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Database: PDB
Entry: 4II3
LinkDB: 4II3
Original site: 4II3 
HEADER    LIGASE                                  19-DEC-12   4II3              
TITLE     CRYSTAL STRUCTURE OF S. POMBE UBIQUITIN ACTIVATING ENZYME 1 (UBA1) IN 
TITLE    2 COMPLEX WITH UBIQUITIN AND ATP/MG                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-ACTIVATING ENZYME E1 1;                          
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UBA1, UNP RESIDUES 13-1012;                                
COMPND   5 SYNONYM: POLY(A)+ RNA TRANSPORT PROTEIN 3;                           
COMPND   6 EC: 6.3.2.19;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: UBIQUITIN-60S RIBOSOMAL PROTEIN L40;                       
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: UNP RESIDUES 1-76;                                         
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;                      
SOURCE   3 ORGANISM_COMMON: FISSION YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 284812;                                              
SOURCE   5 STRAIN: 972 / ATCC 24843;                                            
SOURCE   6 GENE: PTR3, SPBC1604.21C, SPBC211.09, UBIQUITIN ACTIVATING ENZYME 1  
SOURCE   7 (UBA1);                                                              
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;                      
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PSMT3;                                    
SOURCE  13 MOL_ID: 2;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;                      
SOURCE  15 ORGANISM_COMMON: FISSION YEAST;                                      
SOURCE  16 ORGANISM_TAXID: 284812;                                              
SOURCE  17 STRAIN: STRAIN 972 / ATCC 24843;                                     
SOURCE  18 GENE: UBI2;                                                          
SOURCE  19 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  21 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON PLUS;                      
SOURCE  22 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  23 EXPRESSION_SYSTEM_PLASMID: PET-28                                    
KEYWDS    ROSSMANN-LIKE FOLD, UBIQUITIN-LIKE FOLD, UBIQUITIN ACTIVATING ENZYME  
KEYWDS   2 ACTIVITY, ATP BINDING, LIGASE ACTIVITY, ATP/MG BINDING, UBIQUITIN E2 
KEYWDS   3 BINDING, LIGASE                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.K.OLSEN,C.D.LIMA                                                    
REVDAT   3   15-NOV-17 4II3    1       REMARK                                   
REVDAT   2   27-MAR-13 4II3    1       JRNL                                     
REVDAT   1   13-FEB-13 4II3    0                                                
JRNL        AUTH   S.K.OLSEN,C.D.LIMA                                           
JRNL        TITL   STRUCTURE OF A UBIQUITIN E1-E2 COMPLEX: INSIGHTS TO E1-E2    
JRNL        TITL 2 THIOESTER TRANSFER.                                          
JRNL        REF    MOL.CELL                      V.  49   884 2013              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   23416107                                                     
JRNL        DOI    10.1016/J.MOLCEL.2013.01.013                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 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) : 2.90                           
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)   (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 55008                          
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) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2770                            
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           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.00                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4473                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3887                       
REMARK   3   BIN FREE R VALUE                    : 0.3810                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 217                          
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            : 16623                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 76                                      
REMARK   3   SOLVENT ATOMS            : 149                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.78200                                             
REMARK   3    B22 (A**2) : 1.66300                                              
REMARK   3    B33 (A**2) : 3.11900                                              
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) : 0.005                           
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) : 1.155 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.052 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.548 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.537 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 11.07                                                
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:DNA-RNA_REP.PARAM                   
REMARK   3  PARAMETER FILE  3  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  4  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  5  : CNS_TOPPAR:CARBOHYDRATE.PARAM                  
REMARK   3  PARAMETER FILE  6  : ATP.PAR                                        
REMARK   3  PARAMETER FILE  7  : CIS_PEPTIDE.PARAM                              
REMARK   3  PARAMETER FILE  8  : 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  TOPOLOGY FILE  6   : NULL                                           
REMARK   3  TOPOLOGY FILE  7   : NULL                                           
REMARK   3  TOPOLOGY FILE  8   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4II3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000076779.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-APR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 108                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
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                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55035                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.11300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39700                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3CMM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CACODYLATE, 0.2M CALCIUM     
REMARK 280  ACETATE, 11.5% PEG8000, 3% 1,5 DIAMINOPENTANE, PH 6.5, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       90.25000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.65000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       90.25000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.65000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 4730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A    12                                                      
