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Database: PDB
Entry: 5H1C
LinkDB: 5H1C
Original site: 5H1C 
HEADER    DNA BINDING PROTEIN/DNA                 08-OCT-16   5H1C              
TITLE     HUMAN RAD51 POST-SYNAPTIC COMPLEXES                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA REPAIR PROTEIN RAD51 HOMOLOG 1;                        
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: HRAD51,RAD51 HOMOLOG A;                                     
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DNA (5'-D(P*TP*TP*TP*TP*TP*TP*TP*TP*T)-3');                
COMPND   8 CHAIN: D;                                                            
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: DNA (5'-D(P*AP*AP*AP*AP*AP*AP*AP*AP*A)-3');                
COMPND  12 CHAIN: E;                                                            
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RAD51, RAD51A, RECA;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 866768;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 SYNTHETIC: YES;                                                      
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_TAXID: 9606                                                 
KEYWDS    DNA REPAIR, ATPASE, HOMOLOGOUS RECOMBINATION, DNA BINDING PROTEIN-DNA 
KEYWDS   2 COMPLEX                                                              
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    J.XU,L.ZHAO,Y.XU,W.ZHAO,P.SUNG,H.W.WANG                               
REVDAT   3   18-OCT-17 5H1C    1       REMARK                                   
REVDAT   2   25-JAN-17 5H1C    1       JRNL                                     
REVDAT   1   21-DEC-16 5H1C    0                                                
JRNL        AUTH   J.XU,L.ZHAO,Y.XU,W.ZHAO,P.SUNG,H.W.WANG                      
JRNL        TITL   CRYO-EM STRUCTURES OF HUMAN RAD51 RECOMBINASE FILAMENTS      
JRNL        TITL 2 DURING CATALYSIS OF DNA-STRAND EXCHANGE                      
JRNL        REF    NAT. STRUCT. MOL. BIOL.       V.  24    40 2017              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   27941862                                                     
JRNL        DOI    10.1038/NSMB.3336                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : UCSFIMAGE4, CTFFIND3, CHIMERA, SPIDER,    
REMARK   3                            RELION, SPIDER, RELION, IMAGIC-4D,        
REMARK   3                            SPIDER, RELION, COOT, PHENIX              
REMARK   3   RECONSTRUCTION SCHEMA  : BACK PROJECTION                           
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 1SZP                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 4.500                          
REMARK   3   NUMBER OF PARTICLES               : 30194                          
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING ONLY            
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 5H1C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300001713.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : HELICAL                           
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : FILAMENT                          
REMARK 245   PARTICLE TYPE                  : HELICAL                           
REMARK 245   NAME OF SAMPLE                 : HUMAN RAD51 POST-SYNAPTIC         
REMARK 245                                    COMPLEX; HUMAN RAD51; DNA; DNA    
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.08                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : 528                            
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : 1500.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 2500.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 50.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     MET A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     MET A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     ASN A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     ASP A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     GLU A    16                                                      
REMARK 465     GLU A    17                                                      
REMARK 465     GLU A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     PHE A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     MET A   278                                                      
REMARK 465     PHE A   279                                                      
