HEADER LIGASE/ANTAGONIST 12-FEB-13 4J74
TITLE THE 1.2A CRYSTAL STRUCTURE OF HUMANIZED XENOPUS MDM2 WITH RO0503918 -
TITLE 2 A NUTLIN FRAGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE MDM2;
COMPND 3 CHAIN: A;
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 MDM2, IMIDAZOLINE, LIGASE-ANTAGONIST COMPLEX, E3 UBIQUITIN LIGASE,
KEYWDS 2 P53, NUCLEUS
EXPDTA X-RAY DIFFRACTION
AUTHOR C.JANSON,C.LUKACS,U.KAMMLOTT,B.GRAVES
REVDAT 2 24-SEP-14 4J74 1 JRNL
REVDAT 1 07-AUG-13 4J74 0
JRNL AUTH D.C.FRY,C.WARTCHOW,B.GRAVES,C.JANSON,C.LUKACS,U.KAMMLOTT,
JRNL AUTH 2 C.BELUNIS,S.PALME,C.KLEIN,B.VU
JRNL TITL DECONSTRUCTION OF A NUTLIN: DISSECTING THE BINDING
JRNL TITL 2 DETERMINANTS OF A POTENT PROTEIN-PROTEIN INTERACTION
JRNL TITL 3 INHIBITOR.
JRNL REF ACS MED CHEM LETT V. 4 660 2013
JRNL REFN ISSN 1948-5875
JRNL PMID 24900726
JRNL DOI 10.1021/ML400062C
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.VU,P.WOVKULICH,G.PIZZOLATO,N.JIANG,Q.DING,J.-J.LIU,
REMARK 1 AUTH 2 A.LOVEY,C.ZHAO,K.GLENN,Y.WEN,C.TOVAR,T.THOMPSON,L.VASSILEV,
REMARK 1 AUTH 3 B.GRAVES
REMARK 1 TITL DISCOVERY OF RG7112: A SMALL-MOLECULE MDM2 ANTAGONIST IN
REMARK 1 TITL 2 CLINICAL DEVELOPMENT
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 1 REFERENCE 2
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,M.LINN,F.PODLASKI,P.WOVKULICH,
REMARK 1 AUTH 3 B.VU,L.T.VASSILEV
REMARK 1 TITL MDM2 ANTAGONIST, RG7112, ACTIVATES P53 SIGNALLING AND
REMARK 1 TITL 2 REGRESSES HUMAN TUMORS IN PRECLINICAL CANCER MODELS
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 1 REFERENCE 3
REMARK 1 AUTH L.T.VASSILEV,B.T.VU,B.GRAVES,D.CARVAJAL,F.PODLASKI,
REMARK 1 AUTH 2 Z.FILIPOVIC,N.KONG,U.KAMMLOTT,C.LUKACS,C.KLEIN,N.FOTOUHI,
REMARK 1 AUTH 3 E.A.LIU
REMARK 1 TITL IN VIVO ACTIVATION OF THE P53 PATHWAY BY SMALL-MOLECULE
REMARK 1 TITL 2 ANTAGONISTS OF MDM2.
REMARK 1 REF SCIENCE V. 303 844 2004
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 14704432
REMARK 1 DOI 10.1126/SCIENCE.1092472
REMARK 2
REMARK 2 RESOLUTION. 1.20 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) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1760342.390
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 29710
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1456
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) : 0.2660
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2650
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1456
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0070
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 29710
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) : 1.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.21
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3264
REMARK 3 BIN FREE R VALUE : 0.4169
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 33
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 : 698
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 116
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.74000
REMARK 3 B22 (A**2) : 5.07000
REMARK 3 B33 (A**2) : -1.33000
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) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.15
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) : 0.18
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.14
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.000
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.820
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) : 1.120 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.730 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.090 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.060 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 53.61
REMARK 3
REMARK 3 NCS MODEL : NONE
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 : PROTEIN_REP.PARA
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : RO0503918.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 : RO0503918.TPX
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4J74 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAR-13.
