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Database: PDB
Entry: 2P9K
LinkDB: 2P9K
Original site: 2P9K 
HEADER    STRUCTURAL PROTEIN                      26-MAR-07   2P9K              
TITLE     CRYSTAL STRUCTURE OF BOVINE ARP2/3 COMPLEX CO-CRYSTALLIZED WITH ATP   
TITLE    2 AND CROSSLINKED WITH GLUTARALDEHYDE                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACTIN-LIKE PROTEIN 3;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ACTIN-RELATED PROTEIN 3;                                    
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ACTIN-LIKE PROTEIN 2;                                      
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: ACTIN-RELATED PROTEIN 2;                                    
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: ACTIN-RELATED PROTEIN 2/3 COMPLEX SUBUNIT 1B;              
COMPND  13 CHAIN: C;                                                            
COMPND  14 SYNONYM: ARP2/3 COMPLEX 41 KDA SUBUNIT, P41-ARC;                     
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: ACTIN-RELATED PROTEIN 2/3 COMPLEX SUBUNIT 2;               
COMPND  18 CHAIN: D;                                                            
COMPND  19 SYNONYM: ARP2/3 COMPLEX 34 KDA SUBUNIT, P34-ARC;                     
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 5;                                                           
COMPND  22 MOLECULE: ACTIN-RELATED PROTEIN 2/3 COMPLEX SUBUNIT 3;               
COMPND  23 CHAIN: E;                                                            
COMPND  24 SYNONYM: ARP2/3 COMPLEX 21 KDA SUBUNIT, P21-ARC;                     
COMPND  25 ENGINEERED: YES;                                                     
COMPND  26 MOL_ID: 6;                                                           
COMPND  27 MOLECULE: ACTIN-RELATED PROTEIN 2/3 COMPLEX SUBUNIT 4;               
COMPND  28 CHAIN: F;                                                            
COMPND  29 SYNONYM: ARP2/3 COMPLEX 20 KDA SUBUNIT, P20-ARC;                     
COMPND  30 ENGINEERED: YES;                                                     
COMPND  31 MOL_ID: 7;                                                           
COMPND  32 MOLECULE: ACTIN-RELATED PROTEIN 2/3 COMPLEX SUBUNIT 5;               
COMPND  33 CHAIN: G;                                                            
COMPND  34 SYNONYM: ARP2/3 COMPLEX 16 KDA SUBUNIT, P16-ARC;                     
COMPND  35 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 GENE: ACTR3;                                                         
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   8 ORGANISM_COMMON: CATTLE;                                             
SOURCE   9 ORGANISM_TAXID: 9913;                                                
SOURCE  10 GENE: ACTR2;                                                         
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  13 ORGANISM_COMMON: CATTLE;                                             
SOURCE  14 ORGANISM_TAXID: 9913;                                                
SOURCE  15 GENE: ARPC1B;                                                        
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  18 ORGANISM_COMMON: CATTLE;                                             
SOURCE  19 ORGANISM_TAXID: 9913;                                                
SOURCE  20 GENE: ARPC2;                                                         
SOURCE  21 MOL_ID: 5;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  23 ORGANISM_COMMON: CATTLE;                                             
SOURCE  24 ORGANISM_TAXID: 9913;                                                
SOURCE  25 GENE: ARPC3;                                                         
SOURCE  26 MOL_ID: 6;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  28 ORGANISM_COMMON: CATTLE;                                             
SOURCE  29 ORGANISM_TAXID: 9913;                                                
SOURCE  30 GENE: ARPC4;                                                         
SOURCE  31 MOL_ID: 7;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  33 ORGANISM_COMMON: CATTLE;                                             
SOURCE  34 ORGANISM_TAXID: 9913;                                                
SOURCE  35 GENE: ARPC5                                                          
KEYWDS    COMPLEX, ACTIN, WD REPEAT, STRUCTURAL PROTEIN                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.J.NOLEN,T.D.POLLARD                                                 
REVDAT   5   21-FEB-24 2P9K    1       REMARK SEQADV LINK                       
REVDAT   4   18-OCT-17 2P9K    1       REMARK                                   
REVDAT   3   24-MAR-09 2P9K    1       SOURCE DBREF                             
REVDAT   2   24-FEB-09 2P9K    1       VERSN                                    
REVDAT   1   29-MAY-07 2P9K    0                                                
JRNL        AUTH   B.J.NOLEN,T.D.POLLARD                                        
JRNL        TITL   INSIGHTS INTO THE INFLUENCE OF NUCLEOTIDES ON ACTIN FAMILY   
JRNL        TITL 2 PROTEINS FROM SEVEN STRUCTURES OF ARP2/3 COMPLEX.            
JRNL        REF    MOL.CELL                      V.  26   449 2007              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   17499050                                                     
JRNL        DOI    10.1016/J.MOLCEL.2007.04.017                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.59 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 84915                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4286                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13900                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 64                                      
REMARK   3   SOLVENT ATOMS            : 396                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.80000                                             
REMARK   3    B22 (A**2) : -4.05100                                             
REMARK   3    B33 (A**2) : 7.85100                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.339 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.294 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.004 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.037 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 21.31                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  3  : ATP.PARAM                                      
REMARK   3  PARAMETER FILE  4  : CNS_TOPPAR:WATER.PARAM                         
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2P9K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000042137.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.008                              
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 88027                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.580                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.58                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.030                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 7.5% PEG 3350, 50MM HEPES, 100MM KSCN,   
REMARK 280  10% SUCROSE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 278K, PH    
REMARK 280  7                                                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       55.31000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       99.14800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       64.02500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       99.14800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       55.31000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       64.02500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: HEPTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 21880 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 71150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -121.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G                   
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     SER A    40                                                      
REMARK 465     ALA A    41                                                      
REMARK 465     LYS A    42                                                      
REMARK 465     VAL A    43                                                      
REMARK 465     GLY A    44                                                      
REMARK 465     ASP A    45                                                      
REMARK 465     GLN A    46                                                      
REMARK 465     ALA A    47                                                      
REMARK 465     GLN A    48                                                      
REMARK 465     ARG A    49                                                      
REMARK 465     ARG A    50                                                      
REMARK 465     VAL A    51                                                      
REMARK 465     ARG A   156                                                      
REMARK 465     GLN A   157                                                      
REMARK 465     GLY A   355                                                      
REMARK 465     GLY A   356                                                      
REMARK 465     ARG A   357                                                      
REMARK 465     LEU A   358                                                      
REMARK 465     PHE A   414                                                      
REMARK 465     GLY A   415                                                      
REMARK 465     VAL A   416                                                      
REMARK 465     MET A   417                                                      
REMARK 465     SER A   418                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     VAL B     8                                                      
REMARK 465     LEU B    35                                                      
REMARK 465     VAL B    36                                                      
REMARK 465     GLY B    37                                                      
REMARK 465     ARG B    38                                                      
REMARK 465     PRO B    39                                                      
REMARK 465     ILE B    40                                                      
REMARK 465     ILE B    41                                                      
REMARK 465     ARG B    42                                                      
REMARK 465     SER B    43                                                      
