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Database: PDB
Entry: 3FFK
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Original site: 3FFK 
HEADER    STRUCTURAL PROTEIN                      03-DEC-08   3FFK              
TITLE     CRYSTAL STRUCTURE OF HUMAN GELSOLIN DOMAINS G1-G3 BOUND TO ACTIN      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLASMA GELSOLIN;                                           
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 52-426;                                       
COMPND   5 SYNONYM: ACTIN-DEPOLYMERIZING FACTOR; ADF; BREVIN; AGEL;             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: ACTIN, ALPHA SKELETAL MUSCLE;                              
COMPND   9 CHAIN: B, E;                                                         
COMPND  10 SYNONYM: ALPHA-ACTIN-1                                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GSN;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)STAR;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PSY5;                                     
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;                          
SOURCE  13 ORGANISM_COMMON: RABBIT;                                             
SOURCE  14 ORGANISM_TAXID: 9986;                                                
SOURCE  15 ORGAN: MUSCLE;                                                       
SOURCE  16 OTHER_DETAILS: GENE NAME ACTA1, ACTA                                 
KEYWDS    GELSOLIN, ACTIN, CA-DEPENDENT, CA-ACTIVATED, CONTRACTILE PROTEIN,     
KEYWDS   2 STRUCTURAL PROTEIN                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.CHUMNARNSILPA,R.C.ROBINSON,L.D.BURTNICK                             
REVDAT   3   01-NOV-17 3FFK    1       REMARK                                   
REVDAT   2   13-JUL-11 3FFK    1       VERSN                                    
REVDAT   1   06-OCT-09 3FFK    0                                                
JRNL        AUTH   S.NAG,Q.MA,H.WANG,S.CHUMNARNSILPA,W.L.LEE,M.LARSSON,         
JRNL        AUTH 2 B.KANNAN,M.HERNANDEZ-VALLADARES,L.D.BURTNICK,R.C.ROBINSON    
JRNL        TITL   CA2+ BINDING BY DOMAIN 2 PLAYS A CRITICAL ROLE IN THE        
JRNL        TITL 2 ACTIVATION AND STABILIZATION OF GELSOLIN.                    
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 106 13713 2009              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   19666512                                                     
JRNL        DOI    10.1073/PNAS.0812374106                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 42953                          
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) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2264                            
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) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3119                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2730                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 149                          
REMARK   3   BIN FREE R VALUE                    : 0.3380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11084                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 72                                      
REMARK   3   SOLVENT ATOMS            : 473                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : 0.04000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.435         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.315         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.070        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.914                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.845                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11448 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15514 ; 1.263 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1419 ; 5.841 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   529 ;36.876 ;24.310       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1964 ;19.881 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    70 ;19.288 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1682 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8706 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4906 ; 0.228 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  7478 ; 0.315 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   366 ; 0.151 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    20 ; 0.149 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    43 ; 0.260 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.142 ; 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):  7037 ; 0.417 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11344 ; 0.797 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4411 ; 0.993 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4166 ; 1.778 ; 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 :   E    28        E   370                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.1759   7.0463 -33.2537              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0125 T22:   0.0384                                     
REMARK   3      T33:   0.0548 T12:  -0.0143                                     
REMARK   3      T13:  -0.0207 T23:   0.0431                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7505 L22:   1.3323                                     
REMARK   3      L33:   3.4778 L12:  -0.2915                                     
REMARK   3      L13:  -0.0592 L23:   0.9584                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0889 S12:   0.0737 S13:   0.1399                       
REMARK   3      S21:  -0.0123 S22:   0.1485 S23:   0.0976                       
REMARK   3      S31:  -0.0551 S32:   0.0095 S33:  -0.0596                       
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     6        B   365                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.6921  57.6859 -23.4847              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0061 T22:   0.0164                                     
REMARK   3      T33:   0.0243 T12:   0.0081                                     
REMARK   3      T13:  -0.0119 T23:  -0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3433 L22:   3.0017                                     
REMARK   3      L33:   1.2912 L12:   0.2902                                     
REMARK   3      L13:   0.2659 L23:   0.2565                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0428 S12:  -0.0621 S13:   0.1108                       
REMARK   3      S21:  -0.1028 S22:  -0.0572 S23:   0.2090                       
REMARK   3      S31:  -0.0615 S32:  -0.1406 S33:   0.1000                       
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 :   D    27        D   365                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.0502  -2.8921  -8.5955              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0522 T22:   0.0499                                     
REMARK   3      T33:   0.0281 T12:   0.0014                                     
REMARK   3      T13:  -0.0378 T23:   0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4006 L22:   0.6205                                     
