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Database: PDB
Entry: 4WB3
LinkDB: 4WB3
Original site: 4WB3 
HEADER    DNA-RNA HYBRID                          02-SEP-14   4WB3              
TITLE     CRYSTAL STRUCTURE OF THE MIRROR-IMAGE L-RNA/L-DNA APTAMER NOX-D20 IN  
TITLE    2 COMPLEX WITH MOUSE C5A-DESARG COMPLEMENT ANAPHYLATOXIN               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COMPLEMENT C5;                                             
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: HEMOLYTIC COMPLEMENT;                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: MIXED L-RNA/L-DNA APTAMER NOX-D20 (40-MER);                
COMPND   8 CHAIN: D, E;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: C5, HC;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SHUFFLE T7 EXPRESS;                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET32A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  14 ORGANISM_TAXID: 32630                                                
KEYWDS    PROTEIN-RNA COMPLEX, MIRROR-IMAGE APTAMER, G-QUADRUPLEX, COMPLEMENT   
KEYWDS   2 ANAPHYLATOXIN, DNA-RNA HYBRID                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.YATIME,C.MAASCH,K.HOEHLIG,S.KLUSSMANN,A.VATER,G.R.ANDERSEN          
REVDAT   2   17-JAN-18 4WB3    1       REMARK                                   
REVDAT   1   06-MAY-15 4WB3    0                                                
JRNL        AUTH   L.YATIME,C.MAASCH,K.HOEHLIG,S.KLUSSMANN,G.R.ANDERSEN,A.VATER 
JRNL        TITL   STRUCTURAL BASIS FOR THE TARGETING OF COMPLEMENT             
JRNL        TITL 2 ANAPHYLATOXIN C5A USING A MIXED L-RNA/L-DNA APTAMER.         
JRNL        REF    NAT COMMUN                    V.   6  6481 2015              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   25901944                                                     
JRNL        DOI    10.1038/NCOMMS7481                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1702)                     
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.85                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 40265                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2023                            
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 32.8563 -  4.8156    0.98     3014   162  0.1401 0.1849        
REMARK   3     2  4.8156 -  3.8242    0.99     2803   160  0.1379 0.1469        
REMARK   3     3  3.8242 -  3.3413    0.99     2854   144  0.1421 0.1750        
REMARK   3     4  3.3413 -  3.0361    0.98     2741   155  0.1527 0.1907        
REMARK   3     5  3.0361 -  2.8186    0.98     2758   148  0.1754 0.2340        
REMARK   3     6  2.8186 -  2.6525    0.98     2756   145  0.1846 0.2229        
REMARK   3     7  2.6525 -  2.5197    0.97     2710   138  0.1870 0.2278        
REMARK   3     8  2.5197 -  2.4100    0.97     2637   153  0.1839 0.2142        
REMARK   3     9  2.4100 -  2.3173    0.97     2734   128  0.1821 0.2230        
REMARK   3    10  2.3173 -  2.2373    0.96     2685   133  0.1819 0.2386        
REMARK   3    11  2.2373 -  2.1674    0.96     2628   142  0.1854 0.2308        
REMARK   3    12  2.1674 -  2.1055    0.96     2673   136  0.1914 0.2581        
REMARK   3    13  2.1055 -  2.0500    0.95     2650   130  0.2077 0.2479        
REMARK   3    14  2.0500 -  2.0000    0.95     2599   149  0.2172 0.2427        
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)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.220           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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      :  0.007           3638                                  
REMARK   3   ANGLE     :  1.469           5284                                  
REMARK   3   CHIRALITY :  0.066            556                                  
REMARK   3   PLANARITY :  0.006            379                                  
REMARK   3   DIHEDRAL  : 43.995           1615                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -19.2894  23.0218 -16.3148              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2043 T22:   0.2115                                     
REMARK   3      T33:   0.1491 T12:   0.0592                                     
REMARK   3      T13:   0.0241 T23:   0.0417                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8835 L22:   3.2281                                     
REMARK   3      L33:   2.7060 L12:   1.1425                                     
REMARK   3      L13:   0.3801 L23:  -0.6281                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0387 S12:   0.3989 S13:   0.1940                       
REMARK   3      S21:  -0.4994 S22:   0.0566 S23:  -0.0214                       
REMARK   3      S31:  -0.0610 S32:   0.0092 S33:  -0.0402                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -36.0221   7.0856 -10.7311              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0983 T22:   0.2302                                     
REMARK   3      T33:   0.2099 T12:   0.0339                                     
REMARK   3      T13:  -0.0002 T23:   0.0195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9358 L22:   3.6054                                     
REMARK   3      L33:   2.9816 L12:   0.5129                                     
REMARK   3      L13:   0.6589 L23:  -0.3285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1647 S12:   0.0710 S13:   0.3042                       
REMARK   3      S21:  -0.0520 S22:   0.1849 S23:   0.2735                       
REMARK   3      S31:  -0.3161 S32:  -0.1675 S33:  -0.0119                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.9744  57.2623  20.6915              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6095 T22:   0.3485                                     
REMARK   3      T33:   0.5702 T12:  -0.1265                                     
REMARK   3      T13:  -0.0097 T23:  -0.0423                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4184 L22:   2.6422                                     
REMARK   3      L33:   0.5881 L12:   1.7917                                     
REMARK   3      L13:   1.0131 L23:   1.2130                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0367 S12:   0.0565 S13:   0.3194                       
REMARK   3      S21:   0.2571 S22:   0.1502 S23:  -0.8264                       
REMARK   3      S31:  -0.7935 S32:   0.6214 S33:  -0.1401                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN D AND RESID 1:40                                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.5370  21.2456  -1.6082              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1381 T22:   0.1766                                     
REMARK   3      T33:   0.1650 T12:   0.0261                                     
REMARK   3      T13:  -0.0006 T23:  -0.0460                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2405 L22:   3.2762                                     
REMARK   3      L33:   1.8258 L12:  -0.4897                                     
REMARK   3      L13:   0.0933 L23:  -0.1808                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0251 S12:  -0.1615 S13:   0.3031                       
REMARK   3      S21:   0.0572 S22:   0.0331 S23:  -0.2660                       
REMARK   3      S31:  -0.1262 S32:   0.1339 S33:  -0.0622                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN E AND RESID 1:40                                 
REMARK   3    ORIGIN FOR THE GROUP (A): -17.0659  53.8326  16.3845              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5429 T22:   0.2239                                     
REMARK   3      T33:   0.3253 T12:   0.0579                                     
REMARK   3      T13:   0.0214 T23:  -0.0521                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9898 L22:   3.1304                                     
