HEADER APOPTOSIS 04-FEB-15 5AGX
TITLE BCL-2 ALPHA BETA-1 LINEAR COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS REGULATOR BCL-2, BCL-2-LIKE PROTEIN 1,
COMPND 3 APOPTOSIS REGULATOR BCL-2;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: RESIDUES 1-34,29-44,92-207;
COMPND 6 SYNONYM: BCL2-L-1, APOPTOSIS REGULATOR BCL-X;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: CONTAINS RESIDUES 1-34,92-207 OF BCL-2 AND THE
COMPND 9 UNSTRUCTURED LOOP BETWEEN RESIDUES 35-91 REPLACED IS WITH RESIDUES
COMPND 10 35-50 OF BCL-XL;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: APOPTOSIS REGULATOR BCL-2, BCL-2-LIKE PROTEIN 1,
COMPND 13 APOPTOSIS REGULATOR BCL-2;
COMPND 14 CHAIN: B;
COMPND 15 FRAGMENT: RESIDUES 1-34,29-44,92-207;
COMPND 16 SYNONYM: BCL2-L-1, APOPTOSIS REGULATOR BCL-X;
COMPND 17 ENGINEERED: YES;
COMPND 18 OTHER_DETAILS: CONTAINS RESIDUES 1-34,92-207 OF BCL-2 AND THE
COMPND 19 UNSTRUCTURED LOOP BETWEEN RESIDUES 35-91 REPLACED IS WITH RESIDUES
COMPND 20 35-50 OF BCL-XL;
COMPND 21 MOL_ID: 3;
COMPND 22 MOLECULE: BCL-2-LIKE PROTEIN 11;
COMPND 23 CHAIN: C, D;
COMPND 24 FRAGMENT: BIM BH3, RESIDUES 146-166;
COMPND 25 SYNONYM: BCL2-L-11, BCL2-INTERACTING MEDIATOR OF CELL DEATH;
COMPND 26 OTHER_DETAILS: BIM BH3 WITH CYCLIC BETA AMINO ACIDS AT RESIDUES
COMPND 27 2,6,16 AND PENTENY AMINO ACIDS AT RESIDUES 9,13
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: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-3;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-3;
SOURCE 19 MOL_ID: 3;
SOURCE 20 SYNTHETIC: YES;
SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 22 ORGANISM_COMMON: HUMAN;
SOURCE 23 ORGANISM_TAXID: 9606
KEYWDS FOLDAMER, BIM, APOPTOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR B.J.SMITH,E.F LEE,J.W.CHECCO,S.H.GELLMAN,W.D.FAIRLIE
REVDAT 2 23-SEP-15 5AGX 1 JRNL
REVDAT 1 09-SEP-15 5AGX 0
JRNL AUTH J.W.CHECCO,E.F.LEE,M.EVANGELISTA,N.SLEEBS,K.RODGERS,
JRNL AUTH 2 A.PETTIKIRIARACHCHI,N.KERSHAW,G.A.EDDINGER,D.G.BELAIR,
JRNL AUTH 3 J.L.WILSON,C.H.ELLER,R.T.RAINES,W.L.MURPHY,B.J.SMITH,
JRNL AUTH 4 S.H.GELLMAN,W.D.FAIRLIE
JRNL TITL ALPHA BETA PEPTIDE FOLDAMERS TARGETING INTRACELLULAR
JRNL TITL 2 PROTEIN-PROTEIN INTERACTIONS WITH ACTIVITY ON LIVING CELLS
JRNL REF J.AM.CHEM.SOC. V. 137 11365 2015
JRNL REFN ISSN 0002-7863
JRNL PMID 26317395
JRNL DOI 10.1021/JACS.5B05896
REMARK 2
REMARK 2 RESOLUTION. 2.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.009
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.36
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.93
REMARK 3 NUMBER OF REFLECTIONS : 20250
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1906
REMARK 3 R VALUE (WORKING SET) : 0.1878
REMARK 3 FREE R VALUE : 0.2447
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1013
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 40.0151 - 4.2840 1.00 2931 155 0.1647 0.2137
REMARK 3 2 4.2840 - 3.4009 1.00 2767 145 0.1728 0.2256
REMARK 3 3 3.4009 - 2.9711 1.00 2743 145 0.2097 0.2662
REMARK 3 4 2.9711 - 2.6996 1.00 2723 143 0.2022 0.2343
REMARK 3 5 2.6996 - 2.5061 1.00 2705 142 0.2017 0.3084
REMARK 3 6 2.5061 - 2.3584 1.00 2703 143 0.2147 0.2613
REMARK 3 7 2.3584 - 2.2403 0.99 2665 140 0.2630 0.3823
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.29
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.41
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 : 0.007 2773
REMARK 3 ANGLE : 1.105 3773
REMARK 3 CHIRALITY : 0.042 391
REMARK 3 PLANARITY : 0.005 483
REMARK 3 DIHEDRAL : 23.231 1008
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 96.6440 79.1155 8.9341
REMARK 3 T TENSOR
REMARK 3 T11: 0.1879 T22: 0.2929
REMARK 3 T33: 0.2442 T12: 0.0486
REMARK 3 T13: -0.0111 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 1.6971 L22: 4.1170
REMARK 3 L33: 2.9561 L12: 1.4727
REMARK 3 L13: 0.7502 L23: 1.9377
REMARK 3 S TENSOR
REMARK 3 S11: -0.0340 S12: 0.0672 S13: -0.0838
REMARK 3 S21: -0.0545 S22: -0.1406 S23: 0.1295
REMARK 3 S31: 0.0744 S32: -0.0622 S33: 0.1575
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5AGX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-FEB-15.
