GenomeNet

Database: PDB
Entry: 1F0V
LinkDB: 1F0V
Original site: 1F0V 
HEADER    HYDROLASE/DNA                           17-MAY-00   1F0V              
TITLE     CRYSTAL STRUCTURE OF AN RNASE A DIMER DISPLAYING A NEW TYPE OF 3D     
TITLE    2 DOMAIN SWAPPING                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-D(*CP*G)-3';                                            
COMPND   3 CHAIN: M, N, O, P;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: RIBONUCLEASE A;                                            
COMPND   7 CHAIN: A, B, C, D;                                                   
COMPND   8 SYNONYM: RNASE 1, RNASE A;                                           
COMPND   9 EC: 3.1.27.5                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 MOL_ID: 2;                                                           
SOURCE   4 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   5 ORGANISM_COMMON: CATTLE;                                             
SOURCE   6 ORGANISM_TAXID: 9913;                                                
SOURCE   7 ORGAN: PANCREAS                                                      
KEYWDS    DOMAIN SWAPPING, CRYSTAL, RIBONUCLEASE, BOVINE PANCREAS, HYDROLASE-   
KEYWDS   2 DNA COMPLEX                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.S.LIU,G.GOTTE,M.LIBONATI,D.S.EISENBERG                              
REVDAT   6   13-JUL-11 1F0V    1       VERSN                                    
REVDAT   5   24-FEB-09 1F0V    1       VERSN                                    
REVDAT   4   01-AUG-06 1F0V    1       REMARK AUTHOR COMPND                     
REVDAT   3   01-APR-03 1F0V    1       JRNL                                     
REVDAT   2   14-MAR-01 1F0V    1       REMARK                                   
REVDAT   1   21-FEB-01 1F0V    0                                                
JRNL        AUTH   Y.S.LIU,G.GOTTE,M.LIBONATI,D.S.EISENBERG                     
JRNL        TITL   A DOMAIN-SWAPPED RNASE A DIMER WITH IMPLICATIONS FOR AMYLOID 
JRNL        TITL 2 FORMATION                                                    
JRNL        REF    NAT.STRUCT.BIOL.              V.   8   211 2001              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   11224563                                                     
JRNL        DOI    10.1038/84941                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
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)   (%) : 90.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 68191                          
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) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.213                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 11.200                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 7651                            
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            : 3804                                    
REMARK   3   NUCLEIC ACID ATOMS       : 152                                     
REMARK   3   HETEROGEN ATOMS          : 164                                     
REMARK   3   SOLVENT ATOMS            : 554                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.00                          
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) : 0.019                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.07                            
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 1F0V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011107.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.072                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 76047                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 10.000                             
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.08000                            
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: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M PHOSPHATE BUFFER, 16 % PEG 4000,   
REMARK 280  2 % DIOXANE, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       48.17050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 APPLY THE FOLLOWING TO CHAINS: M, A                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, C                                  
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, D                                  
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 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   O    SER D   690     O3   GOL C   919     2555     1.96            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  85   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A  85   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  48       65.48   -100.16                                   
REMARK 500    GLN A  60     -132.50   -108.22                                   