REMARK 465     ALA A   280                                                      
REMARK 465     ALA A   281                                                      
REMARK 465     ALA A   337                                                      
REMARK 465     LYS A   338                                                      
REMARK 465     ASP A   339                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     MET B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     MET B     5                                                      
REMARK 465     GLN B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     GLU B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     ASN B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     ASP B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     VAL B    15                                                      
REMARK 465     GLU B    16                                                      
REMARK 465     GLU B    17                                                      
REMARK 465     GLU B    18                                                      
REMARK 465     SER B    19                                                      
REMARK 465     PHE B    20                                                      
REMARK 465     GLY B    21                                                      
REMARK 465     MET B   278                                                      
REMARK 465     PHE B   279                                                      
REMARK 465     ALA B   280                                                      
REMARK 465     ALA B   281                                                      
REMARK 465     ALA B   337                                                      
REMARK 465     LYS B   338                                                      
REMARK 465     ASP B   339                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     MET C     3                                                      
REMARK 465     GLN C     4                                                      
REMARK 465     MET C     5                                                      
REMARK 465     GLN C     6                                                      
REMARK 465     LEU C     7                                                      
REMARK 465     GLU C     8                                                      
REMARK 465     ALA C     9                                                      
REMARK 465     ASN C    10                                                      
REMARK 465     ALA C    11                                                      
REMARK 465     ASP C    12                                                      
REMARK 465     THR C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     VAL C    15                                                      
REMARK 465     GLU C    16                                                      
REMARK 465     GLU C    17                                                      
REMARK 465     GLU C    18                                                      
REMARK 465     SER C    19                                                      
REMARK 465     PHE C    20                                                      
REMARK 465     GLY C    21                                                      
REMARK 465     MET C   278                                                      
REMARK 465     PHE C   279                                                      
REMARK 465     ALA C   280                                                      
REMARK 465     ALA C   281                                                      
REMARK 465     ALA C   337                                                      
REMARK 465     LYS C   338                                                      
REMARK 465     ASP C   339                                                      
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   CG2  THR B   134    MG     MG B   601              1.63            
REMARK 500   CG2  THR A   134    MG     MG A   601              1.63            
REMARK 500   CG2  THR C   134    MG     MG C   402              1.63            
REMARK 500   CD   PRO C   321     N6   ANP B   602              1.67            
REMARK 500   CD   PRO B   321     N6   ANP A   602              1.67            
REMARK 500   O    GLY A   127     CG2  VAL A   269              1.72            
REMARK 500   O    GLY B   127     CG2  VAL B   269              1.72            
