HEADER APOPTOSIS 12-APR-12 4AQ3
TITLE HUMAN BCL-2 WITH PHENYLACYLSULFONAMIDE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS REGULATOR BCL-2, BCL-2-LIKE PROTEIN 1;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: RESIDUES 1-33 AND 92-207 OF P10415 AND RESIDUES 29-44 OF
COMPND 5 Q07817;
COMPND 6 SYNONYM: BCL2-L-1, APOPTOSIS REGULATOR BCL-X;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: APOPTOSIS REGULATOR BCL-2 WITH PUTATIVE FLEXIBLE
COMPND 9 LOOP REPLACED WITH A PORTION OF APOPTOSIS REGULATOR BCL-X PROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS APOPTOSIS, CHIMERA
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.BERTRAND,M.FASOLINI,M.MODUGNO
REVDAT 2 21-NOV-12 4AQ3 1 SEQADV
REVDAT 1 06-JUN-12 4AQ3 0
JRNL AUTH H.L.PEREZ,P.BANFI,J.A.BERTRAND,Z.W.CAI,J.W.GREBINSKI,K.KIM,
JRNL AUTH 2 J.LIPPY,M.MODUGNO,J.NAGLICH,R.J.SCHMIDT,A.TEBBEN,P.VIANELLO,
JRNL AUTH 3 D.D.WEI,L.ZHANG,A.GALVANI,L.J.LOMBARDO,R.M.BORZILLERI
JRNL TITL IDENTIFICATION OF A PHENYLACYLSULFONAMIDE SERIES OF DUAL
JRNL TITL 2 BCL-2/BCL-XL ANTAGONISTS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 22 3946 2012
JRNL REFN ISSN 0960-894X
JRNL PMID 22608961
JRNL DOI 10.1016/J.BMCL.2012.04.103
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.75
REMARK 3 NUMBER OF REFLECTIONS : 55094
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) : 0.20300
REMARK 3 R VALUE (WORKING SET) : 0.20072
REMARK 3 FREE R VALUE : 0.24494
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2926
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.400
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.462
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3637
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.317
REMARK 3 BIN FREE R VALUE SET COUNT : 174
REMARK 3 BIN FREE R VALUE : 0.409
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6778
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 318
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.235
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.31
REMARK 3 B22 (A**2) : 0.31
REMARK 3 B33 (A**2) : -0.46
REMARK 3 B12 (A**2) : 0.15
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.255
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.216
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.161
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.963
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7311 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9916 ; 1.884 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 802 ; 6.870 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 403 ;35.705 ;22.581
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1108 ;19.747 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 72 ;22.373 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 952 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5854 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 10 A 30 4
REMARK 3 1 B 10 B 30 4
REMARK 3 1 C 10 C 30 4
REMARK 3 1 D 10 D 30 4
REMARK 3 1 E 10 E 30 4
REMARK 3 1 F 10 F 30 4
REMARK 3 2 A 52 A 157 4
REMARK 3 2 B 52 B 157 4
REMARK 3 2 C 52 C 157 4
REMARK 3 2 D 52 D 157 4
REMARK 3 2 E 52 E 157 4
REMARK 3 2 F 52 F 157 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1059 ; 0.32 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 1059 ; 0.27 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 1059 ; 0.35 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 1059 ; 0.32 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 E (A): 1059 ; 0.34 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 F (A): 1059 ; 0.34 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1059 ; 5.65 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1059 ; 4.56 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 1059 ; 5.89 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 1059 ; 5.63 ; 2.00
