HEADER APOPTOSIS 07-JUL-04 1TY4
TITLE CRYSTAL STRUCTURE OF A CED-9/EGL-1 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS REGULATOR CED-9;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: BH1,BH2;
COMPND 5 SYNONYM: CELL DEATH PROTEIN 9;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: EGG LAYING DEFECTIVE EGL-1, PROGRAMMED CELL DEATH
COMPND 9 ACTIVATOR;
COMPND 10 CHAIN: C, D;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;
SOURCE 3 ORGANISM_TAXID: 6239;
SOURCE 4 GENE: CED-9,T07C4.8;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-2T,PBB75;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;
SOURCE 11 ORGANISM_TAXID: 6239;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PGEX-2T,PBB75
KEYWDS APOPTOSIS, CED-9, EGL-1, BCL-2 FAMILY PROTEINS, RECOGNITION
EXPDTA X-RAY DIFFRACTION
AUTHOR N.YAN,L.GU,D.KOKEL,D.XUE,Y.SHI
REVDAT 4 13-JUL-11 1TY4 1 VERSN
REVDAT 3 24-FEB-09 1TY4 1 VERSN
REVDAT 2 12-OCT-04 1TY4 1 JRNL
REVDAT 1 28-SEP-04 1TY4 0
JRNL AUTH N.YAN,L.GU,D.KOKEL,J.CHAI,W.LI,A.HAN,L.CHEN,D.XUE,Y.SHI
JRNL TITL STRUCTURAL, BIOCHEMICAL, AND FUNCTIONAL ANALYSES OF CED-9
JRNL TITL 2 RECOGNITION BY THE PROAPOPTOTIC PROTEINS EGL-1 AND CED-4
JRNL REF MOL.CELL V. 15 999 2004
JRNL REFN ISSN 1097-2765
JRNL PMID 15383288
JRNL DOI 10.1016/J.MOLCEL.2004.08.022
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 24864
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2458
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.28
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3069
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 67
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.14600
REMARK 3 B22 (A**2) : -3.14600
REMARK 3 B33 (A**2) : 6.29200
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.68
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.299 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.002 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.420 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.527 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 45.39
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TY4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-04.
REMARK 100 THE RCSB ID CODE IS RCSB023023.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25359
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 10.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49500
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CACODYLATE, ISOPROPANOL,
REMARK 280 MAGNESIUM ACATATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 28.72350
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 43.08525
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 14.36175
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 2390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 2340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 GLY A 68
