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Database: PDB
Entry: 4G8L
LinkDB: 4G8L
Original site: 4G8L 
HEADER    HYDROLASE                               23-JUL-12   4G8L              
TITLE     ACTIVE STATE OF INTACT SENSOR DOMAIN OF HUMAN RNASE L WITH 2-5A BOUND 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-5A-DEPENDENT RIBONUCLEASE;                               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: 2-5A-SENSOR DOMAIN (ANK DOMAIN);                           
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                                                      
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                                         
KEYWDS    ANKYRIN-REPEAT DOMAIN, SINGLE-STRANDED RNA, HYDROLASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.HAN,G.WHITNEY,J.DONOVAN,A.KORENNYKH                                 
REVDAT   2   14-NOV-12 4G8L    1       JRNL                                     
REVDAT   1   31-OCT-12 4G8L    0                                                
JRNL        AUTH   Y.HAN,G.WHITNEY,J.DONOVAN,A.KORENNYKH                        
JRNL        TITL   INNATE IMMUNE MESSENGER 2-5A TETHERS HUMAN RNASE L INTO      
JRNL        TITL 2 ACTIVE HIGH-ORDER COMPLEXES.                                 
JRNL        REF    CELL REP                      V.   2   902 2012              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   23084743                                                     
JRNL        DOI    10.1016/J.CELREP.2012.09.004                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.5_2)                        
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.75                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 42245                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2115                            
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 38.7538 -  6.8933    0.99     2707   142  0.1778 0.1656        
REMARK   3     2  6.8933 -  5.4764    1.00     2704   143  0.2108 0.2591        
REMARK   3     3  5.4764 -  4.7855    1.00     2665   140  0.1972 0.2309        
REMARK   3     4  4.7855 -  4.3486    1.00     2709   143  0.1854 0.2304        
REMARK   3     5  4.3486 -  4.0373    1.00     2670   141  0.1891 0.2152        
REMARK   3     6  4.0373 -  3.7995    1.00     2690   142  0.2114 0.2648        
REMARK   3     7  3.7995 -  3.6093    1.00     2663   140  0.2093 0.2287        
REMARK   3     8  3.6093 -  3.4523    1.00     2654   140  0.2282 0.2507        
REMARK   3     9  3.4523 -  3.3195    1.00     2648   139  0.2335 0.3126        
REMARK   3    10  3.3195 -  3.2050    1.00     2694   143  0.2651 0.2847        
REMARK   3    11  3.2050 -  3.1048    1.00     2678   141  0.2756 0.3701        
REMARK   3    12  3.1048 -  3.0161    1.00     2655   139  0.3044 0.3175        
REMARK   3    13  3.0161 -  2.9368    1.00     2671   141  0.3041 0.4074        
REMARK   3    14  2.9368 -  2.8651    1.00     2622   138  0.3242 0.3069        
REMARK   3    15  2.8651 -  2.8000    1.00     2700   143  0.3718 0.4074        
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              : 0.34                                          
REMARK   3   B_SOL              : 44.12                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.480           
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) : -17.76900                                            
REMARK   3    B22 (A**2) : -15.21960                                            
REMARK   3    B33 (A**2) : 29.21520                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -10.72930                                            
REMARK   3    B23 (A**2) : -0.00000                                             
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      :  0.006           9547                                  
REMARK   3   ANGLE     :  0.985          12912                                  
REMARK   3   CHIRALITY :  0.063           1523                                  
REMARK   3   PLANARITY :  0.004           1622                                  
REMARK   3   DIHEDRAL  : 23.025           6086                                  
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 16:325                               
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0005 -29.0688  36.4262              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2035 T22:  -0.0972                                     
REMARK   3      T33:   0.2539 T12:  -0.0198                                     
REMARK   3      T13:  -0.0290 T23:  -0.0892                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1926 L22:   0.2660                                     
REMARK   3      L33:   0.2199 L12:  -0.1427                                     
REMARK   3      L13:  -0.0159 L23:   0.2172                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0516 S12:   0.1742 S13:  -0.3087                       
