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Database: PDB
Entry: 4DB1
LinkDB: 4DB1
Original site: 4DB1 
HEADER    CONTRACTILE PROTEIN                     13-JAN-12   4DB1              
TITLE     CARDIAC HUMAN MYOSIN S1DC, BETA ISOFORM COMPLEXED WITH MN-AMPPNP      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOSIN-7;                                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 2-783;                                        
COMPND   5 SYNONYM: MYOSIN HEAVY CHAIN 7, MYOSIN HEAVY CHAIN SLOW ISOFORM, MYHC-
COMPND   6 SLOW, MYOSIN HEAVY CHAIN, CARDIAC MUSCLE BETA ISOFORM, MYHC-BETA;    
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MYH7, MYHCB;                                                   
SOURCE   6 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: C2C12 CELLS;                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: ADENOVIRUS                            
KEYWDS    S1DC, MYOSIN, CARDIAC, BETA ISOFORM, MYH7, MYHCB, MYHC-BETA,          
KEYWDS   2 CONTRACTILE PROTEIN                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.A.KLENCHIN,J.C.DEACON,A.C.COMBS,L.A.LEINWAND,I.RAYMENT              
REVDAT   1   25-JAN-12 4DB1    0                                                
JRNL        AUTH   V.A.KLENCHIN,J.C.DEACON,A.C.COMBS,L.A.LEINWAND,I.RAYMENT     
JRNL        TITL   CARDIAC HUMAN MYOSIN S1DC, BETA ISOFORM COMPLEXED WITH       
JRNL        TITL 2 MN-AMPPNP                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 55440                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2959                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3804                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2790                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 199                          
REMARK   3   BIN FREE R VALUE                    : 0.3270                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11052                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 64                                      
REMARK   3   SOLVENT ATOMS            : 202                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.42                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.32000                                             
REMARK   3    B22 (A**2) : 1.39000                                              
REMARK   3    B33 (A**2) : -0.90000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.22000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.591         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.309         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.219         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.348        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.896                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11381 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15420 ; 1.185 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1427 ; 6.189 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   510 ;38.265 ;24.549       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1858 ;17.999 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    47 ;22.500 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1703 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8623 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  7126 ; 1.401 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11370 ; 2.746 ;30.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4255 ; 3.448 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4048 ; 5.616 ;50.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   496                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0430  43.4440  75.8180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2262 T22:   0.1784                                     
REMARK   3      T33:   0.2776 T12:  -0.0290                                     
REMARK   3      T13:   0.0254 T23:   0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8481 L22:   0.4218                                     
REMARK   3      L33:   1.9180 L12:  -0.0297                                     
REMARK   3      L13:  -0.3526 L23:  -0.0708                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0245 S12:   0.0047 S13:  -0.0886                       
REMARK   3      S21:   0.0038 S22:   0.0163 S23:   0.1006                       
REMARK   3      S31:   0.2112 S32:  -0.1227 S33:  -0.0408                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   497        A   777                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.6320  51.7020  69.3650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2685 T22:   0.4200                                     
REMARK   3      T33:   0.3642 T12:  -0.0026                                     
REMARK   3      T13:   0.0545 T23:   0.0647                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5988 L22:   0.7983                                     
REMARK   3      L33:   2.0354 L12:  -0.0234                                     
REMARK   3      L13:   0.6773 L23:   0.1300                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0011 S12:   0.1529 S13:   0.0260                       
REMARK   3      S21:  -0.1671 S22:  -0.0048 S23:   0.1704                       
REMARK   3      S31:  -0.1931 S32:  -0.6392 S33:   0.0037                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   495                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.6370  44.2320  57.1820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1625 T22:   0.1939                                     
REMARK   3      T33:   0.2462 T12:   0.0095                                     
REMARK   3      T13:   0.0108 T23:   0.0081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8211 L22:   0.6669                                     
REMARK   3      L33:   1.3072 L12:  -0.0875                                     
REMARK   3      L13:  -0.2215 L23:   0.2682                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0164 S12:  -0.1129 S13:  -0.0426                       
REMARK   3      S21:   0.0540 S22:   0.0366 S23:  -0.1233                       
REMARK   3      S31:   0.0931 S32:   0.1568 S33:  -0.0530                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   496        B   775                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.8500  53.2390  62.2270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3185 T22:   0.5124                                     
REMARK   3      T33:   0.3495 T12:  -0.0369                                     
REMARK   3      T13:   0.0081 T23:  -0.0248                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1227 L22:   1.1118                                     
REMARK   3      L33:   0.3602 L12:   0.2931                                     
REMARK   3      L13:   0.5107 L23:  -0.1115                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0329 S12:  -0.2212 S13:   0.1671                       
REMARK   3      S21:   0.3340 S22:  -0.0934 S23:  -0.2307                       
REMARK   3      S31:  -0.1017 S32:   0.2669 S33:   0.0605                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.10                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B           
REMARK   3  FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.  