REMARK   3      L33:   1.0373 L12:   0.3724                                     
REMARK   3      L13:  -0.4512 L23:   0.0659                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1297 S12:  -0.1947 S13:  -0.1042                       
REMARK   3      S21:   0.1386 S22:  -0.0599 S23:  -0.1127                       
REMARK   3      S31:   0.1184 S32:   0.1950 S33:  -0.0699                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   756        A   759                          
REMARK   3    RESIDUE RANGE :   B   380        B   401                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.6393  53.2530 -28.6235              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1014 T22:   0.0372                                     
REMARK   3      T33:   0.0616 T12:   0.0437                                     
REMARK   3      T13:  -0.0147 T23:   0.0262                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4553 L22:   0.6875                                     
REMARK   3      L33:   2.2652 L12:  -0.4552                                     
REMARK   3      L13:  -0.4395 L23:  -0.1425                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0483 S12:   0.0894 S13:   0.1237                       
REMARK   3      S21:   0.0551 S22:  -0.0895 S23:  -0.2020                       
REMARK   3      S31:  -0.4631 S32:  -0.1985 S33:   0.0412                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3FFK 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_1000050528.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 105                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSRRC                              
REMARK 200  BEAMLINE                       : BL13B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44802                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.998                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.5650                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 9% PEG 4000, 100 MM SODIUM ACETATE,      
REMARK 280  100 MM CALCIUM ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 297K                                                    
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       51.08950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.15050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       73.46150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.15050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       51.08950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       73.46150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
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    23                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     MET A    25                                                      
REMARK 465     VAL A    26                                                      
REMARK 465     VAL A    27                                                      
REMARK 465     THR A   375                                                      
REMARK 465     ASP A   376                                                      
REMARK 465     GLY A   377                                                      
REMARK 465     LEU A   378                                                      
REMARK 465     GLY A   379                                                      
REMARK 465     LEU A   380                                                      
REMARK 465     SER A   381                                                      
REMARK 465     TYR A   382                                                      
REMARK 465     LEU A   383                                                      
REMARK 465     SER A   384                                                      
REMARK 465     SER A   385                                                      
REMARK 465     HIS A   386                                                      
REMARK 465     ILE A   387                                                      
REMARK 465     ALA A   388                                                      
REMARK 465     ASN A   389                                                      
REMARK 465     VAL A   390                                                      
REMARK 465     GLU A   391                                                      
REMARK 465     ARG A   392                                                      
REMARK 465     VAL A   393                                                      
REMARK 465     PRO A   394                                                      
REMARK 465     PHE A   395                                                      
REMARK 465     ASP A   396                                                      
REMARK 465     ALA A   397                                                      
REMARK 465     ALA A   398                                                      
REMARK 465     THR A   399                                                      
REMARK 465     MET B    -1                                                      
REMARK 465     CYS B     0                                                      
REMARK 465     ASP B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     GLY B    48                                                      
REMARK 465     ILE B   369                                                      
REMARK 465     VAL B   370                                                      
REMARK 465     HIS B   371                                                      
REMARK 465     ARG B   372                                                      
REMARK 465     LYS B   373                                                      
REMARK 465     CYS B   374                                                      
REMARK 465     PHE B   375                                                      
REMARK 465     GLY D    23                                                      
REMARK 465     PRO D    24                                                      
REMARK 465     MET D    25                                                      
REMARK 465     VAL D    26                                                      
REMARK 465     ASP D   373                                                      
REMARK 465     GLN D   374                                                      
REMARK 465     THR D   375                                                      
REMARK 465     ASP D   376                                                      
REMARK 465     GLY D   377                                                      
REMARK 465     LEU D   378                                                      
REMARK 465     GLY D   379                                                      
REMARK 465     LEU D   380                                                      
REMARK 465     SER D   381                                                      
REMARK 465     TYR D   382                                                      
REMARK 465     LEU D   383                                                      
REMARK 465     SER D   384                                                      
REMARK 465     SER D   385                                                      
REMARK 465     HIS D   386                                                      