REMARK   3      S21:  -0.0947 S22:   0.0238 S23:   0.0439                       
REMARK   3      S31:   0.0345 S32:   0.1528 S33:  -0.0481                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 21:325                               
REMARK   3    ORIGIN FOR THE GROUP (A):   8.5849 -65.4605  37.7839              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2132 T22:   0.0972                                     
REMARK   3      T33:   0.2536 T12:  -0.0152                                     
REMARK   3      T13:  -0.0087 T23:   0.0247                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0902 L22:   0.2246                                     
REMARK   3      L33:   0.0262 L12:  -0.0857                                     
REMARK   3      L13:   0.0924 L23:  -0.1164                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0486 S12:   0.1303 S13:   0.3079                       
REMARK   3      S21:  -0.0317 S22:  -0.0017 S23:  -0.1314                       
REMARK   3      S31:  -0.0059 S32:   0.0388 S33:  -0.0023                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C AND RESID 15:325                               
REMARK   3    ORIGIN FOR THE GROUP (A):  16.3004 -81.4843   5.6532              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1027 T22:   0.3470                                     
REMARK   3      T33:   0.1064 T12:   0.0649                                     
REMARK   3      T13:   0.0237 T23:  -0.2246                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8582 L22:   0.2245                                     
REMARK   3      L33:   0.0274 L12:   0.3250                                     
REMARK   3      L13:   0.0546 L23:   0.0979                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0955 S12:   0.0313 S13:   0.4299                       
REMARK   3      S21:  -0.0523 S22:   0.0998 S23:   0.1047                       
REMARK   3      S31:  -0.0175 S32:  -0.0288 S33:   0.2069                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN D AND RESID 21:325                               
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9787 -44.9563   4.5239              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1003 T22:   0.3249                                     
REMARK   3      T33:   0.4052 T12:   0.0359                                     
REMARK   3      T13:  -0.0018 T23:   0.2071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0938 L22:   0.1579                                     
REMARK   3      L33:   0.0440 L12:   0.0223                                     
REMARK   3      L13:   0.0763 L23:  -0.0003                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0815 S12:   0.1134 S13:  -0.3717                       
REMARK   3      S21:  -0.0115 S22:   0.0379 S23:  -0.1062                       
REMARK   3      S31:   0.0295 S32:  -0.0447 S33:   0.0058                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESID 21:155 OR RESID 168:     
REMARK   3                          500 OR RESID 1996)                          
REMARK   3     SELECTION          : chain B AND (RESID 21:155 OR RESID 168:     
REMARK   3                          500 OR RESID 1996)                          
REMARK   3     ATOM PAIRS NUMBER  : 2292                                        
REMARK   3     RMSD               : 0.026                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESID 21:155 OR RESID 168:     
REMARK   3                          500 OR RESID 1996)                          
REMARK   3     SELECTION          : CHAIN C AND (RESID 21:155 OR RESID 168:     
REMARK   3                          500 OR RESID 1996)                          
REMARK   3     ATOM PAIRS NUMBER  : 2288                                        
REMARK   3     RMSD               : 0.027                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESID 21:155 OR RESID 168:     
REMARK   3                          500 OR RESID 1996)                          
REMARK   3     SELECTION          : CHAIN D AND (RESID 21:155 OR RESID 168:     
REMARK   3                          500 OR RESID 1996)                          
REMARK   3     ATOM PAIRS NUMBER  : 2292                                        
REMARK   3     RMSD               : 0.029                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESID 1:20)                    
REMARK   3     SELECTION          : CHAIN C AND (RESID 1:20)                    
REMARK   3     ATOM PAIRS NUMBER  : 38                                          
REMARK   3     RMSD               : 0.030                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4G8L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073874.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 7.0                                
