HEADER APOPTOSIS 23-MAY-18 6GL8
TITLE CRYSTAL STRUCTURE OF BCL-2 IN COMPLEX WITH THE NOVEL ORALLY ACTIVE
TITLE 2 INHIBITOR S55746
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS REGULATOR BCL-2,APOPTOSIS REGULATOR BCL-2,
COMPND 3 APOPTOSIS REGULATOR BCL-2,BCL-2-LIKE PROTEIN 1,APOPTOSIS REGULATOR
COMPND 4 BCL-2,APOPTOSIS REGULATOR BCL-2,APOPTOSIS REGULATOR BCL-2;
COMPND 5 CHAIN: A;
COMPND 6 SYNONYM: BCL2-L-1,APOPTOSIS 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(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: PLYSS
KEYWDS APOPTOSIS-INHIBITOR COMPLEX, BCL-2, BH3-MIMETICS, APOPTOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR P.CASARA,J.DAVIDSON,A.CLAPERON,G.LE TOUMELIN-BRAIZAT,M.VOGLER,
AUTHOR 2 A.BRUNO,M.CHANRION,G.LYSIAK-AUVITY,T.LE DIGUARHER,J.B.STARCK,I.CHEN,
AUTHOR 3 N.WHITEHEAD,C.GRAHAM,N.MATASSOVA,P.DOKURNO,C.PEDDER,Y.WANG,S.QIU,
AUTHOR 4 A.M.GIRARD,E.SCHNEIDER,F.GRAVE,A.STUDENY,G.GUASCONI,F.ROCCHETTI,
AUTHOR 5 S.MAIGA,J.M.HENLIN,F.COLLAND,L.KRAUS-BERTHIER,S.LE GOUILL,
AUTHOR 6 M.J.S.DYER,R.HUBBARD,M.WOOD,M.AMIOT,G.M.COHEN,J.A.HICKMAN,E.MORRIS,
AUTHOR 7 J.MURRAY,O.GENESTE
REVDAT 2 14-NOV-18 6GL8 1 JRNL
REVDAT 1 07-NOV-18 6GL8 0
JRNL AUTH P.CASARA,J.DAVIDSON,A.CLAPERON,G.LE TOUMELIN-BRAIZAT,
JRNL AUTH 2 M.VOGLER,A.BRUNO,M.CHANRION,G.LYSIAK-AUVITY,T.LE DIGUARHER,
JRNL AUTH 3 J.B.STARCK,I.CHEN,N.WHITEHEAD,C.GRAHAM,N.MATASSOVA,
JRNL AUTH 4 P.DOKURNO,C.PEDDER,Y.WANG,S.QIU,A.M.GIRARD,E.SCHNEIDER,
JRNL AUTH 5 F.GRAVE,A.STUDENY,G.GUASCONI,F.ROCCHETTI,S.MAIGA,J.M.HENLIN,
JRNL AUTH 6 F.COLLAND,L.KRAUS-BERTHIER,S.LE GOUILL,M.J.S.DYER,R.HUBBARD,
JRNL AUTH 7 M.WOOD,M.AMIOT,G.M.COHEN,J.A.HICKMAN,E.MORRIS,J.MURRAY,
JRNL AUTH 8 O.GENESTE
JRNL TITL S55746 IS A NOVEL ORALLY ACTIVE BCL-2 SELECTIVE AND POTENT
JRNL TITL 2 INHIBITOR THAT IMPAIRS HEMATOLOGICAL TUMOR GROWTH.