REMARK 465     ILE D   387                                                      
REMARK 465     ALA D   388                                                      
REMARK 465     ASN D   389                                                      
REMARK 465     VAL D   390                                                      
REMARK 465     GLU D   391                                                      
REMARK 465     ARG D   392                                                      
REMARK 465     VAL D   393                                                      
REMARK 465     PRO D   394                                                      
REMARK 465     PHE D   395                                                      
REMARK 465     ASP D   396                                                      
REMARK 465     ALA D   397                                                      
REMARK 465     ALA D   398                                                      
REMARK 465     THR D   399                                                      
REMARK 465     MET E    -1                                                      
REMARK 465     CYS E     0                                                      
REMARK 465     ASP E     1                                                      
REMARK 465     GLU E     2                                                      
REMARK 465     ASP E     3                                                      
REMARK 465     GLU E     4                                                      
REMARK 465     ARG E    39                                                      
REMARK 465     HIS E    40                                                      
REMARK 465     GLN E    41                                                      
REMARK 465     GLY E    42                                                      
REMARK 465     VAL E    43                                                      
REMARK 465     MET E    44                                                      
REMARK 465     VAL E    45                                                      
REMARK 465     GLY E    46                                                      
REMARK 465     MET E    47                                                      
REMARK 465     GLY E    48                                                      
REMARK 465     GLN E    49                                                      
REMARK 465     HIS E   371                                                      
REMARK 465     ARG E   372                                                      
REMARK 465     LYS E   373                                                      
REMARK 465     CYS E   374                                                      
REMARK 465     PHE E   375                                                      
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     ASP B   3    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LEU E    65     O    HOH E   478              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  48       63.47     36.73                                   
REMARK 500    LEU A 112       34.59    -89.01                                   
REMARK 500    PHE A 125       17.11   -146.03                                   
REMARK 500    SER A 147      152.41    -48.05                                   
REMARK 500    ASN A 185       11.25    -69.93                                   
REMARK 500    ASN A 223      -63.18    -94.64                                   
REMARK 500    SER A 226       28.88     48.95                                   
REMARK 500    ARG A 228       44.12    -74.46                                   
REMARK 500    ALA A 255     -143.93     58.24                                   
REMARK 500    MET A 283       99.12    -67.32                                   
REMARK 500    THR B   5      136.97    -38.38                                   
REMARK 500    ASP B  25      -49.02    -28.83                                   
REMARK 500    LYS B  50     -136.48     73.34                                   
REMARK 500    ALA B 181     -155.42   -149.23                                   
REMARK 500    VAL B 201      -52.10   -125.04                                   
REMARK 500    GLN B 246      144.85     91.41                                   
REMARK 500    PRO B 264       -6.32    -57.95                                   
REMARK 500    ASP B 286      127.20    -39.04                                   
REMARK 500    ASP B 363       15.06    -65.01                                   
REMARK 500    PRO B 367      -79.71      8.69                                   
REMARK 500    GLU D  28       90.45    -49.93                                   
REMARK 500    ASN D  78      -56.02     -6.68                                   
REMARK 500    LEU D 112       42.70    -96.37                                   
REMARK 500    ASN D 113       29.48     47.75                                   
REMARK 500    SER D 147      145.81    -39.16                                   
REMARK 500    ASN D 185        3.37    -67.58                                   
REMARK 500    ASN D 223      -67.17    -97.87                                   
REMARK 500    ARG D 228       36.19    -85.80                                   
REMARK 500    GLU D 235     -158.56   -144.86                                   
REMARK 500    THR D 257     -167.62     75.18                                   
REMARK 500    HIS D 309       57.44   -144.95                                   
REMARK 500    GLN D 347       15.11     83.14                                   
REMARK 500    ASP E  25      -32.94    -37.64                                   
REMARK 500    HIS E  73       35.50     38.51                                   
REMARK 500    GLU E  99       -1.42    -57.49                                   
REMARK 500    SER E 234       73.35   -119.16                                   
REMARK 500    PRO E 322       58.89    -69.06                                   
REMARK 500    SER E 323      -64.07     48.86                                   
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 PRO A  254     ALA A  255                  149.28                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 757  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A  65   O                                                      
REMARK 620 2 ASP A  66   OD2  73.0                                              
REMARK 620 3 GLU A  97   OE1  86.9 119.2                                        
REMARK 620 4 GLU A  97   OE2 101.6  78.3  50.0                                  
REMARK 620 5 VAL A 145   O   159.6  95.0 113.5  91.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 758  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 109   OD2                                                    
REMARK 620 2 GLY A 114   O   105.7                                              
REMARK 620 3 ALA A 116   O    87.7 102.3                                        
REMARK 620 4 GLU B 167   OE1 100.5 153.1  72.8                                  
REMARK 620 5 HOH A 853   O    72.9  93.0 158.1 100.2                            
