Header list of 1c15.pdb file
Complete list - b 16 2 Bytes
HEADER APOPTOSIS 20-JUL-99 1C15
TITLE SOLUTION STRUCTURE OF APAF-1 CARD
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: APAF-1 CARD;
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-2T
KEYWDS PROGRAMMED CELL DEATH, APAF, CARD, DED, DD, CASPASE RECRUITMENT
KEYWDS 2 DOMAIN, HOMOPHILIC INTERACTION, APOPTOSIS
EXPDTA SOLUTION NMR
NUMMDL 16
MDLTYP MINIMIZED AVERAGE
AUTHOR P.ZHOU,J.CHOU,R.S.OLEA,J.YUAN,G.WAGNER
REVDAT 5 16-FEB-22 1C15 1 REMARK
REVDAT 4 24-FEB-09 1C15 1 VERSN
REVDAT 3 05-APR-00 1C15 1 JRNL
REVDAT 2 04-OCT-99 1C15 1 COMPND
REVDAT 1 20-SEP-99 1C15 0
JRNL AUTH P.ZHOU,J.CHOU,R.S.OLEA,J.YUAN,G.WAGNER
JRNL TITL SOLUTION STRUCTURE OF APAF-1 CARD AND ITS INTERACTION WITH
JRNL TITL 2 CASPASE-9 CARD: A STRUCTURAL BASIS FOR SPECIFIC
JRNL TITL 3 ADAPTOR/CASPASE INTERACTION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 96 11265 1999
JRNL REFN ISSN 0027-8424
JRNL PMID 10500165
JRNL DOI 10.1073/PNAS.96.20.11265
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, X-PLOR 3.851
REMARK 3 AUTHORS : GUNTERT ET AL (DYANA), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1C15 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000009364.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM 15N LABELED APAF-1 CARD, 20
REMARK 210 MM PHOSPHATE BUFFER, 50 MM NACL;
REMARK 210 1MM 13C LABELED APAF-1 CARD, 20
REMARK 210 MM PHOSPHATE BUFFER, 50 MM NACL;
REMARK 210 1MM NON-LABELED APAF-1 CARD, 20
REMARK 210 MM PHOSPHATE BUFFER, 50 MM NACL;
REMARK 210 1MM 13C,15N LABELED, 80%
REMARK 210 DEUTERATED APAF-1 CARD, 20 MM
REMARK 210 PHOSPHATE BUFFER, 50 MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY; HMQC-
REMARK 210 J
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; DMX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 16
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: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 16 MET A 1 N MET A 1 CA -0.377
REMARK 500 16 MET A 1 CA MET A 1 CB -0.416
REMARK 500 16 MET A 1 CB MET A 1 CG -0.463
REMARK 500 16 MET A 1 CG MET A 1 SD -0.647
REMARK 500 16 MET A 1 SD MET A 1 CE -1.120
REMARK 500 16 MET A 1 C MET A 1 O -0.193
REMARK 500 16 MET A 1 C ASP A 2 N -0.205
REMARK 500 16 ASP A 2 CA ASP A 2 CB -0.145
REMARK 500 16 ASP A 2 CG ASP A 2 OD1 -0.526
REMARK 500 16 ASP A 2 CG ASP A 2 OD2 -0.642
REMARK 500 16 LYS A 4 CD LYS A 4 CE -0.795
REMARK 500 16 LYS A 4 CE LYS A 4 NZ -0.927
REMARK 500 16 ARG A 6 CD ARG A 6 NE -0.691
REMARK 500 16 ARG A 6 NE ARG A 6 CZ -0.412
