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Database: PDB
Entry: 1BR1
LinkDB: 1BR1
Original site: 1BR1 
HEADER    MUSCLE PROTEIN                          26-AUG-98   1BR1              
TITLE     SMOOTH MUSCLE MYOSIN MOTOR DOMAIN-ESSENTIAL LIGHT CHAIN COMPLEX WITH  
TITLE    2 MGADP.ALF4 BOUND AT THE ACTIVE SITE                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOSIN;                                                    
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 FRAGMENT: CHAINS A, C, E, G, MOTOR DOMAIN, CHAINS B, D, F, H,        
COMPND   5 ESSENTIAL LIGHT;                                                     
COMPND   6 SYNONYM: MDE;                                                        
COMPND   7 EC: 3.6.1.32;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: MG, ADP, ALF(4);                                      
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: MYOSIN;                                                    
COMPND  12 CHAIN: B, D, F, H;                                                   
COMPND  13 FRAGMENT: CHAINS A, C, E, G, MOTOR DOMAIN, CHAINS B, D, F, H,        
COMPND  14 ESSENTIAL LIGHT;                                                     
COMPND  15 SYNONYM: MDE;                                                        
COMPND  16 EC: 3.6.1.32;                                                        
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 OTHER_DETAILS: MG, ADP, ALF(4)                                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE   3 ORGANISM_COMMON: CHICKEN;                                            
SOURCE   4 ORGANISM_TAXID: 9031;                                                
SOURCE   5 CELL_LINE: SF9;                                                      
SOURCE   6 ORGAN: GIZZARD;                                                      
SOURCE   7 TISSUE: SMOOTH MUSCLE;                                               
SOURCE   8 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   9 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  11 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  12 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;                               
SOURCE  13 MOL_ID: 2;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE  15 ORGANISM_COMMON: CHICKEN;                                            
SOURCE  16 ORGANISM_TAXID: 9031;                                                
SOURCE  17 CELL_LINE: SF9;                                                      
SOURCE  18 ORGAN: GIZZARD;                                                      
SOURCE  19 TISSUE: SMOOTH MUSCLE;                                               
SOURCE  20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  21 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  22 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  23 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  24 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS                                
KEYWDS    MUSCLE PROTEIN                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.DOMINGUEZ,K.M.TRYBUS,C.COHEN                                        
REVDAT   5   07-FEB-24 1BR1    1       REMARK LINK                              
REVDAT   4   24-FEB-09 1BR1    1       VERSN                                    
REVDAT   3   30-SEP-03 1BR1    1       DBREF                                    
REVDAT   2   08-JUN-99 1BR1    3       HET    COMPND REMARK HETATM              
REVDAT   2 2                   3       DBREF  SEQADV SCALE  HEADER              
REVDAT   2 3                   3       TER    SOURCE ATOM   SEQRES              
REVDAT   2 4                   3       FORMUL JRNL   HETSYN CONECT              
REVDAT   1   09-SEP-98 1BR1    0                                                
JRNL        AUTH   R.DOMINGUEZ,Y.FREYZON,K.M.TRYBUS,C.COHEN                     
JRNL        TITL   CRYSTAL STRUCTURE OF A VERTEBRATE SMOOTH MUSCLE MYOSIN MOTOR 
JRNL        TITL 2 DOMAIN AND ITS COMPLEX WITH THE ESSENTIAL LIGHT CHAIN:       
JRNL        TITL 3 VISUALIZATION OF THE PRE-POWER STROKE STATE.                 
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V.  94   559 1998              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   9741621                                                      
JRNL        DOI    10.1016/S0092-8674(00)81598-6                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 0.000                          
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 76805                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.305                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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            : 29992                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 132                                     
REMARK   3   SOLVENT ATOMS            : 8                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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) : 0.60                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 27.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.700                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINTS                                              
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1BR1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000172016.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : MAY-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.905                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79993                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.7                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.82                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.30100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 9.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.851                                          
REMARK 200 STARTING MODEL: SMOOTH MUSCLE MYOSIN MOTOR DOMAIN                    
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM SULFATE 100MM HEPES PH     
REMARK 280  7.2 2MM MGADP 2MM AL(NO3)3 8MM NAF PROTEIN CONCENTRATION: 10MG/     
REMARK 280  ML TEMPERATURE: 4 DEGREES CENTIGRADE, TEMPERATURE 277K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: 5380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 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: 5390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 5330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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: 4                                                       
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: 5220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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     LYS A   205                                                      
REMARK 465     ASP A   206                                                      
REMARK 465     THR A   207                                                      
REMARK 465     SER A   208                                                      
REMARK 465     ILE A   209                                                      
REMARK 465     THR A   210                                                      
REMARK 465     LYS A   452                                                      
REMARK 465     THR A   453                                                      
REMARK 465     LYS A   454                                                      
REMARK 465     ARG A   455                                                      
REMARK 465     GLN A   456                                                      
REMARK 465     GLY A   457                                                      
REMARK 465     ASP A   635                                                      
REMARK 465     GLN A   636                                                      
REMARK 465     MET A   637                                                      
REMARK 465     ALA A   638                                                      
REMARK 465     LYS A   639                                                      
REMARK 465     MET A   640                                                      
REMARK 465     THR A   641                                                      
REMARK 465     GLU A   642                                                      
REMARK 465     SER A   643                                                      
REMARK 465     SER A   644                                                      
REMARK 465     LEU A   645                                                      
REMARK 465     PRO A   646                                                      
REMARK 465     SER A   647                                                      
REMARK 465     ALA A   648                                                      
REMARK 465     SER A   649                                                      
REMARK 465     LYS A   650                                                      
REMARK 465     THR A   651                                                      
REMARK 465     LYS A   652                                                      
REMARK 465     LYS A   653                                                      
REMARK 465     GLY A   654                                                      
REMARK 465     MET A   655                                                      
REMARK 465     CYS B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     LYS C   205                                                      
REMARK 465     ASP C   206                                                      
REMARK 465     THR C   207                                                      
REMARK 465     SER C   208                                                      
REMARK 465     ILE C   209                                                      
REMARK 465     THR C   210                                                      
REMARK 465     LYS C   452                                                      
REMARK 465     THR C   453                                                      
REMARK 465     LYS C   454                                                      
REMARK 465     ARG C   455                                                      
REMARK 465     GLN C   456                                                      
REMARK 465     GLY C   457                                                      
REMARK 465     ASP C   635                                                      
REMARK 465     GLN C   636                                                      
REMARK 465     MET C   637                                                      
REMARK 465     ALA C   638                                                      