REMARK 500   O    GLY C   127     CG2  VAL C   269              1.72            
REMARK 500   NH1  ARG A   130     NZ   LYS A   304              1.73            
REMARK 500   NH1  ARG C   130     NZ   LYS C   304              1.73            
REMARK 500   NH1  ARG B   130     NZ   LYS B   304              1.73            
REMARK 500   C    ALA C   217     CG1  VAL C   261              1.74            
REMARK 500   C    ALA B   217     CG1  VAL B   261              1.74            
REMARK 500   C    ALA A   217     CG1  VAL A   261              1.74            
REMARK 500   CB   PRO C   321     N1   ANP B   602              1.82            
REMARK 500   CB   PRO B   321     N1   ANP A   602              1.82            
REMARK 500   N    PRO C   321     N6   ANP B   602              1.85            
REMARK 500   N    PRO B   321     N6   ANP A   602              1.86            
REMARK 500   N    PRO C   321     C6   ANP B   602              1.87            
REMARK 500   N    PRO B   321     C6   ANP A   602              1.88            
REMARK 500   O    ALA B   217     CA   VAL B   261              1.88            
REMARK 500   O    ALA A   217     CA   VAL A   261              1.88            
REMARK 500   O    ALA C   217     CA   VAL C   261              1.88            
REMARK 500   CA   PRO C   321     N1   ANP B   602              1.95            
REMARK 500   CE   MET C   158     CD2  TYR C   216              1.95            
REMARK 500   CE   MET B   158     CD2  TYR B   216              1.95            
REMARK 500   CE   MET A   158     CD2  TYR A   216              1.95            
REMARK 500   CA   PRO B   321     N1   ANP A   602              1.96            
REMARK 500   O    ALA A   217     CB   VAL A   261              1.96            
REMARK 500   O    ALA B   217     CB   VAL B   261              1.96            
REMARK 500   O    ALA C   217     CB   VAL C   261              1.96            
REMARK 500   O    LYS C   156     CD1  TYR C   216              1.97            
REMARK 500   O    LYS B   156     CD1  TYR B   216              1.97            
REMARK 500   O    LYS A   156     CD1  TYR A   216              1.97            
REMARK 500   OE1  GLN C   242     OP2   DT D     7              2.01            
REMARK 500   O    ALA A   217     C    VAL A   261              2.02            
REMARK 500   O    ALA C   217     C    VAL C   261              2.02            
REMARK 500   O    ALA B   217     C    VAL B   261              2.02            
REMARK 500   CD   GLN C   242     OP2   DT D     7              2.08            
REMARK 500   CG2  THR A   134     OD2  ASP A   222              2.09            
REMARK 500   CG2  THR B   134     OD2  ASP B   222              2.09            
REMARK 500   CG2  THR C   134     OD2  ASP C   222              2.09            
REMARK 500   NE2  GLN C   242     OP1   DT D     7              2.10            
REMARK 500   O    VAL C   270     O    LYS C   284              2.11            
REMARK 500   O    VAL B   270     O    LYS B   284              2.11            
REMARK 500   O    VAL A   270     O    LYS A   284              2.12            
REMARK 500   OG1  THR C   162     OG   SER C   223              2.14            
REMARK 500   OG1  THR A   162     OG   SER A   223              2.14            
REMARK 500   OG1  THR B   162     OG   SER B   223              2.14            
REMARK 500   N    LEU C   218     CG1  VAL C   261              2.14            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 CLOSE CONTACTS                                
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    HIS A  47       -1.93   -146.14                                   
REMARK 500    MET A  84       27.51   -140.16                                   
REMARK 500    GLN A 101       90.47     32.81                                   
REMARK 500    GLN A 114       71.84     57.85                                   
REMARK 500    PHE A 129      136.94    159.81                                   
REMARK 500    ARG A 130       32.31     71.07                                   
REMARK 500    ASN A 188     -137.35    -91.98                                   
REMARK 500    VAL A 189       76.62     52.91                                   
REMARK 500    PHE A 195      -62.92   -134.13                                   
REMARK 500    ARG A 215      108.11    -52.39                                   
REMARK 500    GLU A 237     -158.55     68.72                                   
