GenomeNet

Database: PDB
Entry: 4OAV
LinkDB: 4OAV
Original site: 4OAV 
HEADER    HYDROLASE/RNA                           06-JAN-14   4OAV              
TITLE     COMPLETE HUMAN RNASE L IN COMPLEX WITH 2-5A (5'-PPP HEPTAMER), AMPPCP 
TITLE    2 AND RNA SUBSTRATE.                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (RNASE L);                                         
COMPND   3 CHAIN: B, D;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: RNA (5'-R(P*(PO4)P*(PO4)P*AP*AP*AP*AP*(PO4))-2');          
COMPND   7 CHAIN: A, C;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 SYNTHETIC: YES;                                                      
SOURCE   8 OTHER_DETAILS: CHEMICAL SYNTHESIS                                    
KEYWDS    HPC1, 2-5A, 2',5'-OLIGOADENYLATE, INTERFERON, DSRNA, KINASE, RNASE,   
KEYWDS   2 RIDD, IRE1, RNA DECAY, RNASE L PROTEIN KINASE, PSEUDOKINASE, KEN-    
KEYWDS   3 DOMAIN CONTAINING, REGULATED RNA DECAY, INNATE IMMUNE RESPONSE,      
KEYWDS   4 ANTIVIRAL RESPONSE, DSRNA RESPONSE, 2',5'-LINKED OLIGOADENYLATES;    
KEYWDS   5 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 4OAV    1       JRNL                                     
REVDAT   1   12-MAR-14 4OAV    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.    2.10 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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.62                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 128099                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6405                            
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 46.6334 -  6.5194    0.99     4360   230  0.1795 0.1930        
REMARK   3     2  6.5194 -  5.1768    1.00     4200   222  0.1919 0.2220        
REMARK   3     3  5.1768 -  4.5231    1.00     4124   217  0.1572 0.1647        
REMARK   3     4  4.5231 -  4.1098    1.00     4146   218  0.1590 0.1710        
REMARK   3     5  4.1098 -  3.8154    1.00     4101   216  0.1667 0.1901        
REMARK   3     6  3.8154 -  3.5905    1.00     4089   215  0.1790 0.2200        
REMARK   3     7  3.5905 -  3.4108    1.00     4076   214  0.1838 0.1938        
REMARK   3     8  3.4108 -  3.2623    1.00     4038   213  0.1974 0.2339        
REMARK   3     9  3.2623 -  3.1368    1.00     4101   216  0.2051 0.2173        
REMARK   3    10  3.1368 -  3.0285    1.00     4060   214  0.2074 0.2482        
REMARK   3    11  3.0285 -  2.9339    1.00     4006   210  0.2065 0.2553        
REMARK   3    12  2.9339 -  2.8500    1.00     4091   216  0.2098 0.2783        
REMARK   3    13  2.8500 -  2.7750    1.00     4024   211  0.2154 0.2576        
REMARK   3    14  2.7750 -  2.7073    1.00     4045   213  0.2139 0.2570        
REMARK   3    15  2.7073 -  2.6458    1.00     4025   212  0.2143 0.2258        
REMARK   3    16  2.6458 -  2.5895    1.00     4021   212  0.2137 0.2831        
REMARK   3    17  2.5895 -  2.5377    1.00     4020   211  0.2202 0.2615        
REMARK   3    18  2.5377 -  2.4898    1.00     4049   214  0.2239 0.2568        
REMARK   3    19  2.4898 -  2.4453    1.00     4003   210  0.2219 0.2952        
REMARK   3    20  2.4453 -  2.4039    1.00     4036   212  0.2304 0.2865        
REMARK   3    21  2.4039 -  2.3651    1.00     4016   211  0.2378 0.2802        
REMARK   3    22  2.3651 -  2.3287    1.00     4028   212  0.2422 0.2847        
REMARK   3    23  2.3287 -  2.2945    1.00     4034   212  0.2334 0.2928        
REMARK   3    24  2.2945 -  2.2621    1.00     3949   208  0.2440 0.2963        
REMARK   3    25  2.2621 -  2.2316    1.00     4046   213  0.2485 0.2983        
REMARK   3    26  2.2316 -  2.2026    1.00     4047   213  0.2551 0.3062        
REMARK   3    27  2.2026 -  2.1751    1.00     3935   208  0.2656 0.3233        
REMARK   3    28  2.1751 -  2.1489    1.00     4037   211  0.2668 0.3163        
REMARK   3    29  2.1489 -  2.1239    1.00     4042   213  0.2770 0.3021        
REMARK   3    30  2.1239 -  2.1000    1.00     3945   208  0.2850 0.3167        
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.640           
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      :  0.004          11270                                  
REMARK   3   ANGLE     :  0.922          15244                                  
REMARK   3   CHIRALITY :  0.072           1677                                  
REMARK   3   PLANARITY :  0.003           1913                                  
REMARK   3   DIHEDRAL  : 20.844           6924                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN C AND (RESID 1:6 OR RESID 7:7 ) ) OR (CHAIN D   
REMARK   3               AND RESID 26:327 )                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  13.7076 -15.3912 107.7443              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3120 T22:   0.3882                                     
REMARK   3      T33:   0.3249 T12:   0.0432                                     
REMARK   3      T13:   0.0330 T23:  -0.0013                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6028 L22:   3.5428                                     
REMARK   3      L33:   0.4215 L12:   0.8611                                     
REMARK   3      L13:   0.0414 L23:  -0.3807                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0289 S12:  -0.0610 S13:  -0.0636                       
REMARK   3      S21:  -0.0147 S22:   0.0863 S23:   0.0097                       
REMARK   3      S31:   0.0304 S32:   0.0136 S33:  -0.0518                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN D AND RESID 336:436 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  12.6427  11.9779  82.3975              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4404 T22:   0.3465                                     
REMARK   3      T33:   0.2545 T12:  -0.0663                                     
REMARK   3      T13:  -0.0018 T23:  -0.0161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4469 L22:   2.7710                                     
REMARK   3      L33:   3.0227 L12:   0.9971                                     
REMARK   3      L13:   1.6002 L23:   0.6983                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0473 S12:   0.0927 S13:  -0.0024                       
REMARK   3      S21:  -0.1812 S22:   0.1201 S23:  -0.0492                       
REMARK   3      S31:  -0.0036 S32:   0.0369 S33:  -0.0710                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN D AND (RESID 437:586 OR RESID 1001:1003 ) )     
REMARK   3    ORIGIN FOR THE GROUP (A):   0.2438  12.6849  60.0183              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5571 T22:   0.5361                                     
REMARK   3      T33:   0.3302 T12:  -0.0869                                     
REMARK   3      T13:  -0.0338 T23:  -0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6427 L22:   1.9443                                     
REMARK   3      L33:   6.8643 L12:   0.3638                                     
REMARK   3      L13:   1.0175 L23:  -0.2662                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0677 S12:   0.3197 S13:  -0.0116                       
REMARK   3      S21:  -0.2103 S22:   0.0909 S23:   0.0373                       