REMARK 465     ASN A    13                                                      
REMARK 465     ASN A   770                                                      
REMARK 465     GLU A   771                                                      
REMARK 465     ASN A   772                                                      
REMARK 465     GLU A   773                                                      
REMARK 465     GLU A   774                                                      
REMARK 465     ALA A   775                                                      
REMARK 465     PRO A   776                                                      
REMARK 465     GLU A   777                                                      
REMARK 465     THR A   778                                                      
REMARK 465     ALA A   779                                                      
REMARK 465     ALA A   780                                                      
REMARK 465     ASN A   781                                                      
REMARK 465     LYS A   782                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     SER C    12                                                      
REMARK 465     ASN C    13                                                      
REMARK 465     LYS C   766                                                      
REMARK 465     ILE C   767                                                      
REMARK 465     GLN C   768                                                      
REMARK 465     VAL C   769                                                      
REMARK 465     ASN C   770                                                      
REMARK 465     GLU C   771                                                      
REMARK 465     ASN C   772                                                      
REMARK 465     GLU C   773                                                      
REMARK 465     GLU C   774                                                      
REMARK 465     ALA C   775                                                      
REMARK 465     PRO C   776                                                      
REMARK 465     GLU C   777                                                      
REMARK 465     THR C   778                                                      
REMARK 465     PRO C   795                                                      
REMARK 465     PRO C   796                                                      
REMARK 465     PRO C   797                                                      
REMARK 465     SER C   798                                                      
REMARK 465     SER C   799                                                      
REMARK 465     LEU C   800                                                      
REMARK 465     VAL C   801                                                      
REMARK 465     GLY C   802                                                      
REMARK 465     PHE C   803                                                      
REMARK 465     MET D   -19                                                      
REMARK 465     GLY D   -18                                                      
REMARK 465     SER D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     GLY D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     VAL D    -5                                                      
REMARK 465     PRO D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
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    SER A  21      -70.89    -45.73                                   
REMARK 500    ASP A  68       85.99   -162.60                                   
REMARK 500    GLN A  70      151.56    -35.95                                   
REMARK 500    PRO A  71     -139.70    -61.55                                   
REMARK 500    SER A  79       -6.68   -154.42                                   
REMARK 500    TYR A  81        5.42    -60.39                                   
REMARK 500    LEU A 103      -76.32    -66.30                                   
REMARK 500    TYR A 106       -2.38    -57.14                                   
REMARK 500    LYS A 121        3.87    -60.16                                   
REMARK 500    ASN A 169       27.23   -144.53                                   
REMARK 500    ILE A 188      113.47   -169.16                                   
REMARK 500    LEU A 197     -154.45    -67.96                                   
REMARK 500    ASN A 222       26.61    -76.71                                   
REMARK 500    VAL A 242       25.19   -145.13                                   
REMARK 500    ALA A 248      118.62   -175.60                                   
REMARK 500    ASN A 251      107.10      6.91                                   
REMARK 500    PHE A 377      142.21     79.97                                   
REMARK 500    ALA A 452       17.66     59.31                                   
REMARK 500    HIS A 458      128.74    177.09                                   
REMARK 500    ASP A 463      138.60   -178.93                                   
REMARK 500    SER A 501       -5.32    -59.10                                   
REMARK 500    SER A 517       -2.74    -59.18                                   
REMARK 500    GLU A 518       -8.57    -59.06                                   
REMARK 500    GLU A 527       -9.21    -50.08                                   
REMARK 500    LEU A 562       85.46   -154.52                                   
REMARK 500    HIS A 574       25.43     47.31                                   
REMARK 500    LEU A 575      -67.72   -137.67                                   
REMARK 500    PHE A 598       54.00   -118.57                                   
REMARK 500    LYS A 618      -69.72   -133.65                                   
REMARK 500    SER A 629      -53.80   -148.43                                   
REMARK 500    THR A 640      -64.15   -123.06                                   
REMARK 500    SER A 641      133.98    -35.94                                   
REMARK 500    ASN A 643       74.74   -117.67                                   
REMARK 500    VAL A 656      -55.16   -134.41                                   
REMARK 500    LEU A 661       -0.56   -141.48                                   
REMARK 500    ASN A 679      -68.66   -139.41                                   
REMARK 500    LYS A 691       -2.94    -54.57                                   
REMARK 500    PRO A 709     -173.75    -69.37                                   
REMARK 500    THR A 710      109.37   -164.38                                   
REMARK 500    ILE A 716      -17.00    -47.16                                   
REMARK 500    HIS A 717       58.07   -117.33                                   
REMARK 500    PHE A 734      -35.29    -39.07                                   