REMARK 465 LYS A 69
REMARK 465 ILE A 70
REMARK 465 ASN A 71
REMARK 465 ASP A 72
REMARK 465 TRP A 73
REMARK 465 GLY B 68
REMARK 465 LYS B 69
REMARK 465 ILE B 70
REMARK 465 ARG B 237
REMARK 465 ASP C 31
REMARK 465 SER C 32
REMARK 465 SER C 33
REMARK 465 GLN C 34
REMARK 465 PHE C 35
REMARK 465 ALA C 36
REMARK 465 ASP C 37
REMARK 465 ASP C 38
REMARK 465 SER C 39
REMARK 465 GLY C 40
REMARK 465 PHE C 41
REMARK 465 PHE C 42
REMARK 465 ASP C 43
REMARK 465 ASP C 44
REMARK 465 SER C 45
REMARK 465 GLU C 46
REMARK 465 ILE C 47
REMARK 465 SER C 77
REMARK 465 ASP C 78
REMARK 465 ARG C 79
REMARK 465 SER C 80
REMARK 465 LEU C 81
REMARK 465 PHE C 82
REMARK 465 HIS C 83
REMARK 465 ARG C 84
REMARK 465 LEU C 85
REMARK 465 LEU C 86
REMARK 465 ASP C 87
REMARK 465 ASP D 31
REMARK 465 SER D 32
REMARK 465 SER D 33
REMARK 465 GLN D 34
REMARK 465 PHE D 35
REMARK 465 ALA D 36
REMARK 465 ASP D 37
REMARK 465 ASP D 38
REMARK 465 SER D 39
REMARK 465 GLY D 40
REMARK 465 PHE D 41
REMARK 465 PHE D 42
REMARK 465 ASP D 43
REMARK 465 ASP D 44
REMARK 465 SER D 45
REMARK 465 GLU D 46
REMARK 465 ILE D 47
REMARK 465 HIS D 75
REMARK 465 ALA D 76
REMARK 465 SER D 77
REMARK 465 ASP D 78
REMARK 465 ARG D 79
REMARK 465 SER D 80
REMARK 465 LEU D 81
REMARK 465 PHE D 82
REMARK 465 HIS D 83
REMARK 465 ARG D 84
REMARK 465 LEU D 85
REMARK 465 LEU D 86
REMARK 465 ASP D 87
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 GLU A 74 CG CD OE1 OE2
REMARK 470 ASP A 162 CG OD1 OD2
REMARK 470 ASN A 212 CB CG OD1
REMARK 470 LYS A 215 CG CD CE NZ
REMARK 470 GLU A 216 CG CD OE1 OE2
REMARK 470 LYS A 229 CG CD CE NZ
REMARK 470 PHE B 100 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 CYS B 107 CB SG
REMARK 470 GLU B 129 CG CD OE1 OE2
REMARK 470 GLN B 160 CB CG CD OE1 NE2
REMARK 470 LYS B 215 CB CG CD CE NZ
REMARK 470 HIS C 75 CG ND1 CD2 CE1 NE2
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 CYS A 107 CB CYS A 107 SG -0.393
REMARK 500 CYS A 164 CB CYS A 164 SG -0.397
REMARK 500 CYS B 164 CB CYS B 164 SG -0.393
REMARK 500 CYS C 62 CB CYS C 62 SG -0.392
REMARK 500 CYS D 62 CB CYS D 62 SG -0.397
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 ASN A 212 N - CA - C ANGL. DEV. = -19.7 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 ALA A 159 172.66 -52.36
REMARK 500 GLN A 163 -153.21 -134.07
REMARK 500 ASN A 212 14.66 117.59
REMARK 500 ASN A 213 -11.30 -155.91
REMARK 500 LYS A 215 1.63 -68.93
REMARK 500 PRO B 106 35.08 -65.68
REMARK 500 CYS B 107 -16.84 -164.60
REMARK 500 GLN B 163 -154.46 -121.08
REMARK 500 ASN B 213 -38.34 -148.42
REMARK 500 ASN B 218 60.47 34.18
REMARK 500 SER C 49 -26.49 70.24
REMARK 500 HIS C 75 -115.62 -133.73
REMARK 500 SER D 49 -17.32 64.88
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TY4 A 68 237 UNP P41958 CED9_CAEEL 68 237