REMARK 500 16 ARG A 6 CZ ARG A 6 NH1 -0.944
REMARK 500 16 ARG A 6 CZ ARG A 6 NH2 -0.664
REMARK 500 16 ASN A 7 CG ASN A 7 OD1 -0.583
REMARK 500 16 ASN A 7 CG ASN A 7 ND2 -0.588
REMARK 500 16 GLN A 11 CD GLN A 11 OE1 -0.485
REMARK 500 16 GLN A 11 CD GLN A 11 NE2 -0.627
REMARK 500 16 HIS A 12 CG HIS A 12 CD2 -0.403
REMARK 500 16 HIS A 12 CG HIS A 12 ND1 -0.220
REMARK 500 16 HIS A 12 ND1 HIS A 12 CE1 -0.101
REMARK 500 16 HIS A 12 CE1 HIS A 12 NE2 -0.515
REMARK 500 16 ARG A 13 CD ARG A 13 NE -0.265
REMARK 500 16 ARG A 13 NE ARG A 13 CZ -0.484
REMARK 500 16 ARG A 13 CZ ARG A 13 NH1 -0.926
REMARK 500 16 ARG A 13 CZ ARG A 13 NH2 -0.285
REMARK 500 16 GLU A 14 CD GLU A 14 OE1 -0.694
REMARK 500 16 GLU A 14 CD GLU A 14 OE2 -0.646
REMARK 500 16 LEU A 16 CG LEU A 16 CD1 -0.730
REMARK 500 16 LEU A 16 CG LEU A 16 CD2 -0.794
REMARK 500 16 GLU A 17 CD GLU A 17 OE1 -0.702
REMARK 500 16 GLU A 17 CD GLU A 17 OE2 -0.639
REMARK 500 16 LYS A 18 CD LYS A 18 CE -0.448
REMARK 500 16 LYS A 18 CE LYS A 18 NZ -0.486
REMARK 500 16 ASP A 19 CG ASP A 19 OD1 -0.589
REMARK 500 16 ASP A 19 CG ASP A 19 OD2 -0.523
REMARK 500 16 ILE A 20 C ILE A 20 O -0.127
REMARK 500 16 LYS A 21 CG LYS A 21 CD -0.228
REMARK 500 16 LYS A 21 CD LYS A 21 CE -0.575
REMARK 500 16 LYS A 21 CE LYS A 21 NZ -0.589
REMARK 500 16 SER A 23 CB SER A 23 OG -0.638
REMARK 500 16 TYR A 24 CG TYR A 24 CD2 -0.682
REMARK 500 16 TYR A 24 CG TYR A 24 CD1 -0.686
REMARK 500 16 TYR A 24 CE1 TYR A 24 CZ -0.675
REMARK 500 16 TYR A 24 CZ TYR A 24 CE2 -0.679
REMARK 500 16 MET A 26 CG MET A 26 SD -0.677
REMARK 500 16 MET A 26 SD MET A 26 CE -0.585
REMARK 500 16 ASP A 27 CG ASP A 27 OD1 -0.608
REMARK 500
REMARK 500 THIS ENTRY HAS 186 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
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 16 MET A 1 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 16 MET A 1 CG - SD - CE ANGL. DEV. = 31.7 DEGREES
REMARK 500 16 ASP A 2 OD1 - CG - OD2 ANGL. DEV. = -46.1 DEGREES
REMARK 500 16 ASP A 2 CB - CG - OD1 ANGL. DEV. = 27.1 DEGREES
REMARK 500 16 ASP A 2 CB - CG - OD2 ANGL. DEV. = 19.1 DEGREES
REMARK 500 16 LYS A 4 CG - CD - CE ANGL. DEV. = 37.6 DEGREES
REMARK 500 16 LYS A 4 CD - CE - NZ ANGL. DEV. = 59.4 DEGREES
REMARK 500 16 ARG A 6 CG - CD - NE ANGL. DEV. = 14.1 DEGREES
REMARK 500 16 ARG A 6 CD - NE - CZ ANGL. DEV. = 35.8 DEGREES
REMARK 500 16 ARG A 6 NH1 - CZ - NH2 ANGL. DEV. = -60.0 DEGREES
REMARK 500 16 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 21.4 DEGREES
REMARK 500 16 ARG A 6 NE - CZ - NH2 ANGL. DEV. = 38.6 DEGREES