REMARK 3 MEDIUM THERMAL 1 E (A**2): 1059 ; 6.70 ; 2.00
REMARK 3 MEDIUM THERMAL 1 F (A**2): 1059 ; 6.01 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -2 A 166
REMARK 3 ORIGIN FOR THE GROUP (A): -13.8902 14.2160 -10.2099
REMARK 3 T TENSOR
REMARK 3 T11: 0.0879 T22: 0.0672
REMARK 3 T33: 0.0304 T12: 0.0178
REMARK 3 T13: 0.0018 T23: -0.0228
REMARK 3 L TENSOR
REMARK 3 L11: 2.2077 L22: 1.5279
REMARK 3 L33: 1.2490 L12: -0.2539
REMARK 3 L13: 0.5596 L23: 0.1709
REMARK 3 S TENSOR
REMARK 3 S11: -0.0469 S12: -0.0035 S13: 0.1670
REMARK 3 S21: -0.0266 S22: -0.0463 S23: 0.0156
REMARK 3 S31: -0.0903 S32: 0.0446 S33: 0.0932
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -2 B 166
REMARK 3 ORIGIN FOR THE GROUP (A): -42.2120 17.9809 -44.6444
REMARK 3 T TENSOR
REMARK 3 T11: 0.0952 T22: 0.0497
REMARK 3 T33: 0.0425 T12: 0.0392
REMARK 3 T13: 0.0241 T23: 0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 2.1553 L22: 1.3696
REMARK 3 L33: 1.4854 L12: -0.5062
REMARK 3 L13: -0.3255 L23: 0.4285
REMARK 3 S TENSOR
REMARK 3 S11: -0.0857 S12: 0.0387 S13: -0.0572
REMARK 3 S21: 0.1530 S22: 0.0795 S23: -0.0099
REMARK 3 S31: 0.0978 S32: 0.0241 S33: 0.0062
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C -2 C 166
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4064 -21.1416 -11.6370
REMARK 3 T TENSOR
REMARK 3 T11: 0.0892 T22: 0.0697
REMARK 3 T33: 0.0204 T12: -0.0171
REMARK 3 T13: 0.0052 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.6481 L22: 3.1235
REMARK 3 L33: 1.5524 L12: 0.0372
REMARK 3 L13: -0.0388 L23: 0.5744
REMARK 3 S TENSOR
REMARK 3 S11: 0.1068 S12: 0.0135 S13: -0.0601
REMARK 3 S21: -0.0108 S22: -0.1555 S23: 0.1084
REMARK 3 S31: 0.0810 S32: -0.1644 S33: 0.0487
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D -2 D 166
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3502 16.4464 -44.0337
REMARK 3 T TENSOR
REMARK 3 T11: 0.0482 T22: 0.0678
REMARK 3 T33: 0.1338 T12: -0.0170
REMARK 3 T13: -0.0565 T23: 0.0405
REMARK 3 L TENSOR
REMARK 3 L11: 3.3229 L22: 1.5146
REMARK 3 L33: 2.2469 L12: -1.5719
REMARK 3 L13: 0.5386 L23: -0.0427
REMARK 3 S TENSOR
REMARK 3 S11: -0.1976 S12: 0.3195 S13: 0.3311
REMARK 3 S21: 0.0809 S22: -0.0081 S23: 0.0013
REMARK 3 S31: -0.1798 S32: 0.1513 S33: 0.2057
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E -2 E 166
REMARK 3 ORIGIN FOR THE GROUP (A): -45.9430 15.6412 -9.4843
REMARK 3 T TENSOR
REMARK 3 T11: 0.0503 T22: 0.0458
REMARK 3 T33: 0.0997 T12: 0.0004
REMARK 3 T13: 0.0182 T23: 0.0426
REMARK 3 L TENSOR
REMARK 3 L11: 4.7431 L22: 1.7409
REMARK 3 L33: 1.5761 L12: -1.4547
REMARK 3 L13: -0.6513 L23: 0.5865
REMARK 3 S TENSOR
REMARK 3 S11: -0.2777 S12: 0.1166 S13: -0.3711
REMARK 3 S21: -0.0197 S22: 0.1402 S23: 0.3679
REMARK 3 S31: 0.0917 S32: 0.0948 S33: 0.1375
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F -2 F 166
REMARK 3 ORIGIN FOR THE GROUP (A): -50.3924 50.2935 -8.9127
REMARK 3 T TENSOR
REMARK 3 T11: 0.0554 T22: 0.0534
REMARK 3 T33: 0.0843 T12: -0.0098
REMARK 3 T13: -0.0019 T23: 0.0471
REMARK 3 L TENSOR
REMARK 3 L11: 1.5204 L22: 2.2972
REMARK 3 L33: 1.2614 L12: -0.6744
REMARK 3 L13: 0.5222 L23: 0.1825
REMARK 3 S TENSOR
REMARK 3 S11: 0.1009 S12: 0.1569 S13: 0.1134
REMARK 3 S21: -0.1511 S22: -0.1342 S23: -0.1282
REMARK 3 S31: -0.0221 S32: 0.1521 S33: 0.0333
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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 4AQ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-APR-12.