REMARK 500    SER B 222      137.41    170.84                                   
REMARK 500    HIS B 248       65.25   -104.29                                   
REMARK 500    GLN B 260     -133.80   -103.37                                   
REMARK 500    ASN B 271       36.08    -96.82                                   
REMARK 500    ASN B 294       76.91   -114.83                                   
REMARK 500    HIS C 448       63.86   -103.64                                   
REMARK 500    GLN C 460     -133.77   -103.06                                   
REMARK 500    ASN C 494       72.93   -104.18                                   
REMARK 500    ASP D 614       72.19   -150.96                                   
REMARK 500    HIS D 648       68.07   -106.57                                   
REMARK 500    GLN D 660     -130.33   -103.67                                   
REMARK 500    ASN D 671       35.67    -95.78                                   
REMARK 500    LYS D 691      110.05   -165.16                                   
REMARK 500    ASN D 694       69.21   -105.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1537        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH A1538        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH A1574        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH B1536        DISTANCE =  5.63 ANGSTROMS                       
REMARK 525    HOH D1585        DISTANCE =  5.73 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 P 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 905                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 906                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 907                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 908                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 909                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 910                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 911                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 912                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 913                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 914                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 915                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 916                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 917                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 918                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 919                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 920                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 921                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 922                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 923                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 924                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1A2W   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A 3D DOMAIN-SWAPPED DIMER OF RNASE A            
REMARK 900 AT 2.1 A RESOLUTION                                                  
DBREF  1F0V A    1   124  UNP    P61823   RNAS1_BOVIN     27    150             
DBREF  1F0V B  201   324  UNP    P61823   RNAS1_BOVIN     27    150             
DBREF  1F0V C  401   524  UNP    P61823   RNAS1_BOVIN     27    150             
DBREF  1F0V D  601   724  UNP    P61823   RNAS1_BOVIN     27    150             
DBREF  1F0V M  751   752  PDB    1F0V     1F0V           751    752             
DBREF  1F0V N  753   754  PDB    1F0V     1F0V           753    754             
DBREF  1F0V O  755   756  PDB    1F0V     1F0V           755    756             
DBREF  1F0V P  757   758  PDB    1F0V     1F0V           757    758             
SEQRES   1 M    2   DC  DG                                                      
SEQRES   1 N    2   DC  DG                                                      
SEQRES   1 O    2   DC  DG                                                      
SEQRES   1 P    2   DC  DG                                                      
SEQRES   1 A  124  LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET          
SEQRES   2 A  124  ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS          
SEQRES   3 A  124  ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG          
SEQRES   4 A  124  CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA          
SEQRES   5 A  124  ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS          
SEQRES   6 A  124  LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR          
SEQRES   7 A  124  MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS          
SEQRES   8 A  124  TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS          