REMARK   3      L33:   1.7745 L12:  -0.6788                                     
REMARK   3      L13:   0.4891 L23:   0.0621                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0284 S12:   0.0609 S13:   0.2209                       
REMARK   3      S21:  -0.2458 S22:  -0.0283 S23:   0.2628                       
REMARK   3      S31:  -0.6505 S32:  -0.1852 S33:   0.0509                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4WB3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-SEP-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000203511.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41442                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.0100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.720                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: 4WB2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M NA         
REMARK 280  ACETATE PH 4.0, 15% (W/V) PEG 4000, VAPOR DIFFUSION, HANGING        
REMARK 280  DROP, TEMPERATURE 292K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       22.92000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      141.31500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.92000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      141.31500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 915  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 920  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   677                                                      
REMARK 465     ALA A   678                                                      
REMARK 465     PRO A   747                                                      
REMARK 465     HIS A   748                                                      
REMARK 465     LYS A   749                                                      
REMARK 465     PRO A   750                                                      
REMARK 465     VAL A   751                                                      
REMARK 465     GLN A   752                                                      
REMARK 465     LEU A   753                                                      
REMARK 465     GLY A   754                                                      
REMARK 465     GLY B   677                                                      
REMARK 465     ALA B   678                                                      
REMARK 465     ASN B   679                                                      
REMARK 465     LEU B   680                                                      
REMARK 465     LYS B   749                                                      
REMARK 465     PRO B   750                                                      
REMARK 465     VAL B   751                                                      
REMARK 465     GLN B   752                                                      
REMARK 465     LEU B   753                                                      
REMARK 465     GLY B   754                                                      
REMARK 465     GLY C   677                                                      
REMARK 465     PRO C   747                                                      
REMARK 465     HIS C   748                                                      
REMARK 465     LYS C   749                                                      
REMARK 465     PRO C   750                                                      
REMARK 465     VAL C   751                                                      
REMARK 465     GLN C   752                                                      
REMARK 465     LEU C   753                                                      
REMARK 465     GLY C   754                                                      
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     0G D   1   C4     0G D   1   C5      0.089                       
REMARK 500     0G D   1   C5     0G D   1   C6      0.064                       
REMARK 500     0G D   1   C6     0G D   1   N1     -0.050                       
REMARK 500     0G D   1   C5     0G D   1   N7     -0.040                       
REMARK 500     0G D   1   N7     0G D   1   C8      0.056                       
REMARK 500     0C D   2   C5     0C D   2   C6      0.055                       
REMARK 500     0G D   3   C4     0G D   3   C5      0.085                       
REMARK 500     0G D   3   C5     0G D   3   C6      0.064                       
REMARK 500     0G D   3   N7     0G D   3   C8      0.054                       
REMARK 500     0G D   3   N9     0G D   3   C4     -0.054                       
REMARK 500     0A D   4   C4     0A D   4   C5      0.088                       
REMARK 500     0A D   4   C5     0A D   4   C6      0.072                       
REMARK 500     0A D   4   C5     0A D   4   N7     -0.038                       
REMARK 500     0A D   4   N9     0A D   4   C4     -0.050                       
REMARK 500     0U D   5   C5     0U D   5   C6      0.059                       
REMARK 500     0G D   6   C4     0G D   6   C5      0.077                       
REMARK 500     0G D   6   C5     0G D   6   C6      0.062                       
REMARK 500     0G D   6   C6     0G D   6   N1     -0.051                       
REMARK 500     0G D   6   C5     0G D   6   N7     -0.037                       
REMARK 500     0G D   6   N7     0G D   6   C8      0.052                       
REMARK 500     0G D   6   N9     0G D   6   C4     -0.058                       
REMARK 500     0G D   8   C4     0G D   8   C5      0.082                       
REMARK 500     0G D   8   C6     0G D   8   N1     -0.048                       
REMARK 500     0G D   8   C5     0G D   8   N7     -0.043                       
REMARK 500     0G D   8   N7     0G D   8   C8      0.047                       
REMARK 500     0G D   8   N9     0G D   8   C4     -0.050                       
REMARK 500     0G D   9   C4     0G D   9   C5      0.087                       
REMARK 500     0G D   9   C6     0G D   9   N1     -0.054                       
REMARK 500     0G D   9   C5     0G D   9   N7     -0.042                       
REMARK 500     0G D   9   N7     0G D   9   C8      0.058                       
REMARK 500     0U D  10   C2     0U D  10   N3     -0.043                       
REMARK 500     0U D  10   C5     0U D  10   C6      0.059                       
REMARK 500     0G D  11   C4     0G D  11   C5      0.088                       
REMARK 500     0G D  11   C6     0G D  11   N1     -0.054                       
REMARK 500     0G D  11   C5     0G D  11   N7     -0.041                       
REMARK 500     0G D  11   N7     0G D  11   C8      0.054                       
REMARK 500     0G D  12   C4     0G D  12   C5      0.079                       
REMARK 500     0G D  12   C6     0G D  12   N1     -0.044                       
REMARK 500     0G D  12   N7     0G D  12   C8      0.051                       
REMARK 500     0G D  12   N9     0G D  12   C4     -0.054                       
REMARK 500     0U D  13   C5     0U D  13   C6      0.057                       
REMARK 500    0DG D  14   C4    0DG D  14   C5      0.092                       
REMARK 500    0DG D  14   C5    0DG D  14   C6      0.062                       
REMARK 500    0DG D  14   C6    0DG D  14   N1     -0.050                       
REMARK 500    0DG D  14   C5    0DG D  14   N7     -0.044                       
REMARK 500    0DG D  14   N7    0DG D  14   C8      0.053                       
REMARK 500     0A D  16   C4     0A D  16   C5      0.083                       
REMARK 500     0A D  16   C5     0A D  16   C6      0.069                       
REMARK 500     0A D  16   C5     0A D  16   N7     -0.044                       
REMARK 500     0A D  16   N7     0A D  16   C8      0.044                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     224 BOND DEVIATIONS.                              