REMARK 100 THE PDBE ID CODE IS EBI-52041.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-10
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 : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.07200
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 315)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58071
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40
REMARK 200 RESOLUTION RANGE LOW (A) : 40.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.4
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.7
REMARK 200 R MERGE FOR SHELL (I) : 0.58
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.80
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: INTERNAL STRUCTURE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.21200
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 34.10600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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: 3
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
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 ALA A 32
REMARK 465 GLY A 33
REMARK 465 ASP A 34
REMARK 465 ASP A 35
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 GLU A 48
REMARK 465 SER A 49
REMARK 465 GLU A 50
REMARK 465 PRO A 163
REMARK 465 SER A 164
REMARK 465 MET A 165
REMARK 465 ARG A 166
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 HIS B 3
REMARK 465 ALA B 4
REMARK 465 GLY B 5
REMARK 465 ARG B 6
REMARK 465 THR B 7
REMARK 465 GLY B 8
REMARK 465 ALA B 32
REMARK 465 GLY B 33
REMARK 465 ASP B 34
REMARK 465 ASP B 35
REMARK 465 VAL B 36
REMARK 465 GLU B 37
REMARK 465 GLU B 38
REMARK 465 ASN B 39
REMARK 465 ARG B 40
REMARK 465 THR B 41
REMARK 465 GLU B 42
REMARK 465 ALA B 43
REMARK 465 PRO B 44
REMARK 465 GLU B 45
REMARK 465 GLY B 46
REMARK 465 THR B 47
REMARK 465 GLU B 48
REMARK 465 SER B 49
REMARK 465 GLU B 50
REMARK 465 PRO B 163
REMARK 465 SER B 164
REMARK 465 MET B 165
REMARK 465 ARG B 166
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
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 GLY C 8
REMARK 465 ALA C 32
REMARK 465 GLY C 33
REMARK 465 ASP C 34
REMARK 465 ASP C 35
REMARK 465 VAL C 36
REMARK 465 GLU C 37
REMARK 465 GLU C 38
REMARK 465 ASN C 39
REMARK 465 ARG C 40
REMARK 465 THR C 41
REMARK 465 GLU C 42
REMARK 465 ALA C 43
REMARK 465 PRO C 44
REMARK 465 GLU C 45
REMARK 465 GLY C 46
REMARK 465 THR C 47
REMARK 465 GLU C 48
REMARK 465 SER C 49
REMARK 465 GLU C 50
REMARK 465 PRO C 163
REMARK 465 SER C 164
REMARK 465 MET C 165
REMARK 465 ARG C 166
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 HIS D 3
REMARK 465 ALA D 4
REMARK 465 GLY D 5
REMARK 465 ARG D 6
REMARK 465 THR D 7
REMARK 465 GLY D 8
REMARK 465 ALA D 32
REMARK 465 GLY D 33
REMARK 465 ASP D 34
REMARK 465 ASP D 35
REMARK 465 VAL D 36
REMARK 465 GLU D 37
REMARK 465 GLU D 38
REMARK 465 ASN D 39
REMARK 465 ARG D 40
REMARK 465 THR D 41
REMARK 465 GLU D 42
REMARK 465 ALA D 43
REMARK 465 PRO D 44
REMARK 465 GLU D 45
REMARK 465 GLY D 46
REMARK 465 THR D 47
REMARK 465 GLU D 48
REMARK 465 PRO D 163
REMARK 465 SER D 164
REMARK 465 MET D 165
REMARK 465 ARG D 166
REMARK 465 GLY E -2
REMARK 465 SER E -1
REMARK 465 HIS E 0
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 HIS E 3
REMARK 465 ALA E 4
REMARK 465 GLY E 5
REMARK 465 ARG E 6
REMARK 465 THR E 7
REMARK 465 GLY E 8
REMARK 465 TYR E 9
REMARK 465 GLY E 33
REMARK 465 ASP E 34
REMARK 465 ASP E 35
REMARK 465 VAL E 36
REMARK 465 GLU E 37
REMARK 465 GLU E 38
REMARK 465 ASN E 39
REMARK 465 ARG E 40
REMARK 465 THR E 41
REMARK 465 GLU E 42