JRNL REF ONCOTARGET V. 9 20075 2018
JRNL REFN ESSN 1949-2553
JRNL PMID 29732004
JRNL DOI 10.18632/ONCOTARGET.24744
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0222
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 26743
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1447
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.48
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3844
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE SET COUNT : 211
REMARK 3 BIN FREE R VALUE : 0.2660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1188
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 151
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.00000
REMARK 3 B22 (A**2) : -0.62000
REMARK 3 B33 (A**2) : -0.38000
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): 0.066
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.064
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.044
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.120
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1306 ; 0.015 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 1083 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1775 ; 1.820 ; 1.714
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2479 ; 1.139 ; 1.661
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 148 ; 5.360 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 86 ;29.067 ;20.465
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 203 ;16.350 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;17.262 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 148 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1507 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 271 ; 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): 582 ; 2.290 ; 2.093
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 581 ; 2.252 ; 2.085
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 726 ; 3.284 ; 3.118
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 727 ; 3.297 ; 3.122
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 724 ; 3.540 ; 2.498
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 725 ; 3.538 ; 2.497
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1044 ; 5.316 ; 3.595
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6794 ; 8.336 ;43.836
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6649 ; 8.334 ;43.446
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
REMARK 4
REMARK 4 6GL8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1200009904.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.25
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28969
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.390
REMARK 200 RESOLUTION RANGE LOW (A) : 42.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.03400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.54000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.5.02
REMARK 200 STARTING MODEL: 2W3L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 29.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE BUFFER PH 5.25,
REMARK 280 20% JEFFAMINE600, 10% PEG3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 284K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 17.54500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.52000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.45000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.52000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.54500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.45000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 8150 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 -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 HIS A 2
REMARK 465 LEU A 3
REMARK 465 VAL A 4
REMARK 465 PRO A 5
REMARK 465 ARG A 6
REMARK 465 VAL A 36
