HEADER VIRAL PROTEIN/INHIBITOR 09-MAY-16 5JSN
TITLE BCL2-INHIBITOR COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS REGULATOR BCL-2;
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: BCL2 INHIBITOR;
COMPND 7 CHAIN: B, D;
COMPND 8 ENGINEERED: 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;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET29B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: UNIDENTIFIED;
SOURCE 12 ORGANISM_TAXID: 32644;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET29B
KEYWDS BCL-2, ANTIBCL2, COMPLEX, VIRAL PROTEIN-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.W.SHEN,B.L.STODDARD
REVDAT 2 06-MAR-24 5JSN 1 REMARK
REVDAT 1 16-NOV-16 5JSN 0
JRNL AUTH S.BERGER,E.PROCKO,D.MARGINEANTU,E.F.LEE,B.W.SHEN,A.ZELTER,
JRNL AUTH 2 D.A.SILVA,K.CHAWLA,M.J.HEROLD,J.M.GARNIER,R.JOHNSON,
JRNL AUTH 3 M.J.MACCOSS,G.LESSENE,T.N.DAVIS,P.S.STAYTON,B.L.STODDARD,
JRNL AUTH 4 W.D.FAIRLIE,D.M.HOCKENBERY,D.BAKER
JRNL TITL COMPUTATIONALLY DESIGNED HIGH SPECIFICITY INHIBITORS
JRNL TITL 2 DELINEATE THE ROLES OF BCL2 FAMILY PROTEINS IN CANCER.
JRNL REF ELIFE V. 5 2016
JRNL REFN ESSN 2050-084X
JRNL PMID 27805565
JRNL DOI 10.7554/ELIFE.20352
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 30512
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1605
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2108
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 123
REMARK 3 BIN FREE R VALUE : 0.3330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4374
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 152
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 17.56000
REMARK 3 B22 (A**2) : 17.56000
REMARK 3 B33 (A**2) : -35.11000
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): 0.044
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.036
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.107
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.627
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4470 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4316 ; 0.008 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6008 ; 2.010 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9880 ; 1.734 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 526 ; 6.454 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 247 ;34.429 ;23.036
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 838 ;18.695 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 55 ;19.549 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 630 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5034 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1097 ; 0.006 ; 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): 2113 ; 2.452 ; 3.298
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2112 ; 2.452 ; 3.298
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2633 ; 3.520 ; 4.923
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2634 ; 3.519 ; 4.923
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2357 ; 2.744 ; 3.686
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2358 ; 2.743 ; 3.686
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3375 ; 4.179 ; 5.401
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5319 ; 6.602 ;26.514
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5292 ; 6.577 ;26.393
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 2