REMARK   4                                                                      
REMARK   4 4DB1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070105.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97907                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58495                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.15400                            
REMARK 200  R SYM                      (I) : 0.15400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.197                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP 10.2.31                                        
REMARK 200 STARTING MODEL: 2MYS                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PRECIPITANT: 7.5% PEG 8000, 0.05M MES,   
REMARK 280  0.05M ACETATE, 0.25M SODIUM CHLORIDE, 0.01M MANGANESE CHLORIDE,     
REMARK 280  0.1% SODIUM CHOLATE, PH 5.5, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       47.15500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 59560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   205                                                      
REMARK 465     LYS A   206                                                      
REMARK 465     LYS A   207                                                      
REMARK 465     ASP A   208                                                      
REMARK 465     GLN A   209                                                      
REMARK 465     SER A   210                                                      
REMARK 465     PRO A   211                                                      
REMARK 465     VAL A   404                                                      
REMARK 465     LYS A   405                                                      
REMARK 465     VAL A   406                                                      
REMARK 465     GLY A   407                                                      
REMARK 465     ASN A   408                                                      
REMARK 465     GLU A   409                                                      
REMARK 465     ILE A   569                                                      
REMARK 465     LYS A   570                                                      
REMARK 465     GLY A   571                                                      
REMARK 465     LYS A   572                                                      
REMARK 465     GLY A   626                                                      
REMARK 465     ALA A   627                                                      
REMARK 465     ASP A   628                                                      
REMARK 465     ALA A   629                                                      
REMARK 465     PRO A   630                                                      
REMARK 465     ILE A   631                                                      
REMARK 465     GLU A   632                                                      
REMARK 465     LYS A   633                                                      
REMARK 465     GLY A   634                                                      
REMARK 465     LYS A   635                                                      
REMARK 465     GLY A   636                                                      
REMARK 465     LYS A   637                                                      
REMARK 465     ALA A   638                                                      
REMARK 465     LYS A   639                                                      
REMARK 465     LYS A   640                                                      
REMARK 465     GLY A   641                                                      
REMARK 465     SER A   642                                                      
REMARK 465     SER A   643                                                      
REMARK 465     GLY A   716                                                      
REMARK 465     ASP A   717                                                      
REMARK 465     PHE A   718                                                      
REMARK 465     ARG A   719                                                      
REMARK 465     GLN A   720                                                      
REMARK 465     ARG A   721                                                      
REMARK 465     TYR A   722                                                      
REMARK 465     ARG A   723                                                      
REMARK 465     ILE A   724                                                      
REMARK 465     LEU A   725                                                      
REMARK 465     ASN A   726                                                      
REMARK 465     PRO A   727                                                      
REMARK 465     ALA A   728                                                      
REMARK 465     ALA A   729                                                      
REMARK 465     ILE A   730                                                      
REMARK 465     PRO A   731                                                      
REMARK 465     GLU A   732                                                      
REMARK 465     GLY A   733                                                      
REMARK 465     GLN A   734                                                      
REMARK 465     PHE A   735                                                      
REMARK 465     ILE A   736                                                      
REMARK 465     ASP A   737                                                      
REMARK 465     SER A   738                                                      
REMARK 465     ARG A   739                                                      
REMARK 465     LYS A   740                                                      
REMARK 465     GLY A   741                                                      
REMARK 465     ASP A   778                                                      
REMARK 465     GLU A   779                                                      
REMARK 465     ARG A   780                                                      
REMARK 465     LEU A   781                                                      
REMARK 465     SER A   782                                                      
REMARK 465     ARG A   783                                                      
REMARK 465     SER B   205                                                      
REMARK 465     LYS B   206                                                      
REMARK 465     LYS B   207                                                      
REMARK 465     ASP B   208                                                      
REMARK 465     GLN B   209                                                      