REMARK   3      S31:  -0.1989 S32:  -0.3621 S33:  -0.0184                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN D AND (RESID 587:719 OR RESID 1004:1004 ) )     
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6871   8.6889  28.5636              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5925 T22:   0.5813                                     
REMARK   3      T33:   0.3332 T12:  -0.1224                                     
REMARK   3      T13:  -0.0496 T23:   0.0341                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5898 L22:   3.0221                                     
REMARK   3      L33:   6.7573 L12:  -0.7616                                     
REMARK   3      L13:  -0.9733 L23:   0.0659                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1404 S12:  -0.0528 S13:  -0.0525                       
REMARK   3      S21:  -0.0590 S22:  -0.1885 S23:  -0.0311                       
REMARK   3      S31:  -0.0845 S32:  -0.1645 S33:   0.0276                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND (RESID 1:6 OR RESID 7:7 ) ) OR (CHAIN B   
REMARK   3               AND RESID 24:327 )                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   8.5128  15.3748 107.1720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2899 T22:   0.3556                                     
REMARK   3      T33:   0.3111 T12:   0.0243                                     
REMARK   3      T13:  -0.0221 T23:  -0.0340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7005 L22:   2.3519                                     
REMARK   3      L33:   0.3027 L12:   0.8144                                     
REMARK   3      L13:   0.1696 L23:   0.3471                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0653 S12:  -0.0899 S13:   0.0798                       
REMARK   3      S21:  -0.0338 S22:   0.0370 S23:   0.2134                       
REMARK   3      S31:  -0.0027 S32:  -0.0485 S33:   0.0265                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 336:436 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  11.5027 -12.4956  82.5443              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4674 T22:   0.3717                                     
REMARK   3      T33:   0.2883 T12:  -0.0809                                     
REMARK   3      T13:   0.0045 T23:  -0.0254                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1373 L22:   2.7522                                     
REMARK   3      L33:   3.1384 L12:   0.4143                                     
REMARK   3      L13:  -1.6277 L23:  -1.1078                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0368 S12:   0.0804 S13:  -0.0942                       
REMARK   3      S21:  -0.0304 S22:   0.1671 S23:   0.1632                       
REMARK   3      S31:  -0.0859 S32:  -0.1928 S33:  -0.1227                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN B AND (RESID 437:586 OR RESID 801:803 ) )       
REMARK   3    ORIGIN FOR THE GROUP (A):  26.5704 -13.2543  61.8800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4993 T22:   0.4342                                     
REMARK   3      T33:   0.3101 T12:  -0.0766                                     
REMARK   3      T13:   0.0180 T23:  -0.0295                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6831 L22:   2.0537                                     
REMARK   3      L33:   7.1815 L12:   0.0325                                     
REMARK   3      L13:  -1.7812 L23:   0.0268                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0108 S12:   0.2434 S13:  -0.0347                       
REMARK   3      S21:  -0.1650 S22:   0.0291 S23:  -0.0785                       
REMARK   3      S31:   0.1792 S32:   0.3085 S33:  -0.0075                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN B AND (RESID 587:717 OR RESID 1012:1014 ) )     
REMARK   3    ORIGIN FOR THE GROUP (A):  26.5898  -9.1532  29.9256              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6183 T22:   0.6951                                     
REMARK   3      T33:   0.3207 T12:  -0.0464                                     
REMARK   3      T13:   0.0447 T23:   0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3502 L22:   3.8942                                     
REMARK   3      L33:   7.7383 L12:  -0.5285                                     
REMARK   3      L13:   0.6378 L23:   0.3491                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0275 S12:   0.3432 S13:  -0.0897                       
REMARK   3      S21:  -0.4595 S22:  -0.0722 S23:   0.0159                       
REMARK   3      S31:   0.3068 S32:   0.1460 S33:   0.0414                       
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 4OAV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB084260.                                      
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 CHANNEL11                   
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   : 128124                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
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: PDB ENTRY 4G8L                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41                     
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 MGCL2, 5 MM DTT,   
REMARK 280  2.8 MM ATP OR AMP-PCP, AND 10% GLYCEROL) WAS MIXED WITH 2-5A AND    
REMARK 280  RNA18 AT MOLAR RATIO 1:1.5:1, VAPOR DIFFUSION, TEMPERATURE 277K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       29.30500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      115.40000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       80.35000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      115.40000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.30500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       80.35000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: 13820 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 58100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, 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 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 B    21                                                      
REMARK 465     ALA B    22                                                      
REMARK 465     VAL B    23                                                      
REMARK 465     ASP B   328                                                      
REMARK 465     PHE B   329                                                      
REMARK 465     HIS B   330                                                      
REMARK 465     PRO B   331                                                      
REMARK 465     PRO B   332                                                      
REMARK 465     ALA B   333                                                      
REMARK 465     GLU B   334                                                      
REMARK 465     ASP B   335                                                      
REMARK 465     HIS B   448                                                      
REMARK 465     ARG B   449                                                      
REMARK 465     GLY B   450                                                      
REMARK 465     GLU B   451                                                      
REMARK 465     ASP B   452                                                      