SEQRES   9 A  124  HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO          
SEQRES  10 A  124  VAL HIS PHE ASP ALA SER VAL                                  
SEQRES   1 B  124  LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET          
SEQRES   2 B  124  ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS          
SEQRES   3 B  124  ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG          
SEQRES   4 B  124  CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA          
SEQRES   5 B  124  ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS          
SEQRES   6 B  124  LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR          
SEQRES   7 B  124  MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS          
SEQRES   8 B  124  TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS          
SEQRES   9 B  124  HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO          
SEQRES  10 B  124  VAL HIS PHE ASP ALA SER VAL                                  
SEQRES   1 C  124  LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET          
SEQRES   2 C  124  ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS          
SEQRES   3 C  124  ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG          
SEQRES   4 C  124  CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA          
SEQRES   5 C  124  ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS          
SEQRES   6 C  124  LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR          
SEQRES   7 C  124  MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS          
SEQRES   8 C  124  TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS          
SEQRES   9 C  124  HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO          
SEQRES  10 C  124  VAL HIS PHE ASP ALA SER VAL                                  
SEQRES   1 D  124  LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET          
SEQRES   2 D  124  ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS          
SEQRES   3 D  124  ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG          
SEQRES   4 D  124  CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA          
SEQRES   5 D  124  ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS          
SEQRES   6 D  124  LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR          
SEQRES   7 D  124  MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS          
SEQRES   8 D  124  TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS          
SEQRES   9 D  124  HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO          
SEQRES  10 D  124  VAL HIS PHE ASP ALA SER VAL                                  
HET    PO4  A 801       5                                                       
HET    PO4  B 802       5                                                       
HET    PO4  C 803       5                                                       
HET    PO4  P 804       5                                                       
HET    GOL  D 901       6                                                       
HET    GOL  B 902       6                                                       
HET    GOL  C 903       6                                                       
HET    GOL  A 904       6                                                       
HET    GOL  B 905       6                                                       
HET    GOL  B 906       6                                                       
HET    GOL  B 907       6                                                       
HET    GOL  A 908       6                                                       
HET    GOL  D 909       6                                                       
HET    GOL  B 910       6                                                       
HET    GOL  A 911       6                                                       
HET    GOL  C 912       6                                                       
HET    GOL  D 913       6                                                       
HET    GOL  B 914       6                                                       
HET    GOL  A 915       6                                                       
HET    GOL  D 916       6                                                       
HET    GOL  C 917       6                                                       
HET    GOL  A 918       6                                                       
HET    GOL  C 919       6                                                       
HET    GOL  B 920       6                                                       
HET    GOL  B 921       6                                                       
HET    GOL  B 922       6                                                       
HET    GOL  A 923       6                                                       
