HEADER SIGNALING PROTEIN 20-MAR-15 2N14
TITLE MDMX-295
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN MDM4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 23-111;
COMPND 5 SYNONYM: DOUBLE MINUTE 4 PROTEIN, MDM2-LIKE P53-BINDING PROTEIN,
COMPND 6 PROTEIN MDMX, P53-BINDING PROTEIN MDM4;
COMPND 7 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: MDM4, MDMX;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: BL21(DE3)
KEYWDS MDMX, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.R.GRACE,R.W.KRIWACKI
REVDAT 2 04-MAY-16 2N14 1 JRNL
REVDAT 1 27-JAN-16 2N14 0
JRNL AUTH C.R.GRACE,D.BAN,J.MIN,A.MAYASUNDARI,L.MIN,K.E.FINCH,
JRNL AUTH 2 L.GRIFFITHS,N.BHARATHAM,D.BASHFORD,R.KIPLIN GUY,M.A.DYER,
JRNL AUTH 3 R.W.KRIWACKI
JRNL TITL MONITORING LIGAND-INDUCED PROTEIN ORDERING IN DRUG
JRNL TITL 2 DISCOVERY.
JRNL REF J.MOL.BIOL. V. 428 1290 2016
JRNL REFN ISSN 0022-2836
JRNL PMID 26812210
JRNL DOI 10.1016/J.JMB.2016.01.016
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2N14 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-15.
REMARK 100 THE RCSB ID CODE IS RCSB104289.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 200
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM [U-100% 13C; U-100% 15N]
REMARK 210 PROTEIN_1, 0.6 MM PROTEIN_2, 90%
REMARK 210 H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 2D 1H-13C HSQC AROMATIC; 3D HNCA;
REMARK 210 3D HNCACB; 3D CBCA(CO)NH; 3D
REMARK 210 HNCO; 3D HCCH-TOCSY; 3D 1H-15N
REMARK 210 NOESY; 3D 1H-15N TOCSY; 3D 1H-13C
REMARK 210 NOESY ALIPHATIC; 3D 1H-13C NOESY
REMARK 210 AROMATIC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TOPSPIN, CARA, CYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 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 2 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 3 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 5 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 6 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 6 ARG A 103 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 7 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 8 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 9 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 10 ARG A 103 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 12 ARG A 103 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 16 VAL A 52 CA - CB - CG2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 16 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 17 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 18 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 18 ARG A 103 NE - CZ - NH1 ANGL. DEV. = 3.0 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 1 ASN A 25 48.04 -86.27
REMARK 500 1 ALA A 42 -157.75 -85.43
REMARK 500 1 MET A 46 48.65 -74.26
REMARK 500 1 GLU A 70 86.59 -157.40
REMARK 500 1 ASN A 105 -62.97 -93.14
REMARK 500 3 ASN A 25 36.52 -82.40
REMARK 500 3 GLU A 45 19.29 -142.25
REMARK 500 3 MET A 46 38.82 -71.54
REMARK 500 4 ASN A 25 54.42 -91.83
REMARK 500 4 CYS A 76 29.69 -145.24
