HEADER APOPTOSIS 25-MAR-10 2XA0
TITLE CRYSTAL STRUCTURE OF BCL-2 IN COMPLEX WITH A BAX BH3
TITLE 2 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS REGULATOR BCL-2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-207;
COMPND 5 SYNONYM: BCL-2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: APOPTOSIS REGULATOR BAX;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: BH3 DOMAIN, RESIDUES 52-82;
COMPND 11 SYNONYM: BAX
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: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIG;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPROEX HTA;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090
KEYWDS APOPTOSIS, CELL DEATH
EXPDTA X-RAY DIFFRACTION
AUTHOR B.KU,B.H.OH
REVDAT 2 01-JUN-11 2XA0 1 JRNL
REVDAT 1 24-NOV-10 2XA0 0
JRNL AUTH B.KU,C.LIANG,J.U.JUNG,B.H.OH
JRNL TITL EVIDENCE THAT INHIBITION OF BAX ACTIVATION BY BCL- 2
JRNL TITL 2 INVOLVES ITS TIGHT AND PREFERENTIAL INTERACTION WITH THE
JRNL TITL 3 BH3 DOMAIN OF BAX.
JRNL REF CELL RES. V. 21 627 2011
JRNL REFN ISSN 1001-0602
JRNL PMID 21060336
JRNL DOI 10.1038/CR.2010.149
REMARK 2
REMARK 2 RESOLUTION. 2.70 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 14476
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.2223
REMARK 3 FREE R VALUE : 0.2422
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.6
REMARK 3 FREE R VALUE TEST SET COUNT : 708
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
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 : 2712
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 21
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) : -0.222
REMARK 3 B22 (A**2) : -0.222
REMARK 3 B33 (A**2) : 0.443
REMARK 3 B12 (A**2) : 0.000
REMARK 3 B13 (A**2) : 0.000
REMARK 3 B23 (A**2) : 0.000
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) : 0.0092
REMARK 3 BOND ANGLES (DEGREES) : 1.363
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.4
REMARK 3 BSOL : 44.8143
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 35-50 OF BCL-2 ARE REPLACED
REMARK 3 WITH RESIDUES 33-48 OF BCL-XL TO SOLUBILIZE THE PROTEIN AS
REMARK 3 REPORTED EARLIER ( PETROS ET AL, PROC NATL ACAD SCI U S A 98,
REMARK 3 3012-3017(2001)) . HOWEVER, THE FINAL MODEL DOES NOT INCLUDE
REMARK 3 THE ENTIRE BCL- XL SUBSTITUTION REGION, WHOSE ELECTRON
REMARK 3 DENSITIES WERE NOT OBSERVED.
REMARK 4
REMARK 4 2XA0 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-SEP-10.
REMARK 100 THE PDBE ID CODE IS EBI-43418.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14540
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.70
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 9.7
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.40
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.1
REMARK 200 R MERGE FOR SHELL (I) : 0.22
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.50
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1G5M
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE (PH 4.2),
REMARK 280 3.0 M SODIUM FORMATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.28333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 92.56667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 92.56667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 46.28333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.1 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.3 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 HIS A 3
REMARK 465 ALA A 4
REMARK 465 GLY A 5
REMARK 465 ARG A 6
REMARK 465 THR A 7
REMARK 465 GLY A 8
REMARK 465 TYR A 9
REMARK 465 ALA A 32
REMARK 465 GLY A 33
REMARK 465 ASP A 34
REMARK 465 VAL A 35
REMARK 465 GLY A 36
REMARK 465 ALA A 37
REMARK 465 ALA A 38
REMARK 465 PRO A 39