REMARK 500    LEU A 238      -66.05     54.98                                   
REMARK 500    VAL A 261      -79.08     82.69                                   
REMARK 500    ALA A 262      141.96    145.62                                   
REMARK 500    LYS A 284     -114.75   -136.57                                   
REMARK 500    LYS A 285      127.98     66.08                                   
REMARK 500    ASN A 330     -167.40    -73.08                                   
REMARK 500    HIS B  47       -1.98   -146.15                                   
REMARK 500    MET B  84       27.57   -140.14                                   
REMARK 500    GLN B 101       90.47     32.77                                   
REMARK 500    GLN B 114       71.89     57.76                                   
REMARK 500    PHE B 129      136.91    159.79                                   
REMARK 500    ARG B 130       32.27     71.10                                   
REMARK 500    ASN B 188     -137.36    -92.00                                   
REMARK 500    VAL B 189       76.59     52.92                                   
REMARK 500    PHE B 195      -62.95   -134.11                                   
REMARK 500    ARG B 215      108.07    -52.38                                   
REMARK 500    GLU B 237     -158.52     68.78                                   
REMARK 500    LEU B 238      -66.00     54.93                                   
REMARK 500    VAL B 261      -79.11     82.73                                   
REMARK 500    ALA B 262      141.98    145.66                                   
REMARK 500    LYS B 284     -114.73   -136.56                                   
REMARK 500    LYS B 285      127.96     66.09                                   
REMARK 500    ASN B 330     -167.43    -73.10                                   
REMARK 500    HIS C  47       -1.99   -146.11                                   
REMARK 500    MET C  84       27.64   -140.16                                   
REMARK 500    GLN C 101       90.49     32.76                                   
REMARK 500    GLN C 114       71.95     57.75                                   
REMARK 500    PHE C 129      136.91    159.81                                   
REMARK 500    ARG C 130       32.31     71.08                                   
REMARK 500    ASN C 188     -137.38    -91.96                                   
REMARK 500    VAL C 189       76.60     52.89                                   
REMARK 500    PHE C 195      -62.94   -134.07                                   
REMARK 500    ARG C 215      107.99    -52.32                                   
REMARK 500    GLU C 237     -158.48     68.87                                   
REMARK 500    LEU C 238      -65.99     54.87                                   
REMARK 500    VAL C 261      -79.07     82.70                                   
REMARK 500    ALA C 262      141.96    145.60                                   
REMARK 500    LYS C 284     -114.76   -136.54                                   
REMARK 500    LYS C 285      128.00     66.10                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      51 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 222   OD2                                                    
REMARK 620 2 ANP A 602   O1B 176.4                                              
REMARK 620 3 ANP A 602   O2G 128.3  54.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 222   OD2                                                    
REMARK 620 2 ANP B 602   O2G 128.4                                              
REMARK 620 3 ANP B 602   O1B 176.4  54.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 222   OD2                                                    
REMARK 620 2 ANP C 401   O2G 128.4                                              
REMARK 620 3 ANP C 401   O1B 176.4  54.8                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 402                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-9567   RELATED DB: EMDB                              
REMARK 900 HUMAN RAD51 POST-SYNAPTIC COMPLEXES                                  
REMARK 900 RELATED ID: EMD-9568   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-9566   RELATED DB: EMDB                              
REMARK 900 RELATED ID: 5H1B   RELATED DB: PDB                                   
DBREF  5H1C A    1   339  UNP    Q06609   RAD51_HUMAN      1    339             
