GenomeNet

Database: PDB
Entry: 1AOS
LinkDB: 1AOS
Original site: 1AOS 
HEADER    LYASE                                   10-JUL-97   1AOS              
TITLE     HUMAN ARGININOSUCCINATE LYASE                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ARGININOSUCCINATE LYASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 4.3.2.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: LIVER;                                                        
SOURCE   6 CELLULAR_LOCATION: CYTOPLASM;                                        
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    ARGININE BIOSYNTHESIS, LYASE, UREA CYCLE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.TURNER,A.SIMPSON,R.R.MCINNES,P.L.HOWELL                           
REVDAT   4   13-JUL-11 1AOS    1       VERSN                                    
REVDAT   3   24-FEB-09 1AOS    1       VERSN                                    
REVDAT   2   01-APR-03 1AOS    1       JRNL                                     
REVDAT   1   14-JAN-98 1AOS    0                                                
JRNL        AUTH   M.A.TURNER,A.SIMPSON,R.R.MCINNES,P.L.HOWELL                  
JRNL        TITL   HUMAN ARGININOSUCCINATE LYASE: A STRUCTURAL BASIS FOR        
JRNL        TITL 2 INTRAGENIC COMPLEMENTATION.                                  
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  94  9063 1997              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   9256435                                                      
JRNL        DOI    10.1073/PNAS.94.17.9063                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 6474                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.298                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 4.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 4.36                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 647                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1600                       
REMARK   3   BIN FREE R VALUE                    : 0.2700                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 56                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6788                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.39                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.46                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.28                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINTS                                              
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARAM19X.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPH19X.PRO                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1AOS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JUN-94                             
REMARK 200  TEMPERATURE           (KELVIN) : 287                                
REMARK 200  PH                             : 7.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23049                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.3                               
REMARK 200  DATA REDUNDANCY                : 2.660                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN CRYSTALLIZED FROM 1.1M           
REMARK 280  PHOSPHATE, PH 7.1                                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.06667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      122.13333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      122.13333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       61.06667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 28580 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 55540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -154.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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   BIOMT1   2 -0.500000 -0.866025  0.000000      156.90000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000       90.58626            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       61.06667            
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     ALA A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     TRP A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     ARG A    12                                                      
REMARK 465     PHE A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     ALA A    16                                                      