REMARK 465     LYS C   639                                                      
REMARK 465     MET C   640                                                      
REMARK 465     THR C   641                                                      
REMARK 465     GLU C   642                                                      
REMARK 465     SER C   643                                                      
REMARK 465     SER C   644                                                      
REMARK 465     LEU C   645                                                      
REMARK 465     PRO C   646                                                      
REMARK 465     SER C   647                                                      
REMARK 465     ALA C   648                                                      
REMARK 465     SER C   649                                                      
REMARK 465     LYS C   650                                                      
REMARK 465     THR C   651                                                      
REMARK 465     LYS C   652                                                      
REMARK 465     LYS C   653                                                      
REMARK 465     GLY C   654                                                      
REMARK 465     MET C   655                                                      
REMARK 465     CYS D     1                                                      
REMARK 465     ASP D     2                                                      
REMARK 465     LYS E   205                                                      
REMARK 465     ASP E   206                                                      
REMARK 465     THR E   207                                                      
REMARK 465     SER E   208                                                      
REMARK 465     ILE E   209                                                      
REMARK 465     THR E   210                                                      
REMARK 465     LYS E   452                                                      
REMARK 465     THR E   453                                                      
REMARK 465     LYS E   454                                                      
REMARK 465     ARG E   455                                                      
REMARK 465     GLN E   456                                                      
REMARK 465     GLY E   457                                                      
REMARK 465     ASP E   635                                                      
REMARK 465     GLN E   636                                                      
REMARK 465     MET E   637                                                      
REMARK 465     ALA E   638                                                      
REMARK 465     LYS E   639                                                      
REMARK 465     MET E   640                                                      
REMARK 465     THR E   641                                                      
REMARK 465     GLU E   642                                                      
REMARK 465     SER E   643                                                      
REMARK 465     SER E   644                                                      
REMARK 465     LEU E   645                                                      
REMARK 465     PRO E   646                                                      
REMARK 465     SER E   647                                                      
REMARK 465     ALA E   648                                                      
REMARK 465     SER E   649                                                      
REMARK 465     LYS E   650                                                      
REMARK 465     THR E   651                                                      
REMARK 465     LYS E   652                                                      
REMARK 465     LYS E   653                                                      
REMARK 465     GLY E   654                                                      
REMARK 465     MET E   655                                                      
REMARK 465     CYS F     1                                                      
REMARK 465     ASP F     2                                                      
REMARK 465     LYS G   205                                                      
REMARK 465     ASP G   206                                                      
REMARK 465     THR G   207                                                      
REMARK 465     SER G   208                                                      
REMARK 465     ILE G   209                                                      
REMARK 465     THR G   210                                                      
REMARK 465     LYS G   452                                                      
REMARK 465     THR G   453                                                      
REMARK 465     LYS G   454                                                      
REMARK 465     ARG G   455                                                      
REMARK 465     GLN G   456                                                      
REMARK 465     GLY G   457                                                      
REMARK 465     ASP G   635                                                      
REMARK 465     GLN G   636                                                      
REMARK 465     MET G   637                                                      
REMARK 465     ALA G   638                                                      
REMARK 465     LYS G   639                                                      
REMARK 465     MET G   640                                                      
REMARK 465     THR G   641                                                      
REMARK 465     GLU G   642                                                      
REMARK 465     SER G   643                                                      
REMARK 465     SER G   644                                                      
REMARK 465     LEU G   645                                                      
REMARK 465     PRO G   646                                                      
REMARK 465     SER G   647                                                      
REMARK 465     ALA G   648                                                      
REMARK 465     SER G   649                                                      
REMARK 465     LYS G   650                                                      
REMARK 465     THR G   651                                                      
REMARK 465     LYS G   652                                                      
REMARK 465     LYS G   653                                                      
REMARK 465     GLY G   654                                                      
REMARK 465     MET G   655                                                      
REMARK 465     CYS H     1                                                      
REMARK 465     ASP H     2                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    CYS F    84     N    ASP F    87              1.99            
REMARK 500   O    TRP A   625     N    ASP A   627              2.10            
REMARK 500   O    TYR E   663     N    GLU E   665              2.17            
REMARK 500   O    TYR C   663     N    GLU C   665              2.18            
REMARK 500   O    TRP G   625     N    ASP G   627              2.19            
REMARK 500   O    TYR G   663     N    GLU G   665              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CE1  PHE E    19     OE2  GLU G   786     1556     1.59            
REMARK 500   CD1  PHE E    19     OE2  GLU G   786     1556     1.66            
REMARK 500   N    ASP D    23     NH2  ARG G   371     1545     1.81            
REMARK 500   N    GLY D    22     CZ   ARG G   371     1545     1.88            
REMARK 500   CE1  PHE E    19     CD   GLU G   786     1556     1.91            
REMARK 500   NH1  ARG A   371     N    GLY F    22     1544     1.91            
REMARK 500   CA   GLY D    22     NE   ARG G   371     1545     1.96            
REMARK 500   N    GLY D    22     NH1  ARG G   371     1545     1.96            
REMARK 500   C    GLY D    22     NE   ARG G   371     1545     2.07            
REMARK 500   NE   ARG A   371     CA   GLY F    22     1544     2.09            
REMARK 500   CG   ASP D    23     NH2  ARG G   371     1545     2.11            
REMARK 500   OG1  THR D    21     NH1  ARG G   371     1545     2.11            
REMARK 500   NE   ARG A   371     C    GLY F    22     1544     2.13            
REMARK 500   N    GLY D    22     NE   ARG G   371     1545     2.14            
REMARK 500   CD1  PHE E    19     CD   GLU G   786     1556     2.15            
REMARK 500   NE   ARG A   371     O    GLY F    22     1544     2.18            
REMARK 500   CZ   ARG A   371     CA   GLY F    22     1544     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    MET A  78   CG  -  SD  -  CE  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG A 107   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 247   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A 279   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A 285   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A 630   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A 715   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    MET C  78   CG  -  SD  -  CE  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG C 107   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG C 247   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG C 285   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG C 630   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG C 715   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG C 815   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    MET E  78   CG  -  SD  -  CE  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG E 107   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG E 247   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG E 285   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG E 630   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG E 715   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG E 815   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    GLY F  22   N   -  CA  -  C   ANGL. DEV. =  16.4 DEGREES          
REMARK 500    PHE F  85   CA  -  C   -  N   ANGL. DEV. = -15.8 DEGREES          
