HEADER APOPTOSIS 11-JAN-19 6QGG
TITLE STRUCTURE OF HUMAN BCL-2 IN COMPLEX WITH ANALOGUE OF ABT-737
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS REGULATOR BCL-2,BCL-2-LIKE PROTEIN 1,APOPTOSIS
COMPND 3 REGULATOR BCL-2,BCL-2-LIKE PROTEIN 1;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: BCL2-L-1,APOPTOSIS REGULATOR BCL-X,BCL2-L-1,APOPTOSIS
COMPND 6 REGULATOR BCL-X;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BCL2, BCL2L1, BCL2L, BCLX;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: PLYSS
KEYWDS APOPTOSIS, BCL2, ABT-737
EXPDTA X-RAY DIFFRACTION
AUTHOR P.DOKURNO,J.MURRAY,J.DAVIDSON,I.CHEN,B.DAVIS,C.J.GRAHAM,R.HARRIS,
AUTHOR 2 A.M.JORDAN,N.MATASSOVA,C.PEDDER,S.RAY,S.ROUGHLEY,J.SMITH,C.WALMSLEY,
AUTHOR 3 Y.WANG,N.WHITEHEAD,D.S.WILLIAMSON,P.CASARA,T.LE DIGUARHER,J.HICKMAN,
AUTHOR 4 J.STARK,A.KOTSCHY,O.GENESTE,R.E.HUBBARD
REVDAT 2 11-SEP-19 6QGG 1 JRNL
REVDAT 1 12-JUN-19 6QGG 0
JRNL AUTH J.B.MURRAY,J.DAVIDSON,I.CHEN,B.DAVIS,P.DOKURNO,C.J.GRAHAM,
JRNL AUTH 2 R.HARRIS,A.JORDAN,N.MATASSOVA,C.PEDDER,S.RAY,S.D.ROUGHLEY,
JRNL AUTH 3 J.SMITH,C.WALMSLEY,Y.WANG,N.WHITEHEAD,D.S.WILLIAMSON,
JRNL AUTH 4 P.CASARA,T.LE DIGUARHER,J.HICKMAN,J.STARK,A.KOTSCHY,
JRNL AUTH 5 O.GENESTE,R.E.HUBBARD
JRNL TITL ESTABLISHING DRUG DISCOVERY AND IDENTIFICATION OF HIT SERIES
JRNL TITL 2 FOR THE ANTI-APOPTOTIC PROTEINS, BCL-2 AND MCL-1.
JRNL REF ACS OMEGA V. 4 8892 2019
JRNL REFN ESSN 2470-1343
JRNL PMID 31459977
JRNL DOI 10.1021/ACSOMEGA.9B00611
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0230
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 25595
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.152
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1217
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.58
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3776
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.76
REMARK 3 BIN R VALUE (WORKING SET) : 0.1710
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.2100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1136
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.44000
REMARK 3 B22 (A**2) : -0.44000
REMARK 3 B33 (A**2) : 0.88000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.060
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.061
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.034
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.896
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1247 ; 0.019 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 1034 ; 0.001 ; 0.018
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1698 ; 1.908 ; 1.608
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2351 ; 1.189 ; 1.622
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 144 ; 5.207 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 75 ;29.522 ;21.467
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 187 ;12.554 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;21.754 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 145 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1434 ; 0.012 ; 0.019
REMARK 3 GENERAL PLANES OTHERS (A): 258 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6QGG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1292100118.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-AUG-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27361
