HEADER LIGASE/LIGASE INHIBITOR 21-MAR-13 4JRG
TITLE THE 1.9A CRYSTAL STRUCTURE OF HUMANIZED XENOPUS MDM2 WITH RO5313109 -
TITLE 2 A PYRROLIDINE MDM2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE MDM2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN (UNP RESIDUES 21-105);
COMPND 5 SYNONYM: DOUBLE MINUTE 2 PROTEIN, XDM2, P53-BINDING PROTEIN MDM2;
COMPND 6 EC: 6.3.2.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 GENE: MDM2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PUBS 520
KEYWDS PROTEIN-INHIBITOR COMPLEX, PYRROLIDINE, E3 UBIQUITIN LIGASE, P53,
KEYWDS 2 NUCLEUS, LIGASE-LIGASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.J.GRAVES,C.A.JANSON,C.LUKACS
REVDAT 2 05-FEB-14 4JRG 1 JRNL
REVDAT 1 24-JUL-13 4JRG 0
JRNL AUTH Q.DING,Z.ZHANG,J.J.LIU,N.JIANG,J.ZHANG,T.M.ROSS,X.J.CHU,
JRNL AUTH 2 D.BARTKOVITZ,F.PODLASKI,C.JANSON,C.TOVAR,Z.M.FILIPOVIC,
JRNL AUTH 3 B.HIGGINS,K.GLENN,K.PACKMAN,L.T.VASSILEV,B.GRAVES
JRNL TITL DISCOVERY OF RG7388, A POTENT AND SELECTIVE P53-MDM2
JRNL TITL 2 INHIBITOR IN CLINICAL DEVELOPMENT.
JRNL REF J.MED.CHEM. V. 56 5979 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23808545
JRNL DOI 10.1021/JM400487C
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.TOVAR,B.GRAVES,K.PACKMAN,Z.FILIPOVIC,B.HIGGINS,M.XIA,
REMARK 1 AUTH 2 C.TARDELL,R.GARRIDO,E.LEE,K.KOLINSKY,K.H.TO,M.LINN,
REMARK 1 AUTH 3 F.PODLASKI,P.WOVKULICH,B.VU,L.T.VASSILEV
REMARK 1 TITL MDM2 SMALL-MOLECULE ANTAGONIST RG7112 ACTIVATES P53
REMARK 1 TITL 2 SIGNALING AND REGRESSES HUMAN TUMORS IN PRECLINICAL CANCER
REMARK 1 TITL 3 MODELS.
REMARK 1 REF CANCER RES. 2013
REMARK 1 REFN ESSN 1538-7445
REMARK 1 PMID 23400593
REMARK 1 DOI 10.1158/0008-5472.CAN-12-2807
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 957499.440
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 16827
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) : 0.252
REMARK 3 R VALUE (WORKING SET) : 0.250
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 853
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.2980
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2970
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.328
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 853
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0110
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 16827
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2587
REMARK 3 BIN R VALUE (WORKING SET) : 0.4350
REMARK 3 BIN FREE R VALUE : 0.4550
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 142
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.038
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1366
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 128
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 16.13000
REMARK 3 B22 (A**2) : -9.55000
REMARK 3 B33 (A**2) : -6.58000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 4.88000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.50
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) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.51
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.000
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.000
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.680
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) : 1.420 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.280 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.340 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.390 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 50.84
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARA
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : RO5313109-A.PRX
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : RO5313109-A.TPX
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4JRG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-13.
REMARK 100 THE RCSB ID CODE IS RCSB078410.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16829
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.43600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50% SATURATED AMMONIUM SULFATE, 0.1M
REMARK 280 BIS-TRIS, PH 6.0, 5% PEG 550MME, 5 MM DTT, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 278K
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 36.77100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.39800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 36.77100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 36.39800
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 300 REMARK: FULL-LENGTH PROTEIN IS A DIMER, FORMED BY CONTACTS IN THE C
REMARK 300 -TERMINAL DOMAIN BUT THE N-TERMINAL DOMAIN ON ITS OWN IS A MONOMER
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 348 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 365 LIES ON A SPECIAL POSITION.
