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Database: PDB
Entry: 4X6R
LinkDB: 4X6R
Original site: 4X6R 
HEADER    TRANSFERASE                             09-DEC-14   4X6R              
TITLE     AN ISOFORM-SPECIFIC MYRISTYLATION SWITCH TARGETS RIIB PKA HOLOENZYMES 
TITLE    2 TO MEMBRANES                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PKA C-ALPHA;                                                
COMPND   5 EC: 2.7.11.11;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE I-ALPHA REGULATORY      
COMPND  10 SUBUNIT;                                                             
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PRKACA, PKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  10 ORGANISM_COMMON: BOVINE;                                             
SOURCE  11 ORGANISM_TAXID: 9913;                                                
SOURCE  12 GENE: PRKAR1A;                                                       
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PKA, MEMBRANE BINDING, MOLECULAR SWITCH, TRANSFERASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.ZHANG,F.YE,A.C.BASTIDAS,A.P.KORNEV,M.H.GINSBERG,J.WU,S.S.TAYLOR     
REVDAT   7   24-JUN-20 4X6R    1       LINK                                     
REVDAT   6   25-DEC-19 4X6R    1       REMARK                                   
REVDAT   5   20-SEP-17 4X6R    1       JRNL   REMARK                            
REVDAT   4   16-SEP-15 4X6R    1       JRNL                                     
REVDAT   3   02-SEP-15 4X6R    1       JRNL                                     
REVDAT   2   26-AUG-15 4X6R    1       REMARK                                   
REVDAT   1   22-JUL-15 4X6R    0                                                
JRNL        AUTH   P.ZHANG,F.YE,A.C.BASTIDAS,A.P.KORNEV,J.WU,M.H.GINSBERG,      
JRNL        AUTH 2 S.S.TAYLOR                                                   
JRNL        TITL   AN ISOFORM-SPECIFIC MYRISTYLATION SWITCH TARGETS TYPE II PKA 
JRNL        TITL 2 HOLOENZYMES TO MEMBRANES.                                    
JRNL        REF    STRUCTURE                     V.  23  1563 2015              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   26278174                                                     
JRNL        DOI    10.1016/J.STR.2015.07.007                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 62.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.600                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2575                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 62.9016 -  6.2880    1.00     2841   143  0.1834 0.2210        
REMARK   3     2  6.2880 -  4.9916    1.00     2734   158  0.1792 0.2304        
REMARK   3     3  4.9916 -  4.3608    1.00     2698   144  0.1430 0.1872        
REMARK   3     4  4.3608 -  3.9622    1.00     2688   165  0.1463 0.2023        
REMARK   3     5  3.9622 -  3.6782    1.00     2697   146  0.1616 0.2156        
REMARK   3     6  3.6782 -  3.4614    1.00     2648   152  0.1823 0.2081        
REMARK   3     7  3.4614 -  3.2880    1.00     2678   142  0.1963 0.2497        
REMARK   3     8  3.2880 -  3.1449    1.00     2646   128  0.1999 0.2464        
REMARK   3     9  3.1449 -  3.0238    1.00     2683   151  0.2002 0.2552        
REMARK   3    10  3.0238 -  2.9195    1.00     2661   132  0.2032 0.2687        
REMARK   3    11  2.9195 -  2.8282    1.00     2654   146  0.2098 0.2900        
REMARK   3    12  2.8282 -  2.7474    1.00     2671   137  0.2166 0.2788        
REMARK   3    13  2.7474 -  2.6750    1.00     2645   134  0.2088 0.2635        
REMARK   3    14  2.6750 -  2.6098    1.00     2660   145  0.2215 0.3136        
REMARK   3    15  2.6098 -  2.5504    1.00     2636   126  0.2284 0.2452        
REMARK   3    16  2.5504 -  2.4962    1.00     2673   149  0.2342 0.3054        
REMARK   3    17  2.4962 -  2.4462    1.00     2615   140  0.2307 0.3040        
REMARK   3    18  2.4462 -  2.4001    1.00     2681   137  0.2293 0.2952        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 43.35                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.660           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.88910                                              
REMARK   3    B22 (A**2) : 1.88910                                              
REMARK   3    B33 (A**2) : -3.77820                                             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.022           5389                                  
REMARK   3   ANGLE     :  1.857           7277                                  
REMARK   3   CHIRALITY :  0.133            769                                  