REMARK 500    MET G  78   CG  -  SD  -  CE  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG G 107   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    MET G 164   CG  -  SD  -  CE  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG G 168   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG G 247   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG G 285   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG G 630   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG G 715   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 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    LYS A   4      170.73    -42.71                                   
REMARK 500    ALA A  31       34.76    -71.22                                   
REMARK 500    LYS A  32      -32.94    -33.04                                   
REMARK 500    LYS A  33        7.14    -61.63                                   
REMARK 500    PRO A  38      160.05    -31.19                                   
REMARK 500    SER A  39      109.32   -176.62                                   
REMARK 500    GLU A  40       10.52    -69.15                                   
REMARK 500    LYS A  41      -11.23   -144.00                                   
REMARK 500    GLU A  51      117.38   -164.75                                   
REMARK 500    GLN A  62       21.15    -72.58                                   
REMARK 500    GLU A  63      -77.74   -121.49                                   
REMARK 500    LYS A  72       28.96    -70.20                                   
REMARK 500    MET A  89      -35.89    -34.26                                   
REMARK 500    ALA A  90        7.43    -60.55                                   
REMARK 500    THR A  93        4.91    -68.21                                   
REMARK 500    GLU A 106      -76.18    -55.79                                   
REMARK 500    VAL A 123       69.62   -157.54                                   
REMARK 500    TYR A 127       -0.46     78.87                                   
REMARK 500    PRO A 131       70.53   -106.15                                   
REMARK 500    LYS A 145     -168.06    -53.69                                   
REMARK 500    GLU A 148        6.55    -61.12                                   
REMARK 500    ARG A 168       80.37     43.87                                   
REMARK 500    GLU A 169       96.54   -169.69                                   
REMARK 500    ASP A 170      149.66    -28.32                                   
REMARK 500    THR A 176     -151.88    -91.26                                   
REMARK 500    ALA A 181        4.14    -53.73                                   
REMARK 500    ASN A 186      -18.28    -49.38                                   
REMARK 500    LYS A 202       38.40    -87.85                                   
REMARK 500    SER A 214      107.11    -57.84                                   
REMARK 500    PHE A 215      134.56    175.84                                   
REMARK 500    ILE A 230      -61.97    -90.28                                   
REMARK 500    ALA A 233      -82.25    -69.70                                   
REMARK 500    VAL A 240        1.87    -56.94                                   
REMARK 500    ASN A 242      115.08   -168.44                                   
REMARK 500    ARG A 247       34.79    -90.82                                   
REMARK 500    PHE A 248      132.22    176.97                                   
REMARK 500    TYR A 270     -127.17   -125.02                                   
REMARK 500    LEU A 271       78.84    -65.46                                   
REMARK 500    GLU A 273       66.80    -61.04                                   
REMARK 500    ARG A 276       -6.63    -41.53                                   
REMARK 500    HIS A 288      -66.12    -17.10                                   
REMARK 500    GLN A 300      -74.82    -55.36                                   
REMARK 500    PHE A 332      -70.06    -52.10                                   
REMARK 500    PHE A 344      109.45    -54.47                                   
REMARK 500    GLU A 348      -13.20    -46.24                                   
REMARK 500    ILE A 352      -10.88    -48.49                                   
REMARK 500    VAL A 359       -5.28    -55.89                                   
REMARK 500    LEU A 362       -3.68    -48.80                                   
REMARK 500    ILE A 365      125.16    -37.94                                   
REMARK 500    LYS A 369      159.24    -45.46                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     545 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 A 997  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 184   OG1                                                    
REMARK 620 2 SER A 246   OG   75.7                                              
REMARK 620 3 HOH A 995   O    94.8  78.8                                        
REMARK 620 4 ADP A 998   O2B  86.9 160.6  94.3                                  
REMARK 620 5 ALF A 999   F2  152.2  97.2  57.5  94.2                            
REMARK 620 6 ALF A 999   F4  143.6 134.9 108.7  64.5  57.7                      
REMARK 620 7 ALF A 999  AL   160.7 122.5  83.7  74.0  31.6  26.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             ALF A 999  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 245   OG                                                     
REMARK 620 2 ALF A 999   F1  141.3                                              
REMARK 620 3 ALF A 999   F2   38.1 177.4                                        
REMARK 620 4 ALF A 999   F3   53.9  88.4  90.5                                  
REMARK 620 5 ALF A 999   F4  126.7  91.3  89.8 177.7                            
REMARK 620 6 HOH A 995   O    73.6 143.0  36.6 120.1  59.3                      
REMARK 620 7 ADP A 998   O1B 137.5  62.9 115.8 116.4  61.5  82.4                
REMARK 620 8 ADP A 998   O2B 119.0  96.4  83.2 144.3  33.5  46.6  40.6          
REMARK 620 9 ADP A 998   O3B  95.3 100.4  77.5 100.3  77.6  54.5  42.7  44.1    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 997  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 184   OG1                                                    
REMARK 620 2 SER C 246   OG   73.9                                              
REMARK 620 3 HOH C 995   O    91.4  76.3                                        
REMARK 620 4 ADP C 998   O2B  88.7 159.7  94.3                                  
REMARK 620 5 ALF C 999   F2  148.8  95.6  57.4  94.2                            
REMARK 620 6 ALF C 999   F4  146.9 135.4 108.6  64.5  57.7                      
REMARK 620 7 ALF C 999  AL   161.5 121.8  83.7  74.0  31.7  26.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             ALF C 999  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY C 468   N                                                      
REMARK 620 2 ALF C 999   F1   35.6                                              
REMARK 620 3 ALF C 999   F2  146.8 177.4                                        
REMARK 620 4 ALF C 999   F3   94.8  88.3  90.5                                  
REMARK 620 5 ALF C 999   F4   86.2  91.3  89.8 177.7                            
REMARK 620 6 HOH C 995   O   143.8 143.0  36.6 120.1  59.3                      
REMARK 620 7 ADP C 998   O3B 133.1 100.5  77.5 100.2  77.6  54.5                
REMARK 620 8 ADP C 998   O2B 109.5  96.4  83.2 144.3  33.5  46.6  44.1          
REMARK 620 9 ADP C 998   O1B  91.0  62.9 115.8 116.4  61.5  82.4  42.7  40.6    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 997  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR E 184   OG1                                                    
REMARK 620 2 SER E 246   OG   72.7                                              
REMARK 620 3 HOH E 995   O    88.9  74.7                                        
REMARK 620 4 ADP E 998   O2B  92.6 161.5  94.3                                  
REMARK 620 5 ALF E 999   F2  146.0  92.1  57.4  94.2                            
REMARK 620 6 ALF E 999   F4  151.5 132.7 108.7  64.5  57.7                      
REMARK 620 7 ALF E 999  AL   164.2 118.3  83.7  74.0  31.7  26.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             ALF E 999  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY E 468   N                                                      
REMARK 620 2 ALF E 999   F1   38.1                                              
REMARK 620 3 ALF E 999   F2  144.3 177.4                                        
REMARK 620 4 ALF E 999   F3   92.8  88.3  90.4                                  
REMARK 620 5 ALF E 999   F4   88.3  91.4  89.8 177.8                            
REMARK 620 6 HOH E 995   O   144.9 143.0  36.6 120.1  59.3                      
REMARK 620 7 ADP E 998   O3B 136.4 100.5  77.5 100.3  77.6  54.5                
REMARK 620 8 ADP E 998   O1B  94.4  62.9 115.8 116.4  61.6  82.4  42.7          
REMARK 620 9 ADP E 998   O2B 112.6  96.5  83.2 144.3  33.6  46.6  44.1  40.6    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G 997  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR G 184   OG1                                                    
REMARK 620 2 SER G 246   OG   74.4                                              
REMARK 620 3 HOH G 995   O    91.7  76.1                                        
REMARK 620 4 ADP G 998   O2B  91.1 162.2  94.3                                  
REMARK 620 5 ALF G 999   F2  148.9  93.1  57.4  94.3                            
REMARK 620 6 ALF G 999   F4  148.7 132.6 108.6  64.5  57.7                      
REMARK 620 7 ALF G 999  AL   164.0 118.9  83.7  74.0  31.7  26.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             ALF G 999  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY G 468   N                                                      
REMARK 620 2 ALF G 999   F1   37.2                                              
REMARK 620 3 ALF G 999   F2  145.2 177.5                                        
REMARK 620 4 ALF G 999   F3   93.4  88.3  90.4                                  
REMARK 620 5 ALF G 999   F4   87.7  91.3  89.8 177.7                            
REMARK 620 6 HOH G 995   O   144.6 143.1  36.6 120.1  59.3                      
REMARK 620 7 ADP G 998   O3B 135.2 100.5  77.5 100.3  77.6  54.5                
REMARK 620 8 ADP G 998   O2B 111.6  96.5  83.2 144.3  33.5  46.6  44.1          
REMARK 620 9 ADP G 998   O1B  93.2  62.9 115.8 116.4  61.5  82.4  42.7  40.6    
REMARK 620 N                    1     2     3     4     5     6     7     8     
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 997                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF A 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 997                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF C 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 997                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF E 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 997                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF G 999                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 998                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 998                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 998                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 998                 
