HEADER LIGASE 23-APR-15 4ZGK
TITLE STRUCTURE OF MDM2 WITH LOW MOLECULAR WEIGHT INHIBITOR.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE MDM2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 18-114;
COMPND 5 SYNONYM: DOUBLE MINUTE 2 PROTEIN,HDM2,ONCOPROTEIN MDM2,P53-BINDING
COMPND 6 PROTEIN MDM2;
COMPND 7 EC: 6.3.2.-;
COMPND 8 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: MDM2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693
KEYWDS P53-MDM2/MDMX INTERACTION, INHIBITOR, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.TWARDA-CLAPA,K.M.ZAK,E.M.WRONA,P.GRUDNIK,G.DUBIN,T.A.HOLAK
REVDAT 3 10-JAN-24 4ZGK 1 REMARK
REVDAT 2 28-DEC-16 4ZGK 1 JRNL
REVDAT 1 19-OCT-16 4ZGK 0
JRNL AUTH E.SURMIAK,A.TWARDA-CLAPA,K.M.ZAK,B.MUSIELAK,M.D.TOMALA,
JRNL AUTH 2 K.KUBICA,P.GRUDNIK,M.MADEJ,M.JABLONSKI,J.POTEMPA,
JRNL AUTH 3 J.KALINOWSKA-TLUSCIK,A.DOMLING,G.DUBIN,T.A.HOLAK
JRNL TITL A UNIQUE MDM2-BINDING MODE OF THE 3-PYRROLIN-2-ONE- AND
JRNL TITL 2 2-FURANONE-BASED ANTAGONISTS OF THE P53-MDM2 INTERACTION.
JRNL REF ACS CHEM. BIOL. V. 11 3310 2016
JRNL REFN ESSN 1554-8937
JRNL PMID 27709883
JRNL DOI 10.1021/ACSCHEMBIO.6B00596
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.3
REMARK 3 NUMBER OF REFLECTIONS : 11285
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 600
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 840
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.2770
REMARK 3 BIN FREE R VALUE SET COUNT : 48
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1562
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 114
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.27000
REMARK 3 B22 (A**2) : 0.63000
REMARK 3 B33 (A**2) : -2.89000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.262
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.211
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.151
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.920
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1687 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1651 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2288 ; 1.874 ; 2.042
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3799 ; 1.247 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 195 ; 5.956 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 68 ;45.265 ;24.118
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 319 ;19.811 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;11.821 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 251 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1835 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 379 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 771 ; 1.241 ; 1.853
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 770 ; 1.222 ; 1.850
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 963 ; 1.892 ; 2.760
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 18 109 B 18 109 5464 0.150 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 17 A 110
REMARK 3 ORIGIN FOR THE GROUP (A): 9.5938 -3.9201 -22.0759
REMARK 3 T TENSOR
REMARK 3 T11: 0.0277 T22: 0.0134
REMARK 3 T33: 0.0303 T12: 0.0035
REMARK 3 T13: -0.0071 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.3069 L22: 0.5952
REMARK 3 L33: 4.2051 L12: 0.3950
REMARK 3 L13: 0.1780 L23: 0.3736
REMARK 3 S TENSOR
REMARK 3 S11: -0.0300 S12: 0.0028 S13: 0.0036
REMARK 3 S21: -0.0222 S22: 0.0170 S23: -0.0340
REMARK 3 S31: 0.1976 S32: 0.1766 S33: 0.0130
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 18 B 114
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0244 -1.2072 -44.7590
REMARK 3 T TENSOR
REMARK 3 T11: 0.0071 T22: 0.0336
REMARK 3 T33: 0.0824 T12: -0.0114
REMARK 3 T13: 0.0015 T23: -0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 1.2204 L22: 0.8863
REMARK 3 L33: 3.1978 L12: -0.0615
REMARK 3 L13: -0.7898 L23: 0.0731
REMARK 3 S TENSOR
REMARK 3 S11: 0.0130 S12: 0.0469 S13: -0.0409
REMARK 3 S21: -0.0359 S22: -0.0272 S23: -0.0294
REMARK 3 S31: 0.0644 S32: -0.2253 S33: 0.0143
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4ZGK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000209204.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.873
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 : MOSFLM 7.0.9
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11908
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.739
REMARK 200 RESOLUTION RANGE LOW (A) : 48.893
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.8
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.32200
REMARK 200 R SYM FOR SHELL (I) : 0.32200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.5
REMARK 200 STARTING MODEL: 3TJ2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5 CONTAINING 30% PEG
REMARK 280 1000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K
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 18.30500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.65500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.27500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.65500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.30500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.27500
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 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 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 ASN A 111
REMARK 465 GLN A 112
REMARK 465 GLN A 113
REMARK 465 GLU A 114
REMARK 465 MET B 17
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 B 94 CE NZ
REMARK 470 GLN B 113 CG CD OE1 NE2
REMARK 470 GLU B 114 CB CG CD OE1 OE2
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 LEU B 37 CA - CB - CG ANGL. DEV. = 16.5 DEGREES
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 4NX A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4NX B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZFI RELATED DB: PDB
REMARK 900 4ZFI CONTAINS THE SAME PROTEIN IN COMPLEX WITH DIFFERENT SMALL
REMARK 900 MOLECULE GROUP BASED ON THE SAME SCAFFOLD.