REMARK 500 5 ASN A 25 32.62 -80.05
REMARK 500 5 MET A 46 47.59 -78.08
REMARK 500 5 CYS A 76 29.57 -145.95
REMARK 500 5 ASN A 105 -88.87 -96.70
REMARK 500 6 GLN A 26 -160.14 -163.23
REMARK 500 6 MET A 46 49.83 -75.97
REMARK 500 6 CYS A 76 30.69 -88.53
REMARK 500 6 ASN A 105 -65.57 -91.94
REMARK 500 7 ASN A 25 35.43 -82.15
REMARK 500 7 ALA A 42 -161.20 -79.36
REMARK 500 7 GLU A 45 19.62 -141.39
REMARK 500 7 MET A 46 47.55 -77.64
REMARK 500 7 ASN A 105 -71.17 -97.27
REMARK 500 8 ASN A 25 36.70 -83.31
REMARK 500 8 GLU A 45 11.26 -141.62
REMARK 500 9 CYS A 76 24.71 -157.03
REMARK 500 10 ASN A 25 27.84 -77.36
REMARK 500 10 ALA A 42 -161.12 -79.89
REMARK 500 10 CYS A 76 24.87 -148.98
REMARK 500 10 THR A 108 -168.05 46.82
REMARK 500 11 ASN A 25 57.20 -92.43
REMARK 500 11 GLU A 45 20.26 -140.27
REMARK 500 11 MET A 46 42.48 -77.63
REMARK 500 11 CYS A 76 23.62 -150.44
REMARK 500 11 VAL A 107 41.42 -75.21
REMARK 500 12 ASN A 25 35.32 -81.18
REMARK 500 12 GLU A 45 14.80 -143.59
REMARK 500 12 CYS A 76 29.24 -148.62
REMARK 500 12 ASN A 105 -71.31 -82.87
REMARK 500 13 ASN A 25 32.52 -82.47
REMARK 500 13 CYS A 76 28.62 -146.19
REMARK 500 13 VAL A 107 39.94 -78.85
REMARK 500 14 ASN A 25 33.75 -78.51
REMARK 500 14 CYS A 76 25.28 -146.74
REMARK 500 14 ASN A 105 -92.97 -87.65
REMARK 500 15 ASN A 25 45.99 -86.39
REMARK 500 15 ALA A 42 -156.23 -82.24
REMARK 500 15 CYS A 76 24.24 -148.02
REMARK 500 15 ASN A 105 -71.70 -101.96
REMARK 500 16 ASN A 25 35.14 -81.26
REMARK 500
REMARK 500 THIS ENTRY HAS 75 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 49H IS REFERRED AS SJ5/SJ295 IN THE PAPER
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 49H A 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 25546 RELATED DB: BMRB
REMARK 900 RELATED ID: 2N0U RELATED DB: PDB
REMARK 900 RELATED ID: 2N0W RELATED DB: PDB
REMARK 900 RELATED ID: 2N06 RELATED DB: PDB
DBREF 2N14 A 23 111 UNP O15151 MDM4_HUMAN 23 111
SEQRES 1 A 89 GLN ILE ASN GLN VAL ARG PRO LYS LEU PRO LEU LEU LYS
SEQRES 2 A 89 ILE LEU HIS ALA ALA GLY ALA GLN GLY GLU MET PHE THR
SEQRES 3 A 89 VAL LYS GLU VAL MET HIS TYR LEU GLY GLN TYR ILE MET
SEQRES 4 A 89 VAL LYS GLN LEU TYR ASP GLN GLN GLU GLN HIS MET VAL
SEQRES 5 A 89 TYR CYS GLY GLY ASP LEU LEU GLY GLU LEU LEU GLY ARG
SEQRES 6 A 89 GLN SER PHE SER VAL LYS ASP PRO SER PRO LEU TYR ASP
SEQRES 7 A 89 MET LEU ARG LYS ASN LEU VAL THR LEU ALA THR
HET 49H A 200 70
HETNAM 49H 4-({(4S,5R)-4-(3-CHLOROPHENYL)-5-(4-CHLOROPHENYL)-2-[4-
HETNAM 2 49H METHOXY-2-(PROPAN-2-YLOXY)PHENYL]-4,5-DIHYDRO-1H-
HETNAM 3 49H IMIDAZOL-1-YL}CARBONYL)PIPERAZIN-2-ONE
FORMUL 2 49H C30 H30 CL2 N4 O4
HELIX 1 1 LYS A 30 ALA A 39 1 10
HELIX 2 2 THR A 48 GLN A 64 1 17
HELIX 3 3 ASP A 79 GLY A 86 1 8
HELIX 4 4 PRO A 95 ARG A 103 1 9
SHEET 1 A 3 TYR A 66 ASP A 67 0
SHEET 2 A 3 GLU A 70 TYR A 75 -1 O MET A 73 N ASP A 67
SHEET 3 A 3 SER A 89 SER A 91 -1 O PHE A 90 N VAL A 74
SITE 1 AC1 8 MET A 53 LEU A 56 GLY A 57 ILE A 60
SITE 2 AC1 8 MET A 61 GLN A 71 HIS A 72 VAL A 92
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