DBREF  1BR1 A    3   819  UNP    P10587   MYH11_CHICK      2    818             
DBREF  1BR1 B    1   150  UNP    P02607   MLES_CHICK       1    150             
DBREF  1BR1 C    3   819  UNP    P10587   MYH11_CHICK      2    818             
DBREF  1BR1 D    1   150  UNP    P02607   MLES_CHICK       1    150             
DBREF  1BR1 E    3   819  UNP    P10587   MYH11_CHICK      2    818             
DBREF  1BR1 F    1   150  UNP    P02607   MLES_CHICK       1    150             
DBREF  1BR1 G    3   819  UNP    P10587   MYH11_CHICK      2    818             
DBREF  1BR1 H    1   150  UNP    P02607   MLES_CHICK       1    150             
SEQRES   1 A  820  ALA GLN LYS PRO LEU SER ASP ASP GLU LYS PHE LEU PHE          
SEQRES   2 A  820  VAL ASP LYS ASN PHE VAL ASN ASN PRO LEU ALA GLN ALA          
SEQRES   3 A  820  ASP TRP SER ALA LYS LYS LEU VAL TRP VAL PRO SER GLU          
SEQRES   4 A  820  LYS HIS GLY PHE GLU ALA ALA SER ILE LYS GLU GLU LYS          
SEQRES   5 A  820  GLY ASP GLU VAL THR VAL GLU LEU GLN GLU ASN GLY LYS          
SEQRES   6 A  820  LYS VAL THR LEU SER LYS ASP ASP ILE GLN LYS MET ASN          
SEQRES   7 A  820  PRO PRO LYS PHE SER LYS VAL GLU ASP MET ALA GLU LEU          
SEQRES   8 A  820  THR CYS LEU ASN GLU ALA SER VAL LEU HIS ASN LEU ARG          
SEQRES   9 A  820  GLU ARG TYR PHE SER GLY LEU ILE TYR THR TYR SER GLY          
SEQRES  10 A  820  LEU PHE CYS VAL VAL ILE ASN PRO TYR LYS GLN LEU PRO          
SEQRES  11 A  820  ILE TYR SER GLU LYS ILE ILE ASP MET TYR LYS GLY LYS          
SEQRES  12 A  820  LYS ARG HIS GLU MET PRO PRO HIS ILE TYR ALA ILE ALA          
SEQRES  13 A  820  ASP THR ALA TYR ARG SER MET LEU GLN ASP ARG GLU ASP          
SEQRES  14 A  820  GLN SER ILE LEU CYS THR GLY GLU SER GLY ALA GLY LYS          
SEQRES  15 A  820  THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU ALA VAL          
SEQRES  16 A  820  VAL ALA SER SER HIS LYS GLY LYS LYS ASP THR SER ILE          
SEQRES  17 A  820  THR GLN GLY PRO SER PHE SER TYR GLY GLU LEU GLU LYS          
SEQRES  18 A  820  GLN LEU LEU GLN ALA ASN PRO ILE LEU GLU ALA PHE GLY          
SEQRES  19 A  820  ASN ALA LYS THR VAL LYS ASN ASP ASN SER SER ARG PHE          
SEQRES  20 A  820  GLY LYS PHE ILE ARG ILE ASN PHE ASP VAL THR GLY TYR          
SEQRES  21 A  820  ILE VAL GLY ALA ASN ILE GLU THR TYR LEU LEU GLU LYS          
SEQRES  22 A  820  SER ARG ALA ILE ARG GLN ALA LYS ASP GLU ARG THR PHE          
SEQRES  23 A  820  HIS ILE PHE TYR TYR LEU ILE ALA GLY ALA SER GLU GLN          
SEQRES  24 A  820  MET ARG ASN ASP LEU LEU LEU GLU GLY PHE ASN ASN TYR          
SEQRES  25 A  820  THR PHE LEU SER ASN GLY HIS VAL PRO ILE PRO ALA GLN          
SEQRES  26 A  820  GLN ASP ASP GLU MET PHE GLN GLU THR LEU GLU ALA MET          
SEQRES  27 A  820  THR ILE MET GLY PHE THR GLU GLU GLU GLN THR SER ILE          
SEQRES  28 A  820  LEU ARG VAL VAL SER SER VAL LEU GLN LEU GLY ASN ILE          
SEQRES  29 A  820  VAL PHE LYS LYS GLU ARG ASN THR ASP GLN ALA SER MET          
SEQRES  30 A  820  PRO ASP ASN THR ALA ALA GLN LYS VAL CYS HIS LEU MET          
SEQRES  31 A  820  GLY ILE ASN VAL THR ASP PHE THR ARG SER ILE LEU THR          
SEQRES  32 A  820  PRO ARG ILE LYS VAL GLY ARG ASP VAL VAL GLN LYS ALA          
SEQRES  33 A  820  GLN THR LYS GLU GLN ALA ASP PHE ALA ILE GLU ALA LEU          
SEQRES  34 A  820  ALA LYS ALA LYS PHE GLU ARG LEU PHE ARG TRP ILE LEU          
SEQRES  35 A  820  THR ARG VAL ASN LYS ALA LEU ASP LYS THR LYS ARG GLN          
SEQRES  36 A  820  GLY ALA SER PHE LEU GLY ILE LEU ASP ILE ALA GLY PHE          
SEQRES  37 A  820  GLU ILE PHE GLU ILE ASN SER PHE GLU GLN LEU CYS ILE          
SEQRES  38 A  820  ASN TYR THR ASN GLU LYS LEU GLN GLN LEU PHE ASN HIS          
SEQRES  39 A  820  THR MET PHE ILE LEU GLU GLN GLU GLU TYR GLN ARG GLU          
SEQRES  40 A  820  GLY ILE GLU TRP ASN PHE ILE ASP PHE GLY LEU ASP LEU          
SEQRES  41 A  820  GLN PRO CYS ILE GLU LEU ILE GLU ARG PRO THR ASN PRO          
SEQRES  42 A  820  PRO GLY VAL LEU ALA LEU LEU ASP GLU GLU CYS TRP PHE          
SEQRES  43 A  820  PRO LYS ALA THR ASP THR SER PHE VAL GLU LYS LEU ILE          
SEQRES  44 A  820  GLN GLU GLN GLY ASN HIS ALA LYS PHE GLN LYS SER LYS          
SEQRES  45 A  820  GLN LEU LYS ASP LYS THR GLU PHE CYS ILE LEU HIS TYR          
SEQRES  46 A  820  ALA GLY LYS VAL THR TYR ASN ALA SER ALA TRP LEU THR          
SEQRES  47 A  820  LYS ASN MET ASP PRO LEU ASN ASP ASN VAL THR SER LEU          
SEQRES  48 A  820  LEU ASN GLN SER SER ASP LYS PHE VAL ALA ASP LEU TRP          
SEQRES  49 A  820  LYS ASP VAL ASP ARG ILE VAL GLY LEU ASP GLN MET ALA          
SEQRES  50 A  820  LYS MET THR GLU SER SER LEU PRO SER ALA SER LYS THR          
SEQRES  51 A  820  LYS LYS GLY MET PHE ARG THR VAL GLY GLN LEU TYR LYS          
SEQRES  52 A  820  GLU GLN LEU THR LYS LEU MET THR THR LEU ARG ASN THR          
SEQRES  53 A  820  ASN PRO ASN PHE VAL ARG CYS ILE ILE PRO ASN HIS GLU          
SEQRES  54 A  820  LYS ARG ALA GLY LYS LEU ASP ALA HIS LEU VAL LEU GLU          
SEQRES  55 A  820  GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE ARG ILE          
SEQRES  56 A  820  CYS ARG GLN GLY PHE PRO ASN ARG ILE VAL PHE GLN GLU          
SEQRES  57 A  820  PHE ARG GLN ARG TYR GLU ILE LEU ALA ALA ASN ALA ILE          
SEQRES  58 A  820  PRO LYS GLY PHE MET ASP GLY LYS GLN ALA CYS ILE LEU          
SEQRES  59 A  820  MET ILE LYS ALA LEU GLU LEU ASP PRO ASN LEU TYR ARG          
SEQRES  60 A  820  ILE GLY GLN SER LYS ILE PHE PHE ARG THR GLY VAL LEU          
SEQRES  61 A  820  ALA HIS LEU GLU GLU GLU ARG ASP LEU LYS ILE THR ASP          
SEQRES  62 A  820  VAL ILE ILE ALA PHE GLN ALA GLN CYS ARG GLY TYR LEU          
SEQRES  63 A  820  ALA ARG LYS ALA PHE ALA LYS ARG GLN GLN GLN LEU GLY          
SEQRES  64 A  820  SER                                                          
SEQRES   1 B  150  CYS ASP PHE SER GLU GLU GLN THR ALA GLU PHE LYS GLU          
SEQRES   2 B  150  ALA PHE GLN LEU PHE ASP ARG THR GLY ASP GLY LYS ILE          
SEQRES   3 B  150  LEU TYR SER GLN CYS GLY ASP VAL MET ARG ALA LEU GLY          
SEQRES   4 B  150  GLN ASN PRO THR ASN ALA GLU VAL MET LYS VAL LEU GLY          
SEQRES   5 B  150  ASN PRO LYS SER ASP GLU MET ASN LEU LYS THR LEU LYS          
SEQRES   6 B  150  PHE GLU GLN PHE LEU PRO MET MET GLN THR ILE ALA LYS          
SEQRES   7 B  150  ASN LYS ASP GLN GLY CYS PHE GLU ASP TYR VAL GLU GLY          
SEQRES   8 B  150  LEU ARG VAL PHE ASP LYS GLU GLY ASN GLY THR VAL MET          
SEQRES   9 B  150  GLY ALA GLU ILE ARG HIS VAL LEU VAL THR LEU GLY GLU          
SEQRES  10 B  150  LYS MET THR GLU GLU GLU VAL GLU GLN LEU VAL ALA GLY          
SEQRES  11 B  150  HIS GLU ASP SER ASN GLY CYS ILE ASN TYR GLU GLU LEU          
SEQRES  12 B  150  VAL ARG MET VAL LEU SER GLY                                  
SEQRES   1 C  820  ALA GLN LYS PRO LEU SER ASP ASP GLU LYS PHE LEU PHE          
SEQRES   2 C  820  VAL ASP LYS ASN PHE VAL ASN ASN PRO LEU ALA GLN ALA          
SEQRES   3 C  820  ASP TRP SER ALA LYS LYS LEU VAL TRP VAL PRO SER GLU          
SEQRES   4 C  820  LYS HIS GLY PHE GLU ALA ALA SER ILE LYS GLU GLU LYS          
SEQRES   5 C  820  GLY ASP GLU VAL THR VAL GLU LEU GLN GLU ASN GLY LYS          
SEQRES   6 C  820  LYS VAL THR LEU SER LYS ASP ASP ILE GLN LYS MET ASN          
SEQRES   7 C  820  PRO PRO LYS PHE SER LYS VAL GLU ASP MET ALA GLU LEU          
SEQRES   8 C  820  THR CYS LEU ASN GLU ALA SER VAL LEU HIS ASN LEU ARG          
SEQRES   9 C  820  GLU ARG TYR PHE SER GLY LEU ILE TYR THR TYR SER GLY          
SEQRES  10 C  820  LEU PHE CYS VAL VAL ILE ASN PRO TYR LYS GLN LEU PRO          
SEQRES  11 C  820  ILE TYR SER GLU LYS ILE ILE ASP MET TYR LYS GLY LYS          
SEQRES  12 C  820  LYS ARG HIS GLU MET PRO PRO HIS ILE TYR ALA ILE ALA          
SEQRES  13 C  820  ASP THR ALA TYR ARG SER MET LEU GLN ASP ARG GLU ASP          
SEQRES  14 C  820  GLN SER ILE LEU CYS THR GLY GLU SER GLY ALA GLY LYS          
SEQRES  15 C  820  THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU ALA VAL          
SEQRES  16 C  820  VAL ALA SER SER HIS LYS GLY LYS LYS ASP THR SER ILE          
SEQRES  17 C  820  THR GLN GLY PRO SER PHE SER TYR GLY GLU LEU GLU LYS          
SEQRES  18 C  820  GLN LEU LEU GLN ALA ASN PRO ILE LEU GLU ALA PHE GLY          
SEQRES  19 C  820  ASN ALA LYS THR VAL LYS ASN ASP ASN SER SER ARG PHE          
SEQRES  20 C  820  GLY LYS PHE ILE ARG ILE ASN PHE ASP VAL THR GLY TYR          
SEQRES  21 C  820  ILE VAL GLY ALA ASN ILE GLU THR TYR LEU LEU GLU LYS          
SEQRES  22 C  820  SER ARG ALA ILE ARG GLN ALA LYS ASP GLU ARG THR PHE          
SEQRES  23 C  820  HIS ILE PHE TYR TYR LEU ILE ALA GLY ALA SER GLU GLN          
SEQRES  24 C  820  MET ARG ASN ASP LEU LEU LEU GLU GLY PHE ASN ASN TYR          
SEQRES  25 C  820  THR PHE LEU SER ASN GLY HIS VAL PRO ILE PRO ALA GLN          
SEQRES  26 C  820  GLN ASP ASP GLU MET PHE GLN GLU THR LEU GLU ALA MET          
SEQRES  27 C  820  THR ILE MET GLY PHE THR GLU GLU GLU GLN THR SER ILE          
SEQRES  28 C  820  LEU ARG VAL VAL SER SER VAL LEU GLN LEU GLY ASN ILE          
SEQRES  29 C  820  VAL PHE LYS LYS GLU ARG ASN THR ASP GLN ALA SER MET          
SEQRES  30 C  820  PRO ASP ASN THR ALA ALA GLN LYS VAL CYS HIS LEU MET          
SEQRES  31 C  820  GLY ILE ASN VAL THR ASP PHE THR ARG SER ILE LEU THR          
SEQRES  32 C  820  PRO ARG ILE LYS VAL GLY ARG ASP VAL VAL GLN LYS ALA          
SEQRES  33 C  820  GLN THR LYS GLU GLN ALA ASP PHE ALA ILE GLU ALA LEU          
SEQRES  34 C  820  ALA LYS ALA LYS PHE GLU ARG LEU PHE ARG TRP ILE LEU          
SEQRES  35 C  820  THR ARG VAL ASN LYS ALA LEU ASP LYS THR LYS ARG GLN          
SEQRES  36 C  820  GLY ALA SER PHE LEU GLY ILE LEU ASP ILE ALA GLY PHE          
SEQRES  37 C  820  GLU ILE PHE GLU ILE ASN SER PHE GLU GLN LEU CYS ILE          
SEQRES  38 C  820  ASN TYR THR ASN GLU LYS LEU GLN GLN LEU PHE ASN HIS          
SEQRES  39 C  820  THR MET PHE ILE LEU GLU GLN GLU GLU TYR GLN ARG GLU          
SEQRES  40 C  820  GLY ILE GLU TRP ASN PHE ILE ASP PHE GLY LEU ASP LEU          
SEQRES  41 C  820  GLN PRO CYS ILE GLU LEU ILE GLU ARG PRO THR ASN PRO          
SEQRES  42 C  820  PRO GLY VAL LEU ALA LEU LEU ASP GLU GLU CYS TRP PHE          
SEQRES  43 C  820  PRO LYS ALA THR ASP THR SER PHE VAL GLU LYS LEU ILE          
SEQRES  44 C  820  GLN GLU GLN GLY ASN HIS ALA LYS PHE GLN LYS SER LYS          
SEQRES  45 C  820  GLN LEU LYS ASP LYS THR GLU PHE CYS ILE LEU HIS TYR          
SEQRES  46 C  820  ALA GLY LYS VAL THR TYR ASN ALA SER ALA TRP LEU THR          
