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Database: PDB
Entry: 4OAU
LinkDB: 4OAU
Original site: 4OAU 
HEADER    HYDROLASE/RNA                           06-JAN-14   4OAU              
TITLE     COMPLETE HUMAN RNASE L IN COMPLEX WITH BIOLOGICAL ACTIVATORS.         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-5A-DEPENDENT RIBONUCLEASE;                               
COMPND   3 CHAIN: C;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 21-719;                                       
COMPND   5 SYNONYM: 2-5A-DEPENDENT RNASE, RIBONUCLEASE 4, RIBONUCLEASE L, RNASE 
COMPND   6 L;                                                                   
COMPND   7 EC: 3.1.26.-;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: RNA (5'-R(P*A*AP*A)-2');                                   
COMPND  12 CHAIN: A;                                                            
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RNASEL, RNS4;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 OTHER_DETAILS: CHEMICAL SYNTHESIS                                    
KEYWDS    RNASE L, RNASEL, 2-5A, 2',5'-OLIGOADENYLATE, INTERFERON, KEN,         
KEYWDS   2 PSEUDOKINASE, KINASE, INFLAMMATION, IRE1, RIDD, REGULATED RNA DECAY, 
KEYWDS   3 SPLICING CLEAVAGE, HPC1, HEREDITARY PROSTATE CANCER 1, RNASE L       
KEYWDS   4 KINASE-HOMOLOGY AND KEN DOMAIN-CONTAINING, INNATE IMMUNITY,          
KEYWDS   5 INTERFERON RESPONSE, ANTIVIRAL RESPONSE, 2-5A (2',5'-LINKED          
KEYWDS   6 OLIGOADENYLATE)AND RNA, HYDROLASE-RNA COMPLEX                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.HAN,J.DONOVAN,S.RATH,G.WHITNEY,A.CHITRAKAR,A.KORENNYKH              
REVDAT   2   02-APR-14 4OAU    1       JRNL                                     
REVDAT   1   12-MAR-14 4OAU    0                                                
JRNL        AUTH   Y.HAN,J.DONOVAN,S.RATH,G.WHITNEY,A.CHITRAKAR,A.KORENNYKH     
JRNL        TITL   STRUCTURE OF HUMAN RNASE L REVEALS THE BASIS FOR REGULATED   
JRNL        TITL 2 RNA DECAY IN THE IFN RESPONSE.                               
JRNL        REF    SCIENCE                       V. 343  1244 2014              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   24578532                                                     
JRNL        DOI    10.1126/SCIENCE.1249845                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 53.44                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1798                            
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 53.4535 -  6.1107    0.99     2801   147  0.1919 0.2073        
REMARK   3     2  6.1107 -  4.8513    1.00     2691   142  0.2011 0.2138        
REMARK   3     3  4.8513 -  4.2383    1.00     2651   140  0.1588 0.2258        
REMARK   3     4  4.2383 -  3.8509    1.00     2626   138  0.1777 0.2084        
REMARK   3     5  3.8509 -  3.5750    1.00     2630   139  0.1868 0.2515        
REMARK   3     6  3.5750 -  3.3642    1.00     2594   136  0.2010 0.2542        
REMARK   3     7  3.3642 -  3.1958    1.00     2611   138  0.2402 0.3036        
REMARK   3     8  3.1958 -  3.0567    1.00     2600   136  0.2463 0.3034        
REMARK   3     9  3.0567 -  2.9390    1.00     2604   138  0.2715 0.3235        
REMARK   3    10  2.9390 -  2.8376    1.00     2585   136  0.2919 0.3292        
REMARK   3    11  2.8376 -  2.7489    1.00     2574   135  0.3124 0.3750        
REMARK   3    12  2.7489 -  2.6703    1.00     2583   136  0.3239 0.3457        
REMARK   3    13  2.6703 -  2.6000    1.00     2594   137  0.3247 0.3430        
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)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.570           
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      :  0.003           5747                                  
REMARK   3   ANGLE     :  0.788           7761                                  
REMARK   3   CHIRALITY :  0.061            853                                  
REMARK   3   PLANARITY :  0.003            990                                  
