HEADER DNA BINDING PROTEIN 29-MAY-00 1F2R
TITLE NMR STRUCTURE OF THE HETERODIMERIC COMPLEX BETWEEN CAD DOMAINS OF CAD
TITLE 2 AND ICAD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASPASE-ACTIVATED DNASE;
COMPND 3 CHAIN: C;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN (CAD DOMAIN), RESIDUES 1-87;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: INHIBITOR OF CASPASE-ACTIVATED DNASE;
COMPND 8 CHAIN: I;
COMPND 9 FRAGMENT: N-TERMINAL DOMAIN (CAD DOMAIN), RESIDUES 1-100;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET32;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET32
KEYWDS ALPHA-BETA ROLL, PROTEIN-PROTEIN COMPLEX, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR T.OTOMO,H.SAKAHIRA,K.UEGAKI,S.NAGATA,T.YAMAZAKI
REVDAT 4 16-FEB-22 1F2R 1 REMARK
REVDAT 3 24-FEB-09 1F2R 1 VERSN
REVDAT 2 30-AUG-00 1F2R 1 JRNL
REVDAT 1 08-JUN-00 1F2R 0
JRNL AUTH T.OTOMO,H.SAKAHIRA,K.UEGAKI,S.NAGATA,T.YAMAZAKI
JRNL TITL STRUCTURE OF THE HETERODIMERIC COMPLEX BETWEEN CAD DOMAINS
JRNL TITL 2 OF CAD AND ICAD.
JRNL REF NAT.STRUCT.BIOL. V. 7 658 2000
JRNL REFN ISSN 1072-8368
JRNL PMID 10932250
JRNL DOI 10.1038/77957
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.UEGAKI,T.OTOMO,H.SAKAHIRA,M.SHIMIZU,N.YUMOTO,Y.KYOGOKU,
REMARK 1 AUTH 2 S.NAGATA,T.YAMAZAKI
REMARK 1 TITL STRUCTURE OF THE CAD DOMAIN OF CASPASE-ACTIVATED DNASE AND
REMARK 1 TITL 2 INTERACTION WITH THE CAD DOMAIN OF ITS INHIBITOR.
REMARK 1 REF J.MOL.BIOL. V. 297 1121 2000
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.2000.3643
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.ENARI,H.SAKAHIRA,H.YOKOYAMA,K.OKAWA,A.IWAMATSU,S.NAGATA
REMARK 1 TITL A CASPASE-ACTIVATED DNASE THAT DEGRADES DNA DURING
REMARK 1 TITL 2 APOPTOSIS, AND ITS INHIBITOR ICAD.
REMARK 1 REF NATURE V. 391 43 1998
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/34112
REMARK 1 REFERENCE 3
REMARK 1 AUTH H.SAKAHIRA,M.ENARI,S.NAGATA
REMARK 1 TITL CLEAVAGE OF CAD INHIBITOR IN CAD ACTIVATION AND DNA
REMARK 1 TITL 2 DEGRADATION DURING APOPTOSIS.
REMARK 1 REF NATURE V. 391 96 1998
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/34214
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.841, X-PLOR 3.841
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2646 RESTRAINTS, 2503 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 93 DIHEDRAL ANGLE RESTRAINTS,50 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1F2R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1000011172.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6MM CAD U-15N,13C/0.6MM ICAD
REMARK 210 UNLABELED; 20MM PHOPHATE BUFFER
REMARK 210 PH6.4; 0.6MM CAD U-15N,13C/0.6MM
REMARK 210 ICAD UNLABELED; 20MM PHOPHATE
REMARK 210 BUFFER PH6.4; 0.6MM ICAD U-15N,
REMARK 210 13C/0.6MM CAD UNLABELED; 20MM
REMARK 210 PHOPHATE BUFFER PH6.4; 0.6MM
REMARK 210 ICAD U-15N,13C/0.6MM CAD
REMARK 210 UNLABELED; 20MM PHOPHATE BUFFER
REMARK 210 PH6.4
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, I
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ARG I 16 H LEU I 18 1.56
REMARK 500 O PRO I 80 H ASN I 82 1.56
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 CYS C 2 66.76 -114.37
REMARK 500 SER C 47 131.24 170.38
REMARK 500 THR C 59 -148.71 -146.99
REMARK 500 PRO C 67 -159.72 -61.21