REMARK 465     VAL A    17                                                      
REMARK 465     ASP A    18                                                      
REMARK 465     PRO A    19                                                      
REMARK 465     ALA A    71                                                      
REMARK 465     GLU A    72                                                      
REMARK 465     GLU A    73                                                      
REMARK 465     TRP A    74                                                      
REMARK 465     ALA A    75                                                      
REMARK 465     GLN A    76                                                      
REMARK 465     GLY A    77                                                      
REMARK 465     THR A    78                                                      
REMARK 465     PHE A    79                                                      
REMARK 465     GLN A   463                                                      
REMARK 465     ALA A   464                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     GLN B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     TRP B     9                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     ARG B    12                                                      
REMARK 465     PHE B    13                                                      
REMARK 465     VAL B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     ALA B    16                                                      
REMARK 465     VAL B    17                                                      
REMARK 465     ASP B    18                                                      
REMARK 465     PRO B    19                                                      
REMARK 465     ALA B    71                                                      
REMARK 465     GLU B    72                                                      
REMARK 465     GLU B    73                                                      
REMARK 465     TRP B    74                                                      
REMARK 465     ALA B    75                                                      
REMARK 465     GLN B    76                                                      
REMARK 465     GLY B    77                                                      
REMARK 465     THR B    78                                                      
REMARK 465     PHE B    79                                                      
REMARK 465     GLN B   463                                                      
REMARK 465     ALA B   464                                                      
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     GLU A  22    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  95    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 111    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ARG A 246    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  22    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  95    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 111    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ARG B 246    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  31       30.53    -82.10                                   
REMARK 500    GLU A  36        4.67    -66.04                                   
REMARK 500    LEU A  67       36.57    -81.61                                   
REMARK 500    ASP A  68       13.43   -162.16                                   
REMARK 500    ALA A  91      -36.38    -32.27                                   
REMARK 500    ALA A 102      -84.42    -58.61                                   
REMARK 500    LEU A 107      -39.06    -34.92                                   
REMARK 500    HIS A 108       42.48   -104.78                                   
REMARK 500    ARG A 151      -47.48    -27.78                                   
REMARK 500    THR A 159      -91.49   -109.89                                   
REMARK 500    ARG A 163      109.09    -34.38                                   
REMARK 500    ASN A 195       25.50    -67.04                                   
REMARK 500    LEU A 199      128.87    -38.77                                   
REMARK 500    ALA A 203      -50.43   -125.22                                   
REMARK 500    ILE A 204      -59.82   -125.60                                   
REMARK 500    VAL A 211      127.19    -39.68                                   