REMARK 465 PRO A 40
REMARK 465 GLY A 41
REMARK 465 ALA A 42
REMARK 465 ALA A 43
REMARK 465 PRO A 44
REMARK 465 ALA A 45
REMARK 465 PRO A 46
REMARK 465 GLY A 47
REMARK 465 ILE A 48
REMARK 465 PHE A 49
REMARK 465 SER A 50
REMARK 465 SER A 51
REMARK 465 GLN A 52
REMARK 465 PRO A 53
REMARK 465 GLY A 54
REMARK 465 HIS A 55
REMARK 465 THR A 56
REMARK 465 PRO A 57
REMARK 465 HIS A 58
REMARK 465 PRO A 59
REMARK 465 ALA A 60
REMARK 465 ALA A 61
REMARK 465 SER A 62
REMARK 465 ARG A 63
REMARK 465 ASP A 64
REMARK 465 PRO A 65
REMARK 465 VAL A 66
REMARK 465 ALA A 67
REMARK 465 ARG A 68
REMARK 465 THR A 69
REMARK 465 SER A 70
REMARK 465 PRO A 71
REMARK 465 LEU A 72
REMARK 465 GLN A 73
REMARK 465 THR A 74
REMARK 465 PRO A 75
REMARK 465 ALA A 76
REMARK 465 ALA A 77
REMARK 465 PRO A 78
REMARK 465 GLY A 79
REMARK 465 ALA A 80
REMARK 465 ALA A 81
REMARK 465 ALA A 82
REMARK 465 GLY A 83
REMARK 465 PRO A 84
REMARK 465 ALA A 85
REMARK 465 LEU A 86
REMARK 465 SER A 87
REMARK 465 PRO A 88
REMARK 465 VAL A 89
REMARK 465 PRO A 90
REMARK 465 PRO A 91
REMARK 465 ARG A 207
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 HIS B 3
REMARK 465 ALA B 4
REMARK 465 GLY B 5
REMARK 465 ARG B 6
REMARK 465 THR B 7
REMARK 465 GLY B 8
REMARK 465 TYR B 9
REMARK 465 ALA B 32
REMARK 465 GLY B 33
REMARK 465 ASP B 34
REMARK 465 VAL B 35
REMARK 465 GLY B 36
REMARK 465 ALA B 37
REMARK 465 ALA B 38
REMARK 465 PRO B 39
REMARK 465 PRO B 40
REMARK 465 GLY B 41
REMARK 465 ALA B 42
REMARK 465 ALA B 43
REMARK 465 PRO B 44
REMARK 465 ALA B 45
REMARK 465 PRO B 46
REMARK 465 GLY B 47
REMARK 465 ILE B 48
REMARK 465 PHE B 49
REMARK 465 SER B 50
REMARK 465 SER B 51
REMARK 465 GLN B 52
REMARK 465 PRO B 53
REMARK 465 GLY B 54
REMARK 465 HIS B 55
REMARK 465 THR B 56
REMARK 465 PRO B 57
REMARK 465 HIS B 58
REMARK 465 PRO B 59
REMARK 465 ALA B 60
REMARK 465 ALA B 61
REMARK 465 SER B 62
REMARK 465 ARG B 63
REMARK 465 ASP B 64
REMARK 465 PRO B 65
REMARK 465 VAL B 66
REMARK 465 ALA B 67
REMARK 465 ARG B 68
REMARK 465 THR B 69
REMARK 465 SER B 70
REMARK 465 PRO B 71
REMARK 465 LEU B 72
REMARK 465 GLN B 73
REMARK 465 THR B 74
REMARK 465 PRO B 75
REMARK 465 ALA B 76
REMARK 465 ALA B 77
REMARK 465 PRO B 78
REMARK 465 GLY B 79
REMARK 465 ALA B 80
REMARK 465 ALA B 81
REMARK 465 ALA B 82
REMARK 465 GLY B 83
REMARK 465 PRO B 84
REMARK 465 ALA B 85
REMARK 465 LEU B 86
REMARK 465 SER B 87
REMARK 465 PRO B 88
REMARK 465 VAL B 89
REMARK 465 PRO B 90
REMARK 465 PRO B 91
REMARK 465 ARG B 207
REMARK 465 GLN C 52
REMARK 465 ASP C 53
REMARK 465 ALA C 54
REMARK 465 SER C 55
REMARK 465 THR C 56
REMARK 465 GLN D 52
REMARK 465 ASP D 53
REMARK 465 ALA D 54
REMARK 465 SER D 55
REMARK 465 THR D 56
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 OH TYR A 28 OD1 ASN A 163 1.98
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 THR B 122 N - CA - C ANGL. DEV. = -17.0 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 GLN A 25 -3.17 -56.73
REMARK 500 GLU A 114 133.60 -35.48
REMARK 500 MET A 166 33.12 -148.96
REMARK 500 PRO A 204 7.88 -63.14
REMARK 500 ARG B 109 23.96 -76.48
REMARK 500 MET B 166 43.17 -156.33
REMARK 500 THR B 187 -74.92 -51.31
REMARK 500 PRO B 204 7.36 -63.60
REMARK 500 ALA C 81 10.00 -58.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YSW RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE ANTI-APOPTOTIC
REMARK 900 PROTEIN BCL-2COMPLEXED WITH AN ACYL-
REMARK 900 SULFONAMIDE-BASED LIGAND
REMARK 900 RELATED ID: 2W3L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHIMAERIC BCL2-XL AND
REMARK 900 PHENYL TETRAHYDROISOQUINOLINE AMIDE COMPLEX
REMARK 900 RELATED ID: 1G5M RELATED DB: PDB
REMARK 900 HUMAN BCL-2, ISOFORM 1
REMARK 900 RELATED ID: 1GJH RELATED DB: PDB
REMARK 900 HUMAN BCL-2, ISOFORM 2