REMARK 465     VAL B   453                                                      
REMARK 465     GLU B   454                                                      
REMARK 465     ASN B   455                                                      
REMARK 465     GLU B   675                                                      
REMARK 465     GLU B   676                                                      
REMARK 465     LYS B   677                                                      
REMARK 465     HIS B   678                                                      
REMARK 465     LYS B   679                                                      
REMARK 465     GLN B   718                                                      
REMARK 465     THR B   719                                                      
REMARK 465     ALA D    21                                                      
REMARK 465     ALA D    22                                                      
REMARK 465     VAL D    23                                                      
REMARK 465     GLU D    24                                                      
REMARK 465     ASP D    25                                                      
REMARK 465     ASP D   328                                                      
REMARK 465     PHE D   329                                                      
REMARK 465     HIS D   330                                                      
REMARK 465     PRO D   331                                                      
REMARK 465     PRO D   332                                                      
REMARK 465     ALA D   333                                                      
REMARK 465     GLU D   334                                                      
REMARK 465     ASP D   335                                                      
REMARK 465     HIS D   448                                                      
REMARK 465     ARG D   449                                                      
REMARK 465     GLY D   450                                                      
REMARK 465     GLU D   451                                                      
REMARK 465     ASP D   452                                                      
REMARK 465     VAL D   453                                                      
REMARK 465     GLU D   454                                                      
REMARK 465     GLU D   676                                                      
REMARK 465     LYS D   677                                                      
REMARK 465     HIS D   678                                                      
REMARK 465     LYS D   679                                                      
REMARK 465     LYS D   680                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PO4 A   2    O2                                                  
REMARK 470     PO4 A   7    O2                                                  
REMARK 470     PO4 C   2    O2                                                  
REMARK 470     PO4 C   7    O2                                                  
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 B  1042     O    HOH B  1147              1.82            
REMARK 500   OP2    A A     6     O    HOH A   111              1.85            
REMARK 500   OE1  GLN D   261     O    HOH D  1138              1.86            
REMARK 500   O    HOH D  1506     O    HOH D  1513              1.87            
REMARK 500   O    VAL D   532     O    HOH D  1249              1.87            
REMARK 500   OE1  GLU B   248     O    HOH B  1170              1.87            
REMARK 500   O    HOH B  1317     O    HOH A   112              1.88            
REMARK 500   NH1  ARG B   309     OE2  GLU B   327              1.91            
REMARK 500   O    HOH D  1395     O    HOH D  1446              1.94            
REMARK 500   O    HOH B  1260     O    HOH B  1266              1.96            
REMARK 500   OE2  GLU D   237     O    HOH D  1505              1.97            
REMARK 500   O    HOH B  1164     O    HOH B  1203              1.97            
REMARK 500   O    HOH D  1227     O    HOH D  1477              2.00            
REMARK 500   OG   SER B   411     O    HOH B   988              2.01            
REMARK 500   O    HOH B  1241     O    HOH B  1243              2.03            
REMARK 500   O    HOH D  1214     O    HOH D  1359              2.04            
REMARK 500   NZ   LYS D   606     O    HOH D  1475              2.04            
REMARK 500   O    HOH D  1229     O    HOH D  1499              2.04            
REMARK 500   OE2  GLU D   282     O    HOH D  1440              2.04            
REMARK 500   NE2  GLN D   489     O    HOH D  1411              2.05            
REMARK 500   O4   PO4 A     7     O    HOH A   108              2.05            
REMARK 500   OD2  ASP D   674     O    HOH D  1507              2.06            
REMARK 500   OD2  ASP B   160     O    HOH B  1227              2.06            
REMARK 500   O    HOH B  1003     O    HOH B  1197              2.07            
REMARK 500   O    HOH B  1184     O    HOH B  1292              2.08            
REMARK 500   O    CYS D   301     O    HOH D  1235              2.09            
REMARK 500   O    HOH D  1157     O    HOH D  1260              2.09            
REMARK 500   O06  PUP D  1004     O    HOH D  1128              2.09            
REMARK 500   OG   SER B   578     O    HOH B   998              2.10            
REMARK 500   OE2  GLU D    72     O    HOH D  1203              2.10            
REMARK 500   O    HOH D  1348     O    HOH D  1399              2.10            
REMARK 500   OG1  THR D   588     O    HOH D  1380              2.11            
REMARK 500   O3   PO4 C     1     O    HOH C   105              2.11            
REMARK 500   O    HOH D  1447     O    HOH D  1465              2.11            
REMARK 500   O3   PO4 A     1     O    HOH A   106              2.12            
REMARK 500   O    HOH B  1280     O    HOH B  1311              2.12            
REMARK 500   O    HOH B  1288     O    HOH B  1318              2.12            
REMARK 500   OE2  GLU B   474     O    HOH B  1239              2.12            
REMARK 500   O    HOH B  1011     O    HOH B  1182              2.12            
REMARK 500   O    HOH B  1142     O    HOH B  1319              2.13            
REMARK 500   O    HOH D  1421     O    HOH D  1472              2.14            
REMARK 500   O    HOH D  1316     O    HOH D  1528              2.14            
REMARK 500   O    HOH B  1320     O    HOH B  1324              2.15            
REMARK 500   OG   SER D   411     O    HOH D  1155              2.15            
REMARK 500   OD2  ASP D   214     OG   SER D   216              2.15            
REMARK 500   O    GLU B   237     O    HOH B  1035              2.16            
REMARK 500   O    HOH B  1153     O    HOH C   112              2.17            
REMARK 500   O    CYS B   301     O    HOH B   950              2.18            
REMARK 500   O    HOH D  1190     O    HOH D  1215              2.18            
REMARK 500   O    HOH B  1261     O    HOH C   114              2.19            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      51 CLOSE CONTACTS                                