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 7 209 C 7 209 15744 0.14 0.05
REMARK 3 2 B 3 117 D 3 117 13106 0.16 0.05
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.692
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H, K, -L
REMARK 3 TWIN FRACTION : 0.308
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 7 A 209
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5849 -5.6482 58.2767
REMARK 3 T TENSOR
REMARK 3 T11: 0.0190 T22: 0.0499
REMARK 3 T33: 0.2169 T12: -0.0117
REMARK 3 T13: -0.0235 T23: -0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 1.6993 L22: 2.9680
REMARK 3 L33: 3.8507 L12: 0.3465
REMARK 3 L13: 0.1616 L23: 0.7157
REMARK 3 S TENSOR
REMARK 3 S11: 0.0310 S12: 0.2036 S13: -0.0792
REMARK 3 S21: -0.1102 S22: -0.0159 S23: 0.1523
REMARK 3 S31: 0.1937 S32: -0.2935 S33: -0.0151
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 3 B 117
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3315 10.5232 58.8693
REMARK 3 T TENSOR
REMARK 3 T11: 0.0768 T22: 0.0309
REMARK 3 T33: 0.2508 T12: -0.0358
REMARK 3 T13: 0.0058 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 4.8921 L22: 2.2664
REMARK 3 L33: 3.6527 L12: -1.2923
REMARK 3 L13: -1.6137 L23: 0.8614
REMARK 3 S TENSOR
REMARK 3 S11: 0.2251 S12: 0.1255 S13: 0.3492
REMARK 3 S21: -0.1739 S22: -0.0076 S23: -0.2213
REMARK 3 S31: -0.2828 S32: 0.0827 S33: -0.2175
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 7 C 209
REMARK 3 ORIGIN FOR THE GROUP (A): 36.2254 37.2449 72.6643
REMARK 3 T TENSOR
REMARK 3 T11: 0.0361 T22: 0.0655
REMARK 3 T33: 0.1700 T12: -0.0134
REMARK 3 T13: 0.0429 T23: -0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 2.2028 L22: 1.9796
REMARK 3 L33: 4.3307 L12: 0.6088
REMARK 3 L13: 0.9704 L23: 0.1984
REMARK 3 S TENSOR
REMARK 3 S11: 0.0922 S12: -0.1762 S13: 0.1390
REMARK 3 S21: 0.1243 S22: -0.0236 S23: -0.0347
REMARK 3 S31: -0.1187 S32: 0.3290 S33: -0.0686
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 3 D 117
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4555 23.4038 70.2064
REMARK 3 T TENSOR
REMARK 3 T11: 0.0927 T22: 0.0455
REMARK 3 T33: 0.2138 T12: -0.0338
REMARK 3 T13: 0.0319 T23: -0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 2.9751 L22: 3.2358
REMARK 3 L33: 3.8876 L12: -0.9577
REMARK 3 L13: 1.3394 L23: -2.0137
REMARK 3 S TENSOR
REMARK 3 S11: 0.0989 S12: -0.2512 S13: -0.2689
REMARK 3 S21: 0.1059 S22: 0.0916 S23: 0.2737
REMARK 3 S31: 0.1483 S32: -0.0180 S33: -0.1905
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5JSN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221159.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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 FR-D
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 708
REMARK 200 DATA SCALING SOFTWARE : HKL-2000 708
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 32.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : 0.05000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 69.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.52800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.680
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.7
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% JEFFAMINE ED-2001, PH7.0/100 MM
REMARK 280 HEPES PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.15700
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 33.57850