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     0G D   1   C2  -  N3  -  C4  ANGL. DEV. =   9.3 DEGREES          
REMARK 500     0G D   1   N3  -  C4  -  C5  ANGL. DEV. = -10.2 DEGREES          
REMARK 500     0G D   1   C5  -  C6  -  N1  ANGL. DEV. =   6.8 DEGREES          
REMARK 500     0G D   1   C4  -  C5  -  N7  ANGL. DEV. =  -4.5 DEGREES          
REMARK 500     0G D   1   C5  -  N7  -  C8  ANGL. DEV. =   3.4 DEGREES          
REMARK 500     0G D   1   N3  -  C4  -  N9  ANGL. DEV. =   8.9 DEGREES          
REMARK 500     0G D   1   C6  -  C5  -  N7  ANGL. DEV. =   5.9 DEGREES          
REMARK 500     0G D   1   C5  -  C6  -  O6  ANGL. DEV. =  -8.0 DEGREES          
REMARK 500     0G D   3   C2  -  N3  -  C4  ANGL. DEV. =   9.2 DEGREES          
REMARK 500     0G D   3   N3  -  C4  -  C5  ANGL. DEV. =  -8.5 DEGREES          
REMARK 500     0G D   3   C5  -  C6  -  N1  ANGL. DEV. =   6.3 DEGREES          
REMARK 500     0G D   3   C4  -  C5  -  N7  ANGL. DEV. =  -4.7 DEGREES          
REMARK 500     0G D   3   C5  -  N7  -  C8  ANGL. DEV. =   3.5 DEGREES          
REMARK 500     0G D   3   N7  -  C8  -  N9  ANGL. DEV. =  -3.1 DEGREES          
REMARK 500     0G D   3   C8  -  N9  -  C4  ANGL. DEV. =   3.0 DEGREES          
REMARK 500     0G D   3   N3  -  C4  -  N9  ANGL. DEV. =   7.2 DEGREES          
REMARK 500     0G D   3   C6  -  C5  -  N7  ANGL. DEV. =   7.4 DEGREES          
REMARK 500     0G D   3   C5  -  C6  -  O6  ANGL. DEV. =  -7.6 DEGREES          
REMARK 500     0A D   4   N1  -  C2  -  N3  ANGL. DEV. =  -5.1 DEGREES          
REMARK 500     0A D   4   C2  -  N3  -  C4  ANGL. DEV. =   8.7 DEGREES          
REMARK 500     0A D   4   N3  -  C4  -  C5  ANGL. DEV. =  -6.8 DEGREES          
REMARK 500     0A D   4   C4  -  C5  -  N7  ANGL. DEV. =  -3.5 DEGREES          
REMARK 500     0A D   4   C5  -  N7  -  C8  ANGL. DEV. =   3.4 DEGREES          
REMARK 500     0A D   4   N7  -  C8  -  N9  ANGL. DEV. =  -3.2 DEGREES          
REMARK 500     0A D   4   C8  -  N9  -  C4  ANGL. DEV. =   4.0 DEGREES          
REMARK 500     0A D   4   N3  -  C4  -  N9  ANGL. DEV. =   7.5 DEGREES          
REMARK 500     0A D   4   N1  -  C6  -  N6  ANGL. DEV. =   3.9 DEGREES          
REMARK 500     0U D   5   N1  -  C2  -  N3  ANGL. DEV. =   5.4 DEGREES          
REMARK 500     0U D   5   C2  -  N3  -  C4  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500     0U D   5   N3  -  C4  -  C5  ANGL. DEV. =   5.8 DEGREES          
REMARK 500     0U D   5   C5  -  C4  -  O4  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500     0G D   6   C2  -  N3  -  C4  ANGL. DEV. =   8.0 DEGREES          
REMARK 500     0G D   6   N3  -  C4  -  C5  ANGL. DEV. =  -8.1 DEGREES          
REMARK 500     0G D   6   C5  -  C6  -  N1  ANGL. DEV. =   6.1 DEGREES          
REMARK 500     0G D   6   C4  -  C5  -  N7  ANGL. DEV. =  -4.2 DEGREES          
REMARK 500     0G D   6   C5  -  N7  -  C8  ANGL. DEV. =   3.3 DEGREES          
REMARK 500     0G D   6   N7  -  C8  -  N9  ANGL. DEV. =  -3.5 DEGREES          
REMARK 500     0G D   6   C8  -  N9  -  C4  ANGL. DEV. =   3.8 DEGREES          
REMARK 500     0G D   6   N3  -  C4  -  N9  ANGL. DEV. =   7.4 DEGREES          
REMARK 500     0G D   6   C6  -  C5  -  N7  ANGL. DEV. =   6.6 DEGREES          
REMARK 500     0G D   6   C5  -  C6  -  O6  ANGL. DEV. =  -8.0 DEGREES          
REMARK 500     0G D   8   C2  -  N3  -  C4  ANGL. DEV. =   9.1 DEGREES          
REMARK 500     0G D   8   N3  -  C4  -  C5  ANGL. DEV. =  -9.1 DEGREES          
REMARK 500     0G D   8   C5  -  C6  -  N1  ANGL. DEV. =   7.1 DEGREES          
REMARK 500     0G D   8   C4  -  C5  -  N7  ANGL. DEV. =  -2.8 DEGREES          
REMARK 500     0G D   8   C8  -  N9  -  C4  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     0G D   8   N3  -  C4  -  N9  ANGL. DEV. =   9.2 DEGREES          
REMARK 500     0G D   8   C6  -  C5  -  N7  ANGL. DEV. =   5.2 DEGREES          
REMARK 500     0G D   8   C5  -  C6  -  O6  ANGL. DEV. =  -9.6 DEGREES          
REMARK 500     0G D   9   C2  -  N3  -  C4  ANGL. DEV. =   8.3 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     458 ANGLE DEVIATIONS.                             