REMARK 465     SER B   210                                                      
REMARK 465     PRO B   211                                                      
REMARK 465     VAL B   404                                                      
REMARK 465     LYS B   405                                                      
REMARK 465     VAL B   406                                                      
REMARK 465     GLY B   407                                                      
REMARK 465     ASN B   408                                                      
REMARK 465     GLU B   409                                                      
REMARK 465     ALA B   627                                                      
REMARK 465     ASP B   628                                                      
REMARK 465     ALA B   629                                                      
REMARK 465     PRO B   630                                                      
REMARK 465     ILE B   631                                                      
REMARK 465     GLU B   632                                                      
REMARK 465     LYS B   633                                                      
REMARK 465     GLY B   634                                                      
REMARK 465     LYS B   635                                                      
REMARK 465     GLY B   636                                                      
REMARK 465     LYS B   637                                                      
REMARK 465     ALA B   638                                                      
REMARK 465     LYS B   639                                                      
REMARK 465     LYS B   640                                                      
REMARK 465     GLY B   641                                                      
REMARK 465     SER B   642                                                      
REMARK 465     SER B   643                                                      
REMARK 465     PHE B   644                                                      
REMARK 465     GLY B   716                                                      
REMARK 465     ASP B   717                                                      
REMARK 465     PHE B   718                                                      
REMARK 465     ARG B   719                                                      
REMARK 465     GLN B   720                                                      
REMARK 465     ARG B   721                                                      
REMARK 465     TYR B   722                                                      
REMARK 465     ARG B   723                                                      
REMARK 465     ILE B   724                                                      
REMARK 465     LEU B   725                                                      
REMARK 465     ASN B   726                                                      
REMARK 465     PRO B   727                                                      
REMARK 465     ALA B   728                                                      
REMARK 465     ALA B   729                                                      
REMARK 465     ILE B   730                                                      
REMARK 465     PRO B   731                                                      
REMARK 465     GLU B   732                                                      
REMARK 465     GLY B   733                                                      
REMARK 465     GLN B   734                                                      
REMARK 465     PHE B   735                                                      
REMARK 465     ILE B   736                                                      
REMARK 465     ASP B   737                                                      
REMARK 465     SER B   738                                                      
REMARK 465     ARG B   739                                                      
REMARK 465     LYS B   740                                                      
REMARK 465     GLY B   741                                                      
REMARK 465     MET B   776                                                      
REMARK 465     ARG B   777                                                      
REMARK 465     ASP B   778                                                      
REMARK 465     GLU B   779                                                      
REMARK 465     ARG B   780                                                      
REMARK 465     LEU B   781                                                      
REMARK 465     SER B   782                                                      
REMARK 465     ARG B   783                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  21    CG   CD   CE   NZ                                   
REMARK 470     ASP A  32    CB   CG   OD1  OD2                                  
REMARK 470     LYS A  34    CG   CD   CE   NZ                                   
REMARK 470     LYS A  35    CD   CE   NZ                                        
REMARK 470     ASP A  42    CG   OD1  OD2                                       
REMARK 470     LYS A  43    CG   CD   CE   NZ                                   
REMARK 470     GLN A  44    CD   OE1  NE2                                       
REMARK 470     VAL A  47    CG1  CG2                                            
REMARK 470     LYS A  48    CG   CD   CE   NZ                                   
REMARK 470     LYS A  50    CE   NZ                                             
REMARK 470     SER A  53    OG                                                  
REMARK 470     LYS A  58    CE   NZ                                             
REMARK 470     GLU A  62    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  67    CE   NZ                                             
REMARK 470     VAL A  69    CG1  CG2                                            
REMARK 470     THR A  70    OG1  CG2                                            
REMARK 470     VAL A  71    CG1  CG2                                            
REMARK 470     LYS A  72    CD   CE   NZ                                        
REMARK 470     GLU A  73    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 203    CG   OD1  OD2                                       
REMARK 470     ARG A 204    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 213    CG   CD   CE   NZ                                   
REMARK 470     LYS A 278    CG   CD   CE   NZ                                   
REMARK 470     GLU A 327    CD   OE1  OE2                                       