REMARK 100 THE PDBE ID CODE IS EBI-62951.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-SEP-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20251
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.24
REMARK 200 RESOLUTION RANGE LOW (A) : 40.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 14.2
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 14.0
REMARK 200 R MERGE FOR SHELL (I) : 0.78
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.89
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: UNPUBLISHED BCL-2 BECLIN BH3 COMPLEX
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 54.36950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 43.02700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 43.02700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 81.55425
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 43.02700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 43.02700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 27.18475
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 43.02700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.02700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 81.55425
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 43.02700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.02700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 27.18475
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 54.36950
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: 2280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 2120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 33
REMARK 465 ASP A 34
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 SER A 205
REMARK 465 MET A 206
REMARK 465 ARG A 207
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 33
REMARK 465 ASP B 34
REMARK 465 ASP B 76
REMARK 465 VAL B 77
REMARK 465 GLU B 78
REMARK 465 GLU B 79
REMARK 465 ASN B 80
REMARK 465 ARG B 81
REMARK 465 THR B 82
REMARK 465 GLU B 83
REMARK 465 ALA B 84
REMARK 465 PRO B 85
REMARK 465 GLU B 86
REMARK 465 GLY B 87
REMARK 465 THR B 88
REMARK 465 SER B 205
REMARK 465 MET B 206
REMARK 465 ARG B 207
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 TYR A 9 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 91 CG CD OE1 OE2
REMARK 470 ARG A 109 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 110 CG CD NE CZ NH1 NH2
REMARK 470 ALA A 113 CB
REMARK 470 GLN A 118 CG CD OE1 NE2
REMARK 470 HIS A 120 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 164 NE CZ NH1 NH2
REMARK 470 TYR B 9 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 89 CG CD OE1 OE2
REMARK 470 GLU B 91 CG CD OE1 OE2
REMARK 470 ARG B 110 NE CZ NH1 NH2
REMARK 470 ALA B 113 CB
REMARK 470 GLN B 118 CG CD OE1 NE2
REMARK 470 ARG B 164 CD NE CZ NH1 NH2
REMARK 470 ARG C 20 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 21 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 21 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OH TYR A 18 OE2 GLU A 152 2.18
