HEADER APOPTOSIS 16-FEB-19 6O0L
TITLE CRYSTAL STRUCTURE OF BCL-2 G101V MUTATION WITH VENETOCLAX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS REGULATOR BCL-2,BCL-2-LIKE PROTEIN 1,APOPTOSIS
COMPND 3 REGULATOR BCL-2;
COMPND 4 CHAIN: A, C;
COMPND 5 SYNONYM: BCL2-L-1,APOPTOSIS REGULATOR BCL-X;
COMPND 6 ENGINEERED: YES;
COMPND 7 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: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS BCL-2, VENETOCLAX, COMPLEX, PROTEIN-PROTEIN INTERFACE INHIBITOR,
KEYWDS 2 RESISTANCE MUTATION, FDA APPROVED DRUG COMPLEX, APOPTOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR R.W.BIRKINSHAW,C.S.LUO,P.M.COLMAN,P.E.CZABOTAR
REVDAT 5 11-DEC-19 6O0L 1 HETSYN
REVDAT 4 20-NOV-19 6O0L 1 COMPND HETNAM FORMUL
REVDAT 3 10-JUL-19 6O0L 1 COMPND SOURCE DBREF SEQADV
REVDAT 2 19-JUN-19 6O0L 1 JRNL
REVDAT 1 22-MAY-19 6O0L 0
JRNL AUTH R.W.BIRKINSHAW,J.N.GONG,C.S.LUO,D.LIO,C.A.WHITE,
JRNL AUTH 2 M.A.ANDERSON,P.BLOMBERY,G.LESSENE,I.J.MAJEWSKI,R.THIJSSEN,
JRNL AUTH 3 A.W.ROBERTS,D.C.S.HUANG,P.M.COLMAN,P.E.CZABOTAR
JRNL TITL STRUCTURES OF BCL-2 IN COMPLEX WITH VENETOCLAX REVEAL THE
JRNL TITL 2 MOLECULAR BASIS OF RESISTANCE MUTATIONS.
JRNL REF NAT COMMUN V. 10 2385 2019
JRNL REFN ESSN 2041-1723
JRNL PMID 31160589
JRNL DOI 10.1038/S41467-019-10363-1
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.14_3260
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 12924
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860
REMARK 3 FREE R VALUE TEST SET COUNT : 628
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 47.5190 - 3.4919 1.00 3121 155 0.1762 0.2041
REMARK 3 2 3.4919 - 2.7717 1.00 3054 158 0.2059 0.2154
REMARK 3 3 2.7717 - 2.4214 1.00 3095 159 0.2182 0.2920
REMARK 3 4 2.4214 - 2.2000 1.00 3026 156 0.2353 0.2787
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.340
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 2550
REMARK 3 ANGLE : 0.589 3449
REMARK 3 CHIRALITY : 0.038 334
REMARK 3 PLANARITY : 0.003 505
REMARK 3 DIHEDRAL : 18.466 1505
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 9 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2479 7.2737 -5.3664
REMARK 3 T TENSOR
REMARK 3 T11: 0.3344 T22: 0.3400
REMARK 3 T33: 0.2133 T12: -0.0092
REMARK 3 T13: -0.0656 T23: -0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 3.8090 L22: 6.1047
REMARK 3 L33: 2.4332 L12: -0.3261
REMARK 3 L13: 0.7418 L23: -0.5194
REMARK 3 S TENSOR
REMARK 3 S11: 0.1771 S12: 0.4439 S13: -0.2963
REMARK 3 S21: -1.0320 S22: 0.2988 S23: -0.1479
REMARK 3 S31: 0.0642 S32: 0.0586 S33: 0.0930
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 91 THROUGH 107 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.6490 3.2669 -5.0880
REMARK 3 T TENSOR
REMARK 3 T11: 0.6027 T22: 0.4206
REMARK 3 T33: 0.2157 T12: -0.1655
REMARK 3 T13: -0.0976 T23: 0.0829
REMARK 3 L TENSOR
REMARK 3 L11: 4.3850 L22: 3.6291
REMARK 3 L33: 4.7690 L12: 2.2120
REMARK 3 L13: 3.0025 L23: -0.1722
REMARK 3 S TENSOR
REMARK 3 S11: 0.0795 S12: 0.8164 S13: -0.3613
REMARK 3 S21: -0.3519 S22: 0.1691 S23: -0.0911
REMARK 3 S31: 1.1246 S32: 0.0287 S33: -0.4966
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 108 THROUGH 117 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.3031 19.4970 -5.6781
REMARK 3 T TENSOR
REMARK 3 T11: 0.6627 T22: 0.9200
REMARK 3 T33: 0.5580 T12: -0.2248
REMARK 3 T13: -0.2422 T23: 0.1463
REMARK 3 L TENSOR
REMARK 3 L11: 8.2951 L22: 4.7725
REMARK 3 L33: 3.6344 L12: 6.2242
REMARK 3 L13: -5.3592 L23: -4.1540
REMARK 3 S TENSOR
REMARK 3 S11: 0.5597 S12: -0.6487 S13: -0.1045
REMARK 3 S21: 0.9529 S22: -0.2340 S23: -0.0977
REMARK 3 S31: -0.2328 S32: 0.1774 S33: -0.7316