DBREF 2XA0 A 1 207 UNP P10415 BCL2_HUMAN 1 207
DBREF 2XA0 B 1 207 UNP P10415 BCL2_HUMAN 1 207
DBREF 2XA0 C 52 82 UNP Q07813 BAX_MOUSE 52 82
DBREF 2XA0 D 52 82 UNP Q07813 BAX_MOUSE 52 82
SEQRES 1 A 207 MET ALA HIS ALA GLY ARG THR GLY TYR ASP ASN ARG GLU
SEQRES 2 A 207 ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER GLN ARG
SEQRES 3 A 207 GLY TYR GLU TRP ASP ALA GLY ASP VAL GLY ALA ALA PRO
SEQRES 4 A 207 PRO GLY ALA ALA PRO ALA PRO GLY ILE PHE SER SER GLN
SEQRES 5 A 207 PRO GLY HIS THR PRO HIS PRO ALA ALA SER ARG ASP PRO
SEQRES 6 A 207 VAL ALA ARG THR SER PRO LEU GLN THR PRO ALA ALA PRO
SEQRES 7 A 207 GLY ALA ALA ALA GLY PRO ALA LEU SER PRO VAL PRO PRO
SEQRES 8 A 207 VAL VAL HIS LEU THR LEU ARG GLN ALA GLY ASP ASP PHE
SEQRES 9 A 207 SER ARG ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER
SEQRES 10 A 207 GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE
SEQRES 11 A 207 ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN
SEQRES 12 A 207 TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL
SEQRES 13 A 207 MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU
SEQRES 14 A 207 VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN
SEQRES 15 A 207 ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP
SEQRES 16 A 207 ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG
SEQRES 1 B 207 MET ALA HIS ALA GLY ARG THR GLY TYR ASP ASN ARG GLU
SEQRES 2 B 207 ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER GLN ARG
SEQRES 3 B 207 GLY TYR GLU TRP ASP ALA GLY ASP VAL GLY ALA ALA PRO
SEQRES 4 B 207 PRO GLY ALA ALA PRO ALA PRO GLY ILE PHE SER SER GLN
SEQRES 5 B 207 PRO GLY HIS THR PRO HIS PRO ALA ALA SER ARG ASP PRO
SEQRES 6 B 207 VAL ALA ARG THR SER PRO LEU GLN THR PRO ALA ALA PRO
SEQRES 7 B 207 GLY ALA ALA ALA GLY PRO ALA LEU SER PRO VAL PRO PRO
SEQRES 8 B 207 VAL VAL HIS LEU THR LEU ARG GLN ALA GLY ASP ASP PHE
SEQRES 9 B 207 SER ARG ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER
SEQRES 10 B 207 GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE
SEQRES 11 B 207 ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN
SEQRES 12 B 207 TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL
SEQRES 13 B 207 MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU
SEQRES 14 B 207 VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN
SEQRES 15 B 207 ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP
SEQRES 16 B 207 ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG
SEQRES 1 C 31 GLN ASP ALA SER THR LYS LYS LEU SER GLU CYS LEU ARG
SEQRES 2 C 31 ARG ILE GLY ASP GLU LEU ASP SER ASN MET GLU LEU GLN
SEQRES 3 C 31 ARG MET ILE ALA ASP
SEQRES 1 D 31 GLN ASP ALA SER THR LYS LYS LEU SER GLU CYS LEU ARG
SEQRES 2 D 31 ARG ILE GLY ASP GLU LEU ASP SER ASN MET GLU LEU GLN
SEQRES 3 D 31 ARG MET ILE ALA ASP
FORMUL 5 HOH *21(H2 O)
HELIX 1 1 ASN A 11 ARG A 26 1 16
HELIX 2 2 VAL A 93 PHE A 112 1 20
HELIX 3 3 MET A 115 GLN A 118 5 4
HELIX 4 4 THR A 125 ARG A 139 1 15
HELIX 5 5 TRP A 144 ARG A 164 1 21
HELIX 6 6 PRO A 168 LEU A 185 1 18
HELIX 7 7 LEU A 185 ASN A 192 1 8
HELIX 8 8 TRP A 195 GLY A 203 1 9
HELIX 9 9 ASN B 11 ARG B 26 1 16
HELIX 10 10 VAL B 93 PHE B 112 1 20
HELIX 11 11 MET B 115 GLN B 118 5 4
HELIX 12 12 THR B 125 ARG B 139 1 15
HELIX 13 13 TRP B 144 ARG B 164 1 21
HELIX 14 14 PRO B 168 LEU B 185 1 18
HELIX 15 15 LEU B 185 ASN B 192 1 8
HELIX 16 16 TRP B 195 GLY B 203 1 9
HELIX 17 17 LEU C 59 ALA C 81 1 23
HELIX 18 18 LEU D 59 ALA D 81 1 23
CRYST1 81.973 81.973 138.850 90.00 90.00 120.00 P 31 2 1 12
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 0.012199 0.007043 0.000000 0.00000
SCALE2 0.000000 0.014086 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007202 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