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 SER A 105
REMARK 465 SER B 105
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 CYS A 73 20.51 -142.23
REMARK 500 LYS B 41 -169.92 -128.50
REMARK 500 CYS B 73 25.30 -142.26
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 I09 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I09 B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IPF RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH RG7112, A NUTLIN IN CLINICAL DEVELOPMENT
DBREF 4JRG A 21 105 UNP P56273 MDM2_XENLA 21 105
DBREF 4JRG B 21 105 UNP P56273 MDM2_XENLA 21 105
SEQADV 4JRG LEU A 50 UNP P56273 ILE 50 ENGINEERED MUTATION
SEQADV 4JRG HIS A 92 UNP P56273 PRO 92 ENGINEERED MUTATION
SEQADV 4JRG ILE A 95 UNP P56273 LEU 95 ENGINEERED MUTATION
SEQADV 4JRG LEU B 50 UNP P56273 ILE 50 ENGINEERED MUTATION
SEQADV 4JRG HIS B 92 UNP P56273 PRO 92 ENGINEERED MUTATION
SEQADV 4JRG ILE B 95 UNP P56273 LEU 95 ENGINEERED MUTATION
SEQRES 1 A 85 GLU LYS LEU VAL GLN PRO THR PRO LEU LEU LEU SER LEU
SEQRES 2 A 85 LEU LYS SER ALA GLY ALA GLN LYS GLU THR PHE THR MET
SEQRES 3 A 85 LYS GLU VAL LEU TYR HIS LEU GLY GLN TYR ILE MET ALA
SEQRES 4 A 85 LYS GLN LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL HIS
SEQRES 5 A 85 CYS SER ASN ASP PRO LEU GLY GLU LEU PHE GLY VAL GLN
SEQRES 6 A 85 GLU PHE SER VAL LYS GLU HIS ARG ARG ILE TYR ALA MET
SEQRES 7 A 85 ILE SER ARG ASN LEU VAL SER
SEQRES 1 B 85 GLU LYS LEU VAL GLN PRO THR PRO LEU LEU LEU SER LEU
SEQRES 2 B 85 LEU LYS SER ALA GLY ALA GLN LYS GLU THR PHE THR MET
SEQRES 3 B 85 LYS GLU VAL LEU TYR HIS LEU GLY GLN TYR ILE MET ALA
SEQRES 4 B 85 LYS GLN LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL HIS
SEQRES 5 B 85 CYS SER ASN ASP PRO LEU GLY GLU LEU PHE GLY VAL GLN
SEQRES 6 B 85 GLU PHE SER VAL LYS GLU HIS ARG ARG ILE TYR ALA MET
SEQRES 7 B 85 ILE SER ARG ASN LEU VAL SER
HET I09 A 201 35
HET I09 B 201 35
HETNAM I09 (3R,4R,5S)-3-(3-CHLOROPHENYL)-4-(4-CHLOROPHENYL)-4-
HETNAM 2 I09 CYANO-N-[(3S)-3,4-DIHYDROXYBUTYL]-5-(2,2-
HETNAM 3 I09 DIMETHYLPROPYL)-D-PROLINAMIDE
FORMUL 3 I09 2(C27 H33 CL2 N3 O3)
FORMUL 5 HOH *128(H2 O)
HELIX 1 1 THR A 27 ALA A 37 1 11
HELIX 2 2 THR A 45 GLN A 61 1 17
HELIX 3 3 ASP A 76 GLY A 83 1 8
HELIX 4 4 GLU A 91 ARG A 101 1 11
HELIX 5 5 THR B 27 ALA B 37 1 11
HELIX 6 6 THR B 45 LYS B 60 1 16
HELIX 7 7 ASP B 76 GLY B 83 1 8
HELIX 8 8 GLU B 91 ARG B 101 1 11
SHEET 1 A 2 GLN A 25 PRO A 26 0
SHEET 2 A 2 LEU A 103 VAL A 104 -1 O VAL A 104 N GLN A 25
SHEET 1 B 2 ILE A 70 HIS A 72 0
SHEET 2 B 2 GLU A 86 SER A 88 -1 O PHE A 87 N VAL A 71
SHEET 1 C 2 ILE B 70 HIS B 72 0
SHEET 2 C 2 GLU B 86 SER B 88 -1 O PHE B 87 N VAL B 71
SITE 1 AC1 12 LEU A 50 ILE A 57 MET A 58 HIS A 69
SITE 2 AC1 12 PHE A 82 VAL A 89 LYS A 90 HIS A 92
SITE 3 AC1 12 ILE A 95 TYR A 96 HOH A 331 HOH A 332
SITE 1 AC2 9 LEU B 50 GLY B 54 MET B 58 HIS B 69
SITE 2 AC2 9 VAL B 89 LYS B 90 HIS B 92 HOH B 325
SITE 3 AC2 9 HOH B 326
CRYST1 73.542 72.796 43.865 90.00 111.78 90.00 C 1 2 1 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 0.013598 0.000000 0.005434 0.00000
SCALE2 0.000000 0.013737 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024550 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
