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Database: PDB
Entry: 1NM1
LinkDB: 1NM1
Original site: 1NM1 
HEADER    STRUCTURAL PROTEIN                      08-JAN-03   1NM1              
TITLE     CRYSTAL STRUCTURE OF D. DICSOIDEUM ACTIN COMPLEXED WITH               
TITLE    2 GELSOLIN SEGMENT 1 AND MG ATP AT 1.8 A RESOLUTION                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACTIN;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: GELSOLIN;                                                  
COMPND   6 CHAIN: G;                                                            
COMPND   7 FRAGMENT: DOMAIN 1;                                                  
COMPND   8 SYNONYM: ACTIN-DEPOLYMERIZING FACTOR, ADF, BREVIN, AGEL;             
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DICTYOSTELIUM DISCOIDEUM;                       
SOURCE   3 ORGANISM_TAXID: 44689;                                               
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   6 ORGANISM_COMMON: HUMAN;                                              
SOURCE   7 ORGANISM_TAXID: 9606;                                                
SOURCE   8 GENE: GSN;                                                           
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PMW172                                    
KEYWDS    ACTIN, GELSOLIN, CYTOSKELETON ORGANIZATION, ACTIN-                    
KEYWDS   2 ASSOCIATED PROTEIN, STRUCTURAL PROTEIN                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.M.VOROBIEV,S.WELTI,J.CONDEELIS,S.C.ALMO                             
REVDAT   3   24-FEB-09 1NM1    1       VERSN                                    
REVDAT   2   20-MAY-03 1NM1    1       JRNL   SPRSDE                            
REVDAT   1   21-JAN-03 1NM1    0                                                
SPRSDE     21-JAN-03 1NM1      1DGA                                             
JRNL        AUTH   S.M.VOROBIEV,B.STROKOPYTOV,D.G.DRUBIN,C.FRIEDEN,             
JRNL        AUTH 2 S.ONO,J.CONDEELIS,P.A.RUBENSTEIN,S.C.ALMO                    
JRNL        TITL   THE STRUCTURE OF NON-VERTEBRATE ACTIN:                       
JRNL        TITL 2 IMPLICATIONS FOR THE ATP HYDROLYTIC MECHANISM                
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 100  5760 2003              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   12732734                                                     
JRNL        DOI    10.1073/PNAS.0832273100                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 60856                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3773                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 41                                      
REMARK   3   SOLVENT ATOMS            : 362                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.41                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1NM1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB017993.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-APR-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X9B                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07018                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60943                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 2.410                              
REMARK 200  R MERGE                    (I) : 0.04400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20700                            
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: X-PLOR                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1DGA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM CHLORIDE, LITHEIM              
REMARK 280  CHLORIDE, HEPES, ATP, PH 7.5, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       89.26950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.54450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       89.26950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.54450            
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: 3320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G                                  
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 460  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 590  LIES ON A SPECIAL POSITION.                          
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     ASP A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     GLY A    42                                                      
REMARK 465     VAL A    43                                                      
REMARK 465     MET A    44                                                      
REMARK 465     VAL A    45                                                      
REMARK 465     GLY A    46                                                      
REMARK 465     MET A    47                                                      
REMARK 465     GLY A    48                                                      