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.19600
REMARK 200 R SYM FOR SHELL (I) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: 2YXJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M NA/K PHOSPHATE PH 5.6, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 284K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
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+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 29.29650
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 14.64825
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 43.94475
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 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 7
REMARK 465 ALA A 32
REMARK 465 GLY A 33
REMARK 465 ASP A 34
REMARK 465 VAL A 35
REMARK 465 GLU A 36
REMARK 465 GLU A 37
REMARK 465 ASN A 38
REMARK 465 ARG A 39
REMARK 465 THR A 40
REMARK 465 GLU A 41
REMARK 465 ALA A 42
REMARK 465 PRO A 43
REMARK 465 GLU A 44
REMARK 465 GLY A 45
REMARK 465 ASN A 204
REMARK 465 ASN A 205
REMARK 465 ALA A 206
REMARK 465 ALA A 207
REMARK 465 ALA A 208
REMARK 465 GLU A 209
REMARK 465 SER A 210
REMARK 465 ARG A 211
REMARK 465 LYS A 212
REMARK 465 GLY A 213
REMARK 465 GLN A 214
REMARK 465 GLU A 215
REMARK 465 ARG A 216
REMARK 465 PHE A 217
REMARK 465 LEU A 218
REMARK 465 GLU A 219
REMARK 465 HIS A 220
REMARK 465 HIS A 221
REMARK 465 HIS A 222
REMARK 465 HIS A 223
REMARK 465 HIS A 224
REMARK 465 HIS A 225
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 29 CG CD OE1 OE2
REMARK 470 ASP A 31 CG OD1 OD2
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 O HOH A 574 O HOH A 619 1.72
REMARK 500 OG SER A 105 O HOH A 501 1.72
REMARK 500 O HOH A 574 O HOH A 598 1.73
REMARK 500 O HOH A 574 O HOH A 604 1.76
REMARK 500 O HOH A 523 O HOH A 617 2.15
REMARK 500 O HOH A 586 O HOH A 614 2.15
REMARK 500 NH2 ARG A 109 O HOH A 502 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 511 O HOH A 602 3555 1.73
REMARK 500 O HOH A 528 O HOH A 602 3555 1.85
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 TYR A 18 CB - CG - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 TYR A 18 CB - CG - CD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG A 109 NE - CZ - NH2 ANGL. DEV. = 3.1 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 TYR A 108 54.64 -109.71
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 A 12 0.16 SIDE CHAIN
REMARK 500 ARG A 146 0.09 SIDE CHAIN
REMARK 500 ARG A 164 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J1H A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6QG8 RELATED DB: PDB
REMARK 900 BCL-2 COMPLEX WITH PUMA PEPTIDE
REMARK 900 RELATED ID: 6QG8 RELATED DB: PDB
REMARK 900 RELATED ID: 6QGK RELATED DB: PDB
REMARK 900 RELATED ID: 6QGH RELATED DB: PDB
REMARK 900 RELATED ID: 6QGJ RELATED DB: PDB
DBREF 6QGG A 10 33 UNP P10415 BCL2_HUMAN 10 33
DBREF 6QGG A 34 49 UNP Q07817 B2CL1_HUMAN 29 44
DBREF 6QGG A 92 203 UNP P10415 BCL2_HUMAN 92 203
DBREF 6QGG A 204 217 UNP Q07817 B2CL1_HUMAN 197 210
SEQADV 6QGG MET A 7 UNP P10415 INITIATING METHIONINE
SEQADV 6QGG SER A 8 UNP P10415 EXPRESSION TAG
SEQADV 6QGG GLN A 9 UNP P10415 EXPRESSION TAG
