HEADER APOPTOSIS 26-AUG-99 1CWW
TITLE SOLUTION STRUCTURE OF THE CASPASE RECRUITMENT DOMAIN (CARD) FROM APAF-
TITLE 2 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOTIC PROTEASE ACTIVATING FACTOR 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CASPASE RECRUITMENT DOMAIN;
COMPND 5 SYNONYM: CARD OF APAF-1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX 6P-3
KEYWDS HELICAL BUNDLE, APOPTOSIS
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.L.DAY,C.DUPONT,M.LACKMANN,D.L.VAUX,M.G.HINDS
REVDAT 4 21-DEC-22 1CWW 1 SEQADV
REVDAT 3 16-FEB-22 1CWW 1 REMARK
REVDAT 2 24-FEB-09 1CWW 1 VERSN
REVDAT 1 21-JAN-00 1CWW 0
JRNL AUTH C.L.DAY,C.DUPONT,M.LACKMANN,D.L.VAUX,M.G.HINDS
JRNL TITL SOLUTION STRUCTURE AND MUTAGENESIS OF THE CASPASE
JRNL TITL 2 RECRUITMENT DOMAIN (CARD) FROM APAF-1.
JRNL REF CELL DEATH DIFFER. V. 6 1125 1999
JRNL REFN ISSN 1350-9047
JRNL PMID 10578182
JRNL DOI 10.1038/SJ.CDD.4400584
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER (AG) (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 2314 NOE-DERIVED DISTANCE CONSTRAINTS, 31 HYDROGEN BOND
REMARK 3 CONSTRAINTS AND 173 DIHEDRAL ANGLE CONSTRAINTS.
REMARK 4
REMARK 4 1CWW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1000009593.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 30; 30; 30
REMARK 210 PH : 6.7; 6.7; 6.7
REMARK 210 IONIC STRENGTH : NULL; NULL; NULL
REMARK 210 PRESSURE : NULL; NULL; NULL
REMARK 210 SAMPLE CONTENTS : UNLABELLED 1.5MM APAF-1 CARD
REMARK 210 20MM SODIUM PHOSPHATE PH 6.7
REMARK 210 75MM NACL 2MM DITHIOTHREITOL; U-
REMARK 210 15N 1.5MM APAF-1 CARD 20MM
REMARK 210 SODIUM PHOSPHATE PH 6.7 75MM
REMARK 210 NACL 2MM DITHIOTHREITOL; U-15N;
REMARK 210 U-13C 1.5MM APAF-1 CARD 20MM
REMARK 210 SODIUM PHOSPHATE PH 6.7 75MM
REMARK 210 NACL 2MM DITHIOTHREITOL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, DYANA 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY TORSION ANGLE
REMARK 210 DYNAMICS SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 250
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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: 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
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 HIS A 12 43.84 -82.05
REMARK 500 1 LEU A 16 -80.10 -49.28
REMARK 500 1 SER A 23 -92.58 -64.83
REMARK 500 1 GLN A 50 -80.81 -47.83
REMARK 500 1 LYS A 62 50.46 -140.29
REMARK 500 1 LYS A 63 -128.50 -107.58
REMARK 500 1 TYR A 80 50.87 -101.88
REMARK 500 1 SER A 95 -70.68 77.35
REMARK 500 2 SER A -1 -114.81 -125.10
REMARK 500 2 HIS A 12 36.80 -80.11
REMARK 500 2 LEU A 16 -82.29 -44.80