DBREF 1TY4 B 68 237 UNP P41958 CED9_CAEEL 68 237
DBREF 1TY4 C 31 87 UNP O61667 EGL1_CAEEL 46 102
DBREF 1TY4 D 31 87 UNP O61667 EGL1_CAEEL 46 102
SEQADV 1TY4 MSE C 61 UNP O61667 MET 76 MODIFIED RESIDUE
SEQADV 1TY4 MSE C 69 UNP O61667 MET 84 MODIFIED RESIDUE
SEQADV 1TY4 MSE C 70 UNP O61667 MET 85 MODIFIED RESIDUE
SEQADV 1TY4 MSE D 61 UNP O61667 MET 76 MODIFIED RESIDUE
SEQADV 1TY4 MSE D 69 UNP O61667 MET 84 MODIFIED RESIDUE
SEQADV 1TY4 MSE D 70 UNP O61667 MET 85 MODIFIED RESIDUE
SEQADV 1TY4 MSE A 97 UNP P41958 MET 97 MODIFIED RESIDUE
SEQADV 1TY4 MSE A 115 UNP P41958 MET 115 MODIFIED RESIDUE
SEQADV 1TY4 MSE A 116 UNP P41958 MET 116 MODIFIED RESIDUE
SEQADV 1TY4 MSE A 119 UNP P41958 MET 119 MODIFIED RESIDUE
SEQADV 1TY4 PRO A 148 UNP P41958 LEU 148 CONFLICT
SEQADV 1TY4 MSE A 166 UNP P41958 MET 166 MODIFIED RESIDUE
SEQADV 1TY4 MSE A 185 UNP P41958 MET 185 MODIFIED RESIDUE
SEQADV 1TY4 MSE A 186 UNP P41958 MET 186 MODIFIED RESIDUE
SEQADV 1TY4 MSE A 225 UNP P41958 MET 225 MODIFIED RESIDUE
SEQADV 1TY4 MSE A 231 UNP P41958 MET 231 MODIFIED RESIDUE
SEQADV 1TY4 MSE B 97 UNP P41958 MET 97 MODIFIED RESIDUE
SEQADV 1TY4 MSE B 115 UNP P41958 MET 115 MODIFIED RESIDUE
SEQADV 1TY4 MSE B 116 UNP P41958 MET 116 MODIFIED RESIDUE
SEQADV 1TY4 MSE B 119 UNP P41958 MET 119 MODIFIED RESIDUE
SEQADV 1TY4 PRO B 148 UNP P41958 LEU 148 CONFLICT
SEQADV 1TY4 MSE B 166 UNP P41958 MET 166 MODIFIED RESIDUE
SEQADV 1TY4 MSE B 185 UNP P41958 MET 185 MODIFIED RESIDUE
SEQADV 1TY4 MSE B 186 UNP P41958 MET 186 MODIFIED RESIDUE
SEQADV 1TY4 MSE B 225 UNP P41958 MET 225 MODIFIED RESIDUE
SEQADV 1TY4 MSE B 231 UNP P41958 MET 231 MODIFIED RESIDUE
SEQRES 1 A 170 GLY LYS ILE ASN ASP TRP GLU GLU PRO ARG LEU ASP ILE
SEQRES 2 A 170 GLU GLY PHE VAL VAL ASP TYR PHE THR HIS ARG ILE ARG
SEQRES 3 A 170 GLN ASN GLY MSE GLU TRP PHE GLY ALA PRO GLY LEU PRO
SEQRES 4 A 170 CYS GLY VAL GLN PRO GLU HIS GLU MSE MSE ARG VAL MSE
SEQRES 5 A 170 GLY THR ILE PHE GLU LYS LYS HIS ALA GLU ASN PHE GLU
SEQRES 6 A 170 THR PHE CYS GLU GLN LEU LEU ALA VAL PRO ARG ILE SER
SEQRES 7 A 170 PHE SER PRO TYR GLN ASP VAL VAL ARG THR VAL GLY ASN
SEQRES 8 A 170 ALA GLN THR ASP GLN CYS PRO MSE SER TYR GLY ARG LEU
SEQRES 9 A 170 ILE GLY LEU ILE SER PHE GLY GLY PHE VAL ALA ALA LYS
SEQRES 10 A 170 MSE MSE GLU SER VAL GLU LEU GLN GLY GLN VAL ARG ASN
SEQRES 11 A 170 LEU PHE VAL TYR THR SER LEU PHE ILE LYS THR ARG ILE
SEQRES 12 A 170 ARG ASN ASN TRP LYS GLU HIS ASN ARG SER TRP ASP ASP
SEQRES 13 A 170 PHE MSE THR LEU GLY LYS GLN MSE LYS GLU ASP TYR GLU
SEQRES 14 A 170 ARG
SEQRES 1 B 170 GLY LYS ILE ASN ASP TRP GLU GLU PRO ARG LEU ASP ILE
SEQRES 2 B 170 GLU GLY PHE VAL VAL ASP TYR PHE THR HIS ARG ILE ARG
SEQRES 3 B 170 GLN ASN GLY MSE GLU TRP PHE GLY ALA PRO GLY LEU PRO
SEQRES 4 B 170 CYS GLY VAL GLN PRO GLU HIS GLU MSE MSE ARG VAL MSE
