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Database: PDB
Entry: 4M9V
LinkDB: 4M9V
Original site: 4M9V 
HEADER    TRANSCRIPTION/DNA                       15-AUG-13   4M9V              
TITLE     ZFP57 MUTANT (E182Q) IN COMPLEX WITH 5-CARBOXYLCYTOSINE DNA           
CAVEAT     4M9V    CHIRALITY ERROR AT C4 OF MPD B 101, C 203, E 101 AND F 203   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (5'-D(*TP*AP*TP*TP*GP*CP*(5CM)P*GP*CP*AP*G)-3');       
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: DNA (5'-D(*AP*CP*TP*GP*(1CC)P*GP*GP*CP*AP*AP*T)-3');       
COMPND   7 CHAIN: B, E;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: ZINC FINGER PROTEIN 57;                                    
COMPND  11 CHAIN: C, F;                                                         
COMPND  12 SYNONYM: ZFP-57;                                                     
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 OTHER_DETAILS: DNA SYNTHESIS;                                        
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 SYNTHETIC: YES;                                                      
SOURCE   6 OTHER_DETAILS: DNA SYNTHESIS;                                        
SOURCE   7 MOL_ID: 3;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   9 ORGANISM_COMMON: MOUSE;                                              
SOURCE  10 ORGANISM_TAXID: 10090;                                               
SOURCE  11 GENE: ZFP57;                                                         
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PXC1158                                   
KEYWDS    EPIGENETICS, TRANSCRIPTION FACTOR, 5-CARBOXYLCYTOSINE, C2H2 ZINC      
KEYWDS   2 FINGER, DNA BINDING, TRANSCRIPTION-DNA COMPLEX                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.LIU,Y.O.OLANREWAJU,X.ZHANG,X.CHENG                                  
REVDAT   3   24-JUN-20 4M9V    1       REMARK SEQADV LINK   ATOM                
REVDAT   2   22-JAN-14 4M9V    1       JRNL                                     
REVDAT   1   27-NOV-13 4M9V    0                                                
JRNL        AUTH   Y.LIU,Y.O.OLANREWAJU,X.ZHANG,X.CHENG                         
JRNL        TITL   DNA RECOGNITION OF 5-CARBOXYLCYTOSINE BY A ZFP57 MUTANT AT   
JRNL        TITL 2 AN ATOMIC RESOLUTION OF 0.97 ANGSTROM.                       
JRNL        REF    BIOCHEMISTRY                  V.  52  9310 2013              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   24236546                                                     
JRNL        DOI    10.1021/BI401360N                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    0.97 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.46                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 129906                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.131                           
REMARK   3   R VALUE            (WORKING SET) : 0.130                           
REMARK   3   FREE R VALUE                     : 0.143                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6543                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 33.4792 -  3.0088    0.92     3996   224  0.1366 0.1451        
REMARK   3     2  3.0088 -  2.3884    0.96     4182   215  0.1450 0.1345        
REMARK   3     3  2.3884 -  2.0865    0.97     4203   199  0.1306 0.1507        
REMARK   3     4  2.0865 -  1.8958    0.97     4125   249  0.1228 0.1333        
REMARK   3     5  1.8958 -  1.7599    0.97     4187   209  0.1120 0.1284        
REMARK   3     6  1.7599 -  1.6561    0.97     4121   244  0.1044 0.1161        
REMARK   3     7  1.6561 -  1.5732    0.97     4186   226  0.0990 0.1239        
REMARK   3     8  1.5732 -  1.5047    0.98     4213   198  0.1067 0.1201        
REMARK   3     9  1.5047 -  1.4468    0.97     4168   256  0.1027 0.1150        
REMARK   3    10  1.4468 -  1.3969    0.98     4222   203  0.1020 0.1433        
REMARK   3    11  1.3969 -  1.3532    0.98     4208   220  0.1051 0.1265        
REMARK   3    12  1.3532 -  1.3145    0.97     4182   258  0.1086 0.1253        
REMARK   3    13  1.3145 -  1.2799    0.97     4169   216  0.1101 0.1288        
REMARK   3    14  1.2799 -  1.2487    0.97     4127   235  0.1107 0.1253        
REMARK   3    15  1.2487 -  1.2203    0.97     4122   248  0.1187 0.1453        
REMARK   3    16  1.2203 -  1.1943    0.95     4153   211  0.1181 0.1361        
REMARK   3    17  1.1943 -  1.1704    0.97     4124   200  0.1230 0.1399        
