHE THR PRO GLN LYS SER LEU GLU GLU PHE GLN ASP VAL
SEQRES 9 B 370 TYR ILE VAL MET GLU LEU MET ASP ALA ASN LEU CYS GLN
SEQRES 10 B 370 VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR
SEQRES 11 B 370 LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU HIS
SEQRES 12 B 370 SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN
SEQRES 13 B 370 ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU ASP
SEQRES 14 B 370 PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET
SEQRES 15 B 370 GLU PRO GLU VAL VAL THR ARG TYR TYR ARG ALA PRO GLU
SEQRES 16 B 370 VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP LEU
SEQRES 17 B 370 TRP SER VAL GLY CYS ILE MET GLY GLU MET VAL CYS HIS
SEQRES 18 B 370 LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP
SEQRES 19 B 370 ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO GLU
SEQRES 20 B 370 PHE MET LYS LYS LEU GLN PRO THR VAL ARG THR TYR VAL
SEQRES 21 B 370 GLU ASN ARG PRO LYS TYR ALA GLY TYR SER PHE GLU LYS
SEQRES 22 B 370 LEU PHE PRO ASP VAL LEU PHE PRO ALA ASP SER GLU HIS
SEQRES 23 B 370 ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER
SEQRES 24 B 370 LYS MET LEU VAL ILE ASP ALA SER LYS ARG ILE SER VAL
SEQRES 25 B 370 ASP GLU ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR
SEQRES 26 B 370 ASP PRO SER GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO
SEQRES 27 B 370 ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU
SEQRES 28 B 370 TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASP LEU GLU
SEQRES 29 B 370 HIS HIS HIS HIS HIS HIS
SEQRES 1 G 11 ARG PRO LYS ARG PRO THR THR LEU ASN LEU PHE
HET SO4 A 701 5
HET SO4 A 702 5
HET 859 A 901 24
HET SO4 B 801 5
HET SO4 B 802 5
HET 859 B 902 24
HETNAM SO4 SULFATE ION
HETNAM 859 2-({2-[(3-HYDROXYPHENYL)AMINO]PYRIMIDIN-4-YL}AMINO)
HETNAM 2 859 BENZAMIDE
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 7 859 2(C17 H15 N5 O2)
HELIX 1 1 ASN A 63 VAL A 80 1 18
HELIX 2 2 LEU A 115 GLN A 120 1 6
HELIX 3 3 ASP A 124 SER A 144 1 21
HELIX 4 4 LYS A 153 SER A 155 5 3
HELIX 5 5 THR A 188 ARG A 192 5 5
HELIX 6 6 ALA A 193 LEU A 198 1 6
HELIX 7 7 ASN A 205 HIS A 221 1 17
HELIX 8 8 ILE A 231 GLY A 242 1 12
HELIX 9 9 CYS A 245 LYS A 251 1 7
HELIX 10 10 GLN A 253 ASN A 262 1 10
HELIX 11 11 SER A 270 PHE A 275 1 6
HELIX 12 12 PRO A 276 PHE A 280 5 5
HELIX 13 13 LYS A 290 LEU A 302 1 13
HELIX 14 14 ASP A 305 ARG A 309 5 5
HELIX 15 15 SER A 311 HIS A 318 1 8
HELIX 16 16 ILE A 321 TYR A 325 5 5
HELIX 17 17 ASP A 326 GLU A 331 1 6