SEQRES 5 B 170 GLY THR ILE PHE GLU LYS LYS HIS ALA GLU ASN PHE GLU
SEQRES 6 B 170 THR PHE CYS GLU GLN LEU LEU ALA VAL PRO ARG ILE SER
SEQRES 7 B 170 PHE SER PRO TYR GLN ASP VAL VAL ARG THR VAL GLY ASN
SEQRES 8 B 170 ALA GLN THR ASP GLN CYS PRO MSE SER TYR GLY ARG LEU
SEQRES 9 B 170 ILE GLY LEU ILE SER PHE GLY GLY PHE VAL ALA ALA LYS
SEQRES 10 B 170 MSE MSE GLU SER VAL GLU LEU GLN GLY GLN VAL ARG ASN
SEQRES 11 B 170 LEU PHE VAL TYR THR SER LEU PHE ILE LYS THR ARG ILE
SEQRES 12 B 170 ARG ASN ASN TRP LYS GLU HIS ASN ARG SER TRP ASP ASP
SEQRES 13 B 170 PHE MSE THR LEU GLY LYS GLN MSE LYS GLU ASP TYR GLU
SEQRES 14 B 170 ARG
SEQRES 1 C 57 ASP SER SER GLN PHE ALA ASP ASP SER GLY PHE PHE ASP
SEQRES 2 C 57 ASP SER GLU ILE SER SER ILE GLY TYR GLU ILE GLY SER
SEQRES 3 C 57 LYS LEU ALA ALA MSE CYS ASP ASP PHE ASP ALA GLN MSE
SEQRES 4 C 57 MSE SER TYR SER ALA HIS ALA SER ASP ARG SER LEU PHE
SEQRES 5 C 57 HIS ARG LEU LEU ASP
SEQRES 1 D 57 ASP SER SER GLN PHE ALA ASP ASP SER GLY PHE PHE ASP
SEQRES 2 D 57 ASP SER GLU ILE SER SER ILE GLY TYR GLU ILE GLY SER
SEQRES 3 D 57 LYS LEU ALA ALA MSE CYS ASP ASP PHE ASP ALA GLN MSE
SEQRES 4 D 57 MSE SER TYR SER ALA HIS ALA SER ASP ARG SER LEU PHE
SEQRES 5 D 57 HIS ARG LEU LEU ASP
MODRES 1TY4 MSE A 97 MET SELENOMETHIONINE
MODRES 1TY4 MSE A 115 MET SELENOMETHIONINE
MODRES 1TY4 MSE A 116 MET SELENOMETHIONINE
MODRES 1TY4 MSE A 119 MET SELENOMETHIONINE
MODRES 1TY4 MSE A 166 MET SELENOMETHIONINE
MODRES 1TY4 MSE A 185 MET SELENOMETHIONINE
MODRES 1TY4 MSE A 186 MET SELENOMETHIONINE
MODRES 1TY4 MSE A 225 MET SELENOMETHIONINE
MODRES 1TY4 MSE A 231 MET SELENOMETHIONINE
MODRES 1TY4 MSE B 97 MET SELENOMETHIONINE
MODRES 1TY4 MSE B 115 MET SELENOMETHIONINE
MODRES 1TY4 MSE B 116 MET SELENOMETHIONINE
MODRES 1TY4 MSE B 119 MET SELENOMETHIONINE
MODRES 1TY4 MSE B 166 MET SELENOMETHIONINE
MODRES 1TY4 MSE B 185 MET SELENOMETHIONINE
MODRES 1TY4 MSE B 186 MET SELENOMETHIONINE
MODRES 1TY4 MSE B 225 MET SELENOMETHIONINE
MODRES 1TY4 MSE B 231 MET SELENOMETHIONINE
MODRES 1TY4 MSE C 61 MET SELENOMETHIONINE
MODRES 1TY4 MSE C 69 MET SELENOMETHIONINE
MODRES 1TY4 MSE C 70 MET SELENOMETHIONINE
MODRES 1TY4 MSE D 61 MET SELENOMETHIONINE
MODRES 1TY4 MSE D 69 MET SELENOMETHIONINE
MODRES 1TY4 MSE D 70 MET SELENOMETHIONINE
HET MSE A 97 8
HET MSE A 115 8
HET MSE A 116 8
HET MSE A 119 8
HET MSE A 166 8
HET MSE A 185 8
HET MSE A 186 8
HET MSE A 225 8
HET MSE A 231 8
HET MSE B 97 8
HET MSE B 115 8
HET MSE B 116 8
HET MSE B 119 8
HET MSE B 166 8
HET MSE B 185 8
HET MSE B 186 8
HET MSE B 225 8
HET MSE B 231 8
HET MSE C 61 8
HET MSE C 69 8
HET MSE C 70 8
HET MSE D 61 8
HET MSE D 69 8
HET MSE D 70 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 24(C5 H11 N O2 SE)
FORMUL 5 HOH *67(H2 O)
HELIX 1 1 GLU A 75 LEU A 78 5 4
HELIX 2 2 ASP A 79 ASN A 95 1 17
HELIX 3 3 GLN A 110 ALA A 140 1 31
