HEADER APOPTOSIS 11-JAN-19 6QGK
TITLE STRUCTURE OF HUMAN BCL-2 IN COMPLEX WITH THIQ-PHENYL PYRAZOLE COMPOUND
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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS APOPTOSIS, BCL2, DRUG DESIGN, SMALL MOLECULE INHIBITOR
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 3 18-SEP-19 6QGK 1 REMARK
REVDAT 2 11-SEP-19 6QGK 1 JRNL
REVDAT 1 12-JUN-19 6QGK 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. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.7
REMARK 3 NUMBER OF REFLECTIONS : 12725
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 613
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1453
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 66
REMARK 3 BIN FREE R VALUE : 0.2330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1157
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 156
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.74000
REMARK 3 B22 (A**2) : -2.40000
REMARK 3 B33 (A**2) : -0.33000
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): 0.137
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.126
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.090
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.007
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1241 ; 0.012 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 1048 ; 0.001 ; 0.018
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1687 ; 1.450 ; 1.678
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2426 ; 1.063 ; 1.706
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 150 ; 4.869 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 71 ;29.631 ;21.549
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 176 ;14.231 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;14.415 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 150 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1446 ; 0.009 ; 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): 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 6QGK 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_1292100122.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9728
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 : 14748
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.8
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 45.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M CA ACETATE, 15% PEG4K, 0.1M TRIS
REMARK 280 BUFFER PH 7.5, VAPOR DIFFUSION, SITTING DROP, 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 23.78500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.68550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.05200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 32.68550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.78500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.05200
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: 150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 SER A 8
REMARK 465 GLN A 9
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 THR A 46
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 ARG A 12 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 31 CG OD1 OD2
REMARK 470 GLU A 47 CG CD OE1 OE2
REMARK 470 GLU A 49 CG CD OE1 OE2
REMARK 470 GLN A 95 CD OE1 NE2
REMARK 470 GLN A 114 CG CD OE1 NE2
REMARK 470 ARG A 211 CG CD NE CZ NH1 NH2
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 643 O HOH A 649 1.10
REMARK 500 O HOH A 598 O HOH A 629 1.64
REMARK 500 O HOH A 645 O HOH A 651 2.03
REMARK 500 OG SER A 129 O HOH A 501 2.14
REMARK 500 O HOH A 580 O HOH A 630 2.17
REMARK 500 OE1 GLU A 136 O HOH A 502 2.17
