HEADER LIGASE/ANTAGONIST 05-FEB-13 4J3E
TITLE THE 1.9A CRYSTAL STRUCTURE OF HUMANIZED XENOPUS MDM2 WITH NUTLIN-3A
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, PROTEIN-PROTEIN INTERACTION, IMIDAZOLINE, LIGASE-ANTAGONIST
KEYWDS 2 COMPLEX, E3 UBIQUITIN LIGASE, P53, NUCLEUS
EXPDTA X-RAY DIFFRACTION
AUTHOR B.J.GRAVES,C.M.LUKACS,R.U.KAMMLOTT,R.CROWTHER
REVDAT 3 28-FEB-24 4J3E 1 REMARK SEQADV
REVDAT 2 08-OCT-14 4J3E 1 JRNL
REVDAT 1 24-APR-13 4J3E 0
JRNL AUTH B.VU,P.WOVKULICH,G.PIZZOLATO,A.LOVEY,Q.DING,N.JIANG,J.J.LIU,
JRNL AUTH 2 C.ZHAO,K.GLENN,Y.WEN,C.TOVAR,K.PACKMAN,L.VASSILEV,B.GRAVES
JRNL TITL DISCOVERY OF RG7112: A SMALL-MOLECULE MDM2 INHIBITOR IN
JRNL TITL 2 CLINICAL DEVELOPMENT.
JRNL REF ACS MED CHEM LETT V. 4 466 2013
JRNL REFN ISSN 1948-5875
JRNL PMID 24900694
JRNL DOI 10.1021/ML4000657
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.TOVAR,B.GRAVES,K.PACKMAN,Z.FILIPOVIC,B.H.XIA,C.TARDELL,
REMARK 1 AUTH 2 R.GARRIDO,E.LEE,K.KOLINSKY,K.H.TO,M.LINN,F.PODLASKI,
REMARK 1 AUTH 3 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. V. 73 2587 2013
REMARK 1 REFN ISSN 0008-5472
REMARK 1 PMID 23400593
REMARK 1 DOI 10.1158/0008-5472.CAN-12-2807
REMARK 1 REFERENCE 2
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. 1.91 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) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1199476.880
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 7488
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 384
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.012
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.1960
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.1940
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 384
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0120
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 7488
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) : 1.91
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 985
REMARK 3 BIN R VALUE (WORKING SET) : 0.1700
REMARK 3 BIN FREE R VALUE : 0.2380
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 48
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 : 128
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.59000
REMARK 3 B22 (A**2) : -0.39000
REMARK 3 B33 (A**2) : 0.98000
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) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.05
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) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.13
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.130
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) : 1.400 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.160 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.240 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.200 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 46.86
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 : RO4435385.PRX
REMARK 3 PARAMETER FILE 5 : NULL
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 : RO4435385.TPX
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4J3E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1000077545.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7488
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.910
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 (%) : 95.3
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.03900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 46.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.06400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 29.80
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 (%): 49.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM ADA, PH 6, 50% SATURATED
REMARK 280 AMMONIUM SULFATE, 5% PEG200, 5 MM DTT RESERVOIR MIXED IN EQUAL
REMARK 280 VOLUME WITH THE PROTEIN AT 10 MG/ML, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 278K, PH 6.0
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 33.58650
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 33.58650
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 21.44350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.82850
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 21.44350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.82850
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 33.58650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 21.44350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 33.82850
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 33.58650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 21.44350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 33.82850
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 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 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 423 LIES ON A SPECIAL POSITION.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NUT A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IPF RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WITH RO5045337
REMARK 900 RELATED ID: 1RV1 RELATED DB: PDB
REMARK 900 HUMAN MDM2 COMPLEXED WITH NUTLIN-2
DBREF 4J3E A 21 105 UNP P56273 MDM2_XENLA 21 105
SEQADV 4J3E MET A 20 UNP P56273 INITIATING METHIONINE
SEQADV 4J3E LEU A 50 UNP P56273 ILE 50 ENGINEERED MUTATION
SEQADV 4J3E HIS A 92 UNP P56273 PRO 92 ENGINEERED MUTATION
SEQADV 4J3E 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 NUT A 201 40
HET SO4 A 202 5
HETNAM NUT 4-({(4S,5R)-4,5-BIS(4-CHLOROPHENYL)-2-[4-METHOXY-2-
HETNAM 2 NUT (PROPAN-2-YLOXY)PHENYL]-4,5-DIHYDRO-1H-IMIDAZOL-1-
HETNAM 3 NUT YL}CARBONYL)PIPERAZIN-2-ONE
HETNAM SO4 SULFATE ION
HETSYN NUT NUTLIN 3A
FORMUL 2 NUT C30 H30 CL2 N4 O4
FORMUL 3 SO4 O4 S 2-
FORMUL 4 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 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 13 LEU A 50 LEU A 53 GLY A 54 GLN A 55
SITE 2 AC1 13 ILE A 57 MET A 58 VAL A 89 HIS A 92
SITE 3 AC1 13 ILE A 95 TYR A 96 HOH A 306 HOH A 308
SITE 4 AC1 13 HOH A 347
SITE 1 AC2 10 MET A 20 ASN A 75 GLU A 91 HIS A 92
SITE 2 AC2 10 ARG A 93 ARG A 94 HOH A 311 HOH A 335
SITE 3 AC2 10 HOH A 341 HOH A 388
CRYST1 42.887 67.657 67.173 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 0.023317 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014780 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014887 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