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 100.73550
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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 GLY A 33
REMARK 465 ASP A 34
REMARK 465 VAL A 35
REMARK 465 GLY A 36
REMARK 465 ALA A 37
REMARK 465 ALA A 38
REMARK 465 PRO A 39
REMARK 465 PRO A 40
REMARK 465 GLY A 41
REMARK 465 ALA A 42
REMARK 465 ALA A 43
REMARK 465 PRO A 44
REMARK 465 ALA A 45
REMARK 465 PRO A 46
REMARK 465 GLY A 47
REMARK 465 ILE A 48
REMARK 465 PHE A 49
REMARK 465 SER A 50
REMARK 465 SER A 51
REMARK 465 GLN A 52
REMARK 465 PRO A 53
REMARK 465 GLY A 54
REMARK 465 HIS A 55
REMARK 465 THR A 56
REMARK 465 PRO A 57
REMARK 465 HIS A 58
REMARK 465 PRO A 59
REMARK 465 ALA A 60
REMARK 465 ALA A 61
REMARK 465 SER A 62
REMARK 465 ARG A 63
REMARK 465 ASP A 64
REMARK 465 PRO A 65
REMARK 465 VAL A 66
REMARK 465 ALA A 67
REMARK 465 ARG A 68
REMARK 465 THR A 69
REMARK 465 SER A 70
REMARK 465 PRO A 71
REMARK 465 LEU A 72
REMARK 465 GLN A 73
REMARK 465 THR A 74
REMARK 465 PRO A 75
REMARK 465 ALA A 76
REMARK 465 ALA A 77
REMARK 465 PRO A 78
REMARK 465 GLY A 79
REMARK 465 ALA A 80
REMARK 465 ALA A 81
REMARK 465 ALA A 82
REMARK 465 GLY A 83
REMARK 465 PRO A 84
REMARK 465 ALA A 85
REMARK 465 LEU A 86
REMARK 465 HIS A 210
REMARK 465 HIS A 211
REMARK 465 HIS A 212
REMARK 465 HIS A 213
REMARK 465 HIS A 214
REMARK 465 HIS A 215
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLY B 118
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 GLY C 33
REMARK 465 ASP C 34
REMARK 465 VAL C 35
REMARK 465 GLY C 36
REMARK 465 ALA C 37
REMARK 465 ALA C 38
REMARK 465 PRO C 39
REMARK 465 PRO C 40
REMARK 465 GLY C 41
REMARK 465 ALA C 42
REMARK 465 ALA C 43
REMARK 465 PRO C 44
REMARK 465 ALA C 45
REMARK 465 PRO C 46
REMARK 465 GLY C 47
REMARK 465 ILE C 48
REMARK 465 PHE C 49
REMARK 465 SER C 50
REMARK 465 SER C 51
REMARK 465 GLN C 52
REMARK 465 PRO C 53
REMARK 465 GLY C 54
REMARK 465 HIS C 55
REMARK 465 THR C 56
REMARK 465 PRO C 57
REMARK 465 HIS C 58
REMARK 465 PRO C 59
REMARK 465 ALA C 60
REMARK 465 ALA C 61
REMARK 465 SER C 62
REMARK 465 ARG C 63
REMARK 465 ASP C 64
REMARK 465 PRO C 65
REMARK 465 VAL C 66
REMARK 465 ALA C 67
REMARK 465 ARG C 68
REMARK 465 THR C 69
REMARK 465 SER C 70
REMARK 465 PRO C 71
REMARK 465 LEU C 72
REMARK 465 GLN C 73
REMARK 465 THR C 74
REMARK 465 PRO C 75
REMARK 465 ALA C 76
REMARK 465 ALA C 77
REMARK 465 PRO C 78
REMARK 465 GLY C 79
REMARK 465 ALA C 80
REMARK 465 ALA C 81
REMARK 465 ALA C 82
REMARK 465 GLY C 83
REMARK 465 PRO C 84
REMARK 465 ALA C 85
REMARK 465 LEU C 86
REMARK 465 HIS C 210
REMARK 465 HIS C 211
REMARK 465 HIS C 212
REMARK 465 HIS C 213
REMARK 465 HIS C 214
REMARK 465 HIS C 215
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 GLY D 118
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 C 344 O HOH D 223 2.15
REMARK 500 OE1 GLN B 24 NH1 ARG D 20 2.17
REMARK 500 O HOH B 203 O HOH B 210 2.19
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 TYR B 63 CB TYR B 63 CG -0.093