REMARK   3   PLANARITY :  0.010            927                                  
REMARK   3   DIHEDRAL  : 17.822           2029                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4X6R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000205186.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 1                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48209                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 63.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION OF RIB(91-379,R333K):    
REMARK 280  MYRC(K7C) HETERODIMER :RC HETERODIMER THAT WAS CONCENTRATED TO      
REMARK 280  14 MG/ML AND SCREENED AGAINST DIFFERENT AMMONIUM SULFATE            
REMARK 280  CONCENTRATIONS RANGING FROM 0.8-2.5 M IN 0.1 M SODIUM CITRATE       
REMARK 280  BUFFER AND ALSO VARYING THE PH FROM 5.0-6.0 USING THE HANGING       
REMARK 280  DROP VAPOR DIFFUSION METHOD. THE CRYSTAL USED FOR STRUCTURE         
REMARK 280  DETERMINATION WAS OBTAINED FROM A 4 UL DROP CONTAINING 1:1          
REMARK 280  PROTEIN TO WELL SOLUTION WITH THE WELL SOLUTION CONTAINING 1.6 M    
REMARK 280  AMMONIUM SULFATE AND 0.1 M SODIUM CITRATE AT PH 5.5, BATCH MODE,    
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       93.92067            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       46.96033            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       46.96033            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       93.92067            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN A   2    CG   OD1  ND2                                       
REMARK 470     CYS A   7    SG                                                  
REMARK 470     LYS A   8    CG   CD   CE   NZ                                   
REMARK 470     ARG A 256    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     LYS A 319    CG   CD   CE   NZ                                   
REMARK 470     ASN B 307    CG   OD1  ND2                                       
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   O    HOH B   524     O    HOH B   528              1.87            
REMARK 500   O    HOH A   643     O    HOH A   644              1.98            
REMARK 500   O    HOH A   640     O    HOH A   641              1.99            
REMARK 500   O    SER A   252     O    HOH A   613              2.04            
REMARK 500   O    HOH B   501     O    HOH B   514              2.05            
REMARK 500   O    HOH A   616     O    HOH B   529              2.09            
REMARK 500   O    HOH A   631     O    HOH A   633              2.14            
REMARK 500   O    HOH B   619     O    HOH B   620              2.16            
REMARK 500   N    GLY A     1     O1   MYR A   405              2.16            
REMARK 500   O    HOH A   634     O    HOH A   635              2.16            
REMARK 500   O2P  SEP A   139     O    HOH A   592              2.17            
REMARK 500   O    HOH A   524     O    HOH A   525              2.19            
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   O    HOH B   501     O    HOH B   527     6555     2.10            
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    ARG B  93   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS A   7     -124.79     64.73                                   
REMARK 500    ALA A  38     -169.14   -161.53                                   
REMARK 500    ILE A  46      -63.87    -93.32                                   
REMARK 500    ARG A 165       -7.87     77.67                                   
REMARK 500    ASP A 184       79.91     64.18                                   
REMARK 500    ASN B 186       -1.23     73.57                                   
REMARK 500    GLU B 308      177.48    171.90                                   
REMARK 500    SER B 319       -9.75     85.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLY A 136        -11.17                                           
REMARK 500    LEU A 273         13.08                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 407  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 171   OD1                                                    
REMARK 620 2 ATP A 402   O2G 102.6                                              
REMARK 620 3 ATP A 402   O2A  86.6 108.0                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TAM A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MYR A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 407                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 408                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 405                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4X6Q   RELATED DB: PDB                                   