SEQRES  47 C  820  LYS ASN MET ASP PRO LEU ASN ASP ASN VAL THR SER LEU          
SEQRES  48 C  820  LEU ASN GLN SER SER ASP LYS PHE VAL ALA ASP LEU TRP          
SEQRES  49 C  820  LYS ASP VAL ASP ARG ILE VAL GLY LEU ASP GLN MET ALA          
SEQRES  50 C  820  LYS MET THR GLU SER SER LEU PRO SER ALA SER LYS THR          
SEQRES  51 C  820  LYS LYS GLY MET PHE ARG THR VAL GLY GLN LEU TYR LYS          
SEQRES  52 C  820  GLU GLN LEU THR LYS LEU MET THR THR LEU ARG ASN THR          
SEQRES  53 C  820  ASN PRO ASN PHE VAL ARG CYS ILE ILE PRO ASN HIS GLU          
SEQRES  54 C  820  LYS ARG ALA GLY LYS LEU ASP ALA HIS LEU VAL LEU GLU          
SEQRES  55 C  820  GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE ARG ILE          
SEQRES  56 C  820  CYS ARG GLN GLY PHE PRO ASN ARG ILE VAL PHE GLN GLU          
SEQRES  57 C  820  PHE ARG GLN ARG TYR GLU ILE LEU ALA ALA ASN ALA ILE          
SEQRES  58 C  820  PRO LYS GLY PHE MET ASP GLY LYS GLN ALA CYS ILE LEU          
SEQRES  59 C  820  MET ILE LYS ALA LEU GLU LEU ASP PRO ASN LEU TYR ARG          
SEQRES  60 C  820  ILE GLY GLN SER LYS ILE PHE PHE ARG THR GLY VAL LEU          
SEQRES  61 C  820  ALA HIS LEU GLU GLU GLU ARG ASP LEU LYS ILE THR ASP          
SEQRES  62 C  820  VAL ILE ILE ALA PHE GLN ALA GLN CYS ARG GLY TYR LEU          
SEQRES  63 C  820  ALA ARG LYS ALA PHE ALA LYS ARG GLN GLN GLN LEU GLY          
SEQRES  64 C  820  SER                                                          
SEQRES   1 D  150  CYS ASP PHE SER GLU GLU GLN THR ALA GLU PHE LYS GLU          
SEQRES   2 D  150  ALA PHE GLN LEU PHE ASP ARG THR GLY ASP GLY LYS ILE          
SEQRES   3 D  150  LEU TYR SER GLN CYS GLY ASP VAL MET ARG ALA LEU GLY          
SEQRES   4 D  150  GLN ASN PRO THR ASN ALA GLU VAL MET LYS VAL LEU GLY          
SEQRES   5 D  150  ASN PRO LYS SER ASP GLU MET ASN LEU LYS THR LEU LYS          
SEQRES   6 D  150  PHE GLU GLN PHE LEU PRO MET MET GLN THR ILE ALA LYS          
SEQRES   7 D  150  ASN LYS ASP GLN GLY CYS PHE GLU ASP TYR VAL GLU GLY          
SEQRES   8 D  150  LEU ARG VAL PHE ASP LYS GLU GLY ASN GLY THR VAL MET          
SEQRES   9 D  150  GLY ALA GLU ILE ARG HIS VAL LEU VAL THR LEU GLY GLU          
SEQRES  10 D  150  LYS MET THR GLU GLU GLU VAL GLU GLN LEU VAL ALA GLY          
SEQRES  11 D  150  HIS GLU ASP SER ASN GLY CYS ILE ASN TYR GLU GLU LEU          
SEQRES  12 D  150  VAL ARG MET VAL LEU SER GLY                                  
SEQRES   1 E  820  ALA GLN LYS PRO LEU SER ASP ASP GLU LYS PHE LEU PHE          
SEQRES   2 E  820  VAL ASP LYS ASN PHE VAL ASN ASN PRO LEU ALA GLN ALA          
SEQRES   3 E  820  ASP TRP SER ALA LYS LYS LEU VAL TRP VAL PRO SER GLU          
SEQRES   4 E  820  LYS HIS GLY PHE GLU ALA ALA SER ILE LYS GLU GLU LYS          
SEQRES   5 E  820  GLY ASP GLU VAL THR VAL GLU LEU GLN GLU ASN GLY LYS          
SEQRES   6 E  820  LYS VAL THR LEU SER LYS ASP ASP ILE GLN LYS MET ASN          
SEQRES   7 E  820  PRO PRO LYS PHE SER LYS VAL GLU ASP MET ALA GLU LEU          
SEQRES   8 E  820  THR CYS LEU ASN GLU ALA SER VAL LEU HIS ASN LEU ARG          
SEQRES   9 E  820  GLU ARG TYR PHE SER GLY LEU ILE TYR THR TYR SER GLY          
SEQRES  10 E  820  LEU PHE CYS VAL VAL ILE ASN PRO TYR LYS GLN LEU PRO          
SEQRES  11 E  820  ILE TYR SER GLU LYS ILE ILE ASP MET TYR LYS GLY LYS          
SEQRES  12 E  820  LYS ARG HIS GLU MET PRO PRO HIS ILE TYR ALA ILE ALA          
SEQRES  13 E  820  ASP THR ALA TYR ARG SER MET LEU GLN ASP ARG GLU ASP          
SEQRES  14 E  820  GLN SER ILE LEU CYS THR GLY GLU SER GLY ALA GLY LYS          
SEQRES  15 E  820  THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU ALA VAL          
SEQRES  16 E  820  VAL ALA SER SER HIS LYS GLY LYS LYS ASP THR SER ILE          
SEQRES  17 E  820  THR GLN GLY PRO SER PHE SER TYR GLY GLU LEU GLU LYS          
SEQRES  18 E  820  GLN LEU LEU GLN ALA ASN PRO ILE LEU GLU ALA PHE GLY          
SEQRES  19 E  820  ASN ALA LYS THR VAL LYS ASN ASP ASN SER SER ARG PHE          
SEQRES  20 E  820  GLY LYS PHE ILE ARG ILE ASN PHE ASP VAL THR GLY TYR          
SEQRES  21 E  820  ILE VAL GLY ALA ASN ILE GLU THR TYR LEU LEU GLU LYS          
SEQRES  22 E  820  SER ARG ALA ILE ARG GLN ALA LYS ASP GLU ARG THR PHE          
SEQRES  23 E  820  HIS ILE PHE TYR TYR LEU ILE ALA GLY ALA SER GLU GLN          
SEQRES  24 E  820  MET ARG ASN ASP LEU LEU LEU GLU GLY PHE ASN ASN TYR          
SEQRES  25 E  820  THR PHE LEU SER ASN GLY HIS VAL PRO ILE PRO ALA GLN          
SEQRES  26 E  820  GLN ASP ASP GLU MET PHE GLN GLU THR LEU GLU ALA MET          
SEQRES  27 E  820  THR ILE MET GLY PHE THR GLU GLU GLU GLN THR SER ILE          
SEQRES  28 E  820  LEU ARG VAL VAL SER SER VAL LEU GLN LEU GLY ASN ILE          
SEQRES  29 E  820  VAL PHE LYS LYS GLU ARG ASN THR ASP GLN ALA SER MET          
SEQRES  30 E  820  PRO ASP ASN THR ALA ALA GLN LYS VAL CYS HIS LEU MET          
SEQRES  31 E  820  GLY ILE ASN VAL THR ASP PHE THR ARG SER ILE LEU THR          
SEQRES  32 E  820  PRO ARG ILE LYS VAL GLY ARG ASP VAL VAL GLN LYS ALA          
SEQRES  33 E  820  GLN THR LYS GLU GLN ALA ASP PHE ALA ILE GLU ALA LEU          
SEQRES  34 E  820  ALA LYS ALA LYS PHE GLU ARG LEU PHE ARG TRP ILE LEU          
SEQRES  35 E  820  THR ARG VAL ASN LYS ALA LEU ASP LYS THR LYS ARG GLN          
SEQRES  36 E  820  GLY ALA SER PHE LEU GLY ILE LEU ASP ILE ALA GLY PHE          
SEQRES  37 E  820  GLU ILE PHE GLU ILE ASN SER PHE GLU GLN LEU CYS ILE          
SEQRES  38 E  820  ASN TYR THR ASN GLU LYS LEU GLN GLN LEU PHE ASN HIS          
SEQRES  39 E  820  THR MET PHE ILE LEU GLU GLN GLU GLU TYR GLN ARG GLU          
SEQRES  40 E  820  GLY ILE GLU TRP ASN PHE ILE ASP PHE GLY LEU ASP LEU          
SEQRES  41 E  820  GLN PRO CYS ILE GLU LEU ILE GLU ARG PRO THR ASN PRO          
SEQRES  42 E  820  PRO GLY VAL LEU ALA LEU LEU ASP GLU GLU CYS TRP PHE          
SEQRES  43 E  820  PRO LYS ALA THR ASP THR SER PHE VAL GLU LYS LEU ILE          
SEQRES  44 E  820  GLN GLU GLN GLY ASN HIS ALA LYS PHE GLN LYS SER LYS          
SEQRES  45 E  820  GLN LEU LYS ASP LYS THR GLU PHE CYS ILE LEU HIS TYR          
SEQRES  46 E  820  ALA GLY LYS VAL THR TYR ASN ALA SER ALA TRP LEU THR          
SEQRES  47 E  820  LYS ASN MET ASP PRO LEU ASN ASP ASN VAL THR SER LEU          
SEQRES  48 E  820  LEU ASN GLN SER SER ASP LYS PHE VAL ALA ASP LEU TRP          
SEQRES  49 E  820  LYS ASP VAL ASP ARG ILE VAL GLY LEU ASP GLN MET ALA          
SEQRES  50 E  820  LYS MET THR GLU SER SER LEU PRO SER ALA SER LYS THR          
SEQRES  51 E  820  LYS LYS GLY MET PHE ARG THR VAL GLY GLN LEU TYR LYS          
SEQRES  52 E  820  GLU GLN LEU THR LYS LEU MET THR THR LEU ARG ASN THR          
SEQRES  53 E  820  ASN PRO ASN PHE VAL ARG CYS ILE ILE PRO ASN HIS GLU          
SEQRES  54 E  820  LYS ARG ALA GLY LYS LEU ASP ALA HIS LEU VAL LEU GLU          
SEQRES  55 E  820  GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE ARG ILE          
SEQRES  56 E  820  CYS ARG GLN GLY PHE PRO ASN ARG ILE VAL PHE GLN GLU          
SEQRES  57 E  820  PHE ARG GLN ARG TYR GLU ILE LEU ALA ALA ASN ALA ILE          
SEQRES  58 E  820  PRO LYS GLY PHE MET ASP GLY LYS GLN ALA CYS ILE LEU          
SEQRES  59 E  820  MET ILE LYS ALA LEU GLU LEU ASP PRO ASN LEU TYR ARG          
SEQRES  60 E  820  ILE GLY GLN SER LYS ILE PHE PHE ARG THR GLY VAL LEU          
SEQRES  61 E  820  ALA HIS LEU GLU GLU GLU ARG ASP LEU LYS ILE THR ASP          
SEQRES  62 E  820  VAL ILE ILE ALA PHE GLN ALA GLN CYS ARG GLY TYR LEU          
SEQRES  63 E  820  ALA ARG LYS ALA PHE ALA LYS ARG GLN GLN GLN LEU GLY          
SEQRES  64 E  820  SER                                                          
SEQRES   1 F  150  CYS ASP PHE SER GLU GLU GLN THR ALA GLU PHE LYS GLU          
SEQRES   2 F  150  ALA PHE GLN LEU PHE ASP ARG THR GLY ASP GLY LYS ILE          
SEQRES   3 F  150  LEU TYR SER GLN CYS GLY ASP VAL MET ARG ALA LEU GLY          
SEQRES   4 F  150  GLN ASN PRO THR ASN ALA GLU VAL MET LYS VAL LEU GLY          
SEQRES   5 F  150  ASN PRO LYS SER ASP GLU MET ASN LEU LYS THR LEU LYS          
SEQRES   6 F  150  PHE GLU GLN PHE LEU PRO MET MET GLN THR ILE ALA LYS          
SEQRES   7 F  150  ASN LYS ASP GLN GLY CYS PHE GLU ASP TYR VAL GLU GLY          
SEQRES   8 F  150  LEU ARG VAL PHE ASP LYS GLU GLY ASN GLY THR VAL MET          
SEQRES   9 F  150  GLY ALA GLU ILE ARG HIS VAL LEU VAL THR LEU GLY GLU          
SEQRES  10 F  150  LYS MET THR GLU GLU GLU VAL GLU GLN LEU VAL ALA GLY          
SEQRES  11 F  150  HIS GLU ASP SER ASN GLY CYS ILE ASN TYR GLU GLU LEU          
SEQRES  12 F  150  VAL ARG MET VAL LEU SER GLY                                  
SEQRES   1 G  820  ALA GLN LYS PRO LEU SER ASP ASP GLU LYS PHE LEU PHE          
SEQRES   2 G  820  VAL ASP LYS ASN PHE VAL ASN ASN PRO LEU ALA GLN ALA          
SEQRES   3 G  820  ASP TRP SER ALA LYS LYS LEU VAL TRP VAL PRO SER GLU          
SEQRES   4 G  820  LYS HIS GLY PHE GLU ALA ALA SER ILE LYS GLU GLU LYS          
SEQRES   5 G  820  GLY ASP GLU VAL THR VAL GLU LEU GLN GLU ASN GLY LYS          
SEQRES   6 G  820  LYS VAL THR LEU SER LYS ASP ASP ILE GLN LYS MET ASN          
SEQRES   7 G  820  PRO PRO LYS PHE SER LYS VAL GLU ASP MET ALA GLU LEU          
SEQRES   8 G  820  THR CYS LEU ASN GLU ALA SER VAL LEU HIS ASN LEU ARG          
SEQRES   9 G  820  GLU ARG TYR PHE SER GLY LEU ILE TYR THR TYR SER GLY          
SEQRES  10 G  820  LEU PHE CYS VAL VAL ILE ASN PRO TYR LYS GLN LEU PRO          
SEQRES  11 G  820  ILE TYR SER GLU LYS ILE ILE ASP MET TYR LYS GLY LYS          
SEQRES  12 G  820  LYS ARG HIS GLU MET PRO PRO HIS ILE TYR ALA ILE ALA          
SEQRES  13 G  820  ASP THR ALA TYR ARG SER MET LEU GLN ASP ARG GLU ASP          
SEQRES  14 G  820  GLN SER ILE LEU CYS THR GLY GLU SER GLY ALA GLY LYS          
SEQRES  15 G  820  THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU ALA VAL          
SEQRES  16 G  820  VAL ALA SER SER HIS LYS GLY LYS LYS ASP THR SER ILE          
SEQRES  17 G  820  THR GLN GLY PRO SER PHE SER TYR GLY GLU LEU GLU LYS          
SEQRES  18 G  820  GLN LEU LEU GLN ALA ASN PRO ILE LEU GLU ALA PHE GLY          
SEQRES  19 G  820  ASN ALA LYS THR VAL LYS ASN ASP ASN SER SER ARG PHE          
SEQRES  20 G  820  GLY LYS PHE ILE ARG ILE ASN PHE ASP VAL THR GLY TYR          
SEQRES  21 G  820  ILE VAL GLY ALA ASN ILE GLU THR TYR LEU LEU GLU LYS          
SEQRES  22 G  820  SER ARG ALA ILE ARG GLN ALA LYS ASP GLU ARG THR PHE          
SEQRES  23 G  820  HIS ILE PHE TYR TYR LEU ILE ALA GLY ALA SER GLU GLN          
SEQRES  24 G  820  MET ARG ASN ASP LEU LEU LEU GLU GLY PHE ASN ASN TYR          
SEQRES  25 G  820  THR PHE LEU SER ASN GLY HIS VAL PRO ILE PRO ALA GLN          
SEQRES  26 G  820  GLN ASP ASP GLU MET PHE GLN GLU THR LEU GLU ALA MET          
SEQRES  27 G  820  THR ILE MET GLY PHE THR GLU GLU GLU GLN THR SER ILE          
SEQRES  28 G  820  LEU ARG VAL VAL SER SER VAL LEU GLN LEU GLY ASN ILE          
