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Database: PDB
Entry: 4G8K
LinkDB: 4G8K
Original site: 4G8K 
HEADER    HYDROLASE                               23-JUL-12   4G8K              
TITLE     INTACT SENSOR DOMAIN OF HUMAN RNASE L IN THE INACTIVE SIGNALING STATE 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-5A-DEPENDENT RIBONUCLEASE;                               
COMPND   3 CHAIN: A, B;                                                         
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 4G8K    1       JRNL                                     
REVDAT   1   31-OCT-12 4G8K    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.    2.40 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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 60.38                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 38131                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1906                            
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 60.3941 -  5.7828    1.00     2812   148  0.1865 0.2095        
REMARK   3     2  5.7828 -  4.5905    1.00     2686   141  0.1832 0.1957        
REMARK   3     3  4.5905 -  4.0103    1.00     2631   138  0.1675 0.1953        
REMARK   3     4  4.0103 -  3.6437    1.00     2635   139  0.1887 0.2390        
REMARK   3     5  3.6437 -  3.3826    1.00     2612   138  0.2183 0.2475        
REMARK   3     6  3.3826 -  3.1832    1.00     2570   135  0.2405 0.2915        
REMARK   3     7  3.1832 -  3.0238    1.00     2603   137  0.2382 0.2854        
REMARK   3     8  3.0238 -  2.8921    1.00     2583   136  0.2339 0.2897        
REMARK   3     9  2.8921 -  2.7808    1.00     2584   136  0.2411 0.2843        
REMARK   3    10  2.7808 -  2.6848    1.00     2568   135  0.2298 0.2405        
REMARK   3    11  2.6848 -  2.6009    1.00     2561   135  0.2346 0.2454        
REMARK   3    12  2.6009 -  2.5265    0.99     2536   133  0.2475 0.2623        
REMARK   3    13  2.5265 -  2.4600    0.97     2519   133  0.2518 0.3189        
REMARK   3    14  2.4600 -  2.4000    0.92     2325   122  0.2614 0.2649        
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              : 0.33                                          
REMARK   3   B_SOL              : 38.72                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.110           
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) : -5.13020                                             
REMARK   3    B22 (A**2) : 0.31760                                              
REMARK   3    B33 (A**2) : 4.81260                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
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      :  0.002           4620                                  
REMARK   3   ANGLE     :  0.593           6225                                  
REMARK   3   CHIRALITY :  0.045            735                                  
REMARK   3   PLANARITY :  0.002            806                                  
REMARK   3   DIHEDRAL  : 19.665           2897                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 21:327                               
REMARK   3    ORIGIN FOR THE GROUP (A): -10.8141  15.2787 -48.2648              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1660 T22:   0.0919                                     
REMARK   3      T33:   0.1609 T12:   0.0163                                     
REMARK   3      T13:  -0.0123 T23:  -0.0377                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3738 L22:   1.0588                                     
REMARK   3      L33:   0.5265 L12:  -0.5823                                     
REMARK   3      L13:   0.7791 L23:  -0.6255                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1405 S12:  -0.0321 S13:  -0.0739                       
REMARK   3      S21:  -0.0115 S22:   0.0049 S23:   0.2483                       
REMARK   3      S31:   0.0349 S32:   0.0193 S33:   0.0001                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 24:328                               
REMARK   3    ORIGIN FOR THE GROUP (A): -24.0166  24.3440 -21.8106              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2173 T22:   0.3856                                     
REMARK   3      T33:   0.1333 T12:  -0.0221                                     
REMARK   3      T13:  -0.0049 T23:  -0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0161 L22:   0.4005                                     
REMARK   3      L33:   1.2069 L12:   0.4418                                     
REMARK   3      L13:  -0.6640 L23:  -0.5810                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1357 S12:  -0.2734 S13:   0.0676                       
REMARK   3      S21:  -0.0969 S22:  -0.0224 S23:  -0.1141                       
REMARK   3      S31:  -0.0050 S32:  -0.1043 S33:  -0.0041                       
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 4G8K 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 RCSB073873.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-11                          
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   : 38136                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.375                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.870                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
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) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
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 1WDY                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM POTASSIUM ACETATE, 20% PEG3350,    
REMARK 280  PH 7.0, VAPOR DIFFUSION, TEMPERATURE 293K                           
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       31.40000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      120.75000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.50000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      120.75000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.40000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.50000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: MONOMERIC                         
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     ARG A    19                                                      
REMARK 465     ARG A    20                                                      
REMARK 465     GLU A   159                                                      
REMARK 465     ASP A   160                                                      
REMARK 465     GLN A   161                                                      
REMARK 465     GLU A   162                                                      
REMARK 465     ARG A   163                                                      
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     ALA B    21                                                      
REMARK 465     ALA B    22                                                      
REMARK 465     VAL B    23                                                      
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     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 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     LEU A 164    CG   CD1  CD2                                       
REMARK 470     ARG A 165    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  24    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 165    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 166    CG   CD   CE   NZ                                   
REMARK 470     LYS B 326    CG   CD   CE   NZ                                   
REMARK 470     GLU B 327    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 328    CG   OD1  OD2                                       
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    ARG A 165       29.34    -70.37                                   
REMARK 500    SER A 212      -27.73   -141.47                                   
REMARK 500    LYS A 294        6.09    -65.43                                   
REMARK 500    ARG A 295      -17.57   -155.68                                   
REMARK 500    LYS A 326      -98.67    -92.71                                   
REMARK 500    ASP B 199     -168.06    -74.24                                   
REMARK 500    ARG B 238       48.05   -140.79                                   
REMARK 500    LYS B 294       13.52    -68.26                                   
REMARK 500    ARG B 295      -14.97   -168.21                                   
REMARK 500    ASP B 303       38.45    -70.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4G8L   RELATED DB: PDB                                   
DBREF  4G8K A    1   337  UNP    Q05823   RN5A_HUMAN       1    337             
DBREF  4G8K B    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              
FORMUL   3  HOH   *227(H2 O)                                                    
HELIX    1   1 ALA A   21  ASN A   35  1                                  15    
HELIX    2   2 ASP A   37  GLY A   48  1                                  12    
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  SER A  113  1                                  10    
HELIX    7   7 THR A  127  TYR A  135  1                                   9    
HELIX    8   8 LYS A  137  ARG A  147  1                                  11    
HELIX    9   9 THR A  170  GLY A  179  1                                  10    
HELIX   10  10 HIS A  180  MET A  191  1                                  12    
HELIX   11  11 ASN A  204  SER A  213  1                                  10    
HELIX   12  12 ASP A  217  HIS A  228  1                                  12    
HELIX   13  13 GLY A  236  LYS A  240  5                                   5    
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 ASP B   25  ASN B   35  1                                  11    
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  GLY B  103  1                                  10    
HELIX   25  25 SER B  104  SER B  113  1                                  10    
HELIX   26  26 THR B  127  TYR B  135  1                                   9    
HELIX   27  27 LYS B  137  ARG B  147  1                                  11    
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 ALA B  297  GLY B  302  1                                   6    
HELIX   37  37 ASP B  303  ASN B  311  1                                   9    
HELIX   38  38 ASP B  313  SER B  322  1                                  10    
CISPEP   1 GLU B   24    ASP B   25          0        -1.24                     
CRYST1   62.800   63.000  241.500  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      0.015924  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015873  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004141        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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