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Database: PDB
Entry: 2I0E
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HEADER    TRANSFERASE                             10-AUG-06   2I0E              
TITLE     STRUCTURE OF CATALYTIC DOMAIN OF HUMAN PROTEIN KINASE C               
TITLE    2 BETA II COMPLEXED WITH A BISINDOLYLMALEIMIDE INHIBITOR               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN KINASE C-BETA II;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 321-673;                        
COMPND   5 EC: 2.7.11.13;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PACSG2                                    
KEYWDS    PROTEIN KINASE C BETA II, PROTEIN KINASE C,                           
KEYWDS   2 SERINE/THREONINE PROTEIN KINASE, TRANSFERASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.B.GRODSKY,R.L.LOVE                                                  
REVDAT   3   24-FEB-09 2I0E    1       VERSN                                    
REVDAT   2   05-DEC-06 2I0E    1       JRNL                                     
REVDAT   1   14-NOV-06 2I0E    0                                                
JRNL        AUTH   N.GRODSKY,Y.LI,D.BOUZIDA,R.LOVE,J.JENSEN,B.NODES,            
JRNL        AUTH 2 J.NONOMIYA,S.GRANT                                           
JRNL        TITL   STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN PROTEIN           
JRNL        TITL 2 KINASE C BETA II COMPLEXED WITH A                            
JRNL        TITL 3 BISINDOLYLMALEIMIDE INHIBITOR                                
JRNL        REF    BIOCHEMISTRY                  V.  45 13970 2006              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   17115692                                                     
JRNL        DOI    10.1021/BI061128H                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5                                             
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 31651                          
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) : 0.237                           
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.290                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 670                             
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2255                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 50                           
REMARK   3   BIN FREE R VALUE                    : 0.3640                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5112                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 115                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 65.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.40000                                              
REMARK   3    B22 (A**2) : -0.90000                                             
REMARK   3    B33 (A**2) : 0.50000                                              
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): 0.438         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.310         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.259         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.644        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5318 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7187 ; 1.329 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   627 ; 6.280 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   251 ;35.243 ;24.502       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   928 ;19.756 ;15.032       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;17.487 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   736 ; 0.106 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4043 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2383 ; 0.214 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3599 ; 0.314 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   182 ; 0.139 ; 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):    35 ; 0.275 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.146 ; 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):  3218 ; 0.556 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5058 ; 0.996 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2424 ; 1.055 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2129 ; 1.747 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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   : 1.20                                          
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 2I0E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB038979.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-SEP-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32375                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
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     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : 0.04900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.48400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: AKT-1                                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M ADA, 2.5 M SODIUM ACETATE, PH      
REMARK 280  6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 286K                
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       46.54900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       65.70850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       46.54900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       65.70850            
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                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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       93.09800            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      131.41700            
REMARK 350   BIOMT3   2  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     THR A   321                                                      
REMARK 465     THR A   322                                                      
REMARK 465     ASN A   323                                                      
REMARK 465     THR A   324                                                      
REMARK 465     VAL A   325                                                      
REMARK 465     SER A   326                                                      
REMARK 465     LYS A   327                                                      
REMARK 465     PHE A   328                                                      
REMARK 465     ASP A   329                                                      
REMARK 465     ASN A   330                                                      
REMARK 465     ASN A   331                                                      
REMARK 465     GLY A   332                                                      
REMARK 465     ASN A   333                                                      
REMARK 465     ARG A   334                                                      
REMARK 465     ASP A   335                                                      
REMARK 465     ARG A   336                                                      
REMARK 465     MET A   337                                                      
REMARK 465     LYS A   338                                                      