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    ASN A 710       21.79   -150.40                                   
REMARK 500    ASN A 710       37.26   -156.58                                   
REMARK 500    PHE A 711     -145.93   -102.78                                   
REMARK 500    PHE A 711     -145.93   -116.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 801  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 705   OD2                                                    
REMARK 620 2  0U D   5   OP1  71.1                                              
REMARK 620 3  0G D   6   OP1 116.6 100.5                                        
REMARK 620 4  0G D  32   OP2 107.6  69.8 128.7                                  
REMARK 620 5 HOH D 258   O    90.9 116.3  35.2 161.4                            
REMARK 620 6 HOH D 254   O    77.4 143.7 109.6 104.1  81.2                      
REMARK 620 7 HOH D 253   O   152.0 136.0  71.3  82.0  82.3  74.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 801  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 705   OD2                                                    
REMARK 620 2  0U E   5   OP2  75.8                                              
REMARK 620 3  0G E   6   OP1 134.0  73.2                                        
REMARK 620 4  0G E  32   OP2  87.7  79.1 118.0                                  
REMARK 620 5 HOH E 209   O    72.8 144.2 142.4  83.0                            
REMARK 620 6 HOH E 227   O    87.7 118.7  78.7 159.7  76.7                      
REMARK 620 7 HOH E 247   O   147.4 134.7  75.5  87.9  74.6  85.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 103  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  0U D   5   OP2                                                    
REMARK 620 2  0G D  32   OP1  71.8                                              
REMARK 620 3 HOH D 255   O    89.6  71.2                                        
REMARK 620 4 HOH D 252   O   173.0 104.2  83.7                                  
REMARK 620 5 HOH D 259   O    92.0 117.4 171.3  94.9                            
REMARK 620 6 HOH D 266   O    98.6 157.2  88.5  83.0  82.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 101  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  0G D  17   O6                                                     
REMARK 620 2  0G D  18   O6   77.3                                              
REMARK 620 3  0G D  19   O6   74.6  73.7                                        
REMARK 620 4  0G D  22   O6  147.2  72.3  85.1                                  
REMARK 620 5  0G D  25   O6  116.9 134.0  69.4  77.9                            
REMARK 620 6  0G D  26   O6  136.6 124.7 142.9  73.3  76.7                      
REMARK 620 7  0G D  27   O6   70.6 143.2 113.2 142.1  78.3  72.8                
REMARK 620 8  0G D  32   O6   74.9  74.9 140.1 108.0 149.2  76.3  79.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 102  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  0C D  34   OP1                                                    
REMARK 620 2 HOH D 256   O   136.9                                              
REMARK 620 3 HOH D 260   O    82.2 125.9                                        
REMARK 620 4 HOH D 261   O   153.5  66.4  71.8                                  
REMARK 620 5 HOH D 262   O    80.4  75.9  77.9  98.3                            
REMARK 620 6 HOH D 290   O    93.6 119.7  82.1  78.5 159.7                      
REMARK 620 7 HOH D 265   O    84.9  75.3 157.9 118.1 117.5  80.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 103  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  0U E   5   OP1                                                    
REMARK 620 2  0G E  32   OP1  91.7                                              
REMARK 620 3 HOH E 206   O    88.9 106.6                                        
REMARK 620 4 HOH E 207   O   175.4  87.4  87.1                                  
REMARK 620 5 HOH E 208   O    90.4  83.7 169.8  94.0                            
REMARK 620 6 HOH E 213   O    93.1 164.8  88.0  89.0  81.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 101  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  0G E  17   O6                                                     
REMARK 620 2  0G E  18   O6   79.8                                              
REMARK 620 3  0G E  19   O6   76.5  77.2                                        
REMARK 620 4  0G E  22   O6  148.8  71.6  84.9                                  
REMARK 620 5  0G E  25   O6  118.1 134.1  68.1  76.2                            
REMARK 620 6  0G E  26   O6  136.8 123.2 139.4  72.0  74.2                      
REMARK 620 7  0G E  27   O6   70.8 147.2 108.6 139.9  74.6  73.9                
REMARK 620 8  0G E  32   O6   78.6  75.8 145.9 105.6 145.5  73.9  84.3          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 102  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  0C E  34   OP2                                                    
REMARK 620 2 HOH E 222   O    79.3                                              
REMARK 620 3 HOH E 216   O   137.4 129.8                                        
REMARK 620 4 HOH E 217   O   151.4  85.9  70.1                                  
REMARK 620 5 HOH E 229   O    87.6  81.8 122.6  66.0                            
REMARK 620 6 HOH E 230   O    79.7 155.5  74.7 107.4  85.0                      
REMARK 620 7 HOH E 231   O    83.0  76.8  76.6 117.4 157.9 112.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4WB2   RELATED DB: PDB                                   
REMARK 900 4WB2 CONTAINS THE SAME L-RNA/L-DNA APTAMER IN COMPLEX WITH MOUSE C5A 
DBREF  4WB3 A  679   754  UNP    P06684   CO5_MOUSE      679    754             
DBREF  4WB3 B  679   754  UNP    P06684   CO5_MOUSE      679    754             
DBREF  4WB3 C  679   754  UNP    P06684   CO5_MOUSE      679    754             