REMARK 620 6 HOH A 882   O   153.9  68.7  69.5  85.1 131.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 756  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 186   O                                                      
REMARK 620 2 ASP A 187   OD2  80.0                                              
REMARK 620 3 GLU A 209   OE1  92.0 107.5                                        
REMARK 620 4 GLU A 209   OE2 125.2  77.1  50.6                                  
REMARK 620 5 ASP A 259   OD1 160.4 115.8  93.8  71.9                            
REMARK 620 6 HOH A 883   O    82.7 160.0  83.1 121.7  79.4                      
REMARK 620 7 HOH A 789   O    96.2  87.0 164.5 130.9  74.4  84.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 759  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 302   O                                                      
REMARK 620 2 ASP A 303   OD1  68.1                                              
REMARK 620 3 GLU A 327   OE1  82.2  98.8                                        
REMARK 620 4 GLU A 327   OE2 115.3  75.2  53.0                                  
REMARK 620 5 HOH A 802   O    99.6  73.5 170.5 118.6                            
REMARK 620 6 HOH A 777   O    80.0 147.9  78.9 123.6 110.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 757  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY D  65   O                                                      
REMARK 620 2 ASP D  66   OD2  70.4                                              
REMARK 620 3 GLU D  97   OE1  82.4  94.2                                        
REMARK 620 4 VAL D 145   O   140.5  81.4 127.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 758  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 109   OD2                                                    
REMARK 620 2 GLY D 114   O   105.9                                              
REMARK 620 3 ALA D 116   O    67.3  98.4                                        
REMARK 620 4 GLU E 167   OE1  77.9 175.8  84.4                                  
REMARK 620 5 HOH D 833   O   103.1  82.3 170.2  95.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 756  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY D 186   O                                                      
REMARK 620 2 ASP D 187   OD2  76.7                                              
REMARK 620 3 GLU D 209   OE1  89.2 106.8                                        
REMARK 620 4 GLU D 209   OE2 122.3  75.7  53.1                                  
REMARK 620 5 ASP D 259   OD1 157.0 122.6  95.9  77.7                            
REMARK 620 6 HOH D 852   O    95.0 169.4  79.4 114.6  64.2                      
REMARK 620 7 HOH D 784   O    76.4  62.7 163.6 129.2 100.4 109.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 759  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 302   O                                                      
REMARK 620 2 ASP D 303   OD1  73.9                                              
REMARK 620 3 GLU D 327   OE1  77.1  96.2                                        
REMARK 620 4 GLU D 327   OE2 121.9  85.3  51.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP B 380   O2B                                                    
REMARK 620 2 ATP B 380   O3G  78.8                                              
REMARK 620 3 HOH B 398   O    99.6 146.8                                        
REMARK 620 4 HOH B 470   O    78.6 141.3  68.3                                  
REMARK 620 5 HOH B 392   O    93.4  81.9 131.2  68.7                            
REMARK 620 6 HOH B 469   O   163.0 108.5  82.8  86.8  73.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP E 380   O3G                                                    
REMARK 620 2 ATP E 380   O2B  73.6                                              
REMARK 620 3 HOH E 395   O   125.0  75.8                                        
REMARK 620 4 HOH E 490   O    67.3  85.3  65.6                                  
REMARK 620 5 HOH E 433   O   102.3 155.8  88.2  71.5                            
REMARK 620 6 HOH E 441   O   157.4  99.2  71.7 134.4  92.7                      
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 CA A 756                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 757                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 758                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 759                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 380                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 756                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 757                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 758                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 759                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP E 380                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1D0N   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF CALCIUM-FREE EQUINE PLASMA GELSOLIN         
REMARK 900 RELATED ID: 1H1V   RELATED DB: PDB                                   
REMARK 900 GELSOLIN G4-G6/ACTIN COMPLEX                                         
REMARK 900 RELATED ID: 1P8X   RELATED DB: PDB                                   
REMARK 900 THE CALCIUM-ACTIVATED C-TERMINAL HALF OF GELSOLIN                    
REMARK 900 RELATED ID: 1P8Z   RELATED DB: PDB                                   
REMARK 900 COMPLEX BETWEEN RABBIT MUSCLE -ACTIN: HUMAN GELSOLIN RESIDUES VAL26- 
REMARK 900 GLU156                                                               
REMARK 900 RELATED ID: 1RGI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF EQUINE GELSOLIN DOMAINS G1-G3 BOUND TO ACTIN    
REMARK 900 RELATED ID: 2FGH   RELATED DB: PDB                                   
REMARK 900 ATP BOUND GELSOLIN                                                   
REMARK 900 RELATED ID: 3FFK   RELATED DB: PDB                                   
DBREF  3FFK A   25   399  UNP    P06396   GELS_HUMAN      52    426             
DBREF  3FFK B   -1   375  UNP    P68135   ACTS_RABIT       1    377             
DBREF  3FFK D   25   399  UNP    P06396   GELS_HUMAN      52    426             
DBREF  3FFK E   -1   375  UNP    P68135   ACTS_RABIT       1    377             
SEQADV 3FFK GLY A   23  UNP  P06396              EXPRESSION TAG                 
SEQADV 3FFK PRO A   24  UNP  P06396              EXPRESSION TAG                 
SEQADV 3FFK GLY D   23  UNP  P06396              EXPRESSION TAG                 
SEQADV 3FFK PRO D   24  UNP  P06396              EXPRESSION TAG                 
SEQRES   1 A  377  GLY PRO MET VAL VAL GLU HIS PRO GLU PHE LEU LYS ALA          
SEQRES   2 A  377  GLY LYS GLU PRO GLY LEU GLN ILE TRP ARG VAL GLU LYS          
SEQRES   3 A  377  PHE ASP LEU VAL PRO VAL PRO THR ASN LEU TYR GLY ASP          
SEQRES   4 A  377  PHE PHE THR GLY ASP ALA TYR VAL ILE LEU LYS THR VAL          
SEQRES   5 A  377  GLN LEU ARG ASN GLY ASN LEU GLN TYR ASP LEU HIS TYR          
SEQRES   6 A  377  TRP LEU GLY ASN GLU CYS SER GLN ASP GLU SER GLY ALA          
SEQRES   7 A  377  ALA ALA ILE PHE THR VAL GLN LEU ASP ASP TYR LEU ASN          
SEQRES   8 A  377  GLY ARG ALA VAL GLN HIS ARG GLU VAL GLN GLY PHE GLU          
SEQRES   9 A  377  SER ALA THR PHE LEU GLY TYR PHE LYS SER GLY LEU LYS          
SEQRES  10 A  377  TYR LYS LYS GLY GLY VAL ALA SER GLY PHE LYS HIS VAL          
