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Database: PDB
Entry: 3FHI
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Original site: 3FHI 
HEADER    TRANSFERASE                             09-DEC-08   3FHI              
TITLE     CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE CATALYTIC AND REGULATORY   
TITLE    2 (RI{ALPHA}) SUBUNITS OF PKA                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PKA C-ALPHA;                                                
COMPND   5 EC: 2.7.11.11;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE I-ALPHA REGULATORY      
COMPND  10 SUBUNIT;                                                             
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 92-245;                                       
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PRKACA, PKACA;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  10 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;            
SOURCE  11 ORGANISM_TAXID: 9913;                                                
SOURCE  12 GENE: PRKAR1A;                                                       
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CAMP, CAMP DEPENDENT PROTEIN KINASE, PROTEIN-PROTEIN COMPLEX, AMP-    
KEYWDS   2 PNP, PROTEIN KINASE REGULATION, NUCLEOTIDE BINDING, PROTEIN KINASE   
KEYWDS   3 ACTIVITY, PROTEIN SERINE/THREONINE KINASE ACTIVITY, CAMP-DEPENDENT   
KEYWDS   4 PROTEIN KINASE ACTIVITY, PROTEIN BINDING, ATP BINDING, KINASE        
KEYWDS   5 ACTIVITY, TRANSFERASE ACTIVITY, ATP-BINDING, KINASE, LIPOPROTEIN,    
KEYWDS   6 MYRISTATE, NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN,              
KEYWDS   7 SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE, CAMP-BINDING           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.KIM                                                                 
REVDAT   3   01-NOV-17 3FHI    1       REMARK                                   
REVDAT   2   13-JUL-11 3FHI    1       VERSN                                    
REVDAT   1   14-APR-09 3FHI    0                                                
SPRSDE     14-APR-09 3FHI      1U7E                                             
JRNL        AUTH   C.KIM,N.H.XUONG,S.S.TAYLOR                                   
JRNL        TITL   CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE CATALYTIC AND     
JRNL        TITL 2 REGULATORY (RIALPHA) SUBUNITS OF PKA.                        
JRNL        REF    SCIENCE                       V. 307   690 2005              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   15692043                                                     
JRNL        DOI    10.1126/SCIENCE.1104607                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 42244                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2136                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2870                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.34                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 144                          
REMARK   3   BIN FREE R VALUE                    : 0.2700                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3842                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 159                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 34.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.17000                                              
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) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.166         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.146         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.117         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.427         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3966 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2661 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5381 ; 1.406 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6453 ; 0.884 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   486 ; 6.161 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   180 ;35.744 ;23.667       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   645 ;14.052 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;17.701 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   585 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4422 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   861 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   806 ; 0.223 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2789 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1956 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2041 ; 0.087 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   176 ; 0.128 ; 0.200       
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):     4 ; 0.178 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    25 ; 0.228 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.145 ; 0.200       
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):  2597 ; 0.740 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   990 ; 0.157 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3867 ; 1.095 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1735 ; 1.735 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1514 ; 2.505 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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    11        A   128                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.7240   3.1540  29.6710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1812 T22:   0.1740                                     
REMARK   3      T33:  -0.0887 T12:  -0.0864                                     
REMARK   3      T13:   0.0218 T23:  -0.0500                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4533 L22:   2.4387                                     
REMARK   3      L33:   1.8748 L12:   0.3267                                     
REMARK   3      L13:   0.1466 L23:   1.2075                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1127 S12:   0.3550 S13:   0.0602                       
REMARK   3      S21:  -0.9870 S22:   0.1329 S23:  -0.0605                       
REMARK   3      S31:  -0.3178 S32:   0.1779 S33:  -0.0203                       