REMARK 465     GLN A    49                                                      
REMARK 465     MET G     1                                                      
REMARK 465     VAL G     2                                                      
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 A   4    CG   OD1  OD2                                       
REMARK 470     ARG A  28    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A  41    OG1  CG2                                            
REMARK 470     LYS A  50    CG   CD   CE   NZ                                   
REMARK 470     LYS A  68    CG   CD   CE   NZ                                   
REMARK 470     LYS A 113    CG   CD   CE   NZ                                   
REMARK 470     GLU A 195    CG   CD   OE1  OE2                                  
REMARK 470     SER A 199    OG                                                  
REMARK 470     GLN A 225    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 270    CG   CD   OE1  OE2                                  
REMARK 470     VAL G   3    CG1  CG2                                            
REMARK 470     GLU G   4    CG   CD   OE1  OE2                                  
REMARK 470     ARG G  53    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN G  54    CG   OD1  ND2                                       
REMARK 470     LYS G 111    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   S    SO2 A   404     S    SO2 A   404     2555     1.35            
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    ALA A 181     -151.24   -154.84                                   
REMARK 500    ASP A 244      -90.05    -79.35                                   
REMARK 500    ASN A 252        1.80    -67.93                                   
REMARK 500    ASN A 296       59.30   -145.44                                   
REMARK 500    PHE G 101       26.24   -140.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 403  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP A 401   O2G                                                    
REMARK 620 2 HOH A 418   O   169.1                                              
REMARK 620 3 HOH A 445   O    80.8 101.3                                        
REMARK 620 4 HOH A 411   O   107.6  83.1  91.7                                  
REMARK 620 5 HOH A 417   O    78.6  91.1  80.8 169.5                            
REMARK 620 6 ATP A 401   O1B  91.2  86.7 172.0  90.3  98.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA G 402  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH G 414   O                                                      
REMARK 620 2 HOH G 413   O    82.1                                              
REMARK 620 3 VAL G 121   O    76.8  92.1                                        
REMARK 620 4 GLU G  73   OE2 156.8  89.9  81.8                                  
REMARK 620 5 GLU G  73   OE1 143.9  77.1 132.6  52.7                            
REMARK 620 6 ASP G  42   OD2  98.0 177.0  90.8  91.1 101.3                      
REMARK 620 7 GLY G  41   O    78.3 105.0 147.4 124.9  79.0  72.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA G 402                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 403                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 405                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 401                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO2 A 404                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DGA   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX, BUT AT 1.93 A RESOLUTION                   
REMARK 900 RELATED ID: 1NLV   RELATED DB: PDB                                   
REMARK 900 THE D.DISCOIDEUM ACTIN-GELSOLIN COMPLEX BOUND TO CA ATP              
DBREF  1NM1 A    1   375  UNP    P02577   ACT1_DICDI       1    375             
DBREF  1NM1 G    1   125  UNP    P06396   GELS_HUMAN      52    176             
SEQRES   1 A  375  ASP GLY GLU ASP VAL GLN ALA LEU VAL ILE ASP ASN GLY          
SEQRES   2 A  375  SER GLY MET CYS LYS ALA GLY PHE ALA GLY ASP ASP ALA          
SEQRES   3 A  375  PRO ARG ALA VAL PHE PRO SER ILE VAL GLY ARG PRO ARG          
SEQRES   4 A  375  HIS THR GLY VAL MET VAL GLY MET GLY GLN LYS ASP SER          
SEQRES   5 A  375  TYR VAL GLY ASP GLU ALA GLN SER LYS ARG GLY ILE LEU          
SEQRES   6 A  375  THR LEU LYS TYR PRO ILE GLU HIS GLY ILE VAL THR ASN          
SEQRES   7 A  375  TRP ASP ASP MET GLU LYS ILE TRP HIS HIS THR PHE TYR          
SEQRES   8 A  375  ASN GLU LEU ARG VAL ALA PRO GLU GLU HIS PRO VAL LEU          
SEQRES   9 A  375  LEU THR GLU ALA PRO LEU ASN PRO LYS ALA ASN ARG GLU          
SEQRES  10 A  375  LYS MET THR GLN ILE MET PHE GLU THR PHE ASN THR PRO          
SEQRES  11 A  375  ALA MET TYR VAL ALA ILE GLN ALA VAL LEU SER LEU TYR          
SEQRES  12 A  375  ALA SER GLY ARG THR THR GLY ILE VAL MET ASP SER GLY          