REMARK   3   DIHEDRAL  : 20.991           3594                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A and (resid 1:3)                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.1477  -7.8617 -17.1830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4256 T22:   0.4407                                     
REMARK   3      T33:   0.3948 T12:  -0.0337                                     
REMARK   3      T13:  -0.0839 T23:   0.0431                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9528 L22:   0.5120                                     
REMARK   3      L33:   3.6844 L12:   0.0566                                     
REMARK   3      L13:  -2.2491 L23:  -0.2371                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0712 S12:   0.1831 S13:   0.0541                       
REMARK   3      S21:  -0.0723 S22:   0.0537 S23:   0.0961                       
REMARK   3      S31:   0.0847 S32:  -0.3113 S33:   0.0300                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain C and resid 331:437                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.0124 -32.9871  12.3325              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7326 T22:   0.4646                                     
REMARK   3      T33:   0.3941 T12:   0.0537                                     
REMARK   3      T13:   0.0038 T23:  -0.0331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.0326 L22:   7.2187                                     
REMARK   3      L33:   4.6573 L12:   0.2735                                     
REMARK   3      L13:  -0.8627 L23:   1.4975                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0714 S12:  -0.1739 S13:  -0.0632                       
REMARK   3      S21:  -0.0653 S22:  -0.3649 S23:   0.1608                       
REMARK   3      S31:   0.4149 S32:  -0.2258 S33:   0.2316                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain C and (resid 438:584 or resid 801 or resid       
REMARK   3               802:803)                                               
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0602 -55.0227  13.8441              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1017 T22:   0.4811                                     
REMARK   3      T33:   0.7815 T12:   0.1808                                     
REMARK   3      T13:   0.0659 T23:  -0.0122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9714 L22:   7.7501                                     
REMARK   3      L33:   2.3704 L12:  -1.2853                                     
REMARK   3      L13:   1.3603 L23:  -0.8334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0100 S12:  -0.2132 S13:  -0.8229                       
REMARK   3      S21:   0.4748 S22:  -0.0342 S23:  -0.6503                       
REMARK   3      S31:   0.5047 S32:   0.3231 S33:  -0.0118                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain C and resid 585:719                              
REMARK   3    ORIGIN FOR THE GROUP (A):   9.1432 -86.2206   9.0501              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8347 T22:   0.5853                                     
REMARK   3      T33:   1.5589 T12:   0.1614                                     
REMARK   3      T13:   0.2195 T23:   0.0284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4794 L22:   0.6338                                     
REMARK   3      L33:   2.3859 L12:   0.7786                                     
REMARK   3      L13:   0.0611 L23:   0.2491                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3026 S12:  -0.0162 S13:  -0.4112                       
REMARK   3      S21:  -0.1138 S22:   0.1845 S23:   0.5986                       
REMARK   3      S31:   0.5937 S32:  -0.0360 S33:   0.2577                       
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 4OAU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB084259.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28947                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 53.442                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RNASE L (21-719) (15 MG/ML IN BUFFER     
