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Database: PDB
Entry: 2P1L
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Original site: 2P1L 
HEADER    APOPTOSIS                               05-MAR-07   2P1L              
TITLE     STRUCTURE OF THE BCL-XL:BECLIN 1 COMPLEX                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APOPTOSIS REGULATOR BCL-X;                                 
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 FRAGMENT: BCL-XL DELTA-LOOP;                                         
COMPND   5 SYNONYM: BCL-XL; BCL-2-LIKE 1 PROTEIN;                               
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: BECLIN 1;                                                  
COMPND  10 CHAIN: B, D, F, H;                                                   
COMPND  11 FRAGMENT: BECLIN 1;                                                  
COMPND  12 SYNONYM: COILED-COIL MYOSIN-LIKE BCL2-INTERACTING PROTEIN; PROTEIN   
COMPND  13 GT197;                                                               
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 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(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRSF;                                     
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: BECN1, GT197;                                                  
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PGEX-2T                                   
KEYWDS    APOPTOSIS; AUTOPHAGY; BECLIN; BH3 DOMAIN; BCL, APOPTOSIS              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.D.JEFFREY,Y.SHI,A.L.OBERSTEIN                                       
REVDAT   4   26-JUL-17 2P1L    1       SOURCE REMARK                            
REVDAT   3   24-FEB-09 2P1L    1       VERSN                                    
REVDAT   2   05-JUN-07 2P1L    1       JRNL                                     
REVDAT   1   13-MAR-07 2P1L    0                                                
JRNL        AUTH   A.OBERSTEIN,P.D.JEFFREY,Y.SHI                                
JRNL        TITL   CRYSTAL STRUCTURE OF THE BCL-XL-BECLIN 1 PEPTIDE COMPLEX:    
JRNL        TITL 2 BECLIN 1 IS A NOVEL BH3-ONLY PROTEIN                         
JRNL        REF    J.BIOL.CHEM.                  V. 282 13123 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17337444                                                     
JRNL        DOI    10.1074/JBC.M700492200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1611649.830                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 41260                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2107                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6487                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020                       
REMARK   3   BIN FREE R VALUE                    : 0.3500                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 360                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5284                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 16                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 54.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.03000                                             
REMARK   3    B22 (A**2) : 19.33000                                             
REMARK   3    B33 (A**2) : -13.29000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.29                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.39                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.38                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 18.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.000                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 36.97                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2P1L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000041852.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUL-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : SILICON                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46829                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 3.990                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.41300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% (W/V) PEG-400, 0.1M HEPES PH7.5,     
REMARK 280  0.2M SODIUM CITRATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       53.97000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.29500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       53.97000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.29500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7                                     
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: UNIQUE HETERODIMERIC COMPLEX IS FORMED BETWEEN CHAINS A AND  
REMARK 300 B, (BCL-XL AND BECLIN 1 RESPECTIVELY). A DIMER OF HETERODIMERS IS    
REMARK 300 FORMED BETWEEN THE A+B AND C+D COMPLEXES VIA A DOMAIN-SWAPPED        
REMARK 300 HELIX. THERE ARE TWO OF THESE "DIMERS OF HETERODIMERS" IN THE        
REMARK 300 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: 2090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9560 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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: 2070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9740 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 2140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9660 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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: 4                                                       