HET    GOL  D 924       6                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   9  PO4    4(O4 P 3-)                                                   
FORMUL  13  GOL    24(C3 H8 O3)                                                 
FORMUL  37  HOH   *554(H2 O)                                                    
HELIX    1   1 THR A    3  MET A   13  1                                  11    
HELIX    2   2 ASN A   24  ARG A   33  1                                  10    
HELIX    3   3 SER A   50  VAL A   57  1                                   8    
HELIX    4   4 CYS A   58  GLN A   60  5                                   3    
HELIX    5   5 THR B  203  MET B  213  1                                  11    
HELIX    6   6 ASN B  224  ARG B  233  1                                  10    
HELIX    7   7 SER B  250  VAL B  257  1                                   8    
HELIX    8   8 CYS B  258  GLN B  260  5                                   3    
HELIX    9   9 THR C  403  MET C  413  1                                  11    
HELIX   10  10 ASN C  424  ARG C  433  1                                  10    
HELIX   11  11 SER C  450  VAL C  457  1                                   8    
HELIX   12  12 CYS C  458  GLN C  460  5                                   3    
HELIX   13  13 THR D  603  MET D  613  1                                  11    
HELIX   14  14 ASN D  624  ARG D  633  1                                  10    
HELIX   15  15 SER D  650  ALA D  656  1                                   7    
HELIX   16  16 VAL D  657  GLN D  660  5                                   4    
SHEET    1   A 3 VAL A  43  VAL A  47  0                                        
SHEET    2   A 3 MET A  79  GLU A  86 -1  O  THR A  82   N  PHE A  46           
SHEET    3   A 3 TYR A  97  LYS A 104 -1  N  LYS A  98   O  ARG A  85           
SHEET    1   B 6 LYS A  61  VAL A  63  0                                        
SHEET    2   B 6 CYS A  72  GLN A  74 -1  O  CYS A  72   N  VAL A  63           
SHEET    3   B 6 ILE A 106  VAL A 124 -1  O  VAL A 108   N  TYR A  73           
SHEET    4   B 6 TYR B 297  SER B 323 -1  N  HIS B 305   O  VAL A 124           
SHEET    5   B 6 CYS B 272  GLN B 274 -1  N  TYR B 273   O  VAL B 308           
SHEET    6   B 6 LYS B 261  VAL B 263 -1  O  LYS B 261   N  GLN B 274           
SHEET    1   C 6 LYS A  61  VAL A  63  0                                        
SHEET    2   C 6 CYS A  72  GLN A  74 -1  O  CYS A  72   N  VAL A  63           
SHEET    3   C 6 ILE A 106  VAL A 124 -1  O  VAL A 108   N  TYR A  73           
SHEET    4   C 6 TYR B 297  SER B 323 -1  N  HIS B 305   O  VAL A 124           
SHEET    5   C 6 MET B 279  GLU B 286 -1  N  MET B 279   O  LYS B 304           
SHEET    6   C 6 VAL B 243  VAL B 247 -1  O  ASN B 244   N  CYS B 284           
SHEET    1   D 6 LYS D 661  VAL D 663  0                                        
SHEET    2   D 6 CYS D 672  GLN D 674 -1  O  CYS D 672   N  VAL D 663           
SHEET    3   D 6 ILE D 706  VAL D 724 -1  N  VAL D 708   O  TYR D 673           
SHEET    4   D 6 TYR C 497  SER C 523 -1  N  HIS C 505   O  VAL D 724           
SHEET    5   D 6 CYS C 472  GLN C 474 -1  N  TYR C 473   O  VAL C 508           
SHEET    6   D 6 LYS C 461  VAL C 463 -1  O  LYS C 461   N  GLN C 474           
SHEET    1   E 6 LYS D 661  VAL D 663  0                                        
SHEET    2   E 6 CYS D 672  GLN D 674 -1  O  CYS D 672   N  VAL D 663           
SHEET    3   E 6 ILE D 706  VAL D 724 -1  N  VAL D 708   O  TYR D 673           
SHEET    4   E 6 TYR C 497  SER C 523 -1  N  HIS C 505   O  VAL D 724           
SHEET    5   E 6 MET C 479  GLU C 486 -1  N  MET C 479   O  LYS C 504           
SHEET    6   E 6 VAL C 443  VAL C 447 -1  N  ASN C 444   O  CYS C 484           
SHEET    1   F 3 VAL D 643  VAL D 647  0                                        
SHEET    2   F 3 MET D 679  GLU D 686 -1  N  THR D 682   O  PHE D 646           
SHEET    3   F 3 TYR D 697  LYS D 704 -1  N  LYS D 698   O  ARG D 685           
SSBOND   1 CYS A   26    CYS A   84                          1555   1555  2.08  
SSBOND   2 CYS A   40    CYS A   95                          1555   1555  2.06  
SSBOND   3 CYS A   58    CYS A  110                          1555   1555  2.09  
SSBOND   4 CYS A   65    CYS A   72                          1555   1555  2.08  
SSBOND   5 CYS B  226    CYS B  284                          1555   1555  2.08  
SSBOND   6 CYS B  240    CYS B  295                          1555   1555  2.04  
SSBOND   7 CYS B  258    CYS B  310                          1555   1555  2.12  
SSBOND   8 CYS B  265    CYS B  272                          1555   1555  2.11  
SSBOND   9 CYS C  426    CYS C  484                          1555   1555  2.09  
SSBOND  10 CYS C  440    CYS C  495                          1555   1555  2.06  
SSBOND  11 CYS C  458    CYS C  510                          1555   1555  2.08  