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   3   C4'     A A   3   C3'    -0.070                       
REMARK 500      A A   3   C3'     A A   3   C2'    -0.095                       
REMARK 500      A A   3   C6      A A   3   N6      0.125                       
REMARK 500      A A   4   C4'     A A   4   C3'    -0.089                       
REMARK 500      A A   4   C3'     A A   4   C2'    -0.090                       
REMARK 500      A A   4   C2'     A A   4   C1'    -0.051                       
REMARK 500      A A   4   N7      A A   4   C8      0.044                       
REMARK 500      A A   4   C6      A A   4   N6      0.085                       
REMARK 500      A A   5   C3'     A A   5   C2'    -0.091                       
REMARK 500      A A   5   C6      A A   5   N6      0.136                       
REMARK 500      A A   6   C4'     A A   6   C3'    -0.071                       
REMARK 500      A A   6   C3'     A A   6   C2'    -0.077                       
REMARK 500      A A   6   C2'     A A   6   C1'    -0.050                       
REMARK 500      A A   6   N7      A A   6   C8      0.051                       
REMARK 500      A A   6   C6      A A   6   N6      0.145                       
REMARK 500      A C   3   C4'     A C   3   C3'    -0.067                       
REMARK 500      A C   3   C3'     A C   3   C2'    -0.099                       
REMARK 500      A C   3   C6      A C   3   N6      0.120                       
REMARK 500      A C   4   C4'     A C   4   C3'    -0.085                       
REMARK 500      A C   4   C3'     A C   4   C2'    -0.088                       
REMARK 500      A C   4   C2'     A C   4   C1'    -0.051                       
REMARK 500      A C   4   N7      A C   4   C8      0.045                       
REMARK 500      A C   4   C6      A C   4   N6      0.082                       
REMARK 500      A C   5   C3'     A C   5   C2'    -0.088                       
REMARK 500      A C   5   C6      A C   5   N6      0.137                       
REMARK 500      A C   6   C4'     A C   6   C3'    -0.070                       
REMARK 500      A C   6   C3'     A C   6   C2'    -0.085                       
REMARK 500      A C   6   C2'     A C   6   C1'    -0.056                       
REMARK 500      A C   6   N7      A C   6   C8      0.054                       
REMARK 500      A C   6   C6      A C   6   N6      0.143                       
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   3   OP1 -  P   -  OP2 ANGL. DEV. = -16.7 DEGREES          
REMARK 500      A A   3   N1  -  C2  -  N3  ANGL. DEV. =  -8.3 DEGREES          
REMARK 500      A A   3   C2  -  N3  -  C4  ANGL. DEV. =  10.4 DEGREES          
REMARK 500      A A   3   N3  -  C4  -  C5  ANGL. DEV. =  -7.6 DEGREES          
REMARK 500      A A   3   C4  -  C5  -  N7  ANGL. DEV. =  -3.6 DEGREES          
REMARK 500      A A   3   C5  -  N7  -  C8  ANGL. DEV. =   4.9 DEGREES          
REMARK 500      A A   3   N7  -  C8  -  N9  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500      A A   3   C8  -  N9  -  C4  ANGL. DEV. =   2.9 DEGREES          
REMARK 500      A A   3   N3  -  C4  -  N9  ANGL. DEV. =   6.6 DEGREES          
REMARK 500      A A   4   OP1 -  P   -  OP2 ANGL. DEV. = -17.2 DEGREES          
REMARK 500      A A   4   C6  -  N1  -  C2  ANGL. DEV. =   4.4 DEGREES          
REMARK 500      A A   4   N1  -  C2  -  N3  ANGL. DEV. =  -8.9 DEGREES          
REMARK 500      A A   4   C2  -  N3  -  C4  ANGL. DEV. =  10.4 DEGREES          
REMARK 500      A A   4   N3  -  C4  -  C5  ANGL. DEV. =  -8.2 DEGREES          
REMARK 500      A A   4   C4  -  C5  -  C6  ANGL. DEV. =   3.3 DEGREES          
REMARK 500      A A   4   C4  -  C5  -  N7  ANGL. DEV. =  -3.7 DEGREES          
REMARK 500      A A   4   C5  -  N7  -  C8  ANGL. DEV. =   4.4 DEGREES          
REMARK 500      A A   4   N7  -  C8  -  N9  ANGL. DEV. =  -4.4 DEGREES          
REMARK 500      A A   4   N3  -  C4  -  N9  ANGL. DEV. =   6.5 DEGREES          
REMARK 500      A A   5   OP1 -  P   -  OP2 ANGL. DEV. = -15.8 DEGREES          
REMARK 500      A A   5   C6  -  N1  -  C2  ANGL. DEV. =   3.9 DEGREES          
REMARK 500      A A   5   N1  -  C2  -  N3  ANGL. DEV. =  -9.3 DEGREES          
REMARK 500      A A   5   C2  -  N3  -  C4  ANGL. DEV. =  10.3 DEGREES          
REMARK 500      A A   5   N3  -  C4  -  C5  ANGL. DEV. =  -6.9 DEGREES          
REMARK 500      A A   5   C4  -  C5  -  N7  ANGL. DEV. =  -3.2 DEGREES          
REMARK 500      A A   5   C5  -  N7  -  C8  ANGL. DEV. =   4.2 DEGREES          
REMARK 500      A A   5   N7  -  C8  -  N9  ANGL. DEV. =  -4.6 DEGREES          
REMARK 500      A A   5   C8  -  N9  -  C4  ANGL. DEV. =   2.8 DEGREES          
REMARK 500      A A   5   N3  -  C4  -  N9  ANGL. DEV. =   6.1 DEGREES          
REMARK 500      A A   6   OP1 -  P   -  OP2 ANGL. DEV. =  -9.2 DEGREES          
REMARK 500      A A   6   C3' -  C2' -  C1' ANGL. DEV. =   4.8 DEGREES          
REMARK 500      A A   6   N1  -  C2  -  N3  ANGL. DEV. =  -8.4 DEGREES          
REMARK 500      A A   6   C2  -  N3  -  C4  ANGL. DEV. =  10.5 DEGREES          
REMARK 500      A A   6   N3  -  C4  -  C5  ANGL. DEV. =  -7.6 DEGREES          
REMARK 500      A A   6   C4  -  C5  -  N7  ANGL. DEV. =  -3.0 DEGREES          
REMARK 500      A A   6   C5  -  N7  -  C8  ANGL. DEV. =   4.1 DEGREES          
REMARK 500      A A   6   N7  -  C8  -  N9  ANGL. DEV. =  -4.2 DEGREES          
REMARK 500      A A   6   C8  -  N9  -  C4  ANGL. DEV. =   2.4 DEGREES          
REMARK 500      A A   6   N3  -  C4  -  N9  ANGL. DEV. =   6.9 DEGREES          
REMARK 500      A C   3   OP1 -  P   -  OP2 ANGL. DEV. = -16.9 DEGREES          
REMARK 500      A C   3   N1  -  C2  -  N3  ANGL. DEV. =  -8.7 DEGREES          
REMARK 500      A C   3   C2  -  N3  -  C4  ANGL. DEV. =  11.3 DEGREES          
REMARK 500      A C   3   N3  -  C4  -  C5  ANGL. DEV. =  -7.9 DEGREES          
REMARK 500      A C   3   C4  -  C5  -  N7  ANGL. DEV. =  -3.8 DEGREES          
REMARK 500      A C   3   C5  -  N7  -  C8  ANGL. DEV. =   4.9 DEGREES          
REMARK 500      A C   3   N7  -  C8  -  N9  ANGL. DEV. =  -5.3 DEGREES          
REMARK 500      A C   3   C8  -  N9  -  C4  ANGL. DEV. =   2.9 DEGREES          
REMARK 500      A C   3   N3  -  C4  -  N9  ANGL. DEV. =   6.6 DEGREES          
REMARK 500      A C   4   OP1 -  P   -  OP2 ANGL. DEV. = -16.7 DEGREES          
REMARK 500      A C   4   C6  -  N1  -  C2  ANGL. DEV. =   4.0 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      77 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    ASP B 215        1.72    -67.16                                   
REMARK 500    GLU B 237      -75.79    -53.63                                   
REMARK 500    ARG B 238       47.58    -81.97                                   
REMARK 500    CYS B 301       26.29   -150.10                                   
REMARK 500    ILE B 365       99.12    -69.95                                   
REMARK 500    GLU B 385       54.52   -154.31                                   
REMARK 500    HIS B 426      -80.74   -126.41                                   
REMARK 500    GLN B 484       -2.14     69.13                                   
REMARK 500    ASP B 485       38.68   -142.60                                   