SEQADV 6QGG SER A 20 UNP P10415 HIS 20 ENGINEERED MUTATION
SEQADV 6QGG GLN A 95 UNP P10415 LEU 95 ENGINEERED MUTATION
SEQADV 6QGG LEU A 106 UNP P10415 ARG 106 ENGINEERED MUTATION
SEQADV 6QGG GLY A 124 UNP P10415 PHE 124 ENGINEERED MUTATION
SEQADV 6QGG TYR A 127 UNP P10415 ARG 127 ENGINEERED MUTATION
SEQADV 6QGG ALA A 128 UNP P10415 GLY 128 ENGINEERED MUTATION
SEQADV 6QGG SER A 129 UNP P10415 ARG 129 ENGINEERED MUTATION
SEQADV 6QGG VAL A 168 UNP P10415 PRO 168 ENGINEERED MUTATION
SEQADV 6QGG ALA A 175 UNP P10415 LEU 175 ENGINEERED MUTATION
SEQADV 6QGG ALA A 178 UNP P10415 THR 178 ENGINEERED MUTATION
SEQADV 6QGG THR A 179 UNP P10415 GLU 179 ENGINEERED MUTATION
SEQADV 6QGG ASP A 183 UNP P10415 ARG 183 ENGINEERED MUTATION
SEQADV 6QGG LEU A 218 UNP Q07817 EXPRESSION TAG
SEQADV 6QGG GLU A 219 UNP Q07817 EXPRESSION TAG
SEQADV 6QGG HIS A 220 UNP Q07817 EXPRESSION TAG
SEQADV 6QGG HIS A 221 UNP Q07817 EXPRESSION TAG
SEQADV 6QGG HIS A 222 UNP Q07817 EXPRESSION TAG
SEQADV 6QGG HIS A 223 UNP Q07817 EXPRESSION TAG
SEQADV 6QGG HIS A 224 UNP Q07817 EXPRESSION TAG
SEQADV 6QGG HIS A 225 UNP Q07817 EXPRESSION TAG
SEQRES 1 A 177 MET SER GLN ASP ASN ARG GLU ILE VAL MET LYS TYR ILE
SEQRES 2 A 177 SER TYR LYS LEU SER GLN ARG GLY TYR GLU TRP ASP ALA
SEQRES 3 A 177 GLY ASP VAL GLU GLU ASN ARG THR GLU ALA PRO GLU GLY
SEQRES 4 A 177 THR GLU SER GLU VAL VAL HIS GLN THR LEU ARG GLN ALA
SEQRES 5 A 177 GLY ASP ASP PHE SER LEU ARG TYR ARG ARG ASP PHE ALA
SEQRES 6 A 177 GLU MET SER SER GLN LEU HIS LEU THR PRO GLY THR ALA
SEQRES 7 A 177 TYR ALA SER PHE ALA THR VAL VAL GLU GLU LEU PHE ARG
SEQRES 8 A 177 ASP GLY VAL ASN TRP GLY ARG ILE VAL ALA PHE PHE GLU
SEQRES 9 A 177 PHE GLY GLY VAL MET CYS VAL GLU SER VAL ASN ARG GLU
SEQRES 10 A 177 MET SER VAL LEU VAL ASP ASN ILE ALA ALA TRP MET ALA
SEQRES 11 A 177 THR TYR LEU ASN ASP HIS LEU HIS THR TRP ILE GLN ASP
SEQRES 12 A 177 ASN GLY GLY TRP ASP ALA PHE VAL GLU LEU TYR GLY ASN
SEQRES 13 A 177 ASN ALA ALA ALA GLU SER ARG LYS GLY GLN GLU ARG PHE
SEQRES 14 A 177 LEU GLU HIS HIS HIS HIS HIS HIS
HET J1H A 401 60
HETNAM J1H [(3~{R})-3-[[4-[[4-[4-[[2-(4-CHLOROPHENYL)
HETNAM 2 J1H PHENYL]METHYL]PIPERAZIN-1-
HETNAM 3 J1H YL]PHENYL]CARBONYLSULFAMOYL]-2-NITRO-PHENYL]AMINO]-4-
HETNAM 4 J1H PHENYLSULFANYL-BUTYL]-(2-HYDROXY-2-OXOETHYL)-DIMETHYL-
HETNAM 5 J1H AZANIUM
FORMUL 2 J1H C44 H48 CL N6 O7 S2 1+
FORMUL 3 HOH *120(H2 O)
HELIX 1 AA1 ASP A 10 ARG A 26 1 17
HELIX 2 AA2 SER A 48 TYR A 108 1 19
HELIX 3 AA3 TYR A 108 LEU A 119 1 12
HELIX 4 AA4 THR A 125 PHE A 138 1 14
HELIX 5 AA5 ASN A 143 ARG A 164 1 22
HELIX 6 AA6 VAL A 168 LEU A 185 1 18
HELIX 7 AA7 LEU A 185 ASN A 192 1 8
HELIX 8 AA8 GLY A 193 GLY A 203 1 11
SITE 1 AC1 22 ALA A 100 ASP A 103 PHE A 104 TYR A 108
SITE 2 AC1 22 ASP A 111 MET A 115 TYR A 127 LEU A 137
SITE 3 AC1 22 TRP A 144 GLY A 145 VAL A 148 ALA A 149
SITE 4 AC1 22 PHE A 198 TYR A 202 HOH A 518 HOH A 520
SITE 5 AC1 22 HOH A 534 HOH A 542 HOH A 547 HOH A 577
SITE 6 AC1 22 HOH A 585 HOH A 592
CRYST1 55.277 55.277 58.593 90.00 90.00 90.00 P 41 4
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 0.018091 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018091 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017067 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