SEQRES  11 A  377  VAL PRO ASN GLU VAL VAL VAL GLN ARG LEU PHE GLN VAL          
SEQRES  12 A  377  LYS GLY ARG ARG VAL VAL ARG ALA THR GLU VAL PRO VAL          
SEQRES  13 A  377  SER TRP GLU SER PHE ASN ASN GLY ASP CYS PHE ILE LEU          
SEQRES  14 A  377  ASP LEU GLY ASN ASN ILE HIS GLN TRP CYS GLY SER ASN          
SEQRES  15 A  377  SER ASN ARG TYR GLU ARG LEU LYS ALA THR GLN VAL SER          
SEQRES  16 A  377  LYS GLY ILE ARG ASP ASN GLU ARG SER GLY ARG ALA ARG          
SEQRES  17 A  377  VAL HIS VAL SER GLU GLU GLY THR GLU PRO GLU ALA MET          
SEQRES  18 A  377  LEU GLN VAL LEU GLY PRO LYS PRO ALA LEU PRO ALA GLY          
SEQRES  19 A  377  THR GLU ASP THR ALA LYS GLU ASP ALA ALA ASN ARG LYS          
SEQRES  20 A  377  LEU ALA LYS LEU TYR LYS VAL SER ASN GLY ALA GLY THR          
SEQRES  21 A  377  MET SER VAL SER LEU VAL ALA ASP GLU ASN PRO PHE ALA          
SEQRES  22 A  377  GLN GLY ALA LEU LYS SER GLU ASP CYS PHE ILE LEU ASP          
SEQRES  23 A  377  HIS GLY LYS ASP GLY LYS ILE PHE VAL TRP LYS GLY LYS          
SEQRES  24 A  377  GLN ALA ASN THR GLU GLU ARG LYS ALA ALA LEU LYS THR          
SEQRES  25 A  377  ALA SER ASP PHE ILE THR LYS MET ASP TYR PRO LYS GLN          
SEQRES  26 A  377  THR GLN VAL SER VAL LEU PRO GLU GLY GLY GLU THR PRO          
SEQRES  27 A  377  LEU PHE LYS GLN PHE PHE LYS ASN TRP ARG ASP PRO ASP          
SEQRES  28 A  377  GLN THR ASP GLY LEU GLY LEU SER TYR LEU SER SER HIS          
SEQRES  29 A  377  ILE ALA ASN VAL GLU ARG VAL PRO PHE ASP ALA ALA THR          
SEQRES   1 B  377  MET CYS ASP GLU ASP GLU THR THR ALA LEU VAL CYS ASP          
SEQRES   2 B  377  ASN GLY SER GLY LEU VAL LYS ALA GLY PHE ALA GLY ASP          
SEQRES   3 B  377  ASP ALA PRO ARG ALA VAL PHE PRO SER ILE VAL GLY ARG          
SEQRES   4 B  377  PRO ARG HIS GLN GLY VAL MET VAL GLY MET GLY GLN LYS          
SEQRES   5 B  377  ASP SER TYR VAL GLY ASP GLU ALA GLN SER LYS ARG GLY          
SEQRES   6 B  377  ILE LEU THR LEU LYS TYR PRO ILE GLU HIS GLY ILE ILE          
SEQRES   7 B  377  THR ASN TRP ASP ASP MET GLU LYS ILE TRP HIS HIS THR          
SEQRES   8 B  377  PHE TYR ASN GLU LEU ARG VAL ALA PRO GLU GLU HIS PRO          
SEQRES   9 B  377  THR LEU LEU THR GLU ALA PRO LEU ASN PRO LYS ALA ASN          
SEQRES  10 B  377  ARG GLU LYS MET THR GLN ILE MET PHE GLU THR PHE ASN          
SEQRES  11 B  377  VAL PRO ALA MET TYR VAL ALA ILE GLN ALA VAL LEU SER          
SEQRES  12 B  377  LEU TYR ALA SER GLY ARG THR THR GLY ILE VAL LEU ASP          
SEQRES  13 B  377  SER GLY ASP GLY VAL THR HIS ASN VAL PRO ILE TYR GLU          
SEQRES  14 B  377  GLY TYR ALA LEU PRO HIS ALA ILE MET ARG LEU ASP LEU          
SEQRES  15 B  377  ALA GLY ARG ASP LEU THR ASP TYR LEU MET LYS ILE LEU          
SEQRES  16 B  377  THR GLU ARG GLY TYR SER PHE VAL THR THR ALA GLU ARG          
SEQRES  17 B  377  GLU ILE VAL ARG ASP ILE LYS GLU LYS LEU CYS TYR VAL          
SEQRES  18 B  377  ALA LEU ASP PHE GLU ASN GLU MET ALA THR ALA ALA SER          
SEQRES  19 B  377  SER SER SER LEU GLU LYS SER TYR GLU LEU PRO ASP GLY          
SEQRES  20 B  377  GLN VAL ILE THR ILE GLY ASN GLU ARG PHE ARG CYS PRO          
SEQRES  21 B  377  GLU THR LEU PHE GLN PRO SER PHE ILE GLY MET GLU SER          
SEQRES  22 B  377  ALA GLY ILE HIS GLU THR THR TYR ASN SER ILE MET LYS          
SEQRES  23 B  377  CYS ASP ILE ASP ILE ARG LYS ASP LEU TYR ALA ASN ASN          
SEQRES  24 B  377  VAL MET SER GLY GLY THR THR MET TYR PRO GLY ILE ALA          
SEQRES  25 B  377  ASP ARG MET GLN LYS GLU ILE THR ALA LEU ALA PRO SER          
SEQRES  26 B  377  THR MET LYS ILE LYS ILE ILE ALA PRO PRO GLU ARG LYS          
SEQRES  27 B  377  TYR SER VAL TRP ILE GLY GLY SER ILE LEU ALA SER LEU          
SEQRES  28 B  377  SER THR PHE GLN GLN MET TRP ILE THR LYS GLN GLU TYR          
SEQRES  29 B  377  ASP GLU ALA GLY PRO SER ILE VAL HIS ARG LYS CYS PHE          
SEQRES   1 D  377  GLY PRO MET VAL VAL GLU HIS PRO GLU PHE LEU LYS ALA          
SEQRES   2 D  377  GLY LYS GLU PRO GLY LEU GLN ILE TRP ARG VAL GLU LYS          
SEQRES   3 D  377  PHE ASP LEU VAL PRO VAL PRO THR ASN LEU TYR GLY ASP          
SEQRES   4 D  377  PHE PHE THR GLY ASP ALA TYR VAL ILE LEU LYS THR VAL          
SEQRES   5 D  377  GLN LEU ARG ASN GLY ASN LEU GLN TYR ASP LEU HIS TYR          
SEQRES   6 D  377  TRP LEU GLY ASN GLU CYS SER GLN ASP GLU SER GLY ALA          
SEQRES   7 D  377  ALA ALA ILE PHE THR VAL GLN LEU ASP ASP TYR LEU ASN          
SEQRES   8 D  377  GLY ARG ALA VAL GLN HIS ARG GLU VAL GLN GLY PHE GLU          
SEQRES   9 D  377  SER ALA THR PHE LEU GLY TYR PHE LYS SER GLY LEU LYS          
SEQRES  10 D  377  TYR LYS LYS GLY GLY VAL ALA SER GLY PHE LYS HIS VAL          
SEQRES  11 D  377  VAL PRO ASN GLU VAL VAL VAL GLN ARG LEU PHE GLN VAL          
SEQRES  12 D  377  LYS GLY ARG ARG VAL VAL ARG ALA THR GLU VAL PRO VAL          
SEQRES  13 D  377  SER TRP GLU SER PHE ASN ASN GLY ASP CYS PHE ILE LEU          
SEQRES  14 D  377  ASP LEU GLY ASN ASN ILE HIS GLN TRP CYS GLY SER ASN          
SEQRES  15 D  377  SER ASN ARG TYR GLU ARG LEU LYS ALA THR GLN VAL SER          
SEQRES  16 D  377  LYS GLY ILE ARG ASP ASN GLU ARG SER GLY ARG ALA ARG          
SEQRES  17 D  377  VAL HIS VAL SER GLU GLU GLY THR GLU PRO GLU ALA MET          
SEQRES  18 D  377  LEU GLN VAL LEU GLY PRO LYS PRO ALA LEU PRO ALA GLY          
SEQRES  19 D  377  THR GLU ASP THR ALA LYS GLU ASP ALA ALA ASN ARG LYS          
SEQRES  20 D  377  LEU ALA LYS LEU TYR LYS VAL SER ASN GLY ALA GLY THR          
SEQRES  21 D  377  MET SER VAL SER LEU VAL ALA ASP GLU ASN PRO PHE ALA          
SEQRES  22 D  377  GLN GLY ALA LEU LYS SER GLU ASP CYS PHE ILE LEU ASP          
SEQRES  23 D  377  HIS GLY LYS ASP GLY LYS ILE PHE VAL TRP LYS GLY LYS          
SEQRES  24 D  377  GLN ALA ASN THR GLU GLU ARG LYS ALA ALA LEU LYS THR          
SEQRES  25 D  377  ALA SER ASP PHE ILE THR LYS MET ASP TYR PRO LYS GLN          
SEQRES  26 D  377  THR GLN VAL SER VAL LEU PRO GLU GLY GLY GLU THR PRO          
SEQRES  27 D  377  LEU PHE LYS GLN PHE PHE LYS ASN TRP ARG ASP PRO ASP          
SEQRES  28 D  377  GLN THR ASP GLY LEU GLY LEU SER TYR LEU SER SER HIS          
SEQRES  29 D  377  ILE ALA ASN VAL GLU ARG VAL PRO PHE ASP ALA ALA THR          
SEQRES   1 E  377  MET CYS ASP GLU ASP GLU THR THR ALA LEU VAL CYS ASP          
SEQRES   2 E  377  ASN GLY SER GLY LEU VAL LYS ALA GLY PHE ALA GLY ASP          
SEQRES   3 E  377  ASP ALA PRO ARG ALA VAL PHE PRO SER ILE VAL GLY ARG          
SEQRES   4 E  377  PRO ARG HIS GLN GLY VAL MET VAL GLY MET GLY GLN LYS          
SEQRES   5 E  377  ASP SER TYR VAL GLY ASP GLU ALA GLN SER LYS ARG GLY          
SEQRES   6 E  377  ILE LEU THR LEU LYS TYR PRO ILE GLU HIS GLY ILE ILE          
SEQRES   7 E  377  THR ASN TRP ASP ASP MET GLU LYS ILE TRP HIS HIS THR          
SEQRES   8 E  377  PHE TYR ASN GLU LEU ARG VAL ALA PRO GLU GLU HIS PRO          
SEQRES   9 E  377  THR LEU LEU THR GLU ALA PRO LEU ASN PRO LYS ALA ASN          
SEQRES  10 E  377  ARG GLU LYS MET THR GLN ILE MET PHE GLU THR PHE ASN          
SEQRES  11 E  377  VAL PRO ALA MET TYR VAL ALA ILE GLN ALA VAL LEU SER          
SEQRES  12 E  377  LEU TYR ALA SER GLY ARG THR THR GLY ILE VAL LEU ASP          
SEQRES  13 E  377  SER GLY ASP GLY VAL THR HIS ASN VAL PRO ILE TYR GLU          
SEQRES  14 E  377  GLY TYR ALA LEU PRO HIS ALA ILE MET ARG LEU ASP LEU          