REMARK 465     ASN A   625                                                      
REMARK 465     ALA A   626                                                      
REMARK 465     GLU A   670                                                      
REMARK 465     VAL A   671                                                      
REMARK 465     LYS A   672                                                      
REMARK 465     SER A   673                                                      
REMARK 465     THR B   321                                                      
REMARK 465     THR B   322                                                      
REMARK 465     ASN B   323                                                      
REMARK 465     THR B   324                                                      
REMARK 465     VAL B   325                                                      
REMARK 465     SER B   326                                                      
REMARK 465     LYS B   327                                                      
REMARK 465     PHE B   328                                                      
REMARK 465     ASP B   329                                                      
REMARK 465     ASN B   330                                                      
REMARK 465     ASN B   331                                                      
REMARK 465     GLY B   332                                                      
REMARK 465     ASN B   333                                                      
REMARK 465     ARG B   334                                                      
REMARK 465     ASP B   335                                                      
REMARK 465     ARG B   336                                                      
REMARK 465     MET B   337                                                      
REMARK 465     LYS B   338                                                      
REMARK 465     CYS B   622                                                      
REMARK 465     GLY B   623                                                      
REMARK 465     ARG B   624                                                      
REMARK 465     ASN B   625                                                      
REMARK 465     ALA B   626                                                      
REMARK 465     GLU B   627                                                      
REMARK 465     ASN B   628                                                      
REMARK 465     PHE B   629                                                      
REMARK 465     ASP B   630                                                      
REMARK 465     ARG B   631                                                      
REMARK 465     PHE B   632                                                      
REMARK 465     PHE B   633                                                      
REMARK 465     THR B   634                                                      
REMARK 465     ARG B   635                                                      
REMARK 465     HIS B   636                                                      
REMARK 465     PRO B   637                                                      
REMARK 465     PRO B   638                                                      
REMARK 465     VAL B   639                                                      
REMARK 465     LEU B   640                                                      
REMARK 465     TPO B   641                                                      
REMARK 465     PRO B   642                                                      
REMARK 465     PRO B   643                                                      
REMARK 465     ASP B   644                                                      
REMARK 465     GLN B   645                                                      
REMARK 465     GLU B   646                                                      
REMARK 465     VAL B   647                                                      
REMARK 465     ILE B   648                                                      
REMARK 465     ARG B   649                                                      
REMARK 465     ASN B   650                                                      
REMARK 465     GLU B   670                                                      
REMARK 465     VAL B   671                                                      
REMARK 465     LYS B   672                                                      
REMARK 465     SER B   673                                                      
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    LYS A 362       93.22      3.81                                   
REMARK 500    ASP A 365       41.49    -94.19                                   
REMARK 500    ASP A 382       60.13     37.86                                   
REMARK 500    ASP A 466       33.64   -142.52                                   
REMARK 500    ASP A 484       88.95     68.91                                   
REMARK 500    PRO A 505      -54.88    -28.30                                   
REMARK 500    TYR A 515       26.16     43.14                                   
REMARK 500    MET A 576       30.39    -98.43                                   
REMARK 500    PRO A 643       97.04    -40.00                                   
REMARK 500    ASP A 652       93.20    -64.42                                   
REMARK 500    THR B 340       22.23    -73.22                                   
REMARK 500    LYS B 362       84.46     -9.02                                   
REMARK 500    ASP B 382       85.23     24.96                                   
REMARK 500    ARG B 465       -0.74     70.57                                   
REMARK 500    ASP B 484       90.26     74.87                                   
REMARK 500    TYR B 515       26.18     49.29                                   
REMARK 500    PRO B 561      151.08    -47.36                                   
REMARK 500    LYS B 573      -49.99    168.61                                   
REMARK 500    ASP B 652       98.13    -68.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A  461     ILE A  462                 -146.75                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A  19        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH B  17        DISTANCE =  6.57 ANGSTROMS                       
REMARK 525    HOH A  71        DISTANCE =  5.69 ANGSTROMS                       
REMARK 525    HOH A  73        DISTANCE =  5.24 ANGSTROMS                       
REMARK 525    HOH A  74        DISTANCE =  7.23 ANGSTROMS                       
REMARK 525    HOH A  80        DISTANCE =  6.42 ANGSTROMS                       
REMARK 525    HOH A  93        DISTANCE =  5.41 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDS A 901                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDS B 902                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 ACCORDING TO THE AUTHORS OF THE ENTRY, CONFLICTS ARISE               
REMARK 999 BETWEEN THEIR SEQUENCE AND THE UNP REFERENCE SEQUENCE                
REMARK 999 BECAUSE THEIR SEQUENCE IS OF PKC-BETAII AND THE UNP                  
REMARK 999 REFERENCE SEQUENCE IS OF PKC-BETAI.                                  