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 :   B    92        B   240                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.4670  35.2720  48.5000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1200 T22:   0.0316                                     
REMARK   3      T33:  -0.2640 T12:  -0.0518                                     
REMARK   3      T13:  -0.0110 T23:   0.0271                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5522 L22:   1.0946                                     
REMARK   3      L33:   1.0342 L12:   0.0055                                     
REMARK   3      L13:  -0.1544 L23:  -0.1823                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0541 S12:   0.1922 S13:   0.0973                       
REMARK   3      S21:  -0.1134 S22:   0.0324 S23:  -0.0838                       
REMARK   3      S31:   0.0455 S32:  -0.0364 S33:   0.0217                       
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 :   A   400        A   403                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.4130   6.0400  36.5500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2356 T22:   0.3072                                     
REMARK   3      T33:   0.0823 T12:  -0.1240                                     
REMARK   3      T13:  -0.0484 T23:  -0.0445                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.1568 L22:   6.1915                                     
REMARK   3      L33:  14.5148 L12:   9.0039                                     
REMARK   3      L13:   8.7154 L23:   2.3476                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2099 S12:  -0.1288 S13:  -0.3546                       
REMARK   3      S21:  -0.7638 S22:   0.7170 S23:  -0.4087                       
REMARK   3      S31:   0.3891 S32:  -0.9316 S33:  -0.5072                       
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 :   A   129        A   350                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1380   4.5860  48.5950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1612 T22:  -0.0445                                     
REMARK   3      T33:  -0.2646 T12:  -0.0308                                     
REMARK   3      T13:   0.0263 T23:  -0.0296                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1831 L22:   1.9908                                     
REMARK   3      L33:   1.2963 L12:   0.2697                                     
REMARK   3      L13:  -0.2287 L23:   0.2555                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1032 S12:   0.1519 S13:  -0.1666                       
REMARK   3      S21:  -0.3173 S22:   0.0998 S23:   0.0369                       
REMARK   3      S31:  -0.0027 S32:   0.0247 S33:   0.0033                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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                                                           
REMARK   4                                                                      
REMARK   4 3FHI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000050597.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-OCT-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL, SI(111)            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42244                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 23.50                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.25300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER, DM                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 2000, 0.1 M TRIS-HCL, 4 % 1,3   
REMARK 280  -PROPANEDIOL, 2.0 MM CYCLOHEXYL-PENTYL-D-MALTOSIDE, PH 7.0,         
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       27.22650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.02150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.50850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.02150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.22650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.50850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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     GLY A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     LYS A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 465     GLY B    91                                                      
REMARK 465     LYS B   242                                                      
REMARK 465     MET B   243                                                      
REMARK 465     TYR B   244                                                      
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     GLU A  13    CG   CD   OE1  OE2                                  
REMARK 470     SER A  14    OG                                                  
REMARK 470     LYS A  16    CG   CD   CE   NZ                                   
REMARK 470     GLU A  17    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  21    CG   CD   CE   NZ                                   
REMARK 470     LYS A  28    CG   CD   CE   NZ                                   
REMARK 470     GLU A  31    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  35    CG   CD   OE1  NE2                                  
REMARK 470     GLN A  39    CG   CD   OE1  NE2                                  
REMARK 470     ASP A  41    CG   OD1  OD2                                       
REMARK 470     ASP A  44    CG   OD1  OD2                                       
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 176    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 192    CG   CD   CE   NZ                                   
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     PHE A 318    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 319    CG   CD   CE   NZ                                   
REMARK 470     GLU A 331    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 333    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 334    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 335    CG1  CG2  CD1                                       
REMARK 470     ARG A 336    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 345    CG   CD   CE   NZ                                   
