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Database: PDB
Entry: 1K62
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Original site: 1K62 
HEADER    LYASE                                   14-OCT-01   1K62              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN ARGININOSUCCINATE LYASE                
TITLE    2 Q286R MUTANT                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ARGININOSUCCINATE LYASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ARGINOSUCCINASE; ASAL;                                      
COMPND   5 EC: 4.3.2.1;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET3C                                     
KEYWDS    INTRAGENIC COMPLEMENTATION, ARGINIOSUCCINATE LYASE, DELTA             
KEYWDS   2 CRYSTALLIN, ENZYME MECHANISM                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.M.SAMPALEANU,F.VALLEE,G.D.THOMPSON,P.L.HOWELL                       
REVDAT   3   13-MAY-08 1K62    1       REMARK                                   
REVDAT   2   06-MAY-08 1K62    1       COMPND VERSN                             
REVDAT   1   01-FEB-02 1K62    0                                                
JRNL        AUTH   L.M.SAMPALEANU,F.VALLEE,G.D.THOMPSON,P.L.HOWELL              
JRNL        TITL   THREE-DIMENSIONAL STRUCTURE OF THE                           
JRNL        TITL 2 ARGININOSUCCINATE LYASE FREQUENTLY COMPLEMENTING             
JRNL        TITL 3 ALLELE Q286R.                                                
JRNL        REF    BIOCHEMISTRY                  V.  40 15570 2001              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   11747432                                                     
JRNL        DOI    10.1021/BI011525M                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 16.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 8156643.890                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 31478                          
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) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.200                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 3208                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4391                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580                       
REMARK   3   BIN FREE R VALUE                    : 0.2950                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.10                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 495                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.013                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7122                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 222                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.26000                                              
REMARK   3    B22 (A**2) : 2.26000                                              
REMARK   3    B33 (A**2) : -4.53000                                             
REMARK   3    B12 (A**2) : 8.92000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.26                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.35                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.34                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.42                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.10                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 18.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.73                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.31                                                 
REMARK   3   BSOL        : 54.22                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : CIS_PEPTIDE.PARAM                              
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER_REP.TOP                                  
REMARK   3  TOPOLOGY FILE  3   : CIS_PEPTIDE.TOP                                
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1K62 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB014605.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 7                                  
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                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : CRYSTAL MONOCHROMATOR              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79294                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 17.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46000                            
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: AMORE                                                 
REMARK 200 STARTING MODEL: 1AUW                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.1 M PHOSPHATE, PH 7.0, VAPOR           
REMARK 280  DIFFUSION, HANGING DROP AT 298K                                     
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       61.00633            
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      122.01267            
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      122.01267            
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       61.00633            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HOMOTETRAMER GENERATED FROM     
REMARK 300 THE DIMER IN THE ASYMMETRIC UNIT BY THE OPERATION: -X, Y-X, 1/3-Z    
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 30460 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 58850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -161.1 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  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      122.01267            
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     GLY 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     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     SER B     5                                                      
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     ARG A 246    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 286    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ARG B 246    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 286    CB   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        3.22    -69.47                                   
REMARK 500    GLU A  98        6.41    -61.76                                   
REMARK 500    ARG A 151        5.31    -63.45                                   
REMARK 500    ALA A 164      -69.83   -102.45                                   
REMARK 500    ILE A 204      -42.57   -170.83                                   
REMARK 500    PRO A 290       47.26    -74.23                                   
REMARK 500    THR A 320      -82.84   -120.30                                   
REMARK 500    PHE A 420       74.93    -63.44                                   
REMARK 500    SER A 421     -160.24    -71.22                                   
REMARK 500    VAL A 424      -33.66    -21.55                                   
REMARK 500    TRP A 428        3.06    -69.32                                   
REMARK 500    LEU A 440      119.91    -38.41                                   
REMARK 500    LYS B   7      -21.46     64.26                                   
REMARK 500    VAL B  17      -64.84   -136.23                                   
REMARK 500    ASP B  18      103.28     71.30                                   
REMARK 500    ILE B 100      -25.43   -145.09                                   
REMARK 500    ALA B 102      -90.01    -62.71                                   
REMARK 500    ILE B 204      -42.56   -173.26                                   
