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Database: PDB
Entry: 2R3V
LinkDB: 2R3V
Original site: 2R3V 
HEADER    TRANSFERASE                             30-AUG-07   2R3V              
TITLE     THE BIOCHEMICAL AND STRUCTURAL BASIS FOR FEEDBACK                     
TITLE    2 INHIBITION OF MEVALONATE KINASE AND ISOPRENOID METABOLISM            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MEVALONATE KINASE;                                         
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: MK;                                                         
COMPND   5 EC: 2.7.1.36;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: MVK;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL 21 DE3;                                 
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET-3D                                    
KEYWDS    MEVALONATE KINASE, FARNESYL THIODIPHOPHATE, ATP-BINDING,              
KEYWDS   2 CATARACT, CHOLESTEROL BIOSYNTHESIS, CYTOPLASM, DISEASE               
KEYWDS   3 MUTATION, LIPID SYNTHESIS, NUCLEOTIDE-BINDING, PEROXISOME,           
KEYWDS   4 POLYMORPHISM, STEROID BIOSYNTHESIS, STEROL BIOSYNTHESIS,             
KEYWDS   5 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.FU,N.E.VOYNOVA,H.M.MIZIORKO,J.P.KIM                                 
REVDAT   2   24-FEB-09 2R3V    1       VERSN                                    
REVDAT   1   24-JUN-08 2R3V    0                                                
JRNL        AUTH   Z.FU,N.E.VOYNOVA,T.J.HERDENDORF,H.M.MIZIORKO,                
JRNL        AUTH 2 J.J.KIM                                                      
JRNL        TITL   BIOCHEMICAL AND STRUCTURAL BASIS FOR FEEDBACK                
JRNL        TITL 2 INHIBITION OF MEVALONATE KINASE AND ISOPRENOID               
JRNL        TITL 3 METABOLISM.                                                  
JRNL        REF    BIOCHEMISTRY                  V.  47  3715 2008              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   18302342                                                     
JRNL        DOI    10.1021/BI7024386                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.37                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 404877.720                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 84.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 46301                          
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) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3916                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.59                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 44.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2216                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3720                       
REMARK   3   BIN FREE R VALUE                    : 0.3560                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 197                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.025                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11710                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 225                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -14.52000                                            
REMARK   3    B22 (A**2) : 27.20000                                             
REMARK   3    B33 (A**2) : -12.68000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -5.55000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.37                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.58                            
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) : 0.44                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.61                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.91                            
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        : 0.27                                                 
REMARK   3   BSOL        : 32.62                                                
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.PARAM                                    
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 2R3V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044391.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-AUG-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
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 RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46347                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.370                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.1                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 44.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.18000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MERLOT                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1KVK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES BUFFER, PEG5K MME, AMMONIUM          