REMARK 280  CONTAINING 20 MM HEPES PH 7.5, 109 MM NACL, 5 MM MGCL 2, 5 MM       
REMARK 280  DTT, 2.8 MM ATP OR AMP-PCP, AND 10% GLYCEROL) WAS MIXED WITH 2-5A   
REMARK 280  AND RNA18 AT MOLAR RATIO 1:1.5:1.5, VAPOR DIFFUSION, TEMPERATURE    
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21                        
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,-Z+1/2                                         
REMARK 290       4555   -X+1/2,-Y,Z+1/2                                         
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       30.06500            
REMARK 290   SMTRY2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       81.20000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       30.06500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       81.20000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12060 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 60980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, A                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 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     ALA C    21                                                      
REMARK 465     ALA C    22                                                      
REMARK 465     VAL C    23                                                      
REMARK 465     GLU C    24                                                      
REMARK 465     GLY C   621                                                      
REMARK 465     PRO C   622                                                      
REMARK 465     SER C   623                                                      
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   O    HOH C   979     O    HOH C   990              1.91            
REMARK 500   OD2  ASP C   541     O    HOH C   961              1.96            
REMARK 500   OE2  GLU C   327     O    HOH C   931              2.01            
REMARK 500   O    HOH C   906     O    HOH C   918              2.04            
REMARK 500   O    LYS C   496     O    HOH C  1007              2.13            
REMARK 500   OD1  ASN C   601     NH1  ARG C   667              2.16            
REMARK 500   OE1  GLN C   473     OG   SER C   578              2.17            
REMARK 500   O    HIS C   263     O    HOH C   959              2.19            
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      A A   1   O4'     A A   1   C1'     0.086                       
REMARK 500      A A   1   N1      A A   1   C2      0.066                       
REMARK 500      A A   1   C2      A A   1   N3      0.134                       
REMARK 500      A A   1   N3      A A   1   C4      0.079                       
REMARK 500      A A   1   C4      A A   1   C5      0.066                       
REMARK 500      A A   1   C6      A A   1   N1      0.111                       
REMARK 500      A A   1   N7      A A   1   C8      0.196                       
REMARK 500      A A   1   N9      A A   1   C4      0.120                       
REMARK 500      A A   1   C6      A A   1   N6      0.107                       
REMARK 500      A A   2   O4'     A A   2   C1'     0.102                       
REMARK 500      A A   2   N3      A A   2   C4      0.136                       
REMARK 500      A A   2   C6      A A   2   N1      0.136                       
REMARK 500      A A   2   C5      A A   2   N7      0.122                       
REMARK 500      A A   2   N7      A A   2   C8      0.143                       
REMARK 500      A A   2   N9      A A   2   C4      0.158                       
REMARK 500      A A   2   C6      A A   2   N6      0.100                       
REMARK 500      A A   3   O4'     A A   3   C1'     0.082                       
REMARK 500      A A   3   C2      A A   3   N3      0.116                       
REMARK 500      A A   3   N3      A A   3   C4      0.056                       
REMARK 500      A A   3   C6      A A   3   N1      0.074                       
REMARK 500      A A   3   N7      A A   3   C8      0.102                       
REMARK 500      A A   3   C6      A A   3   N6      0.101                       