REMARK 500    ARG A 749       -6.14    -58.92                                   
REMARK 500    PRO A 797      -31.69    -38.87                                   
REMARK 500    MET A 906      149.99    179.78                                   
REMARK 500    ALA A 954      122.32   -170.74                                   
REMARK 500    PRO A 959       -5.73    -57.52                                   
REMARK 500    LEU A 989      110.65   -166.74                                   
REMARK 500    ASP A 997     -166.60    -71.61                                   
REMARK 500    PRO A1006      170.53    -58.46                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     103 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                              MG A1101  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP A1103   O2B                                                    
REMARK 620 2 ATP A1103   O2A  90.8                                              
REMARK 620 3 HOH A1226   O   128.5 131.9                                        
REMARK 620 4 ASP A 537   OD2  75.6  91.0 121.8                                  
REMARK 620 5 ATP A1103   O1G  70.2 106.1  70.8 141.7                            
REMARK 620 6 HOH A1263   O    63.7 151.0  77.0  70.3  79.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C1102  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 468   OE2                                                    
REMARK 620 2 ATP C1103   O1G 112.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1102  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 468   OE2                                                    
REMARK 620 2 ASP A 465   OD2  78.7                                              
REMARK 620 3 ATP A1103   O1B 123.0  75.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C1101  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP C1103   O2B                                                    
REMARK 620 2 HOH C1213   O   113.1                                              
REMARK 620 3 ATP C1103   O2A  75.5 159.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1104  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1202   O                                                      
REMARK 620 2 ASP A 918   OD2 152.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C1104  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 261   OG1                                                    
REMARK 620 2 ASP C 996   OD2 124.1                                              
REMARK 620 3 HOH C1240   O   119.7 111.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C1105  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C1242   O                                                      
REMARK 620 2 HOH C1241   O   128.1                                              
REMARK 620 3 ASP C 918   OD2 104.6  96.3                                        
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 MG A 1101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1106                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1107                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1106                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1107                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1108                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1109                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4II2   RELATED DB: PDB                                   
DBREF  4II3 A   13  1012  UNP    O94609   UBA1_SCHPO      13   1012             
DBREF  4II3 B    1    76  UNP    P0CH07   RL402_SCHPO      1     76             
DBREF  4II3 C   13  1012  UNP    O94609   UBA1_SCHPO      13   1012             
DBREF  4II3 D    1    76  UNP    P0CH07   RL402_SCHPO      1     76             
SEQADV 4II3 SER A   12  UNP  O94609              EXPRESSION TAG                 
SEQADV 4II3 MET B  -19  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 GLY B  -18  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 SER B  -17  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 SER B  -16  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 HIS B  -15  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 HIS B  -14  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 HIS B  -13  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 HIS B  -12  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 HIS B  -11  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 HIS B  -10  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 SER B   -9  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 SER B   -8  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 GLY B   -7  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 LEU B   -6  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 VAL B   -5  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 PRO B   -4  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 ARG B   -3  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 GLY B   -2  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 SER B   -1  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 HIS B    0  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 SER C   12  UNP  O94609              EXPRESSION TAG                 
SEQADV 4II3 MET D  -19  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 GLY D  -18  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 SER D  -17  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 SER D  -16  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 HIS D  -15  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 HIS D  -14  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 HIS D  -13  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 HIS D  -12  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 HIS D  -11  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 HIS D  -10  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 SER D   -9  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 SER D   -8  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 GLY D   -7  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 LEU D   -6  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 VAL D   -5  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 PRO D   -4  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 ARG D   -3  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 GLY D   -2  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 SER D   -1  UNP  P0CH07              EXPRESSION TAG                 
SEQADV 4II3 HIS D    0  UNP  P0CH07              EXPRESSION TAG                 
SEQRES   1 A 1001  SER ASN THR ILE ASP GLU GLY LEU TYR SER ARG GLN LEU          
SEQRES   2 A 1001  TYR VAL LEU GLY HIS GLU ALA MET LYS GLN MET SER GLN          
SEQRES   3 A 1001  SER ASN VAL LEU ILE ILE GLY CYS LYS GLY LEU GLY VAL          