REMARK 500    ASP B 503       91.26     65.74                                   
REMARK 500    ARG B 608       74.51    -50.79                                   
REMARK 500    SER B 610      -72.72    -57.46                                   
REMARK 500    PRO B 620     -176.62    -68.24                                   
REMARK 500    ASN B 657       35.36    -76.29                                   
REMARK 500    GLU D 237       49.79    -88.85                                   
REMARK 500    ARG D 238       44.05   -178.62                                   
REMARK 500    GLU D 385       53.00   -156.10                                   
REMARK 500    HIS D 426      -80.80   -116.87                                   
REMARK 500    GLN D 484       -2.68     73.22                                   
REMARK 500    ASP D 485       37.50   -142.34                                   
REMARK 500    ASP D 494     -174.23    -65.44                                   
REMARK 500    ASP D 503       95.24     64.72                                   
REMARK 500    ARG D 608       74.17    -45.53                                   
REMARK 500    PRO D 620      -90.17    -62.95                                   
REMARK 500    SER D 623       52.27   -116.09                                   
REMARK 500    SER D 626      102.25    -55.35                                   
REMARK 500    ASN D 657       30.07    -78.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU B  624     HIS B  625                 -148.39                    
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    LYS D 496        24.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS D 509        20.0      L          L   OUTSIDE RANGE           
REMARK 500    ASN D 637        24.3      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 B 803  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ACP B 801   O1B                                                    
REMARK 620 2 ASP B 503   OD1  88.4                                              
REMARK 620 3 ASP B 505   OD1 100.1  89.5                                        
REMARK 620 4 ASP B 503   OD2  87.7  60.0 148.5                                  
REMARK 620 5 HOH B1143   O   173.2  93.8  86.4  87.8                            
REMARK 620 6 HOH B 926   O    92.2 171.3  98.9 111.4  84.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 802  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ACP B 801   O2B                                                    
REMARK 620 2 ASP B 503   OD2  85.6                                              
REMARK 620 3 ASN B 490   OD1 170.8  87.8                                        
REMARK 620 4 ACP B 801   O1A  82.3  87.5  91.1                                  
REMARK 620 5 HOH B 907   O    86.4  92.2 100.3 168.7                            
REMARK 620 6 HOH B 918   O    90.7 172.0  96.6  99.0  80.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D1002  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D1492   O                                                      
REMARK 620 2 HOH D1122   O    83.8                                              
REMARK 620 3 ACP D1001   O1A 169.0  93.4                                        
REMARK 620 4 ASP D 503   OD2  91.8 175.4  90.7                                  
REMARK 620 5 ASN D 490   OD1  96.9  92.7  93.9  89.2                            
REMARK 620 6 ACP D1001   O2B  87.4  90.6  82.0  87.8 174.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D1003  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 505   OD1                                                    
REMARK 620 2 ACP D1001   O1B 104.0                                              
REMARK 620 3 HOH D1493   O   111.7  89.2                                        
REMARK 620 4 HOH D1494   O    88.3 167.2  89.3                                  
REMARK 620 5 ASP D 503   OD1  85.8  82.1 161.9  95.7                            
REMARK 620 6 ASP D 503   OD2 142.4  81.2 105.5  86.9  57.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP D 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PUP D 1004                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4OAU   RELATED DB: PDB                                   
DBREF  4OAV B   21   719  UNP    Q05823   RN5A_HUMAN      21    719             
DBREF  4OAV D   21   719  UNP    Q05823   RN5A_HUMAN      21    719             
DBREF  4OAV A    1     7  PDB    4OAV     4OAV             1      7             
DBREF  4OAV C    1     7  PDB    4OAV     4OAV             1      7             
SEQADV 4OAV ASN B  672  UNP  Q05823    HIS   672 ENGINEERED MUTATION            
SEQADV 4OAV ASN D  672  UNP  Q05823    HIS   672 ENGINEERED MUTATION            
SEQRES   1 B  699  ALA ALA VAL GLU ASP ASN HIS LEU LEU ILE LYS ALA VAL          
SEQRES   2 B  699  GLN ASN GLU ASP VAL ASP LEU VAL GLN GLN LEU LEU GLU          
SEQRES   3 B  699  GLY GLY ALA ASN VAL ASN PHE GLN GLU GLU GLU GLY GLY          
SEQRES   4 B  699  TRP THR PRO LEU HIS ASN ALA VAL GLN MET SER ARG GLU          
SEQRES   5 B  699  ASP ILE VAL GLU LEU LEU LEU ARG HIS GLY ALA ASP PRO          
SEQRES   6 B  699  VAL LEU ARG LYS LYS ASN GLY ALA THR PRO PHE ILE LEU          
SEQRES   7 B  699  ALA ALA ILE ALA GLY SER VAL LYS LEU LEU LYS LEU PHE          
SEQRES   8 B  699  LEU SER LYS GLY ALA ASP VAL ASN GLU CYS ASP PHE TYR          
SEQRES   9 B  699  GLY PHE THR ALA PHE MET GLU ALA ALA VAL TYR GLY LYS          
SEQRES  10 B  699  VAL LYS ALA LEU LYS PHE LEU TYR LYS ARG GLY ALA ASN          
SEQRES  11 B  699  VAL ASN LEU ARG ARG LYS THR LYS GLU ASP GLN GLU ARG          
SEQRES  12 B  699  LEU ARG LYS GLY GLY ALA THR ALA LEU MET ASP ALA ALA          
SEQRES  13 B  699  GLU LYS GLY HIS VAL GLU VAL LEU LYS ILE LEU LEU ASP          
SEQRES  14 B  699  GLU MET GLY ALA ASP VAL ASN ALA CYS ASP ASN MET GLY          
SEQRES  15 B  699  ARG ASN ALA LEU ILE HIS ALA LEU LEU SER SER ASP ASP          
SEQRES  16 B  699  SER ASP VAL GLU ALA ILE THR HIS LEU LEU LEU ASP HIS          
SEQRES  17 B  699  GLY ALA ASP VAL ASN VAL ARG GLY GLU ARG GLY LYS THR          
SEQRES  18 B  699  PRO LEU ILE LEU ALA VAL GLU LYS LYS HIS LEU GLY LEU          
SEQRES  19 B  699  VAL GLN ARG LEU LEU GLU GLN GLU HIS ILE GLU ILE ASN          
SEQRES  20 B  699  ASP THR ASP SER ASP GLY LYS THR ALA LEU LEU LEU ALA          
SEQRES  21 B  699  VAL GLU LEU LYS LEU LYS LYS ILE ALA GLU LEU LEU CYS          
SEQRES  22 B  699  LYS ARG GLY ALA SER THR ASP CYS GLY ASP LEU VAL MET          
SEQRES  23 B  699  THR ALA ARG ARG ASN TYR ASP HIS SER LEU VAL LYS VAL          
SEQRES  24 B  699  LEU LEU SER HIS GLY ALA LYS GLU ASP PHE HIS PRO PRO          
SEQRES  25 B  699  ALA GLU ASP TRP LYS PRO GLN SER SER HIS TRP GLY ALA          
SEQRES  26 B  699  ALA LEU LYS ASP LEU HIS ARG ILE TYR ARG PRO MET ILE          
SEQRES  27 B  699  GLY LYS LEU LYS PHE PHE ILE ASP GLU LYS TYR LYS ILE          
SEQRES  28 B  699  ALA ASP THR SER GLU GLY GLY ILE TYR LEU GLY PHE TYR          
SEQRES  29 B  699  GLU LYS GLN GLU VAL ALA VAL LYS THR PHE CYS GLU GLY          
SEQRES  30 B  699  SER PRO ARG ALA GLN ARG GLU VAL SER CYS LEU GLN SER          
SEQRES  31 B  699  SER ARG GLU ASN SER HIS LEU VAL THR PHE TYR GLY SER          
SEQRES  32 B  699  GLU SER HIS ARG GLY HIS LEU PHE VAL CYS VAL THR LEU          
SEQRES  33 B  699  CYS GLU GLN THR LEU GLU ALA CYS LEU ASP VAL HIS ARG          