REMARK 500 OD1 ASP A 103 NH1 ARG A 106 2.14
REMARK 500 OH TYR B 18 OE2 GLU B 152 2.08
REMARK 500 OG SER B 105 OE1 GLU B 152 2.12
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 XCP C 2 CA - C - N ANGL. DEV. = -14.1 DEGREES
REMARK 500 XCP D 2 CA - C - N ANGL. DEV. = -15.9 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 9 -102.10 85.22
REMARK 500 TYR B 9 -150.82 -170.45
REMARK 500 XCP C 2 -86.65 -6.95
REMARK 500 XCP C 16 -77.81 -22.88
REMARK 500 XCP D 2 -89.61 -3.40
REMARK 500 XCP D 16 -74.91 -23.53
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 ILE C 1 XCP C 2 138.02
REMARK 500 ASN C 15 XCP C 16 139.36
REMARK 500 ILE D 1 XCP D 2 139.66
REMARK 500 ASN D 15 XCP D 16 139.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 XCP C 2 16.72
REMARK 500 XCP C 16 18.06
REMARK 500 XCP D 2 16.78
REMARK 500 XCP D 16 17.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 XCP C 2 -102.5 L D WRONG HAND
REMARK 500 XCP C 16 -108.9 L D WRONG HAND
REMARK 500 XCP D 2 -102.6 L D WRONG HAND
REMARK 500 XCP D 16 -107.9 L D WRONG HAND
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AGW RELATED DB: PDB
REMARK 900 BCL-2 ALPHA BETA-1 COMPLEX
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 BCL-2 WITH THE UNSTRUCTURED LOOP BETWEEN RESIDUES 35-91
REMARK 999 REPLACED WITH RESIDUES 35-50 OF BCL-XL
DBREF 5AGX A 1 34 UNP P10415 BCL2_HUMAN 1 34
DBREF 5AGX A 76 91 UNP Q07817 B2CL1_HUMAN 29 44
DBREF 5AGX A 92 207 UNP P10415 BCL2_HUMAN 92 207
DBREF 5AGX B 1 34 UNP P10415 BCL2_HUMAN 1 34
DBREF 5AGX B 76 91 UNP Q07817 B2CL1_HUMAN 29 44
DBREF 5AGX B 92 207 UNP P10415 BCL2_HUMAN 92 207
DBREF 5AGX C 1 21 UNP O43521 B2L11_HUMAN 146 166
DBREF 5AGX D 1 21 UNP O43521 B2L11_HUMAN 146 166
SEQADV 5AGX ACE C -1 UNP O43521 EXPRESSION TAG
SEQADV 5AGX ACE D -1 UNP O43521 EXPRESSION TAG
SEQADV 5AGX XCP C 2 UNP O43521 TRP 147 ENGINEERED MUTATION
SEQADV 5AGX AJE C 6 UNP O43521 GLU 151 ENGINEERED MUTATION
SEQADV 5AGX MH8 C 9 UNP O43521 ARG 154 ENGINEERED MUTATION
SEQADV 5AGX MH8 C 13 UNP O43521 GLU 158 ENGINEERED MUTATION
SEQADV 5AGX XCP C 16 UNP O43521 ALA 161 ENGINEERED MUTATION
SEQADV 5AGX XCP D 2 UNP O43521 TRP 147 ENGINEERED MUTATION
SEQADV 5AGX AJE D 6 UNP O43521 GLU 151 ENGINEERED MUTATION
SEQADV 5AGX MH8 D 9 UNP O43521 ARG 154 ENGINEERED MUTATION
SEQADV 5AGX MH8 D 13 UNP O43521 GLU 158 ENGINEERED MUTATION
SEQADV 5AGX XCP D 16 UNP O43521 ALA 161 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 GLY 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 B 166 MET ALA HIS ALA GLY ARG THR GLY TYR ASP ASN ARG GLU
SEQRES 2 B 166 ILE VAL MET LYS TYR ILE HIS TYR LYS LEU SER GLN ARG
SEQRES 3 B 166 GLY TYR GLU TRP ASP ALA GLY ASP ASP VAL GLU GLU ASN
SEQRES 4 B 166 ARG THR GLU ALA PRO GLU GLY THR GLU SER GLU VAL VAL
SEQRES 5 B 166 HIS LEU THR LEU ARG GLN ALA GLY ASP ASP PHE SER ARG
SEQRES 6 B 166 ARG TYR ARG ARG ASP PHE ALA GLU MET SER SER GLN LEU
SEQRES 7 B 166 HIS LEU THR PRO PHE THR ALA ARG GLY ARG PHE ALA THR