REMARK 465     THR B    44                                                      
REMARK 465     THR B    45                                                      
REMARK 465     LYS B    46                                                      
REMARK 465     VAL B    47                                                      
REMARK 465     GLY B    48                                                      
REMARK 465     ASN B    49                                                      
REMARK 465     ILE B    50                                                      
REMARK 465     GLU B    51                                                      
REMARK 465     ILE B    52                                                      
REMARK 465     LYS B    53                                                      
REMARK 465     ASP B    54                                                      
REMARK 465     LEU B    55                                                      
REMARK 465     MET B    56                                                      
REMARK 465     VAL B    57                                                      
REMARK 465     GLY B    58                                                      
REMARK 465     ASP B    59                                                      
REMARK 465     GLU B    60                                                      
REMARK 465     ALA B    61                                                      
REMARK 465     SER B    62                                                      
REMARK 465     GLU B    63                                                      
REMARK 465     LEU B    64                                                      
REMARK 465     ARG B    65                                                      
REMARK 465     SER B    66                                                      
REMARK 465     MET B    67                                                      
REMARK 465     LEU B    68                                                      
REMARK 465     GLU B    69                                                      
REMARK 465     VAL B    70                                                      
REMARK 465     ASN B    71                                                      
REMARK 465     GLY B    77                                                      
REMARK 465     ILE B    78                                                      
REMARK 465     VAL B    79                                                      
REMARK 465     ARG B    80                                                      
REMARK 465     ASN B    81                                                      
REMARK 465     HIS B    87                                                      
REMARK 465     LEU B    88                                                      
REMARK 465     TRP B    89                                                      
REMARK 465     ASP B    90                                                      
REMARK 465     TYR B    91                                                      
REMARK 465     THR B    92                                                      
REMARK 465     PHE B    93                                                      
REMARK 465     GLY B    94                                                      
REMARK 465     PRO B    95                                                      
REMARK 465     GLU B    96                                                      
REMARK 465     LYS B    97                                                      
REMARK 465     LEU B    98                                                      
REMARK 465     ASN B    99                                                      
REMARK 465     ILE B   100                                                      
REMARK 465     ASP B   101                                                      
REMARK 465     THR B   102                                                      
REMARK 465     ARG B   103                                                      
REMARK 465     ASN B   104                                                      
REMARK 465     CYS B   105                                                      
REMARK 465     LYS B   106                                                      
REMARK 465     ILE B   107                                                      
REMARK 465     GLU B   121                                                      
REMARK 465     LYS B   122                                                      
REMARK 465     ILE B   123                                                      
REMARK 465     VAL B   124                                                      
REMARK 465     GLU B   125                                                      
REMARK 465     VAL B   126                                                      
REMARK 465     MET B   127                                                      
REMARK 465     PHE B   128                                                      
REMARK 465     GLU B   129                                                      
REMARK 465     THR B   130                                                      
REMARK 465     TYR B   131                                                      
REMARK 465     GLN B   132                                                      
REMARK 465     PHE B   133                                                      
REMARK 465     SER B   134                                                      
REMARK 465     GLY B   135                                                      
REMARK 465     VAL B   136                                                      
REMARK 465     TYR B   137                                                      
REMARK 465     VAL B   138                                                      
REMARK 465     MET B   365                                                      
REMARK 465     LYS B   366                                                      
REMARK 465     ASP B   367                                                      
REMARK 465     LYS B   368                                                      
REMARK 465     ASP B   369                                                      
REMARK 465     ASN B   370                                                      
REMARK 465     PHE B   371                                                      
REMARK 465     TRP B   372                                                      
REMARK 465     MET B   373                                                      
REMARK 465     THR B   374                                                      
REMARK 465     ARG B   375                                                      
REMARK 465     GLN B   376                                                      
REMARK 465     GLU B   377                                                      
REMARK 465     TYR B   378                                                      
REMARK 465     GLN B   379                                                      
REMARK 465     GLU B   380                                                      
REMARK 465     LYS B   381                                                      
REMARK 465     GLY B   382                                                      
REMARK 465     VAL B   383                                                      
REMARK 465     ARG B   384                                                      
REMARK 465     VAL B   385                                                      
REMARK 465     LEU B   386                                                      
REMARK 465     GLU B   387                                                      
REMARK 465     LYS B   388                                                      
REMARK 465     LEU B   389                                                      
REMARK 465     GLY B   390                                                      
REMARK 465     VAL B   391                                                      
REMARK 465     THR B   392                                                      
REMARK 465     VAL B   393                                                      
REMARK 465     ARG B   394                                                      
REMARK 465     MET C     1                                                      
REMARK 465     LYS C   289                                                      
REMARK 465     GLN C   290                                                      
REMARK 465     SER C   291                                                      
REMARK 465     SER C   292                                                      
REMARK 465     GLN C   293                                                      
REMARK 465     ARG C   294                                                      
REMARK 465     GLY C   295                                                      
REMARK 465     LEU C   296                                                      
REMARK 465     THR C   297                                                      
REMARK 465     ALA C   298                                                      
REMARK 465     ARG C   299                                                      
REMARK 465     GLU C   300                                                      
REMARK 465     ARG C   301                                                      
REMARK 465     PHE C   302                                                      
REMARK 465     GLN C   303                                                      
REMARK 465     ASN C   304                                                      
REMARK 465     LEU C   305                                                      
REMARK 465     ASP C   306                                                      
REMARK 465     LYS C   307                                                      
REMARK 465     LYS C   308                                                      
REMARK 465     ALA C   309                                                      
REMARK 465     SER C   310                                                      
REMARK 465     SER C   311                                                      
REMARK 465     GLU C   312                                                      
REMARK 465     GLY C   313                                                      
REMARK 465     SER C   314                                                      
REMARK 465     ALA C   315                                                      
REMARK 465     ALA C   316                                                      
REMARK 465     ALA C   317                                                      
REMARK 465     GLY C   318                                                      
REMARK 465     LEU D   207                                                      