SEQRES  34 B  699  GLY GLU ASP VAL GLU ASN GLU GLU ASP GLU PHE ALA ARG          
SEQRES  35 B  699  ASN VAL LEU SER SER ILE PHE LYS ALA VAL GLN GLU LEU          
SEQRES  36 B  699  HIS LEU SER CYS GLY TYR THR HIS GLN ASP LEU GLN PRO          
SEQRES  37 B  699  GLN ASN ILE LEU ILE ASP SER LYS LYS ALA ALA HIS LEU          
SEQRES  38 B  699  ALA ASP PHE ASP LYS SER ILE LYS TRP ALA GLY ASP PRO          
SEQRES  39 B  699  GLN GLU VAL LYS ARG ASP LEU GLU ASP LEU GLY ARG LEU          
SEQRES  40 B  699  VAL LEU TYR VAL VAL LYS LYS GLY SER ILE SER PHE GLU          
SEQRES  41 B  699  ASP LEU LYS ALA GLN SER ASN GLU GLU VAL VAL GLN LEU          
SEQRES  42 B  699  SER PRO ASP GLU GLU THR LYS ASP LEU ILE HIS ARG LEU          
SEQRES  43 B  699  PHE HIS PRO GLY GLU HIS VAL ARG ASP CYS LEU SER ASP          
SEQRES  44 B  699  LEU LEU GLY HIS PRO PHE PHE TRP THR TRP GLU SER ARG          
SEQRES  45 B  699  TYR ARG THR LEU ARG ASN VAL GLY ASN GLU SER ASP ILE          
SEQRES  46 B  699  LYS THR ARG LYS SER GLU SER GLU ILE LEU ARG LEU LEU          
SEQRES  47 B  699  GLN PRO GLY PRO SER GLU HIS SER LYS SER PHE ASP LYS          
SEQRES  48 B  699  TRP THR THR LYS ILE ASN GLU CYS VAL MET LYS LYS MET          
SEQRES  49 B  699  ASN LYS PHE TYR GLU LYS ARG GLY ASN PHE TYR GLN ASN          
SEQRES  50 B  699  THR VAL GLY ASP LEU LEU LYS PHE ILE ARG ASN LEU GLY          
SEQRES  51 B  699  GLU ASN ILE ASP GLU GLU LYS HIS LYS LYS MET LYS LEU          
SEQRES  52 B  699  LYS ILE GLY ASP PRO SER LEU TYR PHE GLN LYS THR PHE          
SEQRES  53 B  699  PRO ASP LEU VAL ILE TYR VAL TYR THR LYS LEU GLN ASN          
SEQRES  54 B  699  THR GLU TYR ARG LYS HIS PHE PRO GLN THR                      
SEQRES   1 A    7  PO4 PO4   A   A   A   A PO4                                  
SEQRES   1 D  699  ALA ALA VAL GLU ASP ASN HIS LEU LEU ILE LYS ALA VAL          
SEQRES   2 D  699  GLN ASN GLU ASP VAL ASP LEU VAL GLN GLN LEU LEU GLU          
SEQRES   3 D  699  GLY GLY ALA ASN VAL ASN PHE GLN GLU GLU GLU GLY GLY          
SEQRES   4 D  699  TRP THR PRO LEU HIS ASN ALA VAL GLN MET SER ARG GLU          
SEQRES   5 D  699  ASP ILE VAL GLU LEU LEU LEU ARG HIS GLY ALA ASP PRO          
SEQRES   6 D  699  VAL LEU ARG LYS LYS ASN GLY ALA THR PRO PHE ILE LEU          
SEQRES   7 D  699  ALA ALA ILE ALA GLY SER VAL LYS LEU LEU LYS LEU PHE          
SEQRES   8 D  699  LEU SER LYS GLY ALA ASP VAL ASN GLU CYS ASP PHE TYR          
SEQRES   9 D  699  GLY PHE THR ALA PHE MET GLU ALA ALA VAL TYR GLY LYS          
SEQRES  10 D  699  VAL LYS ALA LEU LYS PHE LEU TYR LYS ARG GLY ALA ASN          
SEQRES  11 D  699  VAL ASN LEU ARG ARG LYS THR LYS GLU ASP GLN GLU ARG          
SEQRES  12 D  699  LEU ARG LYS GLY GLY ALA THR ALA LEU MET ASP ALA ALA          
SEQRES  13 D  699  GLU LYS GLY HIS VAL GLU VAL LEU LYS ILE LEU LEU ASP          
SEQRES  14 D  699  GLU MET GLY ALA ASP VAL ASN ALA CYS ASP ASN MET GLY          
SEQRES  15 D  699  ARG ASN ALA LEU ILE HIS ALA LEU LEU SER SER ASP ASP          
SEQRES  16 D  699  SER ASP VAL GLU ALA ILE THR HIS LEU LEU LEU ASP HIS          
SEQRES  17 D  699  GLY ALA ASP VAL ASN VAL ARG GLY GLU ARG GLY LYS THR          
SEQRES  18 D  699  PRO LEU ILE LEU ALA VAL GLU LYS LYS HIS LEU GLY LEU          
SEQRES  19 D  699  VAL GLN ARG LEU LEU GLU GLN GLU HIS ILE GLU ILE ASN          
SEQRES  20 D  699  ASP THR ASP SER ASP GLY LYS THR ALA LEU LEU LEU ALA          
SEQRES  21 D  699  VAL GLU LEU LYS LEU LYS LYS ILE ALA GLU LEU LEU CYS          
SEQRES  22 D  699  LYS ARG GLY ALA SER THR ASP CYS GLY ASP LEU VAL MET          
SEQRES  23 D  699  THR ALA ARG ARG ASN TYR ASP HIS SER LEU VAL LYS VAL          
SEQRES  24 D  699  LEU LEU SER HIS GLY ALA LYS GLU ASP PHE HIS PRO PRO          
SEQRES  25 D  699  ALA GLU ASP TRP LYS PRO GLN SER SER HIS TRP GLY ALA          
SEQRES  26 D  699  ALA LEU LYS ASP LEU HIS ARG ILE TYR ARG PRO MET ILE          
SEQRES  27 D  699  GLY LYS LEU LYS PHE PHE ILE ASP GLU LYS TYR LYS ILE          
SEQRES  28 D  699  ALA ASP THR SER GLU GLY GLY ILE TYR LEU GLY PHE TYR          
SEQRES  29 D  699  GLU LYS GLN GLU VAL ALA VAL LYS THR PHE CYS GLU GLY          
SEQRES  30 D  699  SER PRO ARG ALA GLN ARG GLU VAL SER CYS LEU GLN SER          
SEQRES  31 D  699  SER ARG GLU ASN SER HIS LEU VAL THR PHE TYR GLY SER          
SEQRES  32 D  699  GLU SER HIS ARG GLY HIS LEU PHE VAL CYS VAL THR LEU          
SEQRES  33 D  699  CYS GLU GLN THR LEU GLU ALA CYS LEU ASP VAL HIS ARG          
SEQRES  34 D  699  GLY GLU ASP VAL GLU ASN GLU GLU ASP GLU PHE ALA ARG          
SEQRES  35 D  699  ASN VAL LEU SER SER ILE PHE LYS ALA VAL GLN GLU LEU          
SEQRES  36 D  699  HIS LEU SER CYS GLY TYR THR HIS GLN ASP LEU GLN PRO          
SEQRES  37 D  699  GLN ASN ILE LEU ILE ASP SER LYS LYS ALA ALA HIS LEU          
SEQRES  38 D  699  ALA ASP PHE ASP LYS SER ILE LYS TRP ALA GLY ASP PRO          
SEQRES  39 D  699  GLN GLU VAL LYS ARG ASP LEU GLU ASP LEU GLY ARG LEU          
SEQRES  40 D  699  VAL LEU TYR VAL VAL LYS LYS GLY SER ILE SER PHE GLU          
SEQRES  41 D  699  ASP LEU LYS ALA GLN SER ASN GLU GLU VAL VAL GLN LEU          
SEQRES  42 D  699  SER PRO ASP GLU GLU THR LYS ASP LEU ILE HIS ARG LEU          
SEQRES  43 D  699  PHE HIS PRO GLY GLU HIS VAL ARG ASP CYS LEU SER ASP          
SEQRES  44 D  699  LEU LEU GLY HIS PRO PHE PHE TRP THR TRP GLU SER ARG          
SEQRES  45 D  699  TYR ARG THR LEU ARG ASN VAL GLY ASN GLU SER ASP ILE          
SEQRES  46 D  699  LYS THR ARG LYS SER GLU SER GLU ILE LEU ARG LEU LEU          
SEQRES  47 D  699  GLN PRO GLY PRO SER GLU HIS SER LYS SER PHE ASP LYS          
SEQRES  48 D  699  TRP THR THR LYS ILE ASN GLU CYS VAL MET LYS LYS MET          
SEQRES  49 D  699  ASN LYS PHE TYR GLU LYS ARG GLY ASN PHE TYR GLN ASN          
SEQRES  50 D  699  THR VAL GLY ASP LEU LEU LYS PHE ILE ARG ASN LEU GLY          
SEQRES  51 D  699  GLU ASN ILE ASP GLU GLU LYS HIS LYS LYS MET LYS LEU          
SEQRES  52 D  699  LYS ILE GLY ASP PRO SER LEU TYR PHE GLN LYS THR PHE          
SEQRES  53 D  699  PRO ASP LEU VAL ILE TYR VAL TYR THR LYS LEU GLN ASN          
SEQRES  54 D  699  THR GLU TYR ARG LYS HIS PHE PRO GLN THR                      
SEQRES   1 C    7  PO4 PO4   A   A   A   A PO4                                  
HET    PO4  A   1       5                                                       
HET    PO4  A   2       4                                                       
HET    PO4  A   7       4                                                       
HET    PO4  C   1       5                                                       
HET    PO4  C   2       4                                                       
HET    PO4  C   7       4                                                       
HET    ACP  B 801      31                                                       
HET     MG  B 802       1                                                       
HET     MG  B 803       1                                                       
HET    ACP  D1001      31                                                       
HET     MG  D1002       1                                                       
HET     MG  D1003       1                                                       
HET    PUP  D1004      33                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER                     
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     PUP (2R,3S,4R,5R)-5-(2,4-DIOXO-3,4-DIHYDROPYRIMIDIN-1(2H)-           