REMARK 280  SULFATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       39.10000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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 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 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 33150 ANGSTROM**2                         
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                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 32980 ANGSTROM**2                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLU A    76                                                      
REMARK 465     GLN A    77                                                      
REMARK 465     GLY A    78                                                      
REMARK 465     ASP A    79                                                      
REMARK 465     LEU A   396                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LEU B    75                                                      
REMARK 465     GLU B    76                                                      
REMARK 465     GLN B    77                                                      
REMARK 465     GLY B    78                                                      
REMARK 465     ASP B    79                                                      
REMARK 465     VAL B    80                                                      
REMARK 465     LEU B   396                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C    76                                                      
REMARK 465     GLN C    77                                                      
REMARK 465     GLY C    78                                                      
REMARK 465     ASP C    79                                                      
REMARK 465     LEU C   396                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLU D    76                                                      
REMARK 465     GLN D    77                                                      
REMARK 465     GLY D    78                                                      
REMARK 465     ASP D    79                                                      
REMARK 465     VAL D    80                                                      
REMARK 465     LEU D   396                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LEU A   168     N    ASP A   170              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A   3      133.06    177.09                                   
REMARK 500    GLU A  19      -69.19      0.21                                   
REMARK 500    ASN A  34       40.08    -66.70                                   
REMARK 500    LEU A  35       69.79   -105.71                                   
REMARK 500    THR A  72       56.41    -67.65                                   
REMARK 500    PHE A  74       44.10    -79.98                                   
REMARK 500    ALA A  95      -91.04    -44.58                                   
REMARK 500    ASP A  99      -95.24     -0.17                                   
REMARK 500    CYS A 120        2.41    -67.92                                   
REMARK 500    TYR A 149      -71.62    -59.08                                   
REMARK 500    CYS A 161        1.22    -53.46                                   
REMARK 500    LYS A 169      -11.28    -22.66                                   
REMARK 500    ASP A 170      -73.88    -94.60                                   
REMARK 500    ASP A 172     -167.15   -116.12                                   
REMARK 500    ASN A 175      158.86    179.51                                   
REMARK 500    HIS A 217     -130.56   -113.24                                   
REMARK 500    PRO A 228      159.71    -43.03                                   
REMARK 500    ILE A 232     -166.33   -128.04                                   
REMARK 500    LYS A 238       12.00     50.06                                   
REMARK 500    PHE A 257       56.03   -118.18                                   
REMARK 500    GLU A 284     -103.79    -63.10                                   
REMARK 500    PRO A 286       95.07    -60.89                                   
REMARK 500    SER A 362       45.50    -74.91                                   
REMARK 500    CYS A 363       -9.99   -143.67                                   
REMARK 500    THR A 370     -155.71   -135.98                                   
REMARK 500    PRO A 375      -80.56    -29.47                                   
REMARK 500    VAL A 377      126.67    -35.49                                   
REMARK 500    ALA A 382       52.21    -53.24                                   
REMARK 500    THR A 383      -10.43   -156.50                                   