REMARK 470     ARG A 369    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 371    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 379    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 403    CD   NE   CZ   NH1  NH2                             
REMARK 470     TYR A 410    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL A 411    CG1  CG2                                            
REMARK 470     LYS A 413    CG   CD   CE   NZ                                   
REMARK 470     GLU A 499    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 502    CG   CD   CE   NZ                                   
REMARK 470     LYS A 503    CD   CE   NZ                                        
REMARK 470     GLU A 504    CD   OE1  OE2                                       
REMARK 470     GLU A 507    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 536    O    CG   CD   OE1  OE2                             
REMARK 470     LYS A 542    CG   CD   CE   NZ                                   
REMARK 470     LYS A 559    CG   CD   CE   NZ                                   
REMARK 470     LYS A 565    CG   CD   CE   NZ                                   
REMARK 470     ARG A 567    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 574    O    CG   CD   OE1  OE2                             
REMARK 470     LYS A 598    CE   NZ                                             
REMARK 470     ASN A 623    CG   OD1  ND2                                       
REMARK 470     PHE A 644    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     ILE A 713    CG1  CG2  CD1                                       
REMARK 470     LEU A 714    CG   CD1  CD2                                       
REMARK 470     SER A 747    OG                                                  
REMARK 470     ASP A 750    CG   OD1  OD2                                       
REMARK 470     THR A 761    OG1  CG2                                            
REMARK 470     LYS A 762    CG   CD   CE   NZ                                   
REMARK 470     VAL A 763    CG1  CG2                                            
REMARK 470     LEU A 769    CG   CD1  CD2                                       
REMARK 470     LEU A 772    CG   CD1  CD2                                       
REMARK 470     GLU A 774    CD   OE1  OE2                                       
REMARK 470     ARG A 777    CZ   NH1  NH2                                       
REMARK 470     GLU B   5    CD   OE1  OE2                                       
REMARK 470     LYS B  18    CD   CE   NZ                                        
REMARK 470     LYS B  21    CG   CD   CE   NZ                                   
REMARK 470     GLN B  27    CG   CD   OE1  NE2                                  
REMARK 470     LEU B  33    CG   CD1  CD2                                       
REMARK 470     LYS B  34    CG   CD   CE   NZ                                   
REMARK 470     LYS B  35    CE   NZ                                             
REMARK 470     ASP B  42    CG   OD1  OD2                                       
REMARK 470     LYS B  43    CG   CD   CE   NZ                                   
REMARK 470     GLN B  44    CD   OE1  NE2                                       
REMARK 470     LYS B  48    CE   NZ                                             
REMARK 470     LYS B  50    CD   CE   NZ                                        
REMARK 470     SER B  53    OG                                                  
REMARK 470     GLU B  55    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  58    CE   NZ                                             
REMARK 470     GLU B  62    CG   CD   OE1  OE2                                  
REMARK 470     TYR B  65    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B  67    NZ                                                  
REMARK 470     THR B  70    OG1  CG2                                            
REMARK 470     LYS B  72    CD   CE   NZ                                        
REMARK 470     GLU B  73    CD   OE1  OE2                                       
REMARK 470     LYS B  83    CE   NZ                                             
REMARK 470     ARG B 204    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 213    CG   CD   CE   NZ                                   
REMARK 470     LYS B 278    CD   CE   NZ                                        
REMARK 470     GLN B 368    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 369    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 371    CD   OE1  OE2                                       
REMARK 470     ARG B 403    CD   NE   CZ   NH1  NH2                             
REMARK 470     TYR B 410    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     VAL B 411    CG1  CG2                                            
REMARK 470     LYS B 413    CD   CE   NZ                                        
REMARK 470     LYS B 450    CG   CD   CE   NZ                                   
REMARK 470     GLU B 499    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 500    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 502    CG   CD   CE   NZ                                   
REMARK 470     LYS B 503    CD   CE   NZ                                        
REMARK 470     GLU B 504    CD   OE1  OE2                                       
REMARK 470     GLU B 507    CG   CD   OE1  OE2                                  
REMARK 470     THR B 509    OG1  CG2                                            
REMARK 470     ILE B 511    CG1  CG2  CD1                                       
REMARK 470     GLU B 536    CD   OE1  OE2                                       
REMARK 470     MET B 539    SD   CE                                             
REMARK 470     LYS B 542    CD   CE   NZ                                        
REMARK 470     LYS B 565    CE   NZ                                             
REMARK 470     ILE B 569    CG1  CG2  CD1                                       
REMARK 470     LYS B 570    CD   CE   NZ                                        
REMARK 470     LYS B 572    CG   CD   CE   NZ                                   
REMARK 470     GLU B 603    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 623    CG   OD1  ND2                                       
REMARK 470     GLN B 645    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 700    CG   CD   OE1  OE2                                  
REMARK 470     CYS B 705    SG                                                  
REMARK 470     ARG B 706    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B 709    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN B 711    OD1  ND2                                            
REMARK 470     ARG B 712    NE   CZ   NH1  NH2                                  
REMARK 470     ILE B 713    CG1  CG2  CD1                                       