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      A A   1   OP1 -  P   -  OP2 ANGL. DEV. = -10.2 DEGREES          
REMARK 500      A A   1   C5' -  C4' -  O4' ANGL. DEV. =   8.5 DEGREES          
REMARK 500      A A   1   N9  -  C1' -  C2' ANGL. DEV. =  34.3 DEGREES          
REMARK 500      A A   1   O4' -  C1' -  N9  ANGL. DEV. = -12.9 DEGREES          
REMARK 500      A A   1   N1  -  C2  -  N3  ANGL. DEV. =  -9.4 DEGREES          
REMARK 500      A A   1   C2  -  N3  -  C4  ANGL. DEV. =   9.0 DEGREES          
REMARK 500      A A   1   N3  -  C4  -  C5  ANGL. DEV. =  -6.4 DEGREES          
REMARK 500      A A   1   C5  -  N7  -  C8  ANGL. DEV. =   3.6 DEGREES          
REMARK 500      A A   1   N7  -  C8  -  N9  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500      A A   2   C5' -  C4' -  O4' ANGL. DEV. =   8.3 DEGREES          
REMARK 500      A A   2   N9  -  C1' -  C2' ANGL. DEV. =  22.0 DEGREES          
REMARK 500      A A   2   O4' -  C1' -  N9  ANGL. DEV. =  -8.1 DEGREES          
REMARK 500      A A   2   N1  -  C2  -  N3  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500      A A   2   C2  -  N3  -  C4  ANGL. DEV. =   8.5 DEGREES          
REMARK 500      A A   2   N3  -  C4  -  C5  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500      A A   2   C4  -  C5  -  N7  ANGL. DEV. =  -3.1 DEGREES          
REMARK 500      A A   2   C5  -  N7  -  C8  ANGL. DEV. =   4.4 DEGREES          
REMARK 500      A A   2   N7  -  C8  -  N9  ANGL. DEV. =  -5.9 DEGREES          
REMARK 500      A A   2   N9  -  C4  -  C5  ANGL. DEV. =   2.6 DEGREES          
REMARK 500      A A   3   C5' -  C4' -  O4' ANGL. DEV. =   8.1 DEGREES          
REMARK 500      A A   3   N9  -  C1' -  C2' ANGL. DEV. =   9.0 DEGREES          
REMARK 500      A A   3   O4' -  C1' -  N9  ANGL. DEV. =  16.5 DEGREES          
REMARK 500      A A   3   N1  -  C2  -  N3  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500      A A   3   C2  -  N3  -  C4  ANGL. DEV. =   9.2 DEGREES          
REMARK 500      A A   3   N3  -  C4  -  C5  ANGL. DEV. =  -6.7 DEGREES          
REMARK 500      A A   3   C4  -  C5  -  C6  ANGL. DEV. =   3.1 DEGREES          
REMARK 500      A A   3   C4  -  C5  -  N7  ANGL. DEV. =  -3.0 DEGREES          
REMARK 500      A A   3   C5  -  N7  -  C8  ANGL. DEV. =   4.2 DEGREES          
REMARK 500      A A   3   N7  -  C8  -  N9  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP C 160      -70.95    -53.57                                   
REMARK 500    ASP C 270     -166.79    -75.38                                   
REMARK 500    ALA C 333       57.69    -67.90                                   
REMARK 500    TRP C 343     -150.39    -79.00                                   
REMARK 500    HIS C 426      -68.32   -123.34                                   
REMARK 500    ARG C 427       39.71   -140.76                                   
REMARK 500    ASP C 485       48.38   -153.21                                   
REMARK 500    ASP C 494     -176.28    -65.10                                   
REMARK 500    ASP C 503      103.61     59.98                                   
REMARK 500    LYS C 509      -93.91    -69.67                                   
REMARK 500    PRO C 555      -75.10    -56.52                                   
REMARK 500    CYS C 576       37.47    -78.17                                   
REMARK 500    LEU C 577      -31.52   -136.82                                   
REMARK 500    THR C 607       75.94   -100.15                                   
REMARK 500    ASN C 657       40.05    -78.96                                   
REMARK 500    GLU C 676       58.81    -99.57                                   
REMARK 500    LYS C 677       17.73   -153.27                                   
REMARK 500    TYR C 712       34.93    -77.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500      A A   1       -16.5      D          D   OUTSIDE RANGE           
REMARK 500      A A   2       -22.1      D          D   OUTSIDE RANGE           
REMARK 500      A A   3       -19.2      D          D   OUTSIDE RANGE           