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 106 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 127 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 146 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 LEU A 181 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 ARG B 18 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 67 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG B 67 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 92 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 112 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG C 106 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 107 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 146 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 LEU D 38 CA - CB - CG ANGL. DEV. = 16.6 DEGREES
REMARK 500 ARG D 51 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG D 101 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG D 101 NE - CZ - NH2 ANGL. DEV. = -3.6 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 GLN A 118 42.14 -86.47
REMARK 500 GLU A 165 32.81 70.62
REMARK 500 GLN C 118 44.48 -89.12
REMARK 500 LEU D 38 49.03 -99.41
REMARK 500 LEU D 115 -70.31 -61.40
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 ASP B 37 LEU B 38 -149.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JSB RELATED DB: PDB
REMARK 900 RELATED ID: 4OYD RELATED DB: PDB
DBREF 5JSN A 1 207 UNP P10415 BCL2_HUMAN 1 207
DBREF 5JSN B 1 118 PDB 5JSN 5JSN 1 118
DBREF 5JSN C 1 207 UNP P10415 BCL2_HUMAN 1 207
DBREF 5JSN D 1 118 PDB 5JSN 5JSN 1 118
SEQADV 5JSN LEU A 208 UNP P10415 EXPRESSION TAG
SEQADV 5JSN GLU A 209 UNP P10415 EXPRESSION TAG
SEQADV 5JSN HIS A 210 UNP P10415 EXPRESSION TAG
SEQADV 5JSN HIS A 211 UNP P10415 EXPRESSION TAG
SEQADV 5JSN HIS A 212 UNP P10415 EXPRESSION TAG
SEQADV 5JSN HIS A 213 UNP P10415 EXPRESSION TAG
SEQADV 5JSN HIS A 214 UNP P10415 EXPRESSION TAG
SEQADV 5JSN HIS A 215 UNP P10415 EXPRESSION TAG
SEQADV 5JSN LEU C 208 UNP P10415 EXPRESSION TAG
SEQADV 5JSN GLU C 209 UNP P10415 EXPRESSION TAG
SEQADV 5JSN HIS C 210 UNP P10415 EXPRESSION TAG
SEQADV 5JSN HIS C 211 UNP P10415 EXPRESSION TAG
SEQADV 5JSN HIS C 212 UNP P10415 EXPRESSION TAG
SEQADV 5JSN HIS C 213 UNP P10415 EXPRESSION TAG
SEQADV 5JSN HIS C 214 UNP P10415 EXPRESSION TAG
SEQADV 5JSN HIS C 215 UNP P10415 EXPRESSION TAG
SEQRES 1 A 215 MET ALA HIS ALA GLY ARG THR GLY TYR ASP ASN ARG GLU
SEQRES 2 A 215 ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER GLN ARG
SEQRES 3 A 215 GLY TYR GLU TRP ASP ALA GLY ASP VAL GLY ALA ALA PRO
SEQRES 4 A 215 PRO GLY ALA ALA PRO ALA PRO GLY ILE PHE SER SER GLN
SEQRES 5 A 215 PRO GLY HIS THR PRO HIS PRO ALA ALA SER ARG ASP PRO
SEQRES 6 A 215 VAL ALA ARG THR SER PRO LEU GLN THR PRO ALA ALA PRO
SEQRES 7 A 215 GLY ALA ALA ALA GLY PRO ALA LEU SER PRO VAL PRO PRO
SEQRES 8 A 215 VAL VAL HIS LEU THR LEU ARG GLN ALA GLY ASP ASP PHE
SEQRES 9 A 215 SER ARG ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER
SEQRES 10 A 215 GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE
SEQRES 11 A 215 ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN
SEQRES 12 A 215 TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL
SEQRES 13 A 215 MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU
SEQRES 14 A 215 VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN
SEQRES 15 A 215 ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP
SEQRES 16 A 215 ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG LEU
SEQRES 17 A 215 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 118 MET ALA ASP PRO LYS LYS VAL LEU ASP LYS ALA LYS ASP
SEQRES 2 B 118 GLU ALA GLU ASN ARG VAL ARG GLU LEU LYS GLN ARG LEU
SEQRES 3 B 118 GLU GLU LEU TYR LYS GLU ALA ARG LYS LEU ASP LEU THR