SEQRES  29 G  820  VAL PHE LYS LYS GLU ARG ASN THR ASP GLN ALA SER MET          
SEQRES  30 G  820  PRO ASP ASN THR ALA ALA GLN LYS VAL CYS HIS LEU MET          
SEQRES  31 G  820  GLY ILE ASN VAL THR ASP PHE THR ARG SER ILE LEU THR          
SEQRES  32 G  820  PRO ARG ILE LYS VAL GLY ARG ASP VAL VAL GLN LYS ALA          
SEQRES  33 G  820  GLN THR LYS GLU GLN ALA ASP PHE ALA ILE GLU ALA LEU          
SEQRES  34 G  820  ALA LYS ALA LYS PHE GLU ARG LEU PHE ARG TRP ILE LEU          
SEQRES  35 G  820  THR ARG VAL ASN LYS ALA LEU ASP LYS THR LYS ARG GLN          
SEQRES  36 G  820  GLY ALA SER PHE LEU GLY ILE LEU ASP ILE ALA GLY PHE          
SEQRES  37 G  820  GLU ILE PHE GLU ILE ASN SER PHE GLU GLN LEU CYS ILE          
SEQRES  38 G  820  ASN TYR THR ASN GLU LYS LEU GLN GLN LEU PHE ASN HIS          
SEQRES  39 G  820  THR MET PHE ILE LEU GLU GLN GLU GLU TYR GLN ARG GLU          
SEQRES  40 G  820  GLY ILE GLU TRP ASN PHE ILE ASP PHE GLY LEU ASP LEU          
SEQRES  41 G  820  GLN PRO CYS ILE GLU LEU ILE GLU ARG PRO THR ASN PRO          
SEQRES  42 G  820  PRO GLY VAL LEU ALA LEU LEU ASP GLU GLU CYS TRP PHE          
SEQRES  43 G  820  PRO LYS ALA THR ASP THR SER PHE VAL GLU LYS LEU ILE          
SEQRES  44 G  820  GLN GLU GLN GLY ASN HIS ALA LYS PHE GLN LYS SER LYS          
SEQRES  45 G  820  GLN LEU LYS ASP LYS THR GLU PHE CYS ILE LEU HIS TYR          
SEQRES  46 G  820  ALA GLY LYS VAL THR TYR ASN ALA SER ALA TRP LEU THR          
SEQRES  47 G  820  LYS ASN MET ASP PRO LEU ASN ASP ASN VAL THR SER LEU          
SEQRES  48 G  820  LEU ASN GLN SER SER ASP LYS PHE VAL ALA ASP LEU TRP          
SEQRES  49 G  820  LYS ASP VAL ASP ARG ILE VAL GLY LEU ASP GLN MET ALA          
SEQRES  50 G  820  LYS MET THR GLU SER SER LEU PRO SER ALA SER LYS THR          
SEQRES  51 G  820  LYS LYS GLY MET PHE ARG THR VAL GLY GLN LEU TYR LYS          
SEQRES  52 G  820  GLU GLN LEU THR LYS LEU MET THR THR LEU ARG ASN THR          
SEQRES  53 G  820  ASN PRO ASN PHE VAL ARG CYS ILE ILE PRO ASN HIS GLU          
SEQRES  54 G  820  LYS ARG ALA GLY LYS LEU ASP ALA HIS LEU VAL LEU GLU          
SEQRES  55 G  820  GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE ARG ILE          
SEQRES  56 G  820  CYS ARG GLN GLY PHE PRO ASN ARG ILE VAL PHE GLN GLU          
SEQRES  57 G  820  PHE ARG GLN ARG TYR GLU ILE LEU ALA ALA ASN ALA ILE          
SEQRES  58 G  820  PRO LYS GLY PHE MET ASP GLY LYS GLN ALA CYS ILE LEU          
SEQRES  59 G  820  MET ILE LYS ALA LEU GLU LEU ASP PRO ASN LEU TYR ARG          
SEQRES  60 G  820  ILE GLY GLN SER LYS ILE PHE PHE ARG THR GLY VAL LEU          
SEQRES  61 G  820  ALA HIS LEU GLU GLU GLU ARG ASP LEU LYS ILE THR ASP          
SEQRES  62 G  820  VAL ILE ILE ALA PHE GLN ALA GLN CYS ARG GLY TYR LEU          
SEQRES  63 G  820  ALA ARG LYS ALA PHE ALA LYS ARG GLN GLN GLN LEU GLY          
SEQRES  64 G  820  SER                                                          
SEQRES   1 H  150  CYS ASP PHE SER GLU GLU GLN THR ALA GLU PHE LYS GLU          
SEQRES   2 H  150  ALA PHE GLN LEU PHE ASP ARG THR GLY ASP GLY LYS ILE          
SEQRES   3 H  150  LEU TYR SER GLN CYS GLY ASP VAL MET ARG ALA LEU GLY          
SEQRES   4 H  150  GLN ASN PRO THR ASN ALA GLU VAL MET LYS VAL LEU GLY          
SEQRES   5 H  150  ASN PRO LYS SER ASP GLU MET ASN LEU LYS THR LEU LYS          
SEQRES   6 H  150  PHE GLU GLN PHE LEU PRO MET MET GLN THR ILE ALA LYS          
SEQRES   7 H  150  ASN LYS ASP GLN GLY CYS PHE GLU ASP TYR VAL GLU GLY          
SEQRES   8 H  150  LEU ARG VAL PHE ASP LYS GLU GLY ASN GLY THR VAL MET          
SEQRES   9 H  150  GLY ALA GLU ILE ARG HIS VAL LEU VAL THR LEU GLY GLU          
SEQRES  10 H  150  LYS MET THR GLU GLU GLU VAL GLU GLN LEU VAL ALA GLY          
SEQRES  11 H  150  HIS GLU ASP SER ASN GLY CYS ILE ASN TYR GLU GLU LEU          
SEQRES  12 H  150  VAL ARG MET VAL LEU SER GLY                                  
HET     MG  A 997       1                                                       
HET    ALF  A 999       5                                                       
HET    ADP  A 998      27                                                       
HET     MG  C 997       1                                                       
HET    ALF  C 999       5                                                       
HET    ADP  C 998      27                                                       
HET     MG  E 997       1                                                       
HET    ALF  E 999       5                                                       
HET    ADP  E 998      27                                                       
HET     MG  G 997       1                                                       
HET    ALF  G 999       5                                                       
HET    ADP  G 998      27                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ALF TETRAFLUOROALUMINATE ION                                         
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   9   MG    4(MG 2+)                                                     
FORMUL  10  ALF    4(AL F4 1-)                                                  
FORMUL  11  ADP    4(C10 H15 N5 O10 P2)                                         
FORMUL  21  HOH   *8(H2 O)                                                      
HELIX    1   1 GLU A   10  PHE A   12  5                                   3    
HELIX    2   2 ALA A   25  SER A   30  1                                   6    
HELIX    3   3 PRO A   81  PHE A   83  5                                   3    
HELIX    4   4 SER A   99  SER A  110  1                                  12    
HELIX    5   5 GLU A  135  TYR A  141  1                                   7    
HELIX    6   6 ILE A  153  ASP A  167  1                                  15    
HELIX    7   7 GLU A  185  VAL A  197  1                                  13    
HELIX    8   8 LEU A  220  LEU A  231  1                                  12    
HELIX    9   9 SER A  275  ALA A  277  5                                   3    
HELIX   10  10 HIS A  288  GLY A  296  5                                   9    
HELIX   11  11 GLU A  299  LEU A  305  1                                   7    
HELIX   12  12 ASP A  328  MET A  342  1                                  15    
HELIX   13  13 GLU A  346  GLY A  363  1                                  18    
HELIX   14  14 THR A  382  LEU A  390  1                                   9    
HELIX   15  15 VAL A  395  LEU A  403  1                                   9    
HELIX   16  16 LYS A  420  ALA A  449  1                                  30    
HELIX   17  17 PHE A  477  MET A  497  1                                  21    
HELIX   18  18 ILE A  499  GLU A  508  1                                  10    
HELIX   19  19 GLN A  522  GLU A  526  1                                   5    
HELIX   20  20 VAL A  537  GLU A  543  1                                   7    
HELIX   21  21 ASP A  552  GLU A  562  1                                  11    
HELIX   22  22 TRP A  597  LYS A  600  1                                   4    
HELIX   23  23 ASP A  607  ASN A  614  1                                   8    
HELIX   24  24 LYS A  619  TRP A  625  1                                   7    
HELIX   25  25 VAL A  659  ASN A  676  1                                  18    
HELIX   26  26 ALA A  698  CYS A  707  1                                  10    
HELIX   27  27 VAL A  710  GLN A  719  1                                  10    
HELIX   28  28 PHE A  727  ARG A  733  1                                   7    
HELIX   29  29 GLY A  749  LYS A  758  1                                  10    
HELIX   30  30 VAL A  780  LYS A  791  1                                  12    
HELIX   31  31 THR A  793  LEU A  819  1                                  27    
HELIX   32  32 GLU B    5  GLN B   16  1                                  12    
HELIX   33  33 CYS B   31  ALA B   37  1                                   7    
HELIX   34  34 ASN B   44  LEU B   51  1                                   8    
HELIX   35  35 SER B   56  MET B   59  5                                   4    
HELIX   36  36 PHE B   66  ALA B   77  1                                  12    
HELIX   37  37 PHE B   85  VAL B   94  1                                  10    
HELIX   38  38 GLU B  107  VAL B  113  1                                   7    
HELIX   39  39 GLU B  121  VAL B  128  1                                   8    
HELIX   40  40 TYR B  140  LEU B  148  1                                   9    
HELIX   41  41 GLU C   10  PHE C   12  5                                   3    
HELIX   42  42 PRO C   23  SER C   30  1                                   8    
HELIX   43  43 PRO C   81  PHE C   83  5                                   3    
HELIX   44  44 SER C   99  SER C  110  1                                  12    
HELIX   45  45 GLU C  135  TYR C  141  1                                   7    
HELIX   46  46 ILE C  153  ASP C  167  1                                  15    
HELIX   47  47 GLU C  185  VAL C  197  1                                  13    
HELIX   48  48 LEU C  220  LEU C  231  1                                  12    
HELIX   49  49 SER C  275  ALA C  277  5                                   3    
HELIX   50  50 HIS C  288  GLY C  296  5                                   9    
HELIX   51  51 GLU C  299  LEU C  305  1                                   7    
HELIX   52  52 ASP C  328  MET C  342  1                                  15    
HELIX   53  53 GLU C  346  GLY C  363  1                                  18    
HELIX   54  54 THR C  382  LEU C  390  1                                   9    
HELIX   55  55 VAL C  395  LEU C  403  1                                   9    
HELIX   56  56 GLN C  422  ALA C  449  1                                  28    
HELIX   57  57 PHE C  477  MET C  497  1                                  21    
HELIX   58  58 ILE C  499  ARG C  507  1                                   9    
HELIX   59  59 GLN C  522  GLU C  526  1                                   5    
HELIX   60  60 VAL C  537  GLU C  543  1                                   7    
HELIX   61  61 ASP C  552  GLU C  562  1                                  11    
HELIX   62  62 TRP C  597  LYS C  600  1                                   4    
HELIX   63  63 ASP C  607  ASN C  614  1                                   8    
HELIX   64  64 LYS C  619  LEU C  624  1                                   6    
HELIX   65  65 VAL C  659  ASN C  676  1                                  18    
HELIX   66  66 ALA C  698  CYS C  707  1                                  10    
HELIX   67  67 VAL C  710  GLN C  719  1                                  10    
HELIX   68  68 PHE C  727  ARG C  733  1                                   7    
HELIX   69  69 GLY C  749  LYS C  758  1                                  10    
HELIX   70  70 VAL C  780  LYS C  791  1                                  12    