REMARK   3    18  1.1704 -  1.1483    0.96     4128   215  0.1284 0.1502        
REMARK   3    19  1.1483 -  1.1278    0.96     4144   211  0.1297 0.1493        
REMARK   3    20  1.1278 -  1.1087    0.96     4104   213  0.1327 0.1444        
REMARK   3    21  1.1087 -  1.0908    0.95     4145   207  0.1416 0.1527        
REMARK   3    22  1.0908 -  1.0740    0.95     4064   221  0.1482 0.1596        
REMARK   3    23  1.0740 -  1.0582    0.95     4086   205  0.1600 0.1670        
REMARK   3    24  1.0582 -  1.0433    0.95     4122   185  0.1745 0.2038        
REMARK   3    25  1.0433 -  1.0292    0.95     4035   209  0.1909 0.2224        
REMARK   3    26  1.0292 -  1.0159    0.95     4071   226  0.2119 0.2305        
REMARK   3    27  1.0159 -  1.0032    0.95     4025   220  0.2408 0.2518        
REMARK   3    28  1.0032 -  0.9911    0.95     4125   204  0.2550 0.2703        
REMARK   3    29  0.9911 -  0.9796    0.93     3945   207  0.2610 0.2862        
REMARK   3    30  0.9796 -  0.9685    0.84     3681   209  0.2851 0.2821        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.080            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.110           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 8.63                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.70                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           2197                                  
REMARK   3   ANGLE     :  1.815           3190                                  
REMARK   3   CHIRALITY :  0.085            338                                  
REMARK   3   PLANARITY :  0.010            252                                  
REMARK   3   DIHEDRAL  : 26.406            919                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: FLAT BULK SOLVENT MODEL                   
REMARK   4                                                                      
REMARK   4 4M9V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000081648.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8                                
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL - LIQUID NITROGEN   
REMARK 200                                   COOLED                             
REMARK 200  OPTICS                         : SI 111. ROSENBAUM-ROCK DOUBLE      
REMARK 200                                   -CRYSTAL MONOCHROMATOR: LIQUID     
REMARK 200                                   NITROGEN COOLED; SAGITALLY         
REMARK 200                                   FOCUSING 2ND CRYSTAL, ROSENBAUM-   
REMARK 200                                   ROCK VERTICAL FOCUSING MIRROR      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 129957                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.969                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.97                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4GZN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% 2-METHYL-2,4-PENTANEDIOL, 15%        
REMARK 280  POLYETHYLENE GLYCOL 8000, 100 MM CACL2, AND 100 MM ACETATE, PH      
REMARK 280  4.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K                
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       48.04650            
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                                                 
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4790 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7010 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7030 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10240 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 13370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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     LEU C   134                                                      
REMARK 465     GLY C   135                                                      
REMARK 465     ALA C   195                                                      
REMARK 465     LEU F   134                                                      
REMARK 465     GLY F   135                                                      
REMARK 465     ALA F   195                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLY C 132    N    CA                                             
REMARK 470     SER C 136    OG                                                  
REMARK 470     GLU C 137    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 193    CG   CD   CE   NZ                                   
