HEADER APOPTOSIS 04-FEB-15 5AGW
TITLE BCL-2 ALPHA BETA-1 COMPLEX
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, B;
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: BCL-2-LIKE PROTEIN 11;
COMPND 13 CHAIN: C, D;
COMPND 14 FRAGMENT: RESIDUES 148-166;
COMPND 15 SYNONYM: BCL2-L-11, BCL2-INTERACTING MEDIATOR OF CELL DEATH;
COMPND 16 ENGINEERED: YES;
COMPND 17 MUTATION: YES
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
KEYWDS BCL-2, FOLDAMER, BIM, APOPTOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR B.J.SMITH,E.F LEE,J.W.CHECCO,S.H.GELLMAN,W.D.FAIRLIE
REVDAT 3 23-OCT-19 5AGW 1 SEQADV LINK
REVDAT 2 23-SEP-15 5AGW 1 JRNL
REVDAT 1 09-SEP-15 5AGW 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. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 12074
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 603
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 33.9713 - 4.2753 1.00 3020 159 0.1797 0.2450
REMARK 3 2 4.2753 - 3.3944 1.00 2863 150 0.1922 0.2693
REMARK 3 3 3.3944 - 2.9656 1.00 2824 149 0.2572 0.3261
REMARK 3 4 2.9656 - 2.6946 0.99 2764 145 0.3050 0.3864
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) : 0.500
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.150
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 79.51
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 : 0.009 2634
REMARK 3 ANGLE : 1.274 3589
REMARK 3 CHIRALITY : 0.050 373
REMARK 3 PLANARITY : 0.005 456
REMARK 3 DIHEDRAL : 24.161 933
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): 5.9760 11.0786 -18.7110
REMARK 3 T TENSOR
REMARK 3 T11: 0.5839 T22: 0.5244
REMARK 3 T33: 0.4974 T12: 0.0399
REMARK 3 T13: -0.0175 T23: 0.1209
REMARK 3 L TENSOR
REMARK 3 L11: 6.8231 L22: 2.8216
REMARK 3 L33: 3.8444 L12: -2.5406
REMARK 3 L13: -2.2251 L23: 0.8283
REMARK 3 S TENSOR
REMARK 3 S11: -0.5842 S12: -0.6413 S13: -0.2248
REMARK 3 S21: 0.2147 S22: 0.2090 S23: -0.2223
REMARK 3 S31: 0.2106 S32: 0.5912 S33: 0.3604
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 5AGW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1290062950.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-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) : 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 CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12081
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 33.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 13.40
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.2900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 9.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.080
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 (%): 48.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02M CACL2, 0.1M MOPS PH7.0, 10% 2
REMARK 280 -PROPANOL
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 53.74000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 43.83650
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 43.83650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 80.61000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 43.83650
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 43.83650
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.87000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 43.83650
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.83650
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 80.61000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 43.83650
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.83650
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 26.87000
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 53.74000
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: 2120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.7 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 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: 2020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.8 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 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 ALA A 32
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 8
REMARK 465 TYR B 9
REMARK 465 ALA B 32
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 GLU B 89
REMARK 465 SER B 205
REMARK 465 MET B 206
REMARK 465 ARG B 207
REMARK 465 ARG C 20
REMARK 465 ARG C 21
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 LEU A 95 CG CD1 CD2
REMARK 470 ARG A 110 CG CD NE CZ NH1 NH2
REMARK 470 ALA A 113 CB
REMARK 470 MET A 115 CG SD CE
REMARK 470 GLN A 118 CG CD OE1 NE2
REMARK 470 GLU A 135 CG CD OE1 OE2
REMARK 470 ILE A 147 CD1
REMARK 470 GLU A 165 CG CD OE1 OE2
REMARK 470 ARG A 183 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 189 CD1
REMARK 470 LYS B 17 CG CD CE NZ
REMARK 470 ASP B 31 CG OD1 OD2
REMARK 470 GLU B 91 CG CD OE1 OE2
REMARK 470 ARG B 109 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 110 CG CD NE CZ NH1 NH2
REMARK 470 ALA B 113 CB
REMARK 470 GLN B 118 CG CD OE1 NE2
REMARK 470 ILE B 147 CD1