HELIX   71  71 THR C  793  LEU C  819  1                                  27    
HELIX   72  72 GLU D    5  GLN D   16  1                                  12    
HELIX   73  73 CYS D   31  ALA D   37  1                                   7    
HELIX   74  74 ASN D   44  LEU D   51  1                                   8    
HELIX   75  75 SER D   56  MET D   59  5                                   4    
HELIX   76  76 PHE D   66  ALA D   77  1                                  12    
HELIX   77  77 PHE D   85  VAL D   94  1                                  10    
HELIX   78  78 GLU D  107  VAL D  113  1                                   7    
HELIX   79  79 GLU D  121  VAL D  128  1                                   8    
HELIX   80  80 TYR D  140  LEU D  148  1                                   9    
HELIX   81  81 GLU E   10  PHE E   12  5                                   3    
HELIX   82  82 PRO E   23  SER E   30  1                                   8    
HELIX   83  83 PRO E   81  PHE E   83  5                                   3    
HELIX   84  84 SER E   99  SER E  110  1                                  12    
HELIX   85  85 GLU E  135  TYR E  141  1                                   7    
HELIX   86  86 ILE E  153  ASP E  167  1                                  15    
HELIX   87  87 GLU E  185  VAL E  197  1                                  13    
HELIX   88  88 LEU E  220  LEU E  231  1                                  12    
HELIX   89  89 SER E  275  ALA E  277  5                                   3    
HELIX   90  90 HIS E  288  GLY E  296  5                                   9    
HELIX   91  91 GLU E  299  LEU E  305  1                                   7    
HELIX   92  92 ASP E  328  MET E  342  1                                  15    
HELIX   93  93 GLU E  346  GLY E  363  1                                  18    
HELIX   94  94 THR E  382  LEU E  390  1                                   9    
HELIX   95  95 VAL E  395  LEU E  403  1                                   9    
HELIX   96  96 LYS E  420  VAL E  446  1                                  27    
HELIX   97  97 PHE E  477  MET E  497  1                                  21    
HELIX   98  98 ILE E  499  ARG E  507  1                                   9    
HELIX   99  99 GLN E  522  GLU E  526  1                                   5    
HELIX  100 100 VAL E  537  GLU E  543  1                                   7    
HELIX  101 101 ASP E  552  GLU E  562  1                                  11    
HELIX  102 102 TRP E  597  LYS E  600  1                                   4    
HELIX  103 103 ASP E  607  ASN E  614  1                                   8    
HELIX  104 104 LYS E  619  LEU E  624  1                                   6    
HELIX  105 105 VAL E  659  ASN E  676  1                                  18    
HELIX  106 106 ALA E  698  CYS E  707  1                                  10    
HELIX  107 107 VAL E  710  GLN E  719  1                                  10    
HELIX  108 108 PHE E  727  ARG E  733  1                                   7    
HELIX  109 109 GLY E  749  LYS E  758  1                                  10    
HELIX  110 110 VAL E  780  LYS E  791  1                                  12    
HELIX  111 111 THR E  793  LEU E  819  1                                  27    
HELIX  112 112 GLU F    5  GLN F   16  1                                  12    
HELIX  113 113 CYS F   31  ALA F   37  1                                   7    
HELIX  114 114 ASN F   44  LEU F   51  1                                   8    
HELIX  115 115 SER F   56  MET F   59  5                                   4    
HELIX  116 116 PHE F   66  ALA F   77  1                                  12    
HELIX  117 117 TYR F   88  VAL F   94  1                                   7    
HELIX  118 118 GLU F  107  VAL F  113  1                                   7    
HELIX  119 119 GLU F  121  VAL F  128  1                                   8    
HELIX  120 120 TYR F  140  LEU F  148  1                                   9    
HELIX  121 121 GLU G   10  PHE G   12  5                                   3    
HELIX  122 122 PRO G   23  SER G   30  1                                   8    
HELIX  123 123 PRO G   81  PHE G   83  5                                   3    
HELIX  124 124 SER G   99  SER G  110  1                                  12    
HELIX  125 125 GLU G  135  TYR G  141  1                                   7    
HELIX  126 126 ILE G  153  GLN G  166  1                                  14    
HELIX  127 127 GLU G  185  VAL G  197  1                                  13    
HELIX  128 128 LEU G  220  LEU G  231  1                                  12    
HELIX  129 129 SER G  275  ALA G  277  5                                   3    
HELIX  130 130 HIS G  288  GLY G  296  5                                   9    
HELIX  131 131 GLU G  299  LEU G  305  1                                   7    
HELIX  132 132 ASP G  328  MET G  342  1                                  15    
HELIX  133 133 GLU G  346  GLY G  363  1                                  18    
HELIX  134 134 THR G  382  LEU G  390  1                                   9    
HELIX  135 135 VAL G  395  LEU G  403  1                                   9    
HELIX  136 136 LYS G  420  ALA G  449  1                                  30    
HELIX  137 137 PHE G  477  MET G  497  1                                  21    
HELIX  138 138 ILE G  499  ARG G  507  1                                   9    
HELIX  139 139 GLN G  522  GLU G  526  1                                   5    
HELIX  140 140 VAL G  537  GLU G  543  1                                   7    
HELIX  141 141 ASP G  552  GLU G  562  1                                  11    
HELIX  142 142 TRP G  597  LYS G  600  1                                   4    
HELIX  143 143 ASP G  607  ASN G  614  1                                   8    
HELIX  144 144 LYS G  619  TRP G  625  1                                   7    
HELIX  145 145 VAL G  659  ASN G  676  1                                  18    
HELIX  146 146 ALA G  698  CYS G  707  1                                  10    
HELIX  147 147 VAL G  710  GLN G  719  1                                  10    
HELIX  148 148 PHE G  727  ARG G  733  1                                   7    
HELIX  149 149 GLU G  735  LEU G  737  5                                   3    
HELIX  150 150 GLY G  749  LYS G  758  1                                  10    
HELIX  151 151 VAL G  780  LYS G  791  1                                  12    
HELIX  152 152 THR G  793  LEU G  819  1                                  27    
HELIX  153 153 GLU H    5  GLN H   16  1                                  12    
HELIX  154 154 CYS H   31  ALA H   37  1                                   7    
HELIX  155 155 ASN H   44  LEU H   51  1                                   8    
HELIX  156 156 SER H   56  MET H   59  5                                   4    
HELIX  157 157 PHE H   66  ALA H   77  1                                  12    
HELIX  158 158 PHE H   85  PHE H   95  1                                  11    
HELIX  159 159 GLU H  107  VAL H  113  1                                   7    
HELIX  160 160 GLU H  121  VAL H  128  1                                   8    
HELIX  161 161 TYR H  140  LEU H  148  1                                   9    
SHEET    1   A 5 ILE A  75  LYS A  77  0                                        
SHEET    2   A 5 LEU A  34  SER A  39 -1  N  TRP A  36   O  GLN A  76           
SHEET    3   A 5 GLY A  43  LYS A  53 -1  N  ALA A  47   O  VAL A  35           
SHEET    4   A 5 GLU A  56  LEU A  61 -1  N  GLU A  60   O  SER A  48           
SHEET    5   A 5 LYS A  67  SER A  71 -1  N  LEU A  70   O  VAL A  57           
SHEET    1   B 2 TYR A 114  SER A 117  0                                        
SHEET    2   B 2 PHE A 120  VAL A 123 -1  N  VAL A 122   O  THR A 115           
SHEET    1   C 5 ASN A 678  PHE A 681  0                                        
SHEET    2   C 5 GLN A 171  LEU A 174  1  N  SER A 172   O  ASN A 678           
SHEET    3   C 5 SER A 459  ASP A 465  1  N  GLY A 462   O  GLN A 171           
SHEET    4   C 5 LYS A 250  PHE A 256 -1  N  PHE A 256   O  SER A 459           
SHEET    5   C 5 ILE A 262  THR A 269 -1  N  GLU A 268   O  PHE A 251           
SHEET    1   D 3 PHE A 569  LYS A 571  0                                        
SHEET    2   D 3 GLU A 580  LEU A 584 -1  N  CYS A 582   O  GLN A 570           
SHEET    3   D 3 LYS A 589  ASN A 593 -1  N  TYR A 592   O  PHE A 581           
SHEET    1   E 2 ASN A 723  VAL A 726  0                                        
SHEET    2   E 2 LYS A 773  PHE A 776 -1  N  PHE A 776   O  ASN A 723           
SHEET    1   F 5 ILE C  75  LYS C  77  0                                        
SHEET    2   F 5 LEU C  34  SER C  39 -1  N  TRP C  36   O  GLN C  76           
SHEET    3   F 5 GLY C  43  LYS C  53 -1  N  ALA C  47   O  VAL C  35           
SHEET    4   F 5 GLU C  56  LEU C  61 -1  N  GLU C  60   O  SER C  48           
SHEET    5   F 5 LYS C  67  SER C  71 -1  N  LEU C  70   O  VAL C  57           
SHEET    1   G 2 TYR C 114  SER C 117  0                                        
SHEET    2   G 2 PHE C 120  VAL C 123 -1  N  VAL C 122   O  THR C 115           
SHEET    1   H 5 ASN C 678  PHE C 681  0                                        
SHEET    2   H 5 GLN C 171  LEU C 174  1  N  SER C 172   O  ASN C 678           
SHEET    3   H 5 SER C 459  ASP C 465  1  N  GLY C 462   O  GLN C 171           
SHEET    4   H 5 LYS C 250  PHE C 256 -1  N  PHE C 256   O  SER C 459           
SHEET    5   H 5 ILE C 262  THR C 269 -1  N  GLU C 268   O  PHE C 251           
SHEET    1   I 3 PHE C 569  LYS C 571  0                                        
SHEET    2   I 3 GLU C 580  LEU C 584 -1  N  CYS C 582   O  GLN C 570           
SHEET    3   I 3 LYS C 589  ASN C 593 -1  N  TYR C 592   O  PHE C 581           
SHEET    1   J 3 ASN C 723  VAL C 726  0                                        
SHEET    2   J 3 LYS C 773  PHE C 776 -1  N  PHE C 776   O  ASN C 723           
SHEET    3   J 3 TYR C 767  ILE C 769 -1  N  ARG C 768   O  PHE C 775           
SHEET    1   K 5 ILE E  75  LYS E  77  0                                        
SHEET    2   K 5 LEU E  34  SER E  39 -1  N  TRP E  36   O  GLN E  76           
SHEET    3   K 5 GLY E  43  LYS E  53 -1  N  ALA E  47   O  VAL E  35           
SHEET    4   K 5 GLU E  56  LEU E  61 -1  N  GLU E  60   O  SER E  48           
SHEET    5   K 5 LYS E  67  SER E  71 -1  N  LEU E  70   O  VAL E  57           
SHEET    1   L 2 TYR E 114  SER E 117  0                                        
SHEET    2   L 2 PHE E 120  VAL E 123 -1  N  VAL E 122   O  THR E 115           
SHEET    1   M 5 ASN E 678  PHE E 681  0                                        
SHEET    2   M 5 GLN E 171  LEU E 174  1  N  SER E 172   O  ASN E 678           
