HEADER APOPTOSIS 11-JAN-19 6QGH
TITLE STRUCTURE OF HUMAN BCL-2 IN COMPLEX WITH ABT-263
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-263, DRUG DESIGN
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 6QGH 1 REMARK
REVDAT 2 11-SEP-19 6QGH 1 JRNL
REVDAT 1 12-JUN-19 6QGH 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. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 10574
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) : 0.177
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 507
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.11
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1480
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE SET COUNT : 75
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1242
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 97
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.49000
REMARK 3 B22 (A**2) : -0.49000
REMARK 3 B33 (A**2) : -1.00000
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): 0.195
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.154
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.121
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.562
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1363 ; 0.012 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 1141 ; 0.001 ; 0.018
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1859 ; 1.469 ; 1.605
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2589 ; 1.007 ; 1.629
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 160 ; 5.518 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 83 ;30.564 ;21.687
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 205 ;16.294 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;19.047 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 158 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1559 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 279 ; 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 6QGH 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_1292100126.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-AUG-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : D*TREK 9.4SSI
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12847
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 27.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 4.620
REMARK 200 R MERGE (I) : 0.10300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.47100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
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: 6QGG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NACL, 25% PEG3350 AND 0.1 M BIS
REMARK 280 -TRIS BUFFER PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 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 22.20950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.34500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.55500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 32.34500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.20950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.55500
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: 8400 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 SER A 8
REMARK 465 ASP A 31
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 THR A 46
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 GLU A 47 CG CD OE1 OE2
REMARK 470 GLU A 219 CG CD OE1 OE2
REMARK 470 HIS A 220 CG ND1 CD2 CE1 NE2
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 OE2 GLU A 160 O HOH A 501 1.60
REMARK 500 OE1 GLN A 190 O HOH A 502 2.16
REMARK 500 O HOH A 573 O HOH A 595 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 534 O HOH A 555 2454 2.04
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 ARG A 164 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 47.95 -107.31
REMARK 500 GLU A 219 -72.75 -57.76
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 0.21 SIDE CHAIN
REMARK 500 ARG A 98 0.08 SIDE CHAIN
REMARK 500 ARG A 109 0.26 SIDE CHAIN
REMARK 500 ARG A 110 0.23 SIDE CHAIN
REMARK 500 ARG A 146 0.19 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 1XJ 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: 6QGG RELATED DB: PDB
REMARK 900 BCL-2 COMPLEX WITH ANALOGUE OF ABT-737
DBREF 6QGH A 10 33 UNP P10415 BCL2_HUMAN 10 33
DBREF 6QGH A 34 49 UNP Q07817 B2CL1_HUMAN 29 44
DBREF 6QGH A 92 203 UNP P10415 BCL2_HUMAN 92 203
DBREF 6QGH A 204 217 UNP Q07817 B2CL1_HUMAN 197 210
SEQADV 6QGH MET A 7 UNP P10415 INITIATING METHIONINE
SEQADV 6QGH SER A 8 UNP P10415 EXPRESSION TAG
SEQADV 6QGH GLN A 9 UNP P10415 EXPRESSION TAG
SEQADV 6QGH SER A 20 UNP P10415 HIS 20 ENGINEERED MUTATION
SEQADV 6QGH GLN A 95 UNP P10415 LEU 95 ENGINEERED MUTATION
SEQADV 6QGH LEU A 106 UNP P10415 ARG 106 ENGINEERED MUTATION
SEQADV 6QGH GLY A 124 UNP P10415 PHE 124 ENGINEERED MUTATION
SEQADV 6QGH TYR A 127 UNP P10415 ARG 127 ENGINEERED MUTATION
SEQADV 6QGH ALA A 128 UNP P10415 GLY 128 ENGINEERED MUTATION
SEQADV 6QGH SER A 129 UNP P10415 ARG 129 ENGINEERED MUTATION
SEQADV 6QGH VAL A 168 UNP P10415 PRO 168 ENGINEERED MUTATION
SEQADV 6QGH ALA A 175 UNP P10415 LEU 175 ENGINEERED MUTATION
SEQADV 6QGH ALA A 178 UNP P10415 THR 178 ENGINEERED MUTATION
SEQADV 6QGH THR A 179 UNP P10415 GLU 179 ENGINEERED MUTATION
SEQADV 6QGH ASP A 183 UNP P10415 ARG 183 ENGINEERED MUTATION
SEQADV 6QGH LEU A 218 UNP Q07817 EXPRESSION TAG
SEQADV 6QGH GLU A 219 UNP Q07817 EXPRESSION TAG
SEQADV 6QGH HIS A 220 UNP Q07817 EXPRESSION TAG
SEQADV 6QGH HIS A 221 UNP Q07817 EXPRESSION TAG
SEQADV 6QGH HIS A 222 UNP Q07817 EXPRESSION TAG
SEQADV 6QGH HIS A 223 UNP Q07817 EXPRESSION TAG
SEQADV 6QGH HIS A 224 UNP Q07817 EXPRESSION TAG
SEQADV 6QGH 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 1XJ A 401 65
HETNAM 1XJ 4-(4-{[2-(4-CHLOROPHENYL)-5,5-DIMETHYLCYCLOHEX-1-EN-1-
HETNAM 2 1XJ YL]METHYL}PIPERAZIN-1-YL)-N-[(4-{[(2R)-4-(MORPHOLIN-4-
HETNAM 3 1XJ YL)-1-(PHENYLSULFANYL)BUTAN-2-YL]AMINO}-3-
HETNAM 4 1XJ [(TRIFLUOROMETHYL)SULFONYL]PHENYL)SULFONYL]BENZAMIDE
FORMUL 2 1XJ C47 H55 CL F3 N5 O6 S3
FORMUL 3 HOH *97(H2 O)
HELIX 1 AA1 ASP A 10 GLN A 25 1 16
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 ARG A 139 1 15
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 ASN A 204 1 12
HELIX 9 AA9 ASN A 205 HIS A 220 1 16
SITE 1 AC1 23 ALA A 100 ASP A 103 PHE A 104 ARG A 107
SITE 2 AC1 23 TYR A 108 ASP A 111 PHE A 112 HIS A 120
SITE 3 AC1 23 ASN A 143 TRP A 144 GLY A 145 ARG A 146
SITE 4 AC1 23 VAL A 148 ALA A 149 ARG A 164 PHE A 198
SITE 5 AC1 23 LEU A 201 TYR A 202 GLY A 203 ASN A 204
SITE 6 AC1 23 GLU A 209 PHE A 217 HOH A 518
CRYST1 44.419 55.110 64.690 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 0.022513 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018146 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015458 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