REMARK 465 ALA E 43
REMARK 465 PRO E 44
REMARK 465 GLU E 45
REMARK 465 GLY E 46
REMARK 465 THR E 47
REMARK 465 GLU E 48
REMARK 465 SER E 49
REMARK 465 GLU E 50
REMARK 465 PRO E 163
REMARK 465 SER E 164
REMARK 465 MET E 165
REMARK 465 ARG E 166
REMARK 465 GLY F -2
REMARK 465 SER F -1
REMARK 465 HIS F 0
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 HIS F 3
REMARK 465 ALA F 4
REMARK 465 GLY F 5
REMARK 465 ARG F 6
REMARK 465 THR F 7
REMARK 465 GLY F 8
REMARK 465 GLY F 33
REMARK 465 ASP F 34
REMARK 465 ASP F 35
REMARK 465 VAL F 36
REMARK 465 GLU F 37
REMARK 465 GLU F 38
REMARK 465 ASN F 39
REMARK 465 ARG F 40
REMARK 465 THR F 41
REMARK 465 GLU F 42
REMARK 465 ALA F 43
REMARK 465 PRO F 44
REMARK 465 GLU F 45
REMARK 465 GLY F 46
REMARK 465 THR F 47
REMARK 465 GLU F 48
REMARK 465 SER F 49
REMARK 465 PRO F 163
REMARK 465 SER F 164
REMARK 465 MET F 165
REMARK 465 ARG F 166
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 OH TYR A 18 OE2 GLU A 111 2.13
REMARK 500 OE1 GLU A 94 NH2 ARG A 98 2.17
REMARK 500 OH TYR C 9 OD1 ASP C 155 2.09
REMARK 500 OH TYR C 18 OE2 GLU C 111 1.94
REMARK 500 OH TYR D 18 OE2 GLU D 111 2.18
REMARK 500 OH TYR E 18 OE2 GLU E 111 2.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 147 CD2 TRP A 147 CE2 0.073
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 C 66 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP D 61 CB - CG - OD1 ANGL. DEV. = 5.7 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 GLU A 159 27.14 -66.75
REMARK 500 LEU A 160 -63.50 -121.11
REMARK 500 GLN B 25 -42.56 -27.51
REMARK 500 GLN C 25 -38.39 -33.03
REMARK 500 GLU D 50 -47.94 68.94
REMARK 500 TYR D 161 -164.24 103.64
REMARK 500 HIS E 79 71.18 36.33
REMARK 500 ASP F 31 89.14 -63.24
REMARK 500 ASP F 99 24.38 -79.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR D 9 ASP D 10 143.78
REMARK 500 TYR F 9 ASP F 10 -144.50
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 398 A1163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 398 B1163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 398 C1163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 398 D1163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 398 E1163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 398 F1163
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BXL RELATED DB: PDB
REMARK 900 STRUCTURE OF BCL-XL/BAK PEPTIDE COMPLEX, NMR,
REMARK 900 MINIMIZED AVERAGE STRUCTURE
REMARK 900 RELATED ID: 1G5J RELATED DB: PDB
REMARK 900 COMPLEX OF BCL-XL WITH PEPTIDE FROM BAD
REMARK 900 RELATED ID: 1G5M RELATED DB: PDB
REMARK 900 HUMAN BCL-2, ISOFORM 1
REMARK 900 RELATED ID: 1GJH RELATED DB: PDB
REMARK 900 HUMAN BCL-2, ISOFORM 2
REMARK 900 RELATED ID: 1LXL RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF BCL-XL, AN INHIBITOR OF PROGRAMMED
REMARK 900 CELL DEATH, MINIMIZED AVERAGE STRUCTURE
REMARK 900 RELATED ID: 1MAZ RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF BCL-XL, AN INHIBITOR OF
REMARK 900 PROGRAMMED CELL DEATH
REMARK 900 RELATED ID: 1R2D RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN BCL-XL AT 1.95 ANGSTROMS
REMARK 900 RELATED ID: 1R2E RELATED DB: PDB
REMARK 900 HUMAN BCL-XL CONTAINING A GLU TO LEU MUTATION AT
REMARK 900 POSITION 92
REMARK 900 RELATED ID: 1R2G RELATED DB: PDB
REMARK 900 HUMAN BCL-XL CONTAINING A PHE TO TRP MUTATION AT
REMARK 900 POSITION 97
REMARK 900 RELATED ID: 1R2H RELATED DB: PDB
REMARK 900 HUMAN BCL-XL CONTAINING AN ALA TO LEU MUTATION AT
REMARK 900 POSITION142
REMARK 900 RELATED ID: 1R2I RELATED DB: PDB
REMARK 900 HUMAN BCL-XL CONTAINING A PHE TO LEU MUTATION AT