DBREF  5H1C B    1   339  UNP    Q06609   RAD51_HUMAN      1    339             
DBREF  5H1C C    1   339  UNP    Q06609   RAD51_HUMAN      1    339             
DBREF  5H1C D    1     9  PDB    5H1C     5H1C             1      9             
DBREF  5H1C E    1     9  PDB    5H1C     5H1C             1      9             
SEQADV 5H1C GLN A  313  UNP  Q06609    LYS   313 ENGINEERED MUTATION            
SEQADV 5H1C GLN B  313  UNP  Q06609    LYS   313 ENGINEERED MUTATION            
SEQADV 5H1C GLN C  313  UNP  Q06609    LYS   313 ENGINEERED MUTATION            
SEQRES   1 A  339  MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR          
SEQRES   2 A  339  SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER          
SEQRES   3 A  339  ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS          
SEQRES   4 A  339  LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL          
SEQRES   5 A  339  ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY          
SEQRES   6 A  339  ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA          
SEQRES   7 A  339  ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU          
SEQRES   8 A  339  PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR          
SEQRES   9 A  339  GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE          
SEQRES  10 A  339  GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG          
SEQRES  11 A  339  THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR          
SEQRES  12 A  339  CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS          
SEQRES  13 A  339  ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU          
SEQRES  14 A  339  ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY          
SEQRES  15 A  339  SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE          
SEQRES  16 A  339  ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER          
SEQRES  17 A  339  ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL          
SEQRES  18 A  339  ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY          
SEQRES  19 A  339  ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG          
SEQRES  20 A  339  PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY          
SEQRES  21 A  339  VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL          
SEQRES  22 A  339  ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO          
SEQRES  23 A  339  ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG          
SEQRES  24 A  339  LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS          
SEQRES  25 A  339  GLN ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA          
SEQRES  26 A  339  MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS          
SEQRES  27 A  339  ASP                                                          
SEQRES   1 B  339  MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR          
SEQRES   2 B  339  SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER          
SEQRES   3 B  339  ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS          
SEQRES   4 B  339  LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL          
SEQRES   5 B  339  ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY          
SEQRES   6 B  339  ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA          
SEQRES   7 B  339  ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU          
SEQRES   8 B  339  PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR          
SEQRES   9 B  339  GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE          
SEQRES  10 B  339  GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG          
SEQRES  11 B  339  THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR          
SEQRES  12 B  339  CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS          
SEQRES  13 B  339  ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU          
SEQRES  14 B  339  ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY          
SEQRES  15 B  339  SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE          
SEQRES  16 B  339  ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER          
SEQRES  17 B  339  ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL          
SEQRES  18 B  339  ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY          
SEQRES  19 B  339  ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG          
SEQRES  20 B  339  PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY          