SEQRES  15 E  377  ALA GLY ARG ASP LEU THR ASP TYR LEU MET LYS ILE LEU          
SEQRES  16 E  377  THR GLU ARG GLY TYR SER PHE VAL THR THR ALA GLU ARG          
SEQRES  17 E  377  GLU ILE VAL ARG ASP ILE LYS GLU LYS LEU CYS TYR VAL          
SEQRES  18 E  377  ALA LEU ASP PHE GLU ASN GLU MET ALA THR ALA ALA SER          
SEQRES  19 E  377  SER SER SER LEU GLU LYS SER TYR GLU LEU PRO ASP GLY          
SEQRES  20 E  377  GLN VAL ILE THR ILE GLY ASN GLU ARG PHE ARG CYS PRO          
SEQRES  21 E  377  GLU THR LEU PHE GLN PRO SER PHE ILE GLY MET GLU SER          
SEQRES  22 E  377  ALA GLY ILE HIS GLU THR THR TYR ASN SER ILE MET LYS          
SEQRES  23 E  377  CYS ASP ILE ASP ILE ARG LYS ASP LEU TYR ALA ASN ASN          
SEQRES  24 E  377  VAL MET SER GLY GLY THR THR MET TYR PRO GLY ILE ALA          
SEQRES  25 E  377  ASP ARG MET GLN LYS GLU ILE THR ALA LEU ALA PRO SER          
SEQRES  26 E  377  THR MET LYS ILE LYS ILE ILE ALA PRO PRO GLU ARG LYS          
SEQRES  27 E  377  TYR SER VAL TRP ILE GLY GLY SER ILE LEU ALA SER LEU          
SEQRES  28 E  377  SER THR PHE GLN GLN MET TRP ILE THR LYS GLN GLU TYR          
SEQRES  29 E  377  ASP GLU ALA GLY PRO SER ILE VAL HIS ARG LYS CYS PHE          
HET     CA  A 756       1                                                       
HET     CA  A 757       1                                                       
HET     CA  A 758       1                                                       
HET     CA  A 759       1                                                       
HET     CA  B 401       1                                                       
HET    ATP  B 380      31                                                       
HET     CA  D 756       1                                                       
HET     CA  D 757       1                                                       
HET     CA  D 758       1                                                       
HET     CA  D 759       1                                                       
HET     CA  E 401       1                                                       
HET    ATP  E 380      31                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   5   CA    10(CA 2+)                                                    
FORMUL  10  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL  17  HOH   *473(H2 O)                                                    
HELIX    1   1 HIS A   29  LYS A   34  1                                   6    
HELIX    2   2 PRO A   55  TYR A   59  5                                   5    
HELIX    3   3 SER A   94  LEU A  112  1                                  19    
HELIX    4   4 SER A  127  GLY A  132  1                                   6    
HELIX    5   5 SER A  179  PHE A  183  5                                   5    
HELIX    6   6 ASN A  206  ASN A  223  1                                  18    
HELIX    7   7 PRO A  240  GLY A  248  1                                   9    
HELIX    8   8 THR A  260  ARG A  268  1                                   9    
HELIX    9   9 ALA A  295  LEU A  299  5                                   5    
HELIX   10  10 GLY A  310  ASP A  312  5                                   3    
HELIX   11  11 ASN A  324  MET A  342  1                                  19    
HELIX   12  12 THR A  359  GLN A  364  1                                   6    
HELIX   13  13 GLY B   55  ARG B   62  1                                   8    
HELIX   14  14 ASN B   78  ASN B   92  1                                  15    
HELIX   15  15 ALA B   97  HIS B  101  5                                   5    
HELIX   16  16 PRO B  112  THR B  126  1                                  15    
HELIX   17  17 GLN B  137  SER B  145  1                                   9    
HELIX   18  18 PRO B  172  ILE B  175  5                                   4    
HELIX   19  19 ALA B  181  GLY B  197  1                                  17    
HELIX   20  20 ALA B  204  CYS B  217  1                                  14    
HELIX   21  21 ASP B  222  ALA B  231  1                                  10    
HELIX   22  22 ASN B  252  THR B  260  1                                   9    
HELIX   23  23 LEU B  261  PHE B  262  5                                   2    
HELIX   24  24 GLN B  263  GLY B  268  5                                   6    
HELIX   25  25 GLY B  273  LYS B  284  1                                  12    
HELIX   26  26 CYS B  285  ASP B  288  5                                   4    
HELIX   27  27 ILE B  289  ALA B  295  1                                   7    
HELIX   28  28 GLY B  301  TYR B  306  5                                   6    
HELIX   29  29 GLY B  308  ALA B  321  1                                  14    
HELIX   30  30 GLU B  334  LYS B  336  5                                   3    
HELIX   31  31 TYR B  337  LEU B  349  1                                  13    
HELIX   32  32 SER B  350  TRP B  356  5                                   7    
HELIX   33  33 LYS B  359  ASP B  363  1                                   5    
HELIX   34  34 PRO D   55  TYR D   59  5                                   5    
HELIX   35  35 SER D   94  LEU D  112  1                                  19    
HELIX   36  36 SER D  127  GLY D  132  1                                   6    
HELIX   37  37 SER D  179  PHE D  183  5                                   5    
HELIX   38  38 ASN D  206  ASN D  223  1                                  18    
HELIX   39  39 PRO D  240  GLY D  248  1                                   9    
HELIX   40  40 THR D  260  ARG D  268  1                                   9    
HELIX   41  41 ALA D  295  LEU D  299  5                                   5    
HELIX   42  42 ASN D  324  MET D  342  1                                  19    
HELIX   43  43 THR D  359  GLN D  364  1                                   6    
HELIX   44  44 GLY E   55  LYS E   61  1                                   7    
HELIX   45  45 ARG E   62  LEU E   65  5                                   4    
HELIX   46  46 ASN E   78  ASN E   92  1                                  15    
HELIX   47  47 ALA E   97  HIS E  101  5                                   5    
HELIX   48  48 PRO E  112  THR E  126  1                                  15    
HELIX   49  49 GLN E  137  SER E  145  1                                   9    
HELIX   50  50 PRO E  172  ILE E  175  5                                   4    
HELIX   51  51 ALA E  181  GLU E  195  1                                  15    
HELIX   52  52 THR E  202  CYS E  217  1                                  16    
HELIX   53  53 ASP E  222  SER E  233  1                                  12    
HELIX   54  54 ASN E  252  THR E  260  1                                   9    
HELIX   55  55 LEU E  261  PHE E  262  5                                   2    
HELIX   56  56 GLN E  263  GLY E  268  5                                   6    
HELIX   57  57 GLY E  273  LYS E  284  1                                  12    
HELIX   58  58 CYS E  285  ASP E  288  5                                   4    
HELIX   59  59 ILE E  289  ALA E  295  1                                   7    
HELIX   60  60 GLY E  301  MET E  305  5                                   5    
HELIX   61  61 GLY E  308  ALA E  321  1                                  14    