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: 9580 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC              
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 38600 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 55280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -258.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000     -110.59000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000      -53.97000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000      -55.29500            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000       53.97000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      -55.29500            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
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: 7                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A   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     GLN B   129                                                      
REMARK 465     THR B   130                                                      
REMARK 465     ASP B   131                                                      
REMARK 465     VAL B   132                                                      
REMARK 465     ASP B   133                                                      
REMARK 465     HIS B   134                                                      
REMARK 465     PRO B   135                                                      
REMARK 465     MET C     1                                                      
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     GLN D   129                                                      
REMARK 465     THR D   130                                                      
REMARK 465     ASP D   131                                                      
REMARK 465     VAL D   132                                                      
REMARK 465     ASP D   133                                                      
REMARK 465     HIS D   134                                                      
REMARK 465     PRO D   135                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ALA E   199                                                      
REMARK 465     ALA E   200                                                      
REMARK 465     ALA E   201                                                      
REMARK 465     GLU E   202                                                      
REMARK 465     SER E   203                                                      
REMARK 465     ARG E   204                                                      
REMARK 465     LYS E   205                                                      
REMARK 465     GLY E   206                                                      
REMARK 465     GLN E   207                                                      
REMARK 465     GLU E   208                                                      
REMARK 465     ARG E   209                                                      
REMARK 465     GLN F   129                                                      
REMARK 465     THR F   130                                                      
REMARK 465     ASP F   131                                                      
REMARK 465     VAL F   132                                                      
REMARK 465     ASP F   133                                                      
REMARK 465     HIS F   134                                                      
REMARK 465     PRO F   135                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ALA G   199                                                      
REMARK 465     ALA G   200                                                      
REMARK 465     ALA G   201                                                      
REMARK 465     GLU G   202                                                      
REMARK 465     SER G   203                                                      
REMARK 465     ARG G   204                                                      
REMARK 465     LYS G   205                                                      
REMARK 465     GLY G   206                                                      
REMARK 465     GLN G   207                                                      
REMARK 465     GLU G   208                                                      
REMARK 465     ARG G   209                                                      
REMARK 465     GLN H   129                                                      
REMARK 465     THR H   130                                                      
REMARK 465     ASP H   131                                                      
REMARK 465     VAL H   132                                                      
REMARK 465     ASP H   133                                                      
REMARK 465     HIS H   134                                                      
REMARK 465     PRO H   135                                                      
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    LEU G 174   CA  -  CB  -  CG  ANGL. DEV. =  14.6 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    ASP A 107      125.26     -2.28                                   