SEQRES  21 B  339  VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL          
SEQRES  22 B  339  ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO          
SEQRES  23 B  339  ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG          
SEQRES  24 B  339  LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS          
SEQRES  25 B  339  GLN ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA          
SEQRES  26 B  339  MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS          
SEQRES  27 B  339  ASP                                                          
SEQRES   1 C  339  MET ALA MET GLN MET GLN LEU GLU ALA ASN ALA ASP THR          
SEQRES   2 C  339  SER VAL GLU GLU GLU SER PHE GLY PRO GLN PRO ILE SER          
SEQRES   3 C  339  ARG LEU GLU GLN CYS GLY ILE ASN ALA ASN ASP VAL LYS          
SEQRES   4 C  339  LYS LEU GLU GLU ALA GLY PHE HIS THR VAL GLU ALA VAL          
SEQRES   5 C  339  ALA TYR ALA PRO LYS LYS GLU LEU ILE ASN ILE LYS GLY          
SEQRES   6 C  339  ILE SER GLU ALA LYS ALA ASP LYS ILE LEU ALA GLU ALA          
SEQRES   7 C  339  ALA LYS LEU VAL PRO MET GLY PHE THR THR ALA THR GLU          
SEQRES   8 C  339  PHE HIS GLN ARG ARG SER GLU ILE ILE GLN ILE THR THR          
SEQRES   9 C  339  GLY SER LYS GLU LEU ASP LYS LEU LEU GLN GLY GLY ILE          
SEQRES  10 C  339  GLU THR GLY SER ILE THR GLU MET PHE GLY GLU PHE ARG          
SEQRES  11 C  339  THR GLY LYS THR GLN ILE CYS HIS THR LEU ALA VAL THR          
SEQRES  12 C  339  CYS GLN LEU PRO ILE ASP ARG GLY GLY GLY GLU GLY LYS          
SEQRES  13 C  339  ALA MET TYR ILE ASP THR GLU GLY THR PHE ARG PRO GLU          
SEQRES  14 C  339  ARG LEU LEU ALA VAL ALA GLU ARG TYR GLY LEU SER GLY          
SEQRES  15 C  339  SER ASP VAL LEU ASP ASN VAL ALA TYR ALA ARG ALA PHE          
SEQRES  16 C  339  ASN THR ASP HIS GLN THR GLN LEU LEU TYR GLN ALA SER          
SEQRES  17 C  339  ALA MET MET VAL GLU SER ARG TYR ALA LEU LEU ILE VAL          
SEQRES  18 C  339  ASP SER ALA THR ALA LEU TYR ARG THR ASP TYR SER GLY          
SEQRES  19 C  339  ARG GLY GLU LEU SER ALA ARG GLN MET HIS LEU ALA ARG          
SEQRES  20 C  339  PHE LEU ARG MET LEU LEU ARG LEU ALA ASP GLU PHE GLY          
SEQRES  21 C  339  VAL ALA VAL VAL ILE THR ASN GLN VAL VAL ALA GLN VAL          
SEQRES  22 C  339  ASP GLY ALA ALA MET PHE ALA ALA ASP PRO LYS LYS PRO          
SEQRES  23 C  339  ILE GLY GLY ASN ILE ILE ALA HIS ALA SER THR THR ARG          
SEQRES  24 C  339  LEU TYR LEU ARG LYS GLY ARG GLY GLU THR ARG ILE CYS          
SEQRES  25 C  339  GLN ILE TYR ASP SER PRO CYS LEU PRO GLU ALA GLU ALA          
SEQRES  26 C  339  MET PHE ALA ILE ASN ALA ASP GLY VAL GLY ASP ALA LYS          
SEQRES  27 C  339  ASP                                                          
SEQRES   1 D    9   DT  DT  DT  DT  DT  DT  DT  DT  DT                          
SEQRES   1 E    9   DA  DA  DA  DA  DA  DA  DA  DA  DA                          
HET     MG  A 601       1                                                       
HET    ANP  A 602      31                                                       
HET     MG  B 601       1                                                       
HET    ANP  B 602      31                                                       
HET    ANP  C 401      31                                                       
HET     MG  C 402       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
FORMUL   6   MG    3(MG 2+)                                                     
FORMUL   7  ANP    3(C10 H17 N6 O12 P3)                                         
HELIX    1 AA1 PRO A   24  GLU A   29  5                                   6    
HELIX    2 AA2 ASN A   34  GLU A   42  1                                   9    
HELIX    3 AA3 GLU A   43  GLY A   45  5                                   3    
HELIX    4 AA4 THR A   48  TYR A   54  1                                   7    
HELIX    5 AA5 PRO A   56  ILE A   63  1                                   8    
HELIX    6 AA6 SER A   67  VAL A   82  1                                  16    
HELIX    7 AA7 THR A   88  SER A   97  1                                  10    
HELIX    8 AA8 SER A  106  LEU A  113  1                                   8    
HELIX    9 AA9 GLY A  132  CYS A  144  1                                  13    
HELIX   10 AB1 GLN A  145  LEU A  146  5                                   2    
HELIX   11 AB2 PRO A  147  GLY A  151  5                                   5    
HELIX   12 AB3 ARG A  167  GLY A  179  1                                  13    