DBREF  2I0E A  321   670  UNP    P05771   KPCB_HUMAN     320    670             
DBREF  2I0E B  321   670  UNP    P05771   KPCB_HUMAN     320    670             
SEQADV 2I0E TPO A  500  UNP  P05771    THR   499 MODIFIED RESIDUE               
SEQADV 2I0E     A       UNP  P05771    ARG   621 SEE REMARK 999                 
SEQADV 2I0E CYS A  622  UNP  P05771    ASP   622 SEE REMARK 999                 
SEQADV 2I0E GLY A  623  UNP  P05771    LYS   623 SEE REMARK 999                 
SEQADV 2I0E ASN A  625  UNP  P05771    ASP   625 SEE REMARK 999                 
SEQADV 2I0E ALA A  626  UNP  P05771    THR   626 SEE REMARK 999                 
SEQADV 2I0E GLU A  627  UNP  P05771    SER   627 SEE REMARK 999                 
SEQADV 2I0E ARG A  631  UNP  P05771    LYS   631 SEE REMARK 999                 
SEQADV 2I0E PHE A  632  UNP  P05771    GLU   632 SEE REMARK 999                 
SEQADV 2I0E HIS A  636  UNP  P05771    GLN   636 SEE REMARK 999                 
SEQADV 2I0E PRO A  638  UNP  P05771    VAL   638 SEE REMARK 999                 
SEQADV 2I0E VAL A  639  UNP  P05771    GLU   639 SEE REMARK 999                 
SEQADV 2I0E TPO A  641  UNP  P05771    THR   641 MODIFIED RESIDUE               
SEQADV 2I0E PRO A  643  UNP  P05771    THR   643 SEE REMARK 999                 
SEQADV 2I0E GLN A  645  UNP  P05771    LYS   645 SEE REMARK 999                 
SEQADV 2I0E GLU A  646  UNP  P05771    LEU   646 SEE REMARK 999                 
SEQADV 2I0E VAL A  647  UNP  P05771    PHE   647 SEE REMARK 999                 
SEQADV 2I0E ARG A  649  UNP  P05771    MET   649 SEE REMARK 999                 
SEQADV 2I0E ILE A  651  UNP  P05771    LEU   651 SEE REMARK 999                 
SEQADV 2I0E SER A  654  UNP  P05771    ASN   654 SEE REMARK 999                 
SEQADV 2I0E GLU A  657  UNP  P05771    ALA   657 SEE REMARK 999                 
SEQADV 2I0E SEP A  660  UNP  P05771    SER   660 MODIFIED RESIDUE               
SEQADV 2I0E PHE A  661  UNP  P05771    TYR   661 SEE REMARK 999                 
SEQADV 2I0E VAL A  662  UNP  P05771    THR   662 SEE REMARK 999                 
SEQADV 2I0E SER A  664  UNP  P05771    PRO   664 SEE REMARK 999                 
SEQADV 2I0E LEU A  667  UNP  P05771    VAL   667 SEE REMARK 999                 
SEQADV 2I0E LYS A  668  UNP  P05771    ILE   668 SEE REMARK 999                 
SEQADV 2I0E PRO A  669  UNP  P05771    ASN   669 SEE REMARK 999                 
SEQADV 2I0E GLU A  670  UNP  P05771    VAL   670 SEE REMARK 999                 
SEQADV 2I0E VAL A  671  UNP  P05771              SEE REMARK 999                 
SEQADV 2I0E LYS A  672  UNP  P05771              SEE REMARK 999                 
SEQADV 2I0E SER A  673  UNP  P05771              SEE REMARK 999                 
SEQADV 2I0E TPO B  500  UNP  P05771    THR   499 MODIFIED RESIDUE               
SEQADV 2I0E     B       UNP  P05771    ARG   621 SEE REMARK 999                 
SEQADV 2I0E CYS B  622  UNP  P05771    ASP   622 SEE REMARK 999                 
SEQADV 2I0E GLY B  623  UNP  P05771    LYS   623 SEE REMARK 999                 
SEQADV 2I0E ASN B  625  UNP  P05771    ASP   625 SEE REMARK 999                 
SEQADV 2I0E ALA B  626  UNP  P05771    THR   626 SEE REMARK 999                 
SEQADV 2I0E GLU B  627  UNP  P05771    SER   627 SEE REMARK 999                 