SEQRES  13 A  375  ASP GLY VAL SER HIS THR VAL PRO ILE TYR GLU GLY TYR          
SEQRES  14 A  375  ALA LEU PRO HIS ALA ILE LEU ARG LEU ASP LEU ALA GLY          
SEQRES  15 A  375  ARG ASP LEU THR ASP TYR MET MET LYS ILE LEU THR GLU          
SEQRES  16 A  375  ARG GLY TYR SER PHE THR THR THR ALA GLU ARG GLU ILE          
SEQRES  17 A  375  VAL ARG ASP ILE LYS GLU LYS LEU ALA TYR VAL ALA LEU          
SEQRES  18 A  375  ASP PHE GLU GLN GLU MET ALA THR ALA ALA SER SER SER          
SEQRES  19 A  375  ALA LEU GLU LYS SER TYR GLU LEU PRO ASP GLY GLN VAL          
SEQRES  20 A  375  ILE THR ILE GLY ASN GLU ARG PHE ARG CYS PRO GLU ALA          
SEQRES  21 A  375  LEU PHE GLN PRO SER PHE LEU GLY MET GLU SER ALA GLY          
SEQRES  22 A  375  ILE HIS GLU THR THR TYR ASN SER ILE MET LYS CYS ASP          
SEQRES  23 A  375  VAL ASP ILE ARG LYS ASP LEU TYR GLY ASN VAL VAL LEU          
SEQRES  24 A  375  SER GLY GLY THR THR MET PHE PRO GLY ILE ALA ASP ARG          
SEQRES  25 A  375  MET ASN LYS GLU LEU THR ALA LEU ALA PRO SER THR MET          
SEQRES  26 A  375  LYS ILE LYS ILE ILE ALA PRO PRO GLU ARG LYS TYR SER          
SEQRES  27 A  375  VAL TRP ILE GLY GLY SER ILE LEU ALA SER LEU SER THR          
SEQRES  28 A  375  PHE GLN GLN MET TRP ILE SER LYS GLU GLU TYR ASP GLU          
SEQRES  29 A  375  SER GLY PRO SER ILE VAL HIS ARG LYS CYS PHE                  
SEQRES   1 G  125  MET VAL VAL GLU HIS PRO GLU PHE LEU LYS ALA GLY LYS          
SEQRES   2 G  125  GLU PRO GLY LEU GLN ILE TRP ARG VAL GLU LYS PHE ASP          
SEQRES   3 G  125  LEU VAL PRO VAL PRO THR ASN LEU TYR GLY ASP PHE PHE          
SEQRES   4 G  125  THR GLY ASP ALA TYR VAL ILE LEU LYS THR VAL GLN LEU          
SEQRES   5 G  125  ARG ASN GLY ASN LEU GLN TYR ASP LEU HIS TYR TRP LEU          
SEQRES   6 G  125  GLY ASN GLU CYS SER GLN ASP GLU SER GLY ALA ALA ALA          
SEQRES   7 G  125  ILE PHE THR VAL GLN LEU ASP ASP TYR LEU ASN GLY ARG          
SEQRES   8 G  125  ALA VAL GLN HIS ARG GLU VAL GLN GLY PHE GLU SER ALA          
SEQRES   9 G  125  THR PHE LEU GLY TYR PHE LYS SER GLY LEU LYS TYR LYS          
SEQRES  10 G  125  LYS GLY GLY VAL ALA SER GLY PHE                              
HET     CA  G 402       1                                                       
HET     MG  A 403       1                                                       
HET    SO4  A 405       5                                                       
HET    ATP  A 401      31                                                       
HET    SO2  A 404       3                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM     SO2 SULFUR DIOXIDE                                                   
FORMUL   3   CA    CA 2+                                                        
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  SO4    O4 S 2-                                                      
FORMUL   6  ATP    C10 H16 N5 O13 P3                                            
FORMUL   7  SO2    O2 S                                                         
FORMUL   8  HOH   *362(H2 O)                                                    
HELIX    1   1 GLY A   55  LYS A   61  1                                   7    
HELIX    2   2 ASN A   78  ASN A   92  1                                  15    
HELIX    3   3 ALA A   97  HIS A  101  5                                   5    
HELIX    4   4 PRO A  112  THR A  126  1                                  15    
HELIX    5   5 GLN A  137  SER A  145  1                                   9    
HELIX    6   6 PRO A  172  ILE A  175  5                                   4    
HELIX    7   7 ALA A  181  ARG A  196  1                                  16    
HELIX    8   8 THR A  202  ALA A  217  1                                  16    
HELIX    9   9 ASP A  222  SER A  233  1                                  12    
HELIX   10  10 ASN A  252  GLN A  263  1                                  12    
HELIX   11  11 PRO A  264  GLY A  268  5                                   5    
HELIX   12  12 GLY A  273  LYS A  284  1                                  12    
HELIX   13  13 ASP A  286  GLY A  295  1                                  10    
HELIX   14  14 GLY A  301  MET A  305  5                                   5    
HELIX   15  15 GLY A  308  ALA A  321  1                                  14    
HELIX   16  16 TYR A  337  LEU A  349  1                                  13    
HELIX   17  17 THR A  351  TRP A  356  1                                   6    
HELIX   18  18 LYS A  359  GLY A  366  1                                   8    
HELIX   19  19 ILE A  369  CYS A  374  1                                   6    
HELIX   20  20 HIS G    5  ALA G   11  1                                   7    
HELIX   21  21 PRO G   31  TYR G   35  5                                   5    
HELIX   22  22 SER G   70  LEU G   88  1                                  19    
HELIX   23  23 SER G  103  GLY G  108  1                                   6    
SHEET    1   A 6 ALA A  29  PRO A  32  0                                        