HELIX   13 AB4 SER A  181  ASN A  188  1                                   8    
HELIX   14 AB5 ASP A  198  VAL A  212  1                                  15    
HELIX   15 AB6 THR A  225  TYR A  232  1                                   8    
HELIX   16 AB7 LEU A  238  GLY A  260  1                                  23    
HELIX   17 AB8 GLY A  288  SER A  296  1                                   9    
HELIX   18 AB9 PRO B   24  GLU B   29  5                                   6    
HELIX   19 AC1 ASN B   34  GLU B   42  1                                   9    
HELIX   20 AC2 GLU B   43  GLY B   45  5                                   3    
HELIX   21 AC3 THR B   48  TYR B   54  1                                   7    
HELIX   22 AC4 PRO B   56  ILE B   63  1                                   8    
HELIX   23 AC5 SER B   67  VAL B   82  1                                  16    
HELIX   24 AC6 ALA B   89  SER B   97  1                                   9    
HELIX   25 AC7 SER B  106  LEU B  113  1                                   8    
HELIX   26 AC8 GLY B  132  CYS B  144  1                                  13    
HELIX   27 AC9 GLN B  145  LEU B  146  5                                   2    
HELIX   28 AD1 PRO B  147  GLY B  151  5                                   5    
HELIX   29 AD2 ARG B  167  GLY B  179  1                                  13    
HELIX   30 AD3 SER B  181  ASN B  188  1                                   8    
HELIX   31 AD4 ASP B  198  VAL B  212  1                                  15    
HELIX   32 AD5 THR B  225  TYR B  232  1                                   8    
HELIX   33 AD6 LEU B  238  GLY B  260  1                                  23    
HELIX   34 AD7 GLY B  288  SER B  296  1                                   9    
HELIX   35 AD8 PRO C   24  GLU C   29  5                                   6    
HELIX   36 AD9 ASN C   34  GLU C   42  1                                   9    
HELIX   37 AE1 GLU C   43  GLY C   45  5                                   3    
HELIX   38 AE2 THR C   48  TYR C   54  1                                   7    
HELIX   39 AE3 PRO C   56  ILE C   63  1                                   8    
HELIX   40 AE4 SER C   67  VAL C   82  1                                  16    
HELIX   41 AE5 ALA C   89  SER C   97  1                                   9    
HELIX   42 AE6 SER C  106  LEU C  113  1                                   8    
HELIX   43 AE7 GLY C  132  CYS C  144  1                                  13    
HELIX   44 AE8 GLN C  145  LEU C  146  5                                   2    
HELIX   45 AE9 PRO C  147  GLY C  151  5                                   5    
HELIX   46 AF1 ARG C  167  GLY C  179  1                                  13    
HELIX   47 AF2 SER C  181  ASN C  188  1                                   8    
HELIX   48 AF3 ASP C  198  VAL C  212  1                                  15    
HELIX   49 AF4 THR C  225  TYR C  232  1                                   8    
HELIX   50 AF5 LEU C  238  GLY C  260  1                                  23    
HELIX   51 AF6 GLY C  288  SER C  296  1                                   9    
SHEET    1 AA1 6 ILE A 122  PHE A 126  0                                        
SHEET    2 AA1 6 VAL A 263  ASN A 267  1  O  ILE A 265   N  MET A 125           
SHEET    3 AA1 6 TYR A 216  VAL A 221  1  N  VAL A 221   O  THR A 266           
SHEET    4 AA1 6 LYS A 156  ASP A 161  1  N  LYS A 156   O  ALA A 217           
SHEET    5 AA1 6 ALA A 190  ARG A 193  1  O  ALA A 190   N  ALA A 157           
SHEET    6 AA1 6 THR B  87  THR B  88 -1  O  THR B  87   N  TYR A 191           
SHEET    1 AA2 3 ARG A 299  LYS A 304  0                                        
SHEET    2 AA2 3 ARG A 310  TYR A 315 -1  O  ILE A 311   N  ARG A 303           
SHEET    3 AA2 3 GLU A 324  PHE A 327 -1  O  ALA A 325   N  CYS A 312           
SHEET    1 AA3 2 ILE A 329  ASN A 330  0                                        
SHEET    2 AA3 2 GLY A 333  VAL A 334 -1  O  GLY A 333   N  ASN A 330           
SHEET    1 AA4 6 ILE B 122  PHE B 126  0                                        
SHEET    2 AA4 6 VAL B 263  ASN B 267  1  O  ILE B 265   N  MET B 125           
SHEET    3 AA4 6 TYR B 216  VAL B 221  1  N  VAL B 221   O  THR B 266           
SHEET    4 AA4 6 LYS B 156  ASP B 161  1  N  LYS B 156   O  ALA B 217           
SHEET    5 AA4 6 ALA B 190  ARG B 193  1  O  ALA B 190   N  ALA B 157           
SHEET    6 AA4 6 THR C  87  THR C  88 -1  O  THR C  87   N  TYR B 191           