REMARK 465 GLU A 37
REMARK 465 GLU A 38
REMARK 465 ASN A 39
REMARK 465 ARG A 40
REMARK 465 THR A 41
REMARK 465 GLU A 42
REMARK 465 ALA A 43
REMARK 465 PRO A 44
REMARK 465 GLU A 45
REMARK 465 GLY A 46
REMARK 465 THR A 47
REMARK 465 PRO A 204
REMARK 465 SER A 205
REMARK 465 MET A 206
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 50 CG CD OE1 OE2
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 498 O HOH A 503 1.70
REMARK 500 O HOH A 413 O HOH A 515 1.83
REMARK 500 O HOH A 436 O HOH A 515 1.91
REMARK 500 O HOH A 481 O HOH A 529 2.19
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 HIS A 120 59.51 33.91
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 139 0.09 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 F3Q A 301
DBREF 6GL8 A 9 33 UNP P10415 BCL2_HUMAN 9 33
DBREF 6GL8 A 34 50 PDB 6GL8 6GL8 34 50
DBREF 6GL8 A 92 206 UNP P10415 BCL2_HUMAN 92 206
SEQADV 6GL8 MET A -6 UNP P10415 INITIATING METHIONINE
SEQADV 6GL8 HIS A -5 UNP P10415 EXPRESSION TAG
SEQADV 6GL8 HIS A -4 UNP P10415 EXPRESSION TAG
SEQADV 6GL8 HIS A -3 UNP P10415 EXPRESSION TAG
SEQADV 6GL8 HIS A -2 UNP P10415 EXPRESSION TAG
SEQADV 6GL8 HIS A -1 UNP P10415 EXPRESSION TAG
SEQADV 6GL8 HIS A 0 UNP P10415 EXPRESSION TAG
SEQADV 6GL8 HIS A 1 UNP P10415 EXPRESSION TAG
SEQADV 6GL8 HIS A 2 UNP P10415 EXPRESSION TAG
SEQADV 6GL8 LEU A 3 UNP P10415 EXPRESSION TAG
SEQADV 6GL8 VAL A 4 UNP P10415 EXPRESSION TAG
SEQADV 6GL8 PRO A 5 UNP P10415 EXPRESSION TAG
SEQADV 6GL8 ARG A 6 UNP P10415 EXPRESSION TAG
SEQADV 6GL8 GLY A 7 UNP P10415 EXPRESSION TAG
SEQADV 6GL8 SER A 8 UNP P10415 EXPRESSION TAG
SEQADV 6GL8 LYS A 95 UNP P10415 LEU 95 ENGINEERED MUTATION
SEQADV 6GL8 GLU A 99 UNP P10415 GLN 99 ENGINEERED MUTATION
SEQRES 1 A 172 MET HIS HIS HIS HIS HIS HIS HIS HIS LEU VAL PRO ARG
SEQRES 2 A 172 GLY SER TYR ASP ASN ARG GLU ILE VAL MET LYS TYR ILE
SEQRES 3 A 172 HIS TYR LYS LEU SER GLN ARG GLY TYR GLU TRP ASP ALA
SEQRES 4 A 172 GLY ALA ASP VAL GLU GLU ASN ARG THR GLU ALA PRO GLU
SEQRES 5 A 172 GLY THR GLU SER GLU VAL VAL HIS LYS THR LEU ARG GLU
SEQRES 6 A 172 ALA GLY ASP ASP PHE SER ARG ARG TYR ARG ARG ASP PHE
SEQRES 7 A 172 ALA GLU MET SER SER GLN LEU HIS LEU THR PRO PHE THR
SEQRES 8 A 172 ALA ARG GLY ARG PHE ALA THR VAL VAL GLU GLU LEU PHE
SEQRES 9 A 172 ARG ASP GLY VAL ASN TRP GLY ARG ILE VAL ALA PHE PHE
SEQRES 10 A 172 GLU PHE GLY GLY VAL MET CYS VAL GLU SER VAL ASN ARG
SEQRES 11 A 172 GLU MET SER PRO LEU VAL ASP ASN ILE ALA LEU TRP MET
SEQRES 12 A 172 THR GLU TYR LEU ASN ARG HIS LEU HIS THR TRP ILE GLN
SEQRES 13 A 172 ASP ASN GLY GLY TRP ASP ALA PHE VAL GLU LEU TYR GLY
SEQRES 14 A 172 PRO SER MET
HET F3Q A 301 53
HETNAM F3Q ~{N}-(4-HYDROXYPHENYL)-3-[6-[[(3~{S})-3-(MORPHOLIN-4-
HETNAM 2 F3Q YLMETHYL)-3,4-DIHYDRO-1~{H}-ISOQUINOLIN-2-
HETNAM 3 F3Q YL]CARBONYL]-1,3-BENZODIOXOL-5-YL]-~{N}-PHENYL-5,6,7,
HETNAM 4 F3Q 8-TETRAHYDROINDOLIZINE-1-CARBOXAMIDE
FORMUL 2 F3Q C43 H42 N4 O6
FORMUL 3 HOH *151(H2 O)
HELIX 1 AA1 ASP A 10 ARG A 26 1 17
HELIX 2 AA2 TRP A 30 ALA A 34 5 5
HELIX 3 AA3 SER A 49 TYR A 108 1 19
HELIX 4 AA4 TYR A 108 HIS A 120 1 13
HELIX 5 AA5 THR A 125 ARG A 139 1 15
HELIX 6 AA6 ASN A 143 ARG A 164 1 22
HELIX 7 AA7 PRO A 168 LEU A 185 1 18
HELIX 8 AA8 LEU A 185 ASN A 192 1 8
HELIX 9 AA9 GLY A 193 GLY A 203 1 11
SITE 1 AC1 18 PHE A 104 TYR A 108 ASP A 111 PHE A 112
SITE 2 AC1 18 GLN A 118 LEU A 137 GLY A 145 ARG A 146
SITE 3 AC1 18 ALA A 149 PHE A 153 ASP A 171 HOH A 415
SITE 4 AC1 18 HOH A 421 HOH A 431 HOH A 482 HOH A 484
SITE 5 AC1 18 HOH A 489 HOH A 525
CRYST1 35.090 46.900 85.040 90.00 90.00 90.00 P 21 21 21 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 0.028498 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021322 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011759 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