SEQRES 8 B 166 VAL VAL GLU GLU LEU PHE ARG ASP GLY VAL ASN TRP GLY
SEQRES 9 B 166 ARG ILE VAL ALA PHE PHE GLU PHE GLY GLY VAL MET CYS
SEQRES 10 B 166 VAL GLU SER VAL ASN ARG GLU MET SER PRO LEU VAL ASP
SEQRES 11 B 166 ASN ILE ALA ILE TRP MET THR GLU TYR LEU ASN ARG HIS
SEQRES 12 B 166 LEU HIS THR TRP ILE GLN ASP ASN GLY GLY TRP ASP ALA
SEQRES 13 B 166 PHE VAL GLU LEU TYR GLY PRO SER MET ARG
SEQRES 1 C 22 ACE ILE XCP ILE ALA GLN AJE LEU ARG MH8 ILE GLY ASP
SEQRES 2 C 22 MH8 PHE ASN XCP TYR TYR ALA ARG ARG
SEQRES 1 D 22 ACE ILE XCP ILE ALA GLN AJE LEU ARG MH8 ILE GLY ASP
SEQRES 2 D 22 MH8 PHE ASN XCP TYR TYR ALA ARG ARG
HET ACE C -1 3
HET XCP C 2 8
HET AJE C 6 15
HET MH8 C 9 10
HET MH8 C 13 10
HET XCP C 16 8
HET ACE D -1 3
HET XCP D 2 8
HET AJE D 6 15
HET MH8 D 9 10
HET MH8 D 13 10
HET XCP D 16 8
HETNAM ACE ACETYL GROUP
HETNAM XCP (1S,2S)-2-AMINOCYCLOPENTANECARBOXYLIC ACID
HETNAM AJE (3S,4R)-4-AMINO-1-(3-CARBOXYPROPANOYL)
HETNAM 2 AJE PYRROLIDINE-3-CARBOXYLIC ACID
HETNAM MH8 (2S)-2-AMINO-2-METHYLHEPT-6-ENOIC ACID
FORMUL 3 ACE 2(C2 H4 O)
FORMUL 3 XCP 4(C6 H11 N O2)
FORMUL 3 AJE 2(C9 H14 N2 O5)
FORMUL 3 MH8 4(C8 H15 N O2)
FORMUL 5 HOH *44(H2 O)
HELIX 1 1 ASP A 10 ARG A 26 1 17
HELIX 2 2 SER A 90 TYR A 108 1 19
HELIX 3 3 ARG A 109 ALA A 113 5 5
HELIX 4 4 GLU A 114 HIS A 120 1 7
HELIX 5 5 THR A 125 PHE A 138 1 14
HELIX 6 6 ASN A 143 ARG A 164 1 22
HELIX 7 7 PRO A 168 LEU A 185 1 18
HELIX 8 8 LEU A 185 ASN A 192 1 8
HELIX 9 9 GLY A 193 GLY A 203 1 11
HELIX 10 10 ASP B 10 ARG B 26 1 17
HELIX 11 11 SER B 90 TYR B 108 1 19
HELIX 12 12 ARG B 109 ALA B 113 5 5
HELIX 13 13 GLU B 114 HIS B 120 1 7
HELIX 14 14 THR B 125 PHE B 138 1 14
HELIX 15 15 ASN B 143 ARG B 164 1 22
HELIX 16 16 SER B 167 LEU B 185 1 19
HELIX 17 17 LEU B 185 ASN B 192 1 8
HELIX 18 18 GLY B 193 GLY B 203 1 11
LINK C ACE C -1 N ILE C 1 1555 1555 1.32
LINK C ILE C 1 N XCP C 2 1555 1555 1.33
LINK C XCP C 2 N ILE C 3 1555 1555 1.33
LINK C GLN C 5 N AJE C 6 1555 1555 1.33
LINK C AJE C 6 N LEU C 7 1555 1555 1.33
LINK C ARG C 8 N MH8 C 9 1555 1555 1.33
LINK C MH8 C 9 N ILE C 10 1555 1555 1.32
LINK C ASP C 12 N MH8 C 13 1555 1555 1.33
LINK C MH8 C 13 N PHE C 14 1555 1555 1.33
LINK C ASN C 15 N XCP C 16 1555 1555 1.34
LINK C XCP C 16 N TYR C 17 1555 1555 1.33
LINK C ACE D -1 N ILE D 1 1555 1555 1.33
LINK C ILE D 1 N XCP D 2 1555 1555 1.33
LINK C XCP D 2 N ILE D 3 1555 1555 1.33
LINK C GLN D 5 N AJE D 6 1555 1555 1.33
LINK C AJE D 6 N LEU D 7 1555 1555 1.33
LINK C ARG D 8 N MH8 D 9 1555 1555 1.34
LINK C MH8 D 9 N ILE D 10 1555 1555 1.33
LINK C ASP D 12 N MH8 D 13 1555 1555 1.33
LINK C MH8 D 13 N PHE D 14 1555 1555 1.33
LINK C ASN D 15 N XCP D 16 1555 1555 1.34
LINK C XCP D 16 N TYR D 17 1555 1555 1.33
CRYST1 86.054 86.054 108.739 90.00 90.00 90.00 P 43 21 2 16
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 0.011621 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011621 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009196 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