REMARK 500 ND2 ASN A 11 OD1 ASN A 182 2.18
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 72.71 53.45
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 26 0.13 SIDE CHAIN
REMARK 500 ARG A 98 0.12 SIDE CHAIN
REMARK 500 ARG A 139 0.25 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 656 DISTANCE = 5.87 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue J1Q A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 402
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: 6QGG RELATED DB: PDB
REMARK 900 BCL-2 COMPLEX WITH ANALOGUE OF ABT-737
REMARK 900 RELATED ID: 6QGH RELATED DB: PDB
REMARK 900 BCL-2 COMPLEX WITH ABT-263
REMARK 900 RELATED ID: 6QGJ RELATED DB: PDB
REMARK 900 BCL-2 COMPLEX WITH HYBRID INHIBITOR
DBREF 6QGK A 10 33 UNP P10415 BCL2_HUMAN 10 33
DBREF 6QGK A 34 49 UNP Q07817 B2CL1_HUMAN 29 44
DBREF 6QGK A 92 203 UNP P10415 BCL2_HUMAN 92 203
DBREF 6QGK A 204 217 UNP Q07817 B2CL1_HUMAN 197 210
SEQADV 6QGK MET A 7 UNP P10415 INITIATING METHIONINE
SEQADV 6QGK SER A 8 UNP P10415 EXPRESSION TAG
SEQADV 6QGK GLN A 9 UNP P10415 EXPRESSION TAG
SEQADV 6QGK SER A 20 UNP P10415 HIS 20 ENGINEERED MUTATION
SEQADV 6QGK GLN A 95 UNP P10415 LEU 95 ENGINEERED MUTATION
SEQADV 6QGK LEU A 106 UNP P10415 ARG 106 ENGINEERED MUTATION
SEQADV 6QGK GLN A 114 UNP P10415 GLU 114 ENGINEERED MUTATION
SEQADV 6QGK GLY A 124 UNP P10415 PHE 124 ENGINEERED MUTATION
SEQADV 6QGK TYR A 127 UNP P10415 ARG 127 ENGINEERED MUTATION
SEQADV 6QGK ALA A 128 UNP P10415 GLY 128 ENGINEERED MUTATION
SEQADV 6QGK SER A 129 UNP P10415 ARG 129 ENGINEERED MUTATION
SEQADV 6QGK ALA A 135 UNP P10415 GLU 135 ENGINEERED MUTATION
SEQADV 6QGK ALA A 165 UNP P10415 GLU 165 ENGINEERED MUTATION
SEQADV 6QGK VAL A 168 UNP P10415 PRO 168 ENGINEERED MUTATION
SEQADV 6QGK ALA A 175 UNP P10415 LEU 175 ENGINEERED MUTATION
SEQADV 6QGK ALA A 178 UNP P10415 THR 178 ENGINEERED MUTATION
SEQADV 6QGK THR A 179 UNP P10415 GLU 179 ENGINEERED MUTATION
SEQADV 6QGK ASP A 183 UNP P10415 ARG 183 ENGINEERED MUTATION
SEQADV 6QGK LEU A 218 UNP Q07817 EXPRESSION TAG
SEQADV 6QGK GLU A 219 UNP Q07817 EXPRESSION TAG
SEQADV 6QGK HIS A 220 UNP Q07817 EXPRESSION TAG
SEQADV 6QGK HIS A 221 UNP Q07817 EXPRESSION TAG
SEQADV 6QGK HIS A 222 UNP Q07817 EXPRESSION TAG
SEQADV 6QGK HIS A 223 UNP Q07817 EXPRESSION TAG
SEQADV 6QGK HIS A 224 UNP Q07817 EXPRESSION TAG
SEQADV 6QGK 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 GLN MET SER SER GLN LEU HIS LEU THR PRO GLY THR ALA
SEQRES 7 A 177 TYR ALA SER PHE ALA THR VAL VAL ALA 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 ALA
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 J1Q A 401 37
HET ACT A 402 4
HETNAM J1Q 1-[2-[[(3~{S})-3-(AMINOMETHYL)-3,4-DIHYDRO-1~{H}-
HETNAM 2 J1Q ISOQUINOLIN-2-YL]CARBONYL]PHENYL]-~{N},~{N}-DIBUTYL-5-
HETNAM 3 J1Q METHYL-PYRAZOLE-3-CARBOXAMIDE
HETNAM ACT ACETATE ION
FORMUL 2 J1Q C30 H39 N5 O2
FORMUL 3 ACT C2 H3 O2 1-
FORMUL 4 HOH *156(H2 O)
HELIX 1 AA1 ASP A 10 GLN A 25 1 16
HELIX 2 AA2 SER A 48 HIS A 120 1 31
HELIX 3 AA3 THR A 125 PHE A 138 1 14
HELIX 4 AA4 ASN A 143 ARG A 164 1 22
HELIX 5 AA5 VAL A 168 LEU A 185 1 18
HELIX 6 AA6 LEU A 185 ASN A 192 1 8
HELIX 7 AA7 GLY A 193 ARG A 211 1 19
SITE 1 AC1 10 PHE A 104 TYR A 108 ASP A 111 LEU A 137
SITE 2 AC1 10 ASN A 163 ACT A 402 HOH A 509 HOH A 555
SITE 3 AC1 10 HOH A 579 HOH A 588
SITE 1 AC2 7 ARG A 146 GLU A 160 ARG A 164 J1Q A 401
SITE 2 AC2 7 HOH A 510 HOH A 517 HOH A 520
CRYST1 47.570 50.104 65.371 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 0.021022 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019958 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015297 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