REMARK 470     TYR B 715    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B 743    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 745    CG   CD1  CD2                                       
REMARK 470     LEU B 746    CG   CD1  CD2                                       
REMARK 470     SER B 747    OG                                                  
REMARK 470     ASP B 750    CG   OD1  OD2                                       
REMARK 470     ILE B 751    CG1  CG2  CD1                                       
REMARK 470     ASN B 754    CG   OD1  ND2                                       
REMARK 470     GLN B 755    CG   CD   OE1  NE2                                  
REMARK 470     TYR B 756    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B 757    CE   NZ                                             
REMARK 470     PHE B 758    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     HIS B 760    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR B 761    OG1  CG2                                            
REMARK 470     LYS B 762    CG   CD   CE   NZ                                   
REMARK 470     VAL B 763    CG1  CG2                                            
REMARK 470     LYS B 766    CE   NZ                                             
REMARK 470     LEU B 772    CG   CD1  CD2                                       
REMARK 470     LEU B 773    CG   CD1  CD2                                       
REMARK 470     GLU B 774    CD   OE1  OE2                                       
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    ASP A  42      -72.38    -62.73                                   
REMARK 500    GLU A  45      -63.42    -27.27                                   
REMARK 500    TYR A  65        3.17     89.04                                   
REMARK 500    ALA A 279       33.34    -97.85                                   
REMARK 500    GLU A 371       38.48    -90.16                                   
REMARK 500    SER A 472     -160.01   -120.56                                   
REMARK 500    PHE A 510      159.03    -49.92                                   
REMARK 500    ASP A 516       -7.52    -55.78                                   
REMARK 500    HIS A 556      -37.13   -131.75                                   
REMARK 500    SER A 748       62.75   -101.34                                   
REMARK 500    ASP A 750        0.85    -64.41                                   
REMARK 500    LYS B  43      -75.65    -70.94                                   
REMARK 500    TRP B 112       17.73     58.57                                   
REMARK 500    GLU B 269       81.38    -69.57                                   
REMARK 500    GLN B 368      -70.67    -38.78                                   
REMARK 500    GLU B 371       30.39    -98.24                                   
REMARK 500    THR B 509       45.60   -101.65                                   
REMARK 500    ASP B 599       62.71     61.76                                   
REMARK 500    ARG B 703      -63.02    -28.79                                   
REMARK 500    ASP B 750      -83.10    -46.58                                   
REMARK 500    GLN B 755       -3.15   -149.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ILE B  751     ASP B  752                   95.23                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ILE B 751        23.6      L          L   OUTSIDE RANGE           
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                              MN A 802  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP A 801   O3G                                                    
REMARK 620 2 ANP A 801   O2B  80.9                                              
REMARK 620 3 THR A 185   OG1 165.6  85.9                                        
REMARK 620 4 SER A 242   OG   97.8 168.0  94.0                                  
REMARK 620 5 HOH A 902   O    89.5  78.9  82.3  89.2                            
REMARK 620 6 HOH A 901   O    93.9  98.2  93.6  93.8 175.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 802  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP B 801   O3G                                                    
REMARK 620 2 ANP B 801   O2B  85.6                                              
REMARK 620 3 THR B 185   OG1 169.5  84.1                                        
REMARK 620 4 SER B 242   OG   98.6 174.0  91.5                                  
REMARK 620 5 HOH B 902   O    93.6  86.7  87.7  97.4                            
REMARK 620 6 HOH B 901   O    86.3  82.9  90.6  93.0 169.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 802                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2MYS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1MMN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1KQM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1BR4   RELATED DB: PDB                                   
DBREF  4DB1 A    2   783  UNP    P12883   MYH7_HUMAN       2    783             
DBREF  4DB1 B    2   783  UNP    P12883   MYH7_HUMAN       2    783             
SEQADV 4DB1 GLY A    1  UNP  P12883              EXPRESSION TAG                 
SEQADV 4DB1 GLY B    1  UNP  P12883              EXPRESSION TAG                 
SEQRES   1 A  783  GLY GLY ASP SER GLU MET ALA VAL PHE GLY ALA ALA ALA          
SEQRES   2 A  783  PRO TYR LEU ARG LYS SER GLU LYS GLU ARG LEU GLU ALA          
SEQRES   3 A  783  GLN THR ARG PRO PHE ASP LEU LYS LYS ASP VAL PHE VAL          
SEQRES   4 A  783  PRO ASP ASP LYS GLN GLU PHE VAL LYS ALA LYS ILE VAL          
SEQRES   5 A  783  SER ARG GLU GLY GLY LYS VAL THR ALA GLU THR GLU TYR          
SEQRES   6 A  783  GLY LYS THR VAL THR VAL LYS GLU ASP GLN VAL MET GLN          
SEQRES   7 A  783  GLN ASN PRO PRO LYS PHE ASP LYS ILE GLU ASP MET ALA          
SEQRES   8 A  783  MET LEU THR PHE LEU HIS GLU PRO ALA VAL LEU TYR ASN          
SEQRES   9 A  783  LEU LYS ASP ARG TYR GLY SER TRP MET ILE TYR THR TYR          
SEQRES  10 A  783  SER GLY LEU PHE CYS VAL THR VAL ASN PRO TYR LYS TRP          
SEQRES  11 A  783  LEU PRO VAL TYR THR PRO GLU VAL VAL ALA ALA TYR ARG          
SEQRES  12 A  783  GLY LYS LYS ARG SER GLU ALA PRO PRO HIS ILE PHE SER          
SEQRES  13 A  783  ILE SER ASP ASN ALA TYR GLN TYR MET LEU THR ASP ARG          
SEQRES  14 A  783  GLU ASN GLN SER ILE LEU ILE THR GLY GLU SER GLY ALA          
SEQRES  15 A  783  GLY LYS THR VAL ASN THR LYS ARG VAL ILE GLN TYR PHE          
SEQRES  16 A  783  ALA VAL ILE ALA ALA ILE GLY ASP ARG SER LYS LYS ASP          
SEQRES  17 A  783  GLN SER PRO GLY LYS GLY THR LEU GLU ASP GLN ILE ILE          
SEQRES  18 A  783  GLN ALA ASN PRO ALA LEU GLU ALA PHE GLY ASN ALA LYS          
SEQRES  19 A  783  THR VAL ARG ASN ASP ASN SER SER ARG PHE GLY LYS PHE          