SEQRES   4 A 1001  GLU ILE ALA LYS ASN VAL CYS LEU ALA GLY VAL LYS SER          
SEQRES   5 A 1001  VAL THR LEU TYR ASP PRO GLN PRO THR ARG ILE GLU ASP          
SEQRES   6 A 1001  LEU SER SER GLN TYR PHE LEU THR GLU ASP ASP ILE GLY          
SEQRES   7 A 1001  VAL PRO ARG ALA LYS VAL THR VAL SER LYS LEU ALA GLU          
SEQRES   8 A 1001  LEU ASN GLN TYR VAL PRO VAL SER VAL VAL ASP GLU LEU          
SEQRES   9 A 1001  SER THR GLU TYR LEU LYS ASN PHE LYS CYS VAL VAL VAL          
SEQRES  10 A 1001  THR GLU THR SER LEU THR LYS GLN LEU GLU ILE ASN ASP          
SEQRES  11 A 1001  PHE THR HIS LYS ASN HIS ILE ALA TYR ILE ALA ALA ASP          
SEQRES  12 A 1001  SER ARG GLY LEU PHE GLY SER ILE PHE CYS ASP PHE GLY          
SEQRES  13 A 1001  GLU ASN PHE ILE CYS THR ASP THR ASP GLY ASN GLU PRO          
SEQRES  14 A 1001  LEU THR GLY MET ILE ALA SER ILE THR ASP ASP GLY VAL          
SEQRES  15 A 1001  VAL THR MET LEU GLU GLU THR ARG HIS GLY LEU GLU ASN          
SEQRES  16 A 1001  GLY ASP PHE VAL LYS PHE THR GLU VAL LYS GLY MET PRO          
SEQRES  17 A 1001  GLY LEU ASN ASP GLY THR PRO ARG LYS VAL GLU VAL LYS          
SEQRES  18 A 1001  GLY PRO TYR THR PHE SER ILE GLY SER VAL LYS ASP LEU          
SEQRES  19 A 1001  GLY SER ALA GLY TYR ASN GLY VAL PHE THR GLN VAL LYS          
SEQRES  20 A 1001  VAL PRO THR LYS ILE SER PHE LYS SER LEU ARG GLU SER          
SEQRES  21 A 1001  LEU LYS ASP PRO GLU TYR VAL TYR PRO ASP PHE GLY LYS          
SEQRES  22 A 1001  MET MET ARG PRO PRO GLN TYR HIS ILE ALA PHE GLN ALA          
SEQRES  23 A 1001  LEU SER ALA PHE ALA ASP ALA HIS GLU GLY SER LEU PRO          
SEQRES  24 A 1001  ARG PRO ARG ASN ASP ILE ASP ALA ALA GLU PHE PHE GLU          
SEQRES  25 A 1001  PHE CYS LYS LYS ILE ALA SER THR LEU GLN PHE ASP VAL          
SEQRES  26 A 1001  GLU LEU ASP GLU LYS LEU ILE LYS GLU ILE SER TYR GLN          
SEQRES  27 A 1001  ALA ARG GLY ASP LEU VAL ALA MET SER ALA PHE LEU GLY          
SEQRES  28 A 1001  GLY ALA VAL ALA GLN GLU VAL LEU LYS ALA THR THR SER          
SEQRES  29 A 1001  LYS PHE TYR PRO LEU LYS GLN TYR PHE TYR PHE ASP SER          
SEQRES  30 A 1001  LEU GLU SER LEU PRO SER SER VAL THR ILE SER GLU GLU          
SEQRES  31 A 1001  THR CYS LYS PRO ARG GLY CYS ARG TYR ASP GLY GLN ILE          
SEQRES  32 A 1001  ALA VAL PHE GLY SER GLU PHE GLN GLU LYS ILE ALA SER          
SEQRES  33 A 1001  LEU SER THR PHE LEU VAL GLY ALA GLY ALA ILE GLY CYS          
SEQRES  34 A 1001  GLU MET LEU LYS ASN TRP ALA MET MET GLY VAL ALA THR          
SEQRES  35 A 1001  GLY GLU SER GLY HIS ILE SER VAL THR ASP MET ASP SER          
SEQRES  36 A 1001  ILE GLU LYS SER ASN LEU ASN ARG GLN PHE LEU PHE ARG          
SEQRES  37 A 1001  PRO ARG ASP VAL GLY LYS LEU LYS SER GLU CYS ALA SER          
SEQRES  38 A 1001  THR ALA VAL SER ILE MET ASN PRO SER LEU THR GLY LYS          
SEQRES  39 A 1001  ILE THR SER TYR GLN GLU ARG VAL GLY PRO GLU SER GLU          
SEQRES  40 A 1001  GLY ILE PHE GLY ASP GLU PHE PHE GLU LYS LEU SER LEU          
SEQRES  41 A 1001  VAL THR ASN ALA LEU ASP ASN VAL GLU ALA ARG MET TYR          
SEQRES  42 A 1001  VAL ASP ARG ARG CYS VAL PHE PHE GLU LYS PRO LEU LEU          
SEQRES  43 A 1001  GLU SER GLY THR LEU GLY THR LYS GLY ASN THR GLN VAL          
SEQRES  44 A 1001  VAL VAL PRO HIS LEU THR GLU SER TYR GLY SER SER GLN          
SEQRES  45 A 1001  ASP PRO PRO GLU LYS SER PHE PRO ILE CYS THR LEU LYS          
SEQRES  46 A 1001  ASN PHE PRO ASN ARG ILE GLU HIS THR ILE ALA TRP ALA          
SEQRES  47 A 1001  ARG ASP LEU PHE GLU GLY LEU PHE LYS GLN PRO ILE ASP          
SEQRES  48 A 1001  ASN VAL ASN MET TYR LEU SER SER PRO ASN PHE LEU GLU          
SEQRES  49 A 1001  THR SER LEU LYS THR SER SER ASN PRO ARG GLU VAL LEU          
SEQRES  50 A 1001  GLU ASN ILE ARG ASP TYR LEU VAL THR GLU LYS PRO LEU          
SEQRES  51 A 1001  SER PHE GLU GLU CYS ILE MET TRP ALA ARG LEU GLN PHE          
SEQRES  52 A 1001  ASP LYS PHE PHE ASN ASN ASN ILE GLN GLN LEU LEU PHE          
SEQRES  53 A 1001  ASN PHE PRO LYS ASP SER VAL THR SER THR GLY GLN PRO          
SEQRES  54 A 1001  PHE TRP SER GLY PRO LYS ARG ALA PRO THR PRO LEU SER          
SEQRES  55 A 1001  PHE ASP ILE HIS ASN ARG GLU HIS PHE ASP PHE ILE VAL          
SEQRES  56 A 1001  ALA ALA ALA SER LEU TYR ALA PHE ASN TYR GLY LEU LYS          
SEQRES  57 A 1001  SER GLU THR ASP PRO ALA ILE TYR GLU ARG VAL LEU ALA          
SEQRES  58 A 1001  GLY TYR ASN PRO PRO PRO PHE ALA PRO LYS SER GLY ILE          
SEQRES  59 A 1001  LYS ILE GLN VAL ASN GLU ASN GLU GLU ALA PRO GLU THR          
SEQRES  60 A 1001  ALA ALA ASN LYS ASP LYS GLN GLU LEU LYS SER ILE ALA          
SEQRES  61 A 1001  ASP SER LEU PRO PRO PRO SER SER LEU VAL GLY PHE ARG          
SEQRES  62 A 1001  LEU THR PRO ALA GLU PHE GLU LYS ASP ASP ASP SER ASN          
SEQRES  63 A 1001  HIS HIS ILE ASP PHE ILE THR ALA ALA SER ASN LEU ARG          
SEQRES  64 A 1001  ALA MET ASN TYR ASP ILE THR PRO ALA ASP ARG PHE LYS          
SEQRES  65 A 1001  THR LYS PHE VAL ALA GLY LYS ILE VAL PRO ALA MET CYS          
SEQRES  66 A 1001  THR SER THR ALA VAL VAL SER GLY LEU VAL CYS LEU GLU          
SEQRES  67 A 1001  LEU VAL LYS LEU VAL ASP GLY LYS LYS LYS ILE GLU GLU          
SEQRES  68 A 1001  TYR LYS ASN GLY PHE PHE ASN LEU ALA ILE GLY LEU PHE          
SEQRES  69 A 1001  THR PHE SER ASP PRO ILE ALA SER PRO LYS MET LYS VAL          
SEQRES  70 A 1001  ASN GLY LYS GLU ILE ASP LYS ILE TRP ASP ARG TYR ASN          
SEQRES  71 A 1001  LEU PRO ASP CYS THR LEU GLN GLU LEU ILE ASP TYR PHE          
SEQRES  72 A 1001  GLN LYS GLU GLU GLY LEU GLU VAL THR MET LEU SER SER          
SEQRES  73 A 1001  GLY VAL SER LEU LEU TYR ALA ASN PHE GLN PRO PRO LYS          
SEQRES  74 A 1001  LYS LEU ALA GLU ARG LEU PRO LEU LYS ILE SER GLU LEU          
SEQRES  75 A 1001  VAL GLU GLN ILE THR LYS LYS LYS LEU GLU PRO PHE ARG          
SEQRES  76 A 1001  LYS HIS LEU VAL LEU GLU ILE CYS CYS ASP ASP ALA ASN          
SEQRES  77 A 1001  GLY GLU ASP VAL GLU VAL PRO PHE ILE CYS ILE LYS LEU          
SEQRES   1 B   96  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B   96  LEU VAL PRO ARG GLY SER HIS MET GLN ILE PHE VAL LYS          
SEQRES   3 B   96  THR LEU THR GLY LYS THR ILE THR LEU GLU VAL GLU SER          
SEQRES   4 B   96  SER ASP THR ILE ASP ASN VAL LYS SER LYS ILE GLN ASP          
SEQRES   5 B   96  LYS GLU GLY ILE PRO PRO ASP GLN GLN ARG LEU ILE PHE          
SEQRES   6 B   96  ALA GLY LYS GLN LEU GLU ASP GLY ARG THR LEU SER ASP          
SEQRES   7 B   96  TYR ASN ILE GLN LYS GLU SER THR LEU HIS LEU VAL LEU          
SEQRES   8 B   96  ARG LEU ARG GLY GLY                                          
SEQRES   1 C 1001  SER ASN THR ILE ASP GLU GLY LEU TYR SER ARG GLN LEU          
SEQRES   2 C 1001  TYR VAL LEU GLY HIS GLU ALA MET LYS GLN MET SER GLN          
SEQRES   3 C 1001  SER ASN VAL LEU ILE ILE GLY CYS LYS GLY LEU GLY VAL          
SEQRES   4 C 1001  GLU ILE ALA LYS ASN VAL CYS LEU ALA GLY VAL LYS SER          
SEQRES   5 C 1001  VAL THR LEU TYR ASP PRO GLN PRO THR ARG ILE GLU ASP          