REMARK 500    LEU A 385     -169.56     83.11                                   
REMARK 500    ASP A 394      -63.33   -136.33                                   
REMARK 500    SER B   3      164.07    169.01                                   
REMARK 500    HIS B  24       49.52   -106.45                                   
REMARK 500    ASN B  34       29.78    -78.98                                   
REMARK 500    HIS B  44     -158.28   -137.76                                   
REMARK 500    SER B  45      -22.52   -159.50                                   
REMARK 500    ASN B  46       22.58    -74.24                                   
REMARK 500    LEU B  53       78.05   -114.27                                   
REMARK 500    VAL B  64      -19.45    -47.21                                   
REMARK 500    ALA B  65      -81.99    -53.33                                   
REMARK 500    SER B  69        0.98    -68.59                                   
REMARK 500    LEU B  70      147.73    -31.22                                   
REMARK 500    THR B  72      102.52     28.70                                   
REMARK 500    SER B  73       65.63   -117.53                                   
REMARK 500    PRO B  83      -95.01    -88.55                                   
REMARK 500    GLU B  86      -74.56    -63.28                                   
REMARK 500    VAL B  88      -77.65    -69.44                                   
REMARK 500    ASP B 100      -99.04     76.64                                   
REMARK 500    CYS B 101      117.56     45.37                                   
REMARK 500    ALA B 102      120.62    -27.10                                   
REMARK 500    SER B 118      -64.88    -99.12                                   
REMARK 500    CYS B 120       35.68    -87.08                                   
REMARK 500    LYS B 122       24.92    -75.06                                   
REMARK 500    LEU B 153      -70.26    -51.10                                   
REMARK 500    CYS B 161       20.73    -69.36                                   
REMARK 500    GLU B 162       26.28     33.84                                   
REMARK 500    LYS B 169        0.69   -159.27                                   
REMARK 500    ASP B 172     -111.02    -95.96                                   
REMARK 500    CYS B 173      -55.60   -140.29                                   
REMARK 500    VAL B 174      -93.76   -124.02                                   
REMARK 500    ASN B 175      111.90     63.86                                   
REMARK 500    THR B 209      -70.79    -71.90                                   
REMARK 500    HIS B 217     -138.50    -97.25                                   
REMARK 500    LYS B 238      -21.80     69.98                                   
REMARK 500    ARG B 251      -71.27    -56.82                                   
REMARK 500    PHE B 257       47.93   -146.53                                   
REMARK 500    GLU B 281      -15.90   -172.04                                   
REMARK 500    PRO B 286     -175.76    -38.77                                   
REMARK 500    GLU B 349     -165.18    -78.18                                   
REMARK 500    PRO B 351      -84.88    -44.37                                   
REMARK 500    GLU B 352      -67.11    -19.52                                   
REMARK 500    CYS B 363       -5.50    -54.99                                   
REMARK 500    THR B 370     -151.76   -101.81                                   
REMARK 500    PRO B 375      -76.21    -41.10                                   
REMARK 500    VAL B 377      112.95    -30.90                                   
REMARK 500    SER B 381      -86.22    -36.07                                   
REMARK 500    ALA B 382      -52.83    169.72                                   
REMARK 500    LEU B 385      120.50   -178.45                                   
REMARK 500    ASP B 386      158.27    -35.55                                   
REMARK 500    SER B 387      -71.43    -54.33                                   
REMARK 500    GLN B 391      -73.88    -46.44                                   
REMARK 500    ASP B 394      -89.95    -88.97                                   
REMARK 500    SER C   3     -133.16    -93.35                                   
REMARK 500    GLU C   4      -18.65   -165.67                                   
REMARK 500    GLU C  19      -72.71     -6.59                                   
REMARK 500    VAL C  23      -36.24    -37.74                                   
REMARK 500    HIS C  24       42.31   -104.10                                   
REMARK 500    ARG C  36      159.98    -36.03                                   
REMARK 500    SER C  45       77.36    -35.01                                   
REMARK 500    ASN C  46      -27.68   -158.91                                   