REMARK 500    THR A 109      -97.00    -64.28                                   
REMARK 500    GLN A 111      -57.90   -164.78                                   
REMARK 500    ASP C 107      120.66      5.38                                   
REMARK 500    THR C 109     -101.02    -63.25                                   
REMARK 500    GLN C 111      -62.51   -159.99                                   
REMARK 500    ASP C 133       40.14   -108.27                                   
REMARK 500    GLN E   3      -76.27   -142.80                                   
REMARK 500    SER E   4      100.53    -48.37                                   
REMARK 500    ASP E 107      123.79     -1.28                                   
REMARK 500    THR E 109      -94.46    -64.67                                   
REMARK 500    GLN E 111      -67.20   -163.50                                   
REMARK 500    ASP E 133       31.28    -99.09                                   
REMARK 500    PHE G 105     -159.51   -125.07                                   
REMARK 500    ASP G 107      120.38      7.87                                   
REMARK 500    THR G 109      -93.89    -64.89                                   
REMARK 500    GLN G 111      -64.81   -165.30                                   
REMARK 500    ASP G 133       44.27   -100.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2P1L A    1    26  UNP    Q07817   BCLX_HUMAN       1     26             
DBREF  2P1L C    1    26  UNP    Q07817   BCLX_HUMAN       1     26             
DBREF  2P1L E    1    26  UNP    Q07817   BCLX_HUMAN       1     26             
DBREF  2P1L G    1    26  UNP    Q07817   BCLX_HUMAN       1     26             
DBREF  2P1L A   83   209  UNP    Q07817   BCLX_HUMAN      83    209             
DBREF  2P1L C   83   209  UNP    Q07817   BCLX_HUMAN      83    209             
DBREF  2P1L E   83   209  UNP    Q07817   BCLX_HUMAN      83    209             
DBREF  2P1L G   83   209  UNP    Q07817   BCLX_HUMAN      83    209             
DBREF  2P1L B  107   135  UNP    Q14457   BCN1_HUMAN     107    135             
DBREF  2P1L D  107   135  UNP    Q14457   BCN1_HUMAN     107    135             
DBREF  2P1L F  107   135  UNP    Q14457   BCN1_HUMAN     107    135             
DBREF  2P1L H  107   135  UNP    Q14457   BCN1_HUMAN     107    135             
SEQADV 2P1L GLY B  105  UNP  Q14457              CLONING ARTIFACT               
SEQADV 2P1L SER B  106  UNP  Q14457              CLONING ARTIFACT               
SEQADV 2P1L GLY D  105  UNP  Q14457              CLONING ARTIFACT               
SEQADV 2P1L SER D  106  UNP  Q14457              CLONING ARTIFACT               
SEQADV 2P1L GLY F  105  UNP  Q14457              CLONING ARTIFACT               
SEQADV 2P1L SER F  106  UNP  Q14457              CLONING ARTIFACT               
SEQADV 2P1L GLY H  105  UNP  Q14457              CLONING ARTIFACT               
SEQADV 2P1L SER H  106  UNP  Q14457              CLONING ARTIFACT               
SEQRES   1 A  153  MET SER GLN SER ASN ARG GLU LEU VAL VAL ASP PHE LEU          
SEQRES   2 A  153  SER TYR LYS LEU SER GLN LYS GLY TYR SER TRP SER GLN          
SEQRES   3 A  153  MET ALA ALA VAL LYS GLN ALA LEU ARG GLU ALA GLY ASP          
SEQRES   4 A  153  GLU PHE GLU LEU ARG TYR ARG ARG ALA PHE SER ASP LEU          
SEQRES   5 A  153  THR SER GLN LEU HIS ILE THR PRO GLY THR ALA TYR GLN          
SEQRES   6 A  153  SER PHE GLU GLN VAL VAL ASN GLU LEU PHE ARG ASP GLY          
SEQRES   7 A  153  VAL ASN TRP GLY ARG ILE VAL ALA PHE PHE SER PHE GLY          
SEQRES   8 A  153  GLY ALA LEU CYS VAL GLU SER VAL ASP LYS GLU MET GLN          
SEQRES   9 A  153  VAL LEU VAL SER ARG ILE ALA ALA TRP MET ALA THR TYR          
SEQRES  10 A  153  LEU ASN ASP HIS LEU GLU PRO TRP ILE GLN GLU ASN GLY          
SEQRES  11 A  153  GLY TRP ASP THR PHE VAL GLU LEU TYR GLY ASN ASN ALA          
SEQRES  12 A  153  ALA ALA GLU SER ARG LYS GLY GLN GLU ARG                      
SEQRES   1 B   31  GLY SER GLY THR MET GLU ASN LEU SER ARG ARG LEU LYS          
SEQRES   2 B   31  VAL THR GLY ASP LEU PHE ASP ILE MET SER GLY GLN THR          
SEQRES   3 B   31  ASP VAL ASP HIS PRO                                          
SEQRES   1 C  153  MET SER GLN SER ASN ARG GLU LEU VAL VAL ASP PHE LEU          
SEQRES   2 C  153  SER TYR LYS LEU SER GLN LYS GLY TYR SER TRP SER GLN          
SEQRES   3 C  153  MET ALA ALA VAL LYS GLN ALA LEU ARG GLU ALA GLY ASP          
SEQRES   4 C  153  GLU PHE GLU LEU ARG TYR ARG ARG ALA PHE SER ASP LEU          
SEQRES   5 C  153  THR SER GLN LEU HIS ILE THR PRO GLY THR ALA TYR GLN          
SEQRES   6 C  153  SER PHE GLU GLN VAL VAL ASN GLU LEU PHE ARG ASP GLY          
SEQRES   7 C  153  VAL ASN TRP GLY ARG ILE VAL ALA PHE PHE SER PHE GLY          
SEQRES   8 C  153  GLY ALA LEU CYS VAL GLU SER VAL ASP LYS GLU MET GLN          
SEQRES   9 C  153  VAL LEU VAL SER ARG ILE ALA ALA TRP MET ALA THR TYR          
SEQRES  10 C  153  LEU ASN ASP HIS LEU GLU PRO TRP ILE GLN GLU ASN GLY          
SEQRES  11 C  153  GLY TRP ASP THR PHE VAL GLU LEU TYR GLY ASN ASN ALA          
SEQRES  12 C  153  ALA ALA GLU SER ARG LYS GLY GLN GLU ARG                      
SEQRES   1 D   31  GLY SER GLY THR MET GLU ASN LEU SER ARG ARG LEU LYS          
SEQRES   2 D   31  VAL THR GLY ASP LEU PHE ASP ILE MET SER GLY GLN THR          
SEQRES   3 D   31  ASP VAL ASP HIS PRO                                          