REMARK 465     GLU D   208                                                      
REMARK 465     LEU D   209                                                      
REMARK 465     LYS D   210                                                      
REMARK 465     ASP D   211                                                      
REMARK 465     ASP D   283                                                      
REMARK 465     ALA D   284                                                      
REMARK 465     GLU D   285                                                      
REMARK 465     LYS D   286                                                      
REMARK 465     LYS D   287                                                      
REMARK 465     GLU D   288                                                      
REMARK 465     MET D   289                                                      
REMARK 465     LYS D   290                                                      
REMARK 465     THR D   291                                                      
REMARK 465     ILE D   292                                                      
REMARK 465     THR D   293                                                      
REMARK 465     GLY D   294                                                      
REMARK 465     LYS D   295                                                      
REMARK 465     THR D   296                                                      
REMARK 465     PHE D   297                                                      
REMARK 465     SER D   298                                                      
REMARK 465     SER D   299                                                      
REMARK 465     ARG D   300                                                      
REMARK 465     MET E     1                                                      
REMARK 465     PRO E   176                                                      
REMARK 465     GLY E   177                                                      
REMARK 465     GLN E   178                                                      
REMARK 465     MET F     1                                                      
REMARK 465     MET G     1                                                      
REMARK 465     SER G     2                                                      
REMARK 465     LYS G     3                                                      
REMARK 465     ASN G     4                                                      
REMARK 465     THR G     5                                                      
REMARK 465     VAL G     6                                                      
REMARK 465     SER G     7                                                      
REMARK 465     SER G     8                                                      
REMARK 465     ASP G    28                                                      
REMARK 465     ASP G    29                                                      
REMARK 465     GLY G    30                                                      
REMARK 465     GLY G    31                                                      
REMARK 465     ASP G    32                                                      
REMARK 465     GLY G    33                                                      
REMARK 465     GLN G    34                                                      
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     VAL B   9    CG1  CG2                                            
REMARK 470     VAL B  10    CG1  CG2                                            
REMARK 470     PHE B  17    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B  29    CG   CD   OE1  OE2                                  
REMARK 470     ILE B  31    CG1  CG2  CD1                                       
REMARK 470     TYR B  72    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B  75    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  83    CG   OD1  OD2                                       
REMARK 470     ASP B  84    CG   OD1  OD2                                       
REMARK 470     MET B  85    CG   SD   CE                                        
REMARK 470     LYS B  86    CG   CD   CE   NZ                                   
REMARK 470     LEU B 108    CG   CD1  CD2                                       
REMARK 470     LEU B 109    CG   CD1  CD2                                       
REMARK 470     THR B 110    OG1  CG2                                            
REMARK 470     GLU B 111    CG   CD   OE1  OE2                                  
REMARK 470     MET B 114    CG   SD   CE                                        
REMARK 470     PRO B 116    CG   CD                                             
REMARK 470     THR B 117    OG1  CG2                                            
REMARK 470     LYS B 118    CG   CD   CE   NZ                                   
REMARK 470     ASN B 119    CG   OD1  ND2                                       
REMARK 470     ILE B 140    CG1  CG2  CD1                                       
REMARK 470     VAL B 143    CG1  CG2                                            
REMARK 470     LYS B 331    CG   CD   CE   NZ                                   
REMARK 470     ASP B 333    CG   OD1  OD2                                       
REMARK 470     VAL B 334    CG1  CG2                                            
REMARK 470     GLU B 335    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 336    CG   CD   CE   NZ                                   
REMARK 470     LEU B 337    CG   CD1  CD2                                       
REMARK 470     SER B 338    OG                                                  
REMARK 470     LYS B 339    CG   CD   CE   NZ                                   
REMARK 470     PHE B 340    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 341    CG   CD   CE   NZ                                   
REMARK 470     ARG B 343    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 345    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 349    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 356    CG   CD1  CD2                                       
REMARK 470     VAL B 360    CG1  CG2                                            
REMARK 470     LEU B 361    CG   CD1  CD2                                       
REMARK 470     ASP B 363    CG   OD1  OD2                                       
REMARK 470     ILE B 364    CG1  CG2  CD1                                       
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    PRO A  77   C   -  N   -  CA  ANGL. DEV. =   9.0 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    LEU A 117       33.17     77.92                                   
REMARK 500    PRO A 194       42.92    -65.74                                   
REMARK 500    ASP A 248       56.40   -157.43                                   
REMARK 500    SER A 263       -9.71   -176.27                                   
REMARK 500    LYS A 264      -22.99     63.72                                   
REMARK 500    LYS A 265      162.27    -45.10                                   
REMARK 500    LEU A 353       -3.92    -52.92                                   
REMARK 500    TYR A 375       44.76   -140.26                                   
REMARK 500    TYR A 391        1.68    -62.19                                   
REMARK 500    PRO B 113       24.53    -63.44                                   
REMARK 500    MET B 114       32.79    178.42                                   
REMARK 500    GLU B 171       88.78      9.68                                   
REMARK 500    LEU B 178        4.28     99.45                                   
REMARK 500    ASP B 183       43.90    -75.06                                   
REMARK 500    ALA B 185     -151.99   -158.96                                   
REMARK 500    ALA B 288       31.66    -76.32                                   
REMARK 500    HIS B 300       51.07   -146.52                                   
REMARK 500    LYS B 331      -23.95     59.49                                   
REMARK 500    ASP B 346       68.18   -118.19                                   
REMARK 500    ALA B 359      -72.19    -47.69                                   
REMARK 500    LEU B 361        2.23    -67.86                                   
REMARK 500    ASN C  29     -153.05   -142.08                                   
REMARK 500    GLU C  50      -41.65   -153.52                                   
REMARK 500    GLU C 128      -37.05   -151.04                                   
REMARK 500    PRO C 140       41.30   -108.56                                   
REMARK 500    SER C 154       17.46     55.28                                   
REMARK 500    ARG C 179      112.05    -23.13                                   
REMARK 500    SER C 199       79.22   -113.79                                   
REMARK 500    LYS C 234       14.81     57.43                                   
REMARK 500    ARG C 284       81.63     81.00                                   
REMARK 500    LYS C 341       65.99   -165.91                                   
REMARK 500    LYS C 370     -100.13    -90.20                                   
REMARK 500    ILE C 371       96.39     88.54                                   
REMARK 500    VAL D  85     -169.63   -124.12                                   
REMARK 500    SER D 105       77.98   -105.14                                   
REMARK 500    LYS D 170      -76.67    -56.60                                   
REMARK 500    ARG D 203       -6.79     66.15                                   
REMARK 500    LYS E  37      171.14    -56.01                                   
REMARK 500    PHE E  49      -70.36    -30.92                                   
REMARK 500    SER E  87      137.24    135.46                                   
REMARK 500    PRO E 106      141.24    -38.57                                   
REMARK 500    PRO E 151      -13.93    -39.97                                   
REMARK 500    ASN E 153      166.34    -25.44                                   
REMARK 500    TRP E 160      -46.77   -131.45                                   
REMARK 500    ALA F   3      -16.43     64.72                                   
REMARK 500    ASN F  56     -156.86   -165.98                                   
REMARK 500    PHE F 101       53.96   -107.04                                   
REMARK 500    PHE F 102      -23.13    -32.93                                   
REMARK 500    ASN G  22      -28.28   -176.76                                   
REMARK 500    ASN G  61       73.75     44.35                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 RAMACHANDRAN OUTLIERS.                        