REMARK 900 POSITION146
REMARK 900 RELATED ID: 1YSG RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE ANTI-APOPTOTIC PROTEIN BCL-
REMARK 900 XL INCOMPLEX WITH "SAR BY NMR" LIGANDS
REMARK 900 RELATED ID: 1YSI RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE ANTI-APOPTOTIC PROTEIN BCL-
REMARK 900 XL INCOMPLEX WITH AN ACYL-SULFONAMIDE-BASED LIGAND
REMARK 900 RELATED ID: 1YSN RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE ANTI-APOPTOTIC PROTEIN BCL-
REMARK 900 XLCOMPLEXED WITH AN ACYL-SULFONAMIDE-BASED LIGAND
REMARK 900 RELATED ID: 1YSW RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE ANTI-APOPTOTIC PROTEIN BCL-
REMARK 900 2COMPLEXED WITH AN ACYL-SULFONAMIDE-BASED LIGAND
REMARK 900 RELATED ID: 2B48 RELATED DB: PDB
REMARK 900 BCL-XL 3D DOMAIN SWAPPED DIMER
REMARK 900 RELATED ID: 2W3L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHIMAERIC BCL2-XL AND PHENYL
REMARK 900 TETRAHYDROISOQUINOLINE AMIDE COMPLEX
REMARK 900 RELATED ID: 2XA0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BCL-2 IN COMPLEX WITH A BAX
REMARK 900 BH3 PEPTIDE
REMARK 900 RELATED ID: 2YJ1 RELATED DB: PDB
REMARK 900 PUMA BH3 FOLDAMER IN COMPLEX WITH BCL-XL
REMARK 900 RELATED ID: 4A1U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ALPHA-BETA-FOLDAMER 2C IN COMPLEX
REMARK 900 WITH BCL-XL
REMARK 900 RELATED ID: 4A1W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ALPHA-BETA FOLDAMER 4C IN COMPLEX
REMARK 900 WITH BCL-XL
DBREF 4AQ3 A 1 33 UNP P10415 BCL2_HUMAN 1 33
DBREF 4AQ3 A 35 50 UNP Q07817 BCLX_HUMAN 29 44
DBREF 4AQ3 A 51 166 UNP P10415 BCL2_HUMAN 92 207
DBREF 4AQ3 B 1 33 UNP P10415 BCL2_HUMAN 1 33
DBREF 4AQ3 B 35 50 UNP Q07817 BCLX_HUMAN 29 44
DBREF 4AQ3 B 51 166 UNP P10415 BCL2_HUMAN 92 207
DBREF 4AQ3 C 1 33 UNP P10415 BCL2_HUMAN 1 33
DBREF 4AQ3 C 35 50 UNP Q07817 BCLX_HUMAN 29 44
DBREF 4AQ3 C 51 166 UNP P10415 BCL2_HUMAN 92 207
DBREF 4AQ3 D 1 33 UNP P10415 BCL2_HUMAN 1 33
DBREF 4AQ3 D 35 50 UNP Q07817 BCLX_HUMAN 29 44
DBREF 4AQ3 D 51 166 UNP P10415 BCL2_HUMAN 92 207
DBREF 4AQ3 E 1 33 UNP P10415 BCL2_HUMAN 1 33
DBREF 4AQ3 E 35 50 UNP Q07817 BCLX_HUMAN 29 44
DBREF 4AQ3 E 51 166 UNP P10415 BCL2_HUMAN 92 207
DBREF 4AQ3 F 1 33 UNP P10415 BCL2_HUMAN 1 33
DBREF 4AQ3 F 35 50 UNP Q07817 BCLX_HUMAN 29 44
DBREF 4AQ3 F 51 166 UNP P10415 BCL2_HUMAN 92 207
SEQADV 4AQ3 GLY A -2 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 SER A -1 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 HIS A 0 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 ASP A 34 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 ALA A 55 UNP P10415 THR 96 VARIANT
SEQADV 4AQ3 GLY A 69 UNP P10415 ARG 110 VARIANT
SEQADV 4AQ3 GLY B -2 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 SER B -1 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 HIS B 0 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 ASP B 34 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 ALA B 55 UNP P10415 THR 96 VARIANT
SEQADV 4AQ3 GLY B 69 UNP P10415 ARG 110 VARIANT
SEQADV 4AQ3 GLY C -2 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 SER C -1 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 HIS C 0 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 ASP C 34 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 ALA C 55 UNP P10415 THR 96 VARIANT
SEQADV 4AQ3 GLY C 69 UNP P10415 ARG 110 VARIANT
SEQADV 4AQ3 GLY D -2 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 SER D -1 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 HIS D 0 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 ASP D 34 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 ALA D 55 UNP P10415 THR 96 VARIANT