DBREF  4X6R A    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  4X6R B   90   379  UNP    P00514   KAP0_BOVIN      91    380             
SEQADV 4X6R CYS A    7  UNP  P05132    LYS     8 ENGINEERED MUTATION            
SEQADV 4X6R LYS B  333  UNP  P00514    ARG   334 ENGINEERED MUTATION            
SEQRES   1 A  350  GLY ASN ALA ALA ALA ALA CYS LYS GLY SER GLU GLN GLU          
SEQRES   2 A  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 A  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 A  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 A  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 A  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 A  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 A  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 A  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 A  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 A  350  HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU PRO HIS ALA          
SEQRES  12 A  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 A  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 A  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 A  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 A  350  TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 A  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 A  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 A  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 A  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 A  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 A  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 A  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 A  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 A  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 A  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 A  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
SEQRES   1 B  290  LYS GLY ARG ARG ARG ARG GLY ALA ILE SER ALA GLU VAL          
SEQRES   2 B  290  TYR THR GLU GLU ASP ALA ALA SER TYR VAL ARG LYS VAL          
SEQRES   3 B  290  ILE PRO LYS ASP TYR LYS THR MET ALA ALA LEU ALA LYS          
SEQRES   4 B  290  ALA ILE GLU LYS ASN VAL LEU PHE SER HIS LEU ASP ASP          
SEQRES   5 B  290  ASN GLU ARG SER ASP ILE PHE ASP ALA MET PHE PRO VAL          
SEQRES   6 B  290  SER PHE ILE ALA GLY GLU THR VAL ILE GLN GLN GLY ASP          
SEQRES   7 B  290  GLU GLY ASP ASN PHE TYR VAL ILE ASP GLN GLY GLU MET          
SEQRES   8 B  290  ASP VAL TYR VAL ASN ASN GLU TRP ALA THR SER VAL GLY          
SEQRES   9 B  290  GLU GLY GLY SER PHE GLY GLU LEU ALA LEU ILE TYR GLY          
SEQRES  10 B  290  THR PRO ARG ALA ALA THR VAL LYS ALA LYS THR ASN VAL          
SEQRES  11 B  290  LYS LEU TRP GLY ILE ASP ARG ASP SER TYR ARG ARG ILE          
SEQRES  12 B  290  LEU MET GLY SER THR LEU ARG LYS ARG LYS MET TYR GLU          
SEQRES  13 B  290  GLU PHE LEU SER LYS VAL SER ILE LEU GLU SER LEU ASP          
SEQRES  14 B  290  LYS TRP GLU ARG LEU THR VAL ALA ASP ALA LEU GLU PRO          
SEQRES  15 B  290  VAL GLN PHE GLU ASP GLY GLN LYS ILE VAL VAL GLN GLY          
SEQRES  16 B  290  GLU PRO GLY ASP GLU PHE PHE ILE ILE LEU GLU GLY SER          
SEQRES  17 B  290  ALA ALA VAL LEU GLN ARG ARG SER GLU ASN GLU GLU PHE          
SEQRES  18 B  290  VAL GLU VAL GLY ARG LEU GLY PRO SER ASP TYR PHE GLY          
SEQRES  19 B  290  GLU ILE ALA LEU LEU MET ASN ARG PRO LYS ALA ALA THR          
SEQRES  20 B  290  VAL VAL ALA ARG GLY PRO LEU LYS CYS VAL LYS LEU ASP          
SEQRES  21 B  290  ARG PRO ARG PHE GLU ARG VAL LEU GLY PRO CYS SER ASP          
SEQRES  22 B  290  ILE LEU LYS ARG ASN ILE GLN GLN TYR ASN SER PHE VAL          
SEQRES  23 B  290  SER LEU SER VAL                                              
MODRES 4X6R SEP A  139  SER  MODIFIED RESIDUE                                   
MODRES 4X6R TPO A  197  THR  MODIFIED RESIDUE                                   
MODRES 4X6R SEP A  338  SER  MODIFIED RESIDUE                                   
HET    SEP  A 139      10                                                       
HET    TPO  A 197      11                                                       
HET    SEP  A 338      10                                                       
HET    SO4  A 401       5                                                       
HET    ATP  A 402      31                                                       
HET    TAM  A 403      11                                                       
HET    GOL  A 404       6                                                       
HET    MYR  A 405      15                                                       