HELIX   62  62 TYR E  337  LEU E  349  1                                  13    
HELIX   63  63 SER E  350  MET E  355  5                                   6    
HELIX   64  64 LYS E  359  GLY E  366  1                                   8    
SHEET    1   A 5 ASP A  50  PRO A  53  0                                        
SHEET    2   A 5 GLY A  40  GLU A  47 -1  N  ARG A  45   O  VAL A  52           
SHEET    3   A 5 ALA A  67  GLN A  75 -1  O  VAL A  69   N  TRP A  44           
SHEET    4   A 5 LEU A  81  LEU A  89 -1  O  HIS A  86   N  ILE A  70           
SHEET    5   A 5 ALA A 116  VAL A 122  1  O  HIS A 119   N  LEU A  85           
SHEET    1   B 2 ASP A  61  PHE A  63  0                                        
SHEET    2   B 2 LYS A 139  LYS A 141  1  O  LYS A 139   N  PHE A  62           
SHEET    1   C 5 ARG A 172  VAL A 176  0                                        
SHEET    2   C 5 ARG A 161  LYS A 166 -1  N  GLN A 164   O  THR A 174           
SHEET    3   C 5 CYS A 188  ASP A 192 -1  O  CYS A 188   N  VAL A 165           
SHEET    4   C 5 ASN A 196  CYS A 201 -1  O  TRP A 200   N  PHE A 189           
SHEET    5   C 5 ARG A 230  SER A 234  1  O  HIS A 232   N  ILE A 197           
SHEET    1   D 5 SER A 284  ALA A 289  0                                        
SHEET    2   D 5 LYS A 272  SER A 277 -1  N  SER A 277   O  SER A 284           
SHEET    3   D 5 CYS A 304  HIS A 309 -1  O  ILE A 306   N  TYR A 274           
SHEET    4   D 5 LYS A 314  LYS A 319 -1  O  TRP A 318   N  PHE A 305           
SHEET    5   D 5 GLN A 349  PRO A 354  1  O  LEU A 353   N  VAL A 317           
SHEET    1   E 6 ALA B  29  PRO B  32  0                                        
SHEET    2   E 6 LEU B  16  PHE B  21 -1  N  VAL B  17   O  PHE B  31           
SHEET    3   E 6 LEU B   8  ASN B  12 -1  N  ASP B  11   O  LYS B  18           
SHEET    4   E 6 THR B 103  GLU B 107  1  O  LEU B 104   N  LEU B   8           
SHEET    5   E 6 ALA B 131  ILE B 136  1  O  ALA B 135   N  LEU B 105           
SHEET    6   E 6 ILE B 357  THR B 358 -1  O  ILE B 357   N  MET B 132           
SHEET    1   F 3 TYR B  53  VAL B  54  0                                        
SHEET    2   F 3 VAL B  35  PRO B  38 -1  N  GLY B  36   O  TYR B  53           
SHEET    3   F 3 LEU B  65  LYS B  68 -1  O  THR B  66   N  ARG B  37           
SHEET    1   G 2 ILE B  71  GLU B  72  0                                        
SHEET    2   G 2 ILE B  75  ILE B  76 -1  O  ILE B  75   N  GLU B  72           
SHEET    1   H 3 TYR B 169  ALA B 170  0                                        
SHEET    2   H 3 THR B 160  TYR B 166 -1  N  TYR B 166   O  TYR B 169           
SHEET    3   H 3 MET B 176  LEU B 178 -1  O  LEU B 178   N  THR B 160           
SHEET    1   I 5 TYR B 169  ALA B 170  0                                        
SHEET    2   I 5 THR B 160  TYR B 166 -1  N  TYR B 166   O  TYR B 169           
SHEET    3   I 5 GLY B 150  SER B 155 -1  N  GLY B 150   O  ILE B 165           
SHEET    4   I 5 ASN B 297  SER B 300  1  O  SER B 300   N  LEU B 153           
SHEET    5   I 5 ILE B 329  ILE B 330  1  O  ILE B 330   N  ASN B 297           
SHEET    1   J 2 LYS B 238  GLU B 241  0                                        
SHEET    2   J 2 VAL B 247  ILE B 250 -1  O  ILE B 250   N  LYS B 238           
SHEET    1   K 5 ASP D  50  PRO D  53  0                                        
SHEET    2   K 5 GLY D  40  GLU D  47 -1  N  ARG D  45   O  VAL D  52           
SHEET    3   K 5 ALA D  67  GLN D  75 -1  O  VAL D  69   N  TRP D  44           
SHEET    4   K 5 LEU D  81  LEU D  89 -1  O  HIS D  86   N  ILE D  70           
SHEET    5   K 5 ALA D 116  VAL D 122  1  O  GLU D 121   N  LEU D  89           
SHEET    1   L 2 ASP D  61  PHE D  63  0                                        
SHEET    2   L 2 LYS D 139  LYS D 141  1  O  LYS D 141   N  PHE D  62           
SHEET    1   M 5 ARG D 172  VAL D 176  0                                        
SHEET    2   M 5 ARG D 161  LYS D 166 -1  N  GLN D 164   O  THR D 174           
SHEET    3   M 5 CYS D 188  ASP D 192 -1  O  CYS D 188   N  VAL D 165           
SHEET    4   M 5 ASN D 196  CYS D 201 -1  O  TRP D 200   N  PHE D 189           
SHEET    5   M 5 ARG D 230  SER D 234  1  O  HIS D 232   N  ILE D 197           
SHEET    1   N 5 SER D 284  ALA D 289  0                                        
SHEET    2   N 5 LYS D 272  SER D 277 -1  N  LYS D 275   O  SER D 286           
SHEET    3   N 5 CYS D 304  HIS D 309 -1  O  CYS D 304   N  VAL D 276           
SHEET    4   N 5 LYS D 314  LYS D 319 -1  O  TRP D 318   N  PHE D 305           
SHEET    5   N 5 GLN D 349  PRO D 354  1  O  LEU D 353   N  VAL D 317           
SHEET    1   O 6 ALA E  29  PRO E  32  0                                        
SHEET    2   O 6 LEU E  16  PHE E  21 -1  N  VAL E  17   O  PHE E  31           
SHEET    3   O 6 LEU E   8  ASN E  12 -1  N  ASP E  11   O  LYS E  18           
SHEET    4   O 6 THR E 103  GLU E 107  1  O  LEU E 104   N  LEU E   8           
SHEET    5   O 6 ALA E 131  ILE E 136  1  O  TYR E 133   N  LEU E 105           
SHEET    6   O 6 ILE E 357  THR E 358 -1  O  ILE E 357   N  MET E 132           
SHEET    1   P 3 TYR E  53  VAL E  54  0                                        
SHEET    2   P 3 VAL E  35  ARG E  37 -1  N  GLY E  36   O  TYR E  53           
SHEET    3   P 3 THR E  66  LYS E  68 -1  O  THR E  66   N  ARG E  37           
SHEET    1   Q 2 ILE E  71  GLU E  72  0                                        
SHEET    2   Q 2 ILE E  75  ILE E  76 -1  O  ILE E  75   N  GLU E  72           
SHEET    1   R 3 TYR E 169  ALA E 170  0                                        
SHEET    2   R 3 THR E 160  TYR E 166 -1  N  TYR E 166   O  TYR E 169           
SHEET    3   R 3 MET E 176  LEU E 178 -1  O  LEU E 178   N  THR E 160           
SHEET    1   S 5 TYR E 169  ALA E 170  0                                        
SHEET    2   S 5 THR E 160  TYR E 166 -1  N  TYR E 166   O  TYR E 169           
SHEET    3   S 5 GLY E 150  SER E 155 -1  N  GLY E 150   O  ILE E 165           
SHEET    4   S 5 ASN E 297  SER E 300  1  O  SER E 300   N  LEU E 153           
SHEET    5   S 5 ILE E 329  ILE E 330  1  O  ILE E 330   N  ASN E 297           
SHEET    1   T 2 LYS E 238  GLU E 241  0                                        
SHEET    2   T 2 VAL E 247  ILE E 250 -1  O  ILE E 250   N  LYS E 238           
SSBOND   1 CYS A  188    CYS A  201                          1555   1555  2.05  
SSBOND   2 CYS D  188    CYS D  201                          1555   1555  2.84  
LINK         O   GLY A  65                CA    CA A 757     1555   1555  2.36  
LINK         OD2 ASP A  66                CA    CA A 757     1555   1555  2.31  
LINK         OE1 GLU A  97                CA    CA A 757     1555   1555  2.36  
LINK         OE2 GLU A  97                CA    CA A 757     1555   1555  2.76  
LINK         OD2 ASP A 109                CA    CA A 758     1555   1555  2.56  
LINK         O   GLY A 114                CA    CA A 758     1555   1555  2.66  
LINK         O   ALA A 116                CA    CA A 758     1555   1555  2.67  
LINK         O   VAL A 145                CA    CA A 757     1555   1555  2.43  
LINK         O   GLY A 186                CA    CA A 756     1555   1555  2.15  