REMARK 500 ASN C 68 -136.96 -61.12
REMARK 500 ASP C 69 82.53 -28.68
REMARK 500 GLU C 71 86.32 -59.11
REMARK 500 ALA C 77 73.82 -68.26
REMARK 500 TYR C 84 89.86 -50.31
REMARK 500 SER I 4 102.98 -51.03
REMARK 500 ALA I 7 -31.11 171.79
REMARK 500 ALA I 9 151.24 59.47
REMARK 500 PRO I 10 -157.63 -61.67
REMARK 500 ARG I 16 63.12 63.10
REMARK 500 PRO I 17 58.25 -63.63
REMARK 500 LEU I 18 119.35 57.74
REMARK 500 PRO I 20 83.86 -62.81
REMARK 500 ASN I 26 165.19 -45.90
REMARK 500 ARG I 29 70.63 -64.14
REMARK 500 SER I 37 -71.51 -85.30
REMARK 500 ASP I 53 156.82 -46.10
REMARK 500 VAL I 70 69.91 -106.78
REMARK 500 ASP I 73 30.51 -141.27
REMARK 500 LEU I 79 153.83 -40.89
REMARK 500 PRO I 80 173.36 -59.34
REMARK 500 SER I 81 59.11 -66.81
REMARK 500 ASN I 82 116.78 173.12
REMARK 500 ALA I 89 63.23 -66.65
REMARK 500 ASN I 91 -57.82 -158.46
REMARK 500 THR I 95 31.75 -89.60
REMARK 500 TYR I 96 -60.37 -127.01
REMARK 500 SER I 99 51.73 -94.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG C 6 0.19 SIDE CHAIN
REMARK 500 ARG C 14 0.19 SIDE CHAIN
REMARK 500 ARG C 27 0.21 SIDE CHAIN
REMARK 500 ARG C 34 0.21 SIDE CHAIN
REMARK 500 ARG C 39 0.30 SIDE CHAIN
REMARK 500 ARG C 48 0.29 SIDE CHAIN
REMARK 500 ARG I 5 0.27 SIDE CHAIN
REMARK 500 ARG I 16 0.30 SIDE CHAIN
REMARK 500 ARG I 24 0.29 SIDE CHAIN
REMARK 500 ARG I 25 0.31 SIDE CHAIN
REMARK 500 ARG I 29 0.29 SIDE CHAIN
REMARK 500 ARG I 43 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1C9F RELATED DB: PDB
REMARK 900 1C9F IS THE NMR STRUCTURE OF THE CAD DOMAIN OF CAD IN THE FREE
REMARK 900 STATE.
DBREF 1F2R C 1 87 UNP O54788 DFFB_MOUSE 1 87
DBREF 1F2R I 1 100 UNP O54786 DFFA_MOUSE 1 100
SEQRES 1 C 87 MET CYS ALA VAL LEU ARG GLN PRO LYS CYS VAL LYS LEU
SEQRES 2 C 87 ARG ALA LEU HIS SER ALA CYS LYS PHE GLY VAL ALA ALA
SEQRES 3 C 87 ARG SER CYS GLN GLU LEU LEU ARG LYS GLY CYS VAL ARG
SEQRES 4 C 87 PHE GLN LEU PRO MET PRO GLY SER ARG LEU CYS LEU TYR
SEQRES 5 C 87 GLU ASP GLY THR GLU VAL THR ASP ASP CYS PHE PRO GLY
SEQRES 6 C 87 LEU PRO ASN ASP ALA GLU LEU LEU LEU LEU THR ALA GLY
SEQRES 7 C 87 GLU THR TRP HIS GLY TYR VAL SER ASP
SEQRES 1 I 100 MET GLU LEU SER ARG GLY ALA SER ALA PRO ASP PRO ASP
SEQRES 2 I 100 ASP VAL ARG PRO LEU LYS PRO CYS LEU LEU ARG ARG ASN
SEQRES 3 I 100 HIS SER ARG ASP GLN HIS GLY VAL ALA ALA SER SER LEU
SEQRES 4 I 100 GLU GLU LEU ARG SER LYS ALA CYS GLU LEU LEU ALA ILE
SEQRES 5 I 100 ASP LYS SER LEU THR PRO ILE THR LEU VAL LEU ALA GLU
SEQRES 6 I 100 ASP GLY THR ILE VAL ASP ASP ASP ASP TYR PHE LEU CYS
SEQRES 7 I 100 LEU PRO SER ASN THR LYS PHE VAL ALA LEU ALA CYS ASN
SEQRES 8 I 100 GLU LYS TRP THR TYR ASN ASP SER ASP
HELIX 1 1 SER C 28 GLN C 41 1 14
HELIX 2 2 SER I 38 ALA I 51 1 14
HELIX 3 3 ASP I 53 THR I 57 5 5
SHEET 1 A 5 LYS C 21 ALA C 26 0
SHEET 2 A 5 LYS C 9 ARG C 14 -1 N LYS C 9 O ALA C 26
SHEET 3 A 5 ALA C 70 LEU C 75 1 O ALA C 70 N LYS C 12
SHEET 4 A 5 ARG C 48 LEU C 51 -1 N ARG C 48 O LEU C 75
SHEET 5 A 5 GLU C 57 VAL C 58 -1 N VAL C 58 O LEU C 49
SHEET 1 B 4 SER I 28 ALA I 36 0
SHEET 2 B 4 LYS I 19 ARG I 25 -1 N LYS I 19 O ALA I 36
SHEET 3 B 4 LYS I 84 LEU I 88 1 N PHE I 85 O LEU I 22
SHEET 4 B 4 THR I 60 LEU I 63 -1 O THR I 60 N LEU I 88
CISPEP 1 THR I 57 PRO I 58 0 -0.69
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
(ATOM LINES ARE NOT SHOWN.)
END
