GenomeNet

Database: PDB
Entry: 2A26
LinkDB: 2A26
Original site: 2A26 
HEADER    APOPTOSIS                               21-JUN-05   2A26              
TITLE     CRYSTAL STRUCTURE OF THE N-TERMINAL, DIMERIZATION DOMAIN OF           
TITLE    2 SIAH INTERACTING PROTEIN                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALCYCLIN-BINDING PROTEIN;                                 
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN (RESIDUES 1-47);                         
COMPND   5 SYNONYM: CACYBP, HCACYBP, SIAH-INTERACTING PROTEIN, S100A6-          
COMPND   6 BINDING PROTEIN, PNAS-107;                                           
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CACYBP, S100A6BP, SIP;                                         
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: PET15B                                    
KEYWDS    HELICAL HAIRPIN, DIMERIZATION, APOPTOSIS                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.SANTELLI,M.LEONE,C.LI,T.FUKUSHIMA,N.E.PREECE,A.J.OLSON,             
AUTHOR   2 K.R.ELY,J.C.REED,M.PELLECCHIA,R.C.LIDDINGTON,S.MATSUZAWA             
REVDAT   3   24-FEB-09 2A26    1       VERSN                                    
REVDAT   2   18-OCT-05 2A26    1       JRNL                                     
REVDAT   1   09-AUG-05 2A26    0                                                
JRNL        AUTH   E.SANTELLI,M.LEONE,C.LI,T.FUKUSHIMA,N.E.PREECE,              
JRNL        AUTH 2 A.J.OLSON,K.R.ELY,J.C.REED,M.PELLECCHIA,                     
JRNL        AUTH 3 R.C.LIDDINGTON,S.MATSUZAWA                                   
JRNL        TITL   STRUCTURAL ANALYSIS OF SIAH1-SIAH-INTERACTING                
JRNL        TITL 2 PROTEIN INTERACTIONS AND INSIGHTS INTO THE                   
JRNL        TITL 3 ASSEMBLY OF AN E3 LIGASE MULTIPROTEIN COMPLEX                
JRNL        REF    J.BIOL.CHEM.                  V. 280 34278 2005              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16085652                                                     
JRNL        DOI    10.1074/JBC.M506707200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 50769                          
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 + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2568                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.23                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2735                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 149                          
REMARK   3   BIN FREE R VALUE                    : 0.2450                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1244                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 19                                      
REMARK   3   SOLVENT ATOMS            : 230                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.64000                                              
REMARK   3    B22 (A**2) : -0.38000                                             
REMARK   3    B33 (A**2) : -0.26000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.043         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.042         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.024         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.517         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1205 ; 0.017 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1607 ; 1.936 ; 2.003       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   150 ; 4.043 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   199 ; 0.110 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   803 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   572 ; 0.236 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   113 ; 0.175 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    64 ; 0.215 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    38 ; 0.180 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   752 ; 1.828 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1222 ; 2.859 ; 2.500       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   453 ; 3.409 ; 3.500       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   385 ; 4.770 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  1205 ; 1.690 ; 2.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   230 ; 5.421 ; 2.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  1203 ; 5.333 ; 2.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2A26 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB033398.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-02; 30-MAR-02               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 10.5                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SSRL; SSRL                         
REMARK 200  BEAMLINE                       : BL9-1; BL9-2                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.826533; 0.91833, 0.83208,        
REMARK 200                                   0.92014, 0.95369                   
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315; ADSC             
REMARK 200                                   QUANTUM 4                          
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50772                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -4.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 8.300                              
REMARK 200  R MERGE                    (I) : 0.04600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 65.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.22                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, CAPS, LITHIUM         
REMARK 280  SULPHATE, PH 10.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       18.49400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       18.49400            
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  1.000000  0.000000  0.000000       29.39650            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       76.30450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       29.39650            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       76.30450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       18.49400            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       29.39650            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       76.30450            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       18.49400            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       29.39650            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       76.30450            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 A DIMER COMPRISING CHAINS A       
REMARK 300 AND B. A SECOND DIMERIC BIOLOGICAL ASSEMBLY IS GENERATED BY          
REMARK 300 CHAIN C BY APPLYING THE TRANSFORMATIONS X, Y, Z AND -X, Y, 1/2-Z     
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: 2070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 6790 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 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 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       18.49400            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       18.49400            
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 C 120  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 129  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 133  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 134  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    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     GLN B    45                                                      