REMARK 500    LYS C 496        23.7      L          L   OUTSIDE RANGE           
REMARK 500    ASN C 637        23.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 802  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP C 801   O1B                                                    
REMARK 620 2 ASN C 490   OD1 140.6                                              
REMARK 620 3 ASP C 503   OD2  82.4  91.3                                        
REMARK 620 4 ADP C 801   O2A  64.0  76.6  77.1                                  
REMARK 620 5 HOH C 923   O    91.9  72.7 147.0  71.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 803  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP C 801   O3B                                                    
REMARK 620 2 ASP C 503   OD2  83.4                                              
REMARK 620 3 ASP C 505   OD1  84.1 121.1                                        
REMARK 620 4 ASP C 503   OD1  75.5  54.7  66.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 803                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4OAV   RELATED DB: PDB                                   
DBREF  4OAU C   21   719  UNP    Q05823   RN5A_HUMAN      21    719             
DBREF  4OAU A    1     3  PDB    4OAU     4OAU             1      3             
SEQADV 4OAU ASN C  672  UNP  Q05823    HIS   672 ENGINEERED MUTATION            
SEQRES   1 C  699  ALA ALA VAL GLU ASP ASN HIS LEU LEU ILE LYS ALA VAL          
SEQRES   2 C  699  GLN ASN GLU ASP VAL ASP LEU VAL GLN GLN LEU LEU GLU          
SEQRES   3 C  699  GLY GLY ALA ASN VAL ASN PHE GLN GLU GLU GLU GLY GLY          
SEQRES   4 C  699  TRP THR PRO LEU HIS ASN ALA VAL GLN MET SER ARG GLU          
SEQRES   5 C  699  ASP ILE VAL GLU LEU LEU LEU ARG HIS GLY ALA ASP PRO          
SEQRES   6 C  699  VAL LEU ARG LYS LYS ASN GLY ALA THR PRO PHE ILE LEU          
SEQRES   7 C  699  ALA ALA ILE ALA GLY SER VAL LYS LEU LEU LYS LEU PHE          
SEQRES   8 C  699  LEU SER LYS GLY ALA ASP VAL ASN GLU CYS ASP PHE TYR          
SEQRES   9 C  699  GLY PHE THR ALA PHE MET GLU ALA ALA VAL TYR GLY LYS          
SEQRES  10 C  699  VAL LYS ALA LEU LYS PHE LEU TYR LYS ARG GLY ALA ASN          
SEQRES  11 C  699  VAL ASN LEU ARG ARG LYS THR LYS GLU ASP GLN GLU ARG          
SEQRES  12 C  699  LEU ARG LYS GLY GLY ALA THR ALA LEU MET ASP ALA ALA          
SEQRES  13 C  699  GLU LYS GLY HIS VAL GLU VAL LEU LYS ILE LEU LEU ASP          
SEQRES  14 C  699  GLU MET GLY ALA ASP VAL ASN ALA CYS ASP ASN MET GLY          
SEQRES  15 C  699  ARG ASN ALA LEU ILE HIS ALA LEU LEU SER SER ASP ASP          
SEQRES  16 C  699  SER ASP VAL GLU ALA ILE THR HIS LEU LEU LEU ASP HIS          
SEQRES  17 C  699  GLY ALA ASP VAL ASN VAL ARG GLY GLU ARG GLY LYS THR          
SEQRES  18 C  699  PRO LEU ILE LEU ALA VAL GLU LYS LYS HIS LEU GLY LEU          
SEQRES  19 C  699  VAL GLN ARG LEU LEU GLU GLN GLU HIS ILE GLU ILE ASN          
SEQRES  20 C  699  ASP THR ASP SER ASP GLY LYS THR ALA LEU LEU LEU ALA          
SEQRES  21 C  699  VAL GLU LEU LYS LEU LYS LYS ILE ALA GLU LEU LEU CYS          
SEQRES  22 C  699  LYS ARG GLY ALA SER THR ASP CYS GLY ASP LEU VAL MET          
SEQRES  23 C  699  THR ALA ARG ARG ASN TYR ASP HIS SER LEU VAL LYS VAL          
SEQRES  24 C  699  LEU LEU SER HIS GLY ALA LYS GLU ASP PHE HIS PRO PRO          
SEQRES  25 C  699  ALA GLU ASP TRP LYS PRO GLN SER SER HIS TRP GLY ALA          
SEQRES  26 C  699  ALA LEU LYS ASP LEU HIS ARG ILE TYR ARG PRO MET ILE          
SEQRES  27 C  699  GLY LYS LEU LYS PHE PHE ILE ASP GLU LYS TYR LYS ILE          
SEQRES  28 C  699  ALA ASP THR SER GLU GLY GLY ILE TYR LEU GLY PHE TYR          
SEQRES  29 C  699  GLU LYS GLN GLU VAL ALA VAL LYS THR PHE CYS GLU GLY          
SEQRES  30 C  699  SER PRO ARG ALA GLN ARG GLU VAL SER CYS LEU GLN SER          
SEQRES  31 C  699  SER ARG GLU ASN SER HIS LEU VAL THR PHE TYR GLY SER          
SEQRES  32 C  699  GLU SER HIS ARG GLY HIS LEU PHE VAL CYS VAL THR LEU          
SEQRES  33 C  699  CYS GLU GLN THR LEU GLU ALA CYS LEU ASP VAL HIS ARG          
SEQRES  34 C  699  GLY GLU ASP VAL GLU ASN GLU GLU ASP GLU PHE ALA ARG          