SSBOND  12 CYS C  465    CYS C  472                          1555   1555  2.08  
SSBOND  13 CYS D  626    CYS D  684                          1555   1555  2.06  
SSBOND  14 CYS D  640    CYS D  695                          1555   1555  2.02  
SSBOND  15 CYS D  658    CYS D  710                          1555   1555  2.10  
SSBOND  16 CYS D  665    CYS D  672                          1555   1555  2.09  
CISPEP   1 TYR A   92    PRO A   93          0         0.69                     
CISPEP   2 TYR B  292    PRO B  293          0         1.06                     
CISPEP   3 TYR C  492    PRO C  493          0         0.01                     
CISPEP   4 TYR D  692    PRO D  693          0        -0.53                     
SITE     1 AC1  9 GLN A  11  HIS A  12  LYS A  41  HOH A1004                    
SITE     2 AC1  9 HOH A1252  HOH A1553  HIS B 319  PHE B 320                    
SITE     3 AC1  9  DG M 752                                                     
SITE     1 AC2 10 HIS A 119  PHE A 120  GLN B 211  HIS B 212                    
SITE     2 AC2 10 LYS B 241  HOH B1074  HOH B1396  HOH B1554                    
SITE     3 AC2 10 HOH B1555   DG N 754                                          
SITE     1 AC3  8 GLN C 411  HIS C 412  LYS C 441  HOH C1045                    
SITE     2 AC3  8 HOH C1571  HIS D 719  PHE D 720   DG O 756                    
SITE     1 AC4  8 HIS C 519  PHE C 520  GLN D 611  HIS D 612                    
SITE     2 AC4  8 LYS D 641   DG P 758  HOH P1029  HOH P1273                    
SITE     1 AC5  9 ALA C 405  GLU C 511  ASN D 713  PRO D 714                    
SITE     2 AC5  9 HOH D1051  HOH D1254  HOH D1355  HOH D1575                    
SITE     3 AC5  9 HOH D1576                                                     
SITE     1 AC6  4 GLN B 301  ALA B 302  ASN B 303  HOH B1442                    
SITE     1 AC7  2 PRO C 442  HOH C1179                                          
SITE     1 AC8  2 GLN A  69  THR A  70                                          
SITE     1 AC9  7 GLU B 202  ALA B 206  GLU B 209  ARG B 210                    
SITE     2 AC9  7 GOL B 922  HOH B1307  HOH B1514                               
SITE     1 BC1  4 SER B 223  THR B 299  THR B 300  GLN B 301                    
SITE     1 BC2  6 VAL A 124  VAL B 263  ALA B 264  GLN B 274                    
SITE     2 BC2  6 ILE B 307  HOH B1192                                          
SITE     1 BC3  3 SER A  50  ALA A  52  ASP A  53                               
SITE     1 BC4  6 GLU D 711  GLY D 712  ASN D 713  HOH D1303                    
SITE     2 BC4  6 HOH D1581  HOH D1582                                          
SITE     1 BC5  9 ASN A 113  PRO A 114  VAL A 116  GLU B 311                    
SITE     2 BC5  9 GLY B 312  ASN B 313  GOL B 920  HOH B1056                    
SITE     3 BC5  9 HOH B1123                                                     
SITE     1 BC6  2 ASN C 503  GOL C 912                                          
SITE     1 BC7  5 THR A  78  GOL A 911  THR C 478  ASN C 503                    
SITE     2 BC7  5 HOH C1157                                                     
SITE     1 BC8  4 GLN D 701  ALA D 702  ASN D 703  HOH D1509                    
SITE     1 BC9  4 ARG B 239  CYS B 240  LYS B 241  PRO B 242                    
SITE     1 CC1  3 ARG A  39  PRO A  42  HOH A1330                               
SITE     1 CC2  5 SER D 623  THR D 699  THR D 700  GLN D 701                    
SITE     2 CC2  5 HOH D1281                                                     
SITE     1 CC3  4 SER C 422  THR C 499  THR C 500  GLN C 501                    
SITE     1 CC4  3 SER A  23  THR A  99  HOH A1062                               
SITE     1 CC5  3 SER C 450  ASP C 453  HOH C1437                               
SITE     1 CC6  6 ALA B 204  GLU B 311  ASN B 313  GOL B 910                    
SITE     2 CC6  6 HOH B1332  HOH B1494                                          
SITE     1 CC7  6 ALA B 256  SER B 259  GLN B 260  HOH B1010                    
SITE     2 CC7  6 HOH B1348  HOH B1431                                          
SITE     1 CC8  5 GLU B 202  ARG B 210  ASN B 234  GOL B 905                    
SITE     2 CC8  5 HOH B1269                                                     
SITE     1 CC9  5 SER A  77  HOH A1140  HOH A1579  THR C 478                    
SITE     2 CC9  5 HIS C 505                                                     
SITE     1 DC1  4 ASP D 653  ALA D 656  HOH D1021  HOH D1028                    
CRYST1   83.569   96.341   48.240  90.00 107.50  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011966  0.000000  0.003773        0.00000                         
SCALE2      0.000000  0.010380  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021736        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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