SEQADV 2I0E ARG B  631  UNP  P05771    LYS   631 SEE REMARK 999                 
SEQADV 2I0E PHE B  632  UNP  P05771    GLU   632 SEE REMARK 999                 
SEQADV 2I0E HIS B  636  UNP  P05771    GLN   636 SEE REMARK 999                 
SEQADV 2I0E PRO B  638  UNP  P05771    VAL   638 SEE REMARK 999                 
SEQADV 2I0E VAL B  639  UNP  P05771    GLU   639 SEE REMARK 999                 
SEQADV 2I0E TPO B  641  UNP  P05771    THR   641 MODIFIED RESIDUE               
SEQADV 2I0E PRO B  643  UNP  P05771    THR   643 SEE REMARK 999                 
SEQADV 2I0E GLN B  645  UNP  P05771    LYS   645 SEE REMARK 999                 
SEQADV 2I0E GLU B  646  UNP  P05771    LEU   646 SEE REMARK 999                 
SEQADV 2I0E VAL B  647  UNP  P05771    PHE   647 SEE REMARK 999                 
SEQADV 2I0E ARG B  649  UNP  P05771    MET   649 SEE REMARK 999                 
SEQADV 2I0E ILE B  651  UNP  P05771    LEU   651 SEE REMARK 999                 
SEQADV 2I0E SER B  654  UNP  P05771    ASN   654 SEE REMARK 999                 
SEQADV 2I0E GLU B  657  UNP  P05771    ALA   657 SEE REMARK 999                 
SEQADV 2I0E SEP B  660  UNP  P05771    SER   660 MODIFIED RESIDUE               
SEQADV 2I0E PHE B  661  UNP  P05771    TYR   661 SEE REMARK 999                 
SEQADV 2I0E VAL B  662  UNP  P05771    THR   662 SEE REMARK 999                 
SEQADV 2I0E SER B  664  UNP  P05771    PRO   664 SEE REMARK 999                 
SEQADV 2I0E LEU B  667  UNP  P05771    VAL   667 SEE REMARK 999                 
SEQADV 2I0E LYS B  668  UNP  P05771    ILE   668 SEE REMARK 999                 
SEQADV 2I0E PRO B  669  UNP  P05771    ASN   669 SEE REMARK 999                 
SEQADV 2I0E GLU B  670  UNP  P05771    VAL   670 SEE REMARK 999                 
SEQADV 2I0E VAL B  671  UNP  P05771              SEE REMARK 999                 
SEQADV 2I0E LYS B  672  UNP  P05771              SEE REMARK 999                 
SEQADV 2I0E SER B  673  UNP  P05771              SEE REMARK 999                 
SEQRES   1 A  353  THR THR ASN THR VAL SER LYS PHE ASP ASN ASN GLY ASN          
SEQRES   2 A  353  ARG ASP ARG MET LYS LEU THR ASP PHE ASN PHE LEU MET          
SEQRES   3 A  353  VAL LEU GLY LYS GLY SER PHE GLY LYS VAL MET LEU SER          
SEQRES   4 A  353  GLU ARG LYS GLY THR ASP GLU LEU TYR ALA VAL LYS ILE          
SEQRES   5 A  353  LEU LYS LYS ASP VAL VAL ILE GLN ASP ASP ASP VAL GLU          
SEQRES   6 A  353  CYS THR MET VAL GLU LYS ARG VAL LEU ALA LEU PRO GLY          
SEQRES   7 A  353  LYS PRO PRO PHE LEU THR GLN LEU HIS SER CYS PHE GLN          
SEQRES   8 A  353  THR MET ASP ARG LEU TYR PHE VAL MET GLU TYR VAL ASN          
SEQRES   9 A  353  GLY GLY ASP LEU MET TYR HIS ILE GLN GLN VAL GLY ARG          
SEQRES  10 A  353  PHE LYS GLU PRO HIS ALA VAL PHE TYR ALA ALA GLU ILE          
SEQRES  11 A  353  ALA ILE GLY LEU PHE PHE LEU GLN SER LYS GLY ILE ILE          
SEQRES  12 A  353  TYR ARG ASP LEU LYS LEU ASP ASN VAL MET LEU ASP SER          
SEQRES  13 A  353  GLU GLY HIS ILE LYS ILE ALA ASP PHE GLY MET CYS LYS          
SEQRES  14 A  353  GLU ASN ILE TRP ASP GLY VAL THR THR LYS TPO PHE CYS          
SEQRES  15 A  353  GLY THR PRO ASP TYR ILE ALA PRO GLU ILE ILE ALA TYR          
SEQRES  16 A  353  GLN PRO TYR GLY LYS SER VAL ASP TRP TRP ALA PHE GLY          
SEQRES  17 A  353  VAL LEU LEU TYR GLU MET LEU ALA GLY GLN ALA PRO PHE          