SEQRES   6 C 1001  LEU SER SER GLN TYR PHE LEU THR GLU ASP ASP ILE GLY          
SEQRES   7 C 1001  VAL PRO ARG ALA LYS VAL THR VAL SER LYS LEU ALA GLU          
SEQRES   8 C 1001  LEU ASN GLN TYR VAL PRO VAL SER VAL VAL ASP GLU LEU          
SEQRES   9 C 1001  SER THR GLU TYR LEU LYS ASN PHE LYS CYS VAL VAL VAL          
SEQRES  10 C 1001  THR GLU THR SER LEU THR LYS GLN LEU GLU ILE ASN ASP          
SEQRES  11 C 1001  PHE THR HIS LYS ASN HIS ILE ALA TYR ILE ALA ALA ASP          
SEQRES  12 C 1001  SER ARG GLY LEU PHE GLY SER ILE PHE CYS ASP PHE GLY          
SEQRES  13 C 1001  GLU ASN PHE ILE CYS THR ASP THR ASP GLY ASN GLU PRO          
SEQRES  14 C 1001  LEU THR GLY MET ILE ALA SER ILE THR ASP ASP GLY VAL          
SEQRES  15 C 1001  VAL THR MET LEU GLU GLU THR ARG HIS GLY LEU GLU ASN          
SEQRES  16 C 1001  GLY ASP PHE VAL LYS PHE THR GLU VAL LYS GLY MET PRO          
SEQRES  17 C 1001  GLY LEU ASN ASP GLY THR PRO ARG LYS VAL GLU VAL LYS          
SEQRES  18 C 1001  GLY PRO TYR THR PHE SER ILE GLY SER VAL LYS ASP LEU          
SEQRES  19 C 1001  GLY SER ALA GLY TYR ASN GLY VAL PHE THR GLN VAL LYS          
SEQRES  20 C 1001  VAL PRO THR LYS ILE SER PHE LYS SER LEU ARG GLU SER          
SEQRES  21 C 1001  LEU LYS ASP PRO GLU TYR VAL TYR PRO ASP PHE GLY LYS          
SEQRES  22 C 1001  MET MET ARG PRO PRO GLN TYR HIS ILE ALA PHE GLN ALA          
SEQRES  23 C 1001  LEU SER ALA PHE ALA ASP ALA HIS GLU GLY SER LEU PRO          
SEQRES  24 C 1001  ARG PRO ARG ASN ASP ILE ASP ALA ALA GLU PHE PHE GLU          
SEQRES  25 C 1001  PHE CYS LYS LYS ILE ALA SER THR LEU GLN PHE ASP VAL          
SEQRES  26 C 1001  GLU LEU ASP GLU LYS LEU ILE LYS GLU ILE SER TYR GLN          
SEQRES  27 C 1001  ALA ARG GLY ASP LEU VAL ALA MET SER ALA PHE LEU GLY          
SEQRES  28 C 1001  GLY ALA VAL ALA GLN GLU VAL LEU LYS ALA THR THR SER          
SEQRES  29 C 1001  LYS PHE TYR PRO LEU LYS GLN TYR PHE TYR PHE ASP SER          
SEQRES  30 C 1001  LEU GLU SER LEU PRO SER SER VAL THR ILE SER GLU GLU          
SEQRES  31 C 1001  THR CYS LYS PRO ARG GLY CYS ARG TYR ASP GLY GLN ILE          
SEQRES  32 C 1001  ALA VAL PHE GLY SER GLU PHE GLN GLU LYS ILE ALA SER          
SEQRES  33 C 1001  LEU SER THR PHE LEU VAL GLY ALA GLY ALA ILE GLY CYS          
SEQRES  34 C 1001  GLU MET LEU LYS ASN TRP ALA MET MET GLY VAL ALA THR          
SEQRES  35 C 1001  GLY GLU SER GLY HIS ILE SER VAL THR ASP MET ASP SER          
SEQRES  36 C 1001  ILE GLU LYS SER ASN LEU ASN ARG GLN PHE LEU PHE ARG          
SEQRES  37 C 1001  PRO ARG ASP VAL GLY LYS LEU LYS SER GLU CYS ALA SER          
SEQRES  38 C 1001  THR ALA VAL SER ILE MET ASN PRO SER LEU THR GLY LYS          
SEQRES  39 C 1001  ILE THR SER TYR GLN GLU ARG VAL GLY PRO GLU SER GLU          
SEQRES  40 C 1001  GLY ILE PHE GLY ASP GLU PHE PHE GLU LYS LEU SER LEU          
SEQRES  41 C 1001  VAL THR ASN ALA LEU ASP ASN VAL GLU ALA ARG MET TYR          
SEQRES  42 C 1001  VAL ASP ARG ARG CYS VAL PHE PHE GLU LYS PRO LEU LEU          
SEQRES  43 C 1001  GLU SER GLY THR LEU GLY THR LYS GLY ASN THR GLN VAL          
SEQRES  44 C 1001  VAL VAL PRO HIS LEU THR GLU SER TYR GLY SER SER GLN          
SEQRES  45 C 1001  ASP PRO PRO GLU LYS SER PHE PRO ILE CYS THR LEU LYS          
SEQRES  46 C 1001  ASN PHE PRO ASN ARG ILE GLU HIS THR ILE ALA TRP ALA          
SEQRES  47 C 1001  ARG ASP LEU PHE GLU GLY LEU PHE LYS GLN PRO ILE ASP          
SEQRES  48 C 1001  ASN VAL ASN MET TYR LEU SER SER PRO ASN PHE LEU GLU          
SEQRES  49 C 1001  THR SER LEU LYS THR SER SER ASN PRO ARG GLU VAL LEU          
SEQRES  50 C 1001  GLU ASN ILE ARG ASP TYR LEU VAL THR GLU LYS PRO LEU          
SEQRES  51 C 1001  SER PHE GLU GLU CYS ILE MET TRP ALA ARG LEU GLN PHE          
SEQRES  52 C 1001  ASP LYS PHE PHE ASN ASN ASN ILE GLN GLN LEU LEU PHE          
SEQRES  53 C 1001  ASN PHE PRO LYS ASP SER VAL THR SER THR GLY GLN PRO          
SEQRES  54 C 1001  PHE TRP SER GLY PRO LYS ARG ALA PRO THR PRO LEU SER          
SEQRES  55 C 1001  PHE ASP ILE HIS ASN ARG GLU HIS PHE ASP PHE ILE VAL          
SEQRES  56 C 1001  ALA ALA ALA SER LEU TYR ALA PHE ASN TYR GLY LEU LYS          
SEQRES  57 C 1001  SER GLU THR ASP PRO ALA ILE TYR GLU ARG VAL LEU ALA          
SEQRES  58 C 1001  GLY TYR ASN PRO PRO PRO PHE ALA PRO LYS SER GLY ILE          
SEQRES  59 C 1001  LYS ILE GLN VAL ASN GLU ASN GLU GLU ALA PRO GLU THR          
SEQRES  60 C 1001  ALA ALA ASN LYS ASP LYS GLN GLU LEU LYS SER ILE ALA          
SEQRES  61 C 1001  ASP SER LEU PRO PRO PRO SER SER LEU VAL GLY PHE ARG          
SEQRES  62 C 1001  LEU THR PRO ALA GLU PHE GLU LYS ASP ASP ASP SER ASN          
SEQRES  63 C 1001  HIS HIS ILE ASP PHE ILE THR ALA ALA SER ASN LEU ARG          
SEQRES  64 C 1001  ALA MET ASN TYR ASP ILE THR PRO ALA ASP ARG PHE LYS          
SEQRES  65 C 1001  THR LYS PHE VAL ALA GLY LYS ILE VAL PRO ALA MET CYS          
SEQRES  66 C 1001  THR SER THR ALA VAL VAL SER GLY LEU VAL CYS LEU GLU          
SEQRES  67 C 1001  LEU VAL LYS LEU VAL ASP GLY LYS LYS LYS ILE GLU GLU          
SEQRES  68 C 1001  TYR LYS ASN GLY PHE PHE ASN LEU ALA ILE GLY LEU PHE          
SEQRES  69 C 1001  THR PHE SER ASP PRO ILE ALA SER PRO LYS MET LYS VAL          
SEQRES  70 C 1001  ASN GLY LYS GLU ILE ASP LYS ILE TRP ASP ARG TYR ASN          
SEQRES  71 C 1001  LEU PRO ASP CYS THR LEU GLN GLU LEU ILE ASP TYR PHE          
SEQRES  72 C 1001  GLN LYS GLU GLU GLY LEU GLU VAL THR MET LEU SER SER          
SEQRES  73 C 1001  GLY VAL SER LEU LEU TYR ALA ASN PHE GLN PRO PRO LYS          
SEQRES  74 C 1001  LYS LEU ALA GLU ARG LEU PRO LEU LYS ILE SER GLU LEU          
SEQRES  75 C 1001  VAL GLU GLN ILE THR LYS LYS LYS LEU GLU PRO PHE ARG          
SEQRES  76 C 1001  LYS HIS LEU VAL LEU GLU ILE CYS CYS ASP ASP ALA ASN          
SEQRES  77 C 1001  GLY GLU ASP VAL GLU VAL PRO PHE ILE CYS ILE LYS LEU          
SEQRES   1 D   96  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D   96  LEU VAL PRO ARG GLY SER HIS MET GLN ILE PHE VAL LYS          
SEQRES   3 D   96  THR LEU THR GLY LYS THR ILE THR LEU GLU VAL GLU SER          
SEQRES   4 D   96  SER ASP THR ILE ASP ASN VAL LYS SER LYS ILE GLN ASP          
SEQRES   5 D   96  LYS GLU GLY ILE PRO PRO ASP GLN GLN ARG LEU ILE PHE          
SEQRES   6 D   96  ALA GLY LYS GLN LEU GLU ASP GLY ARG THR LEU SER ASP          
SEQRES   7 D   96  TYR ASN ILE GLN LYS GLU SER THR LEU HIS LEU VAL LEU          
SEQRES   8 D   96  ARG LEU ARG GLY GLY                                          
HET     MG  A1101       1                                                       
HET     MG  A1102       1                                                       
HET    ATP  A1103      31                                                       
HET     CA  A1104       1                                                       
HET     CA  A1105       1                                                       
HET     CA  A1106       1                                                       
HET     CA  A1107       1                                                       