REMARK 500    LYS C  48      103.88    159.92                                   
REMARK 500    ALA C  61      139.08   -177.11                                   
REMARK 500    SER C  69      -71.92    -81.07                                   
REMARK 500    LEU C  70      141.04    -22.61                                   
REMARK 500    THR C  72       53.13    -59.83                                   
REMARK 500    PHE C  74       -7.72    -45.41                                   
REMARK 500    PRO C  83       74.53    -68.05                                   
REMARK 500    CYS C 101     -166.93    -57.53                                   
REMARK 500    ARG C 121      -73.84    -96.27                                   
REMARK 500    ARG C 124      -84.04    -38.16                                   
REMARK 500    PRO C 139      177.81    -53.63                                   
REMARK 500    ALA C 141       12.06   -171.15                                   
REMARK 500    SER C 150      -19.25    -49.34                                   
REMARK 500    ALA C 155      -79.29    -68.39                                   
REMARK 500    ALA C 156      -17.66    -43.01                                   
REMARK 500    LEU C 158      -14.27    -48.78                                   
REMARK 500    PRO C 165     -107.81    -51.86                                   
REMARK 500    ASN C 166      149.96    170.65                                   
REMARK 500    LEU C 168       31.65    -65.18                                   
REMARK 500    ASP C 172     -167.24    -74.17                                   
REMARK 500    ASN C 175      141.07   -179.24                                   
REMARK 500    TRP C 177     -160.70    -72.98                                   
REMARK 500    LYS C 179      -73.73    -30.12                                   
REMARK 500    HIS C 197       -8.34   -150.45                                   
REMARK 500    PRO C 200      172.16    -53.91                                   
REMARK 500    HIS C 217     -136.30   -106.34                                   
REMARK 500    SER C 222      147.65   -177.53                                   
REMARK 500    SER C 227      132.80    179.73                                   
REMARK 500    THR C 237      -15.30    -48.47                                   
REMARK 500    GLU C 281       -3.22   -158.38                                   
REMARK 500    ALA C 285       50.62   -115.61                                   
REMARK 500    PRO C 286      151.01    -27.63                                   
REMARK 500    GLN C 290      -38.95   -131.82                                   
REMARK 500    PRO C 346      158.45    -49.18                                   
REMARK 500    THR C 370     -159.35   -166.71                                   
REMARK 500    ALA C 374      177.52    -55.16                                   
REMARK 500    ALA C 382       -1.74     61.14                                   
REMARK 500    VAL C 389      -78.81    -70.76                                   
REMARK 500    ASP C 394      -70.62    -68.54                                   
REMARK 500    GLU D   4      -71.48    -69.16                                   
REMARK 500    GLU D  19      -63.71     -6.75                                   
REMARK 500    VAL D  23      -12.82    -46.37                                   
REMARK 500    ASN D  34       48.51    -75.19                                   
REMARK 500    LEU D  35       66.90   -111.64                                   
REMARK 500    LEU D  53       71.13   -119.10                                   
REMARK 500    SER D  69        2.12    -68.56                                   
REMARK 500    LEU D  70       10.27    -66.33                                   
REMARK 500    PHE D  74      -13.16   -163.67                                   
REMARK 500    GLU D  89      -71.99    -60.25                                   
REMARK 500    ALA D  95     -107.40   -106.93                                   
REMARK 500    ALA D 102     -123.95     35.90                                   
REMARK 500    VAL D 103      -39.77   -154.96                                   
REMARK 500    LEU D 129      147.48   -178.23                                   
REMARK 500    ALA D 155      -66.91    -93.91                                   
REMARK 500    PRO D 165     -169.53    -51.53                                   
REMARK 500    PRO D 167        9.15    -62.55                                   
REMARK 500    LYS D 169       88.48    -49.07                                   
REMARK 500    ASP D 170       12.59    169.72                                   
REMARK 500    ASP D 172     -152.48   -178.09                                   
REMARK 500    CYS D 173      -60.98   -103.49                                   