SEQRES   1 E  153  MET SER GLN SER ASN ARG GLU LEU VAL VAL ASP PHE LEU          
SEQRES   2 E  153  SER TYR LYS LEU SER GLN LYS GLY TYR SER TRP SER GLN          
SEQRES   3 E  153  MET ALA ALA VAL LYS GLN ALA LEU ARG GLU ALA GLY ASP          
SEQRES   4 E  153  GLU PHE GLU LEU ARG TYR ARG ARG ALA PHE SER ASP LEU          
SEQRES   5 E  153  THR SER GLN LEU HIS ILE THR PRO GLY THR ALA TYR GLN          
SEQRES   6 E  153  SER PHE GLU GLN VAL VAL ASN GLU LEU PHE ARG ASP GLY          
SEQRES   7 E  153  VAL ASN TRP GLY ARG ILE VAL ALA PHE PHE SER PHE GLY          
SEQRES   8 E  153  GLY ALA LEU CYS VAL GLU SER VAL ASP LYS GLU MET GLN          
SEQRES   9 E  153  VAL LEU VAL SER ARG ILE ALA ALA TRP MET ALA THR TYR          
SEQRES  10 E  153  LEU ASN ASP HIS LEU GLU PRO TRP ILE GLN GLU ASN GLY          
SEQRES  11 E  153  GLY TRP ASP THR PHE VAL GLU LEU TYR GLY ASN ASN ALA          
SEQRES  12 E  153  ALA ALA GLU SER ARG LYS GLY GLN GLU ARG                      
SEQRES   1 F   31  GLY SER GLY THR MET GLU ASN LEU SER ARG ARG LEU LYS          
SEQRES   2 F   31  VAL THR GLY ASP LEU PHE ASP ILE MET SER GLY GLN THR          
SEQRES   3 F   31  ASP VAL ASP HIS PRO                                          
SEQRES   1 G  153  MET SER GLN SER ASN ARG GLU LEU VAL VAL ASP PHE LEU          
SEQRES   2 G  153  SER TYR LYS LEU SER GLN LYS GLY TYR SER TRP SER GLN          
SEQRES   3 G  153  MET ALA ALA VAL LYS GLN ALA LEU ARG GLU ALA GLY ASP          
SEQRES   4 G  153  GLU PHE GLU LEU ARG TYR ARG ARG ALA PHE SER ASP LEU          
SEQRES   5 G  153  THR SER GLN LEU HIS ILE THR PRO GLY THR ALA TYR GLN          
SEQRES   6 G  153  SER PHE GLU GLN VAL VAL ASN GLU LEU PHE ARG ASP GLY          
SEQRES   7 G  153  VAL ASN TRP GLY ARG ILE VAL ALA PHE PHE SER PHE GLY          
SEQRES   8 G  153  GLY ALA LEU CYS VAL GLU SER VAL ASP LYS GLU MET GLN          
SEQRES   9 G  153  VAL LEU VAL SER ARG ILE ALA ALA TRP MET ALA THR TYR          
SEQRES  10 G  153  LEU ASN ASP HIS LEU GLU PRO TRP ILE GLN GLU ASN GLY          
SEQRES  11 G  153  GLY TRP ASP THR PHE VAL GLU LEU TYR GLY ASN ASN ALA          
SEQRES  12 G  153  ALA ALA GLU SER ARG LYS GLY GLN GLU ARG                      
SEQRES   1 H   31  GLY SER GLY THR MET GLU ASN LEU SER ARG ARG LEU LYS          
SEQRES   2 H   31  VAL THR GLY ASP LEU PHE ASP ILE MET SER GLY GLN THR          
SEQRES   3 H   31  ASP VAL ASP HIS PRO                                          
FORMUL   9  HOH   *16(H2 O)                                                     
HELIX    1   1 SER A    2  GLN A   19  1                                  18    
HELIX    2   2 SER A   25  ARG A  103  1                                  23    
HELIX    3   3 THR A  115  PHE A  131  1                                  17    
HELIX    4   4 ASN A  136  LYS A  157  1                                  22    
HELIX    5   5 VAL A  161  LEU A  178  1                                  18    
HELIX    6   6 LEU A  178  ASN A  185  1                                   8    
HELIX    7   7 GLY A  186  GLY A  196  1                                  11    
HELIX    8   8 SER B  106  MET B  126  1                                  21    
HELIX    9   9 SER C    2  GLN C   19  1                                  18    
HELIX   10  10 SER C   25  ARG C  103  1                                  23    
HELIX   11  11 THR C  118  ARG C  132  1                                  15    
HELIX   12  12 ASN C  136  LYS C  157  1                                  22    
HELIX   13  13 VAL C  161  LEU C  178  1                                  18    
HELIX   14  14 LEU C  178  ASN C  185  1                                   8    
HELIX   15  15 GLY C  186  GLY C  196  1                                  11    
HELIX   16  16 SER D  106  MET D  126  1                                  21    
HELIX   17  17 SER E    4  GLN E   19  1                                  16    
HELIX   18  18 SER E   25  ARG E  103  1                                  23    
HELIX   19  19 THR E  118  PHE E  131  1                                  14    
HELIX   20  20 ASN E  136  LYS E  157  1                                  22    
HELIX   21  21 VAL E  161  LEU E  178  1                                  18    
HELIX   22  22 LEU E  178  ASN E  185  1                                   8    
HELIX   23  23 GLY E  186  GLY E  196  1                                  11    
HELIX   24  24 SER F  106  MET F  126  1                                  21    
HELIX   25  25 SER G    2  GLN G   19  1                                  18    
HELIX   26  26 SER G   25  ARG G  103  1                                  23    
HELIX   27  27 THR G  118  PHE G  131  1                                  14    
HELIX   28  28 ASN G  136  LYS G  157  1                                  22    
HELIX   29  29 GLN G  160  LEU G  178  1                                  19    
HELIX   30  30 LEU G  178  ASN G  185  1                                   8    
HELIX   31  31 GLY G  186  GLY G  196  1                                  11    
HELIX   32  32 SER H  106  MET H  126  1                                  21    
CRYST1  107.940  110.590  100.520  90.00  90.00  90.00 P 21 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      0.009264  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009042  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009948        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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