HELIX 18 18 THR A 348 MET A 361 1 14
HELIX 19 19 ASP A 362 GLU A 364 5 3
HELIX 20 20 THR B 65 VAL B 80 1 16
HELIX 21 21 ASN B 114 GLN B 120 1 7
HELIX 22 22 ASP B 124 SER B 144 1 21
HELIX 23 23 LYS B 153 SER B 155 5 3
HELIX 24 24 THR B 188 ARG B 192 5 5
HELIX 25 25 ALA B 193 LEU B 198 1 6
HELIX 26 26 GLU B 204 HIS B 221 1 18
HELIX 27 27 ILE B 231 GLY B 242 1 12
HELIX 28 28 CYS B 245 LYS B 250 1 6
HELIX 29 29 GLN B 253 ARG B 263 1 11
HELIX 30 30 PRO B 276 PHE B 280 5 5
HELIX 31 31 LYS B 290 LEU B 302 1 13
HELIX 32 32 SER B 311 GLN B 317 1 7
HELIX 33 33 HIS B 318 VAL B 323 1 6
HELIX 34 34 ILE B 349 VAL B 360 1 12
SHEET 1 A 2 VAL A 13 GLU A 14 0
SHEET 2 A 2 THR A 19 PHE A 20 -1 O PHE A 20 N VAL A 13
SHEET 1 B 3 TYR A 26 GLN A 27 0
SHEET 2 B 3 ILE A 39 ASP A 45 -1 O TYR A 44 N GLN A 27
SHEET 3 B 3 PRO A 31 SER A 34 -1 N GLY A 33 O VAL A 40
SHEET 1 C 5 TYR A 26 GLN A 27 0
SHEET 2 C 5 ILE A 39 ASP A 45 -1 O TYR A 44 N GLN A 27
SHEET 3 C 5 ARG A 50 LEU A 57 -1 O VAL A 52 N ALA A 43
SHEET 4 C 5 VAL A 104 MET A 108 -1 O ILE A 106 N LYS A 55
SHEET 5 C 5 LEU A 88 PHE A 92 -1 N ASN A 90 O VAL A 107
SHEET 1 D 3 ALA A 113 ASN A 114 0
SHEET 2 D 3 ILE A 157 VAL A 159 -1 O VAL A 159 N ALA A 113
SHEET 3 D 3 LEU A 165 ILE A 167 -1 O LYS A 166 N VAL A 158
SHEET 1 E 2 ILE A 147 ILE A 148 0
SHEET 2 E 2 ARG A 174 THR A 175 -1 O ARG A 174 N ILE A 148
SHEET 1 F 5 TYR B 26 GLY B 33 0
SHEET 2 F 5 ILE B 39 ASP B 45 -1 O VAL B 40 N GLY B 33
SHEET 3 F 5 ARG B 50 LEU B 57 -1 O ILE B 54 N CYS B 41
SHEET 4 F 5 VAL B 104 GLU B 109 -1 O MET B 108 N ALA B 53
SHEET 5 F 5 LEU B 88 PHE B 92 -1 N ASN B 90 O VAL B 107
SHEET 1 G 2 ILE B 157 VAL B 158 0
SHEET 2 G 2 LYS B 166 ILE B 167 -1 O LYS B 166 N VAL B 158
SITE 1 AC1 4 ARG A 189 ARG A 192 TYR A 230 THR B 255
SITE 1 AC2 2 ARG A 69 ARG A 150
SITE 1 AC3 4 THR A 255 ARG B 189 ARG B 192 TYR B 230
SITE 1 AC4 3 LYS B 68 ARG B 150 MET B 182
SITE 1 AC5 11 GLY A 33 VAL A 40 LYS A 55 MET A 108
SITE 2 AC5 11 GLU A 109 LEU A 110 MET A 111 ASP A 112
SITE 3 AC5 11 ASN A 114 LEU A 168 ASP A 169
SITE 1 AC6 14 ARG A 50 ILE B 32 GLY B 33 VAL B 40
SITE 2 AC6 14 ILE B 86 MET B 108 GLU B 109 LEU B 110
SITE 3 AC6 14 MET B 111 ASP B 112 ALA B 113 ASN B 114
SITE 4 AC6 14 VAL B 158 LEU B 168
CRYST1 157.201 157.201 123.362 90.00 90.00 120.00 P 32 2 1 12
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 0.006361 0.003673 0.000000 0.00000
SCALE2 0.000000 0.007345 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008106 0.00000
(ATOM LINES ARE NOT SHOWN.)
END