REMARK 500    LYS D 179      -82.53    -15.34                                   
REMARK 500    ASN D 199       52.31   -160.72                                   
REMARK 500    HIS D 217     -128.85   -124.27                                   
REMARK 500    GLN D 218       39.29    -73.20                                   
REMARK 500    LYS D 225      -95.67    -81.12                                   
REMARK 500    ARG D 226      -33.94    -38.84                                   
REMARK 500    SER D 227      109.19    -24.06                                   
REMARK 500    PRO D 228     -136.86    -82.01                                   
REMARK 500    ILE D 232     -158.94   -111.68                                   
REMARK 500    LEU D 233       89.93   -151.77                                   
REMARK 500    THR D 243      -48.89    -29.47                                   
REMARK 500    GLU D 281      -23.67   -147.98                                   
REMARK 500    GLU D 284      -79.29   -104.76                                   
REMARK 500    PRO D 346       54.53    -65.79                                   
REMARK 500    GLN D 358      -70.84    -56.70                                   
REMARK 500    THR D 370     -148.51   -110.58                                   
REMARK 500    ALA D 374      171.51    -46.09                                   
REMARK 500    PRO D 375      -83.46    -51.66                                   
REMARK 500    HIS D 380     -159.94   -110.45                                   
REMARK 500    ALA D 382       15.99     50.79                                   
REMARK 500    LEU D 385      150.33    -43.97                                   
REMARK 500    ASP D 386        0.08    -69.95                                   
REMARK 500    SER D 387     -161.59     45.29                                   
REMARK 500    ARG D 388     -129.62     44.59                                   
REMARK 500    VAL D 389      -12.68    -49.27                                   
REMARK 500    GLN D 390      -91.38    -72.26                                   
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 C 397        DISTANCE =  6.54 ANGSTROMS                       
REMARK 525    HOH D 406        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH A 420        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH B 423        DISTANCE =  5.71 ANGSTROMS                       
REMARK 525    HOH C 431        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH D 432        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH A 439        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH C 440        DISTANCE =  5.64 ANGSTROMS                       
REMARK 525    HOH B 459        DISTANCE =  6.39 ANGSTROMS                       
DBREF  2R3V A    1   396  UNP    Q03426   KIME_HUMAN       1    396             
DBREF  2R3V B    1   396  UNP    Q03426   KIME_HUMAN       1    396             
DBREF  2R3V C    1   396  UNP    Q03426   KIME_HUMAN       1    396             
DBREF  2R3V D    1   396  UNP    Q03426   KIME_HUMAN       1    396             
SEQRES   1 A  396  MET LEU SER GLU VAL LEU LEU VAL SER ALA PRO GLY LYS          
SEQRES   2 A  396  VAL ILE LEU HIS GLY GLU HIS ALA VAL VAL HIS GLY LYS          
SEQRES   3 A  396  VAL ALA LEU ALA VAL SER LEU ASN LEU ARG THR PHE LEU          
SEQRES   4 A  396  ARG LEU GLN PRO HIS SER ASN GLY LYS VAL ASP LEU SER          
SEQRES   5 A  396  LEU PRO ASN ILE GLY ILE LYS ARG ALA TRP ASP VAL ALA          
SEQRES   6 A  396  ARG LEU GLN SER LEU ASP THR SER PHE LEU GLU GLN GLY          
SEQRES   7 A  396  ASP VAL THR THR PRO THR SER GLU GLN VAL GLU LYS LEU          
SEQRES   8 A  396  LYS GLU VAL ALA GLY LEU PRO ASP ASP CYS ALA VAL THR          
SEQRES   9 A  396  GLU ARG LEU ALA VAL LEU ALA PHE LEU TYR LEU TYR LEU          
SEQRES  10 A  396  SER ILE CYS ARG LYS GLN ARG ALA LEU PRO SER LEU ASP          
SEQRES  11 A  396  ILE VAL VAL TRP SER GLU LEU PRO PRO GLY ALA GLY LEU          
SEQRES  12 A  396  GLY SER SER ALA ALA TYR SER VAL CYS LEU ALA ALA ALA          
SEQRES  13 A  396  LEU LEU THR VAL CYS GLU GLU ILE PRO ASN PRO LEU LYS          
SEQRES  14 A  396  ASP GLY ASP CYS VAL ASN ARG TRP THR LYS GLU ASP LEU          
SEQRES  15 A  396  GLU LEU ILE ASN LYS TRP ALA PHE GLN GLY GLU ARG MET          
SEQRES  16 A  396  ILE HIS GLY ASN PRO SER GLY VAL ASP ASN ALA VAL SER          
SEQRES  17 A  396  THR TRP GLY GLY ALA LEU ARG TYR HIS GLN GLY LYS ILE          
SEQRES  18 A  396  SER SER LEU LYS ARG SER PRO ALA LEU GLN ILE LEU LEU          
SEQRES  19 A  396  THR ASN THR LYS VAL PRO ARG ASN THR ARG ALA LEU VAL          
SEQRES  20 A  396  ALA GLY VAL ARG ASN ARG LEU LEU LYS PHE PRO GLU ILE          
SEQRES  21 A  396  VAL ALA PRO LEU LEU THR SER ILE ASP ALA ILE SER LEU          
SEQRES  22 A  396  GLU CYS GLU ARG VAL LEU GLY GLU MET GLY GLU ALA PRO          