HET    SO4  A 406       5                                                       
HET     MG  A 407       1                                                       
HET     MG  A 408       1                                                       
HET    SO4  B 401       5                                                       
HET    SO4  B 402       5                                                       
HET    SO4  B 403       5                                                       
HET    SO4  B 404       5                                                       
HET    GOL  B 405       6                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM     TAM TRIS(HYDROXYETHYL)AMINOMETHANE                                   
HETNAM     GOL GLYCEROL                                                         
HETNAM     MYR MYRISTIC ACID                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   3  SO4    6(O4 S 2-)                                                   
FORMUL   4  ATP    C10 H16 N5 O13 P3                                            
FORMUL   5  TAM    C7 H17 N O3                                                  
FORMUL   6  GOL    2(C3 H8 O3)                                                  
FORMUL   7  MYR    C14 H28 O2                                                   
FORMUL   9   MG    2(MG 2+)                                                     
FORMUL  16  HOH   *269(H2 O)                                                    
HELIX    1 AA1 CYS A    7  THR A   32  1                                  26    
HELIX    2 AA2 GLN A   39  ASP A   41  5                                   3    
HELIX    3 AA3 LYS A   76  LEU A   82  1                                   7    
HELIX    4 AA4 GLN A   84  VAL A   98  1                                  15    
HELIX    5 AA5 GLU A  127  GLY A  136  1                                  10    
HELIX    6 AA6 SEP A  139  LEU A  160  1                                  22    
HELIX    7 AA7 LYS A  168  GLU A  170  5                                   3    
HELIX    8 AA8 THR A  201  LEU A  205  5                                   5    
HELIX    9 AA9 ALA A  206  LEU A  211  1                                   6    
HELIX   10 AB1 LYS A  217  GLY A  234  1                                  18    
HELIX   11 AB2 GLN A  242  SER A  252  1                                  11    
HELIX   12 AB3 SER A  262  LEU A  273  1                                  12    
HELIX   13 AB4 VAL A  288  ASN A  293  1                                   6    
HELIX   14 AB5 HIS A  294  ALA A  298  5                                   5    
HELIX   15 AB6 ASP A  301  GLN A  307  1                                   7    
HELIX   16 AB7 THR B  104  SER B  110  1                                   7    
HELIX   17 AB8 ASP B  119  ILE B  130  1                                  12    
HELIX   18 AB9 ASN B  133  HIS B  138  1                                   6    
HELIX   19 AC1 ASP B  140  MET B  151  1                                  12    
HELIX   20 AC2 GLY B  199  ILE B  204  5                                   6    
HELIX   21 AC3 ARG B  226  LYS B  250  1                                  25    
HELIX   22 AC4 VAL B  251  GLU B  255  5                                   5    
HELIX   23 AC5 ASP B  258  LEU B  269  1                                  12    
HELIX   24 AC6 GLU B  324  MET B  329  1                                   6    
HELIX   25 AC7 ARG B  350  GLY B  358  1                                   9    
HELIX   26 AC8 PRO B  359  LYS B  365  1                                   7    
HELIX   27 AC9 ASN B  367  VAL B  375  1                                   9    
SHEET    1 AA1 5 PHE A  43  THR A  51  0                                        
SHEET    2 AA1 5 ARG A  56  HIS A  62 -1  O  VAL A  57   N  LEU A  49           
SHEET    3 AA1 5 HIS A  68  ASP A  75 -1  O  MET A  71   N  MET A  58           
SHEET    4 AA1 5 ASN A 115  GLU A 121 -1  O  MET A 120   N  ALA A  70           
SHEET    5 AA1 5 LEU A 106  LYS A 111 -1  N  PHE A 108   O  VAL A 119           
SHEET    1 AA2 2 LEU A 162  ILE A 163  0                                        
SHEET    2 AA2 2 LYS A 189  ARG A 190 -1  O  LYS A 189   N  ILE A 163           
SHEET    1 AA3 2 LEU A 172  ILE A 174  0                                        
SHEET    2 AA3 2 ILE A 180  VAL A 182 -1  O  GLN A 181   N  LEU A 173           
SHEET    1 AA4 2 CYS A 199  GLY A 200  0                                        
SHEET    2 AA4 2 ILE B  98  SER B  99 -1  O  ILE B  98   N  GLY A 200           
SHEET    1 AA5 4 PHE B 152  PHE B 156  0                                        
SHEET    2 AA5 4 VAL B 219  ASP B 225 -1  O  LEU B 221   N  VAL B 154           
SHEET    3 AA5 4 ASN B 171  GLN B 177 -1  N  VAL B 174   O  TRP B 222           