HET     MG  C1101       1                                                       
HET     MG  C1102       1                                                       
HET    ATP  C1103      31                                                       
HET     CA  C1104       1                                                       
HET     CA  C1105       1                                                       
HET     CA  C1106       1                                                       
HET     CA  C1107       1                                                       
HET     CA  C1108       1                                                       
HET     CA  C1109       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM      CA CALCIUM ION                                                      
FORMUL   5   MG    4(MG 2+)                                                     
FORMUL   7  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL   8   CA    10(CA 2+)                                                    
FORMUL  21  HOH   *149(H2 O)                                                    
HELIX    1   1 TYR A   20  GLY A   28  1                                   9    
HELIX    2   2 GLY A   28  SER A   36  1                                   9    
HELIX    3   3 LYS A   46  GLY A   60  1                                  15    
HELIX    4   4 ARG A   73  SER A   79  5                                   7    
HELIX    5   5 THR A   84  ILE A   88  5                                   5    
HELIX    6   6 PRO A   91  ALA A  101  1                                  11    
HELIX    7   7 THR A  117  PHE A  123  5                                   7    
HELIX    8   8 SER A  132  ASN A  146  1                                  15    
HELIX    9   9 MET A  218  GLY A  224  5                                   7    
HELIX   10  10 SER A  267  LEU A  272  1                                   6    
HELIX   11  11 ARG A  287  HIS A  305  1                                  19    
HELIX   12  12 ASN A  314  LEU A  332  1                                  19    
HELIX   13  13 ASP A  339  GLN A  349  1                                  11    
HELIX   14  14 ALA A  350  GLY A  352  5                                   3    
HELIX   15  15 LEU A  354  THR A  373  1                                  20    
HELIX   16  16 LEU A  389  LEU A  392  5                                   4    
HELIX   17  17 TYR A  410  GLY A  418  1                                   9    
HELIX   18  18 GLY A  418  SER A  427  1                                  10    
HELIX   19  19 GLY A  436  GLY A  450  1                                  15    
HELIX   20  20 GLU A  468  ARG A  474  5                                   7    
HELIX   21  21 ARG A  479  VAL A  483  5                                   5    
HELIX   22  22 LEU A  486  ASN A  499  1                                  14    
HELIX   23  23 PRO A  500  THR A  503  5                                   4    
HELIX   24  24 PRO A  515  ILE A  520  5                                   6    
HELIX   25  25 GLY A  522  GLU A  527  1                                   6    
HELIX   26  26 ASN A  538  PHE A  552  1                                  15    
HELIX   27  27 SER A  578  SER A  582  5                                   5    
HELIX   28  28 PRO A  591  ASN A  597  1                                   7    
HELIX   29  29 ARG A  601  LYS A  618  1                                  18    
HELIX   30  30 LYS A  618  LEU A  628  1                                  11    
HELIX   31  31 ASN A  632  THR A  640  1                                   9    
HELIX   32  32 ASN A  643  VAL A  656  1                                  14    
HELIX   33  33 SER A  662  ASN A  679  1                                  18    
HELIX   34  34 ASN A  679  PHE A  689  1                                  11    
HELIX   35  35 ASN A  718  GLY A  737  1                                  20    
HELIX   36  36 ASP A  743  ALA A  752  1                                  10    
HELIX   37  37 GLN A  785  ALA A  791  1                                   7    
HELIX   38  38 PRO A  796  VAL A  801  5                                   6    
HELIX   39  39 HIS A  818  TYR A  834  1                                  17    
HELIX   40  40 ASP A  840  GLY A  849  1                                  10    
HELIX   41  41 MET A  855  ASP A  875  1                                  21    
HELIX   42  42 LYS A  879  TYR A  883  5                                   5    
HELIX   43  43 ALA A  891  GLY A  893  5                                   3    
HELIX   44  44 THR A  926  GLU A  937  1                                  12    
HELIX   45  45 PRO A  958  LEU A  966  1                                   9    
HELIX   46  46 LYS A  969  LYS A  979  1                                  11    
HELIX   47  47 THR B   22  GLY B   35  1                                  14    
HELIX   48  48 PRO B   37  GLN B   41  5                                   5    
HELIX   49  49 THR B   55  ASN B   60  5                                   6    
HELIX   50  50 TYR C   20  GLY C   28  1                                   9    
HELIX   51  51 GLY C   28  SER C   36  1                                   9    
HELIX   52  52 LYS C   46  GLY C   60  1                                  15    
HELIX   53  53 ARG C   73  SER C   79  5                                   7    
HELIX   54  54 THR C   84  ILE C   88  5                                   5    
HELIX   55  55 PRO C   91  ALA C  101  1                                  11    
HELIX   56  56 THR C  117  PHE C  123  5                                   7    
HELIX   57  57 SER C  132  ASN C  146  1                                  15    
HELIX   58  58 MET C  218  GLY C  224  5                                   7    
HELIX   59  59 SER C  267  LEU C  272  1                                   6    
HELIX   60  60 ARG C  287  HIS C  305  1                                  19    
HELIX   61  61 ASN C  314  LEU C  332  1                                  19    
HELIX   62  62 ASP C  339  GLN C  349  1                                  11    
HELIX   63  63 ALA C  350  GLY C  352  5                                   3    
HELIX   64  64 LEU C  354  THR C  373  1                                  20    
HELIX   65  65 LEU C  389  LEU C  392  5                                   4    
HELIX   66  66 TYR C  410  GLY C  418  1                                   9    
HELIX   67  67 GLY C  418  SER C  427  1                                  10    
HELIX   68  68 GLY C  436  GLY C  450  1                                  15    
HELIX   69  69 GLU C  468  ARG C  474  5                                   7    
HELIX   70  70 ARG C  479  VAL C  483  5                                   5    
HELIX   71  71 LEU C  486  ASN C  499  1                                  14    
HELIX   72  72 PRO C  500  THR C  503  5                                   4    