REMARK 470 ARG B 164 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 173 CD1
REMARK 470 GLU B 179 CG CD OE1 OE2
REMARK 470 ARG B 183 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 190 CG CD OE1 NE2
REMARK 470 ASP B 196 CG OD1 OD2
REMARK 470 GLU B 200 CG CD OE1 OE2
REMARK 470 LEU B 201 CG CD1 CD2
REMARK 470 TYR C 17 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG D 20 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
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2002 O HOH A 2002 8554 2.05
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. = -19.6 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 TYR A 9 -111.94 71.27
REMARK 500 TYR A 108 45.71 -108.34
REMARK 500 GLN A 118 37.09 -85.53
REMARK 500 MET A 166 78.85 -159.28
REMARK 500 HIS A 184 -13.62 -158.60
REMARK 500 TYR A 202 -60.22 -90.60
REMARK 500 GLN B 25 28.09 -73.75
REMARK 500 VAL B 92 -59.26 -126.07
REMARK 500 HIS B 120 85.46 56.49
REMARK 500 HIS B 184 -25.71 -145.22
REMARK 500 ASP B 191 6.16 -61.54
REMARK 500 ASN B 192 21.87 -146.39
REMARK 500 AJE C 6 -62.59 -28.75
REMARK 500 TYR D 18 45.37 -94.71
REMARK 500 ARG D 20 -93.33 -142.26
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 2 139.82
REMARK 500 ASN C 15 XCP C 16 141.48
REMARK 500 ILE D 1 XCP D 2 132.47
REMARK 500 ASN D 15 XCP D 16 134.96
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 17.36
REMARK 500 XCP C 16 16.73
REMARK 500 XCP D 2 18.11
REMARK 500 XCP D 16 16.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AGX RELATED DB: PDB
REMARK 900 BCL-2 ALPHA BETA-1 LINEAR COMPLEX
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 CONTAINS RESIDUES 1-34, 92-207 OF BCL-2 AND THE
REMARK 999 UNSTRUCTURED LOOP BETWEEN RESIDUES 35-91 REPLACED IS WITH
REMARK 999 RESIDUES 35-50 OF BCL-XL
REMARK 999 RESIDUES 2,6,16 ARE CYCLIC BETA AMINO ACIDS RESIDUES 9,13
REMARK 999 ARE PENETENYL S5 AMINO ACIDS THAT ARE CROSS-LINKED
DBREF 5AGW A 1 34 UNP P10415 BCL2_HUMAN 1 34
DBREF 5AGW A 76 91 UNP Q07817 B2CL1_HUMAN 29 44
DBREF 5AGW A 92 207 UNP P10415 BCL2_HUMAN 92 207
DBREF 5AGW B 1 34 UNP P10415 BCL2_HUMAN 1 34
DBREF 5AGW B 76 91 UNP Q07817 B2CL1_HUMAN 29 44
DBREF 5AGW B 92 207 UNP P10415 BCL2_HUMAN 92 207
DBREF 5AGW C 1 21 UNP O43521 B2L11_HUMAN 146 166
DBREF 5AGW D 1 21 UNP O43521 B2L11_HUMAN 146 166
SEQADV 5AGW ACE C -1 UNP O43521 ACETYLATION
SEQADV 5AGW ACE D -1 UNP O43521 ACETYLATION
SEQADV 5AGW XCP C 2 UNP O43521 TRP 147 ENGINEERED MUTATION
SEQADV 5AGW AJE C 6 UNP O43521 GLU 151 ENGINEERED MUTATION
SEQADV 5AGW MH8 C 9 UNP O43521 ARG 154 ENGINEERED MUTATION
SEQADV 5AGW MH8 C 13 UNP O43521 GLU 158 ENGINEERED MUTATION
SEQADV 5AGW XCP C 16 UNP O43521 ALA 161 ENGINEERED MUTATION
SEQADV 5AGW XCP D 2 UNP O43521 TRP 147 ENGINEERED MUTATION
SEQADV 5AGW AJE D 6 UNP O43521 GLU 151 ENGINEERED MUTATION
SEQADV 5AGW MH8 D 9 UNP O43521 ARG 154 ENGINEERED MUTATION
SEQADV 5AGW MH8 D 13 UNP O43521 GLU 158 ENGINEERED MUTATION
SEQADV 5AGW 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 LEU 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 9
HET MH8 C 13 9
HET XCP C 16 8
HET ACE D -1 3
HET XCP D 2 8
HET AJE D 6 15
HET MH8 D 9 9
HET MH8 D 13 9
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)PYRROLIDINE-3-
HETNAM 2 AJE 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 *6(H2 O)
HELIX 1 1 ASP A 10 ARG A 26 1 17
HELIX 2 2 GLU A 91 TYR A 108 1 18
HELIX 3 3 TYR A 108 GLN A 118 1 11
HELIX 4 4 THR A 125 PHE A 138 1 14
HELIX 5 5 ASN A 143 ARG A 164 1 22
HELIX 6 6 PRO A 168 LEU A 185 1 18
HELIX 7 7 LEU A 185 ASN A 192 1 8
HELIX 8 8 GLY A 194 GLY A 203 1 10
HELIX 9 9 ASP B 10 GLN B 25 1 16
HELIX 10 10 VAL B 92 TYR B 108 1 17
HELIX 11 11 TYR B 108 SER B 117 1 10
HELIX 12 12 THR B 122 PHE B 138 1 17
HELIX 13 13 ASN B 143 ARG B 164 1 22
HELIX 14 14 MET B 166 LEU B 185 1 20
HELIX 15 15 LEU B 185 ASP B 191 1 7
HELIX 16 16 GLY B 193 GLY B 203 1 11
LINK C ACE C -1 N ILE C 1 1555 1555 1.33
LINK C ILE C 1 N XCP C 2 1555 1555 1.33
LINK C XCP C 2 N ILE C 3 1555 1555 1.32
LINK C GLN C 5 N AJE C 6 1555 1555 1.34
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 CE MH8 C 9 CE MH8 C 13 1555 1555 1.34
LINK C MH8 C 9 N ILE C 10 1555 1555 1.33
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 1.33
LINK C XCP C 16 N TYR C 17 1555 1555 1.33
LINK C ACE D -1 N ILE D 1 1555 1555 1.34
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 1.34
LINK C ARG D 8 N MH8 D 9 1555 1555 1.33
LINK C MH8 D 9 N ILE D 10 1555 1555 1.32
LINK CE MH8 D 9 CE MH8 D 13 1555 1555 1.41
LINK C ASP D 12 N MH8 D 13 1555 1555 1.33
LINK C MH8 D 13 N PHE D 14 1555 1555 1.32
LINK C ASN D 15 N XCP D 16 1555 1555 1.33
LINK C XCP D 16 N TYR D 17 1555 1555 1.33
CISPEP 1 GLY A 203 PRO A 204 0 3.90
CRYST1 87.673 87.673 107.480 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 0.011406 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011406 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009304 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