SHEET    4 AA5 4 SER B 197  PHE B 198 -1  O  PHE B 198   N  TYR B 173           
SHEET    1 AA6 4 THR B 161  ILE B 163  0                                        
SHEET    2 AA6 4 THR B 212  ALA B 215 -1  O  VAL B 213   N  ILE B 163           
SHEET    3 AA6 4 MET B 180  VAL B 184 -1  N  TYR B 183   O  THR B 212           
SHEET    4 AA6 4 GLU B 187  VAL B 192 -1  O  THR B 190   N  VAL B 182           
SHEET    1 AA7 4 GLU B 270  PHE B 274  0                                        
SHEET    2 AA7 4 THR B 336  ASP B 349 -1  O  LEU B 343   N  PHE B 274           
SHEET    3 AA7 4 GLU B 289  ARG B 303 -1  N  LEU B 294   O  LYS B 344           
SHEET    4 AA7 4 PHE B 310  LEU B 316 -1  O  GLY B 314   N  VAL B 300           
SHEET    1 AA8 4 LYS B 279  VAL B 281  0                                        
SHEET    2 AA8 4 THR B 336  ASP B 349 -1  O  VAL B 337   N  ILE B 280           
SHEET    3 AA8 4 GLU B 289  ARG B 303 -1  N  LEU B 294   O  LYS B 344           
SHEET    4 AA8 4 TYR B 321  PHE B 322 -1  O  PHE B 322   N  PHE B 291           
LINK         N   GLY A   1                 C1  MYR A 405     1555   1555  1.35  
LINK         C   PHE A 138                 N   SEP A 139     1555   1555  1.35  
LINK         C   SEP A 139                 N   GLU A 140     1555   1555  1.32  
LINK         OD1 ASN A 171                MG    MG A 407     1555   1555  2.41  
LINK         C   TRP A 196                 N   TPO A 197     1555   1555  1.33  
LINK         C   TPO A 197                 N   LEU A 198     1555   1555  1.31  
LINK         C   VAL A 337                 N   SEP A 338     1555   1555  1.32  
LINK         C   SEP A 338                 N   ILE A 339     1555   1555  1.33  
LINK         O2G ATP A 402                MG    MG A 407     1555   1555  2.72  
LINK         O2B ATP A 402                MG    MG A 408     1555   1555  2.46  
LINK         O2A ATP A 402                MG    MG A 407     1555   1555  2.27  
SITE     1 AC1  2 ARG A 137  HOH A 539                                          
SITE     1 AC2 25 GLY A  50  THR A  51  GLY A  52  SER A  53                    
SITE     2 AC2 25 PHE A  54  GLY A  55  VAL A  57  ALA A  70                    
SITE     3 AC2 25 LYS A  72  MET A 120  GLU A 121  VAL A 123                    
SITE     4 AC2 25 GLU A 127  ASP A 166  LYS A 168  GLU A 170                    
SITE     5 AC2 25 ASN A 171  LEU A 173  THR A 183  ASP A 184                    
SITE     6 AC2 25 PHE A 327   MG A 407   MG A 408  ARG B  94                    
SITE     7 AC2 25 ALA B  97                                                     
SITE     1 AC3 10 LYS A 189  ARG A 194  THR A 195  TRP A 196                    
SITE     2 AC3 10 TPO A 197  TYR B 103  THR B 104  GLU B 105                    
SITE     3 AC3 10 GLU B 106  HOH B 610                                          
SITE     1 AC4  5 ASP A 329  TYR A 330  HOH A 560  HOH A 567                    
SITE     2 AC4  5 LYS B  90                                                     
SITE     1 AC5  7 GLY A   1  ASN A   2  PHE A  18  LEU A 152                    
SITE     2 AC5  7 GLU A 155  GLN A 307  LYS A 309                               
SITE     1 AC6  4 ARG A 194  ASN A 216  LYS A 217  HOH A 561                    
SITE     1 AC7  3 ASN A 171  ASP A 184  ATP A 402                               
SITE     1 AC8  3 PHE A  54  ASP A 184  ATP A 402                               
SITE     1 AC9 11 PHE B 322  GLY B 323  GLU B 324  ILE B 325                    
SITE     2 AC9 11 HOH B 548  HOH B 550  HOH B 551  HOH B 579                    
SITE     3 AC9 11 HOH B 582  HOH B 619  HOH B 621                               
SITE     1 AD1  5 PRO A 258  SER A 259  GLN B 283  GLY B 284                    
SITE     2 AD1  5 ARG B 303                                                     
SITE     1 AD2  7 ILE B 163  GLY B 169  ASP B 170  ASN B 171                    
SITE     2 AD2  7 TYR B 173  ARG B 209  HOH B 567                               
SITE     1 AD3  6 ARG B  93  MET B 329  ASN B 330  ARG B 350                    
SITE     2 AD3  6 HOH B 505  HOH B 509                                          
SITE     1 AD4  6 LYS A  83  SER B  99  ALA B 100  GLU B 101                    
SITE     2 AD4  6 GLY B 206  ARG B 226                                          
CRYST1  125.760  125.760  140.881  90.00  90.00 120.00 P 32 2 1      6          
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      0.007952  0.004591  0.000000        0.00000                         
SCALE2      0.000000  0.009182  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007098        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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