REMARK 465     GLN B    46                                                      
REMARK 465     LYS B    47                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     GLN C    45                                                      
REMARK 465     GLN C    46                                                      
REMARK 465     LYS C    47                                                      
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     MET A    1   CG    SD    CE                                      
REMARK 480     GLU A    4   CG    CD    OE1   OE2                               
REMARK 480     LYS A    8   CE    NZ                                            
REMARK 480     GLU A   11   CD    OE1   OE2                                     
REMARK 480     LYS A   23   CD    CE    NZ                                      
REMARK 480     ARG A   26   CZ    NH1   NH2                                     
REMARK 480     LYS A   41   CE    NZ                                            
REMARK 480     LYS A   47   CE    NZ                                            
REMARK 480     GLU B    4   CD    OE1   OE2                                     
REMARK 480     LYS B    8   CE    NZ                                            
REMARK 480     LYS B   23   CE    NZ                                            
REMARK 480     LYS B   41   CD    CE    NZ                                      
REMARK 480     MET B   44   CB    CG    SD    CE                                
REMARK 480     SER C    3   OG                                                  
REMARK 480     GLU C    4   CG    CD    OE1   OE2                               
REMARK 480     LYS C    8   CE    NZ                                            
REMARK 480     GLU C   11   CD    OE1   OE2                                     
REMARK 480     LYS C   14   NZ                                                  
REMARK 480     LYS C   19   CE    NZ                                            
REMARK 480     LYS C   33   CE    NZ                                            
REMARK 480     LYS C   41   CE    NZ                                            
REMARK 480     MET C   44   CB    CG    SD    CE                                
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A    11     O    HOH A   110              1.15            
REMARK 500   OE1  GLU A    11     O    HOH A   110              1.52            
REMARK 500   NZ   LYS B    23     O    HOH B   373              1.64            
REMARK 500   CD   GLU A    11     O    HOH A   110              1.86            
REMARK 500   OE2  GLU A     4     O    HOH A    92              2.05            
REMARK 500   N    SER B    -1     O    HOH B   380              2.08            
REMARK 500   O    HOH C    88     O    HOH C   123              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS A     8     O    HOH B   379     6554     2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MET A   1   CB    MET A   1   CG     -0.346                       
REMARK 500    ARG A  26   NE    ARG A  26   CZ     -0.120                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    MET A   1   CA  -  CB  -  CG  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    ARG A  26   CD  -  NE  -  CZ  ANGL. DEV. =  23.5 DEGREES          
REMARK 500    ARG A  26   NE  -  CZ  -  NH1 ANGL. DEV. = -19.1 DEGREES          
REMARK 500    ARG A  26   NE  -  CZ  -  NH2 ANGL. DEV. =  16.9 DEGREES          
REMARK 500    MET C  44   CB  -  CA  -  C   ANGL. DEV. = -13.9 DEGREES          
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 SO4 B 301                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CXS B 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2A25   RELATED DB: PDB                                   
DBREF  2A26 A    1    47  UNP    Q9HB71   CYBP_HUMAN       1     47             
DBREF  2A26 B    1    47  UNP    Q9HB71   CYBP_HUMAN       1     47             
DBREF  2A26 C    1    47  UNP    Q9HB71   CYBP_HUMAN       1     47             
SEQADV 2A26 GLY A   -2  UNP  Q9HB71              CLONING ARTIFACT               
SEQADV 2A26 SER A   -1  UNP  Q9HB71              CLONING ARTIFACT               
SEQADV 2A26 HIS A    0  UNP  Q9HB71              CLONING ARTIFACT               
SEQADV 2A26 GLY B   -2  UNP  Q9HB71              CLONING ARTIFACT               
SEQADV 2A26 SER B   -1  UNP  Q9HB71              CLONING ARTIFACT               
SEQADV 2A26 HIS B    0  UNP  Q9HB71              CLONING ARTIFACT               
SEQADV 2A26 GLY C   -2  UNP  Q9HB71              CLONING ARTIFACT               
SEQADV 2A26 SER C   -1  UNP  Q9HB71              CLONING ARTIFACT               
SEQADV 2A26 HIS C    0  UNP  Q9HB71              CLONING ARTIFACT               
SEQRES   1 A   50  GLY SER HIS MET ALA SER GLU GLU LEU GLN LYS ASP LEU          
SEQRES   2 A   50  GLU GLU VAL LYS VAL LEU LEU GLU LYS ALA THR ARG LYS          
SEQRES   3 A   50  ARG VAL ARG ASP ALA LEU THR ALA GLU LYS SER LYS ILE          
SEQRES   4 A   50  GLU THR GLU ILE LYS ASN LYS MET GLN GLN LYS                  
SEQRES   1 B   50  GLY SER HIS MET ALA SER GLU GLU LEU GLN LYS ASP LEU          
SEQRES   2 B   50  GLU GLU VAL LYS VAL LEU LEU GLU LYS ALA THR ARG LYS          
SEQRES   3 B   50  ARG VAL ARG ASP ALA LEU THR ALA GLU LYS SER LYS ILE          
SEQRES   4 B   50  GLU THR GLU ILE LYS ASN LYS MET GLN GLN LYS                  
SEQRES   1 C   50  GLY SER HIS MET ALA SER GLU GLU LEU GLN LYS ASP LEU          
SEQRES   2 C   50  GLU GLU VAL LYS VAL LEU LEU GLU LYS ALA THR ARG LYS          
SEQRES   3 C   50  ARG VAL ARG ASP ALA LEU THR ALA GLU LYS SER LYS ILE          
SEQRES   4 C   50  GLU THR GLU ILE LYS ASN LYS MET GLN GLN LYS                  
HET    SO4  B 301       5                                                       
HET    CXS  B 302      14                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     CXS 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID                               
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5  CXS    C9 H19 N O3 S                                                
FORMUL   6  HOH   *230(H2 O)                                                    
HELIX    1   1 ALA A    2  ALA A   20  1                                  19    
HELIX    2   2 ARG A   22  LYS A   47  1                                  26    
HELIX    3   3 ALA B    2  ALA B   20  1                                  19    
HELIX    4   4 ARG B   22  LYS B   43  1                                  22    
HELIX    5   5 ALA C    2  ALA C   20  1                                  19    
HELIX    6   6 ARG C   22  LYS C   43  1                                  22    
SITE     1 AC1  6 SER B   3  LYS B  43  HOH B 329  HOH B 355                    
SITE     2 AC1  6 HOH B 370  LYS C  23                                          
SITE     1 AC2  7 HOH A  68  GLU B  18  THR B  21  ARG B  26                    
SITE     2 AC2  7 HOH B 316  HOH B 357  HOH B 381                               
CRYST1   58.793  152.609   36.988  90.00  90.00  90.00 C 2 2 21     24          
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      0.017009  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006553  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.027036        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system