REMARK 470     PRO C 194    C    O    CB   CG   CD                              
REMARK 470     GLY F 132    N    CA                                             
REMARK 470     GLU F 137    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 193    CG   CD   CE   NZ                                   
REMARK 470     PRO F 194    O    CB   CG   CD                                   
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   OP2   DC B     2     O    HOH B   244              1.93            
REMARK 500   O    HOH B   238     O    HOH C   336              1.94            
REMARK 500   OP2   DC E     2     O    HOH E   263              1.95            
REMARK 500   O    HOH E   250     O    HOH F   342              1.95            
REMARK 500   O    HOH D   120     O    HOH E   259              2.02            
REMARK 500   O    HOH E   250     O    HOH E   278              2.05            
REMARK 500   O    HOH F   379     O    HOH F   395              2.11            
REMARK 500   O    HOH C   338     O    HOH C   391              2.12            
REMARK 500   O    HOH F   357     O    HOH F   394              2.12            
REMARK 500   OP1   DG A     5     O    HOH A   145              2.15            
REMARK 500   O    HOH E   248     O    HOH E   251              2.16            
REMARK 500   OXT  ACT B   102     O    HOH B   265              2.18            
REMARK 500   O    HOH C   364     O    HOH C   384              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   OE2  GLU C   172     O    HOH F   393     1556     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DT A   3   O3'    DT A   3   C3'    -0.054                       
REMARK 500     DT A   4   O3'    DT A   4   C3'    -0.040                       
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     DT A   1   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DT A   3   O5' -  C5' -  C4' ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DT A   3   O4' -  C1' -  C2' ANGL. DEV. =   3.7 DEGREES          
REMARK 500     DT A   4   C3' -  C2' -  C1' ANGL. DEV. =  -7.7 DEGREES          
REMARK 500     DG A  11   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DT B  11   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DT D   3   O4' -  C4' -  C3' ANGL. DEV. =   5.0 DEGREES          
REMARK 500     DT D   4   C3' -  C2' -  C1' ANGL. DEV. =  -7.1 DEGREES          
REMARK 500     DT D   4   O4' -  C1' -  N1  ANGL. DEV. =   3.1 DEGREES          
REMARK 500     DT D   4   O4' -  C1' -  N1  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     DG D  11   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES          
REMARK 500     DT E  11   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
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 A 144        DISTANCE =  6.01 ANGSTROMS                       
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                              ZN F 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F 162   NE2                                                    
REMARK 620 2 HIS F 158   NE2  95.0                                              
REMARK 620 3 CYS F 145   SG  121.8 104.1                                        
REMARK 620 4 CYS F 142   SG  108.0 105.3 118.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 158   NE2                                                    
REMARK 620 2 HIS C 162   NE2  94.2                                              
REMARK 620 3 CYS C 145   SG  105.2 122.0                                        
REMARK 620 4 CYS C 142   SG  105.6 107.2 118.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F 190   NE2                                                    
REMARK 620 2 HIS F 186   NE2 107.5                                              
REMARK 620 3 CYS F 173   SG  112.8 106.7                                        
REMARK 620 4 CYS F 170   SG  109.1 105.3 114.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 186   NE2                                                    
REMARK 620 2 HIS C 190   NE2 108.8                                              
REMARK 620 3 CYS C 173   SG  106.3 112.2                                        
REMARK 620 4 CYS C 170   SG  105.6 109.2 114.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 103  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH E 281   O                                                      
REMARK 620 2 HOH D 146   O   165.4                                              
REMARK 620 3 HOH E 206   O    97.7  87.0                                        