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                              CA A 500  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP A 601   O2G                                                    
REMARK 620 2 ATP A 601   O1B  62.7                                              
REMARK 620 3 HOH A 619   O   111.6 165.0                                        
REMARK 620 4 HOH A 620   O   129.3  81.7  93.4                                  
REMARK 620 5 HOH A 621   O    64.2  82.8  82.3  77.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP B 602   O1B                                                    
REMARK 620 2 ATP B 602   O2G  64.8                                              
REMARK 620 3 ATP B 602   O3G  63.4  49.3                                        
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 CA B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2P9I   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2P9L   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2P9N   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2P9P   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2P9S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2P9U   RELATED DB: PDB                                   
DBREF  2P9K A    1   418  UNP    P61157   ARP3_BOVIN       1    418             
DBREF  2P9K B    1   394  UNP    A7MB62   ARP2_BOVIN       1    394             
DBREF  2P9K C    1   372  UNP    Q58CQ2   ARC1B_BOVIN      1    372             
DBREF  2P9K D    1   300  UNP    Q3MHR7   ARPC2_BOVIN      1    300             
DBREF  2P9K E    1   178  UNP    Q3T035   ARPC3_BOVIN      1    178             
DBREF  2P9K F    1   168  UNP    Q148J6   ARPC4_BOVIN      1    168             
DBREF  2P9K G    1   151  UNP    Q3SYX9   ARPC5_BOVIN      1    151             
SEQADV 2P9K VAL C   58  UNP  Q58CQ2    ILE    58 CONFLICT                       
SEQADV 2P9K ASP G   17  UNP  Q3SYX9    GLY    17 CONFLICT                       
SEQADV 2P9K ASP G   28  UNP  Q3SYX9    GLU    28 CONFLICT                       
SEQRES   1 A  418  MET ALA GLY ARG LEU PRO ALA CYS VAL VAL ASP CYS GLY          
SEQRES   2 A  418  THR GLY TYR THR LYS LEU GLY TYR ALA GLY ASN THR GLU          
SEQRES   3 A  418  PRO GLN PHE ILE ILE PRO SER CYS ILE ALA ILE LYS GLU          
SEQRES   4 A  418  SER ALA LYS VAL GLY ASP GLN ALA GLN ARG ARG VAL MET          
SEQRES   5 A  418  LYS GLY VAL ASP ASP LEU ASP PHE PHE ILE GLY ASP GLU          
SEQRES   6 A  418  ALA ILE GLU LYS PRO THR TYR ALA THR LYS TRP PRO ILE          
SEQRES   7 A  418  ARG HIS GLY ILE VAL GLU ASP TRP ASP LEU MET GLU ARG          
SEQRES   8 A  418  PHE MET GLU GLN VAL ILE PHE LYS TYR LEU ARG ALA GLU          
SEQRES   9 A  418  PRO GLU ASP HIS TYR PHE LEU LEU THR GLU PRO PRO LEU          
SEQRES  10 A  418  ASN THR PRO GLU ASN ARG GLU TYR THR ALA GLU ILE MET          
SEQRES  11 A  418  PHE GLU SER PHE ASN VAL PRO GLY LEU TYR ILE ALA VAL          
SEQRES  12 A  418  GLN ALA VAL LEU ALA LEU ALA ALA SER TRP THR SER ARG          
SEQRES  13 A  418  GLN VAL GLY GLU ARG THR LEU THR GLY THR VAL ILE ASP          
SEQRES  14 A  418  SER GLY ASP GLY VAL THR HIS VAL ILE PRO VAL ALA GLU          
SEQRES  15 A  418  GLY TYR VAL ILE GLY SER CYS ILE LYS HIS ILE PRO ILE          
SEQRES  16 A  418  ALA GLY ARG ASP ILE THR TYR PHE ILE GLN GLN LEU LEU          
SEQRES  17 A  418  ARG ASP ARG GLU VAL GLY ILE PRO PRO GLU GLN SER LEU          
SEQRES  18 A  418  GLU THR ALA LYS ALA VAL LYS GLU ARG TYR SER TYR VAL          
SEQRES  19 A  418  CYS PRO ASP LEU VAL LYS GLU PHE ASN LYS TYR ASP THR          
SEQRES  20 A  418  ASP GLY SER LYS TRP ILE LYS GLN TYR THR GLY ILE ASN          
SEQRES  21 A  418  ALA ILE SER LYS LYS GLU PHE SER ILE ASP VAL GLY TYR          
SEQRES  22 A  418  GLU ARG PHE LEU GLY PRO GLU ILE PHE PHE HIS PRO GLU          
SEQRES  23 A  418  PHE ALA ASN PRO ASP PHE THR GLN PRO ILE SER GLU VAL          
SEQRES  24 A  418  VAL ASP GLU VAL ILE GLN ASN CYS PRO ILE ASP VAL ARG          
SEQRES  25 A  418  ARG PRO LEU TYR LYS ASN ILE VAL LEU SER GLY GLY SER          
SEQRES  26 A  418  THR MET PHE ARG ASP PHE GLY ARG ARG LEU GLN ARG ASP          
SEQRES  27 A  418  LEU LYS ARG THR VAL ASP ALA ARG LEU LYS LEU SER GLU          
SEQRES  28 A  418  GLU LEU SER GLY GLY ARG LEU LYS PRO LYS PRO ILE ASP          
SEQRES  29 A  418  VAL GLN VAL ILE THR HIS HIS MET GLN ARG TYR ALA VAL          
SEQRES  30 A  418  TRP PHE GLY GLY SER MET LEU ALA SER THR PRO GLU PHE          
SEQRES  31 A  418  TYR GLN VAL CYS HIS THR LYS LYS ASP TYR GLU GLU ILE          
SEQRES  32 A  418  GLY PRO SER ILE CYS ARG HIS ASN PRO VAL PHE GLY VAL          
SEQRES  33 A  418  MET SER                                                      
SEQRES   1 B  394  MET ASP SER GLN GLY ARG LYS VAL VAL VAL CYS ASP ASN          
SEQRES   2 B  394  GLY THR GLY PHE VAL LYS CYS GLY TYR ALA GLY SER ASN          
SEQRES   3 B  394  PHE PRO GLU HIS ILE PHE PRO SER LEU VAL GLY ARG PRO          
SEQRES   4 B  394  ILE ILE ARG SER THR THR LYS VAL GLY ASN ILE GLU ILE          
SEQRES   5 B  394  LYS ASP LEU MET VAL GLY ASP GLU ALA SER GLU LEU ARG          
SEQRES   6 B  394  SER MET LEU GLU VAL ASN TYR PRO MET GLU ASN GLY ILE          
SEQRES   7 B  394  VAL ARG ASN TRP ASP ASP MET LYS HIS LEU TRP ASP TYR          
SEQRES   8 B  394  THR PHE GLY PRO GLU LYS LEU ASN ILE ASP THR ARG ASN          
SEQRES   9 B  394  CYS LYS ILE LEU LEU THR GLU PRO PRO MET ASN PRO THR          
SEQRES  10 B  394  LYS ASN ARG GLU LYS ILE VAL GLU VAL MET PHE GLU THR          
SEQRES  11 B  394  TYR GLN PHE SER GLY VAL TYR VAL ALA ILE GLN ALA VAL          
SEQRES  12 B  394  LEU THR LEU TYR ALA GLN GLY LEU LEU THR GLY VAL VAL          
SEQRES  13 B  394  VAL ASP SER GLY ASP GLY VAL THR HIS ILE CYS PRO VAL          
SEQRES  14 B  394  TYR GLU GLY PHE SER LEU PRO HIS LEU THR ARG ARG LEU          
SEQRES  15 B  394  ASP ILE ALA GLY ARG ASP ILE THR ARG TYR LEU ILE LYS          
