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Database: PDB
Entry: 3IO8
LinkDB: 3IO8
Original site: 3IO8 
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   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                     
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                     
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                                                                             
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