SEQRES 4 B 118 GLN GLU MET ARG GLN GLU LEU VAL ASP LYS ALA ARG ALA
SEQRES 5 B 118 ALA SER LEU GLN ALA ASN GLY ASP ILE PHE TYR ALA ILE
SEQRES 6 B 118 LEU ARG ALA LEU ALA GLU ALA GLU LYS LEU LYS LYS ALA
SEQRES 7 B 118 GLY LEU VAL ASN SER GLN GLN LEU ASP GLU LEU LYS ARG
SEQRES 8 B 118 ARG LEU GLU GLU LEU ALA GLU GLU ALA ARG ARG LYS ALA
SEQRES 9 B 118 GLU LYS LEU ARG ASP GLU PHE ARG LEU LYS LEU GLU TYR
SEQRES 10 B 118 GLY
SEQRES 1 C 215 MET ALA HIS ALA GLY ARG THR GLY TYR ASP ASN ARG GLU
SEQRES 2 C 215 ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER GLN ARG
SEQRES 3 C 215 GLY TYR GLU TRP ASP ALA GLY ASP VAL GLY ALA ALA PRO
SEQRES 4 C 215 PRO GLY ALA ALA PRO ALA PRO GLY ILE PHE SER SER GLN
SEQRES 5 C 215 PRO GLY HIS THR PRO HIS PRO ALA ALA SER ARG ASP PRO
SEQRES 6 C 215 VAL ALA ARG THR SER PRO LEU GLN THR PRO ALA ALA PRO
SEQRES 7 C 215 GLY ALA ALA ALA GLY PRO ALA LEU SER PRO VAL PRO PRO
SEQRES 8 C 215 VAL VAL HIS LEU THR LEU ARG GLN ALA GLY ASP ASP PHE
SEQRES 9 C 215 SER ARG ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER
SEQRES 10 C 215 GLN LEU HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE
SEQRES 11 C 215 ALA THR VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN
SEQRES 12 C 215 TRP GLY ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL
SEQRES 13 C 215 MET CYS VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU
SEQRES 14 C 215 VAL ASP ASN ILE ALA LEU TRP MET THR GLU TYR LEU ASN
SEQRES 15 C 215 ARG HIS LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP
SEQRES 16 C 215 ASP ALA PHE VAL GLU LEU TYR GLY PRO SER MET ARG LEU
SEQRES 17 C 215 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 118 MET ALA ASP PRO LYS LYS VAL LEU ASP LYS ALA LYS ASP
SEQRES 2 D 118 GLU ALA GLU ASN ARG VAL ARG GLU LEU LYS GLN ARG LEU
SEQRES 3 D 118 GLU GLU LEU TYR LYS GLU ALA ARG LYS LEU ASP LEU THR
SEQRES 4 D 118 GLN GLU MET ARG GLN GLU LEU VAL ASP LYS ALA ARG ALA
SEQRES 5 D 118 ALA SER LEU GLN ALA ASN GLY ASP ILE PHE TYR ALA ILE
SEQRES 6 D 118 LEU ARG ALA LEU ALA GLU ALA GLU LYS LEU LYS LYS ALA
SEQRES 7 D 118 GLY LEU VAL ASN SER GLN GLN LEU ASP GLU LEU LYS ARG
SEQRES 8 D 118 ARG LEU GLU GLU LEU ALA GLU GLU ALA ARG ARG LYS ALA
SEQRES 9 D 118 GLU LYS LEU ARG ASP GLU PHE ARG LEU LYS LEU GLU TYR
SEQRES 10 D 118 GLY
FORMUL 5 HOH *152(H2 O)
HELIX 1 AA1 ASP A 10 GLN A 25 1 16
HELIX 2 AA2 PRO A 90 GLN A 118 1 29
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 PRO 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 207 1 15
HELIX 8 AA8 LEU A 208 GLU A 209 5 2
HELIX 9 AA9 ASP B 3 ASP B 3 5 1
HELIX 10 AB1 PRO B 4 LYS B 35 1 32
HELIX 11 AB2 THR B 39 ALA B 78 1 40
HELIX 12 AB3 ASN B 82 TYR B 117 1 36
HELIX 13 AB4 ASP C 10 GLN C 25 1 16
HELIX 14 AB5 PRO C 90 TYR C 108 1 19
HELIX 15 AB6 TYR C 108 GLN C 118 1 11
HELIX 16 AB7 PHE C 124 PHE C 138 1 15
HELIX 17 AB8 ASN C 143 ARG C 164 1 22
HELIX 18 AB9 PRO C 168 LEU C 185 1 18
HELIX 19 AC1 LEU C 185 ASN C 192 1 8
HELIX 20 AC2 GLY C 193 ARG C 207 1 15
HELIX 21 AC3 PRO D 4 LYS D 35 1 32
HELIX 22 AC4 THR D 39 ALA D 78 1 40
HELIX 23 AC5 ASN D 82 TYR D 117 1 36
CRYST1 65.005 65.005 134.314 90.00 90.00 90.00 P 41 8
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 0.015383 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015383 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007445 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