REMARK 620 4 HOH D 145   O   109.9  77.0 128.5                                  
REMARK 620 5 HOH D 147   O    81.7  87.3 150.2  78.3                            
REMARK 620 6 HOH E 280   O    87.0  81.2  72.3 148.3  77.9                      
REMARK 620 7 HOH E 279   O    80.0 114.6  73.4  69.9 134.9 141.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 103  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 271   O                                                      
REMARK 620 2 HOH A 159   O   165.5                                              
REMARK 620 3 HOH B 268   O    97.7  87.7                                        
REMARK 620 4 HOH B 270   O    86.8  82.0  72.7                                  
REMARK 620 5 HOH A 160   O    81.6  87.1 151.0  78.3                            
REMARK 620 6 HOH A 161   O   110.2  76.1 128.0 148.3  78.1                      
REMARK 620 7 HOH B 269   O    80.9 113.6  72.5 141.0 135.1  69.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 103                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD C 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 103                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD F 203                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4GZN   RELATED DB: PDB                                   
REMARK 900 MOUSE ZFP57 ZINC FINGERS IN COMPLEX WITH METHYLATED DNA              
DBREF  4M9V C  137   195  UNP    Q8C6P8   ZFP57_MOUSE    137    195             
DBREF  4M9V F  137   195  UNP    Q8C6P8   ZFP57_MOUSE    137    195             
DBREF  4M9V A    1    11  PDB    4M9V     4M9V             1     11             
DBREF  4M9V D    1    11  PDB    4M9V     4M9V             1     11             
DBREF  4M9V B    1    11  PDB    4M9V     4M9V             1     11             
DBREF  4M9V E    1    11  PDB    4M9V     4M9V             1     11             
SEQADV 4M9V GLY C  132  UNP  Q8C6P8              EXPRESSION TAG                 
SEQADV 4M9V PRO C  133  UNP  Q8C6P8              EXPRESSION TAG                 
SEQADV 4M9V LEU C  134  UNP  Q8C6P8              EXPRESSION TAG                 
SEQADV 4M9V GLY C  135  UNP  Q8C6P8              EXPRESSION TAG                 
SEQADV 4M9V SER C  136  UNP  Q8C6P8              EXPRESSION TAG                 
SEQADV 4M9V GLN C  182  UNP  Q8C6P8    GLU   182 ENGINEERED MUTATION            
SEQADV 4M9V GLY F  132  UNP  Q8C6P8              EXPRESSION TAG                 
SEQADV 4M9V PRO F  133  UNP  Q8C6P8              EXPRESSION TAG                 
SEQADV 4M9V LEU F  134  UNP  Q8C6P8              EXPRESSION TAG                 
SEQADV 4M9V GLY F  135  UNP  Q8C6P8              EXPRESSION TAG                 
SEQADV 4M9V SER F  136  UNP  Q8C6P8              EXPRESSION TAG                 
SEQADV 4M9V GLN F  182  UNP  Q8C6P8    GLU   182 ENGINEERED MUTATION            
SEQRES   1 A   11   DT  DA  DT  DT  DG  DC 5CM  DG  DC  DA  DG                  
SEQRES   1 B   11   DA  DC  DT  DG 1CC  DG  DG  DC  DA  DA  DT                  
SEQRES   1 C   64  GLY PRO LEU GLY SER GLU ARG PRO PHE PHE CYS ASN PHE          
SEQRES   2 C   64  CYS GLY LYS THR TYR ARG ASP ALA SER GLY LEU SER ARG          
SEQRES   3 C   64  HIS ARG ARG ALA HIS LEU GLY TYR ARG PRO ARG SER CYS          
SEQRES   4 C   64  PRO GLU CYS GLY LYS CYS PHE ARG ASP GLN SER GLN VAL          
SEQRES   5 C   64  ASN ARG HIS LEU LYS VAL HIS GLN ASN LYS PRO ALA              
SEQRES   1 D   11   DT  DA  DT  DT  DG  DC 5CM  DG  DC  DA  DG                  
SEQRES   1 E   11   DA  DC  DT  DG 1CC  DG  DG  DC  DA  DA  DT                  
SEQRES   1 F   64  GLY PRO LEU GLY SER GLU ARG PRO PHE PHE CYS ASN PHE          
SEQRES   2 F   64  CYS GLY LYS THR TYR ARG ASP ALA SER GLY LEU SER ARG          
SEQRES   3 F   64  HIS ARG ARG ALA HIS LEU GLY TYR ARG PRO ARG SER CYS          
SEQRES   4 F   64  PRO GLU CYS GLY LYS CYS PHE ARG ASP GLN SER GLN VAL          
SEQRES   5 F   64  ASN ARG HIS LEU LYS VAL HIS GLN ASN LYS PRO ALA              
MODRES 4M9V 5CM A    7   DC                                                     
MODRES 4M9V 1CC B    5   DC                                                     
MODRES 4M9V 5CM D    7   DC                                                     
MODRES 4M9V 1CC E    5   DC                                                     
HET    5CM  A   7      33                                                       
HET    1CC  B   5      32                                                       
HET    5CM  D   7      33                                                       