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) : 1.072                              
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, SCALA                         
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42322                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.820                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
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) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
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: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4G8K                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM SODIUM ACETATE, 18% PEG 3350,     
REMARK 280  1.3M SODIUM CITRATE, PH 7.0, VAPOR DIFFUSION, TEMPERATURE 293K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       82.05500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     ASN A     8                                                      
REMARK 465     PRO A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     PRO A    13                                                      
REMARK 465     THR A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     LYS A   166                                                      
REMARK 465     GLY A   167                                                      
REMARK 465     ASP A   300                                                      
REMARK 465     LYS A   326                                                      
REMARK 465     GLU A   327                                                      
REMARK 465     ASP A   328                                                      
REMARK 465     PHE A   329                                                      
REMARK 465     HIS A   330                                                      
REMARK 465     PRO A   331                                                      
REMARK 465     PRO A   332                                                      
REMARK 465     ALA A   333                                                      
REMARK 465     GLU A   334                                                      
REMARK 465     ASP A   335                                                      
REMARK 465     TRP A   336                                                      
REMARK 465     LYS A   337                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     ARG B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     ASN B     8                                                      
REMARK 465     PRO B     9                                                      
REMARK 465     GLN B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     PRO B    13                                                      
REMARK 465     THR B    14                                                      
REMARK 465     SER B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     SER B    17                                                      
REMARK 465     GLY B    18                                                      
REMARK 465     ARG B    19                                                      
REMARK 465     ARG B    20                                                      
REMARK 465     LYS B   156                                                      
REMARK 465     THR B   157                                                      
REMARK 465     LYS B   158                                                      
REMARK 465     GLU B   159                                                      
REMARK 465     ASP B   160                                                      
REMARK 465     GLN B   161                                                      
REMARK 465     GLU B   162                                                      
REMARK 465     ARG B   163                                                      
REMARK 465     LEU B   164                                                      
REMARK 465     ASP B   300                                                      
REMARK 465     CYS B   301                                                      
REMARK 465     LYS B   326                                                      
REMARK 465     GLU B   327                                                      
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     TRP B   336                                                      
REMARK 465     LYS B   337                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     ARG C     4                                                      
REMARK 465     ASP C     5                                                      
REMARK 465     HIS C     6                                                      
REMARK 465     ASN C     7                                                      
REMARK 465     ASN C     8                                                      
REMARK 465     PRO C     9                                                      