SHEET    1 AA5 3 ARG B 299  LYS B 304  0                                        
SHEET    2 AA5 3 ARG B 310  TYR B 315 -1  O  ILE B 311   N  ARG B 303           
SHEET    3 AA5 3 GLU B 324  PHE B 327 -1  O  ALA B 325   N  CYS B 312           
SHEET    1 AA6 2 ILE B 329  ASN B 330  0                                        
SHEET    2 AA6 2 GLY B 333  VAL B 334 -1  O  GLY B 333   N  ASN B 330           
SHEET    1 AA7 5 ILE C 122  PHE C 126  0                                        
SHEET    2 AA7 5 VAL C 263  ASN C 267  1  O  ILE C 265   N  MET C 125           
SHEET    3 AA7 5 TYR C 216  VAL C 221  1  N  VAL C 221   O  THR C 266           
SHEET    4 AA7 5 LYS C 156  ASP C 161  1  N  LYS C 156   O  ALA C 217           
SHEET    5 AA7 5 ALA C 190  ARG C 193  1  O  ALA C 190   N  ALA C 157           
SHEET    1 AA8 3 ARG C 299  LYS C 304  0                                        
SHEET    2 AA8 3 ARG C 310  TYR C 315 -1  O  ILE C 311   N  ARG C 303           
SHEET    3 AA8 3 GLU C 324  PHE C 327 -1  O  ALA C 325   N  CYS C 312           
SHEET    1 AA9 2 ILE C 329  ASN C 330  0                                        
SHEET    2 AA9 2 GLY C 333  VAL C 334 -1  O  GLY C 333   N  ASN C 330           
LINK         O   ALA A 217                 CG1 VAL A 261     1555   1555  1.45  
LINK         OD2 ASP A 222                MG    MG A 601     1555   1555  2.49  
LINK         CG2 VAL A 270                 CG2 ILE A 287     1555   1555  1.58  
LINK         O   ALA B 217                 CG1 VAL B 261     1555   1555  1.45  
LINK         OD2 ASP B 222                MG    MG B 601     1555   1555  2.49  
LINK         CG2 VAL B 270                 CG2 ILE B 287     1555   1555  1.58  
LINK         O   ALA C 217                 CG1 VAL C 261     1555   1555  1.45  
LINK         OD2 ASP C 222                MG    MG C 402     1555   1555  2.49  
LINK         CG2 VAL C 270                 CG2 ILE C 287     1555   1555  1.58  
LINK        MG    MG A 601                 O1B ANP A 602     1555   1555  1.73  
LINK        MG    MG A 601                 O2G ANP A 602     1555   1555  2.57  
LINK        MG    MG B 601                 O2G ANP B 602     1555   1555  2.57  
LINK        MG    MG B 601                 O1B ANP B 602     1555   1555  1.73  
LINK         O2G ANP C 401                MG    MG C 402     1555   1555  2.57  
LINK         O1B ANP C 401                MG    MG C 402     1555   1555  1.73  
CISPEP   1 GLY A  234    ARG A  235          0         0.06                     
CISPEP   2 ARG A  235    GLY A  236          0         0.07                     
CISPEP   3 GLY A  236    GLU A  237          0         0.92                     
CISPEP   4 GLY B  234    ARG B  235          0         0.03                     
CISPEP   5 ARG B  235    GLY B  236          0        -0.01                     
CISPEP   6 GLY B  236    GLU B  237          0         0.85                     
CISPEP   7 GLY C  234    ARG C  235          0         0.07                     
CISPEP   8 ARG C  235    GLY C  236          0        -0.05                     
CISPEP   9 GLY C  236    GLU C  237          0         0.74                     
SITE     1 AC1  3 THR A 134  ASP A 222  ANP A 602                               
SITE     1 AC2 19 ARG A 130  THR A 131  GLY A 132  LYS A 133                    
SITE     2 AC2 19 THR A 134  GLN A 135  GLU A 163  ARG A 170                    
SITE     3 AC2 19 GLN A 268  ARG A 310   MG A 601  HIS B 294                    
SITE     4 AC2 19 SER B 296  ASP B 316  SER B 317  PRO B 318                    
SITE     5 AC2 19 CYS B 319  LEU B 320  PRO B 321                               
SITE     1 AC3  3 THR B 134  ASP B 222  ANP B 602                               
SITE     1 AC4 19 ARG B 130  THR B 131  GLY B 132  LYS B 133                    
SITE     2 AC4 19 THR B 134  GLN B 135  GLU B 163  ARG B 170                    
SITE     3 AC4 19 GLN B 268  ARG B 310   MG B 601  HIS C 294                    
SITE     4 AC4 19 SER C 296  ASP C 316  SER C 317  PRO C 318                    
SITE     5 AC4 19 CYS C 319  LEU C 320  PRO C 321                               
SITE     1 AC5 11 ARG C 130  THR C 131  GLY C 132  LYS C 133                    
SITE     2 AC5 11 THR C 134  GLN C 135  GLU C 163  ARG C 170                    
SITE     3 AC5 11 GLN C 268  ARG C 310   MG C 402                               
SITE     1 AC6  3 THR C 134  ASP C 222  ANP C 401                               
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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