HEADER APOPTOSIS 14-AUG-09 3IO8
TITLE BIML12F IN COMPLEX WITH BCL-XL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BCL-2-LIKE PROTEIN 1;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: RESIDUES 1-26, AND RESIDUES 83-209;
COMPND 5 SYNONYM: BCL2-L-1, APOPTOSIS REGULATOR BCL-X;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BCL-2-LIKE PROTEIN 11;
COMPND 9 CHAIN: B, D;
COMPND 10 FRAGMENT: BH3 PEPTIDE, RESIDUES 141-166;
COMPND 11 SYNONYM: BCL2-L-11, BCL2-INTERACTING MEDIATOR OF CELL DEATH;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BCL2L1, BCL2L, BCLX;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS HELICAL BUNDLE, BCL-2-LIKE FOLD, ALTERNATIVE SPLICING, APOPTOSIS,
KEYWDS 2 MEMBRANE, MITOCHONDRION, NUCLEUS, TRANSMEMBRANE, PHOSPHOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.M.COLMAN,E.F.LEE,W.D.FAIRLIE,B.J.SMITH,P.E.CZABOTAR,H.YANG,
AUTHOR 2 B.E.SLEEBS,G.LESSENE
REVDAT 6 06-SEP-23 3IO8 1 REMARK
REVDAT 5 13-OCT-21 3IO8 1 REMARK SEQADV
REVDAT 4 26-JUL-17 3IO8 1 SOURCE REMARK
REVDAT 3 29-DEC-09 3IO8 1 REMARK
REVDAT 2 10-NOV-09 3IO8 1 JRNL
REVDAT 1 01-SEP-09 3IO8 0
JRNL AUTH E.F.LEE,P.E.CZABOTAR,H.YANG,B.E.SLEEBS,G.LESSENE,P.M.COLMAN,
JRNL AUTH 2 B.J.SMITH,W.D.FAIRLIE
JRNL TITL CONFORMATIONAL CHANGES IN BCL-2 PRO-SURVIVAL PROTEINS
JRNL TITL 2 DETERMINE THEIR CAPACITY TO BIND LIGANDS.
JRNL REF J.BIOL.CHEM. V. 284 30508 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19726685
JRNL DOI 10.1074/JBC.M109.040725
REMARK 2
REMARK 2 RESOLUTION. 2.30 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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 18425
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.150
REMARK 3 FREE R VALUE TEST SET COUNT : 948
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 47.3090 - 4.7828 0.98 1954 99 0.1028 0.1904
REMARK 3 2 4.7828 - 3.7968 0.98 1958 100 0.1358 0.1988
REMARK 3 3 3.7968 - 3.3170 0.98 1935 114 0.2013 0.2246
REMARK 3 4 3.3170 - 3.0138 0.98 1947 108 0.2386 0.2361
REMARK 3 5 3.0138 - 2.7978 0.98 1932 115 0.2534 0.2755
REMARK 3 6 2.7978 - 2.6328 0.98 1918 96 0.2730 0.2822
REMARK 3 7 2.6328 - 2.5010 0.98 1966 108 0.3039 0.3307
REMARK 3 8 2.5010 - 2.3921 0.98 1944 95 0.2954 0.3111
REMARK 3 9 2.3921 - 2.3000 0.98 1925 111 0.3165 0.3193
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 : 0.36
REMARK 3 B_SOL : 63.18
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 39.780
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 : 0.004 2754
REMARK 3 ANGLE : 0.765 3721
REMARK 3 CHIRALITY : 0.055 380
REMARK 3 PLANARITY : 0.002 482
REMARK 3 DIHEDRAL : 15.845 967
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 3IO8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054656.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9566
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18464
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.14700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.83500
REMARK 200 R SYM FOR SHELL (I) : 0.83500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: PDB ID: 2P1L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02M ZINC ACETATE 2.5M SODIUM
REMARK 280 CHLORIDE 0.1M IMIDAZOLE, PH 8.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
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 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 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 113.39600
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 56.69800
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 113.39600
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 56.69800
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS ONE HALF OF THE ASYMMETRIC UNIT.
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: 2110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 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: 1900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 36 LIES ON A SPECIAL POSITION.