DBREF  4WB3 D    1    40  PDB    4WB3     4WB3             1     40             
DBREF  4WB3 E    1    40  PDB    4WB3     4WB3             1     40             
SEQADV 4WB3 GLY A  677  UNP  P06684              EXPRESSION TAG                 
SEQADV 4WB3 ALA A  678  UNP  P06684              EXPRESSION TAG                 
SEQADV 4WB3 GLY B  677  UNP  P06684              EXPRESSION TAG                 
SEQADV 4WB3 ALA B  678  UNP  P06684              EXPRESSION TAG                 
SEQADV 4WB3 GLY C  677  UNP  P06684              EXPRESSION TAG                 
SEQADV 4WB3 ALA C  678  UNP  P06684              EXPRESSION TAG                 
SEQRES   1 A   78  GLY ALA ASN LEU HIS LEU LEU ARG GLN LYS ILE GLU GLU          
SEQRES   2 A   78  GLN ALA ALA LYS TYR LYS HIS SER VAL PRO LYS LYS CYS          
SEQRES   3 A   78  CYS TYR ASP GLY ALA ARG VAL ASN PHE TYR GLU THR CYS          
SEQRES   4 A   78  GLU GLU ARG VAL ALA ARG VAL THR ILE GLY PRO LEU CYS          
SEQRES   5 A   78  ILE ARG ALA PHE ASN GLU CYS CYS THR ILE ALA ASN LYS          
SEQRES   6 A   78  ILE ARG LYS GLU SER PRO HIS LYS PRO VAL GLN LEU GLY          
SEQRES   1 B   78  GLY ALA ASN LEU HIS LEU LEU ARG GLN LYS ILE GLU GLU          
SEQRES   2 B   78  GLN ALA ALA LYS TYR LYS HIS SER VAL PRO LYS LYS CYS          
SEQRES   3 B   78  CYS TYR ASP GLY ALA ARG VAL ASN PHE TYR GLU THR CYS          
SEQRES   4 B   78  GLU GLU ARG VAL ALA ARG VAL THR ILE GLY PRO LEU CYS          
SEQRES   5 B   78  ILE ARG ALA PHE ASN GLU CYS CYS THR ILE ALA ASN LYS          
SEQRES   6 B   78  ILE ARG LYS GLU SER PRO HIS LYS PRO VAL GLN LEU GLY          
SEQRES   1 C   78  GLY ALA ASN LEU HIS LEU LEU ARG GLN LYS ILE GLU GLU          
SEQRES   2 C   78  GLN ALA ALA LYS TYR LYS HIS SER VAL PRO LYS LYS CYS          
SEQRES   3 C   78  CYS TYR ASP GLY ALA ARG VAL ASN PHE TYR GLU THR CYS          
SEQRES   4 C   78  GLU GLU ARG VAL ALA ARG VAL THR ILE GLY PRO LEU CYS          
SEQRES   5 C   78  ILE ARG ALA PHE ASN GLU CYS CYS THR ILE ALA ASN LYS          
SEQRES   6 C   78  ILE ARG LYS GLU SER PRO HIS LYS PRO VAL GLN LEU GLY          
SEQRES   1 D   40   0G  0C  0G  0A  0U  0G 3KA  0G  0G  0U  0G  0G  0U          
SEQRES   2 D   40  0DG 0DA  0A  0G  0G  0G  0U  0U  0G  0U  0U  0G  0G          
SEQRES   3 D   40   0G 3KA  0G 3KA  0C  0G  0A  0C  0G  0C  0A 0DC  0G          
SEQRES   4 D   40   0C                                                          
SEQRES   1 E   40   0G  0C  0G  0A  0U  0G 3KA  0G  0G  0U  0G  0G  0U          
SEQRES   2 E   40  0DG 0DA  0A  0G  0G  0G  0U  0U  0G  0U  0U  0G  0G          
SEQRES   3 E   40   0G 3KA  0G 3KA  0C  0G  0A  0C  0G  0C  0A 0DC  0G          
SEQRES   4 E   40   0C                                                          
HET     0G  D   1      20                                                       
HET     0C  D   2      20                                                       
HET     0G  D   3      23                                                       
HET     0A  D   4      22                                                       
HET     0U  D   5      20                                                       
HET     0G  D   6      23                                                       
HET    3KA  D   7      19                                                       
HET     0G  D   8      23                                                       
HET     0G  D   9      23                                                       
HET     0U  D  10      20                                                       
HET     0G  D  11      23                                                       
HET     0G  D  12      23                                                       
HET     0U  D  13      20                                                       
HET    0DG  D  14      22                                                       
HET    0DA  D  15      21                                                       
HET     0A  D  16      22                                                       
HET     0G  D  17      23                                                       
HET     0G  D  18      23                                                       
HET     0G  D  19      23                                                       
HET     0U  D  20      20                                                       
HET     0U  D  21      20                                                       
HET     0G  D  22      23                                                       
HET     0U  D  23      20                                                       
HET     0U  D  24      20                                                       
HET     0G  D  25      23                                                       
HET     0G  D  26      23                                                       
HET     0G  D  27      23                                                       
HET    3KA  D  28      19                                                       
HET     0G  D  29      23                                                       
HET    3KA  D  30      19                                                       
HET     0C  D  31      20                                                       
HET     0G  D  32      23                                                       
HET     0A  D  33      22                                                       
HET     0C  D  34      20                                                       
HET     0G  D  35      23                                                       
HET     0C  D  36      20                                                       
HET     0A  D  37      22                                                       
HET    0DC  D  38      19                                                       
HET     0G  D  39      23                                                       