SEQRES  23 A  396  ALA PRO GLU GLN TYR LEU VAL LEU GLU GLU LEU ILE ASP          
SEQRES  24 A  396  MET ASN GLN HIS HIS LEU ASN ALA LEU GLY VAL GLY HIS          
SEQRES  25 A  396  ALA SER LEU ASP GLN LEU CYS GLN VAL THR ARG ALA ARG          
SEQRES  26 A  396  GLY LEU HIS SER LYS LEU THR GLY ALA GLY GLY GLY GLY          
SEQRES  27 A  396  CYS GLY ILE THR LEU LEU LYS PRO GLY LEU GLU GLN PRO          
SEQRES  28 A  396  GLU VAL GLU ALA THR LYS GLN ALA LEU THR SER CYS GLY          
SEQRES  29 A  396  PHE ASP CYS LEU GLU THR SER ILE GLY ALA PRO GLY VAL          
SEQRES  30 A  396  SER ILE HIS SER ALA THR SER LEU ASP SER ARG VAL GLN          
SEQRES  31 A  396  GLN ALA LEU ASP GLY LEU                                      
SEQRES   1 B  396  MET LEU SER GLU VAL LEU LEU VAL SER ALA PRO GLY LYS          
SEQRES   2 B  396  VAL ILE LEU HIS GLY GLU HIS ALA VAL VAL HIS GLY LYS          
SEQRES   3 B  396  VAL ALA LEU ALA VAL SER LEU ASN LEU ARG THR PHE LEU          
SEQRES   4 B  396  ARG LEU GLN PRO HIS SER ASN GLY LYS VAL ASP LEU SER          
SEQRES   5 B  396  LEU PRO ASN ILE GLY ILE LYS ARG ALA TRP ASP VAL ALA          
SEQRES   6 B  396  ARG LEU GLN SER LEU ASP THR SER PHE LEU GLU GLN GLY          
SEQRES   7 B  396  ASP VAL THR THR PRO THR SER GLU GLN VAL GLU LYS LEU          
SEQRES   8 B  396  LYS GLU VAL ALA GLY LEU PRO ASP ASP CYS ALA VAL THR          
SEQRES   9 B  396  GLU ARG LEU ALA VAL LEU ALA PHE LEU TYR LEU TYR LEU          
SEQRES  10 B  396  SER ILE CYS ARG LYS GLN ARG ALA LEU PRO SER LEU ASP          
SEQRES  11 B  396  ILE VAL VAL TRP SER GLU LEU PRO PRO GLY ALA GLY LEU          
SEQRES  12 B  396  GLY SER SER ALA ALA TYR SER VAL CYS LEU ALA ALA ALA          
SEQRES  13 B  396  LEU LEU THR VAL CYS GLU GLU ILE PRO ASN PRO LEU LYS          
SEQRES  14 B  396  ASP GLY ASP CYS VAL ASN ARG TRP THR LYS GLU ASP LEU          
SEQRES  15 B  396  GLU LEU ILE ASN LYS TRP ALA PHE GLN GLY GLU ARG MET          
SEQRES  16 B  396  ILE HIS GLY ASN PRO SER GLY VAL ASP ASN ALA VAL SER          
SEQRES  17 B  396  THR TRP GLY GLY ALA LEU ARG TYR HIS GLN GLY LYS ILE          
SEQRES  18 B  396  SER SER LEU LYS ARG SER PRO ALA LEU GLN ILE LEU LEU          
SEQRES  19 B  396  THR ASN THR LYS VAL PRO ARG ASN THR ARG ALA LEU VAL          
SEQRES  20 B  396  ALA GLY VAL ARG ASN ARG LEU LEU LYS PHE PRO GLU ILE          
SEQRES  21 B  396  VAL ALA PRO LEU LEU THR SER ILE ASP ALA ILE SER LEU          
SEQRES  22 B  396  GLU CYS GLU ARG VAL LEU GLY GLU MET GLY GLU ALA PRO          
SEQRES  23 B  396  ALA PRO GLU GLN TYR LEU VAL LEU GLU GLU LEU ILE ASP          
SEQRES  24 B  396  MET ASN GLN HIS HIS LEU ASN ALA LEU GLY VAL GLY HIS          
SEQRES  25 B  396  ALA SER LEU ASP GLN LEU CYS GLN VAL THR ARG ALA ARG          
SEQRES  26 B  396  GLY LEU HIS SER LYS LEU THR GLY ALA GLY GLY GLY GLY          
SEQRES  27 B  396  CYS GLY ILE THR LEU LEU LYS PRO GLY LEU GLU GLN PRO          
SEQRES  28 B  396  GLU VAL GLU ALA THR LYS GLN ALA LEU THR SER CYS GLY          
SEQRES  29 B  396  PHE ASP CYS LEU GLU THR SER ILE GLY ALA PRO GLY VAL          
SEQRES  30 B  396  SER ILE HIS SER ALA THR SER LEU ASP SER ARG VAL GLN          
SEQRES  31 B  396  GLN ALA LEU ASP GLY LEU                                      
SEQRES   1 C  396  MET LEU SER GLU VAL LEU LEU VAL SER ALA PRO GLY LYS          
SEQRES   2 C  396  VAL ILE LEU HIS GLY GLU HIS ALA VAL VAL HIS GLY LYS          
SEQRES   3 C  396  VAL ALA LEU ALA VAL SER LEU ASN LEU ARG THR PHE LEU          
SEQRES   4 C  396  ARG LEU GLN PRO HIS SER ASN GLY LYS VAL ASP LEU SER          
SEQRES   5 C  396  LEU PRO ASN ILE GLY ILE LYS ARG ALA TRP ASP VAL ALA          
SEQRES   6 C  396  ARG LEU GLN SER LEU ASP THR SER PHE LEU GLU GLN GLY          
SEQRES   7 C  396  ASP VAL THR THR PRO THR SER GLU GLN VAL GLU LYS LEU          
SEQRES   8 C  396  LYS GLU VAL ALA GLY LEU PRO ASP ASP CYS ALA VAL THR          
SEQRES   9 C  396  GLU ARG LEU ALA VAL LEU ALA PHE LEU TYR LEU TYR LEU          
SEQRES  10 C  396  SER ILE CYS ARG LYS GLN ARG ALA LEU PRO SER LEU ASP          
SEQRES  11 C  396  ILE VAL VAL TRP SER GLU LEU PRO PRO GLY ALA GLY LEU          
SEQRES  12 C  396  GLY SER SER ALA ALA TYR SER VAL CYS LEU ALA ALA ALA          
SEQRES  13 C  396  LEU LEU THR VAL CYS GLU GLU ILE PRO ASN PRO LEU LYS          
SEQRES  14 C  396  ASP GLY ASP CYS VAL ASN ARG TRP THR LYS GLU ASP LEU          
SEQRES  15 C  396  GLU LEU ILE ASN LYS TRP ALA PHE GLN GLY GLU ARG MET          
SEQRES  16 C  396  ILE HIS GLY ASN PRO SER GLY VAL ASP ASN ALA VAL SER          
SEQRES  17 C  396  THR TRP GLY GLY ALA LEU ARG TYR HIS GLN GLY LYS ILE          
SEQRES  18 C  396  SER SER LEU LYS ARG SER PRO ALA LEU GLN ILE LEU LEU          
SEQRES  19 C  396  THR ASN THR LYS VAL PRO ARG ASN THR ARG ALA LEU VAL          
SEQRES  20 C  396  ALA GLY VAL ARG ASN ARG LEU LEU LYS PHE PRO GLU ILE          
SEQRES  21 C  396  VAL ALA PRO LEU LEU THR SER ILE ASP ALA ILE SER LEU          