SEQRES  18 A  353  GLU GLY GLU ASP GLU ASP GLU LEU PHE GLN SER ILE MET          
SEQRES  19 A  353  GLU HIS ASN VAL ALA TYR PRO LYS SER MET SER LYS GLU          
SEQRES  20 A  353  ALA VAL ALA ILE CYS LYS GLY LEU MET THR LYS HIS PRO          
SEQRES  21 A  353  GLY LYS ARG LEU GLY CYS GLY PRO GLU GLY GLU ARG ASP          
SEQRES  22 A  353  ILE LYS GLU HIS ALA PHE PHE ARG TYR ILE ASP TRP GLU          
SEQRES  23 A  353  LYS LEU GLU ARG LYS GLU ILE GLN PRO PRO TYR LYS PRO          
SEQRES  24 A  353  LYS ALA CYS GLY ARG ASN ALA GLU ASN PHE ASP ARG PHE          
SEQRES  25 A  353  PHE THR ARG HIS PRO PRO VAL LEU TPO PRO PRO ASP GLN          
SEQRES  26 A  353  GLU VAL ILE ARG ASN ILE ASP GLN SER GLU PHE GLU GLY          
SEQRES  27 A  353  PHE SEP PHE VAL ASN SER GLU PHE LEU LYS PRO GLU VAL          
SEQRES  28 A  353  LYS SER                                                      
SEQRES   1 B  353  THR THR ASN THR VAL SER LYS PHE ASP ASN ASN GLY ASN          
SEQRES   2 B  353  ARG ASP ARG MET LYS LEU THR ASP PHE ASN PHE LEU MET          
SEQRES   3 B  353  VAL LEU GLY LYS GLY SER PHE GLY LYS VAL MET LEU SER          
SEQRES   4 B  353  GLU ARG LYS GLY THR ASP GLU LEU TYR ALA VAL LYS ILE          
SEQRES   5 B  353  LEU LYS LYS ASP VAL VAL ILE GLN ASP ASP ASP VAL GLU          
SEQRES   6 B  353  CYS THR MET VAL GLU LYS ARG VAL LEU ALA LEU PRO GLY          
SEQRES   7 B  353  LYS PRO PRO PHE LEU THR GLN LEU HIS SER CYS PHE GLN          
SEQRES   8 B  353  THR MET ASP ARG LEU TYR PHE VAL MET GLU TYR VAL ASN          
SEQRES   9 B  353  GLY GLY ASP LEU MET TYR HIS ILE GLN GLN VAL GLY ARG          
SEQRES  10 B  353  PHE LYS GLU PRO HIS ALA VAL PHE TYR ALA ALA GLU ILE          
SEQRES  11 B  353  ALA ILE GLY LEU PHE PHE LEU GLN SER LYS GLY ILE ILE          
SEQRES  12 B  353  TYR ARG ASP LEU LYS LEU ASP ASN VAL MET LEU ASP SER          
SEQRES  13 B  353  GLU GLY HIS ILE LYS ILE ALA ASP PHE GLY MET CYS LYS          
SEQRES  14 B  353  GLU ASN ILE TRP ASP GLY VAL THR THR LYS TPO PHE CYS          
SEQRES  15 B  353  GLY THR PRO ASP TYR ILE ALA PRO GLU ILE ILE ALA TYR          
SEQRES  16 B  353  GLN PRO TYR GLY LYS SER VAL ASP TRP TRP ALA PHE GLY          
SEQRES  17 B  353  VAL LEU LEU TYR GLU MET LEU ALA GLY GLN ALA PRO PHE          
SEQRES  18 B  353  GLU GLY GLU ASP GLU ASP GLU LEU PHE GLN SER ILE MET          
SEQRES  19 B  353  GLU HIS ASN VAL ALA TYR PRO LYS SER MET SER LYS GLU          
SEQRES  20 B  353  ALA VAL ALA ILE CYS LYS GLY LEU MET THR LYS HIS PRO          
SEQRES  21 B  353  GLY LYS ARG LEU GLY CYS GLY PRO GLU GLY GLU ARG ASP          
SEQRES  22 B  353  ILE LYS GLU HIS ALA PHE PHE ARG TYR ILE ASP TRP GLU          
SEQRES  23 B  353  LYS LEU GLU ARG LYS GLU ILE GLN PRO PRO TYR LYS PRO          
SEQRES  24 B  353  LYS ALA CYS GLY ARG ASN ALA GLU ASN PHE ASP ARG PHE          
SEQRES  25 B  353  PHE THR ARG HIS PRO PRO VAL LEU TPO PRO PRO ASP GLN          
SEQRES  26 B  353  GLU VAL ILE ARG ASN ILE ASP GLN SER GLU PHE GLU GLY          
SEQRES  27 B  353  PHE SEP PHE VAL ASN SER GLU PHE LEU LYS PRO GLU VAL          
SEQRES  28 B  353  LYS SER                                                      
MODRES 2I0E TPO A  500  THR  PHOSPHOTHREONINE                                   
MODRES 2I0E TPO A  641  THR  PHOSPHOTHREONINE                                   