HET     0C  D  40      20                                                       
HET     0G  E   1      20                                                       
HET     0C  E   2      20                                                       
HET     0G  E   3      23                                                       
HET     0A  E   4      22                                                       
HET     0U  E   5      20                                                       
HET     0G  E   6      23                                                       
HET    3KA  E   7      19                                                       
HET     0G  E   8      23                                                       
HET     0G  E   9      23                                                       
HET     0U  E  10      20                                                       
HET     0G  E  11      23                                                       
HET     0G  E  12      23                                                       
HET     0U  E  13      20                                                       
HET    0DG  E  14      22                                                       
HET    0DA  E  15      21                                                       
HET     0A  E  16      22                                                       
HET     0G  E  17      23                                                       
HET     0G  E  18      23                                                       
HET     0G  E  19      23                                                       
HET     0U  E  20      20                                                       
HET     0U  E  21      20                                                       
HET     0G  E  22      23                                                       
HET     0U  E  23      20                                                       
HET     0U  E  24      20                                                       
HET     0G  E  25      23                                                       
HET     0G  E  26      23                                                       
HET     0G  E  27      23                                                       
HET    3KA  E  28      19                                                       
HET     0G  E  29      23                                                       
HET    3KA  E  30      19                                                       
HET     0C  E  31      20                                                       
HET     0G  E  32      23                                                       
HET     0A  E  33      22                                                       
HET     0C  E  34      20                                                       
HET     0G  E  35      23                                                       
HET     0C  E  36      20                                                       
HET     0A  E  37      22                                                       
HET    0DC  E  38      19                                                       
HET     0G  E  39      23                                                       
HET     0C  E  40      20                                                       
HET     CA  A 801       1                                                       
HET    ACT  B 801       4                                                       
HET    ACT  B 802       4                                                       
HET     CA  C 801       1                                                       
HET     CA  D 101       1                                                       
HET     CA  D 102       1                                                       
HET     MG  D 103       1                                                       
HET    ACT  D 104       4                                                       
HET     CA  E 101       1                                                       
HET     CA  E 102       1                                                       
HET     MG  E 103       1                                                       
HETNAM      0G L-GUANOSINE-5'-MONOPHOSPHATE                                     
HETNAM      0C L-CYTIDINE-5'-MONOPHOSPHATE                                      
HETNAM      0A L-ADENOSINE-5'-MONOPHOSPHATE                                     
HETNAM      0U L-URIDINE-5'-MONOPHOSPHATE                                       
HETNAM     3KA 1-(2-DEOXY-5-O-PHOSPHONO-BETA-L-ERYTHRO-                         
HETNAM   2 3KA  PENTOFURANOSYL)PYRIMIDINE-2,4(1H,3H)-DIONE                      
HETNAM     0DG 2'-DEOXY-L-RIBO-FURANOSYL GUANINE-5'-MONOPHOSPHATE               
HETNAM     0DA 2'-DEOXY-L-RIBO-FURANOSYL ADENOSINE-5'-MONOPHOSPHATE             
HETNAM     0DC 2'-DEOXY-L-RIBO-FURANOSYL CYTOSINE-5'-MONOPHOSPHATE              
HETNAM      CA CALCIUM ION                                                      
HETNAM     ACT ACETATE ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     3KA L-2'-DEOXYURIDINE-5'-MONOPHOSPHATE                               
FORMUL   4   0G    36(C10 H14 N5 O8 P)                                          
FORMUL   4   0C    10(C9 H14 N3 O8 P)                                           
FORMUL   4   0A    8(C10 H14 N5 O7 P)                                           
FORMUL   4   0U    14(C9 H13 N2 O9 P)                                           
FORMUL   4  3KA    6(C9 H13 N2 O8 P)                                            
FORMUL   4  0DG    2(C10 H14 N5 O7 P)                                           
FORMUL   4  0DA    2(C10 H14 N5 O6 P)                                           
FORMUL   4  0DC    2(C9 H14 N3 O7 P)                                            
FORMUL   6   CA    6(CA 2+)                                                     