LINK         OD2 ASP A 187                CA    CA A 756     1555   1555  2.29  
LINK         OE1 GLU A 209                CA    CA A 756     1555   1555  2.30  
LINK         OE2 GLU A 209                CA    CA A 756     1555   1555  2.71  
LINK         OD1 ASP A 259                CA    CA A 756     1555   1555  2.74  
LINK         O   GLU A 302                CA    CA A 759     1555   1555  2.31  
LINK         OD1 ASP A 303                CA    CA A 759     1555   1555  2.59  
LINK         OE1 GLU A 327                CA    CA A 759     1555   1555  2.60  
LINK         OE2 GLU A 327                CA    CA A 759     1555   1555  2.25  
LINK         OE1 GLU B 167                CA    CA A 758     1555   1555  2.42  
LINK         O   GLY D  65                CA    CA D 757     1555   1555  2.36  
LINK         OD2 ASP D  66                CA    CA D 757     1555   1555  2.59  
LINK         OE1 GLU D  97                CA    CA D 757     1555   1555  2.25  
LINK         OD2 ASP D 109                CA    CA D 758     1555   1555  2.54  
LINK         O   GLY D 114                CA    CA D 758     1555   1555  2.40  
LINK         O   ALA D 116                CA    CA D 758     1555   1555  2.56  
LINK         O   VAL D 145                CA    CA D 757     1555   1555  2.18  
LINK         O   GLY D 186                CA    CA D 756     1555   1555  2.17  
LINK         OD2 ASP D 187                CA    CA D 756     1555   1555  2.47  
LINK         OE1 GLU D 209                CA    CA D 756     1555   1555  2.56  
LINK         OE2 GLU D 209                CA    CA D 756     1555   1555  2.33  
LINK         OD1 ASP D 259                CA    CA D 756     1555   1555  2.46  
LINK         O   GLU D 302                CA    CA D 759     1555   1555  2.48  
LINK         OD1 ASP D 303                CA    CA D 759     1555   1555  2.60  
LINK         OE1 GLU D 327                CA    CA D 759     1555   1555  2.57  
LINK         OE2 GLU D 327                CA    CA D 759     1555   1555  2.47  
LINK         OE1 GLU E 167                CA    CA D 758     1555   1555  2.30  
LINK        CA    CA B 401                 O2B ATP B 380     1555   1555  2.12  
LINK        CA    CA B 401                 O3G ATP B 380     1555   1555  2.16  
LINK        CA    CA E 401                 O3G ATP E 380     1555   1555  2.47  
LINK        CA    CA E 401                 O2B ATP E 380     1555   1555  2.27  
LINK        CA    CA A 756                 O   HOH A 883     1555   1555  2.40  
LINK        CA    CA A 756                 O   HOH A 789     1555   1555  2.19  
LINK        CA    CA A 758                 O   HOH A 853     1555   1555  2.71  
LINK        CA    CA A 758                 O   HOH A 882     1555   1555  2.31  
LINK        CA    CA A 759                 O   HOH A 802     1555   1555  2.16  
LINK        CA    CA A 759                 O   HOH A 777     1555   1555  2.69  
LINK        CA    CA B 401                 O   HOH B 398     1555   1555  2.59  
LINK        CA    CA B 401                 O   HOH B 470     1555   1555  2.18  
LINK        CA    CA B 401                 O   HOH B 392     1555   1555  2.53  
LINK        CA    CA B 401                 O   HOH B 469     1555   1555  2.26  
LINK        CA    CA D 756                 O   HOH D 852     1555   1555  2.47  
LINK        CA    CA D 756                 O   HOH D 784     1555   1555  2.74  
LINK        CA    CA D 758                 O   HOH D 833     1555   1555  2.77  
LINK        CA    CA E 401                 O   HOH E 395     1555   1555  2.27  
LINK        CA    CA E 401                 O   HOH E 490     1555   1555  2.58  
LINK        CA    CA E 401                 O   HOH E 433     1555   1555  2.32  
LINK        CA    CA E 401                 O   HOH E 441     1555   1555  2.74  
CISPEP   1 GLU A   28    HIS A   29          0        -5.78                     
CISPEP   2 ALA A   35    GLY A   36          0       -29.70                     
CISPEP   3 ALA A  255    GLY A  256          0        -0.35                     
CISPEP   4 ASN A  292    PRO A  293          0        -9.11                     
CISPEP   5 LYS A  346    GLN A  347          0         9.19                     
CISPEP   6 LYS A  346    GLN A  347          0         9.38                     
CISPEP   7 ASP B    3    GLU B    4          0        -4.27                     
CISPEP   8 GLY B  245    GLN B  246          0         8.67                     
CISPEP   9 ALA D   35    GLY D   36          0        -9.39                     
CISPEP  10 ARG D   77    ASN D   78          0        11.92                     
CISPEP  11 ASN D  292    PRO D  293          0         1.96                     
SITE     1 AC1  6 GLY A 186  ASP A 187  GLU A 209  ASP A 259                    
SITE     2 AC1  6 HOH A 789  HOH A 883                                          
SITE     1 AC2  4 GLY A  65  ASP A  66  GLU A  97  VAL A 145                    
SITE     1 AC3  6 ASP A 109  GLY A 114  ALA A 116  HOH A 853                    
SITE     2 AC3  6 HOH A 882  GLU B 167                                          
SITE     1 AC4  5 GLU A 302  ASP A 303  GLU A 327  HOH A 777                    
SITE     2 AC4  5 HOH A 802                                                     
SITE     1 AC5  5 ATP B 380  HOH B 392  HOH B 398  HOH B 469                    
SITE     2 AC5  5 HOH B 470                                                     
SITE     1 AC6 22 GLY B  13  SER B  14  GLY B  15  LEU B  16                    
SITE     2 AC6 22 LYS B  18  GLY B 156  ASP B 157  GLY B 158                    
SITE     3 AC6 22 VAL B 159  GLY B 182  ARG B 210  LYS B 213                    
SITE     4 AC6 22 GLU B 214  GLY B 301  GLY B 302  THR B 303                    
SITE     5 AC6 22 MET B 305  TYR B 306  HOH B 379  HOH B 392                    
SITE     6 AC6 22  CA B 401  HOH B 470                                          
SITE     1 AC7  6 GLY D 186  ASP D 187  GLU D 209  ASP D 259                    
SITE     2 AC7  6 HOH D 784  HOH D 852                                          
SITE     1 AC8  4 GLY D  65  ASP D  66  GLU D  97  VAL D 145                    
SITE     1 AC9  5 ASP D 109  GLY D 114  ALA D 116  HOH D 833                    
SITE     2 AC9  5 GLU E 167                                                     
SITE     1 BC1  3 GLU D 302  ASP D 303  GLU D 327                               
SITE     1 BC2  5 ATP E 380  HOH E 395  HOH E 433  HOH E 441                    
SITE     2 BC2  5 HOH E 490                                                     
SITE     1 BC3 23 GLY E  13  SER E  14  GLY E  15  LEU E  16                    
SITE     2 BC3 23 LYS E  18  GLY E 156  ASP E 157  GLY E 158                    
SITE     3 BC3 23 VAL E 159  GLY E 182  LYS E 213  GLU E 214                    
SITE     4 BC3 23 GLY E 301  GLY E 302  THR E 303  MET E 305                    
SITE     5 BC3 23 TYR E 306  HOH E 395   CA E 401  HOH E 440                    
SITE     6 BC3 23 HOH E 450  HOH E 490  HOH E 495                               
CRYST1  102.179  146.923  148.301  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009787  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006806  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006743        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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