REMARK 470     GLU A 349    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 350    O                                                   
REMARK 470     ARG B  92    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  93    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 106    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 107    CG   OD1  OD2                                       
REMARK 470     SER B 110    OG                                                  
REMARK 470     LYS B 114    CG   CD   CE   NZ                                   
REMARK 470     LYS B 121    CG   CD   CE   NZ                                   
REMARK 470     GLU B 168    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 241    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 137   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 144   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG A 144   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 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    ASP A 112     -158.30   -130.88                                   
REMARK 500    ASP A 166       46.35   -143.44                                   
REMARK 500    ASP A 184       75.70     64.04                                   
REMARK 500    LEU A 273       41.75    -88.22                                   
REMARK 500    LYS A 319       54.68   -109.88                                   
REMARK 500    ILE A 335       85.94    -41.43                                   
REMARK 500    ASN B 186       16.30     59.82                                   
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 TYR B  205     GLY B  206                   43.12                    
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 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 171   OD1                                                    
REMARK 620 2 ASP A 184   OD1  88.6                                              
REMARK 620 3 ANP A 400   O2G 118.0  86.4                                        
REMARK 620 4 ANP A 400   O2A  93.7  91.0 148.0                                  
REMARK 620 5 HOH A 416   O    96.3 173.2  87.1  93.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 184   OD2                                                    
REMARK 620 2 ANP A 400   O1G 143.8                                              
REMARK 620 3 ANP A 400   O2B  88.3  85.6                                        
REMARK 620 4 HOH A 372   O   103.5 111.7  86.3                                  
REMARK 620 5 HOH A 356   O    94.4  96.6 171.8  85.5                            
REMARK 620 N                    1     2     3     4                             
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 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402                  
DBREF  3FHI A    1   350  UNP    P05132   KAPCA_MOUSE      2    351             
DBREF  3FHI B   91   244  UNP    P00514   KAP0_BOVIN      92    245             
SEQADV 3FHI ALA A  199  UNP  P05132    CYS   200 ENGINEERED                     
SEQRES   1 A  350  GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU          
SEQRES   2 A  350  SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE          
SEQRES   3 A  350  LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN          
SEQRES   4 A  350  LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY          
SEQRES   5 A  350  SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER          
SEQRES   6 A  350  GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS          
SEQRES   7 A  350  VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU          
SEQRES   8 A  350  LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL          
SEQRES   9 A  350  LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR          
SEQRES  10 A  350  MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER          
SEQRES  11 A  350  HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA          
SEQRES  12 A  350  ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR          
SEQRES  13 A  350  LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO          
SEQRES  14 A  350  GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL          
SEQRES  15 A  350  THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR          
SEQRES  16 A  350  TRP TPO LEU ALA GLY THR PRO GLU TYR LEU ALA PRO GLU          
SEQRES  17 A  350  ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP          
SEQRES  18 A  350  TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY          
SEQRES  19 A  350  TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR          
SEQRES  20 A  350  GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS          
SEQRES  21 A  350  PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU          
SEQRES  22 A  350  GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN          
SEQRES  23 A  350  GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR          
SEQRES  24 A  350  THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA          
SEQRES  25 A  350  PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER          
SEQRES  26 A  350  ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP          
SEQRES  27 A  350  ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE              
SEQRES   1 B  154  GLY ARG ARG ARG ARG GLY ALA ILE SER ALA GLU VAL TYR          
SEQRES   2 B  154  THR GLU GLU ASP ALA ALA SER TYR VAL ARG LYS VAL ILE          
SEQRES   3 B  154  PRO LYS ASP TYR LYS THR MET ALA ALA LEU ALA LYS ALA          
SEQRES   4 B  154  ILE GLU LYS ASN VAL LEU PHE SER HIS LEU ASP ASP ASN          
SEQRES   5 B  154  GLU ARG SER ASP ILE PHE ASP ALA MET PHE PRO VAL SER          
SEQRES   6 B  154  PHE ILE ALA GLY GLU THR VAL ILE GLN GLN GLY ASP GLU          
SEQRES   7 B  154  GLY ASP ASN PHE TYR VAL ILE ASP GLN GLY GLU MET ASP          
SEQRES   8 B  154  VAL TYR VAL ASN ASN GLU TRP ALA THR SER VAL GLY GLU          
SEQRES   9 B  154  GLY GLY SER PHE GLY GLU LEU ALA LEU ILE TYR GLY THR          
SEQRES  10 B  154  PRO ARG ALA ALA THR VAL LYS ALA LYS THR ASN VAL LYS          
SEQRES  11 B  154  LEU TRP GLY ILE ASP ARG ASP SER TYR ARG ARG ILE LEU          
SEQRES  12 B  154  MET GLY SER THR LEU ARG LYS ARG LYS MET TYR                  
MODRES 3FHI TPO A  197  THR  PHOSPHOTHREONINE                                   