HETNAM   2 PUP  YL)-4-HYDROXY-2-({[(S)-HYDROXY{[(2R,3S,4S)-4-HYDROXY-           
HETNAM   3 PUP  2-(HYDROXYMETHYL)TETRAHYDROFURAN-3-                             
HETNAM   4 PUP  YL]OXY}PHOSPHORYL]OXY}METHYL)TETRAHYDROFURAN-3-YL               
HETNAM   5 PUP  DIHYDROGEN PHOSPHATE                                            
HETSYN     ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE                 
FORMUL   2  PO4    6(O4 P 3-)                                                   
FORMUL   5  ACP    2(C11 H18 N5 O12 P3)                                         
FORMUL   6   MG    4(MG 2+)                                                     
FORMUL  11  PUP    C14 H22 N2 O15 P2                                            
FORMUL  12  HOH   *911(H2 O)                                                    
HELIX    1   1 GLU B   24  ASN B   35  1                                  12    
HELIX    2   2 ASP B   37  GLY B   47  1                                  11    
HELIX    3   3 THR B   61  MET B   69  1                                   9    
HELIX    4   4 ARG B   71  HIS B   81  1                                  11    
HELIX    5   5 THR B   94  GLY B  103  1                                  10    
HELIX    6   6 SER B  104  SER B  113  1                                  10    
HELIX    7   7 THR B  127  TYR B  135  1                                   9    
HELIX    8   8 LYS B  137  ARG B  147  1                                  11    
HELIX    9   9 LYS B  158  LEU B  164  1                                   7    
HELIX   10  10 THR B  170  LYS B  178  1                                   9    
HELIX   11  11 HIS B  180  MET B  191  1                                  12    
HELIX   12  12 ASN B  204  LEU B  210  1                                   7    
HELIX   13  13 ASP B  217  HIS B  228  1                                  12    
HELIX   14  14 THR B  241  LYS B  249  1                                   9    
HELIX   15  15 HIS B  251  GLU B  260  1                                  10    
HELIX   16  16 THR B  275  LEU B  283  1                                   9    
HELIX   17  17 LEU B  285  ARG B  295  1                                  11    
HELIX   18  18 ASP B  303  ASN B  311  1                                   9    
HELIX   19  19 ASP B  313  HIS B  323  1                                  11    
HELIX   20  20 GLY B  344  ILE B  353  1                                  10    
HELIX   21  21 ASP B  366  LYS B  368  5                                   3    
HELIX   22  22 SER B  398  SER B  410  1                                  13    
HELIX   23  23 LEU B  441  ASP B  446  1                                   6    
HELIX   24  24 ASP B  458  SER B  478  1                                  21    
HELIX   25  25 GLN B  487  GLN B  489  5                                   3    
HELIX   26  26 ASP B  513  LYS B  533  1                                  21    
HELIX   27  27 SER B  538  GLN B  545  1                                   8    
HELIX   28  28 SER B  546  GLN B  552  1                                   7    
HELIX   29  29 ASP B  556  HIS B  568  1                                  13    
HELIX   30  30 ASP B  575  LEU B  581  1                                   7    
HELIX   31  31 GLY B  582  TRP B  587  5                                   6    
HELIX   32  32 THR B  588  ASN B  601  1                                  14    
HELIX   33  33 GLU B  602  THR B  607  1                                   6    
HELIX   34  34 SER B  612  GLN B  619  1                                   8    
HELIX   35  35 LYS B  631  LYS B  635  5                                   5    
HELIX   36  36 ASN B  637  LYS B  646  1                                  10    
HELIX   37  37 PHE B  647  GLU B  649  5                                   3    
HELIX   38  38 THR B  658  ILE B  673  1                                  16    
HELIX   39  39 MET B  681  GLY B  686  1                                   6    
HELIX   40  40 ASP B  687  PHE B  696  1                                  10    
HELIX   41  41 ASP B  698  GLN B  708  1                                  11    
HELIX   42  42 THR B  710  PHE B  716  5                                   7    
HELIX   43  43 HIS D   27  ASN D   35  1                                   9    
HELIX   44  44 ASP D   37  GLY D   47  1                                  11    
HELIX   45  45 THR D   61  MET D   69  1                                   9    
HELIX   46  46 ARG D   71  HIS D   81  1                                  11    
HELIX   47  47 THR D   94  GLY D  103  1                                  10    
HELIX   48  48 SER D  104  SER D  113  1                                  10    
HELIX   49  49 THR D  127  TYR D  135  1                                   9    
HELIX   50  50 LYS D  137  ARG D  147  1                                  11    
HELIX   51  53 HIS D  180  MET D  191  1                                  12    
HELIX   52  54 ASN D  204  LEU D  210  1                                   7    
HELIX   53  56 THR D  241  LYS D  249  1                                   9    
HELIX   54  57 HIS D  251  GLU D  260  1                                  10    
HELIX   55  58 THR D  275  LEU D  283  1                                   9    
HELIX   56  59 LEU D  285  ARG D  295  1                                  11    
HELIX   57  60 ASP D  303  ASN D  311  1                                   9    
HELIX   58  61 ASP D  313  HIS D  323  1                                  11    
HELIX   59  64 SER D  398  SER D  410  1                                  13    
HELIX   60  65 LEU D  441  VAL D  447  1                                   7    
HELIX   61  66 ASP D  458  SER D  478  1                                  21    
HELIX   62  67 GLN D  487  GLN D  489  5                                   3    
HELIX   63  68 ASP D  513  LYS D  533  1                                  21    
HELIX   64  69 SER D  538  GLN D  545  1                                   8    
HELIX   65  70 SER D  546  GLN D  552  1                                   7    
HELIX   66  71 ASP D  556  HIS D  568  1                                  13    
HELIX   67  72 ASP D  575  LEU D  581  1                                   7    
HELIX   68  73 GLY D  582  TRP D  587  5                                   6    
HELIX   69  74 THR D  588  ASN D  601  1                                  14    
HELIX   70  75 GLU D  602  THR D  607  1                                   6    
HELIX   71  76 SER D  612  GLN D  619  1                                   8    
HELIX   72  77 LYS D  631  LYS D  635  5                                   5    
HELIX   73  78 GLU D  638  LYS D  646  1                                   9    
HELIX   74  79 PHE D  647  GLU D  649  5                                   3    
HELIX   75  80 THR D  658  GLU D  675  1                                  18    
HELIX   76  81 LYS D  682  GLY D  686  1                                   5    
HELIX   77  82 ASP D  687  PHE D  696  1                                  10    
HELIX   78  83 ASP D  698  GLN D  708  1                                  11    
SHEET    1   A 3 LYS B 362  PHE B 363  0                                        
SHEET    2   A 3 GLY B 377  PHE B 383 -1  O  PHE B 383   N  LYS B 362           
SHEET    3   A 3 LYS B 370  THR B 374 -1  N  ILE B 371   O  ILE B 379           