SEQRES  35 C  699  ASN VAL LEU SER SER ILE PHE LYS ALA VAL GLN GLU LEU          
SEQRES  36 C  699  HIS LEU SER CYS GLY TYR THR HIS GLN ASP LEU GLN PRO          
SEQRES  37 C  699  GLN ASN ILE LEU ILE ASP SER LYS LYS ALA ALA HIS LEU          
SEQRES  38 C  699  ALA ASP PHE ASP LYS SER ILE LYS TRP ALA GLY ASP PRO          
SEQRES  39 C  699  GLN GLU VAL LYS ARG ASP LEU GLU ASP LEU GLY ARG LEU          
SEQRES  40 C  699  VAL LEU TYR VAL VAL LYS LYS GLY SER ILE SER PHE GLU          
SEQRES  41 C  699  ASP LEU LYS ALA GLN SER ASN GLU GLU VAL VAL GLN LEU          
SEQRES  42 C  699  SER PRO ASP GLU GLU THR LYS ASP LEU ILE HIS ARG LEU          
SEQRES  43 C  699  PHE HIS PRO GLY GLU HIS VAL ARG ASP CYS LEU SER ASP          
SEQRES  44 C  699  LEU LEU GLY HIS PRO PHE PHE TRP THR TRP GLU SER ARG          
SEQRES  45 C  699  TYR ARG THR LEU ARG ASN VAL GLY ASN GLU SER ASP ILE          
SEQRES  46 C  699  LYS THR ARG LYS SER GLU SER GLU ILE LEU ARG LEU LEU          
SEQRES  47 C  699  GLN PRO GLY PRO SER GLU HIS SER LYS SER PHE ASP LYS          
SEQRES  48 C  699  TRP THR THR LYS ILE ASN GLU CYS VAL MET LYS LYS MET          
SEQRES  49 C  699  ASN LYS PHE TYR GLU LYS ARG GLY ASN PHE TYR GLN ASN          
SEQRES  50 C  699  THR VAL GLY ASP LEU LEU LYS PHE ILE ARG ASN LEU GLY          
SEQRES  51 C  699  GLU ASN ILE ASP GLU GLU LYS HIS LYS LYS MET LYS LEU          
SEQRES  52 C  699  LYS ILE GLY ASP PRO SER LEU TYR PHE GLN LYS THR PHE          
SEQRES  53 C  699  PRO ASP LEU VAL ILE TYR VAL TYR THR LYS LEU GLN ASN          
SEQRES  54 C  699  THR GLU TYR ARG LYS HIS PHE PRO GLN THR                      
SEQRES   1 A    3    A   A   A                                                  
HET    ADP  C 801      27                                                       
HET     MG  C 802       1                                                       
HET     MG  C 803       1                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3  ADP    C10 H15 N5 O10 P2                                            
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   6  HOH   *139(H2 O)                                                    
HELIX    1   1 HIS C   27  ASN C   35  1                                   9    
HELIX    2   2 ASP C   37  GLY C   48  1                                  12    
HELIX    3   3 THR C   61  MET C   69  1                                   9    
HELIX    4   4 ARG C   71  HIS C   81  1                                  11    
HELIX    5   5 THR C   94  GLY C  103  1                                  10    
HELIX    6   6 SER C  104  SER C  113  1                                  10    
HELIX    7   7 THR C  127  TYR C  135  1                                   9    
HELIX    8   8 LYS C  137  ARG C  147  1                                  11    
HELIX    9   9 LYS C  158  LEU C  164  1                                   7    
HELIX   10  10 THR C  170  GLY C  179  1                                  10    
HELIX   11  11 HIS C  180  GLU C  190  1                                  11    
HELIX   12  12 ASN C  204  SER C  212  1                                   9    
HELIX   13  13 ASP C  217  HIS C  228  1                                  12    
HELIX   14  14 THR C  241  LYS C  249  1                                   9    
HELIX   15  15 HIS C  251  LEU C  259  1                                   9    
HELIX   16  16 THR C  275  LEU C  283  1                                   9    
HELIX   17  17 LEU C  285  ARG C  295  1                                  11    
HELIX   18  18 ASP C  303  ASN C  311  1                                   9    
HELIX   19  19 ASP C  313  HIS C  323  1                                  11    
HELIX   20  20 GLY C  344  ILE C  353  1                                  10    
HELIX   21  21 SER C  398  SER C  410  1                                  13    
HELIX   22  22 LEU C  441  ASP C  452  1                                  12    
HELIX   23  23 ASP C  458  SER C  478  1                                  21    
HELIX   24  24 GLN C  487  GLN C  489  5                                   3    