SEQRES  16 B  394  LEU LEU LEU LEU ARG GLY TYR ALA PHE ASN HIS SER ALA          
SEQRES  17 B  394  ASP PHE GLU THR VAL ARG MET ILE LYS GLU LYS LEU CYS          
SEQRES  18 B  394  TYR VAL GLY TYR ASN ILE GLU GLN GLU GLN LYS LEU ALA          
SEQRES  19 B  394  LEU GLU THR THR VAL LEU VAL GLU SER TYR THR LEU PRO          
SEQRES  20 B  394  ASP GLY ARG ILE ILE LYS VAL GLY GLY GLU ARG PHE GLU          
SEQRES  21 B  394  ALA PRO GLU ALA LEU PHE GLN PRO HIS LEU ILE ASN VAL          
SEQRES  22 B  394  GLU GLY VAL GLY VAL ALA GLU LEU LEU PHE ASN THR ILE          
SEQRES  23 B  394  GLN ALA ALA ASP ILE ASP THR ARG SER GLU PHE TYR LYS          
SEQRES  24 B  394  HIS ILE VAL LEU SER GLY GLY SER THR MET TYR PRO GLY          
SEQRES  25 B  394  LEU PRO SER ARG LEU GLU ARG GLU LEU LYS GLN LEU TYR          
SEQRES  26 B  394  LEU GLU ARG VAL LEU LYS GLY ASP VAL GLU LYS LEU SER          
SEQRES  27 B  394  LYS PHE LYS ILE ARG ILE GLU ASP PRO PRO ARG ARG LYS          
SEQRES  28 B  394  HIS MET VAL PHE LEU GLY GLY ALA VAL LEU ALA ASP ILE          
SEQRES  29 B  394  MET LYS ASP LYS ASP ASN PHE TRP MET THR ARG GLN GLU          
SEQRES  30 B  394  TYR GLN GLU LYS GLY VAL ARG VAL LEU GLU LYS LEU GLY          
SEQRES  31 B  394  VAL THR VAL ARG                                              
SEQRES   1 C  372  MET ALA TYR HIS SER PHE LEU VAL GLU PRO ILE SER CYS          
SEQRES   2 C  372  HIS ALA TRP ASN LYS ASP ARG THR GLN ILE ALA ILE CYS          
SEQRES   3 C  372  PRO ASN ASN HIS GLU VAL HIS ILE TYR GLU LYS SER GLY          
SEQRES   4 C  372  ASN LYS TRP VAL GLN VAL HIS GLU LEU LYS GLU HIS ASN          
SEQRES   5 C  372  GLY GLN VAL THR GLY VAL ASP TRP ALA PRO ASP SER ASN          
SEQRES   6 C  372  ARG ILE VAL THR CYS GLY THR ASP ARG ASN ALA TYR VAL          
SEQRES   7 C  372  TRP THR LEU LYS GLY ARG THR TRP LYS PRO THR LEU VAL          
SEQRES   8 C  372  ILE LEU ARG ILE ASN ARG ALA ALA ARG CYS VAL ARG TRP          
SEQRES   9 C  372  ALA PRO ASN GLU LYS LYS PHE ALA VAL GLY SER GLY SER          
SEQRES  10 C  372  ARG VAL ILE SER ILE CYS TYR PHE GLU GLN GLU ASN ASP          
SEQRES  11 C  372  TRP TRP VAL CYS LYS HIS ILE LYS LYS PRO ILE ARG SER          
SEQRES  12 C  372  THR VAL LEU SER LEU ASP TRP HIS PRO ASN SER VAL LEU          
SEQRES  13 C  372  LEU ALA ALA GLY SER CYS ASP PHE LYS CYS ARG ILE PHE          
SEQRES  14 C  372  SER ALA TYR ILE LYS GLU VAL GLU GLU ARG PRO ALA PRO          
SEQRES  15 C  372  THR PRO TRP GLY SER LYS MET PRO PHE GLY GLU LEU MET          
SEQRES  16 C  372  PHE GLU SER SER SER SER CYS GLY TRP VAL HIS GLY VAL          
SEQRES  17 C  372  CYS PHE SER ALA ASN GLY SER ARG VAL ALA TRP VAL SER          
SEQRES  18 C  372  HIS ASP SER THR VAL CYS LEU ALA ASP ALA ASP LYS LYS          
SEQRES  19 C  372  MET ALA VAL ALA THR LEU ALA SER GLU THR LEU PRO LEU          
SEQRES  20 C  372  LEU ALA VAL THR PHE ILE THR GLU SER SER LEU VAL ALA          
SEQRES  21 C  372  ALA GLY HIS ASP CYS PHE PRO VAL LEU PHE THR TYR ASP          
SEQRES  22 C  372  SER ALA ALA GLY LYS LEU SER PHE GLY GLY ARG LEU ASP          
SEQRES  23 C  372  VAL PRO LYS GLN SER SER GLN ARG GLY LEU THR ALA ARG          
SEQRES  24 C  372  GLU ARG PHE GLN ASN LEU ASP LYS LYS ALA SER SER GLU          
SEQRES  25 C  372  GLY SER ALA ALA ALA GLY ALA GLY LEU ASP SER LEU HIS          
SEQRES  26 C  372  LYS ASN SER VAL SER GLN ILE SER VAL LEU SER GLY GLY          
SEQRES  27 C  372  LYS ALA LYS CYS SER GLN PHE CYS THR THR GLY MET ASP          
SEQRES  28 C  372  GLY GLY MET SER ILE TRP ASP VAL ARG SER LEU GLU SER          
SEQRES  29 C  372  ALA LEU LYS ASP LEU LYS ILE VAL                              
SEQRES   1 D  300  MET ILE LEU LEU GLU VAL ASN ASN ARG ILE ILE GLU GLU          
SEQRES   2 D  300  THR LEU ALA LEU LYS PHE GLU ASN ALA ALA ALA GLY ASN          
SEQRES   3 D  300  LYS PRO GLU ALA VAL GLU VAL THR PHE ALA ASP PHE ASP          
SEQRES   4 D  300  GLY VAL LEU TYR HIS ILE SER ASN PRO ASN GLY ASP LYS          
SEQRES   5 D  300  THR LYS VAL MET VAL SER ILE SER LEU LYS PHE TYR LYS          
SEQRES   6 D  300  GLU LEU GLN ALA HIS GLY ALA ASP GLU LEU LEU LYS ARG          
SEQRES   7 D  300  VAL TYR GLY SER TYR LEU VAL ASN PRO GLU SER GLY TYR          
SEQRES   8 D  300  ASN VAL SER LEU LEU TYR ASP LEU GLU ASN LEU PRO ALA          
SEQRES   9 D  300  SER LYS ASP SER ILE VAL HIS GLN ALA GLY MET LEU LYS          
SEQRES  10 D  300  ARG ASN CYS PHE ALA SER VAL PHE GLU LYS TYR PHE GLN          
SEQRES  11 D  300  PHE GLN GLU GLU GLY LYS GLU GLY GLU ASN ARG ALA VAL          
SEQRES  12 D  300  ILE HIS TYR ARG ASP ASP GLU THR MET TYR VAL GLU SER          
SEQRES  13 D  300  LYS LYS ASP ARG VAL THR VAL VAL PHE SER THR VAL PHE          
SEQRES  14 D  300  LYS ASP ASP ASP ASP VAL VAL ILE GLY LYS VAL PHE MET          
SEQRES  15 D  300  GLN GLU PHE LYS GLU GLY ARG ARG ALA SER HIS THR ALA          
SEQRES  16 D  300  PRO GLN VAL LEU PHE SER HIS ARG GLU PRO PRO LEU GLU          
SEQRES  17 D  300  LEU LYS ASP THR ASP ALA ALA VAL GLY ASP ASN ILE GLY          
SEQRES  18 D  300  TYR ILE THR PHE VAL LEU PHE PRO ARG HIS THR ASN ALA          
SEQRES  19 D  300  SER ALA ARG ASP ASN THR ILE ASN LEU ILE HIS THR PHE          
SEQRES  20 D  300  ARG ASP TYR LEU HIS TYR HIS ILE LYS CYS SER LYS ALA          
SEQRES  21 D  300  TYR ILE HIS THR ARG MET ARG ALA LYS THR SER ASP PHE          
SEQRES  22 D  300  LEU LYS VAL LEU ASN ARG ALA ARG PRO ASP ALA GLU LYS          
SEQRES  23 D  300  LYS GLU MET LYS THR ILE THR GLY LYS THR PHE SER SER          
SEQRES  24 D  300  ARG                                                          
SEQRES   1 E  178  MET PRO ALA TYR HIS SER SER LEU MET ASP PRO ASP THR          
SEQRES   2 E  178  LYS LEU ILE GLY ASN MET ALA LEU LEU PRO ILE ARG SER          
SEQRES   3 E  178  GLN PHE LYS GLY PRO ALA PRO ARG GLU THR LYS ASP THR          
SEQRES   4 E  178  ASP ILE VAL ASP GLU ALA ILE TYR TYR PHE LYS ALA ASN          
SEQRES   5 E  178  VAL PHE PHE LYS ASN TYR GLU ILE LYS ASN GLU ALA ASP          