SHEET    3   M 5 SER E 459  ASP E 465  1  N  GLY E 462   O  GLN E 171           
SHEET    4   M 5 LYS E 250  PHE E 256 -1  N  PHE E 256   O  SER E 459           
SHEET    5   M 5 ILE E 262  THR E 269 -1  N  GLU E 268   O  PHE E 251           
SHEET    1   N 3 PHE E 569  LYS E 571  0                                        
SHEET    2   N 3 GLU E 580  LEU E 584 -1  N  CYS E 582   O  GLN E 570           
SHEET    3   N 3 LYS E 589  ASN E 593 -1  N  TYR E 592   O  PHE E 581           
SHEET    1   O 3 ASN E 723  VAL E 726  0                                        
SHEET    2   O 3 LYS E 773  PHE E 776 -1  N  PHE E 776   O  ASN E 723           
SHEET    3   O 3 TYR E 767  ILE E 769 -1  N  ARG E 768   O  PHE E 775           
SHEET    1   P 5 ILE G  75  LYS G  77  0                                        
SHEET    2   P 5 LEU G  34  SER G  39 -1  N  TRP G  36   O  GLN G  76           
SHEET    3   P 5 GLY G  43  LYS G  53 -1  N  ALA G  47   O  VAL G  35           
SHEET    4   P 5 GLU G  56  LEU G  61 -1  N  GLU G  60   O  SER G  48           
SHEET    5   P 5 LYS G  67  SER G  71 -1  N  LEU G  70   O  VAL G  57           
SHEET    1   Q 2 TYR G 114  SER G 117  0                                        
SHEET    2   Q 2 PHE G 120  VAL G 123 -1  N  VAL G 122   O  THR G 115           
SHEET    1   R 5 ASN G 678  PHE G 681  0                                        
SHEET    2   R 5 GLN G 171  LEU G 174  1  N  SER G 172   O  ASN G 678           
SHEET    3   R 5 SER G 459  ASP G 465  1  N  GLY G 462   O  GLN G 171           
SHEET    4   R 5 LYS G 250  PHE G 256 -1  N  PHE G 256   O  SER G 459           
SHEET    5   R 5 ILE G 262  THR G 269 -1  N  GLU G 268   O  PHE G 251           
SHEET    1   S 3 PHE G 569  LYS G 571  0                                        
SHEET    2   S 3 GLU G 580  LEU G 584 -1  N  CYS G 582   O  GLN G 570           
SHEET    3   S 3 LYS G 589  ASN G 593 -1  N  TYR G 592   O  PHE G 581           
SHEET    1   T 3 ASN G 723  VAL G 726  0                                        
SHEET    2   T 3 LYS G 773  PHE G 776 -1  N  PHE G 776   O  ASN G 723           
SHEET    3   T 3 TYR G 767  ILE G 769 -1  N  ARG G 768   O  PHE G 775           
LINK         OG1 THR A 184                MG    MG A 997     1555   1555  2.16  
LINK         OG  SER A 245                AL   ALF A 999     1555   1555  3.67  
LINK         OG  SER A 246                MG    MG A 997     1555   1555  2.58  
LINK         O   HOH A 995                MG    MG A 997     1555   1555  1.84  
LINK         O   HOH A 995                AL   ALF A 999     1555   1555  3.71  
LINK        MG    MG A 997                 O2B ADP A 998     1555   1555  2.04  
LINK        MG    MG A 997                 F2  ALF A 999     1555   1555  2.96  
LINK        MG    MG A 997                 F4  ALF A 999     1555   1555  2.09  
LINK        MG    MG A 997                AL   ALF A 999     1555   1555  3.43  
LINK         O1B ADP A 998                AL   ALF A 999     1555   1555  3.59  
LINK         O2B ADP A 998                AL   ALF A 999     1555   1555  3.48  
LINK         O3B ADP A 998                AL   ALF A 999     1555   1555  2.08  
LINK         OG1 THR C 184                MG    MG C 997     1555   1555  2.17  
LINK         OG  SER C 246                MG    MG C 997     1555   1555  2.60  
LINK         N   GLY C 468                AL   ALF C 999     1555   1555  3.69  
LINK         O   HOH C 995                MG    MG C 997     1555   1555  1.84  
LINK         O   HOH C 995                AL   ALF C 999     1555   1555  3.71  
LINK        MG    MG C 997                 O2B ADP C 998     1555   1555  2.04  
LINK        MG    MG C 997                 F2  ALF C 999     1555   1555  2.96  
LINK        MG    MG C 997                 F4  ALF C 999     1555   1555  2.08  
LINK        MG    MG C 997                AL   ALF C 999     1555   1555  3.43  
LINK         O3B ADP C 998                AL   ALF C 999     1555   1555  2.08  
LINK         O2B ADP C 998                AL   ALF C 999     1555   1555  3.48  
LINK         O1B ADP C 998                AL   ALF C 999     1555   1555  3.59  
LINK         OG1 THR E 184                MG    MG E 997     1555   1555  2.08  
LINK         OG  SER E 246                MG    MG E 997     1555   1555  2.73  
LINK         N   GLY E 468                AL   ALF E 999     1555   1555  3.63  
LINK         O   HOH E 995                MG    MG E 997     1555   1555  1.84  
LINK         O   HOH E 995                AL   ALF E 999     1555   1555  3.71  
LINK        MG    MG E 997                 O2B ADP E 998     1555   1555  2.04  
LINK        MG    MG E 997                 F2  ALF E 999     1555   1555  2.96  
LINK        MG    MG E 997                 F4  ALF E 999     1555   1555  2.08  
LINK        MG    MG E 997                AL   ALF E 999     1555   1555  3.43  
LINK         O3B ADP E 998                AL   ALF E 999     1555   1555  2.08  
LINK         O1B ADP E 998                AL   ALF E 999     1555   1555  3.59  
LINK         O2B ADP E 998                AL   ALF E 999     1555   1555  3.48  
LINK         OG1 THR G 184                MG    MG G 997     1555   1555  2.07  
LINK         OG  SER G 246                MG    MG G 997     1555   1555  2.66  
LINK         N   GLY G 468                AL   ALF G 999     1555   1555  3.71  
LINK         O   HOH G 995                MG    MG G 997     1555   1555  1.84  
LINK         O   HOH G 995                AL   ALF G 999     1555   1555  3.71  
LINK        MG    MG G 997                 O2B ADP G 998     1555   1555  2.04  
LINK        MG    MG G 997                 F2  ALF G 999     1555   1555  2.96  
LINK        MG    MG G 997                 F4  ALF G 999     1555   1555  2.09  
LINK        MG    MG G 997                AL   ALF G 999     1555   1555  3.43  
LINK         O3B ADP G 998                AL   ALF G 999     1555   1555  2.08  
LINK         O2B ADP G 998                AL   ALF G 999     1555   1555  3.48  
LINK         O1B ADP G 998                AL   ALF G 999     1555   1555  3.59  
SITE     1 AC1  5 THR A 184  SER A 246  HOH A 995  ADP A 998                    
SITE     2 AC1  5 ALF A 999                                                     
SITE     1 AC2  9 SER A 179  GLY A 180  LYS A 183  SER A 245                    
SITE     2 AC2  9 SER A 246  GLY A 468  HOH A 995   MG A 997                    
SITE     3 AC2  9 ADP A 998                                                     
SITE     1 AC3  5 THR C 184  SER C 246  HOH C 995  ADP C 998                    
SITE     2 AC3  5 ALF C 999                                                     
SITE     1 AC4  9 SER C 179  LYS C 183  SER C 245  SER C 246                    
SITE     2 AC4  9 ALA C 467  GLY C 468  HOH C 995   MG C 997                    
SITE     3 AC4  9 ADP C 998                                                     
SITE     1 AC5  5 THR E 184  SER E 246  HOH E 995  ADP E 998                    
SITE     2 AC5  5 ALF E 999                                                     
SITE     1 AC6 10 SER E 179  GLY E 180  LYS E 183  SER E 245                    
SITE     2 AC6 10 SER E 246  ALA E 467  GLY E 468  HOH E 995                    
SITE     3 AC6 10  MG E 997  ADP E 998                                          
SITE     1 AC7  5 THR G 184  SER G 246  HOH G 995  ADP G 998                    
SITE     2 AC7  5 ALF G 999                                                     
SITE     1 AC8  9 SER G 179  GLY G 180  LYS G 183  SER G 245                    
SITE     2 AC8  9 SER G 246  GLY G 468  HOH G 995   MG G 997                    
SITE     3 AC8  9 ADP G 998                                                     
SITE     1 AC9 15 ASN A 125  PRO A 126  TYR A 127  TYR A 133                    
SITE     2 AC9 15 GLY A 180  ALA A 181  GLY A 182  LYS A 183                    
SITE     3 AC9 15 THR A 184  GLU A 185  ASN A 242  HOH A 995                    
SITE     4 AC9 15 HOH A 996   MG A 997  ALF A 999                               
SITE     1 BC1 15 ASN C 125  PRO C 126  TYR C 127  TYR C 133                    
SITE     2 BC1 15 GLY C 180  ALA C 181  GLY C 182  LYS C 183                    
SITE     3 BC1 15 THR C 184  GLU C 185  ASN C 242  HOH C 995                    
SITE     4 BC1 15 HOH C 996   MG C 997  ALF C 999                               
SITE     1 BC2 15 ASN E 125  PRO E 126  TYR E 127  TYR E 133                    
SITE     2 BC2 15 GLY E 180  ALA E 181  GLY E 182  LYS E 183                    
SITE     3 BC2 15 THR E 184  GLU E 185  ASN E 242  HOH E 995                    
SITE     4 BC2 15 HOH E 996   MG E 997  ALF E 999                               
SITE     1 BC3 15 ASN G 125  PRO G 126  TYR G 127  TYR G 133                    
SITE     2 BC3 15 GLY G 180  ALA G 181  GLY G 182  LYS G 183                    
SITE     3 BC3 15 THR G 184  GLU G 185  ASN G 242  HOH G 995                    
SITE     4 BC3 15 HOH G 996   MG G 997  ALF G 999                               
CRYST1   95.320  144.660  147.290 111.21 106.10  92.58 P 1           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      0.010491  0.000473  0.003489        0.00000                         
SCALE2      0.000000  0.006920  0.002930        0.00000                         
SCALE3      0.000000  0.000000  0.007674        0.00000                         
MTRIX1   1  0.636300  0.759920  0.132790       74.91910    1                    
MTRIX2   1  0.765970 -0.642820  0.008300       36.46862    1                    
MTRIX3   1  0.091670  0.096430 -0.991110       57.02822    1                    
MTRIX1   2  0.707040  0.668210  0.231470      -16.38862    1                    
MTRIX2   2 -0.687720  0.725960  0.004980      -10.04698    1                    
MTRIX3   2 -0.164710 -0.162710  0.972830       82.88082    1                    
MTRIX1   3  0.996000  0.082670 -0.033900       45.17225    1                    
MTRIX2   3  0.085230 -0.992920  0.082690       81.93243    1                    
MTRIX3   3 -0.026830 -0.085250 -0.996000        9.46068    1                    
MTRIX1   4  0.618640  0.774410  0.132600       74.12373    1                    
MTRIX2   4  0.779830 -0.625780  0.016390       36.34917    1                    
MTRIX3   4  0.095670  0.093260 -0.991030       57.19003    1                    
MTRIX1   5  0.678740  0.687340  0.258610      -17.56703    1                    
MTRIX2   5 -0.712770  0.701370  0.006610       -9.98185    1                    
MTRIX3   5 -0.176840 -0.188820  0.965960       83.36942    1                    
MTRIX1   6  0.999380  0.023850  0.025980       46.73965    1                    
MTRIX2   6  0.019120 -0.985410  0.169090       80.05285    1                    
MTRIX3   6  0.029640 -0.168490 -0.985260       13.21120    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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