REMARK 500    LEU A 227       36.98    -87.02                                   
REMARK 500    ASN A 228      134.19   -177.94                                   
REMARK 500    ASP A 275       23.41    -74.61                                   
REMARK 500    LEU A 283       -9.06     54.35                                   
REMARK 500    MET A 284       62.50   -156.50                                   
REMARK 500    PRO A 285       -8.93    -55.79                                   
REMARK 500    LYS A 288       77.51    -67.11                                   
REMARK 500    ASP A 291      -52.94   -167.57                                   
REMARK 500    PRO A 318      -81.46    -40.45                                   
REMARK 500    SER A 319     -164.42   -122.41                                   
REMARK 500    TYR A 321       93.15     35.18                                   
REMARK 500    LEU A 325       -0.75    -53.21                                   
REMARK 500    LEU A 353      118.48    -20.14                                   
REMARK 500    ALA A 404      173.94    -44.88                                   
REMARK 500    ALA A 439       71.16     40.94                                   
REMARK 500    LEU A 440      114.74     34.33                                   
REMARK 500    ASP B  31       30.33    -82.45                                   
REMARK 500    GLU B  36        4.25    -66.35                                   
REMARK 500    LEU B  67       35.51    -81.89                                   
REMARK 500    ASP B  68       13.43   -160.98                                   
REMARK 500    ALA B  91      -36.41    -31.95                                   
REMARK 500    ALA B 102      -85.16    -58.80                                   
REMARK 500    LEU B 107      -39.27    -35.03                                   
REMARK 500    HIS B 108       41.99   -104.86                                   
REMARK 500    ARG B 151      -47.84    -27.83                                   
REMARK 500    THR B 159      -91.52   -110.17                                   
REMARK 500    ARG B 163      110.11    -34.39                                   
REMARK 500    ASN B 195       25.59    -67.42                                   
REMARK 500    LEU B 199      130.07    -38.66                                   
REMARK 500    ILE B 204      -60.14   -126.45                                   
REMARK 500    VAL B 211      126.49    -39.55                                   
REMARK 500    LEU B 227       36.87    -86.23                                   
REMARK 500    ASN B 228      134.24   -178.16                                   
REMARK 500    ASP B 275       23.42    -74.67                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      63 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 376         0.07    SIDE CHAIN                              
REMARK 500    TYR A 437         0.08    SIDE CHAIN                              
REMARK 500    TYR B 277         0.07    SIDE CHAIN                              
REMARK 500    TYR B 376         0.06    SIDE CHAIN                              
REMARK 500    TYR B 437         0.09    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1AOS A    1   464  UNP    P04424   ARLY_HUMAN       1    464             
DBREF  1AOS B    1   464  UNP    P04424   ARLY_HUMAN       1    464             
SEQADV 1AOS GLN A    6  UNP  P04424    GLY     6 CONFLICT                       
SEQADV 1AOS GLN B    6  UNP  P04424    GLY     6 CONFLICT                       
SEQRES   1 A  464  MET ALA SER GLU SER GLN LYS LEU TRP GLY GLY ARG PHE          
SEQRES   2 A  464  VAL GLY ALA VAL ASP PRO ILE MET GLU LYS PHE ASN ALA          
SEQRES   3 A  464  SER ILE ALA TYR ASP ARG HIS LEU TRP GLU VAL ASP VAL          
SEQRES   4 A  464  GLN GLY SER LYS ALA TYR SER ARG GLY LEU GLU LYS ALA          
SEQRES   5 A  464  GLY LEU LEU THR LYS ALA GLU MET ASP GLN ILE LEU HIS          
SEQRES   6 A  464  GLY LEU ASP LYS VAL ALA GLU GLU TRP ALA GLN GLY THR          
SEQRES   7 A  464  PHE LYS LEU ASN SER ASN ASP GLU ASP ILE HIS THR ALA          
SEQRES   8 A  464  ASN GLU ARG ARG LEU LYS GLU LEU ILE GLY ALA THR ALA          
SEQRES   9 A  464  GLY LYS LEU HIS THR GLY ARG SER ARG ASN ASP GLN VAL          
SEQRES  10 A  464  VAL THR ASP LEU ARG LEU TRP MET ARG GLN THR CYS SER          
SEQRES  11 A  464  THR LEU SER GLY LEU LEU TRP GLU LEU ILE ARG THR MET          
SEQRES  12 A  464  VAL ASP ARG ALA GLU ALA GLU ARG ASP VAL LEU PHE PRO          