REMARK 500 16 ASN A 7 OD1 - CG - ND2 ANGL. DEV. = -71.1 DEGREES
REMARK 500 16 ASN A 7 CB - CG - OD1 ANGL. DEV. = 32.4 DEGREES
REMARK 500 16 ASN A 7 CB - CG - ND2 ANGL. DEV. = 38.5 DEGREES
REMARK 500 16 GLN A 11 OE1 - CD - NE2 ANGL. DEV. = -53.0 DEGREES
REMARK 500 16 GLN A 11 CG - CD - OE1 ANGL. DEV. = 27.1 DEGREES
REMARK 500 16 GLN A 11 CG - CD - NE2 ANGL. DEV. = 25.7 DEGREES
REMARK 500 16 HIS A 12 CB - CG - CD2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 16 HIS A 12 ND1 - CG - CD2 ANGL. DEV. = -27.5 DEGREES
REMARK 500 16 HIS A 12 CB - CG - ND1 ANGL. DEV. = 18.7 DEGREES
REMARK 500 16 HIS A 12 CG - ND1 - CE1 ANGL. DEV. = 23.2 DEGREES
REMARK 500 16 HIS A 12 ND1 - CE1 - NE2 ANGL. DEV. = -12.7 DEGREES
REMARK 500 16 HIS A 12 CG - CD2 - NE2 ANGL. DEV. = 16.9 DEGREES
REMARK 500 16 ARG A 13 CD - NE - CZ ANGL. DEV. = 35.1 DEGREES
REMARK 500 16 ARG A 13 NH1 - CZ - NH2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 16 ARG A 13 NE - CZ - NH1 ANGL. DEV. = -47.4 DEGREES
REMARK 500 16 ARG A 13 NE - CZ - NH2 ANGL. DEV. = 38.0 DEGREES
REMARK 500 16 GLU A 14 OE1 - CD - OE2 ANGL. DEV. = -92.9 DEGREES
REMARK 500 16 GLU A 14 CG - CD - OE1 ANGL. DEV. = 45.9 DEGREES
REMARK 500 16 GLU A 14 CG - CD - OE2 ANGL. DEV. = 47.1 DEGREES
REMARK 500 16 LEU A 16 CD1 - CG - CD2 ANGL. DEV. = -38.9 DEGREES
REMARK 500 16 LEU A 16 CB - CG - CD1 ANGL. DEV. = 28.6 DEGREES
REMARK 500 16 LEU A 16 CB - CG - CD2 ANGL. DEV. = 24.0 DEGREES
REMARK 500 16 GLU A 17 OE1 - CD - OE2 ANGL. DEV. = -89.7 DEGREES
REMARK 500 16 GLU A 17 CG - CD - OE1 ANGL. DEV. = 44.0 DEGREES
REMARK 500 16 GLU A 17 CG - CD - OE2 ANGL. DEV. = 45.9 DEGREES
REMARK 500 16 ASP A 19 OD1 - CG - OD2 ANGL. DEV. = -51.4 DEGREES
REMARK 500 16 ASP A 19 CB - CG - OD1 ANGL. DEV. = 23.8 DEGREES
REMARK 500 16 ASP A 19 CB - CG - OD2 ANGL. DEV. = 27.7 DEGREES
REMARK 500 16 LYS A 21 CG - CD - CE ANGL. DEV. = 20.6 DEGREES
REMARK 500 16 SER A 23 CA - CB - OG ANGL. DEV. = 16.6 DEGREES
REMARK 500 16 TYR A 24 CB - CG - CD2 ANGL. DEV. = 52.0 DEGREES
REMARK 500 16 TYR A 24 CD1 - CG - CD2 ANGL. DEV. = 104.8 DEGREES
REMARK 500 16 TYR A 24 CB - CG - CD1 ANGL. DEV. = 52.9 DEGREES
REMARK 500 16 TYR A 24 CG - CD1 - CE1 ANGL. DEV. = 52.1 DEGREES
REMARK 500 16 TYR A 24 CG - CD2 - CE2 ANGL. DEV. = 52.2 DEGREES
REMARK 500 16 TYR A 24 CD1 - CE1 - CZ ANGL. DEV. = 53.7 DEGREES
REMARK 500 16 TYR A 24 OH - CZ - CE2 ANGL. DEV. = 53.4 DEGREES
REMARK 500 16 TYR A 24 CE1 - CZ - OH ANGL. DEV. = 53.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 213 ANGLE DEVIATIONS.