DBREF 4ZGK A 18 114 UNP Q00987 MDM2_HUMAN 18 114
DBREF 4ZGK B 18 114 UNP Q00987 MDM2_HUMAN 18 114
SEQADV 4ZGK MET A 17 UNP Q00987 INITIATING METHIONINE
SEQADV 4ZGK MET B 17 UNP Q00987 INITIATING METHIONINE
SEQRES 1 A 98 MET GLN ILE PRO ALA SER GLU GLN GLU THR LEU VAL ARG
SEQRES 2 A 98 PRO LYS PRO LEU LEU LEU LYS LEU LEU LYS SER VAL GLY
SEQRES 3 A 98 ALA GLN LYS ASP THR TYR THR MET LYS GLU VAL LEU PHE
SEQRES 4 A 98 TYR LEU GLY GLN TYR ILE MET THR LYS ARG LEU TYR ASP
SEQRES 5 A 98 GLU LYS GLN GLN HIS ILE VAL TYR CYS SER ASN ASP LEU
SEQRES 6 A 98 LEU GLY ASP LEU PHE GLY VAL PRO SER PHE SER VAL LYS
SEQRES 7 A 98 GLU HIS ARG LYS ILE TYR THR MET ILE TYR ARG ASN LEU
SEQRES 8 A 98 VAL VAL VAL ASN GLN GLN GLU
SEQRES 1 B 98 MET GLN ILE PRO ALA SER GLU GLN GLU THR LEU VAL ARG
SEQRES 2 B 98 PRO LYS PRO LEU LEU LEU LYS LEU LEU LYS SER VAL GLY
SEQRES 3 B 98 ALA GLN LYS ASP THR TYR THR MET LYS GLU VAL LEU PHE
SEQRES 4 B 98 TYR LEU GLY GLN TYR ILE MET THR LYS ARG LEU TYR ASP
SEQRES 5 B 98 GLU LYS GLN GLN HIS ILE VAL TYR CYS SER ASN ASP LEU
SEQRES 6 B 98 LEU GLY ASP LEU PHE GLY VAL PRO SER PHE SER VAL LYS
SEQRES 7 B 98 GLU HIS ARG LYS ILE TYR THR MET ILE TYR ARG ASN LEU
SEQRES 8 B 98 VAL VAL VAL ASN GLN GLN GLU
HET 4NX A 201 33
HET 4NX B 201 33
HETNAM 4NX (5R)-3,5-BIS(4-CHLOROBENZYL)-4-(6-CHLORO-1H-INDOL-3-
HETNAM 2 4NX YL)-5-HYDROXYFURAN-2(5H)-ONE
FORMUL 3 4NX 2(C26 H18 CL3 N O3)
FORMUL 5 HOH *114(H2 O)
HELIX 1 AA1 PRO A 20 GLU A 25 1 6
HELIX 2 AA2 LYS A 31 VAL A 41 1 11
HELIX 3 AA3 MET A 50 LYS A 64 1 15
HELIX 4 AA4 ASP A 80 GLY A 87 1 8
HELIX 5 AA5 GLU A 95 ARG A 105 1 11
HELIX 6 AA6 PRO B 20 GLU B 25 1 6
HELIX 7 AA7 LYS B 31 VAL B 41 1 11
HELIX 8 AA8 MET B 50 LYS B 64 1 15
HELIX 9 AA9 ASP B 80 GLY B 87 1 8
HELIX 10 AB1 GLU B 95 ARG B 105 1 11
SHEET 1 AA1 3 TYR A 48 THR A 49 0
SHEET 2 AA1 3 LEU A 27 PRO A 30 -1 N VAL A 28 O TYR A 48
SHEET 3 AA1 3 LEU A 107 VAL A 109 -1 O VAL A 108 N ARG A 29
SHEET 1 AA2 2 ILE A 74 TYR A 76 0
SHEET 2 AA2 2 SER A 90 SER A 92 -1 O PHE A 91 N VAL A 75
SHEET 1 AA3 3 TYR B 48 THR B 49 0
SHEET 2 AA3 3 LEU B 27 PRO B 30 -1 N VAL B 28 O TYR B 48
SHEET 3 AA3 3 LEU B 107 VAL B 109 -1 O VAL B 108 N ARG B 29
SHEET 1 AA4 2 ILE B 74 TYR B 76 0
SHEET 2 AA4 2 SER B 90 SER B 92 -1 O PHE B 91 N VAL B 75
SITE 1 AC1 12 LEU A 54 PHE A 55 GLY A 58 TYR A 67
SITE 2 AC1 12 VAL A 93 HIS A 96 ILE A 99 TYR A 100
SITE 3 AC1 12 HOH A 304 HOH A 309 HOH A 327 LYS B 51
SITE 1 AC2 12 LYS A 51 LEU B 54 PHE B 55 GLY B 58
SITE 2 AC2 12 ILE B 61 TYR B 67 VAL B 93 HIS B 96
SITE 3 AC2 12 ILE B 99 TYR B 100 HOH B 318 HOH B 323
CRYST1 36.610 56.550 97.310 90.00 90.00 90.00 P 21 21 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 0.027315 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017683 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010276 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