MODRES 2I0E SEP A  660  SER  PHOSPHOSERINE                                      
MODRES 2I0E TPO B  500  THR  PHOSPHOTHREONINE                                   
MODRES 2I0E SEP B  660  SER  PHOSPHOSERINE                                      
HET    TPO  A 500      11                                                       
HET    TPO  A 641      11                                                       
HET    SEP  A 660      10                                                       
HET    TPO  B 500      11                                                       
HET    SEP  B 660      10                                                       
HET    PDS  A 901      33                                                       
HET    PDS  B 902      33                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     PDS 3-{1-[3-(DIMETHYLAMINO)PROPYL]-2-METHYL-1H-INDOL-3-              
HETNAM   2 PDS  YL}-4-(2-METHYL-1H-INDOL-3-YL)-1H-PYRROLE-2,5-DIONE             
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    3(C4 H10 N O6 P)                                             
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   3  PDS    2(C27 H28 N4 O2)                                             
FORMUL   5  HOH   *115(H2 O)                                                    
HELIX    1   1 LYS A  375  ASP A  381  1                                   7    
HELIX    2   2 ASP A  383  ALA A  395  1                                  13    
HELIX    3   3 ASP A  427  GLY A  436  1                                  10    
HELIX    4   4 LYS A  439  LYS A  460  1                                  22    
HELIX    5   5 LYS A  468  ASP A  470  5                                   3    
HELIX    6   6 THR A  504  ILE A  508  5                                   5    
HELIX    7   7 ALA A  509  ALA A  514  1                                   6    
HELIX    8   8 LYS A  520  GLY A  537  1                                  18    
HELIX    9   9 ASP A  545  HIS A  556  1                                  12    
HELIX   10  10 SER A  565  MET A  576  1                                  12    
HELIX   11  11 GLU A  589  GLU A  596  1                                   8    
HELIX   12  12 HIS A  597  ARG A  601  5                                   5    
HELIX   13  13 ASP A  604  ARG A  610  1                                   7    
HELIX   14  14 GLU A  627  HIS A  636  1                                  10    
HELIX   15  15 ASP A  644  ILE A  651  1                                   8    
HELIX   16  16 LYS B  375  ASP B  382  1                                   8    
HELIX   17  17 ASP B  383  ALA B  395  1                                  13    
HELIX   18  18 ASP B  427  GLN B  434  1                                   8    
HELIX   19  19 LYS B  439  LYS B  460  1                                  22    
HELIX   20  20 LYS B  468  ASP B  470  5                                   3    
HELIX   21  21 ALA B  509  ALA B  514  1                                   6    
HELIX   22  22 LYS B  520  GLY B  537  1                                  18    
HELIX   23  23 ASP B  545  HIS B  556  1                                  12    
HELIX   24  24 SER B  565  LEU B  575  1                                  11    
HELIX   25  25 HIS B  579  ARG B  583  5                                   5    
HELIX   26  26 GLU B  589  GLU B  596  1                                   8    