FORMUL   7  ACT    3(C2 H3 O2 1-)                                               
FORMUL  12   MG    2(MG 2+)                                                     
FORMUL  17  HOH   *373(H2 O)                                                    
HELIX    1 AA1 ASN A  679  ALA A  692  1                                  14    
HELIX    2 AA2 HIS A  696  ARG A  708  1                                  13    
HELIX    3 AA3 THR A  714  ALA A  720  1                                   7    
HELIX    4 AA4 GLY A  725  SER A  746  1                                  22    
HELIX    5 AA5 LEU B  682  ALA B  692  1                                  11    
HELIX    6 AA6 HIS B  696  ARG B  708  1                                  13    
HELIX    7 AA7 THR B  714  ALA B  720  1                                   7    
HELIX    8 AA8 GLY B  725  GLU B  745  1                                  21    
HELIX    9 AA9 ASN C  679  ALA C  692  1                                  14    
HELIX   10 AB1 HIS C  696  ALA C  707  1                                  12    
HELIX   11 AB2 THR C  714  ALA C  720  1                                   7    
HELIX   12 AB3 GLY C  725  GLU C  745  1                                  21    
SSBOND   1 CYS A  702    CYS A  728                          1555   1555  2.02  
SSBOND   2 CYS A  703    CYS A  735                          1555   1555  2.03  
SSBOND   3 CYS A  715    CYS A  736                          1555   1555  2.03  
SSBOND   4 CYS B  702    CYS B  728                          1555   1555  2.03  
SSBOND   5 CYS B  703    CYS B  735                          1555   1555  2.00  
SSBOND   6 CYS B  715    CYS B  736                          1555   1555  2.01  
SSBOND   7 CYS C  702    CYS C  728                          1555   1555  2.02  
SSBOND   8 CYS C  703    CYS C  735                          1555   1555  2.03  
SSBOND   9 CYS C  715    CYS C  736                          1555   1555  2.03  
LINK         OD2 ASP A 705                CA    CA A 801     1555   1555  2.50  
LINK         OD2 ASP C 705                CA    CA C 801     1555   1555  2.47  
LINK         O3'  0G D   1                 P    0C D   2     1555   1555  1.61  
LINK         O3'  0C D   2                 P    0G D   3     1555   1555  1.61  
LINK         OP1  0U D   5                CA    CA A 801     1555   1555  2.40  
LINK         OP2  0U D   5                MG    MG D 103     1555   1555  1.92  
LINK         O3'  0U D   5                 P    0G D   6     1555   1555  1.61  
LINK         OP1  0G D   6                CA    CA A 801     1555   1555  3.95  
LINK         O3'  0G D   6                 P   3KA D   7     1555   1555  1.59  
LINK         O3' 3KA D   7                 P    0G D   8     1555   1555  1.62  
LINK         O3'  0G D   8                 P    0G D   9     1555   1555  1.61  
LINK         O3'  0G D   9                 P    0U D  10     1555   1555  1.62  
LINK         O3'  0U D  10                 P    0G D  11     1555   1555  1.62  
LINK         O3'  0G D  11                 P    0G D  12     1555   1555  1.60  
LINK         O3'  0G D  12                 P    0U D  13     1555   1555  1.59  
LINK         O3'  0U D  13                 P   0DG D  14     1555   1555  1.61  
LINK         O3' 0DG D  14                 P   0DA D  15     1555   1555  1.61  
LINK         O3'  0G D  17                 P    0G D  18     1555   1555  1.61  
LINK         O6   0G D  17                CA    CA D 101     1555   1555  2.57  
LINK         O3'  0G D  18                 P    0G D  19     1555   1555  1.60  
LINK         O6   0G D  18                CA    CA D 101     1555   1555  2.52  
LINK         O3'  0G D  19                 P    0U D  20     1555   1555  1.60  
LINK         O6   0G D  19                CA    CA D 101     1555   1555  2.48  
LINK         O3'  0U D  20                 P    0U D  21     1555   1555  1.60  
LINK         O3'  0U D  21                 P    0G D  22     1555   1555  1.61  
LINK         O3'  0G D  22                 P    0U D  23     1555   1555  1.60  
LINK         O6   0G D  22                CA    CA D 101     1555   1555  2.52  
LINK         O3'  0U D  23                 P    0U D  24     1555   1555  1.61  
LINK         O3'  0U D  24                 P    0G D  25     1555   1555  1.60  
LINK         O3'  0G D  25                 P    0G D  26     1555   1555  1.61  
LINK         O6   0G D  25                CA    CA D 101     1555   1555  2.54  
LINK         O3'  0G D  26                 P    0G D  27     1555   1555  1.61  
LINK         O6   0G D  26                CA    CA D 101     1555   1555  2.44  
LINK         O3'  0G D  27                 P   3KA D  28     1555   1555  1.61  
LINK         O6   0G D  27                CA    CA D 101     1555   1555  2.42  
LINK         O3' 3KA D  28                 P    0G D  29     1555   1555  1.61  
LINK         O3'  0G D  29                 P   3KA D  30     1555   1555  1.61  
LINK         O3' 3KA D  30                 P    0C D  31     1555   1555  1.62  
LINK         O3'  0C D  31                 P    0G D  32     1555   1555  1.61  
LINK         OP1  0G D  32                MG    MG D 103     1555   1555  3.90  
LINK         OP2  0G D  32                CA    CA A 801     1555   1555  4.28  
LINK         O6   0G D  32                CA    CA D 101     1555   1555  2.50  
LINK         OP1  0C D  34                CA    CA D 102     1555   1555  2.28  
LINK         O3'  0C D  34                 P    0G D  35     1555   1555  1.60  
LINK         O3'  0G D  35                 P    0C D  36     1555   1555  1.61  
LINK         O3' 0DC D  38                 P    0G D  39     1555   1555  1.61  
LINK         O3'  0G D  39                 P    0C D  40     1555   1555  1.60  
LINK         O3'  0G E   1                 P    0C E   2     1555   1555  1.61  
LINK         O3'  0C E   2                 P    0G E   3     1555   1555  1.60  