REMARK 465     GLN C    10                                                      
REMARK 465     GLU C    11                                                      
REMARK 465     GLY C    12                                                      
REMARK 465     PRO C    13                                                      
REMARK 465     THR C    14                                                      
REMARK 465     GLU C   159                                                      
REMARK 465     ASP C   160                                                      
REMARK 465     GLN C   161                                                      
REMARK 465     GLU C   162                                                      
REMARK 465     ARG C   163                                                      
REMARK 465     LEU C   164                                                      
REMARK 465     ARG C   165                                                      
REMARK 465     LYS C   166                                                      
REMARK 465     ASP C   300                                                      
REMARK 465     CYS C   301                                                      
REMARK 465     GLY C   302                                                      
REMARK 465     LYS C   326                                                      
REMARK 465     GLU C   327                                                      
REMARK 465     ASP C   328                                                      
REMARK 465     PHE C   329                                                      
REMARK 465     HIS C   330                                                      
REMARK 465     PRO C   331                                                      
REMARK 465     PRO C   332                                                      
REMARK 465     ALA C   333                                                      
REMARK 465     GLU C   334                                                      
REMARK 465     ASP C   335                                                      
REMARK 465     TRP C   336                                                      
REMARK 465     LYS C   337                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     ARG D     4                                                      
REMARK 465     ASP D     5                                                      
REMARK 465     HIS D     6                                                      
REMARK 465     ASN D     7                                                      
REMARK 465     ASN D     8                                                      
REMARK 465     PRO D     9                                                      
REMARK 465     GLN D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     GLY D    12                                                      
REMARK 465     PRO D    13                                                      
REMARK 465     THR D    14                                                      
REMARK 465     SER D    15                                                      
REMARK 465     SER D    16                                                      
REMARK 465     SER D    17                                                      
REMARK 465     GLY D    18                                                      
REMARK 465     ARG D    19                                                      
REMARK 465     ARG D    20                                                      
REMARK 465     LYS D   158                                                      
REMARK 465     GLU D   159                                                      
REMARK 465     ASP D   160                                                      
REMARK 465     GLN D   161                                                      
REMARK 465     GLU D   162                                                      
REMARK 465     ARG D   163                                                      
REMARK 465     LEU D   164                                                      
REMARK 465     ARG D   165                                                      
REMARK 465     LYS D   166                                                      
REMARK 465     ASP D   300                                                      
REMARK 465     CYS D   301                                                      
REMARK 465     LYS D   326                                                      
REMARK 465     GLU D   327                                                      
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     TRP D   336                                                      
REMARK 465     LYS D   337                                                      
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    GLU A  57      -72.20    -61.64                                   
REMARK 500    GLU A 159       39.11    -78.06                                   