HELIX   73  73 GLU C  516  ILE C  520  5                                   5    
HELIX   74  74 GLY C  522  GLU C  527  1                                   6    
HELIX   75  75 ASN C  538  PHE C  552  1                                  15    
HELIX   76  76 SER C  578  SER C  582  5                                   5    
HELIX   77  77 PRO C  591  ASN C  597  1                                   7    
HELIX   78  78 ARG C  601  LYS C  618  1                                  18    
HELIX   79  79 LYS C  618  LEU C  628  1                                  11    
HELIX   80  80 ASN C  632  THR C  640  1                                   9    
HELIX   81  81 ASN C  643  VAL C  656  1                                  14    
HELIX   82  82 SER C  662  ASN C  679  1                                  18    
HELIX   83  83 ASN C  679  PHE C  689  1                                  11    
HELIX   84  84 ASN C  718  GLY C  737  1                                  20    
HELIX   85  85 ASP C  743  ALA C  752  1                                  10    
HELIX   86  86 LYS C  782  ALA C  791  1                                  10    
HELIX   87  87 HIS C  818  TYR C  834  1                                  17    
HELIX   88  88 ASP C  840  GLY C  849  1                                  10    
HELIX   89  89 MET C  855  ASP C  875  1                                  21    
HELIX   90  90 LYS C  879  TYR C  883  5                                   5    
HELIX   91  91 ALA C  891  GLY C  893  5                                   3    
HELIX   92  92 THR C  926  GLU C  937  1                                  12    
HELIX   93  93 PRO C  958  GLU C  964  1                                   7    
HELIX   94  94 LYS C  969  LYS C  979  1                                  11    
HELIX   95  95 THR D   22  GLY D   35  1                                  14    
HELIX   96  96 PRO D   37  GLN D   41  5                                   5    
HELIX   97  97 THR D   55  ASN D   60  5                                   6    
SHEET    1   A 7 VAL A 109  VAL A 111  0                                        
SHEET    2   A 7 SER A  63  TYR A  67  1  N  LEU A  66   O  SER A 110           
SHEET    3   A 7 ASN A  39  ILE A  43  1  N  ILE A  42   O  THR A  65           
SHEET    4   A 7 CYS A 125  THR A 129  1  O  VAL A 127   N  LEU A  41           
SHEET    5   A 7 ALA A 149  ARG A 156  1  O  ILE A 151   N  VAL A 128           
SHEET    6   A 7 PHE A 159  ASP A 165 -1  O  ASP A 165   N  TYR A 150           
SHEET    7   A 7 TYR A 383  ASP A 387 -1  O  PHE A 384   N  ILE A 162           
SHEET    1   B 2 PHE A 170  CYS A 172  0                                        
SHEET    2   B 2 THR A 261  ILE A 263 -1  O  THR A 261   N  CYS A 172           
SHEET    1   C 7 ARG A 227  LYS A 228  0                                        
SHEET    2   C 7 PHE A 209  THR A 213 -1  N  VAL A 210   O  ARG A 227           
SHEET    3   C 7 VAL A 253  VAL A 257 -1  O  VAL A 257   N  PHE A 209           
SHEET    4   C 7 THR A 182  THR A 189 -1  N  GLY A 183   O  PHE A 254           
SHEET    5   C 7 VAL A 193  MET A 196 -1  O  THR A 195   N  ALA A 186           
SHEET    6   C 7 THR A 236  SER A 238 -1  O  PHE A 237   N  VAL A 194           
SHEET    7   C 7 GLU A 230  VAL A 231 -1  N  GLU A 230   O  SER A 238           
SHEET    1   D 5 ARG A 227  LYS A 228  0                                        
SHEET    2   D 5 PHE A 209  THR A 213 -1  N  VAL A 210   O  ARG A 227           
SHEET    3   D 5 VAL A 253  VAL A 257 -1  O  VAL A 257   N  PHE A 209           
SHEET    4   D 5 THR A 182  THR A 189 -1  N  GLY A 183   O  PHE A 254           
SHEET    5   D 5 ALA A 248  TYR A 250 -1  O  GLY A 249   N  ILE A 188           
SHEET    1   E 8 ILE A 506  TYR A 509  0                                        
SHEET    2   E 8 ILE A 459  THR A 462  1  N  ILE A 459   O  THR A 507           
SHEET    3   E 8 THR A 430  VAL A 433  1  N  LEU A 432   O  SER A 460           
SHEET    4   E 8 LEU A 531  ASN A 534  1  O  THR A 533   N  VAL A 433           
SHEET    5   E 8 LEU A 556  LEU A 562  1  O  LEU A 557   N  ASN A 534           
SHEET    6   E 8 LYS A 565  VAL A 571 -1  O  LYS A 565   N  LEU A 562           
SHEET    7   E 8 ASN A 885  ASN A 889 -1  O  GLY A 886   N  THR A 568           
SHEET    8   E 8 LEU A 894  SER A 898 -1  O  SER A 898   N  ASN A 885           
SHEET    1   F 2 LYS A 907  VAL A 908  0                                        
SHEET    2   F 2 LYS A 911  GLU A 912 -1  O  LYS A 911   N  VAL A 908           
SHEET    1   G 5 TYR A 920  LEU A 922  0                                        
SHEET    2   G 5 ILE A1008  ILE A1010  1  O  CYS A1009   N  TYR A 920           
SHEET    3   G 5 VAL A 990  ASP A 996 -1  N  LEU A 991   O  ILE A1008           
SHEET    4   G 5 GLU A 941  SER A 947 -1  N  THR A 943   O  CYS A 994           
SHEET    5   G 5 SER A 950  ALA A 954 -1  O  TYR A 953   N  LEU A 945           
SHEET    1   H 4 TYR A 920  LEU A 922  0                                        
SHEET    2   H 4 ILE A1008  ILE A1010  1  O  CYS A1009   N  TYR A 920           
SHEET    3   H 4 VAL A 990  ASP A 996 -1  N  LEU A 991   O  ILE A1008           
SHEET    4   H 4 ASP A1002  VAL A1003 -1  O  VAL A1003   N  CYS A 995           
SHEET    1   I 5 THR B  12  GLU B  16  0                                        
SHEET    2   I 5 GLN B   2  THR B   7 -1  N  VAL B   5   O  ILE B  13           
SHEET    3   I 5 THR B  66  VAL B  70  1  O  LEU B  67   N  PHE B   4           
SHEET    4   I 5 ARG B  42  PHE B  45 -1  N  ILE B  44   O  HIS B  68           
SHEET    5   I 5 LYS B  48  GLN B  49 -1  O  LYS B  48   N  PHE B  45           
SHEET    1   J 7 VAL C 109  VAL C 111  0                                        
SHEET    2   J 7 SER C  63  TYR C  67  1  N  LEU C  66   O  SER C 110           
SHEET    3   J 7 ASN C  39  ILE C  43  1  N  ILE C  42   O  THR C  65           
SHEET    4   J 7 CYS C 125  THR C 129  1  O  VAL C 127   N  LEU C  41           
SHEET    5   J 7 ALA C 149  ARG C 156  1  O  ILE C 151   N  VAL C 128           
SHEET    6   J 7 PHE C 159  ASP C 165 -1  O  PHE C 163   N  ALA C 152           
SHEET    7   J 7 TYR C 383  ASP C 387 -1  O  PHE C 384   N  ILE C 162           
SHEET    1   K 2 PHE C 170  CYS C 172  0                                        
SHEET    2   K 2 THR C 261  ILE C 263 -1  O  THR C 261   N  CYS C 172           
SHEET    1   L 7 ARG C 227  LYS C 228  0                                        
SHEET    2   L 7 PHE C 209  THR C 213 -1  N  VAL C 210   O  ARG C 227           
SHEET    3   L 7 VAL C 253  VAL C 257 -1  O  VAL C 257   N  PHE C 209           
SHEET    4   L 7 THR C 182  THR C 189 -1  N  GLY C 183   O  PHE C 254           
SHEET    5   L 7 VAL C 193  MET C 196 -1  O  THR C 195   N  SER C 187           
SHEET    6   L 7 THR C 236  SER C 238 -1  O  PHE C 237   N  VAL C 194           
SHEET    7   L 7 GLU C 230  VAL C 231 -1  N  GLU C 230   O  SER C 238           
SHEET    1   M 5 ARG C 227  LYS C 228  0                                        