SEQADV 4AQ3 GLY D 69 UNP P10415 ARG 110 VARIANT
SEQADV 4AQ3 GLY E -2 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 SER E -1 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 HIS E 0 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 ASP E 34 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 ALA E 55 UNP P10415 THR 96 VARIANT
SEQADV 4AQ3 GLY E 69 UNP P10415 ARG 110 VARIANT
SEQADV 4AQ3 GLY F -2 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 SER F -1 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 HIS F 0 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 ASP F 34 UNP P10415 EXPRESSION TAG
SEQADV 4AQ3 ALA F 55 UNP P10415 THR 96 VARIANT
SEQADV 4AQ3 GLY F 69 UNP P10415 ARG 110 VARIANT
SEQRES 1 A 169 GLY SER HIS MET ALA HIS ALA GLY ARG THR GLY TYR ASP
SEQRES 2 A 169 ASN ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU
SEQRES 3 A 169 SER GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL
SEQRES 4 A 169 GLU GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER
SEQRES 5 A 169 GLU VAL VAL HIS LEU ALA LEU ARG GLN ALA GLY ASP ASP
SEQRES 6 A 169 PHE SER ARG ARG TYR ARG GLY ASP PHE ALA GLU MET SER
SEQRES 7 A 169 SER GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG
SEQRES 8 A 169 PHE ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL
SEQRES 9 A 169 ASN TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY
SEQRES 10 A 169 VAL MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO
SEQRES 11 A 169 LEU VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU
SEQRES 12 A 169 ASN ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY
SEQRES 13 A 169 TRP ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG
SEQRES 1 B 169 GLY SER HIS MET ALA HIS ALA GLY ARG THR GLY TYR ASP
SEQRES 2 B 169 ASN ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU
SEQRES 3 B 169 SER GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL
SEQRES 4 B 169 GLU GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER
SEQRES 5 B 169 GLU VAL VAL HIS LEU ALA LEU ARG GLN ALA GLY ASP ASP
SEQRES 6 B 169 PHE SER ARG ARG TYR ARG GLY ASP PHE ALA GLU MET SER
SEQRES 7 B 169 SER GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG
SEQRES 8 B 169 PHE ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL
SEQRES 9 B 169 ASN TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY
SEQRES 10 B 169 VAL MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO
SEQRES 11 B 169 LEU VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU
SEQRES 12 B 169 ASN ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY
SEQRES 13 B 169 TRP ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG
SEQRES 1 C 169 GLY SER HIS MET ALA HIS ALA GLY ARG THR GLY TYR ASP
SEQRES 2 C 169 ASN ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU
SEQRES 3 C 169 SER GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL
SEQRES 4 C 169 GLU GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER
SEQRES 5 C 169 GLU VAL VAL HIS LEU ALA LEU ARG GLN ALA GLY ASP ASP
SEQRES 6 C 169 PHE SER ARG ARG TYR ARG GLY ASP PHE ALA GLU MET SER
SEQRES 7 C 169 SER GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG
SEQRES 8 C 169 PHE ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL
SEQRES 9 C 169 ASN TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY
SEQRES 10 C 169 VAL MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO
SEQRES 11 C 169 LEU VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU
SEQRES 12 C 169 ASN ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY
SEQRES 13 C 169 TRP ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG
SEQRES 1 D 169 GLY SER HIS MET ALA HIS ALA GLY ARG THR GLY TYR ASP
SEQRES 2 D 169 ASN ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU
SEQRES 3 D 169 SER GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL
SEQRES 4 D 169 GLU GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER
SEQRES 5 D 169 GLU VAL VAL HIS LEU ALA LEU ARG GLN ALA GLY ASP ASP
SEQRES 6 D 169 PHE SER ARG ARG TYR ARG GLY ASP PHE ALA GLU MET SER
SEQRES 7 D 169 SER GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG
SEQRES 8 D 169 PHE ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL
SEQRES 9 D 169 ASN TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY
SEQRES 10 D 169 VAL MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO
SEQRES 11 D 169 LEU VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU
SEQRES 12 D 169 ASN ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY
SEQRES 13 D 169 TRP ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG
SEQRES 1 E 169 GLY SER HIS MET ALA HIS ALA GLY ARG THR GLY TYR ASP
SEQRES 2 E 169 ASN ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU
SEQRES 3 E 169 SER GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL
SEQRES 4 E 169 GLU GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER
SEQRES 5 E 169 GLU VAL VAL HIS LEU ALA LEU ARG GLN ALA GLY ASP ASP
SEQRES 6 E 169 PHE SER ARG ARG TYR ARG GLY ASP PHE ALA GLU MET SER
SEQRES 7 E 169 SER GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG
SEQRES 8 E 169 PHE ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL
SEQRES 9 E 169 ASN TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY
SEQRES 10 E 169 VAL MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO
SEQRES 11 E 169 LEU VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU
SEQRES 12 E 169 ASN ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY
SEQRES 13 E 169 TRP ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG
SEQRES 1 F 169 GLY SER HIS MET ALA HIS ALA GLY ARG THR GLY TYR ASP
SEQRES 2 F 169 ASN ARG GLU ILE VAL MET LYS TYR ILE HIS TYR LYS LEU
SEQRES 3 F 169 SER GLN ARG GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL
SEQRES 4 F 169 GLU GLU ASN ARG THR GLU ALA PRO GLU GLY THR GLU SER
SEQRES 5 F 169 GLU VAL VAL HIS LEU ALA LEU ARG GLN ALA GLY ASP ASP
SEQRES 6 F 169 PHE SER ARG ARG TYR ARG GLY ASP PHE ALA GLU MET SER
SEQRES 7 F 169 SER GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG
SEQRES 8 F 169 PHE ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL
SEQRES 9 F 169 ASN TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY
SEQRES 10 F 169 VAL MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO
SEQRES 11 F 169 LEU VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU
SEQRES 12 F 169 ASN ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY
SEQRES 13 F 169 TRP ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG
HET 398 A1163 53
HET 398 B1163 53
HET 398 C1163 53
HET 398 D1163 53
HET 398 E1163 53
HET 398 F1163 53
HETNAM 398 N,N-DIBUTYL-4-CHLORANYL-1-[2-(3,4-DIHYDRO-1H-
HETNAM 2 398 ISOQUINOLIN-2-YLCARBONYL)-4-[(7-
HETNAM 3 398 IODANYLNAPHTHALEN-2-YL)SULFONYLCARBAMOYL]PHENYL]-5-METHYL-
HETNAM 4 398 PYRAZOLE-3-CARBOXAMIDE
FORMUL 7 398 6(C40 H41 CL I N5 O5 S)
HELIX 1 1 ASP A 10 ARG A 26 1 17
HELIX 2 2 VAL A 51 TYR A 67 1 17
HELIX 3 3 TYR A 67 LEU A 78 1 12
HELIX 4 4 THR A 84 PHE A 97 1 14
HELIX 5 5 ASN A 102 ARG A 123 1 22