SEQRES  20 A  783  ILE ARG ILE HIS PHE GLY ALA THR GLY LYS LEU ALA SER          
SEQRES  21 A  783  ALA ASP ILE GLU THR TYR LEU LEU GLU LYS SER ARG VAL          
SEQRES  22 A  783  ILE PHE GLN LEU LYS ALA GLU ARG ASP TYR HIS ILE PHE          
SEQRES  23 A  783  TYR GLN ILE LEU SER ASN LYS LYS PRO GLU LEU LEU ASP          
SEQRES  24 A  783  MET LEU LEU ILE THR ASN ASN PRO TYR ASP TYR ALA PHE          
SEQRES  25 A  783  ILE SER GLN GLY GLU THR THR VAL ALA SER ILE ASP ASP          
SEQRES  26 A  783  ALA GLU GLU LEU MET ALA THR ASP ASN ALA PHE ASP VAL          
SEQRES  27 A  783  LEU GLY PHE THR SER GLU GLU LYS ASN SER MET TYR LYS          
SEQRES  28 A  783  LEU THR GLY ALA ILE MET HIS PHE GLY ASN MET LYS PHE          
SEQRES  29 A  783  LYS LEU LYS GLN ARG GLU GLU GLN ALA GLU PRO ASP GLY          
SEQRES  30 A  783  THR GLU GLU ALA ASP LYS SER ALA TYR LEU MET GLY LEU          
SEQRES  31 A  783  ASN SER ALA ASP LEU LEU LYS GLY LEU CYS HIS PRO ARG          
SEQRES  32 A  783  VAL LYS VAL GLY ASN GLU TYR VAL THR LYS GLY GLN ASN          
SEQRES  33 A  783  VAL GLN GLN VAL ILE TYR ALA THR GLY ALA LEU ALA LYS          
SEQRES  34 A  783  ALA VAL TYR GLU ARG MET PHE ASN TRP MET VAL THR ARG          
SEQRES  35 A  783  ILE ASN ALA THR LEU GLU THR LYS GLN PRO ARG GLN TYR          
SEQRES  36 A  783  PHE ILE GLY VAL LEU ASP ILE ALA GLY PHE GLU ILE PHE          
SEQRES  37 A  783  ASP PHE ASN SER PHE GLU GLN LEU CYS ILE ASN PHE THR          
SEQRES  38 A  783  ASN GLU LYS LEU GLN GLN PHE PHE ASN HIS HIS MET PHE          
SEQRES  39 A  783  VAL LEU GLU GLN GLU GLU TYR LYS LYS GLU GLY ILE GLU          
SEQRES  40 A  783  TRP THR PHE ILE ASP PHE GLY MET ASP LEU GLN ALA CYS          
SEQRES  41 A  783  ILE ASP LEU ILE GLU LYS PRO MET GLY ILE MET SER ILE          
SEQRES  42 A  783  LEU GLU GLU GLU CYS MET PHE PRO LYS ALA THR ASP MET          
SEQRES  43 A  783  THR PHE LYS ALA LYS LEU PHE ASP ASN HIS LEU GLY LYS          
SEQRES  44 A  783  SER ALA ASN PHE GLN LYS PRO ARG ASN ILE LYS GLY LYS          
SEQRES  45 A  783  PRO GLU ALA HIS PHE SER LEU ILE HIS TYR ALA GLY ILE          
SEQRES  46 A  783  VAL ASP TYR ASN ILE ILE GLY TRP LEU GLN LYS ASN LYS          
SEQRES  47 A  783  ASP PRO LEU ASN GLU THR VAL VAL GLY LEU TYR GLN LYS          
SEQRES  48 A  783  SER SER LEU LYS LEU LEU SER THR LEU PHE ALA ASN TYR          
SEQRES  49 A  783  ALA GLY ALA ASP ALA PRO ILE GLU LYS GLY LYS GLY LYS          
SEQRES  50 A  783  ALA LYS LYS GLY SER SER PHE GLN THR VAL SER ALA LEU          
SEQRES  51 A  783  HIS ARG GLU ASN LEU ASN LYS LEU MET THR ASN LEU ARG          
SEQRES  52 A  783  SER THR HIS PRO HIS PHE VAL ARG CYS ILE ILE PRO ASN          
SEQRES  53 A  783  GLU THR LYS SER PRO GLY VAL MET ASP ASN PRO LEU VAL          
SEQRES  54 A  783  MET HIS GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE          
SEQRES  55 A  783  ARG ILE CYS ARG LYS GLY PHE PRO ASN ARG ILE LEU TYR          
SEQRES  56 A  783  GLY ASP PHE ARG GLN ARG TYR ARG ILE LEU ASN PRO ALA          
SEQRES  57 A  783  ALA ILE PRO GLU GLY GLN PHE ILE ASP SER ARG LYS GLY          
SEQRES  58 A  783  ALA GLU LYS LEU LEU SER SER LEU ASP ILE ASP HIS ASN          
SEQRES  59 A  783  GLN TYR LYS PHE GLY HIS THR LYS VAL PHE PHE LYS ALA          
SEQRES  60 A  783  GLY LEU LEU GLY LEU LEU GLU GLU MET ARG ASP GLU ARG          
SEQRES  61 A  783  LEU SER ARG                                                  
SEQRES   1 B  783  GLY GLY ASP SER GLU MET ALA VAL PHE GLY ALA ALA ALA          
SEQRES   2 B  783  PRO TYR LEU ARG LYS SER GLU LYS GLU ARG LEU GLU ALA          
SEQRES   3 B  783  GLN THR ARG PRO PHE ASP LEU LYS LYS ASP VAL PHE VAL          
SEQRES   4 B  783  PRO ASP ASP LYS GLN GLU PHE VAL LYS ALA LYS ILE VAL          
SEQRES   5 B  783  SER ARG GLU GLY GLY LYS VAL THR ALA GLU THR GLU TYR          
SEQRES   6 B  783  GLY LYS THR VAL THR VAL LYS GLU ASP GLN VAL MET GLN          
SEQRES   7 B  783  GLN ASN PRO PRO LYS PHE ASP LYS ILE GLU ASP MET ALA          
SEQRES   8 B  783  MET LEU THR PHE LEU HIS GLU PRO ALA VAL LEU TYR ASN          
SEQRES   9 B  783  LEU LYS ASP ARG TYR GLY SER TRP MET ILE TYR THR TYR          
SEQRES  10 B  783  SER GLY LEU PHE CYS VAL THR VAL ASN PRO TYR LYS TRP          
SEQRES  11 B  783  LEU PRO VAL TYR THR PRO GLU VAL VAL ALA ALA TYR ARG          
SEQRES  12 B  783  GLY LYS LYS ARG SER GLU ALA PRO PRO HIS ILE PHE SER          
SEQRES  13 B  783  ILE SER ASP ASN ALA TYR GLN TYR MET LEU THR ASP ARG          
SEQRES  14 B  783  GLU ASN GLN SER ILE LEU ILE THR GLY GLU SER GLY ALA          
SEQRES  15 B  783  GLY LYS THR VAL ASN THR LYS ARG VAL ILE GLN TYR PHE          
SEQRES  16 B  783  ALA VAL ILE ALA ALA ILE GLY ASP ARG SER LYS LYS ASP          
SEQRES  17 B  783  GLN SER PRO GLY LYS GLY THR LEU GLU ASP GLN ILE ILE          
SEQRES  18 B  783  GLN ALA ASN PRO ALA LEU GLU ALA PHE GLY ASN ALA LYS          
SEQRES  19 B  783  THR VAL ARG ASN ASP ASN SER SER ARG PHE GLY LYS PHE          
SEQRES  20 B  783  ILE ARG ILE HIS PHE GLY ALA THR GLY LYS LEU ALA SER          
SEQRES  21 B  783  ALA ASP ILE GLU THR TYR LEU LEU GLU LYS SER ARG VAL          
SEQRES  22 B  783  ILE PHE GLN LEU LYS ALA GLU ARG ASP TYR HIS ILE PHE          
SEQRES  23 B  783  TYR GLN ILE LEU SER ASN LYS LYS PRO GLU LEU LEU ASP          
SEQRES  24 B  783  MET LEU LEU ILE THR ASN ASN PRO TYR ASP TYR ALA PHE          
SEQRES  25 B  783  ILE SER GLN GLY GLU THR THR VAL ALA SER ILE ASP ASP          
SEQRES  26 B  783  ALA GLU GLU LEU MET ALA THR ASP ASN ALA PHE ASP VAL          
SEQRES  27 B  783  LEU GLY PHE THR SER GLU GLU LYS ASN SER MET TYR LYS          
SEQRES  28 B  783  LEU THR GLY ALA ILE MET HIS PHE GLY ASN MET LYS PHE          
SEQRES  29 B  783  LYS LEU LYS GLN ARG GLU GLU GLN ALA GLU PRO ASP GLY          
SEQRES  30 B  783  THR GLU GLU ALA ASP LYS SER ALA TYR LEU MET GLY LEU          
SEQRES  31 B  783  ASN SER ALA ASP LEU LEU LYS GLY LEU CYS HIS PRO ARG          
SEQRES  32 B  783  VAL LYS VAL GLY ASN GLU TYR VAL THR LYS GLY GLN ASN          
SEQRES  33 B  783  VAL GLN GLN VAL ILE TYR ALA THR GLY ALA LEU ALA LYS          
SEQRES  34 B  783  ALA VAL TYR GLU ARG MET PHE ASN TRP MET VAL THR ARG          
SEQRES  35 B  783  ILE ASN ALA THR LEU GLU THR LYS GLN PRO ARG GLN TYR          
SEQRES  36 B  783  PHE ILE GLY VAL LEU ASP ILE ALA GLY PHE GLU ILE PHE          
SEQRES  37 B  783  ASP PHE ASN SER PHE GLU GLN LEU CYS ILE ASN PHE THR          
SEQRES  38 B  783  ASN GLU LYS LEU GLN GLN PHE PHE ASN HIS HIS MET PHE          
SEQRES  39 B  783  VAL LEU GLU GLN GLU GLU TYR LYS LYS GLU GLY ILE GLU          
SEQRES  40 B  783  TRP THR PHE ILE ASP PHE GLY MET ASP LEU GLN ALA CYS          
SEQRES  41 B  783  ILE ASP LEU ILE GLU LYS PRO MET GLY ILE MET SER ILE          
SEQRES  42 B  783  LEU GLU GLU GLU CYS MET PHE PRO LYS ALA THR ASP MET          