SEQRES  13 A  464  GLY TYR THR HIS LEU GLN ARG ALA GLN PRO ILE ARG TRP          
SEQRES  14 A  464  SER HIS TRP ILE LEU SER HIS ALA VAL ALA LEU THR ARG          
SEQRES  15 A  464  ASP SER GLU ARG LEU LEU GLU VAL ARG LYS ARG ILE ASN          
SEQRES  16 A  464  VAL LEU PRO LEU GLY SER GLY ALA ILE ALA GLY ASN PRO          
SEQRES  17 A  464  LEU GLY VAL ASP ARG GLU LEU LEU ARG ALA GLU LEU ASN          
SEQRES  18 A  464  PHE GLY ALA ILE THR LEU ASN SER MET ASP ALA THR SER          
SEQRES  19 A  464  GLU ARG ASP PHE VAL ALA GLU PHE LEU PHE TRP ARG SER          
SEQRES  20 A  464  LEU CYS MET THR HIS LEU SER ARG MET ALA GLU ASP LEU          
SEQRES  21 A  464  ILE LEU TYR CYS THR LYS GLU PHE SER PHE VAL GLN LEU          
SEQRES  22 A  464  SER ASP ALA TYR SER THR GLY SER SER LEU MET PRO GLN          
SEQRES  23 A  464  LYS LYS ASN PRO ASP SER LEU GLU LEU ILE ARG SER LYS          
SEQRES  24 A  464  ALA GLY ARG VAL PHE GLY ARG CYS ALA GLY LEU LEU MET          
SEQRES  25 A  464  THR LEU LYS GLY LEU PRO SER THR TYR ASN LYS ASP LEU          
SEQRES  26 A  464  GLN GLU ASP LYS GLU ALA VAL PHE GLU VAL SER ASP THR          
SEQRES  27 A  464  MET SER ALA VAL LEU GLN VAL ALA THR GLY VAL ILE SER          
SEQRES  28 A  464  THR LEU GLN ILE HIS GLN GLU ASN MET GLY GLN ALA LEU          
SEQRES  29 A  464  SER PRO ASP MET LEU ALA THR ASP LEU ALA TYR TYR LEU          
SEQRES  30 A  464  VAL ARG LYS GLY MET PRO PHE ARG GLN ALA HIS GLU ALA          
SEQRES  31 A  464  SER GLY LYS ALA VAL PHE MET ALA GLU THR LYS GLY VAL          
SEQRES  32 A  464  ALA LEU ASN GLN LEU SER LEU GLN GLU LEU GLN THR ILE          
SEQRES  33 A  464  SER PRO LEU PHE SER GLY ASP VAL ILE CYS VAL TRP ASP          
SEQRES  34 A  464  TYR ARG HIS SER VAL GLU GLN TYR GLY ALA LEU GLY GLY          
SEQRES  35 A  464  THR ALA ARG SER SER VAL ASP TRP GLN ILE ARG GLN VAL          
SEQRES  36 A  464  ARG ALA LEU LEU GLN ALA GLN GLN ALA                          
SEQRES   1 B  464  MET ALA SER GLU SER GLN LYS LEU TRP GLY GLY ARG PHE          
SEQRES   2 B  464  VAL GLY ALA VAL ASP PRO ILE MET GLU LYS PHE ASN ALA          
SEQRES   3 B  464  SER ILE ALA TYR ASP ARG HIS LEU TRP GLU VAL ASP VAL          
SEQRES   4 B  464  GLN GLY SER LYS ALA TYR SER ARG GLY LEU GLU LYS ALA          
SEQRES   5 B  464  GLY LEU LEU THR LYS ALA GLU MET ASP GLN ILE LEU HIS          
SEQRES   6 B  464  GLY LEU ASP LYS VAL ALA GLU GLU TRP ALA GLN GLY THR          
SEQRES   7 B  464  PHE LYS LEU ASN SER ASN ASP GLU ASP ILE HIS THR ALA          
SEQRES   8 B  464  ASN GLU ARG ARG LEU LYS GLU LEU ILE GLY ALA THR ALA          
SEQRES   9 B  464  GLY LYS LEU HIS THR GLY ARG SER ARG ASN ASP GLN VAL          
SEQRES  10 B  464  VAL THR ASP LEU ARG LEU TRP MET ARG GLN THR CYS SER          
SEQRES  11 B  464  THR LEU SER GLY LEU LEU TRP GLU LEU ILE ARG THR MET          
SEQRES  12 B  464  VAL ASP ARG ALA GLU ALA GLU ARG ASP VAL LEU PHE PRO          
SEQRES  13 B  464  GLY TYR THR HIS LEU GLN ARG ALA GLN PRO ILE ARG TRP          
SEQRES  14 B  464  SER HIS TRP ILE LEU SER HIS ALA VAL ALA LEU THR ARG          
SEQRES  15 B  464  ASP SER GLU ARG LEU LEU GLU VAL ARG LYS ARG ILE ASN          
SEQRES  16 B  464  VAL LEU PRO LEU GLY SER GLY ALA ILE ALA GLY ASN PRO          
SEQRES  17 B  464  LEU GLY VAL ASP ARG GLU LEU LEU ARG ALA GLU LEU ASN          
SEQRES  18 B  464  PHE GLY ALA ILE THR LEU ASN SER MET ASP ALA THR SER          
SEQRES  19 B  464  GLU ARG ASP PHE VAL ALA GLU PHE LEU PHE TRP ARG SER          
SEQRES  20 B  464  LEU CYS MET THR HIS LEU SER ARG MET ALA GLU ASP LEU          
SEQRES  21 B  464  ILE LEU TYR CYS THR LYS GLU PHE SER PHE VAL GLN LEU          
SEQRES  22 B  464  SER ASP ALA TYR SER THR GLY SER SER LEU MET PRO GLN          
SEQRES  23 B  464  LYS LYS ASN PRO ASP SER LEU GLU LEU ILE ARG SER LYS          
SEQRES  24 B  464  ALA GLY ARG VAL PHE GLY ARG CYS ALA GLY LEU LEU MET          
SEQRES  25 B  464  THR LEU LYS GLY LEU PRO SER THR TYR ASN LYS ASP LEU          
SEQRES  26 B  464  GLN GLU ASP LYS GLU ALA VAL PHE GLU VAL SER ASP THR          
SEQRES  27 B  464  MET SER ALA VAL LEU GLN VAL ALA THR GLY VAL ILE SER          
SEQRES  28 B  464  THR LEU GLN ILE HIS GLN GLU ASN MET GLY GLN ALA LEU          
SEQRES  29 B  464  SER PRO ASP MET LEU ALA THR ASP LEU ALA TYR TYR LEU          
SEQRES  30 B  464  VAL ARG LYS GLY MET PRO PHE ARG GLN ALA HIS GLU ALA          
SEQRES  31 B  464  SER GLY LYS ALA VAL PHE MET ALA GLU THR LYS GLY VAL          