REMARK 500    ASP A 160      -38.38   -131.27                                   
REMARK 500    ASP A 215       11.89    -69.62                                   
REMARK 500    LYS A 240      105.59    -54.67                                   
REMARK 500    GLU A 265       76.19    -69.48                                   
REMARK 500    ASP A 270     -165.37    -72.90                                   
REMARK 500    LYS A 294       20.51    -70.24                                   
REMARK 500    ARG A 295      -34.11   -164.49                                   
REMARK 500    ASP A 303       26.73    -72.87                                   
REMARK 500    GLU B  57      -72.17    -61.81                                   
REMARK 500    LYS B 146        0.38    -64.29                                   
REMARK 500    LYS B 166      162.48    -47.90                                   
REMARK 500    ASP B 215       12.26    -69.37                                   
REMARK 500    LYS B 240      106.81    -54.23                                   
REMARK 500    ASP B 270     -164.30    -72.62                                   
REMARK 500    LYS B 294       20.31    -71.17                                   
REMARK 500    ARG B 295      -33.70   -164.34                                   
REMARK 500    ASP B 303       25.95    -72.97                                   
REMARK 500    GLU C  57      -72.59    -61.43                                   
REMARK 500    ARG C 155      109.88    -51.76                                   
REMARK 500    ASP C 215       12.07    -69.41                                   
REMARK 500    LYS C 240      105.57    -54.47                                   
REMARK 500    ASP C 270     -164.76    -72.09                                   
REMARK 500    LYS C 294       20.60    -71.52                                   
REMARK 500    ARG C 295      -33.36   -164.06                                   
REMARK 500    GLU D  57      -72.48    -62.15                                   
REMARK 500    ASP D 215       12.02    -68.23                                   
REMARK 500    LYS D 240      105.51    -54.55                                   
REMARK 500    ASP D 270     -163.95    -72.30                                   
REMARK 500    LYS D 294       20.17    -70.96                                   
REMARK 500    ARG D 295      -33.04   -164.34                                   
REMARK 500    ASP D 303       26.72    -73.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 25A A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 25A B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 25A C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 25A D 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4G8K   RELATED DB: PDB                                   
DBREF  4G8L A    1   337  UNP    Q05823   RN5A_HUMAN       1    337             
DBREF  4G8L B    1   337  UNP    Q05823   RN5A_HUMAN       1    337             
DBREF  4G8L C    1   337  UNP    Q05823   RN5A_HUMAN       1    337             
DBREF  4G8L D    1   337  UNP    Q05823   RN5A_HUMAN       1    337             
SEQRES   1 A  337  MET GLU SER ARG ASP HIS ASN ASN PRO GLN GLU GLY PRO          
SEQRES   2 A  337  THR SER SER SER GLY ARG ARG ALA ALA VAL GLU ASP ASN          
SEQRES   3 A  337  HIS LEU LEU ILE LYS ALA VAL GLN ASN GLU ASP VAL ASP          
SEQRES   4 A  337  LEU VAL GLN GLN LEU LEU GLU GLY GLY ALA ASN VAL ASN          
SEQRES   5 A  337  PHE GLN GLU GLU GLU GLY GLY TRP THR PRO LEU HIS ASN          
SEQRES   6 A  337  ALA VAL GLN MET SER ARG GLU ASP ILE VAL GLU LEU LEU          
SEQRES   7 A  337  LEU ARG HIS GLY ALA ASP PRO VAL LEU ARG LYS LYS ASN          
SEQRES   8 A  337  GLY ALA THR PRO PHE ILE LEU ALA ALA ILE ALA GLY SER          
SEQRES   9 A  337  VAL LYS LEU LEU LYS LEU PHE LEU SER LYS GLY ALA ASP          
SEQRES  10 A  337  VAL ASN GLU CYS ASP PHE TYR GLY PHE THR ALA PHE MET          
SEQRES  11 A  337  GLU ALA ALA VAL TYR GLY LYS VAL LYS ALA LEU LYS PHE          
SEQRES  12 A  337  LEU TYR LYS ARG GLY ALA ASN VAL ASN LEU ARG ARG LYS          
SEQRES  13 A  337  THR LYS GLU ASP GLN GLU ARG LEU ARG LYS GLY GLY ALA          
SEQRES  14 A  337  THR ALA LEU MET ASP ALA ALA GLU LYS GLY HIS VAL GLU          
SEQRES  15 A  337  VAL LEU LYS ILE LEU LEU ASP GLU MET GLY ALA ASP VAL          
SEQRES  16 A  337  ASN ALA CYS ASP ASN MET GLY ARG ASN ALA LEU ILE HIS          
SEQRES  17 A  337  ALA LEU LEU SER SER ASP ASP SER ASP VAL GLU ALA ILE          
SEQRES  18 A  337  THR HIS LEU LEU LEU ASP HIS GLY ALA ASP VAL ASN VAL          
SEQRES  19 A  337  ARG GLY GLU ARG GLY LYS THR PRO LEU ILE LEU ALA VAL          
SEQRES  20 A  337  GLU LYS LYS HIS LEU GLY LEU VAL GLN ARG LEU LEU GLU          
SEQRES  21 A  337  GLN GLU HIS ILE GLU ILE ASN ASP THR ASP SER ASP GLY          
SEQRES  22 A  337  LYS THR ALA LEU LEU LEU ALA VAL GLU LEU LYS LEU LYS          