HELIX   27  27 HIS B  597  ARG B  601  5                                   5    
HELIX   28  28 ASP B  604  ARG B  610  1                                   7    
HELIX   29  29 ASP B  652  GLU B  657  5                                   6    
SHEET    1   A 6 PHE A 342  GLY A 351  0                                        
SHEET    2   A 6 GLY A 354  ARG A 361 -1  O  VAL A 356   N  LEU A 348           
SHEET    3   A 6 THR A 364  LYS A 374 -1  O  ILE A 372   N  LYS A 355           
SHEET    4   A 6 ARG A 415  GLU A 421 -1  O  LEU A 416   N  LEU A 373           
SHEET    5   A 6 LEU A 406  GLN A 411 -1  N  HIS A 407   O  VAL A 419           
SHEET    6   A 6 PHE A 661  VAL A 662 -1  O  PHE A 661   N  CYS A 409           
SHEET    1   B 2 VAL A 472  LEU A 474  0                                        
SHEET    2   B 2 ILE A 480  ILE A 482 -1  O  LYS A 481   N  MET A 473           
SHEET    1   C 6 PHE B 342  GLY B 351  0                                        
SHEET    2   C 6 GLY B 354  ARG B 361 -1  O  GLY B 354   N  GLY B 351           
SHEET    3   C 6 LEU B 367  LYS B 374 -1  O  ILE B 372   N  LYS B 355           
SHEET    4   C 6 ARG B 415  GLU B 421 -1  O  LEU B 416   N  LEU B 373           
SHEET    5   C 6 LEU B 406  THR B 412 -1  N  THR B 412   O  ARG B 415           
SHEET    6   C 6 PHE B 661  VAL B 662 -1  O  PHE B 661   N  CYS B 409           
SHEET    1   D 2 VAL B 472  LEU B 474  0                                        
SHEET    2   D 2 ILE B 480  ILE B 482 -1  O  LYS B 481   N  MET B 473           
LINK         C   LYS A 499                 N   TPO A 500     1555   1555  1.33  
LINK         C   TPO A 500                 N   PHE A 501     1555   1555  1.33  
LINK         C   LEU A 640                 N   TPO A 641     1555   1555  1.34  
LINK         C   TPO A 641                 N   PRO A 642     1555   1555  1.35  
LINK         C   PHE A 659                 N   SEP A 660     1555   1555  1.33  
LINK         C   SEP A 660                 N   PHE A 661     1555   1555  1.33  
LINK         C   LYS B 499                 N   TPO B 500     1555   1555  1.33  
LINK         C   TPO B 500                 N   PHE B 501     1555   1555  1.33  
LINK         C   PHE B 659                 N   SEP B 660     1555   1555  1.33  
LINK         C   SEP B 660                 N   PHE B 661     1555   1555  1.33  
SITE     1 AC1 14 HOH A  57  LEU A 348  PHE A 353  VAL A 356                    
SITE     2 AC1 14 ALA A 369  THR A 404  GLU A 421  TYR A 422                    
SITE     3 AC1 14 VAL A 423  ASP A 470  ASN A 471  MET A 473                    
SITE     4 AC1 14 ALA A 483  ASP A 484                                          
SITE     1 AC2 13 HOH B  59  LEU B 348  VAL B 356  ALA B 369                    
SITE     2 AC2 13 THR B 404  MET B 420  GLU B 421  TYR B 422                    
SITE     3 AC2 13 VAL B 423  ASP B 470  ASN B 471  ALA B 483                    
SITE     4 AC2 13 ASP B 484                                                     
CRYST1   93.098  131.417   83.801  90.00  90.00  90.00 P 21 21 2     8          
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      0.010741  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007609  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011933        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system