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 118 THROUGH 203 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9757 13.6087 4.0071
REMARK 3 T TENSOR
REMARK 3 T11: 0.2752 T22: 0.2197
REMARK 3 T33: 0.1604 T12: 0.0033
REMARK 3 T13: -0.0514 T23: 0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 3.4963 L22: 4.4856
REMARK 3 L33: 3.6884 L12: 2.1552
REMARK 3 L13: -1.2569 L23: -1.8068
REMARK 3 S TENSOR
REMARK 3 S11: 0.0757 S12: -0.0248 S13: 0.2609
REMARK 3 S21: 0.0121 S22: 0.0423 S23: 0.2914
REMARK 3 S31: -0.2136 S32: 0.0058 S33: -0.1039
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 8 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2728 37.0448 18.5847
REMARK 3 T TENSOR
REMARK 3 T11: 0.4071 T22: 0.4030
REMARK 3 T33: 0.2829 T12: 0.0435
REMARK 3 T13: -0.0472 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 3.3195 L22: 6.2783
REMARK 3 L33: 3.8076 L12: 1.1681
REMARK 3 L13: -1.2793 L23: 1.9208
REMARK 3 S TENSOR
REMARK 3 S11: -0.0383 S12: 0.3794 S13: 0.2960
REMARK 3 S21: -0.8625 S22: 0.1371 S23: 0.0797
REMARK 3 S31: 0.1750 S32: -0.7281 S33: 0.0562
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 91 THROUGH 107 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2653 40.8833 18.6098
REMARK 3 T TENSOR
REMARK 3 T11: 0.5095 T22: 0.4285
REMARK 3 T33: 0.3098 T12: -0.1638
REMARK 3 T13: 0.0373 T23: 0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 6.6553 L22: 4.7351
REMARK 3 L33: 7.5730 L12: -1.0930
REMARK 3 L13: -4.8840 L23: 4.1487
REMARK 3 S TENSOR
REMARK 3 S11: -0.2229 S12: 1.0357 S13: 0.7811
REMARK 3 S21: -0.8855 S22: 0.3675 S23: -0.2476
REMARK 3 S31: -0.9613 S32: 0.1756 S33: -0.8028
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 108 THROUGH 117 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9519 24.7179 17.9498
REMARK 3 T TENSOR
REMARK 3 T11: 0.8272 T22: 0.8687
REMARK 3 T33: 0.4928 T12: 0.0736
REMARK 3 T13: 0.1285 T23: -0.3370
REMARK 3 L TENSOR
REMARK 3 L11: 0.5340 L22: 1.0236
REMARK 3 L33: 1.3204 L12: 0.1186
REMARK 3 L13: -0.3319 L23: 0.6865
REMARK 3 S TENSOR
REMARK 3 S11: 0.0918 S12: -0.1489 S13: 0.1130
REMARK 3 S21: 0.2347 S22: 0.0676 S23: -0.1701
REMARK 3 S31: 0.3800 S32: 0.2134 S33: 0.9681
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 118 THROUGH 143 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2094 22.5434 29.3811
REMARK 3 T TENSOR
REMARK 3 T11: 0.3731 T22: 0.2877
REMARK 3 T33: 0.3973 T12: 0.0295
REMARK 3 T13: -0.0920 T23: -0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 4.5499 L22: 2.8032
REMARK 3 L33: 6.3474 L12: 2.7276
REMARK 3 L13: 2.0088 L23: 2.3679
REMARK 3 S TENSOR
REMARK 3 S11: 0.3670 S12: 0.2827 S13: -0.8606
REMARK 3 S21: 0.8069 S22: 0.4779 S23: -0.7723
REMARK 3 S31: 0.8037 S32: 0.2250 S33: -0.5902
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 144 THROUGH 203 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8089 33.9406 27.0697
REMARK 3 T TENSOR
REMARK 3 T11: 0.2805 T22: 0.2647
REMARK 3 T33: 0.1677 T12: 0.0085
REMARK 3 T13: 0.0183 T23: 0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 4.6277 L22: 5.5927
REMARK 3 L33: 4.2495 L12: 3.5222
REMARK 3 L13: 2.7365 L23: 2.1242
REMARK 3 S TENSOR
REMARK 3 S11: -0.0123 S12: 0.0182 S13: -0.0839
REMARK 3 S21: -0.1777 S22: 0.1392 S23: -0.0272
REMARK 3 S31: -0.1538 S32: -0.0022 S33: -0.1526
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: AUTHORS STATE THAT THE DATA WERE
REMARK 3 PROCESSED AND REFINED IN SPACEGROUP P21, DESPITE BEING POSSIBLE
REMARK 3 TO MERGE AND REFINE IN ORTHORHOMBIC SPACEGROUP P212121. THIS WAS
REMARK 3 DUE TO POORER REFINEMENT STATISTICS IN THE ORTHORHOMBIC
REMARK 3 SPACEGROUP.