SEQRES  43 B  783  THR PHE LYS ALA LYS LEU PHE ASP ASN HIS LEU GLY LYS          
SEQRES  44 B  783  SER ALA ASN PHE GLN LYS PRO ARG ASN ILE LYS GLY LYS          
SEQRES  45 B  783  PRO GLU ALA HIS PHE SER LEU ILE HIS TYR ALA GLY ILE          
SEQRES  46 B  783  VAL ASP TYR ASN ILE ILE GLY TRP LEU GLN LYS ASN LYS          
SEQRES  47 B  783  ASP PRO LEU ASN GLU THR VAL VAL GLY LEU TYR GLN LYS          
SEQRES  48 B  783  SER SER LEU LYS LEU LEU SER THR LEU PHE ALA ASN TYR          
SEQRES  49 B  783  ALA GLY ALA ASP ALA PRO ILE GLU LYS GLY LYS GLY LYS          
SEQRES  50 B  783  ALA LYS LYS GLY SER SER PHE GLN THR VAL SER ALA LEU          
SEQRES  51 B  783  HIS ARG GLU ASN LEU ASN LYS LEU MET THR ASN LEU ARG          
SEQRES  52 B  783  SER THR HIS PRO HIS PHE VAL ARG CYS ILE ILE PRO ASN          
SEQRES  53 B  783  GLU THR LYS SER PRO GLY VAL MET ASP ASN PRO LEU VAL          
SEQRES  54 B  783  MET HIS GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE          
SEQRES  55 B  783  ARG ILE CYS ARG LYS GLY PHE PRO ASN ARG ILE LEU TYR          
SEQRES  56 B  783  GLY ASP PHE ARG GLN ARG TYR ARG ILE LEU ASN PRO ALA          
SEQRES  57 B  783  ALA ILE PRO GLU GLY GLN PHE ILE ASP SER ARG LYS GLY          
SEQRES  58 B  783  ALA GLU LYS LEU LEU SER SER LEU ASP ILE ASP HIS ASN          
SEQRES  59 B  783  GLN TYR LYS PHE GLY HIS THR LYS VAL PHE PHE LYS ALA          
SEQRES  60 B  783  GLY LEU LEU GLY LEU LEU GLU GLU MET ARG ASP GLU ARG          
SEQRES  61 B  783  LEU SER ARG                                                  
HET    ANP  A 801      31                                                       
HET     MN  A 802       1                                                       
HET    ANP  B 801      31                                                       
HET     MN  B 802       1                                                       
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   3  ANP    2(C10 H17 N6 O12 P3)                                         
FORMUL   4   MN    2(MN 2+)                                                     
FORMUL   7  HOH   *202(H2 O)                                                    
HELIX    1   1 ASP A    3  LEU A   16  5                                  14    
HELIX    2   2 SER A   19  ARG A   29  1                                  11    
HELIX    3   3 ASP A   74  VAL A   76  5                                   3    
HELIX    4   4 PRO A   81  ASP A   85  5                                   5    
HELIX    5   5 ASP A   89  LEU A   93  5                                   5    
HELIX    6   6 HIS A   97  SER A  111  1                                  15    
HELIX    7   7 THR A  135  ARG A  143  1                                   9    
HELIX    8   8 LYS A  146  ALA A  150  5                                   5    
HELIX    9   9 HIS A  153  ARG A  169  1                                  17    
HELIX   10  10 GLY A  183  ALA A  199  1                                  17    
HELIX   11  11 THR A  215  GLY A  231  1                                  17    
HELIX   12  12 GLU A  269  ILE A  274  5                                   6    
HELIX   13  13 TYR A  283  SER A  291  1                                   9    
HELIX   14  14 LYS A  294  LEU A  301  1                                   8    
HELIX   15  15 ASN A  306  SER A  314  5                                   9    
HELIX   16  16 ASP A  324  LEU A  339  1                                  16    
HELIX   17  17 THR A  342  GLY A  360  1                                  19    
HELIX   18  18 THR A  378  MET A  388  1                                  11    
HELIX   19  19 ASN A  391  HIS A  401  1                                  11    
HELIX   20  20 ASN A  416  GLU A  448  1                                  33    
HELIX   21  21 SER A  472  GLY A  505  1                                  34    
HELIX   22  22 ASP A  512  ASP A  516  5                                   5    
HELIX   23  23 LEU A  517  LYS A  526  1                                  10    
HELIX   24  24 GLY A  529  GLU A  536  1                                   8    
HELIX   25  25 THR A  544  LEU A  557  1                                  14    
HELIX   26  26 GLY A  592  ASP A  599  1                                   8    
HELIX   27  27 ASN A  602  LYS A  611  1                                  10    
HELIX   28  28 LEU A  614  ASN A  623  1                                  10    
HELIX   29  29 THR A  646  SER A  664  1                                  19    
HELIX   30  30 ASP A  685  ASN A  696  1                                  12    
HELIX   31  31 GLY A  697  LYS A  707  1                                  11    
HELIX   32  32 GLU A  743  SER A  748  1                                   6    
HELIX   33  33 ASP A  752  ASN A  754  5                                   3    
HELIX   34  34 GLY A  768  ARG A  777  1                                  10    
HELIX   35  35 ASP B    3  LEU B   16  5                                  14    
HELIX   36  36 SER B   19  ARG B   29  1                                  11    
HELIX   37  37 ASP B   74  VAL B   76  5                                   3    
HELIX   38  38 PRO B   81  ASP B   85  5                                   5    
HELIX   39  39 ASP B   89  LEU B   93  5                                   5    
HELIX   40  40 HIS B   97  GLY B  110  1                                  14    
HELIX   41  41 THR B  135  ARG B  143  1                                   9    
HELIX   42  42 LYS B  146  ALA B  150  5                                   5    
HELIX   43  43 HIS B  153  ARG B  169  1                                  17    
HELIX   44  44 GLY B  183  ALA B  199  1                                  17    
HELIX   45  45 THR B  215  GLY B  231  1                                  17    
HELIX   46  46 GLU B  269  ILE B  274  5                                   6    
HELIX   47  47 TYR B  283  SER B  291  1                                   9    
HELIX   48  48 LYS B  294  LEU B  302  1                                   9    
HELIX   49  49 ASN B  306  SER B  314  5                                   9    
HELIX   50  50 ASP B  324  LEU B  339  1                                  16    
HELIX   51  51 THR B  342  GLY B  360  1                                  19    
HELIX   52  52 THR B  378  MET B  388  1                                  11    
HELIX   53  53 ASN B  391  HIS B  401  1                                  11    
HELIX   54  54 ASN B  416  GLU B  448  1                                  33    
HELIX   55  55 SER B  472  LYS B  503  1                                  32    
HELIX   56  56 ASP B  512  ASP B  516  5                                   5    
HELIX   57  57 LEU B  517  LYS B  526  1                                  10    