REMARK 500    ALA B 224     -179.79   -170.37                                   
REMARK 500    ARG B 236       33.56   -142.57                                   
REMARK 500    PRO B 290       42.83    -78.12                                   
REMARK 500    THR B 320      -82.44   -104.78                                   
REMARK 500    HIS B 356       79.09   -115.97                                   
REMARK 500    MET B 397      -72.27    -58.79                                   
REMARK 500    SER B 421     -164.19   -100.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 562        DISTANCE =  5.43 ANGSTROMS                       
REMARK 525    HOH B 574        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH B 578        DISTANCE =  5.25 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AOS   RELATED DB: PDB                                   
REMARK 900 ARGININOSUCCINATE LYASE (HUMAN)                                      
REMARK 900 RELATED ID: 1HY1   RELATED DB: PDB                                   
REMARK 900 WILD TYPE DUCK DELTA 2 CRYSTALLIN                                    
REMARK 900 RELATED ID: 1HY0   RELATED DB: PDB                                   
REMARK 900 WILD TYPE DUCK DELTA 1 CRYSTALLIN                                    
REMARK 900 RELATED ID: 1AUW   RELATED DB: PDB                                   
REMARK 900 DUCK DELTA 2 CRYSTALLIN H91N MUTANT                                  
REMARK 900 RELATED ID: 1DCN   RELATED DB: PDB                                   
REMARK 900 DUCK DELTA 2 CRYSTALLIN H162N MUTANT                                 
REMARK 900 RELATED ID: 1I0A   RELATED DB: PDB                                   
REMARK 900 WILD TYPE TURKEY DELTA 1 CRYSTALLIN                                  
DBREF  1K62 A    1   464  UNP    P04424   ARLY_HUMAN       1    464             
DBREF  1K62 B    1   464  UNP    P04424   ARLY_HUMAN       1    464             
SEQADV 1K62 ARG A  286  UNP  P04424    GLN   286 ENGINEERED                     
SEQADV 1K62 ARG B  286  UNP  P04424    GLN   286 ENGINEERED                     
SEQRES   1 A  464  MET ALA SER GLU SER GLY 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 ARG          
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 GLY 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 ARG          
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                          
FORMUL   3  HOH   *222(H2 O)                                                    
HELIX    1   1 ASP A   18  ALA A   26  1                                   9    
HELIX    2   2 SER A   27  ARG A   32  1                                   6    
HELIX    3   3 LEU A   34  ALA A   52  1                                  19    
HELIX    4   4 THR A   56  GLY A   77  1                                  22    
HELIX    5   5 ASP A   87  GLY A  101  1                                  15    
HELIX    6   6 ALA A  102  LEU A  107  5                                   6    
HELIX    7   7 SER A  112  ARG A  151  1                                  40    
HELIX    8   8 TRP A  169  ASN A  195  1                                  27    
HELIX    9   9 ASP A  212  LEU A  220  1                                   9    
HELIX   10  10 ASN A  228  THR A  233  1                                   6    
HELIX   11  11 ARG A  236  THR A  265  1                                  30    
HELIX   12  12 PRO A  290  LYS A  315  1                                  26    
HELIX   13  13 ASN A  322  GLN A  326  5                                   5    
HELIX   14  14 GLU A  327  LEU A  353  1                                  27    
HELIX   15  15 HIS A  356  ALA A  363  1                                   8    
HELIX   16  16 SER A  365  MET A  368  5                                   4    
HELIX   17  17 LEU A  369  LYS A  380  1                                  12    
HELIX   18  18 PRO A  383  LYS A  401  1                                  19    
HELIX   19  19 ALA A  404  LEU A  408  5                                   5    
HELIX   20  20 SER A  409  THR A  415  1                                   7    
HELIX   21  21 GLY A  422  TRP A  428  5                                   7    
HELIX   22  22 ASP A  429  GLU A  435  1                                   7    
HELIX   23  23 ALA A  444  ALA A  464  1                                  21    
HELIX   24  24 ASP B   18  PHE B   24  1                                   7    
HELIX   25  25 SER B   27  ARG B   32  1                                   6    
HELIX   26  26 LEU B   34  GLY B   53  1                                  20    
HELIX   27  27 THR B   56  GLN B   76  1                                  21    
HELIX   28  28 ASP B   87  LEU B   99  1                                  13    
HELIX   29  29 ALA B  102  LEU B  107  5                                   6    
HELIX   30  30 SER B  112  GLU B  150  1                                  39    
HELIX   31  31 TRP B  169  ASN B  195  1                                  27    
HELIX   32  32 ASP B  212  LEU B  220  1                                   9    
HELIX   33  33 ASN B  228  GLU B  235  1                                   8    
HELIX   34  34 ARG B  236  CYS B  264  1                                  29    
HELIX   35  35 SER B  274  SER B  278  5                                   5    
HELIX   36  36 PRO B  290  LYS B  315  1                                  26    
HELIX   37  37 ASN B  322  GLN B  326  5                                   5    
HELIX   38  38 GLU B  327  LEU B  353  1                                  27    
HELIX   39  39 HIS B  356  ALA B  363  1                                   8    
HELIX   40  40 SER B  365  MET B  368  5                                   4    
HELIX   41  41 LEU B  369  ARG B  379  1                                  11    
HELIX   42  42 PRO B  383  LYS B  401  1                                  19    
HELIX   43  43 ALA B  404  LEU B  408  5                                   5    
HELIX   44  44 SER B  409  THR B  415  1                                   7    
HELIX   45  45 SER B  421  VAL B  427  5                                   7    
HELIX   46  46 ASP B  429  GLU B  435  1                                   7    
HELIX   47  47 ALA B  444  ALA B  464  1                                  21    
SHEET    1   A 2 LEU A 154  THR A 159  0                                        
SHEET    2   A 2 GLN A 162  ARG A 168 -1  O  ALA A 164   N  GLY A 157           
SHEET    1   B 2 VAL A 196  LEU A 197  0                                        
SHEET    2   B 2 ALA A 224  ILE A 225  1  O  ALA A 224   N  LEU A 197           
SHEET    1   C 2 VAL A 271  GLN A 272  0                                        
SHEET    2   C 2 GLN A 354  ILE A 355 -1  O  GLN A 354   N  GLN A 272           
SHEET    1   D 2 LEU B 154  THR B 159  0                                        
SHEET    2   D 2 GLN B 162  ARG B 168 -1  O  ILE B 167   N  PHE B 155           
SHEET    1   E 2 VAL B 271  GLN B 272  0                                        
SHEET    2   E 2 GLN B 354  ILE B 355 -1  O  GLN B 354   N  GLN B 272           
SHEET    1   F 2 THR B 279  GLY B 280  0                                        
SHEET    2   F 2 LYS B 288  ASN B 289 -1  O  ASN B 289   N  THR B 279           
CISPEP   1 SER A  319    THR A  320          0         8.09                     
CISPEP   2 SER B  319    THR B  320          0        -4.67                     
CRYST1  104.202  104.202  183.019  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      0.009597  0.005541  0.000000        0.00000                         
SCALE2      0.000000  0.011081  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005464        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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