SEQRES  23 A  337  LYS ILE ALA GLU LEU LEU CYS LYS ARG GLY ALA SER THR          
SEQRES  24 A  337  ASP CYS GLY ASP LEU VAL MET THR ALA ARG ARG ASN TYR          
SEQRES  25 A  337  ASP HIS SER LEU VAL LYS VAL LEU LEU SER HIS GLY ALA          
SEQRES  26 A  337  LYS GLU ASP PHE HIS PRO PRO ALA GLU ASP TRP LYS              
SEQRES   1 B  337  MET GLU SER ARG ASP HIS ASN ASN PRO GLN GLU GLY PRO          
SEQRES   2 B  337  THR SER SER SER GLY ARG ARG ALA ALA VAL GLU ASP ASN          
SEQRES   3 B  337  HIS LEU LEU ILE LYS ALA VAL GLN ASN GLU ASP VAL ASP          
SEQRES   4 B  337  LEU VAL GLN GLN LEU LEU GLU GLY GLY ALA ASN VAL ASN          
SEQRES   5 B  337  PHE GLN GLU GLU GLU GLY GLY TRP THR PRO LEU HIS ASN          
SEQRES   6 B  337  ALA VAL GLN MET SER ARG GLU ASP ILE VAL GLU LEU LEU          
SEQRES   7 B  337  LEU ARG HIS GLY ALA ASP PRO VAL LEU ARG LYS LYS ASN          
SEQRES   8 B  337  GLY ALA THR PRO PHE ILE LEU ALA ALA ILE ALA GLY SER          
SEQRES   9 B  337  VAL LYS LEU LEU LYS LEU PHE LEU SER LYS GLY ALA ASP          
SEQRES  10 B  337  VAL ASN GLU CYS ASP PHE TYR GLY PHE THR ALA PHE MET          
SEQRES  11 B  337  GLU ALA ALA VAL TYR GLY LYS VAL LYS ALA LEU LYS PHE          
SEQRES  12 B  337  LEU TYR LYS ARG GLY ALA ASN VAL ASN LEU ARG ARG LYS          
SEQRES  13 B  337  THR LYS GLU ASP GLN GLU ARG LEU ARG LYS GLY GLY ALA          
SEQRES  14 B  337  THR ALA LEU MET ASP ALA ALA GLU LYS GLY HIS VAL GLU          
SEQRES  15 B  337  VAL LEU LYS ILE LEU LEU ASP GLU MET GLY ALA ASP VAL          
SEQRES  16 B  337  ASN ALA CYS ASP ASN MET GLY ARG ASN ALA LEU ILE HIS          
SEQRES  17 B  337  ALA LEU LEU SER SER ASP ASP SER ASP VAL GLU ALA ILE          
SEQRES  18 B  337  THR HIS LEU LEU LEU ASP HIS GLY ALA ASP VAL ASN VAL          
SEQRES  19 B  337  ARG GLY GLU ARG GLY LYS THR PRO LEU ILE LEU ALA VAL          
SEQRES  20 B  337  GLU LYS LYS HIS LEU GLY LEU VAL GLN ARG LEU LEU GLU          
SEQRES  21 B  337  GLN GLU HIS ILE GLU ILE ASN ASP THR ASP SER ASP GLY          
SEQRES  22 B  337  LYS THR ALA LEU LEU LEU ALA VAL GLU LEU LYS LEU LYS          
SEQRES  23 B  337  LYS ILE ALA GLU LEU LEU CYS LYS ARG GLY ALA SER THR          
SEQRES  24 B  337  ASP CYS GLY ASP LEU VAL MET THR ALA ARG ARG ASN TYR          
SEQRES  25 B  337  ASP HIS SER LEU VAL LYS VAL LEU LEU SER HIS GLY ALA          
SEQRES  26 B  337  LYS GLU ASP PHE HIS PRO PRO ALA GLU ASP TRP LYS              
SEQRES   1 C  337  MET GLU SER ARG ASP HIS ASN ASN PRO GLN GLU GLY PRO          
SEQRES   2 C  337  THR SER SER SER GLY ARG ARG ALA ALA VAL GLU ASP ASN          
SEQRES   3 C  337  HIS LEU LEU ILE LYS ALA VAL GLN ASN GLU ASP VAL ASP          
SEQRES   4 C  337  LEU VAL GLN GLN LEU LEU GLU GLY GLY ALA ASN VAL ASN          
SEQRES   5 C  337  PHE GLN GLU GLU GLU GLY GLY TRP THR PRO LEU HIS ASN          
SEQRES   6 C  337  ALA VAL GLN MET SER ARG GLU ASP ILE VAL GLU LEU LEU          
SEQRES   7 C  337  LEU ARG HIS GLY ALA ASP PRO VAL LEU ARG LYS LYS ASN          
SEQRES   8 C  337  GLY ALA THR PRO PHE ILE LEU ALA ALA ILE ALA GLY SER          
SEQRES   9 C  337  VAL LYS LEU LEU LYS LEU PHE LEU SER LYS GLY ALA ASP          
SEQRES  10 C  337  VAL ASN GLU CYS ASP PHE TYR GLY PHE THR ALA PHE MET          
SEQRES  11 C  337  GLU ALA ALA VAL TYR GLY LYS VAL LYS ALA LEU LYS PHE          
SEQRES  12 C  337  LEU TYR LYS ARG GLY ALA ASN VAL ASN LEU ARG ARG LYS          
SEQRES  13 C  337  THR LYS GLU ASP GLN GLU ARG LEU ARG LYS GLY GLY ALA          
SEQRES  14 C  337  THR ALA LEU MET ASP ALA ALA GLU LYS GLY HIS VAL GLU          
SEQRES  15 C  337  VAL LEU LYS ILE LEU LEU ASP GLU MET GLY ALA ASP VAL          
SEQRES  16 C  337  ASN ALA CYS ASP ASN MET GLY ARG ASN ALA LEU ILE HIS          
SEQRES  17 C  337  ALA LEU LEU SER SER ASP ASP SER ASP VAL GLU ALA ILE          
SEQRES  18 C  337  THR HIS LEU LEU LEU ASP HIS GLY ALA ASP VAL ASN VAL          
SEQRES  19 C  337  ARG GLY GLU ARG GLY LYS THR PRO LEU ILE LEU ALA VAL          
SEQRES  20 C  337  GLU LYS LYS HIS LEU GLY LEU VAL GLN ARG LEU LEU GLU          
SEQRES  21 C  337  GLN GLU HIS ILE GLU ILE ASN ASP THR ASP SER ASP GLY          
SEQRES  22 C  337  LYS THR ALA LEU LEU LEU ALA VAL GLU LEU LYS LEU LYS          
SEQRES  23 C  337  LYS ILE ALA GLU LEU LEU CYS LYS ARG GLY ALA SER THR          
SEQRES  24 C  337  ASP CYS GLY ASP LEU VAL MET THR ALA ARG ARG ASN TYR          
SEQRES  25 C  337  ASP HIS SER LEU VAL LYS VAL LEU LEU SER HIS GLY ALA          
SEQRES  26 C  337  LYS GLU ASP PHE HIS PRO PRO ALA GLU ASP TRP LYS              
SEQRES   1 D  337  MET GLU SER ARG ASP HIS ASN ASN PRO GLN GLU GLY PRO          
SEQRES   2 D  337  THR SER SER SER GLY ARG ARG ALA ALA VAL GLU ASP ASN          
SEQRES   3 D  337  HIS LEU LEU ILE LYS ALA VAL GLN ASN GLU ASP VAL ASP          
SEQRES   4 D  337  LEU VAL GLN GLN LEU LEU GLU GLY GLY ALA ASN VAL ASN          
SEQRES   5 D  337  PHE GLN GLU GLU GLU GLY GLY TRP THR PRO LEU HIS ASN          
SEQRES   6 D  337  ALA VAL GLN MET SER ARG GLU ASP ILE VAL GLU LEU LEU          