HELIX   25  25 ASP C  513  LYS C  533  1                                  21    
HELIX   26  26 SER C  538  LYS C  543  1                                   6    
HELIX   27  27 GLU C  548  LEU C  553  1                                   6    
HELIX   28  28 ASP C  556  HIS C  568  1                                  13    
HELIX   29  29 SER C  578  TRP C  587  5                                  10    
HELIX   30  30 THR C  588  GLY C  600  1                                  13    
HELIX   31  31 GLU C  602  THR C  607  1                                   6    
HELIX   32  32 SER C  612  LEU C  618  1                                   7    
HELIX   33  33 LYS C  631  ILE C  636  1                                   6    
HELIX   34  34 GLU C  638  LYS C  646  1                                   9    
HELIX   35  35 PHE C  647  GLU C  649  5                                   3    
HELIX   36  36 THR C  658  ILE C  673  1                                  16    
HELIX   37  37 LYS C  679  GLY C  686  1                                   8    
HELIX   38  38 ASP C  687  PHE C  696  1                                  10    
HELIX   39  39 ASP C  698  GLN C  708  1                                  11    
SHEET    1   A 3 LYS C 362  PHE C 363  0                                        
SHEET    2   A 3 GLY C 377  PHE C 383 -1  O  PHE C 383   N  LYS C 362           
SHEET    3   A 3 LYS C 370  THR C 374 -1  N  ALA C 372   O  ILE C 379           
SHEET    1   B 5 LYS C 362  PHE C 363  0                                        
SHEET    2   B 5 GLY C 377  PHE C 383 -1  O  PHE C 383   N  LYS C 362           
SHEET    3   B 5 GLU C 388  CYS C 395 -1  O  VAL C 391   N  TYR C 380           
SHEET    4   B 5 HIS C 429  THR C 435 -1  O  VAL C 434   N  ALA C 390           
SHEET    5   B 5 PHE C 420  SER C 425 -1  N  GLY C 422   O  CYS C 433           
SHEET    1   C 3 GLN C 439  THR C 440  0                                        
SHEET    2   C 3 ILE C 491  ILE C 493 -1  O  ILE C 493   N  GLN C 439           
SHEET    3   C 3 ALA C 499  LEU C 501 -1  O  HIS C 500   N  LEU C 492           
LINK         O1B ADP C 801                MG    MG C 802     1555   1555  2.08  
LINK         O3B ADP C 801                MG    MG C 803     1555   1555  2.11  
LINK         OD1 ASN C 490                MG    MG C 802     1555   1555  2.14  
LINK         OD2 ASP C 503                MG    MG C 802     1555   1555  2.19  
LINK         OD2 ASP C 503                MG    MG C 803     1555   1555  2.30  
LINK         OD1 ASP C 505                MG    MG C 803     1555   1555  2.30  
LINK         OD1 ASP C 503                MG    MG C 803     1555   1555  2.46  
LINK         O2A ADP C 801                MG    MG C 802     1555   1555  2.46  
LINK        MG    MG C 802                 O   HOH C 923     1555   1555  2.21  
LINK         O2'   A A   2                 P     A A   3     1555   1555  1.58  
LINK         O2'   A A   1                 P     A A   2     1555   1555  1.58  
CISPEP   1 LYS C  496    LYS C  497          0         0.95                     
CISPEP   2 ASN C  637    GLU C  638          0         8.64                     
SITE     1 AC1 20 ILE C 371  ALA C 372  THR C 374  ILE C 379                    
SITE     2 AC1 20 ALA C 390  LYS C 392  VAL C 434  THR C 435                    
SITE     3 AC1 20 CYS C 437  THR C 440  GLN C 489  ASN C 490                    
SITE     4 AC1 20 LEU C 492  ASP C 503  ASP C 505   MG C 802                    
SITE     5 AC1 20  MG C 803  HOH C 923  HOH C 925  HOH C 993                    
SITE     1 AC2  6 GLN C 487  ASN C 490  ASP C 503  ADP C 801                    
SITE     2 AC2  6  MG C 803  HOH C 923                                          
SITE     1 AC3  4 ASP C 503  ASP C 505  ADP C 801   MG C 802                    
CRYST1   60.130  116.600  162.400  90.00  90.00  90.00 P 21 2 21     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      0.016631  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008576  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006158        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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