HELIX 6 6 PRO A 127 LEU A 144 1 18
HELIX 7 7 LEU A 144 ASN A 151 1 8
HELIX 8 8 GLY A 152 GLU A 159 1 8
HELIX 9 9 ASP B 10 ARG B 26 1 17
HELIX 10 10 VAL B 51 TYR B 67 1 17
HELIX 11 11 TYR B 67 LEU B 78 1 12
HELIX 12 12 THR B 84 PHE B 97 1 14
HELIX 13 13 ASN B 102 ARG B 123 1 22
HELIX 14 14 PRO B 127 HIS B 143 1 17
HELIX 15 15 LEU B 144 ASN B 151 1 8
HELIX 16 16 GLY B 152 GLY B 162 1 11
HELIX 17 17 ASP C 10 ARG C 26 1 17
HELIX 18 18 VAL C 51 TYR C 67 1 17
HELIX 19 19 TYR C 67 LEU C 78 1 12
HELIX 20 20 THR C 84 ARG C 98 1 15
HELIX 21 21 ASN C 102 ARG C 123 1 22
HELIX 22 22 PRO C 127 LEU C 144 1 18
HELIX 23 23 LEU C 144 ASN C 151 1 8
HELIX 24 24 GLY C 153 GLY C 162 1 10
HELIX 25 25 ASP D 10 GLN D 25 1 16
HELIX 26 26 GLU D 50 TYR D 67 1 18
HELIX 27 27 TYR D 67 GLN D 77 1 11
HELIX 28 28 THR D 84 PHE D 97 1 14
HELIX 29 29 ASN D 102 ARG D 123 1 22
HELIX 30 30 PRO D 127 LEU D 144 1 18
HELIX 31 31 LEU D 144 ASN D 151 1 8
HELIX 32 32 GLY D 152 LEU D 160 1 9
HELIX 33 33 ASP E 10 ARG E 26 1 17
HELIX 34 34 VAL E 51 TYR E 67 1 17
HELIX 35 35 TYR E 67 GLN E 77 1 11
HELIX 36 36 THR E 84 ARG E 98 1 15
HELIX 37 37 ASN E 102 ARG E 123 1 22
HELIX 38 38 SER E 126 LEU E 144 1 19
HELIX 39 39 LEU E 144 ASN E 151 1 8
HELIX 40 40 GLY E 152 GLY E 162 1 11
HELIX 41 41 ASP F 10 GLN F 25 1 16
HELIX 42 42 GLU F 50 TYR F 67 1 18
HELIX 43 43 TYR F 67 SER F 76 1 10
HELIX 44 44 THR F 84 PHE F 97 1 14
HELIX 45 45 ASN F 102 ARG F 123 1 22
HELIX 46 46 PRO F 127 LEU F 144 1 18
HELIX 47 47 LEU F 144 ASN F 151 1 8
HELIX 48 48 GLY F 152 GLY F 162 1 11
CISPEP 1 TYR F 161 GLY F 162 0 -29.13
SITE 1 AC1 10 TYR A 67 ASP A 70 MET A 74 GLU A 95
SITE 2 AC1 10 LEU A 96 ARG A 105 GLN E 58 LEU E 160
SITE 3 AC1 10 TYR E 161 GLY E 162
SITE 1 AC2 15 PHE B 63 TYR B 67 ASP B 70 PHE B 71
SITE 2 AC2 15 MET B 74 VAL B 92 GLU B 95 GLY B 104
SITE 3 AC2 15 ALA B 108 PHE B 112 TYR B 161 GLN D 58
SITE 4 AC2 15 TYR D 161 GLY D 162 PRO E 82
SITE 1 AC3 11 PHE C 63 TYR C 67 ASP C 70 MET C 74
SITE 2 AC3 11 GLU C 95 LEU C 96 TYR C 161 PRO D 82
SITE 3 AC3 11 GLN F 58 TYR F 161 GLY F 162
SITE 1 AC4 11 PRO A 82 GLN B 58 LEU B 160 TYR B 161
SITE 2 AC4 11 GLY B 162 PHE D 63 TYR D 67 ASP D 70
SITE 3 AC4 11 MET D 74 GLU D 95 ALA D 108
SITE 1 AC5 11 GLN A 58 LEU A 160 TYR A 161 GLY A 162
SITE 2 AC5 11 PHE E 63 TYR E 67 ASP E 70 MET E 74
SITE 3 AC5 11 VAL E 92 GLU E 95 ALA E 108
SITE 1 AC6 11 PHE B 83 GLN C 58 LEU C 160 TYR C 161
SITE 2 AC6 11 GLY C 162 PHE F 63 TYR F 67 ASP F 70
SITE 3 AC6 11 VAL F 92 GLU F 95 ALA F 108
CRYST1 115.214 115.214 102.318 90.00 90.00 120.00 P 32 18
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 0.008680 0.005011 0.000000 0.00000
SCALE2 0.000000 0.010022 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009773 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.999896 -0.002574 -0.014206 -56.68136 1
MTRIX2 2 0.004890 -0.986189 -0.165554 24.74994 1
MTRIX3 2 -0.013583 -0.165606 0.986098 36.21980 1
MTRIX1 3 -0.501065 0.860651 -0.090629 -0.46102 1
MTRIX2 3 -0.833152 -0.508062 -0.218473 -5.25083 1
MTRIX3 3 -0.234074 -0.033961 0.971625 -1.35637 1
MTRIX1 4 0.998112 -0.011743 0.060290 -0.82415 1
MTRIX2 4 0.011612 0.999929 0.002517 -1.77654 1
MTRIX3 4 -0.060316 -0.001812 0.998178 33.11996 1
MTRIX1 5 -0.999594 -0.006045 0.027859 -59.37437 1
MTRIX2 5 0.002596 -0.992501 -0.122213 28.60782 1
MTRIX3 5 0.028389 -0.122091 0.992113 2.53127 1
MTRIX1 6 0.477377 -0.870284 0.121313 54.98487 1
MTRIX2 6 0.870083 0.487455 0.073092 34.36977 1
MTRIX3 6 -0.122745 0.070660 0.989920 -11.18358 1
(ATOM LINES ARE NOT SHOWN.)
END