SHEET    1   B 5 LYS B 362  PHE B 363  0                                        
SHEET    2   B 5 GLY B 377  PHE B 383 -1  O  PHE B 383   N  LYS B 362           
SHEET    3   B 5 GLU B 388  CYS B 395 -1  O  VAL B 391   N  TYR B 380           
SHEET    4   B 5 HIS B 429  THR B 435 -1  O  VAL B 434   N  ALA B 390           
SHEET    5   B 5 PHE B 420  SER B 425 -1  N  GLU B 424   O  PHE B 431           
SHEET    1   C 3 GLN B 439  THR B 440  0                                        
SHEET    2   C 3 ILE B 491  ILE B 493 -1  O  ILE B 493   N  GLN B 439           
SHEET    3   C 3 ALA B 499  LEU B 501 -1  O  HIS B 500   N  LEU B 492           
SHEET    1   D 2 TYR B 481  THR B 482  0                                        
SHEET    2   D 2 ILE B 508  LYS B 509 -1  O  ILE B 508   N  THR B 482           
SHEET    1   E 3 LYS D 362  PHE D 363  0                                        
SHEET    2   E 3 LYS D 370  THR D 374 -1  N  ILE D 371   O  ILE D 379           
SHEET    1   F 5 LYS D 362  PHE D 363  0                                        
SHEET    2   F 5 GLU D 388  CYS D 395 -1  O  VAL D 391   N  TYR D 380           
SHEET    3   F 5 HIS D 429  THR D 435 -1  O  VAL D 432   N  LYS D 392           
SHEET    4   F 5 PHE D 420  SER D 425 -1  N  GLU B 404   O  PHE D 431           
SHEET    1   G 3 GLN D 439  THR D 440  0                                        
SHEET    2   G 3 ILE D 491  ILE D 493 -1  O  ILE D 493   N  GLN D 439           
SHEET    3   G 3 ALA D 499  LEU D 501 -1  O  HIS D 500   N  LEU D 492           
LINK         O1B ACP B 801                MG    MG B 803     1555   1555  2.03  
LINK         OD1 ASP B 503                MG    MG B 803     1555   1555  2.03  
LINK         O2B ACP B 801                MG    MG B 802     1555   1555  2.07  
LINK         OD2 ASP B 503                MG    MG B 802     1555   1555  2.08  
LINK         OD1 ASN B 490                MG    MG B 802     1555   1555  2.09  
LINK         O1A ACP B 801                MG    MG B 802     1555   1555  2.10  
LINK         OD1 ASP B 505                MG    MG B 803     1555   1555  2.19  
LINK         OD2 ASP B 503                MG    MG B 803     1555   1555  2.32  
LINK        MG    MG D1002                 O   HOH D1492     1555   1555  1.86  
LINK        MG    MG B 803                 O   HOH B1143     1555   1555  1.95  
LINK        MG    MG D1002                 O   HOH D1122     1555   1555  1.98  
LINK        MG    MG B 803                 O   HOH B 926     1555   1555  2.01  
LINK         OD1 ASP D 505                MG    MG D1003     1555   1555  2.02  
LINK         O1A ACP D1001                MG    MG D1002     1555   1555  2.03  
LINK         O1B ACP D1001                MG    MG D1003     1555   1555  2.04  
LINK         OD2 ASP D 503                MG    MG D1002     1555   1555  2.07  
LINK        MG    MG D1003                 O   HOH D1493     1555   1555  2.08  
LINK        MG    MG B 802                 O   HOH B 907     1555   1555  2.09  
LINK        MG    MG D1003                 O   HOH D1494     1555   1555  2.09  
LINK         OD1 ASN D 490                MG    MG D1002     1555   1555  2.12  
LINK         O2B ACP D1001                MG    MG D1002     1555   1555  2.13  
LINK         OD1 ASP D 503                MG    MG D1003     1555   1555  2.13  
LINK        MG    MG B 802                 O   HOH B 918     1555   1555  2.19  
LINK         OD2 ASP D 503                MG    MG D1003     1555   1555  2.39  
LINK         O1  PO4 A   1                 P   PO4 A   2     1555   1555  1.56  
LINK         O3  PO4 C   2                 P     A C   3     1555   1555  1.56  
LINK         O3  PO4 A   2                 P     A A   3     1555   1555  1.56  
LINK         O1  PO4 C   1                 P   PO4 C   2     1555   1555  1.56  
LINK         O2'   A C   3                 P     A C   4     1555   1555  1.58  
LINK         O2'   A C   6                 P   PO4 C   7     1555   1555  1.58  
LINK         O2'   A A   3                 P     A A   4     1555   1555  1.58  
LINK         O2'   A A   6                 P   PO4 A   7     1555   1555  1.58  
LINK         O2'   A A   5                 P     A A   6     1555   1555  1.59  
LINK         O2'   A C   5                 P     A C   6     1555   1555  1.59  
LINK         O2'   A A   4                 P     A A   5     1555   1555  1.60  
LINK         O2'   A C   4                 P     A C   5     1555   1555  1.61  
CISPEP   1 LYS B  496    LYS B  497          0         7.25                     
CISPEP   2 PRO B  622    SER B  623          0        -3.55                     
CISPEP   3 LYS D  496    LYS D  497          0         6.12                     
CISPEP   4 LYS D  509    TRP D  510          0        10.01                     
CISPEP   5 PRO D  622    SER D  623          0        -4.44                     
CISPEP   6 ASN D  637    GLU D  638          0        11.05                     
SITE     1 AC1 25 ILE B 371  ALA B 372  THR B 374  SER B 375                    
SITE     2 AC1 25 ILE B 379  ALA B 390  LYS B 392  ARG B 400                    
SITE     3 AC1 25 VAL B 434  THR B 435  CYS B 437  THR B 440                    
SITE     4 AC1 25 GLN B 489  ASN B 490  LEU B 492  ASP B 503                    
SITE     5 AC1 25 ASP B 505   MG B 802   MG B 803  HOH B 907                    
SITE     6 AC1 25 HOH B 918  HOH B 926  HOH B 955  HOH B 989                    
SITE     7 AC1 25 HOH B1072                                                     
SITE     1 AC2  5 ASN B 490  ASP B 503  ACP B 801  HOH B 907                    
SITE     2 AC2  5 HOH B 918                                                     
SITE     1 AC3  6 ASP B 485  ASP B 503  ASP B 505  ACP B 801                    
SITE     2 AC3  6 HOH B 926  HOH B1143                                          
SITE     1 AC4 30 ILE D 371  ALA D 372  THR D 374  SER D 375                    
SITE     2 AC4 30 ILE D 379  ALA D 390  LYS D 392  ARG D 400                    
SITE     3 AC4 30 VAL D 434  THR D 435  CYS D 437  THR D 440                    
SITE     4 AC4 30 GLN D 489  ASN D 490  LEU D 492  ASP D 503                    
SITE     5 AC4 30 ASP D 505   MG D1002   MG D1003  HOH D1122                    
SITE     6 AC4 30 HOH D1147  HOH D1191  HOH D1196  HOH D1242                    
SITE     7 AC4 30 HOH D1281  HOH D1318  HOH D1402  HOH D1468                    
SITE     8 AC4 30 HOH D1492  HOH D1493                                          
SITE     1 AC5  5 ASN D 490  ASP D 503  ACP D1001  HOH D1122                    
SITE     2 AC5  5 HOH D1492                                                     
SITE     1 AC6  5 ASP D 503  ASP D 505  ACP D1001  HOH D1493                    
SITE     2 AC6  5 HOH D1494                                                     
SITE     1 AC7 12 LYS D 606  THR D 607  MET D 644  PHE D 647                    
SITE     2 AC7 12 TYR D 648  ARG D 651  ARG D 667  ASN D 668                    
SITE     3 AC7 12 ASN D 672  HOH D1128  HOH D1270  HOH D1350                    
CRYST1   58.610  160.700  230.800  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017062  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006223  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004333        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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