SEQRES   6 E  178  ARG THR LEU ILE TYR ILE THR LEU TYR ILE SER GLU CYS          
SEQRES   7 E  178  LEU LYS LYS LEU GLN LYS CYS ASN SER LYS SER GLN GLY          
SEQRES   8 E  178  GLU LYS GLU MET TYR THR LEU GLY ILE THR ASN PHE PRO          
SEQRES   9 E  178  ILE PRO GLY GLU PRO GLY PHE PRO LEU ASN ALA ILE TYR          
SEQRES  10 E  178  ALA LYS PRO ALA ASN LYS GLN GLU ASP GLU VAL MET ARG          
SEQRES  11 E  178  ALA TYR LEU GLN GLN LEU ARG GLN GLU THR GLY LEU ARG          
SEQRES  12 E  178  LEU CYS GLU LYS VAL PHE ASP PRO GLN ASN ASP LYS PRO          
SEQRES  13 E  178  SER LYS TRP TRP THR CYS PHE VAL LYS ARG GLN PHE MET          
SEQRES  14 E  178  ASN LYS SER LEU SER GLY PRO GLY GLN                          
SEQRES   1 F  168  MET THR ALA THR LEU ARG PRO TYR LEU SER ALA VAL ARG          
SEQRES   2 F  168  ALA THR LEU GLN ALA ALA LEU CYS LEU GLU ASN PHE SER          
SEQRES   3 F  168  SER GLN VAL VAL GLU ARG HIS ASN LYS PRO GLU VAL GLU          
SEQRES   4 F  168  VAL ARG SER SER LYS GLU LEU LEU LEU GLN PRO VAL THR          
SEQRES   5 F  168  ILE SER ARG ASN GLU LYS GLU LYS VAL LEU ILE GLU GLY          
SEQRES   6 F  168  SER ILE ASN SER VAL ARG VAL SER ILE ALA VAL LYS GLN          
SEQRES   7 F  168  ALA ASP GLU ILE GLU LYS ILE LEU CYS HIS LYS PHE MET          
SEQRES   8 F  168  ARG PHE MET MET MET ARG ALA GLU ASN PHE PHE ILE LEU          
SEQRES   9 F  168  ARG ARG LYS PRO VAL GLU GLY TYR ASP ILE SER PHE LEU          
SEQRES  10 F  168  ILE THR ASN PHE HIS THR GLU GLN MET TYR LYS HIS LYS          
SEQRES  11 F  168  LEU VAL ASP PHE VAL ILE HIS PHE MET GLU GLU ILE ASP          
SEQRES  12 F  168  LYS GLU ILE SER GLU MET LYS LEU SER VAL ASN ALA ARG          
SEQRES  13 F  168  ALA ARG ILE VAL ALA GLU GLU PHE LEU LYS ASN PHE              
SEQRES   1 G  151  MET SER LYS ASN THR VAL SER SER ALA ARG PHE ARG LYS          
SEQRES   2 G  151  VAL ASP VAL ASP GLU TYR ASP GLU ASN LYS PHE VAL ASP          
SEQRES   3 G  151  GLU ASP ASP GLY GLY ASP GLY GLN ALA GLY PRO ASP GLU          
SEQRES   4 G  151  GLY GLU VAL ASP SER CYS LEU ARG GLN GLY ASN MET THR          
SEQRES   5 G  151  ALA ALA LEU GLN ALA ALA LEU LYS ASN PRO PRO ILE ASN          
SEQRES   6 G  151  THR LYS SER GLN ALA VAL LYS ASP ARG ALA GLY SER ILE          
SEQRES   7 G  151  VAL LEU LYS VAL LEU ILE SER PHE LYS ALA ASN ASP ILE          
SEQRES   8 G  151  GLU LYS ALA VAL GLN SER LEU ASP LYS ASN GLY VAL ASP          
SEQRES   9 G  151  LEU LEU MET LYS TYR ILE TYR LYS GLY PHE GLU SER PRO          
SEQRES  10 G  151  SER ASP ASN SER SER ALA VAL LEU LEU GLN TRP HIS GLU          
SEQRES  11 G  151  LYS ALA LEU ALA ALA GLY GLY VAL GLY SER ILE VAL ARG          
SEQRES  12 G  151  VAL LEU THR ALA ARG LYS THR VAL                              
HET     CA  A 500       1                                                       
HET    ATP  A 601      31                                                       
HET     CA  B 501       1                                                       
HET    ATP  B 602      31                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   8   CA    2(CA 2+)                                                     
FORMUL   9  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL  12  HOH   *396(H2 O)                                                    
HELIX    1   1 VAL A   55  ASP A   59  5                                   5    
HELIX    2   2 ASP A   64  ILE A   67  5                                   4    
HELIX    3   3 ASP A   85  LYS A   99  1                                  15    
HELIX    4   4 GLU A  104  ASP A  107  5                                   4    
HELIX    5   5 THR A  119  SER A  133  1                                  15    
HELIX    6   6 GLN A  144  TRP A  153  1                                  10    
HELIX    7   7 GLY A  187  ILE A  190  5                                   4    
HELIX    8   8 ALA A  196  GLU A  212  1                                  17    
HELIX    9   9 PRO A  216  GLU A  218  5                                   3    
HELIX   10  10 GLN A  219  SER A  232  1                                  14    
HELIX   11  11 ASP A  237  ASP A  248  1                                  12    
HELIX   12  12 ASP A  248  ILE A  253  1                                   6    
HELIX   13  13 TYR A  273  ILE A  281  1                                   9    
HELIX   14  14 PHE A  282  PHE A  283  5                                   2    
HELIX   15  15 HIS A  284  ALA A  288  5                                   5    
HELIX   16  16 PRO A  295  CYS A  307  1                                  13    
HELIX   17  17 PRO A  308  ASP A  310  5                                   3    
HELIX   18  18 VAL A  311  LYS A  317  1                                   7    
HELIX   19  19 GLY A  323  MET A  327  5                                   5    
HELIX   20  20 ASP A  330  LEU A  353  1                                  24    
HELIX   21  21 TYR A  375  SER A  386  1                                  12    
HELIX   22  22 GLU A  389  CYS A  394  1                                   6    
HELIX   23  23 LYS A  397  GLY A  404  1                                   8    
HELIX   24  24 PRO A  405  HIS A  410  5                                   6    
HELIX   25  25 ILE B  140  GLN B  149  1                                  10    
HELIX   26  26 ALA B  185  ARG B  200  1                                  16    
HELIX   27  27 ASP B  209  CYS B  221  1                                  13    
HELIX   28  28 ASN B  226  THR B  237  1                                  12    
HELIX   29  29 GLY B  256  ALA B  261  1                                   6    
HELIX   30  30 PRO B  262  PHE B  266  5                                   5    
HELIX   31  31 GLN B  267  ASN B  272  5                                   6    
HELIX   32  32 GLY B  277  ALA B  288  1                                  12    
HELIX   33  33 THR B  293  LYS B  299  1                                   7    