REMARK 100 THE RCSB ID CODE IS RCSB077679.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34640
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.120
REMARK 200 RESOLUTION RANGE LOW (A) : 65.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.51200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
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 (%): 50.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40-50% SATURATED AMMONIUM SULFATE,
REMARK 280 0.1M MES, PH 6.5, 5% PEG200, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 278.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 33.59150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.59150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 21.47500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.27700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 21.47500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.27700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 33.59150
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 21.47500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 34.27700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 33.59150
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 21.47500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 34.27700
REMARK 290 SMTRY3 8 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 300 REMARK: THE N-TERMINAL DOMAIN OF MDM2 EXISTS AS A MONOMER WHILE THE
REMARK 300 FULL-LENGTH MOLECULE FORMS DIMERS
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 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 410 DISTANCE = 5.24 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I18 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I18 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IPF RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH RG7112 BOUND
REMARK 900 RELATED ID: 1RV1 RELATED DB: PDB
REMARK 900 HUMAN MDM2 WITH NUTLIN-2 BOUND
REMARK 900 RELATED ID: 4J3E RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH NUTLIN-3 BOUND
REMARK 900 RELATED ID: 4J7D RELATED DB: PDB
REMARK 900 RELATED ID: 4J7E RELATED DB: PDB
DBREF 4J74 A 21 105 UNP P56273 MDM2_XENLA 21 105
SEQADV 4J74 MET A 20 UNP P56273 INITIATING METHIONINE
SEQADV 4J74 LEU A 50 UNP P56273 ILE 50 ENGINEERED MUTATION
SEQADV 4J74 HIS A 92 UNP P56273 PRO 92 ENGINEERED MUTATION
SEQADV 4J74 ILE A 95 UNP P56273 LEU 95 ENGINEERED MUTATION
SEQRES 1 A 86 MET GLU LYS LEU VAL GLN PRO THR PRO LEU LEU LEU SER
SEQRES 2 A 86 LEU LEU LYS SER ALA GLY ALA GLN LYS GLU THR PHE THR
SEQRES 3 A 86 MET LYS GLU VAL LEU TYR HIS LEU GLY GLN TYR ILE MET
SEQRES 4 A 86 ALA LYS GLN LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL
SEQRES 5 A 86 HIS CYS SER ASN ASP PRO LEU GLY GLU LEU PHE GLY VAL
SEQRES 6 A 86 GLN GLU PHE SER VAL LYS GLU HIS ARG ARG ILE TYR ALA
SEQRES 7 A 86 MET ILE SER ARG ASN LEU VAL SER
HET I18 A 201 20
HET I18 A 202 20
HET SO4 A 203 5
HETNAM I18 (4S,5R)-4,5-BIS(4-CHLOROPHENYL)-2-METHYL-4,5-DIHYDRO-
HETNAM 2 I18 1H-IMIDAZOLE
HETNAM SO4 SULFATE ION
FORMUL 2 I18 2(C16 H14 CL2 N2)
FORMUL 4 SO4 O4 S 2-
FORMUL 5 HOH *116(H2 O)
HELIX 1 1 THR A 27 ALA A 37 1 11
HELIX 2 2 THR A 45 LYS A 60 1 16
HELIX 3 3 PRO A 77 GLY A 83 1 7
HELIX 4 4 GLU A 91 ARG A 101 1 11
SHEET 1 A 2 ILE A 70 HIS A 72 0
SHEET 2 A 2 GLU A 86 SER A 88 -1 O PHE A 87 N VAL A 71
SITE 1 AC1 8 LEU A 50 TYR A 63 VAL A 89 HIS A 92
SITE 2 AC1 8 ILE A 95 TYR A 96 HOH A 341 HOH A 368
SITE 1 AC2 8 SER A 36 ALA A 37 GLN A 55 MET A 58
SITE 2 AC2 8 TYR A 63 GLN A 68 HOH A 344 HOH A 365
SITE 1 AC3 9 ASN A 75 GLU A 91 HIS A 92 ARG A 93
SITE 2 AC3 9 ARG A 94 HOH A 340 HOH A 356 HOH A 373
SITE 3 AC3 9 HOH A 381
CRYST1 42.950 68.554 67.183 90.00 90.00 90.00 C 2 2 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 0.023283 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014587 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014885 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