REMARK 4
REMARK 4 6O0L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-19.
REMARK 100 THE DEPOSITION ID IS D_1000239798.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUL-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12909
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 47.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.560
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6O0G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 26.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% PEG4K, 35% PEG400, 0.08M MES PH
REMARK 280 6.0, VAPOR DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 41.00250
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 ASP A 75
REMARK 465 ASP A 76
REMARK 465 VAL A 77
REMARK 465 GLU A 78
REMARK 465 GLU A 79
REMARK 465 ASN A 80
REMARK 465 ARG A 81
REMARK 465 THR A 82
REMARK 465 GLU A 83
REMARK 465 ALA A 84
REMARK 465 PRO A 85
REMARK 465 GLU A 86
REMARK 465 GLY A 87
REMARK 465 THR A 88
REMARK 465 GLU A 89
REMARK 465 PRO A 204
REMARK 465 SER A 205
REMARK 465 MET A 206
REMARK 465 ARG A 207
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 HIS C 3
REMARK 465 ALA C 4
REMARK 465 GLY C 5
REMARK 465 ARG C 6
REMARK 465 THR C 7
REMARK 465 ASP C 75
REMARK 465 ASP C 76
REMARK 465 VAL C 77
REMARK 465 GLU C 78
REMARK 465 GLU C 79
REMARK 465 ASN C 80
REMARK 465 ARG C 81
REMARK 465 THR C 82
REMARK 465 GLU C 83
REMARK 465 ALA C 84
REMARK 465 PRO C 85
REMARK 465 GLU C 86
REMARK 465 GLY C 87
REMARK 465 THR C 88
REMARK 465 GLU C 89
REMARK 465 PRO C 204
REMARK 465 SER C 205
REMARK 465 MET C 206
REMARK 465 ARG C 207
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LBM A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LBM C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 304
DBREF 6O0L A 1 75 UNP P10415 BCL2_HUMAN 1 34
DBREF 6O0L A 76 91 UNP Q07817 B2CL1_HUMAN 29 44
DBREF 6O0L A 92 207 UNP P10415 BCL2_HUMAN 92 207
DBREF 6O0L C 1 75 UNP P10415 BCL2_HUMAN 1 34
DBREF 6O0L C 76 91 UNP Q07817 B2CL1_HUMAN 29 44
DBREF 6O0L C 92 207 UNP P10415 BCL2_HUMAN 92 207
SEQADV 6O0L VAL A 101 UNP P10415 GLY 101 ENGINEERED MUTATION
SEQADV 6O0L VAL C 101 UNP P10415 GLY 101 ENGINEERED MUTATION
SEQRES 1 A 166 MET ALA HIS ALA GLY ARG THR GLY TYR ASP ASN ARG GLU
SEQRES 2 A 166 ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER GLN ARG
SEQRES 3 A 166 GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL GLU GLU ASN
SEQRES 4 A 166 ARG THR GLU ALA PRO GLU GLY THR GLU SER GLU VAL VAL
SEQRES 5 A 166 HIS LEU THR LEU ARG GLN ALA VAL ASP ASP PHE SER ARG
SEQRES 6 A 166 ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER GLN LEU
SEQRES 7 A 166 HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE ALA THR
SEQRES 8 A 166 VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN TRP GLY
SEQRES 9 A 166 ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL MET CYS
SEQRES 10 A 166 VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU VAL ASP
SEQRES 11 A 166 ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN ARG HIS
SEQRES 12 A 166 LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP ASP ALA
SEQRES 13 A 166 PHE VAL GLU LEU TYR GLY PRO SER MET ARG
SEQRES 1 C 166 MET ALA HIS ALA GLY ARG THR GLY TYR ASP ASN ARG GLU
SEQRES 2 C 166 ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER GLN ARG