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 THR A 22 97.40 -24.44
REMARK 500 1 THR A 48 -38.23 -135.84
REMARK 500 1 GLN A 49 -157.46 -104.25
REMARK 500 1 GLU A 78 -75.16 -108.01
REMARK 500 1 PRO A 92 -88.44 -72.09
REMARK 500 1 SER A 95 -52.89 -164.91
REMARK 500 1 SER A 96 -60.57 -93.69
REMARK 500 2 THR A 22 98.75 -24.23
REMARK 500 2 TYR A 24 -38.94 -32.87
REMARK 500 2 ASN A 45 14.36 -145.26
REMARK 500 2 THR A 48 -45.41 -145.86
REMARK 500 2 GLU A 78 -75.24 -112.03
REMARK 500 2 PRO A 92 -89.46 -71.29
REMARK 500 3 HIS A 12 45.00 -142.41
REMARK 500 3 THR A 22 97.34 -23.75
REMARK 500 3 ASN A 45 21.70 -145.42
REMARK 500 3 THR A 48 -42.96 -137.40
REMARK 500 3 GLU A 78 -75.15 -112.53
REMARK 500 3 PRO A 92 -89.76 -70.44
REMARK 500 3 SER A 95 -73.50 -56.75
REMARK 500 3 SER A 96 -71.05 -100.48
REMARK 500 4 THR A 22 98.33 -24.68
REMARK 500 4 TYR A 24 -39.35 -33.55
REMARK 500 4 ASN A 45 23.82 -144.99
REMARK 500 4 THR A 48 -41.97 -136.69
REMARK 500 4 GLN A 49 -152.88 -100.20
REMARK 500 4 GLU A 78 -75.46 -109.49
REMARK 500 4 PRO A 92 -83.85 -71.84
REMARK 500 4 VAL A 94 -62.90 -91.82
REMARK 500 4 SER A 95 -55.74 -164.83
REMARK 500 5 THR A 22 97.53 -24.10
REMARK 500 5 PHE A 34 -72.33 -56.23
REMARK 500 5 ASN A 45 15.40 -142.69
REMARK 500 5 GLN A 49 -153.48 -104.31
REMARK 500 5 GLU A 78 -75.10 -103.26
REMARK 500 5 VAL A 94 -78.41 -71.67
REMARK 500 6 HIS A 12 43.54 -146.39
REMARK 500 6 THR A 22 96.50 -24.63
REMARK 500 6 TYR A 24 -37.26 -33.08
REMARK 500 6 PHE A 34 -71.56 -53.15
REMARK 500 6 ASN A 45 15.20 -144.49
REMARK 500 6 THR A 48 -42.93 -136.44
REMARK 500 6 GLN A 49 -159.23 -96.20
REMARK 500 6 GLU A 78 -75.34 -109.66
REMARK 500 6 PRO A 92 -85.17 -71.72
REMARK 500 7 THR A 22 96.20 -24.97
REMARK 500 7 ASN A 45 21.82 -145.26
REMARK 500 7 THR A 48 -40.07 -136.51
REMARK 500 7 GLU A 78 -75.05 -112.64
REMARK 500 8 THR A 22 98.37 -24.05
REMARK 500
REMARK 500 THIS ENTRY HAS 117 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CRD RELATED DB: PDB
REMARK 900 RAIDD CARD
REMARK 900 RELATED ID: 1A1W RELATED DB: PDB
REMARK 900 FADD DEATH EFFECTOR DOMAIN
REMARK 900 RELATED ID: 1DDF RELATED DB: PDB
REMARK 900 FAS DEATH DOMAIN
DBREF 1C15 A 1 97 UNP O14727 APAF_HUMAN 1 97
SEQRES 1 A 97 MET ASP ALA LYS ALA ARG ASN CYS LEU LEU GLN HIS ARG
SEQRES 2 A 97 GLU ALA LEU GLU LYS ASP ILE LYS THR SER TYR ILE MET
SEQRES 3 A 97 ASP HIS MET ILE SER ASP GLY PHE LEU THR ILE SER GLU
SEQRES 4 A 97 GLU GLU LYS VAL ARG ASN GLU PRO THR GLN GLN GLN ARG
SEQRES 5 A 97 ALA ALA MET LEU ILE LYS MET ILE LEU LYS LYS ASP ASN
SEQRES 6 A 97 ASP SER TYR VAL SER PHE TYR ASN ALA LEU LEU HIS GLU
SEQRES 7 A 97 GLY TYR LYS ASP LEU ALA ALA LEU LEU HIS ASP GLY ILE
SEQRES 8 A 97 PRO VAL VAL SER SER SER
HELIX 1 1 ASP A 2 HIS A 12 1 11
HELIX 2 2 HIS A 12 ILE A 20 1 9
HELIX 3 3 SER A 23 SER A 31 1 9
HELIX 4 4 ILE A 37 GLU A 46 1 10
HELIX 5 5 GLN A 50 ASP A 64 1 15
HELIX 6 6 ASN A 65 HIS A 77 1 13
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
Complete list - b 16 2 Bytes