MODRES 3FHI SEP A  338  SER  PHOSPHOSERINE                                      
HET    TPO  A 197      11                                                       
HET    SEP  A 338      10                                                       
HET    ANP  A 400      31                                                       
HET     MN  A 401       1                                                       
HET     MN  A 402       1                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM      MN MANGANESE (II) ION                                               
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   3  ANP    C10 H17 N6 O12 P3                                            
FORMUL   4   MN    2(MN 2+)                                                     
FORMUL   6  HOH   *159(H2 O)                                                    
HELIX    1   1 GLU A   13  THR A   32  1                                  20    
HELIX    2   2 GLN A   39  ASP A   41  5                                   3    
HELIX    3   3 LYS A   76  LEU A   82  1                                   7    
HELIX    4   4 GLN A   84  VAL A   98  1                                  15    
HELIX    5   5 GLU A  127  GLY A  136  1                                  10    
HELIX    6   6 SER A  139  LEU A  160  1                                  22    
HELIX    7   7 LYS A  168  GLU A  170  5                                   3    
HELIX    8   8 THR A  201  LEU A  205  5                                   5    
HELIX    9   9 ALA A  206  LEU A  211  1                                   6    
HELIX   10  10 ALA A  218  GLY A  234  1                                  17    
HELIX   11  11 GLN A  242  GLY A  253  1                                  12    
HELIX   12  12 SER A  262  LEU A  273  1                                  12    
HELIX   13  13 ASP A  276  ARG A  280  5                                   5    
HELIX   14  14 VAL A  288  ASN A  293  1                                   6    
HELIX   15  15 HIS A  294  ALA A  298  5                                   5    
HELIX   16  16 ASP A  301  GLN A  307  1                                   7    
HELIX   17  17 THR B  104  ALA B  109  5                                   6    
HELIX   18  18 ASP B  119  ILE B  130  1                                  12    
HELIX   19  19 ASP B  140  MET B  151  1                                  12    
HELIX   20  20 GLY B  199  ILE B  204  5                                   6    
HELIX   21  21 ARG B  226  LYS B  240  1                                  15    
SHEET    1   A 5 PHE A  43  THR A  51  0                                        
SHEET    2   A 5 ARG A  56  HIS A  62 -1  O  LEU A  59   N  LYS A  47           
SHEET    3   A 5 HIS A  68  ASP A  75 -1  O  ILE A  73   N  ARG A  56           
SHEET    4   A 5 ASN A 115  GLU A 121 -1  O  MET A 118   N  LYS A  72           
SHEET    5   A 5 LEU A 106  LYS A 111 -1  N  PHE A 108   O  VAL A 119           
SHEET    1   B 2 LEU A 162  ILE A 163  0                                        
SHEET    2   B 2 LYS A 189  ARG A 190 -1  O  LYS A 189   N  ILE A 163           
SHEET    1   C 2 LEU A 172  ILE A 174  0                                        
SHEET    2   C 2 ILE A 180  VAL A 182 -1  O  GLN A 181   N  LEU A 173           
SHEET    1   D 2 ALA A 199  GLY A 200  0                                        
SHEET    2   D 2 ILE B  98  SER B  99 -1  O  ILE B  98   N  GLY A 200           
SHEET    1   E 4 PHE B 152  PHE B 156  0                                        
SHEET    2   E 4 VAL B 219  ASP B 225 -1  O  LEU B 221   N  VAL B 154           
SHEET    3   E 4 ASN B 171  GLN B 177 -1  N  PHE B 172   O  ILE B 224           
SHEET    4   E 4 SER B 197  PHE B 198 -1  O  PHE B 198   N  TYR B 173           
SHEET    1   F 4 THR B 161  ILE B 163  0                                        
SHEET    2   F 4 THR B 212  ALA B 215 -1  O  VAL B 213   N  ILE B 163           
SHEET    3   F 4 MET B 180  VAL B 184 -1  N  ASP B 181   O  LYS B 214           
SHEET    4   F 4 GLU B 187  VAL B 192 -1  O  ALA B 189   N  VAL B 182           
LINK         C   TRP A 196                 N   TPO A 197     1555   1555  1.33  
LINK         C   TPO A 197                 N   LEU A 198     1555   1555  1.32  
LINK         C   VAL A 337                 N   SEP A 338     1555   1555  1.34  
LINK         C   SEP A 338                 N   ILE A 339     1555   1555  1.33  
LINK         OD1 ASN A 171                MN    MN A 401     1555   1555  2.01  
LINK         OD1 ASP A 184                MN    MN A 401     1555   1555  1.78  
LINK         OD2 ASP A 184                MN    MN A 402     1555   1555  2.06  
LINK         O1G ANP A 400                MN    MN A 402     1555   1555  1.89  
LINK         O2G ANP A 400                MN    MN A 401     1555   1555  2.24  
LINK         O2B ANP A 400                MN    MN A 402     1555   1555  2.24  
LINK         O2A ANP A 400                MN    MN A 401     1555   1555  2.13  
LINK        MN    MN A 401                 O   HOH A 416     1555   1555  1.91  
LINK        MN    MN A 402                 O   HOH A 372     1555   1555  2.21  
LINK        MN    MN A 402                 O   HOH A 356     1555   1555  2.26  
SITE     1 AC1 31 GLY A  50  THR A  51  GLY A  52  SER A  53                    
SITE     2 AC1 31 PHE A  54  GLY A  55  VAL A  57  ALA A  70                    
SITE     3 AC1 31 LYS A  72  VAL A 104  MET A 120  GLU A 121                    
SITE     4 AC1 31 VAL A 123  GLU A 127  ASP A 166  LYS A 168                    
SITE     5 AC1 31 GLU A 170  ASN A 171  LEU A 173  THR A 183                    
SITE     6 AC1 31 ASP A 184  PHE A 327  HOH A 372   MN A 401                    
SITE     7 AC1 31  MN A 402  HOH A 416  HOH A 497  HOH A 505                    
SITE     8 AC1 31 ARG B  94  GLY B  96  ALA B  97                               
SITE     1 AC2  4 ASN A 171  ASP A 184  ANP A 400  HOH A 416                    
SITE     1 AC3  4 ASP A 184  HOH A 356  HOH A 372  ANP A 400                    
CRYST1   54.453   93.017  122.043  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018364  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010751  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008194        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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