SEQRES 3 C 166 GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL GLU GLU ASN
SEQRES 4 C 166 ARG THR GLU ALA PRO GLU GLY THR GLU SER GLU VAL VAL
SEQRES 5 C 166 HIS LEU THR LEU ARG GLN ALA VAL ASP ASP PHE SER ARG
SEQRES 6 C 166 ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER GLN LEU
SEQRES 7 C 166 HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE ALA THR
SEQRES 8 C 166 VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN TRP GLY
SEQRES 9 C 166 ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL MET CYS
SEQRES 10 C 166 VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU VAL ASP
SEQRES 11 C 166 ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN ARG HIS
SEQRES 12 C 166 LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP ASP ALA
SEQRES 13 C 166 PHE VAL GLU LEU TYR GLY PRO SER MET ARG
HET LBM A 301 61
HET PEG A 302 7
HET PEG A 303 7
HET CL A 304 1
HET LBM C 301 61
HET PEG C 302 7
HET PEG C 303 7
HET CL C 304 1
HETNAM LBM 4-{4-[(4'-CHLORO-5,5-DIMETHYL[3,4,5,6-TETRAHYDRO[1,1'-
HETNAM 2 LBM BIPHENYL]]-2-YL)METHYL]PIPERAZIN-1-YL}-N-[(3-NITRO-4-
HETNAM 3 LBM {[(OXAN-4-YL)METHYL]AMINO}PHENYL)SULFONYL]-2-[(1H-
HETNAM 4 LBM PYRROLO[2,3-B]PYRIDIN-5-YL)OXY]BENZAMIDE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM CL CHLORIDE ION
HETSYN LBM VENETOCLAX, 2-((1H-PYRROLO[2,3-B]PYRIDIN-5-YL)OXY)-4-
HETSYN 2 LBM (4-((4'-CHLORO-5,5-DIMETHYL-3,4,5,6-TETRAHYDRO-[1,1'-
HETSYN 3 LBM BIPHENYL]-2-YL)METHYL)PIPERAZIN-1-YL)-N-((3-NITRO-4-
HETSYN 4 LBM (((TETRAHYDRO-2H-PYRAN-4-YL)METHYL)AMINO)PHENYL)
HETSYN 5 LBM SULFONYL)BENZAMIDE
FORMUL 3 LBM 2(C45 H50 CL N7 O7 S)
FORMUL 4 PEG 4(C4 H10 O3)
FORMUL 6 CL 2(CL 1-)
FORMUL 11 HOH *22(H2 O)
HELIX 1 AA1 ASP A 10 GLN A 25 1 16
HELIX 2 AA2 GLU A 91 TYR A 108 1 18
HELIX 3 AA3 TYR A 108 GLN A 118 1 11
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 SER A 167 HIS A 184 1 18
HELIX 7 AA7 LEU A 185 ASN A 192 1 8
HELIX 8 AA8 GLY A 193 GLY A 203 1 11
HELIX 9 AA9 ASP C 10 GLN C 25 1 16
HELIX 10 AB1 GLU C 91 TYR C 108 1 18
HELIX 11 AB2 TYR C 108 GLN C 118 1 11
HELIX 12 AB3 THR C 125 PHE C 138 1 14
HELIX 13 AB4 ASN C 143 ARG C 164 1 22
HELIX 14 AB5 SER C 167 HIS C 184 1 18
HELIX 15 AB6 LEU C 185 ASN C 192 1 8
HELIX 16 AB7 GLY C 193 GLY C 203 1 11
SITE 1 AC1 17 ARG A 12 ALA A 100 ASP A 103 ARG A 107
SITE 2 AC1 17 TYR A 108 LEU A 137 TRP A 144 GLY A 145
SITE 3 AC1 17 VAL A 148 ALA A 149 GLU A 152 PHE A 153
SITE 4 AC1 17 VAL A 156 PHE A 198 TYR A 202 PEG A 303
SITE 5 AC1 17 HOH A 403
SITE 1 AC2 3 ARG A 12 MET A 16 PEG A 303
SITE 1 AC3 5 ASN A 143 THR A 178 LBM A 301 PEG A 302
SITE 2 AC3 5 CL A 304
SITE 1 AC4 4 GLU A 179 ASN A 182 ARG A 183 PEG A 303
SITE 1 AC5 19 ARG C 12 ALA C 100 ASP C 103 ARG C 107
SITE 2 AC5 19 TYR C 108 GLU C 136 LEU C 137 TRP C 144
SITE 3 AC5 19 GLY C 145 VAL C 148 ALA C 149 GLU C 152
SITE 4 AC5 19 PHE C 153 VAL C 156 PHE C 198 TYR C 202
SITE 5 AC5 19 PEG C 303 HOH C 401 HOH C 404
SITE 1 AC6 2 ARG C 12 PEG C 303
SITE 1 AC7 6 ARG C 12 ASN C 143 ARG C 146 LBM C 301
SITE 2 AC7 6 PEG C 302 CL C 304
SITE 1 AC8 4 GLU C 179 ASN C 182 ARG C 183 PEG C 303
CRYST1 33.147 82.005 47.508 90.00 90.08 90.00 P 1 21 1 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 0.030169 0.000000 0.000043 0.00000
SCALE2 0.000000 0.012194 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021049 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