HET    1CC  E   5      32                                                       
HET    MPD  B 101      22                                                       
HET    ACT  B 102       7                                                       
HET     CA  B 103       1                                                       
HET     ZN  C 201       1                                                       
HET     ZN  C 202       1                                                       
HET    MPD  C 203      22                                                       
HET    ACT  C 204       7                                                       
HET    ACT  C 205       7                                                       
HET    MPD  E 101      22                                                       
HET    ACT  E 102       7                                                       
HET     CA  E 103       1                                                       
HET     ZN  F 201       1                                                       
HET     ZN  F 202       1                                                       
HET    MPD  F 203      22                                                       
HETNAM     5CM 5-METHYL-2'-DEOXY-CYTIDINE-5'-MONOPHOSPHATE                      
HETNAM     1CC 5-CARBOXY-2'-DEOXYCYTIDINE MONOPHOSPHATE                         
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETNAM     ACT ACETATE ION                                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM      ZN ZINC ION                                                         
FORMUL   1  5CM    2(C10 H16 N3 O7 P)                                           
FORMUL   2  1CC    2(C10 H14 N3 O9 P)                                           
FORMUL   7  MPD    4(C6 H14 O2)                                                 
FORMUL   8  ACT    4(C2 H3 O2 1-)                                               
FORMUL   9   CA    2(CA 2+)                                                     
FORMUL  10   ZN    4(ZN 2+)                                                     
FORMUL  21  HOH   *472(H2 O)                                                    
HELIX    1   1 ASP C  151  GLY C  164  1                                  14    
HELIX    2   2 ASP C  179  LEU C  187  1                                   9    
HELIX    3   3 LYS C  188  GLN C  191  5                                   4    
HELIX    4   4 ASP F  151  GLY F  164  1                                  14    
HELIX    5   5 ASP F  179  LEU F  187  1                                   9    
HELIX    6   6 LYS F  188  GLN F  191  5                                   4    
SHEET    1   A 2 PHE C 140  PHE C 141  0                                        
SHEET    2   A 2 THR C 148  TYR C 149 -1  O  TYR C 149   N  PHE C 140           
SHEET    1   B 2 ARG C 168  SER C 169  0                                        
SHEET    2   B 2 CYS C 176  PHE C 177 -1  O  PHE C 177   N  ARG C 168           
SHEET    1   C 2 PHE F 140  PHE F 141  0                                        
SHEET    2   C 2 THR F 148  TYR F 149 -1  O  TYR F 149   N  PHE F 140           
SHEET    1   D 2 ARG F 168  SER F 169  0                                        
SHEET    2   D 2 CYS F 176  PHE F 177 -1  O  PHE F 177   N  ARG F 168           
LINK         O3'  DC A   6                 P   5CM A   7     1555   1555  1.60  
LINK         O3' 5CM A   7                 P    DG A   8     1555   1555  1.60  
LINK         O3'  DG B   4                 P   1CC B   5     1555   1555  1.61  
LINK         O3'  DC D   6                 P   5CM D   7     1555   1555  1.60  
LINK         O3' 5CM D   7                 P    DG D   8     1555   1555  1.61  
LINK         O3'  DG E   4                 P   1CC E   5     1555   1555  1.61  
LINK         NE2 HIS F 162                ZN    ZN F 202     1555   1555  2.01  
LINK         NE2 HIS C 158                ZN    ZN C 202     1555   1555  2.03  
LINK         NE2 HIS C 162                ZN    ZN C 202     1555   1555  2.03  
LINK         NE2 HIS F 190                ZN    ZN F 201     1555   1555  2.03  
LINK         NE2 HIS C 186                ZN    ZN C 201     1555   1555  2.04  
LINK         NE2 HIS C 190                ZN    ZN C 201     1555   1555  2.04  
LINK         NE2 HIS F 158                ZN    ZN F 202     1555   1555  2.05  
LINK         NE2 HIS F 186                ZN    ZN F 201     1555   1555  2.06  
LINK         SG  CYS C 145                ZN    ZN C 202     1555   1555  2.26  