SHEET    2   A 6 MET A  16  PHE A  21 -1  N  CYS A  17   O  PHE A  31           
SHEET    3   A 6 LEU A   8  ASN A  12 -1  N  ASP A  11   O  LYS A  18           
SHEET    4   A 6 VAL A 103  GLU A 107  1  O  LEU A 104   N  ILE A  10           
SHEET    5   A 6 ALA A 131  ILE A 136  1  O  TYR A 133   N  LEU A 105           
SHEET    6   A 6 ILE A 357  SER A 358 -1  O  ILE A 357   N  MET A 132           
SHEET    1   B 3 TYR A  53  VAL A  54  0                                        
SHEET    2   B 3 VAL A  35  PRO A  38 -1  N  GLY A  36   O  TYR A  53           
SHEET    3   B 3 LEU A  65  LYS A  68 -1  O  THR A  66   N  ARG A  37           
SHEET    1   C 2 ILE A  71  GLU A  72  0                                        
SHEET    2   C 2 ILE A  75  VAL A  76 -1  O  ILE A  75   N  GLU A  72           
SHEET    1   D 5 ILE A 329  ILE A 330  0                                        
SHEET    2   D 5 VAL A 297  SER A 300  1  N  VAL A 297   O  ILE A 330           
SHEET    3   D 5 GLY A 150  SER A 155  1  N  MET A 153   O  VAL A 298           
SHEET    4   D 5 SER A 160  TYR A 166 -1  O  VAL A 163   N  VAL A 152           
SHEET    5   D 5 TYR A 169  ALA A 170 -1  O  TYR A 169   N  TYR A 166           
SHEET    1   E 5 ILE A 329  ILE A 330  0                                        
SHEET    2   E 5 VAL A 297  SER A 300  1  N  VAL A 297   O  ILE A 330           
SHEET    3   E 5 GLY A 150  SER A 155  1  N  MET A 153   O  VAL A 298           
SHEET    4   E 5 SER A 160  TYR A 166 -1  O  VAL A 163   N  VAL A 152           
SHEET    5   E 5 LEU A 176  LEU A 178 -1  O  LEU A 178   N  SER A 160           
SHEET    1   F 2 LYS A 238  GLU A 241  0                                        
SHEET    2   F 2 VAL A 247  ILE A 250 -1  O  ILE A 248   N  TYR A 240           
SHEET    1   G 5 ASP G  26  PRO G  29  0                                        
SHEET    2   G 5 GLY G  16  GLU G  23 -1  N  ARG G  21   O  VAL G  28           
SHEET    3   G 5 ALA G  43  GLN G  51 -1  O  THR G  49   N  GLY G  16           
SHEET    4   G 5 LEU G  57  LEU G  65 -1  O  GLN G  58   N  VAL G  50           
SHEET    5   G 5 ALA G  92  VAL G  98  1  O  GLU G  97   N  LEU G  65           
SHEET    1   H 2 ASP G  37  PHE G  39  0                                        
SHEET    2   H 2 LYS G 115  LYS G 117  1  O  LYS G 115   N  PHE G  38           
LINK        MG    MG A 403                 O2G ATP A 401     1555   1555  2.21  
LINK        MG    MG A 403                 O   HOH A 418     1555   1555  2.24  
LINK        MG    MG A 403                 O   HOH A 445     1555   1555  2.40  
LINK        MG    MG A 403                 O   HOH A 411     1555   1555  2.20  
LINK        MG    MG A 403                 O   HOH A 417     1555   1555  2.61  
LINK        MG    MG A 403                 O1B ATP A 401     1555   1555  2.63  
LINK        CA    CA G 402                 O   HOH G 414     1555   1555  2.55  
LINK        CA    CA G 402                 O   HOH G 413     1555   1555  2.46  
LINK        CA    CA G 402                 O   VAL G 121     1555   1555  2.38  
LINK        CA    CA G 402                 OE2 GLU G  73     1555   1555  2.46  
LINK        CA    CA G 402                 OE1 GLU G  73     1555   1555  2.52  
LINK        CA    CA G 402                 OD2 ASP G  42     1555   1555  2.49  
LINK        CA    CA G 402                 O   GLY G  41     1555   1555  2.38  
SITE     1 AC1  6 GLY G  41  ASP G  42  GLU G  73  VAL G 121                    
SITE     2 AC1  6 HOH G 413  HOH G 414                                          
SITE     1 AC2  5 ATP A 401  HOH A 411  HOH A 417  HOH A 418                    
SITE     2 AC2  5 HOH A 445                                                     
SITE     1 AC3  7 GLY A 308  ILE A 309  ALA A 310  ASP A 311                    
SITE     2 AC3  7 HOH A 481  HOH A 621  LYS G  13                               
SITE     1 AC4 30 GLY A  13  SER A  14  GLY A  15  MET A  16                    
SITE     2 AC4 30 LYS A  18  GLY A 156  ASP A 157  GLY A 158                    
SITE     3 AC4 30 GLY A 182  ARG A 183  ARG A 210  LYS A 213                    
SITE     4 AC4 30 GLU A 214  GLY A 301  GLY A 302  THR A 303                    
SITE     5 AC4 30 MET A 305  PHE A 306  LYS A 336   MG A 403                    
SITE     6 AC4 30 HOH A 409  HOH A 417  HOH A 426  HOH A 432                    
SITE     7 AC4 30 HOH A 444  HOH A 445  HOH A 457  HOH A 493                    
SITE     8 AC4 30 HOH A 561  HOH A 580                                          
SITE     1 AC5  4 ARG A  62  THR A 202  THR A 203  ALA A 204                    
CRYST1  178.539   69.089   56.552  90.00 104.34  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005600  0.000000  0.001430        0.00000                         
SCALE2      0.000000  0.014470  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018250        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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