SHEET    2   M 5 PHE C 209  THR C 213 -1  N  VAL C 210   O  ARG C 227           
SHEET    3   M 5 VAL C 253  VAL C 257 -1  O  VAL C 257   N  PHE C 209           
SHEET    4   M 5 THR C 182  THR C 189 -1  N  GLY C 183   O  PHE C 254           
SHEET    5   M 5 ALA C 248  TYR C 250 -1  O  GLY C 249   N  ILE C 188           
SHEET    1   N 8 ILE C 506  TYR C 509  0                                        
SHEET    2   N 8 ILE C 459  THR C 462  1  N  ILE C 459   O  THR C 507           
SHEET    3   N 8 LEU C 432  VAL C 433  1  N  LEU C 432   O  SER C 460           
SHEET    4   N 8 VAL C 532  ASN C 534  1  O  THR C 533   N  VAL C 433           
SHEET    5   N 8 LEU C 556  LEU C 562  1  O  LEU C 557   N  ASN C 534           
SHEET    6   N 8 LYS C 565  VAL C 571 -1  O  GLN C 569   N  GLU C 558           
SHEET    7   N 8 ASN C 885  ASN C 889 -1  O  GLY C 886   N  THR C 568           
SHEET    8   N 8 LEU C 894  SER C 898 -1  O  SER C 898   N  ASN C 885           
SHEET    1   O 2 LYS C 907  VAL C 908  0                                        
SHEET    2   O 2 LYS C 911  GLU C 912 -1  O  LYS C 911   N  VAL C 908           
SHEET    1   P 5 ARG C 919  LEU C 922  0                                        
SHEET    2   P 5 PHE C1007  ILE C1010  1  O  PHE C1007   N  TYR C 920           
SHEET    3   P 5 VAL C 990  ASP C 996 -1  N  LEU C 991   O  ILE C1008           
SHEET    4   P 5 GLU C 941  SER C 947 -1  N  THR C 943   O  CYS C 994           
SHEET    5   P 5 SER C 950  ALA C 954 -1  O  TYR C 953   N  LEU C 945           
SHEET    1   Q 4 ARG C 919  LEU C 922  0                                        
SHEET    2   Q 4 PHE C1007  ILE C1010  1  O  PHE C1007   N  TYR C 920           
SHEET    3   Q 4 VAL C 990  ASP C 996 -1  N  LEU C 991   O  ILE C1008           
SHEET    4   Q 4 ASP C1002  VAL C1003 -1  O  VAL C1003   N  CYS C 995           
SHEET    1   R 5 THR D  12  GLU D  16  0                                        
SHEET    2   R 5 GLN D   2  THR D   7 -1  N  ILE D   3   O  LEU D  15           
SHEET    3   R 5 THR D  66  VAL D  70  1  O  LEU D  67   N  PHE D   4           
SHEET    4   R 5 ARG D  42  PHE D  45 -1  N  ILE D  44   O  HIS D  68           
SHEET    5   R 5 LYS D  48  GLN D  49 -1  O  LYS D  48   N  PHE D  45           
LINK        MG    MG A1101                 O2B ATP A1103     1555   1555  2.35  
LINK        MG    MG A1101                 O2A ATP A1103     1555   1555  2.40  
LINK        MG    MG A1101                 O   HOH A1226     1555   1555  2.58  
LINK         OD2 ASP A 537                MG    MG A1101     1555   1555  2.62  
LINK         OE2 GLU C 468                MG    MG C1102     1555   1555  2.64  
LINK         OE2 GLU A 468                MG    MG A1102     1555   1555  2.66  
LINK        MG    MG A1101                 O1G ATP A1103     1555   1555  2.67  
LINK        MG    MG C1101                 O2B ATP C1103     1555   1555  2.70  
LINK        MG    MG C1101                 O   HOH C1213     1555   1555  2.70  
LINK        MG    MG C1101                 O2A ATP C1103     1555   1555  2.71  
LINK         OD2 ASP A 465                MG    MG A1102     1555   1555  2.73  
LINK        MG    MG A1101                 O   HOH A1263     1555   1555  2.75  
LINK        CA    CA A1104                 O   HOH A1202     1555   1555  2.83  
LINK         OG1 THR A 261                CA    CA C1104     1555   1555  2.85  
LINK         OD2 ASP C 996                CA    CA C1104     1555   1555  2.88  
LINK        CA    CA C1105                 O   HOH C1242     1555   1555  2.88  
LINK         O   THR C 657                CA    CA C1109     1555   1555  2.91  
LINK        MG    MG A1102                 O1B ATP A1103     1555   1555  2.94  
LINK         OD2 ASP A 918                CA    CA A1104     1555   1555  2.94  
LINK        CA    CA C1104                 O   HOH C1240     1555   1555  2.95  
LINK        CA    CA C1105                 O   HOH C1241     1555   1555  2.96  
LINK        MG    MG C1102                 O1G ATP C1103     1555   1555  2.97  
LINK        CA    CA A1105                 O   HOH A1230     1555   1555  3.00  
LINK         OE1 GLU A 938                CA    CA A1107     1555   1555  3.01  
LINK         OD2 ASP C 918                CA    CA C1105     1555   1555  3.08  
LINK        CA    CA A1106                 O   HOH A1231     1555   1555  3.10  
LINK         OE1 GLU C 938                CA    CA C1107     1555   1555  3.15  
LINK        CA    CA C1108                 O   HOH C1211     1555   1555  3.16  
CISPEP   1 LYS A  381    GLN A  382          0        -0.14                     
CISPEP   2 LYS C  381    GLN C  382          0         0.16                     
SITE     1 AC1  4 ASP A 537  ATP A1103  HOH A1226  HOH A1263                    
SITE     1 AC2  3 ASP A 465  GLU A 468  ATP A1103                               
SITE     1 AC3 20 ARG A  22  GLY A 436  ALA A 437  ASP A 463                    
SITE     2 AC3 20 MET A 464  ASP A 465  ARG A 474  LYS A 487                    
SITE     3 AC3 20 VAL A 513  ALA A 535  ASP A 537  ASN A 538                    
SITE     4 AC3 20 ALA A 541   MG A1101   MG A1102  HOH A1226                    
SITE     5 AC3 20 HOH A1246  HOH A1259  HOH A1263  GLY B  76                    
SITE     1 AC4  2 ASP A 918  HOH A1202                                          
SITE     1 AC5  2 GLU A 205  HOH A1230                                          
SITE     1 AC6  1 GLU A 665                                                     
SITE     1 AC7  2 TYR A 920  GLU A 938                                          
SITE     1 AC8  3 ASP C 537  ATP C1103  HOH C1213                               
SITE     1 AC9  3 ASP C 465  GLU C 468  ATP C1103                               
SITE     1 BC1 18 ARG C  22  GLY C 436  ALA C 437  ASP C 463                    
SITE     2 BC1 18 MET C 464  ASP C 465  ASN C 471  ARG C 474                    
SITE     3 BC1 18 LYS C 487  ARG C 512  VAL C 513  ALA C 535                    
SITE     4 BC1 18 ASP C 537  ASN C 538   MG C1101   MG C1102                    
SITE     5 BC1 18 HOH C1213  GLY D  76                                          
SITE     1 BC2  4 THR A 261  ASP C 996  GLY C1000  HOH C1240                    
SITE     1 BC3  3 ASP C 918  HOH C1241  HOH C1242                               
SITE     1 BC4  2 ASP C 611  GLN C 619                                          
SITE     1 BC5  1 GLU C 938                                                     
SITE     1 BC6  1 TYR C 920                                                     
SITE     1 BC7  1 THR C 657                                                     
CRYST1  180.500  113.300  126.600  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005540  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008826  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007899        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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