SEQRES  32 B  464  ALA LEU ASN GLN LEU SER LEU GLN GLU LEU GLN THR ILE          
SEQRES  33 B  464  SER PRO LEU PHE SER GLY ASP VAL ILE CYS VAL TRP ASP          
SEQRES  34 B  464  TYR ARG HIS SER VAL GLU GLN TYR GLY ALA LEU GLY GLY          
SEQRES  35 B  464  THR ALA ARG SER SER VAL ASP TRP GLN ILE ARG GLN VAL          
SEQRES  36 B  464  ARG ALA LEU LEU GLN ALA GLN GLN ALA                          
HELIX    1   1 GLU A   22  ASN A   25  1                                   4    
HELIX    2   2 ASP A   31  LYS A   51  5                                  21    
HELIX    3   3 LYS A   57  LYS A   69  1                                  13    
HELIX    4   4 ILE A   88  LEU A   99  1                                  12    
HELIX    5   5 ALA A  102  HIS A  108  1                                   7    
HELIX    6   6 ARG A  113  GLU A  150  1                                  38    
HELIX    7   7 TRP A  169  ILE A  194  1                                  26    
HELIX    8   8 ARG A  213  GLU A  219  1                                   7    
HELIX    9   9 SER A  229  SER A  234  1                                   6    
HELIX   10  10 ASP A  237  TYR A  263  1                                  27    
HELIX   11  11 SER A  292  LEU A  310  1                                  19    
HELIX   12  12 LYS A  323  THR A  352  5                                  30    
HELIX   13  13 GLN A  357  ALA A  363  1                                   7    
HELIX   14  14 PRO A  366  ARG A  379  1                                  14    
HELIX   15  15 PHE A  384  LYS A  401  1                                  18    
HELIX   16  16 LEU A  405  GLN A  407  5                                   3    
HELIX   17  17 LEU A  410  ILE A  416  1                                   7    
HELIX   18  18 GLY A  422  TRP A  428  5                                   7    
HELIX   19  19 TYR A  430  GLN A  436  1                                   7    
HELIX   20  20 ARG A  445  GLN A  460  1                                  16    
HELIX   21  21 GLU B   22  ASN B   25  1                                   4    
HELIX   22  22 ASP B   31  LYS B   51  5                                  21    
HELIX   23  23 LYS B   57  LYS B   69  1                                  13    
HELIX   24  24 ILE B   88  LEU B   99  1                                  12    
HELIX   25  25 ALA B  102  HIS B  108  1                                   7    
HELIX   26  26 ARG B  113  GLU B  150  1                                  38    
HELIX   27  27 TRP B  169  ILE B  194  1                                  26    
HELIX   28  28 ARG B  213  GLU B  219  1                                   7    
HELIX   29  29 SER B  229  SER B  234  1                                   6    
HELIX   30  30 ASP B  237  TYR B  263  1                                  27    
HELIX   31  31 SER B  292  LEU B  310  1                                  19    
HELIX   32  32 LYS B  323  THR B  352  5                                  30    
HELIX   33  33 GLN B  357  ALA B  363  1                                   7    
HELIX   34  34 PRO B  366  ARG B  379  1                                  14    
HELIX   35  35 PHE B  384  LYS B  401  1                                  18    
HELIX   36  36 LEU B  405  GLN B  407  5                                   3    
HELIX   37  37 LEU B  410  ILE B  416  1                                   7    
HELIX   38  38 GLY B  422  TRP B  428  5                                   7    
HELIX   39  39 TYR B  430  GLN B  436  1                                   7    
HELIX   40  40 ARG B  445  GLN B  460  1                                  16    
SHEET    1   A 2 LEU A 154  TYR A 158  0                                        
SHEET    2   A 2 ARG A 163  ARG A 168 -1  N  ILE A 167   O  PHE A 155           
SHEET    1   B 2 LEU B 154  TYR B 158  0                                        
SHEET    2   B 2 ARG B 163  ARG B 168 -1  N  ILE B 167   O  PHE B 155           
CRYST1  104.600  104.600  183.200  90.00  90.00 120.00 P 31 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009560  0.005520  0.000000        0.00000                         
SCALE2      0.000000  0.011039  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005459        0.00000                         
MTRIX1   1  0.246600  0.716500 -0.652500       46.12400    1                    
MTRIX2   1  0.716600 -0.588100 -0.375000       28.02300    1                    
MTRIX3   1 -0.652500 -0.375100 -0.658500      118.81200    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system