HELIX   58  58 GLY B  529  MET B  539  1                                  11    
HELIX   59  59 THR B  544  LEU B  557  1                                  14    
HELIX   60  60 GLY B  592  ASP B  599  1                                   8    
HELIX   61  61 ASN B  602  LYS B  611  1                                  10    
HELIX   62  62 LEU B  614  ASN B  623  1                                  10    
HELIX   63  63 THR B  646  ARG B  663  1                                  18    
HELIX   64  64 ASP B  685  GLY B  697  1                                  13    
HELIX   65  65 GLY B  701  GLY B  708  1                                   8    
HELIX   66  66 GLY B  768  GLU B  774  1                                   7    
SHEET    1   A 5 LYS A  67  LYS A  72  0                                        
SHEET    2   A 5 LYS A  58  THR A  63 -1  N  VAL A  59   O  VAL A  71           
SHEET    3   A 5 PHE A  46  ARG A  54 -1  N  LYS A  50   O  GLU A  62           
SHEET    4   A 5 ASP A  36  PRO A  40 -1  N  VAL A  37   O  ALA A  49           
SHEET    5   A 5 MET A  77  GLN A  78 -1  O  MET A  77   N  PHE A  38           
SHEET    1   B 7 TYR A 115  SER A 118  0                                        
SHEET    2   B 7 PHE A 121  VAL A 125 -1  O  VAL A 123   N  THR A 116           
SHEET    3   B 7 HIS A 666  ILE A 673  1  O  ILE A 673   N  THR A 124           
SHEET    4   B 7 GLN A 172  THR A 177  1  N  THR A 177   O  CYS A 672           
SHEET    5   B 7 TYR A 455  ASP A 461  1  O  GLY A 458   N  ILE A 174           
SHEET    6   B 7 GLY A 245  PHE A 252 -1  N  ILE A 248   O  VAL A 459           
SHEET    7   B 7 LEU A 258  TYR A 266 -1  O  ALA A 259   N  HIS A 251           
SHEET    1   C 2 ASN A 232  ALA A 233  0                                        
SHEET    2   C 2 SER A 241  SER A 242 -1  O  SER A 241   N  ALA A 233           
SHEET    1   D 2 PHE A 364  LEU A 366  0                                        
SHEET    2   D 2 ALA A 373  PRO A 375 -1  O  GLU A 374   N  LYS A 365           
SHEET    1   E 3 PHE A 563  GLN A 564  0                                        
SHEET    2   E 3 PHE A 577  HIS A 581 -1  O  SER A 578   N  GLN A 564           
SHEET    3   E 3 GLY A 584  TYR A 588 -1  O  TYR A 588   N  PHE A 577           
SHEET    1   F 3 ASN A 711  LEU A 714  0                                        
SHEET    2   F 3 LYS A 762  PHE A 765 -1  O  PHE A 765   N  ASN A 711           
SHEET    3   F 3 TYR A 756  PHE A 758 -1  N  LYS A 757   O  PHE A 764           
SHEET    1   G 5 THR B  68  LYS B  72  0                                        
SHEET    2   G 5 LYS B  58  THR B  63 -1  N  ALA B  61   O  VAL B  69           
SHEET    3   G 5 PHE B  46  ARG B  54 -1  N  SER B  53   O  THR B  60           
SHEET    4   G 5 ASP B  36  PRO B  40 -1  N  VAL B  37   O  ALA B  49           
SHEET    5   G 5 MET B  77  GLN B  78 -1  O  MET B  77   N  PHE B  38           
SHEET    1   H 7 TYR B 115  SER B 118  0                                        
SHEET    2   H 7 PHE B 121  VAL B 125 -1  O  VAL B 123   N  THR B 116           
SHEET    3   H 7 HIS B 666  ILE B 673  1  O  ARG B 671   N  CYS B 122           
SHEET    4   H 7 GLN B 172  GLY B 178  1  N  LEU B 175   O  VAL B 670           
SHEET    5   H 7 TYR B 455  ASP B 461  1  O  LEU B 460   N  ILE B 176           
SHEET    6   H 7 GLY B 245  PHE B 252 -1  N  ILE B 248   O  VAL B 459           
SHEET    7   H 7 LEU B 258  TYR B 266 -1  O  ASP B 262   N  ARG B 249           
SHEET    1   I 2 ASN B 232  ALA B 233  0                                        
SHEET    2   I 2 SER B 241  SER B 242 -1  O  SER B 241   N  ALA B 233           
SHEET    1   J 2 PHE B 364  LEU B 366  0                                        
SHEET    2   J 2 ALA B 373  PRO B 375 -1  O  GLU B 374   N  LYS B 365           
SHEET    1   K 3 PHE B 563  GLN B 564  0                                        
SHEET    2   K 3 PHE B 577  HIS B 581 -1  O  SER B 578   N  GLN B 564           
SHEET    3   K 3 GLY B 584  TYR B 588 -1  O  TYR B 588   N  PHE B 577           
SHEET    1   L 3 ASN B 711  ILE B 713  0                                        
SHEET    2   L 3 VAL B 763  PHE B 765 -1  O  VAL B 763   N  ILE B 713           
SHEET    3   L 3 TYR B 756  PHE B 758 -1  N  LYS B 757   O  PHE B 764           
LINK         O3G ANP A 801                MN    MN A 802     1555   1555  1.80  
LINK         O3G ANP B 801                MN    MN B 802     1555   1555  1.85  
LINK         O2B ANP B 801                MN    MN B 802     1555   1555  1.94  
LINK         O2B ANP A 801                MN    MN A 802     1555   1555  2.06  
LINK         OG1 THR A 185                MN    MN A 802     1555   1555  2.13  
LINK         OG1 THR B 185                MN    MN B 802     1555   1555  2.19  
LINK         OG  SER A 242                MN    MN A 802     1555   1555  2.29  
LINK         OG  SER B 242                MN    MN B 802     1555   1555  2.36  
LINK        MN    MN A 802                 O   HOH A 902     1555   1555  2.03  
LINK        MN    MN A 802                 O   HOH A 901     1555   1555  2.05  
LINK        MN    MN B 802                 O   HOH B 902     1555   1555  2.11  
LINK        MN    MN B 802                 O   HOH B 901     1555   1555  2.23  
SITE     1 AC1 19 ASN A 126  PRO A 127  LYS A 129  TRP A 130                    
SITE     2 AC1 19 TYR A 134  SER A 180  GLY A 181  ALA A 182                    
SITE     3 AC1 19 GLY A 183  LYS A 184  THR A 185  VAL A 186                    
SITE     4 AC1 19 ASN A 238  SER A 241  SER A 242   MN A 802                    
SITE     5 AC1 19 HOH A 901  HOH A 902  HOH A 921                               
SITE     1 AC2  5 THR A 185  SER A 242  ANP A 801  HOH A 901                    
SITE     2 AC2  5 HOH A 902                                                     
SITE     1 AC3 22 ASN B 126  PRO B 127  LYS B 129  TRP B 130                    
SITE     2 AC3 22 TYR B 134  SER B 180  GLY B 181  ALA B 182                    
SITE     3 AC3 22 GLY B 183  LYS B 184  THR B 185  VAL B 186                    
SITE     4 AC3 22 ASN B 238  ASN B 240  SER B 241  SER B 242                    
SITE     5 AC3 22  MN B 802  HOH B 901  HOH B 902  HOH B 910                    
SITE     6 AC3 22 HOH B 947  HOH B 967                                          
SITE     1 AC4  5 THR B 185  SER B 242  ANP B 801  HOH B 901                    
SITE     2 AC4  5 HOH B 902                                                     
CRYST1  100.206   94.310  110.894  90.00 112.29  90.00 P 1 21 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      0.009979  0.000000  0.004091        0.00000                         
SCALE2      0.000000  0.010603  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009746        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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