LINK         OP1  0U E   5                MG    MG E 103     1555   1555  1.93  
LINK         OP2  0U E   5                CA    CA C 801     1555   1555  2.40  
LINK         O3'  0U E   5                 P    0G E   6     1555   1555  1.60  
LINK         OP1  0G E   6                CA    CA C 801     1555   1555  2.55  
LINK         O3'  0G E   6                 P   3KA E   7     1555   1555  1.60  
LINK         O3' 3KA E   7                 P    0G E   8     1555   1555  1.61  
LINK         O3'  0G E   8                 P    0G E   9     1555   1555  1.61  
LINK         O3'  0G E   9                 P    0U E  10     1555   1555  1.62  
LINK         O3'  0U E  10                 P    0G E  11     1555   1555  1.62  
LINK         O3'  0G E  11                 P    0G E  12     1555   1555  1.61  
LINK         O3'  0G E  12                 P    0U E  13     1555   1555  1.60  
LINK         O3'  0U E  13                 P   0DG E  14     1555   1555  1.61  
LINK         O3' 0DG E  14                 P   0DA E  15     1555   1555  1.60  
LINK         O3'  0G E  17                 P    0G E  18     1555   1555  1.62  
LINK         O6   0G E  17                CA    CA E 101     1555   1555  2.46  
LINK         O3'  0G E  18                 P    0G E  19     1555   1555  1.61  
LINK         O6   0G E  18                CA    CA E 101     1555   1555  2.51  
LINK         O3'  0G E  19                 P    0U E  20     1555   1555  1.61  
LINK         O6   0G E  19                CA    CA E 101     1555   1555  2.40  
LINK         O3'  0U E  20                 P    0U E  21     1555   1555  1.60  
LINK         O3'  0U E  21                 P    0G E  22     1555   1555  1.60  
LINK         O3'  0G E  22                 P    0U E  23     1555   1555  1.61  
LINK         O6   0G E  22                CA    CA E 101     1555   1555  2.42  
LINK         O3'  0U E  23                 P    0U E  24     1555   1555  1.60  
LINK         O3'  0U E  24                 P    0G E  25     1555   1555  1.61  
LINK         O3'  0G E  25                 P    0G E  26     1555   1555  1.60  
LINK         O6   0G E  25                CA    CA E 101     1555   1555  2.59  
LINK         O3'  0G E  26                 P    0G E  27     1555   1555  1.61  
LINK         O6   0G E  26                CA    CA E 101     1555   1555  2.49  
LINK         O3'  0G E  27                 P   3KA E  28     1555   1555  1.60  
LINK         O6   0G E  27                CA    CA E 101     1555   1555  2.45  
LINK         O3' 3KA E  28                 P    0G E  29     1555   1555  1.62  
LINK         O3'  0G E  29                 P   3KA E  30     1555   1555  1.60  
LINK         O3' 3KA E  30                 P    0C E  31     1555   1555  1.60  
LINK         O3'  0C E  31                 P    0G E  32     1555   1555  1.59  
LINK         OP1  0G E  32                MG    MG E 103     1555   1555  2.07  
LINK         OP2  0G E  32                CA    CA C 801     1555   1555  2.27  
LINK         O6   0G E  32                CA    CA E 101     1555   1555  2.46  
LINK         OP2  0C E  34                CA    CA E 102     1555   1555  2.44  
LINK         O3'  0C E  34                 P    0G E  35     1555   1555  1.60  
LINK         O3'  0G E  35                 P    0C E  36     1555   1555  1.60  
LINK         O3' 0DC E  38                 P    0G E  39     1555   1555  1.60  
LINK         O3'  0G E  39                 P    0C E  40     1555   1555  1.60  
LINK        CA    CA A 801                 O   HOH D 258     1555   1555  2.42  
LINK        CA    CA A 801                 O   HOH D 254     1555   1555  2.57  
LINK        CA    CA A 801                 O   HOH D 253     1555   1555  2.51  
LINK        CA    CA C 801                 O   HOH E 209     1555   1555  2.61  
LINK        CA    CA C 801                 O   HOH E 227     1555   1555  2.40  
LINK        CA    CA C 801                 O   HOH E 247     1555   1555  2.40  
LINK        CA    CA D 102                 O   HOH D 256     1555   1555  2.41  
LINK        CA    CA D 102                 O   HOH D 260     1555   1555  2.45  
LINK        CA    CA D 102                 O   HOH D 261     1555   1555  2.48  
LINK        CA    CA D 102                 O   HOH D 262     1555   1555  2.48  
LINK        CA    CA D 102                 O   HOH D 290     1555   1555  2.34  
LINK        CA    CA D 102                 O   HOH D 265     1555   1555  2.47  
LINK        MG    MG D 103                 O   HOH D 255     1555   1555  2.12  
LINK        MG    MG D 103                 O   HOH D 252     1555   1555  2.16  
LINK        MG    MG D 103                 O   HOH D 259     1555   1555  2.08  
LINK        MG    MG D 103                 O   HOH D 266     1555   1555  2.26  
LINK        CA    CA E 102                 O   HOH E 222     1555   1555  2.51  
LINK        CA    CA E 102                 O   HOH E 216     1555   1555  2.43  
LINK        CA    CA E 102                 O   HOH E 217     1555   1555  2.50  
LINK        CA    CA E 102                 O   HOH E 229     1555   1555  2.50  
LINK        CA    CA E 102                 O   HOH E 230     1555   1555  2.52  
LINK        CA    CA E 102                 O   HOH E 231     1555   1555  2.34  
LINK        MG    MG E 103                 O   HOH E 206     1555   1555  2.05  
LINK        MG    MG E 103                 O   HOH E 207     1555   1555  2.08  
LINK        MG    MG E 103                 O   HOH E 208     1555   1555  2.22  
LINK        MG    MG E 103                 O   HOH E 213     1555   1555  2.22  
CRYST1   45.840  282.630   45.760  90.00  90.00  90.00 P 21 21 2    12          
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      0.021815  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.003538  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021853        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system