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 -4
REMARK 465 THR A 109
REMARK 465 SER A 110
REMARK 465 GLN A 111
REMARK 465 ASN A 198
REMARK 465 ALA A 199
REMARK 465 ALA A 200
REMARK 465 ALA A 201
REMARK 465 GLU A 202
REMARK 465 SER A 203
REMARK 465 ARG A 204
REMARK 465 LYS A 205
REMARK 465 GLY A 206
REMARK 465 GLN A 207
REMARK 465 GLU A 208
REMARK 465 ARG A 209
REMARK 465 ASP B 51
REMARK 465 MET B 52
REMARK 465 ARG B 53
REMARK 465 ASN C 198
REMARK 465 ALA C 199
REMARK 465 ALA C 200
REMARK 465 ALA C 201
REMARK 465 GLU C 202
REMARK 465 SER C 203
REMARK 465 ARG C 204
REMARK 465 LYS C 205
REMARK 465 GLY C 206
REMARK 465 GLN C 207
REMARK 465 GLU C 208
REMARK 465 ARG C 209
REMARK 465 ASP D 51
REMARK 465 MET D 52
REMARK 465 TYR D 72
REMARK 465 TYR D 73
REMARK 465 ALA D 74
REMARK 465 ARG D 75
REMARK 465 ARG D 76
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 GLU B 55 CG CD OE1 OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 160 CD
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 ASP A 107 55.37 36.06
REMARK 500 HIS A 113 70.69 45.35
REMARK 500 THR A 118 30.11 -96.22
REMARK 500 GLU A 158 -0.55 61.81
REMARK 500 MET A 159 21.43 -66.77
REMARK 500 HIS A 177 -39.87 -131.59
REMARK 500 ILE A 182 -36.26 -37.79
REMARK 500 ASN A 185 37.77 -91.17
REMARK 500 ILE B 56 -48.94 -25.41
REMARK 500 ARG C 100 -70.90 -58.13
REMARK 500 ASP C 107 66.22 31.05
REMARK 500 HIS C 113 50.80 77.48
REMARK 500 GLU C 124 -73.33 -55.93
REMARK 500 PHE C 131 41.91 -108.38
REMARK 500 LYS C 157 40.28 -89.44
REMARK 500 GLU C 158 -21.07 64.68
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 ZN A 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 211
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FDL RELATED DB: PDB
REMARK 900 HBIM IN COMPLEX WITH HBCL-XL
REMARK 900 RELATED ID: 1PQ1 RELATED DB: PDB
REMARK 900 MBIM IN COMPLEX WITH MBCL-XL
REMARK 900 RELATED ID: 3IO9 RELATED DB: PDB
REMARK 900 BIML12Y IN COMPLEX WITH MCL-1
DBREF 3IO8 A 1 26 UNP Q07817 B2CL1_HUMAN 1 26
DBREF 3IO8 A 83 209 UNP Q07817 B2CL1_HUMAN 83 209
DBREF 3IO8 B 51 76 UNP O43521 B2L11_HUMAN 141 166
DBREF 3IO8 C 1 26 UNP Q07817 B2CL1_HUMAN 1 26
DBREF 3IO8 C 83 209 UNP Q07817 B2CL1_HUMAN 83 209
DBREF 3IO8 D 51 76 UNP O43521 B2L11_HUMAN 141 166
SEQADV 3IO8 GLY A -4 UNP Q07817 EXPRESSION TAG
SEQADV 3IO8 PRO A -3 UNP Q07817 EXPRESSION TAG
SEQADV 3IO8 LEU A -2 UNP Q07817 EXPRESSION TAG
SEQADV 3IO8 GLY A -1 UNP Q07817 EXPRESSION TAG
SEQADV 3IO8 SER A 0 UNP Q07817 EXPRESSION TAG
SEQADV 3IO8 PHE B 62 UNP O43521 LEU 152 ENGINEERED MUTATION
SEQADV 3IO8 GLY C -4 UNP Q07817 EXPRESSION TAG
SEQADV 3IO8 PRO C -3 UNP Q07817 EXPRESSION TAG
SEQADV 3IO8 LEU C -2 UNP Q07817 EXPRESSION TAG
SEQADV 3IO8 GLY C -1 UNP Q07817 EXPRESSION TAG
SEQADV 3IO8 SER C 0 UNP Q07817 EXPRESSION TAG
SEQADV 3IO8 PHE D 62 UNP O43521 LEU 152 ENGINEERED MUTATION
SEQRES 1 A 158 GLY PRO LEU GLY SER MET SER GLN SER ASN ARG GLU LEU
SEQRES 2 A 158 VAL VAL ASP PHE LEU SER TYR LYS LEU SER GLN LYS GLY
SEQRES 3 A 158 TYR SER TRP SER GLN MET ALA ALA VAL LYS GLN ALA LEU