LINK         SG  CYS F 145                ZN    ZN F 202     1555   1555  2.27  
LINK         SG  CYS F 173                ZN    ZN F 201     1555   1555  2.29  
LINK         SG  CYS C 173                ZN    ZN C 201     1555   1555  2.30  
LINK         SG  CYS F 170                ZN    ZN F 201     1555   1555  2.31  
LINK         SG  CYS C 170                ZN    ZN C 201     1555   1555  2.31  
LINK         SG  CYS C 142                ZN    ZN C 202     1555   1555  2.32  
LINK         SG  CYS F 142                ZN    ZN F 202     1555   1555  2.32  
LINK        CA    CA E 103                 O   HOH E 281     1555   1555  2.34  
LINK        CA    CA B 103                 O   HOH B 271     1555   1555  2.34  
LINK        CA    CA B 103                 O   HOH A 159     1555   1555  2.38  
LINK        CA    CA E 103                 O   HOH D 146     1555   1555  2.38  
LINK        CA    CA E 103                 O   HOH E 206     1555   1555  2.40  
LINK        CA    CA B 103                 O   HOH B 268     1555   1555  2.41  
LINK        CA    CA B 103                 O   HOH B 270     1555   1555  2.42  
LINK        CA    CA B 103                 O   HOH A 160     1555   1555  2.42  
LINK        CA    CA E 103                 O   HOH D 145     1555   1555  2.42  
LINK        CA    CA E 103                 O   HOH D 147     1555   1555  2.42  
LINK        CA    CA E 103                 O   HOH E 280     1555   1555  2.43  
LINK        CA    CA B 103                 O   HOH A 161     1555   1555  2.43  
LINK        CA    CA E 103                 O   HOH E 279     1555   1555  2.45  
LINK        CA    CA B 103                 O   HOH B 269     1555   1555  2.45  
LINK         O3' 1CC B   5                 P    DG B   6     1555   1555  1.60  
LINK         O3' 1CC E   5                 P    DG E   6     1555   1555  1.61  
SITE     1 AC1  9 1CC B   5  HOH B 276  HIS C 158  ALA C 161                    
SITE     2 AC1  9 HOH C 350  MPD E 101  ALA F 161  HIS F 162                    
SITE     3 AC1  9 GLY F 164                                                     
SITE     1 AC2  9 HOH A 139  HOH A 158   DA B  10   DT B  11                    
SITE     2 AC2  9 HOH B 241  HOH B 243  HOH B 264  HOH B 265                    
SITE     3 AC2  9 HOH B 272                                                     
SITE     1 AC3  7 HOH A 159  HOH A 160  HOH A 161  HOH B 268                    
SITE     2 AC3  7 HOH B 269  HOH B 270  HOH B 271                               
SITE     1 AC4  4 CYS C 170  CYS C 173  HIS C 186  HIS C 190                    
SITE     1 AC5  5 CYS C 142  PHE C 144  CYS C 145  HIS C 158                    
SITE     2 AC5  5 HIS C 162                                                     
SITE     1 AC6  5 PHE C 141  ASN C 184  HOH C 344  HOH C 347                    
SITE     2 AC6  5 HOH C 358                                                     
SITE     1 AC7  6 HOH A 109  LEU C 163  TYR C 165  HOH C 390                    
SITE     2 AC7  6 HIS F 190  HOH F 372                                          
SITE     1 AC8  5 HIS C 190  HOH C 388  HOH D 143  TYR F 165                    
SITE     2 AC8  5 HOH F 393                                                     
SITE     1 AC9  9 MPD B 101  ALA C 161  HIS C 162  GLY C 164                    
SITE     2 AC9  9 HOH C 385  HOH C 393  1CC E   5  HIS F 158                    
SITE     3 AC9  9 ALA F 161                                                     
SITE     1 BC1  5 HOH D 132   DA E  10   DT E  11  HOH E 256                    
SITE     2 BC1  5 HOH E 277                                                     
SITE     1 BC2  7 HOH D 145  HOH D 146  HOH D 147  HOH E 206                    
SITE     2 BC2  7 HOH E 279  HOH E 280  HOH E 281                               
SITE     1 BC3  4 CYS F 170  CYS F 173  HIS F 186  HIS F 190                    
SITE     1 BC4  5 CYS F 142  PHE F 144  CYS F 145  HIS F 158                    
SITE     2 BC4  5 HIS F 162                                                     
SITE     1 BC5  6 HOH D 133  PHE F 141  ASN F 184  HOH F 345                    
SITE     2 BC5  6 HOH F 360  HOH F 374                                          
CRYST1   36.388   96.093   36.408  90.00 113.14  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.027482  0.000000  0.011745        0.00000                         
SCALE2      0.000000  0.010407  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.029870        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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