REMARK 500 2 THR A 22 -102.09 -66.29
REMARK 500 2 SER A 23 -101.94 29.09
REMARK 500 2 GLN A 50 -87.03 -41.47
REMARK 500 2 LYS A 63 -120.94 -94.00
REMARK 500 2 GLU A 78 -139.45 -116.80
REMARK 500 2 VAL A 94 49.89 -102.42
REMARK 500 2 SER A 95 -62.79 74.56
REMARK 500 3 HIS A 12 40.51 -85.38
REMARK 500 3 LEU A 16 -84.46 -44.76
REMARK 500 3 THR A 22 -101.77 -82.40
REMARK 500 3 SER A 23 -111.86 49.21
REMARK 500 3 GLN A 49 -30.49 -38.21
REMARK 500 3 GLN A 50 -92.13 -41.02
REMARK 500 3 LYS A 63 -163.20 -127.18
REMARK 500 3 GLU A 78 -140.20 -92.64
REMARK 500 3 PRO A 92 -83.64 -61.26
REMARK 500 3 SER A 95 81.88 -69.16
REMARK 500 3 SER A 96 76.36 43.24
REMARK 500 4 HIS A 12 39.23 -83.19
REMARK 500 4 LEU A 16 -84.73 -46.63
REMARK 500 4 THR A 22 -89.45 -113.88
REMARK 500 4 SER A 23 -77.88 -8.91
REMARK 500 4 GLN A 50 -83.89 -43.46
REMARK 500 4 LYS A 63 -157.23 -132.17
REMARK 500 4 TYR A 80 53.25 -104.89
REMARK 500 5 PRO A -4 45.66 -82.91
REMARK 500 5 HIS A 12 36.29 -81.81
REMARK 500 5 LEU A 16 -88.95 -50.85
REMARK 500 5 THR A 22 -103.29 -120.50
REMARK 500 5 SER A 23 -101.36 30.45
REMARK 500 5 GLN A 50 -73.37 -42.79
REMARK 500 5 LYS A 63 -145.84 -123.78
REMARK 500 5 GLU A 78 -144.63 -108.05
REMARK 500 6 SER A -1 -155.56 -166.07
REMARK 500 6 HIS A 12 41.03 -86.79
REMARK 500 6 LEU A 16 -85.70 -49.44
REMARK 500 6 THR A 22 -104.06 -120.43
REMARK 500 6 SER A 23 -107.57 44.48
REMARK 500 6 GLN A 50 -84.38 -37.77
REMARK 500
REMARK 500 THIS ENTRY HAS 177 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CWW A 1 97 UNP O14727 APAF_HUMAN 1 97
SEQADV 1CWW GLY A -5 UNP O14727 CLONING ARTIFACT
SEQADV 1CWW PRO A -4 UNP O14727 CLONING ARTIFACT
SEQADV 1CWW LEU A -3 UNP O14727 CLONING ARTIFACT
SEQADV 1CWW GLY A -2 UNP O14727 CLONING ARTIFACT
SEQADV 1CWW SER A -1 UNP O14727 CLONING ARTIFACT
SEQRES 1 A 102 GLY PRO LEU GLY SER MET ASP ALA LYS ALA ARG ASN CYS
SEQRES 2 A 102 LEU LEU GLN HIS ARG GLU ALA LEU GLU LYS ASP ILE LYS
SEQRES 3 A 102 THR SER TYR ILE MET ASP HIS MET ILE SER ASP GLY PHE
SEQRES 4 A 102 LEU THR ILE SER GLU GLU GLU LYS VAL ARG ASN GLU PRO
SEQRES 5 A 102 THR GLN GLN GLN ARG ALA ALA MET LEU ILE LYS MET ILE
SEQRES 6 A 102 LEU LYS LYS ASP ASN ASP SER TYR VAL SER PHE TYR ASN
SEQRES 7 A 102 ALA LEU LEU HIS GLU GLY TYR LYS ASP LEU ALA ALA LEU
SEQRES 8 A 102 LEU HIS ASP GLY ILE PRO VAL VAL SER SER SER
HELIX 1 1 ASP A 2 GLN A 11 1 10
HELIX 2 2 ALA A 15 ILE A 20 1 6
HELIX 3 3 THR A 22 ASP A 32 1 11
HELIX 4 4 THR A 36 GLU A 46 1 11
HELIX 5 5 THR A 48 LEU A 61 1 14
HELIX 6 6 ASP A 64 GLU A 78 1 15
HELIX 7 7 TYR A 80 ASP A 89 1 10
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