HELIX   34  34 GLY B  305  MET B  309  5                                   5    
HELIX   35  35 GLY B  312  VAL B  329  1                                  18    
HELIX   36  36 GLU B  335  PHE B  340  5                                   6    
HELIX   37  37 ARG B  349  LYS B  351  5                                   3    
HELIX   38  38 HIS B  352  LEU B  361  1                                  10    
HELIX   39  39 ASP C  232  LYS C  234  5                                   3    
HELIX   40  40 VAL C  359  LEU C  366  1                                   8    
HELIX   41  41 ASN D    8  GLY D   25  1                                  18    
HELIX   42  42 PRO D   48  ASP D   51  5                                   4    
HELIX   43  43 PHE D   63  ALA D   69  1                                   7    
HELIX   44  44 GLY D   71  GLY D   81  1                                  11    
HELIX   45  45 SER D  105  MET D  115  1                                  11    
HELIX   46  46 MET D  115  GLU D  134  1                                  20    
HELIX   47  47 ASP D  171  GLU D  187  1                                  17    
HELIX   48  48 GLY D  188  ALA D  191  5                                   4    
HELIX   49  49 PHE D  228  ASN D  233  1                                   6    
HELIX   50  50 ALA D  236  HIS D  245  1                                  10    
HELIX   51  51 THR D  246  ARG D  279  1                                  34    
HELIX   52  52 ASP E   40  VAL E   53  1                                  14    
HELIX   53  53 ASN E   62  LYS E   84  1                                  23    
HELIX   54  54 SER E   87  THR E  101  1                                  15    
HELIX   55  55 ASN E  122  PHE E  149  1                                  28    
HELIX   56  56 SER E  157  CYS E  162  1                                   6    
HELIX   57  57 GLN E  167  LYS E  171  5                                   5    
HELIX   58  58 THR F    4  LEU F   20  1                                  17    
HELIX   59  59 PRO F   36  ARG F   41  1                                   6    
HELIX   60  60 SER F   43  LEU F   47  5                                   5    
HELIX   61  61 ASP F   80  ARG F   97  1                                  18    
HELIX   62  62 ALA F   98  PHE F  102  5                                   5    
HELIX   63  63 ASN F  120  MET F  126  1                                   7    
HELIX   64  64 TYR F  127  LYS F  166  1                                  40    
HELIX   65  65 ASN F  167  PHE F  168  5                                   2    
HELIX   66  66 ALA G    9  VAL G   14  5                                   6    
HELIX   67  67 ASP G   15  ASP G   20  5                                   6    
HELIX   68  68 ASP G   38  GLN G   48  1                                  11    
HELIX   69  69 ASN G   50  LEU G   59  1                                  10    
HELIX   70  70 SER G   68  PHE G   86  1                                  19    
HELIX   71  71 LYS G   87  ASN G   89  5                                   3    
HELIX   72  72 ASP G   90  GLN G   96  1                                   7    
HELIX   73  73 ASP G   99  GLU G  115  1                                  17    
HELIX   74  74 ASN G  120  GLY G  137  1                                  18    
HELIX   75  75 GLY G  137  ALA G  147  1                                  11    
SHEET    1   A 6 PHE A  29  PRO A  32  0                                        
SHEET    2   A 6 TYR A  16  TYR A  21 -1  N  THR A  17   O  ILE A  31           
SHEET    3   A 6 CYS A   8  CYS A  12 -1  N  ASP A  11   O  LYS A  18           
SHEET    4   A 6 TYR A 109  GLU A 114  1  O  LEU A 111   N  VAL A  10           
SHEET    5   A 6 GLY A 138  VAL A 143  1  O  ALA A 142   N  LEU A 112           
SHEET    6   A 6 HIS A 395  THR A 396 -1  O  HIS A 395   N  LEU A 139           
SHEET    1   B 3 PHE A  61  ILE A  62  0                                        
SHEET    2   B 3 ILE A  35  ILE A  37 -1  N  ALA A  36   O  PHE A  61           
SHEET    3   B 3 ALA A  73  LYS A  75 -1  O  LYS A  75   N  ILE A  35           
SHEET    1   C 2 ILE A  78  ARG A  79  0                                        
SHEET    2   C 2 ILE A  82  VAL A  83 -1  O  ILE A  82   N  ARG A  79           
SHEET    1   D 3 TYR A 184  VAL A 185  0                                        
SHEET    2   D 3 THR A 175  ALA A 181 -1  N  ALA A 181   O  TYR A 184           
SHEET    3   D 3 LYS A 191  ILE A 193 -1  O  ILE A 193   N  THR A 175           
SHEET    1   E 5 TYR A 184  VAL A 185  0                                        
SHEET    2   E 5 THR A 175  ALA A 181 -1  N  ALA A 181   O  TYR A 184           
SHEET    3   E 5 GLY A 165  SER A 170 -1  N  VAL A 167   O  ILE A 178           
SHEET    4   E 5 ILE A 319  SER A 322  1  O  VAL A 320   N  ILE A 168           
SHEET    5   E 5 VAL A 367  ILE A 368  1  O  ILE A 368   N  ILE A 319           
SHEET    1   F 2 LYS A 254  ILE A 259  0                                        
SHEET    2   F 2 GLU A 266  VAL A 271 -1  O  PHE A 267   N  GLY A 258           
SHEET    1   G 3 CYS B  11  ASN B  13  0                                        
SHEET    2   G 3 PHE B  17  CYS B  20 -1  O  LYS B  19   N  ASP B  12           
SHEET    3   G 3 HIS B  30  PRO B  33 -1  O  PHE B  32   N  VAL B  18           
SHEET    1   H 3 PHE B 173  SER B 174  0                                        
SHEET    2   H 3 THR B 164  TYR B 170 -1  N  TYR B 170   O  PHE B 173           
SHEET    3   H 3 ARG B 180  LEU B 182 -1  O  LEU B 182   N  THR B 164           
SHEET    1   I 5 PHE B 173  SER B 174  0                                        
SHEET    2   I 5 THR B 164  TYR B 170 -1  N  TYR B 170   O  PHE B 173           
SHEET    3   I 5 GLY B 154  SER B 159 -1  N  GLY B 154   O  VAL B 169           
SHEET    4   I 5 ILE B 301  SER B 304  1  O  SER B 304   N  SER B 159           