SEQRES  22 C  396  GLU CYS GLU ARG VAL LEU GLY GLU MET GLY GLU ALA PRO          
SEQRES  23 C  396  ALA PRO GLU GLN TYR LEU VAL LEU GLU GLU LEU ILE ASP          
SEQRES  24 C  396  MET ASN GLN HIS HIS LEU ASN ALA LEU GLY VAL GLY HIS          
SEQRES  25 C  396  ALA SER LEU ASP GLN LEU CYS GLN VAL THR ARG ALA ARG          
SEQRES  26 C  396  GLY LEU HIS SER LYS LEU THR GLY ALA GLY GLY GLY GLY          
SEQRES  27 C  396  CYS GLY ILE THR LEU LEU LYS PRO GLY LEU GLU GLN PRO          
SEQRES  28 C  396  GLU VAL GLU ALA THR LYS GLN ALA LEU THR SER CYS GLY          
SEQRES  29 C  396  PHE ASP CYS LEU GLU THR SER ILE GLY ALA PRO GLY VAL          
SEQRES  30 C  396  SER ILE HIS SER ALA THR SER LEU ASP SER ARG VAL GLN          
SEQRES  31 C  396  GLN ALA LEU ASP GLY LEU                                      
SEQRES   1 D  396  MET LEU SER GLU VAL LEU LEU VAL SER ALA PRO GLY LYS          
SEQRES   2 D  396  VAL ILE LEU HIS GLY GLU HIS ALA VAL VAL HIS GLY LYS          
SEQRES   3 D  396  VAL ALA LEU ALA VAL SER LEU ASN LEU ARG THR PHE LEU          
SEQRES   4 D  396  ARG LEU GLN PRO HIS SER ASN GLY LYS VAL ASP LEU SER          
SEQRES   5 D  396  LEU PRO ASN ILE GLY ILE LYS ARG ALA TRP ASP VAL ALA          
SEQRES   6 D  396  ARG LEU GLN SER LEU ASP THR SER PHE LEU GLU GLN GLY          
SEQRES   7 D  396  ASP VAL THR THR PRO THR SER GLU GLN VAL GLU LYS LEU          
SEQRES   8 D  396  LYS GLU VAL ALA GLY LEU PRO ASP ASP CYS ALA VAL THR          
SEQRES   9 D  396  GLU ARG LEU ALA VAL LEU ALA PHE LEU TYR LEU TYR LEU          
SEQRES  10 D  396  SER ILE CYS ARG LYS GLN ARG ALA LEU PRO SER LEU ASP          
SEQRES  11 D  396  ILE VAL VAL TRP SER GLU LEU PRO PRO GLY ALA GLY LEU          
SEQRES  12 D  396  GLY SER SER ALA ALA TYR SER VAL CYS LEU ALA ALA ALA          
SEQRES  13 D  396  LEU LEU THR VAL CYS GLU GLU ILE PRO ASN PRO LEU LYS          
SEQRES  14 D  396  ASP GLY ASP CYS VAL ASN ARG TRP THR LYS GLU ASP LEU          
SEQRES  15 D  396  GLU LEU ILE ASN LYS TRP ALA PHE GLN GLY GLU ARG MET          
SEQRES  16 D  396  ILE HIS GLY ASN PRO SER GLY VAL ASP ASN ALA VAL SER          
SEQRES  17 D  396  THR TRP GLY GLY ALA LEU ARG TYR HIS GLN GLY LYS ILE          
SEQRES  18 D  396  SER SER LEU LYS ARG SER PRO ALA LEU GLN ILE LEU LEU          
SEQRES  19 D  396  THR ASN THR LYS VAL PRO ARG ASN THR ARG ALA LEU VAL          
SEQRES  20 D  396  ALA GLY VAL ARG ASN ARG LEU LEU LYS PHE PRO GLU ILE          
SEQRES  21 D  396  VAL ALA PRO LEU LEU THR SER ILE ASP ALA ILE SER LEU          
SEQRES  22 D  396  GLU CYS GLU ARG VAL LEU GLY GLU MET GLY GLU ALA PRO          
SEQRES  23 D  396  ALA PRO GLU GLN TYR LEU VAL LEU GLU GLU LEU ILE ASP          
SEQRES  24 D  396  MET ASN GLN HIS HIS LEU ASN ALA LEU GLY VAL GLY HIS          
SEQRES  25 D  396  ALA SER LEU ASP GLN LEU CYS GLN VAL THR ARG ALA ARG          
SEQRES  26 D  396  GLY LEU HIS SER LYS LEU THR GLY ALA GLY GLY GLY GLY          
SEQRES  27 D  396  CYS GLY ILE THR LEU LEU LYS PRO GLY LEU GLU GLN PRO          
SEQRES  28 D  396  GLU VAL GLU ALA THR LYS GLN ALA LEU THR SER CYS GLY          
SEQRES  29 D  396  PHE ASP CYS LEU GLU THR SER ILE GLY ALA PRO GLY VAL          
SEQRES  30 D  396  SER ILE HIS SER ALA THR SER LEU ASP SER ARG VAL GLN          
SEQRES  31 D  396  GLN ALA LEU ASP GLY LEU                                      
FORMUL   5  HOH   *225(H2 O)                                                    
HELIX    1   1 ALA A   21  GLY A   25  5                                   5    
HELIX    2   2 VAL A   64  LEU A   70  1                                   7    
HELIX    3   3 THR A   84  GLY A   96  1                                  13    
HELIX    4   4 ALA A  102  CYS A  120  1                                  19    
HELIX    5   5 GLY A  144  CYS A  161  1                                  18    
HELIX    6   6 THR A  178  HIS A  197  1                                  20    
HELIX    7   7 GLY A  202  GLY A  211  1                                  10    
HELIX    8   8 ASN A  242  PHE A  257  1                                  16    
HELIX    9   9 PHE A  257  GLU A  284  1                                  28    
HELIX   10  10 ALA A  287  LEU A  308  1                                  22    
HELIX   11  11 HIS A  312  ALA A  324  1                                  13    
HELIX   12  12 GLU A  349  SER A  362  1                                  14    
HELIX   13  13 ASP A  386  LEU A  393  1                                   8    
HELIX   14  14 HIS B   20  GLY B   25  5                                   6    
HELIX   15  15 PRO B   54  GLY B   57  5                                   4    
HELIX   16  16 VAL B   64  LEU B   70  1                                   7    
HELIX   17  17 PRO B   83  VAL B   94  1                                  12    
HELIX   18  18 ALA B  102  CYS B  120  1                                  19    
HELIX   19  19 GLY B  144  CYS B  161  1                                  18    