SEQRES   7 D  337  LEU ARG HIS GLY ALA ASP PRO VAL LEU ARG LYS LYS ASN          
SEQRES   8 D  337  GLY ALA THR PRO PHE ILE LEU ALA ALA ILE ALA GLY SER          
SEQRES   9 D  337  VAL LYS LEU LEU LYS LEU PHE LEU SER LYS GLY ALA ASP          
SEQRES  10 D  337  VAL ASN GLU CYS ASP PHE TYR GLY PHE THR ALA PHE MET          
SEQRES  11 D  337  GLU ALA ALA VAL TYR GLY LYS VAL LYS ALA LEU LYS PHE          
SEQRES  12 D  337  LEU TYR LYS ARG GLY ALA ASN VAL ASN LEU ARG ARG LYS          
SEQRES  13 D  337  THR LYS GLU ASP GLN GLU ARG LEU ARG LYS GLY GLY ALA          
SEQRES  14 D  337  THR ALA LEU MET ASP ALA ALA GLU LYS GLY HIS VAL GLU          
SEQRES  15 D  337  VAL LEU LYS ILE LEU LEU ASP GLU MET GLY ALA ASP VAL          
SEQRES  16 D  337  ASN ALA CYS ASP ASN MET GLY ARG ASN ALA LEU ILE HIS          
SEQRES  17 D  337  ALA LEU LEU SER SER ASP ASP SER ASP VAL GLU ALA ILE          
SEQRES  18 D  337  THR HIS LEU LEU LEU ASP HIS GLY ALA ASP VAL ASN VAL          
SEQRES  19 D  337  ARG GLY GLU ARG GLY LYS THR PRO LEU ILE LEU ALA VAL          
SEQRES  20 D  337  GLU LYS LYS HIS LEU GLY LEU VAL GLN ARG LEU LEU GLU          
SEQRES  21 D  337  GLN GLU HIS ILE GLU ILE ASN ASP THR ASP SER ASP GLY          
SEQRES  22 D  337  LYS THR ALA LEU LEU LEU ALA VAL GLU LEU LYS LEU LYS          
SEQRES  23 D  337  LYS ILE ALA GLU LEU LEU CYS LYS ARG GLY ALA SER THR          
SEQRES  24 D  337  ASP CYS GLY ASP LEU VAL MET THR ALA ARG ARG ASN TYR          
SEQRES  25 D  337  ASP HIS SER LEU VAL LYS VAL LEU LEU SER HIS GLY ALA          
SEQRES  26 D  337  LYS GLU ASP PHE HIS PRO PRO ALA GLU ASP TRP LYS              
HET    25A  A 401      67                                                       
HET    25A  B 401      67                                                       
HET    25A  C 401      67                                                       
HET    25A  D 401      67                                                       
HETNAM     25A 5'-O-MONOPHOSPHORYLADENYLYL(2'->5')ADENYLYL(2'->5')              
HETNAM   2 25A  ADENOSINE                                                       
FORMUL   5  25A    4(C30 H38 N15 O19 P3)                                        
HELIX    1   1 SER A   16  ASN A   35  1                                  20    
HELIX    2   2 ASP A   37  GLY A   47  1                                  11    
HELIX    3   3 THR A   61  MET A   69  1                                   9    
HELIX    4   4 ARG A   71  HIS A   81  1                                  11    
HELIX    5   5 THR A   94  GLY A  103  1                                  10    
HELIX    6   6 SER A  104  LYS A  114  1                                  11    
HELIX    7   7 THR A  127  TYR A  135  1                                   9    
HELIX    8   8 LYS A  137  LYS A  146  1                                  10    
HELIX    9   9 THR A  157  GLU A  162  1                                   6    
HELIX   10  10 THR A  170  LYS A  178  1                                   9    
HELIX   11  11 HIS A  180  GLU A  190  1                                  11    
HELIX   12  12 ASN A  204  SER A  212  1                                   9    
HELIX   13  13 ASP A  217  HIS A  228  1                                  12    
HELIX   14  14 THR A  241  LYS A  249  1                                   9    
HELIX   15  15 HIS A  251  GLU A  260  1                                  10    
HELIX   16  16 THR A  275  LEU A  283  1                                   9    
HELIX   17  17 LEU A  285  LYS A  294  1                                  10    
HELIX   18  18 ASP A  303  ASN A  311  1                                   9    
HELIX   19  19 ASP A  313  HIS A  323  1                                  11    
HELIX   20  20 ALA B   22  ASN B   35  1                                  14    
HELIX   21  21 ASP B   37  GLY B   47  1                                  11    
HELIX   22  22 THR B   61  MET B   69  1                                   9    
HELIX   23  23 ARG B   71  HIS B   81  1                                  11    
HELIX   24  24 THR B   94  ALA B  102  1                                   9    
HELIX   25  25 SER B  104  LYS B  114  1                                  11    
HELIX   26  26 THR B  127  TYR B  135  1                                   9    
HELIX   27  27 LYS B  137  LYS B  146  1                                  10    
HELIX   28  28 THR B  170  LYS B  178  1                                   9    
HELIX   29  29 HIS B  180  GLU B  190  1                                  11    
HELIX   30  30 ASN B  204  SER B  212  1                                   9    
HELIX   31  31 ASP B  217  HIS B  228  1                                  12    
HELIX   32  32 THR B  241  LYS B  249  1                                   9    
HELIX   33  33 HIS B  251  GLU B  260  1                                  10    
HELIX   34  34 THR B  275  LEU B  283  1                                   9    