SEQRES 4 A 158 ARG GLU ALA GLY ASP GLU PHE GLU LEU ARG TYR ARG ARG
SEQRES 5 A 158 ALA PHE SER ASP LEU THR SER GLN LEU HIS ILE THR PRO
SEQRES 6 A 158 GLY THR ALA TYR GLN SER PHE GLU GLN VAL VAL ASN GLU
SEQRES 7 A 158 LEU PHE ARG ASP GLY VAL ASN TRP GLY ARG ILE VAL ALA
SEQRES 8 A 158 PHE PHE SER PHE GLY GLY ALA LEU CYS VAL GLU SER VAL
SEQRES 9 A 158 ASP LYS GLU MET GLN VAL LEU VAL SER ARG ILE ALA ALA
SEQRES 10 A 158 TRP MET ALA THR TYR LEU ASN ASP HIS LEU GLU PRO TRP
SEQRES 11 A 158 ILE GLN GLU ASN GLY GLY TRP ASP THR PHE VAL GLU LEU
SEQRES 12 A 158 TYR GLY ASN ASN ALA ALA ALA GLU SER ARG LYS GLY GLN
SEQRES 13 A 158 GLU ARG
SEQRES 1 B 26 ASP MET ARG PRO GLU ILE TRP ILE ALA GLN GLU PHE ARG
SEQRES 2 B 26 ARG ILE GLY ASP GLU PHE ASN ALA TYR TYR ALA ARG ARG
SEQRES 1 C 158 GLY PRO LEU GLY SER MET SER GLN SER ASN ARG GLU LEU
SEQRES 2 C 158 VAL VAL ASP PHE LEU SER TYR LYS LEU SER GLN LYS GLY
SEQRES 3 C 158 TYR SER TRP SER GLN MET ALA ALA VAL LYS GLN ALA LEU
SEQRES 4 C 158 ARG GLU ALA GLY ASP GLU PHE GLU LEU ARG TYR ARG ARG
SEQRES 5 C 158 ALA PHE SER ASP LEU THR SER GLN LEU HIS ILE THR PRO
SEQRES 6 C 158 GLY THR ALA TYR GLN SER PHE GLU GLN VAL VAL ASN GLU
SEQRES 7 C 158 LEU PHE ARG ASP GLY VAL ASN TRP GLY ARG ILE VAL ALA
SEQRES 8 C 158 PHE PHE SER PHE GLY GLY ALA LEU CYS VAL GLU SER VAL
SEQRES 9 C 158 ASP LYS GLU MET GLN VAL LEU VAL SER ARG ILE ALA ALA
SEQRES 10 C 158 TRP MET ALA THR TYR LEU ASN ASP HIS LEU GLU PRO TRP
SEQRES 11 C 158 ILE GLN GLU ASN GLY GLY TRP ASP THR PHE VAL GLU LEU
SEQRES 12 C 158 TYR GLY ASN ASN ALA ALA ALA GLU SER ARG LYS GLY GLN
SEQRES 13 C 158 GLU ARG
SEQRES 1 D 26 ASP MET ARG PRO GLU ILE TRP ILE ALA GLN GLU PHE ARG
SEQRES 2 D 26 ARG ILE GLY ASP GLU PHE ASN ALA TYR TYR ALA ARG ARG
HET ZN A 210 1
HET ZN C 210 1
HET ZN C 211 1
HETNAM ZN ZINC ION
FORMUL 5 ZN 3(ZN 2+)
FORMUL 8 HOH *29(H2 O)
HELIX 1 1 SER A 0 LYS A 20 1 21
HELIX 2 2 SER A 25 TYR A 101 1 21
HELIX 3 3 ARG A 102 SER A 106 5 5
HELIX 4 4 THR A 118 PHE A 131 1 14
HELIX 5 5 ASN A 136 ASP A 156 1 21
HELIX 6 6 LYS A 157 MET A 159 5 3
HELIX 7 7 GLN A 160 HIS A 177 1 18
HELIX 8 8 HIS A 177 ASN A 185 1 9
HELIX 9 9 GLY A 187 GLY A 196 1 10
HELIX 10 10 GLU B 55 ARG B 76 1 22
HELIX 11 11 SER C 0 GLY C 21 1 22
HELIX 12 12 SER C 25 TYR C 101 1 21
HELIX 13 13 ARG C 102 SER C 106 5 5
HELIX 14 14 ASP C 107 HIS C 113 1 7
HELIX 15 15 THR C 118 PHE C 131 1 14
HELIX 16 16 ASN C 136 LYS C 157 1 22
HELIX 17 17 GLU C 158 GLN C 160 5 3
HELIX 18 18 VAL C 161 ASN C 185 1 25
HELIX 19 19 GLY C 187 GLY C 196 1 10
HELIX 20 20 ARG D 53 ALA D 71 1 19
LINK ND1 HIS C 113 ZN ZN C 210 1555 1555 2.35
CISPEP 1 GLY C -4 PRO C -3 0 0.48
SITE 1 AC1 1 HOH A 211
SITE 1 AC2 4 HOH A 28 HIS A 177 HIS C 113 HOH C 215
SITE 1 AC3 1 GLY C -4
CRYST1 65.717 65.717 170.094 90.00 90.00 120.00 P 62 12
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 0.015217 0.008785 0.000000 0.00000
SCALE2 0.000000 0.017571 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005879 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