SHEET    5   I 5 ILE B 344  GLU B 345  1  O  GLU B 345   N  ILE B 301           
SHEET    1   J 2 GLU B 242  THR B 245  0                                        
SHEET    2   J 2 ILE B 251  VAL B 254 -1  O  VAL B 254   N  GLU B 242           
SHEET    1   K 4 TYR C   3  SER C   5  0                                        
SHEET    2   K 4 GLY C 353  ASP C 358 -1  O  MET C 354   N  HIS C   4           
SHEET    3   K 4 GLN C 344  GLY C 349 -1  N  PHE C 345   O  TRP C 357           
SHEET    4   K 4 VAL C 329  SER C 336 -1  N  SER C 333   O  CYS C 346           
SHEET    1   L 4 HIS C  14  TRP C  16  0                                        
SHEET    2   L 4 GLN C  22  ILE C  25 -1  O  ALA C  24   N  ALA C  15           
SHEET    3   L 4 GLU C  31  SER C  38 -1  O  TYR C  35   N  ILE C  23           
SHEET    4   L 4 LYS C  41  LYS C  49 -1  O  VAL C  43   N  GLU C  36           
SHEET    1   M 4 VAL C  55  ALA C  61  0                                        
SHEET    2   M 4 ARG C  66  GLY C  71 -1  O  ARG C  66   N  ALA C  61           
SHEET    3   M 4 ALA C  76  LYS C  82 -1  O  TRP C  79   N  ILE C  67           
SHEET    4   M 4 THR C  85  VAL C  91 -1  O  LYS C  87   N  THR C  80           
SHEET    1   N 4 ALA C  99  TRP C 104  0                                        
SHEET    2   N 4 LYS C 110  SER C 115 -1  O  GLY C 114   N  ARG C 100           
SHEET    3   N 4 ILE C 120  GLU C 126 -1  O  CYS C 123   N  PHE C 111           
SHEET    4   N 4 TRP C 131  ILE C 137 -1  O  ILE C 137   N  ILE C 120           
SHEET    1   O 4 VAL C 145  TRP C 150  0                                        
SHEET    2   O 4 LEU C 156  SER C 161 -1  O  ALA C 158   N  ASP C 149           
SHEET    3   O 4 CYS C 166  SER C 170 -1  O  PHE C 169   N  LEU C 157           
SHEET    4   O 4 LEU C 194  GLU C 197 -1  O  MET C 195   N  ILE C 168           
SHEET    1   P 4 VAL C 205  PHE C 210  0                                        
SHEET    2   P 4 ARG C 216  SER C 221 -1  O  ALA C 218   N  CYS C 209           
SHEET    3   P 4 THR C 225  ASP C 230 -1  O  ALA C 229   N  VAL C 217           
SHEET    4   P 4 VAL C 237  ALA C 241 -1  O  ALA C 238   N  LEU C 228           
SHEET    1   Q 4 LEU C 247  THR C 254  0                                        
SHEET    2   Q 4 SER C 257  GLY C 262 -1  O  ALA C 261   N  LEU C 248           
SHEET    3   Q 4 VAL C 268  ASP C 273 -1  O  PHE C 270   N  LEU C 258           
SHEET    4   Q 4 LYS C 278  PHE C 281 -1  O  LYS C 278   N  ASP C 273           
SHEET    1   R 5 GLU D  32  ASP D  37  0                                        
SHEET    2   R 5 VAL D  41  SER D  46 -1  O  TYR D  43   N  PHE D  35           
SHEET    3   R 5 LYS D  54  SER D  60 -1  O  MET D  56   N  SER D  46           
SHEET    4   R 5 VAL D  93  ASP D  98 -1  O  LEU D  95   N  VAL D  57           
SHEET    5   R 5 LEU D  84  VAL D  85 -1  N  VAL D  85   O  SER D  94           
SHEET    1   S 5 ALA D 142  ARG D 147  0                                        
SHEET    2   S 5 GLU D 150  SER D 156 -1  O  VAL D 154   N  ALA D 142           
SHEET    3   S 5 VAL D 161  VAL D 168 -1  O  THR D 162   N  GLU D 155           
SHEET    4   S 5 ILE D 220  LEU D 227 -1  O  ILE D 223   N  PHE D 165           
SHEET    5   S 5 GLN D 197  HIS D 202 -1  N  LEU D 199   O  THR D 224           
SHEET    1   T 2 LYS E  14  ILE E  16  0                                        
SHEET    2   T 2 MET E  19  LEU E  21 -1  O  LEU E  21   N  LYS E  14           
SHEET    1   U 4 VAL F  51  SER F  54  0                                        
SHEET    2   U 4 LYS F  60  GLY F  65 -1  O  ILE F  63   N  VAL F  51           
SHEET    3   U 4 SER F  69  ALA F  75 -1  O  ALA F  75   N  LYS F  60           
SHEET    4   U 4 ILE F 114  THR F 119 -1  O  PHE F 116   N  VAL F  72           
LINK        CA    CA A 500                 O2G ATP A 601     1555   1555  2.67  
LINK        CA    CA A 500                 O1B ATP A 601     1555   1555  2.62  
LINK        CA    CA A 500                 O   HOH A 619     1555   1555  2.96  
LINK        CA    CA A 500                 O   HOH A 620     1555   1555  2.97  
LINK        CA    CA A 500                 O   HOH A 621     1555   1555  3.12  
LINK        CA    CA B 501                 O1B ATP B 602     1555   1555  2.65  
LINK        CA    CA B 501                 O2G ATP B 602     1555   1555  2.99  
LINK        CA    CA B 501                 O3G ATP B 602     1555   1555  3.15  
CISPEP   1 LYS C  139    PRO C  140          0        -0.10                     
SITE     1 AC1  1 ATP B 602                                                     
SITE     1 AC2  3 ATP A 601  HOH A 619  HOH A 620                               
SITE     1 AC3 22 GLY A  13  THR A  14  GLY A  15  TYR A  16                    
SITE     2 AC3 22 LYS A  18  GLY A 171  ASP A 172  GLY A 173                    
SITE     3 AC3 22 GLY A 197  LYS A 225  LYS A 228  GLU A 229                    
SITE     4 AC3 22 GLY A 323  GLY A 324  SER A 325  MET A 327                    
SITE     5 AC3 22 PHE A 328   CA A 500  HOH A 602  HOH A 616                    
SITE     6 AC3 22 HOH A 621  HOH A 624                                          
SITE     1 AC4 22 GLY B  14  THR B  15  GLY B  16  PHE B  17                    
SITE     2 AC4 22 LYS B  19  GLY B 160  ASP B 161  GLY B 162                    
SITE     3 AC4 22 GLY B 186  ARG B 214  LYS B 217  GLU B 218                    
SITE     4 AC4 22 GLY B 305  GLY B 306  SER B 307  MET B 309                    
SITE     5 AC4 22 TYR B 310   CA B 501  HOH B 606  HOH B 607                    
SITE     6 AC4 22 HOH B 612  HOH B 620                                          
CRYST1  110.620  128.050  198.296  90.00  90.00  90.00 P 21 21 21    4          
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      0.009040  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007809  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005043        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system