HELIX   35  35 LEU B  285  LYS B  294  1                                  10    
HELIX   36  36 ASP B  303  ASN B  311  1                                   9    
HELIX   37  37 ASP B  313  HIS B  323  1                                  11    
HELIX   38  38 SER C   16  ASN C   35  1                                  20    
HELIX   39  39 ASP C   37  GLY C   47  1                                  11    
HELIX   40  40 THR C   61  MET C   69  1                                   9    
HELIX   41  41 ARG C   71  HIS C   81  1                                  11    
HELIX   42  42 THR C   94  ALA C  102  1                                   9    
HELIX   43  43 SER C  104  LYS C  114  1                                  11    
HELIX   44  44 THR C  127  TYR C  135  1                                   9    
HELIX   45  45 LYS C  137  LYS C  146  1                                  10    
HELIX   46  46 THR C  170  LYS C  178  1                                   9    
HELIX   47  47 HIS C  180  GLU C  190  1                                  11    
HELIX   48  48 ASN C  204  SER C  212  1                                   9    
HELIX   49  49 ASP C  217  HIS C  228  1                                  12    
HELIX   50  50 THR C  241  LYS C  249  1                                   9    
HELIX   51  51 HIS C  251  GLU C  260  1                                  10    
HELIX   52  52 THR C  275  LEU C  283  1                                   9    
HELIX   53  53 LEU C  285  LYS C  294  1                                  10    
HELIX   54  54 LEU C  304  ASN C  311  1                                   8    
HELIX   55  55 ASP C  313  HIS C  323  1                                  11    
HELIX   56  56 ALA D   22  ASN D   35  1                                  14    
HELIX   57  57 ASP D   37  GLY D   47  1                                  11    
HELIX   58  58 THR D   61  MET D   69  1                                   9    
HELIX   59  59 ARG D   71  HIS D   81  1                                  11    
HELIX   60  60 THR D   94  GLY D  103  1                                  10    
HELIX   61  61 SER D  104  LYS D  114  1                                  11    
HELIX   62  62 THR D  127  TYR D  135  1                                   9    
HELIX   63  63 LYS D  137  LYS D  146  1                                  10    
HELIX   64  64 THR D  170  LYS D  178  1                                   9    
HELIX   65  65 HIS D  180  GLU D  190  1                                  11    
HELIX   66  66 ASN D  204  SER D  212  1                                   9    
HELIX   67  67 ASP D  217  HIS D  228  1                                  12    
HELIX   68  68 THR D  241  LYS D  249  1                                   9    
HELIX   69  69 HIS D  251  GLU D  260  1                                  10    
HELIX   70  70 THR D  275  LEU D  283  1                                   9    
HELIX   71  71 LEU D  285  LYS D  294  1                                  10    
HELIX   72  72 ASP D  303  ASN D  311  1                                   9    
HELIX   73  73 ASP D  313  HIS D  323  1                                  11    
SITE     1 AC1 17 GLU A  55  GLU A  57  GLY A  58  TRP A  60                    
SITE     2 AC1 17 ASN A  65  GLN A  68  LYS A  89  ASN A  91                    
SITE     3 AC1 17 ASP A 122  PHE A 126  GLU A 131  TYR A 135                    
SITE     4 AC1 17 ARG A 155  MET B 306  ARG B 309  ARG B 310                    
SITE     5 AC1 17 TYR B 312                                                     
SITE     1 AC2 17 MET A 306  ARG A 309  ARG A 310  TYR A 312                    
SITE     2 AC2 17 GLU B  55  GLU B  57  GLY B  58  TRP B  60                    
SITE     3 AC2 17 ASN B  65  GLN B  68  LYS B  89  ASN B  91                    
SITE     4 AC2 17 ASP B 122  PHE B 126  GLU B 131  TYR B 135                    
SITE     5 AC2 17 ARG B 155                                                     
SITE     1 AC3 16 GLU C  55  GLU C  57  GLY C  58  TRP C  60                    
SITE     2 AC3 16 ASN C  65  GLN C  68  LYS C  89  ASP C 122                    
SITE     3 AC3 16 PHE C 126  GLU C 131  TYR C 135  ARG C 155                    
SITE     4 AC3 16 MET D 306  ARG D 309  ARG D 310  TYR D 312                    
SITE     1 AC4 16 MET C 306  ARG C 309  ARG C 310  TYR C 312                    
SITE     2 AC4 16 GLU D  55  GLU D  57  GLY D  58  TRP D  60                    
SITE     3 AC4 16 ASN D  65  GLN D  68  LYS D  89  ASP D 122                    
SITE     4 AC4 16 PHE D 126  GLU D 131  TYR D 135  ARG D 155                    
CRYST1   62.980  164.110   86.220  90.00 100.20  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015878  0.000000  0.002858        0.00000                         
SCALE2      0.000000  0.006093  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011785        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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