HELIX 4 4 VAL A 141 SER A 145 5 5
HELIX 5 5 PHE A 146 ALA A 159 1 14
HELIX 6 6 SER A 167 GLU A 187 1 21
HELIX 7 7 LEU A 191 GLY A 193 5 3
HELIX 8 8 GLN A 194 ARG A 211 1 18
HELIX 9 9 SER A 220 GLU A 236 1 17
HELIX 10 10 ARG A 237 ARG A 237 5 1
HELIX 11 11 ASN B 71 LEU B 78 5 8
HELIX 12 12 ASP B 79 ASN B 95 1 17
HELIX 13 13 GLN B 110 HIS B 127 1 18
HELIX 14 14 HIS B 127 ALA B 140 1 14
HELIX 15 15 VAL B 141 SER B 145 5 5
HELIX 16 16 PHE B 146 ALA B 159 1 14
HELIX 17 17 SER B 167 MSE B 186 1 20
HELIX 18 18 SER B 188 GLY B 193 1 6
HELIX 19 19 GLN B 194 ASN B 212 1 19
HELIX 20 20 SER B 220 GLU B 236 1 17
HELIX 21 21 SER C 49 MSE C 70 1 22
HELIX 22 22 SER C 71 SER C 73 5 3
HELIX 23 23 SER D 49 SER D 71 1 23
LINK C GLY A 96 N MSE A 97 1555 1555 1.33
LINK C MSE A 97 N GLU A 98 1555 1555 1.33
LINK C GLU A 114 N MSE A 115 1555 1555 1.33
LINK C MSE A 115 N MSE A 116 1555 1555 1.33
LINK C MSE A 116 N ARG A 117 1555 1555 1.33
LINK C VAL A 118 N MSE A 119 1555 1555 1.33
LINK C MSE A 119 N GLY A 120 1555 1555 1.33
LINK C PRO A 165 N MSE A 166 1555 1555 1.33
LINK C MSE A 166 N SER A 167 1555 1555 1.33
LINK C LYS A 184 N MSE A 185 1555 1555 1.33
LINK C MSE A 185 N MSE A 186 1555 1555 1.33
LINK C MSE A 186 N GLU A 187 1555 1555 1.33
LINK C PHE A 224 N MSE A 225 1555 1555 1.33
LINK C MSE A 225 N THR A 226 1555 1555 1.33
LINK C GLN A 230 N MSE A 231 1555 1555 1.33
LINK C MSE A 231 N LYS A 232 1555 1555 1.33
LINK C GLY B 96 N MSE B 97 1555 1555 1.33
LINK C MSE B 97 N GLU B 98 1555 1555 1.33
LINK C GLU B 114 N MSE B 115 1555 1555 1.33
LINK C MSE B 115 N MSE B 116 1555 1555 1.34
LINK C MSE B 116 N ARG B 117 1555 1555 1.33
LINK C VAL B 118 N MSE B 119 1555 1555 1.33
LINK C MSE B 119 N GLY B 120 1555 1555 1.33
LINK C PRO B 165 N MSE B 166 1555 1555 1.33
LINK C MSE B 166 N SER B 167 1555 1555 1.33
LINK C LYS B 184 N MSE B 185 1555 1555 1.33
LINK C MSE B 185 N MSE B 186 1555 1555 1.33
LINK C MSE B 186 N GLU B 187 1555 1555 1.33
LINK C PHE B 224 N MSE B 225 1555 1555 1.33
LINK C MSE B 225 N THR B 226 1555 1555 1.33
LINK C GLN B 230 N MSE B 231 1555 1555 1.33
LINK C MSE B 231 N LYS B 232 1555 1555 1.33
LINK C ALA C 60 N MSE C 61 1555 1555 1.33
LINK C MSE C 61 N CYS C 62 1555 1555 1.33
LINK C GLN C 68 N MSE C 69 1555 1555 1.33
LINK C MSE C 69 N MSE C 70 1555 1555 1.33
LINK C MSE C 70 N SER C 71 1555 1555 1.33
LINK C ALA D 60 N MSE D 61 1555 1555 1.33
LINK C MSE D 61 N CYS D 62 1555 1555 1.33
LINK C GLN D 68 N MSE D 69 1555 1555 1.33
LINK C MSE D 69 N MSE D 70 1555 1555 1.33
LINK C MSE D 70 N SER D 71 1555 1555 1.33
CRYST1 93.713 93.713 57.447 90.00 90.00 90.00 P 43 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 0.010671 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010671 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017407 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