HELIX   20  20 THR B  178  HIS B  197  1                                  20    
HELIX   21  21 GLY B  202  GLY B  211  1                                  10    
HELIX   22  22 ASN B  242  PHE B  257  1                                  16    
HELIX   23  23 PHE B  257  GLY B  280  1                                  24    
HELIX   24  24 ALA B  287  LEU B  308  1                                  22    
HELIX   25  25 HIS B  312  ARG B  325  1                                  14    
HELIX   26  26 GLU B  349  CYS B  363  1                                  15    
HELIX   27  27 ASP B  386  ASP B  394  1                                   9    
HELIX   28  28 ALA C   21  GLY C   25  5                                   5    
HELIX   29  29 ALA C   65  LEU C   70  1                                   6    
HELIX   30  30 THR C   84  GLY C   96  1                                  13    
HELIX   31  31 ALA C  102  CYS C  120  1                                  19    
HELIX   32  32 GLY C  144  CYS C  161  1                                  18    
HELIX   33  33 THR C  178  ILE C  196  1                                  19    
HELIX   34  34 GLY C  202  GLY C  211  1                                  10    
HELIX   35  35 ASN C  242  PHE C  257  1                                  16    
HELIX   36  36 PHE C  257  GLY C  280  1                                  24    
HELIX   37  37 ALA C  287  GLY C  309  1                                  23    
HELIX   38  38 HIS C  312  ALA C  324  1                                  13    
HELIX   39  39 GLU C  349  SER C  362  1                                  14    
HELIX   40  40 ARG C  388  GLY C  395  1                                   8    
HELIX   41  41 ALA D   21  GLY D   25  5                                   5    
HELIX   42  42 VAL D   64  SER D   69  1                                   6    
HELIX   43  43 THR D   84  VAL D   94  1                                  11    
HELIX   44  44 VAL D  103  LYS D  122  1                                  20    
HELIX   45  45 GLY D  144  CYS D  161  1                                  18    
HELIX   46  46 THR D  178  HIS D  197  1                                  20    
HELIX   47  47 GLY D  202  GLY D  211  1                                  10    
HELIX   48  48 ASN D  242  PHE D  257  1                                  16    
HELIX   49  49 PHE D  257  GLY D  283  1                                  27    
HELIX   50  50 ALA D  287  LEU D  308  1                                  22    
HELIX   51  51 HIS D  312  ALA D  324  1                                  13    
HELIX   52  52 GLU D  349  CYS D  363  1                                  15    
HELIX   53  53 GLN D  390  ASP D  394  5                                   5    
SHEET    1   A 7 LYS A  59  ASP A  63  0                                        
SHEET    2   A 7 LYS A  48  SER A  52 -1  N  LEU A  51   O  ARG A  60           
SHEET    3   A 7 LEU A 129  SER A 135  1  O  ILE A 131   N  ASP A  50           
SHEET    4   A 7 ALA A  28  PRO A  43 -1  N  PHE A  38   O  TRP A 134           
SHEET    5   A 7 LEU A   6  HIS A  17 -1  N  GLY A  12   O  LEU A  33           
SHEET    6   A 7 SER A 378  HIS A 380 -1  O  SER A 378   N  SER A   9           
SHEET    7   A 7 VAL A 174  ASN A 175 -1  N  ASN A 175   O  ILE A 379           
SHEET    1   B 6 LYS A  59  ASP A  63  0                                        
SHEET    2   B 6 LYS A  48  SER A  52 -1  N  LEU A  51   O  ARG A  60           
SHEET    3   B 6 LEU A 129  SER A 135  1  O  ILE A 131   N  ASP A  50           
SHEET    4   B 6 ALA A  28  PRO A  43 -1  N  PHE A  38   O  TRP A 134           
SHEET    5   B 6 ALA A 213  TYR A 216 -1  O  LEU A 214   N  ALA A  30           
SHEET    6   B 6 ILE A 221  SER A 223 -1  O  SER A 222   N  ARG A 215           
SHEET    1   C 4 HIS A 328  LEU A 331  0                                        
SHEET    2   C 4 CYS A 339  LEU A 343 -1  O  ILE A 341   N  LYS A 330           
SHEET    3   C 4 LEU A 230  ASN A 236 -1  N  THR A 235   O  GLY A 340           
SHEET    4   C 4 ASP A 366  ILE A 372 -1  O  ILE A 372   N  LEU A 230           
SHEET    1   D 6 ILE B  58  ASP B  63  0                                        
SHEET    2   D 6 LYS B  48  LEU B  53 -1  N  LEU B  53   O  ILE B  58           
SHEET    3   D 6 LEU B 129  SER B 135  1  O  ILE B 131   N  ASP B  50           
SHEET    4   D 6 ALA B  28  PRO B  43 -1  N  ARG B  40   O  VAL B 132           
SHEET    5   D 6 ALA B 213  TYR B 216 -1  O  LEU B 214   N  ALA B  30           
SHEET    6   D 6 ILE B 221  SER B 223 -1  O  SER B 222   N  ARG B 215           
SHEET    1   E 6 ILE B  58  ASP B  63  0                                        
SHEET    2   E 6 LYS B  48  LEU B  53 -1  N  LEU B  53   O  ILE B  58           
SHEET    3   E 6 LEU B 129  SER B 135  1  O  ILE B 131   N  ASP B  50           
SHEET    4   E 6 ALA B  28  PRO B  43 -1  N  ARG B  40   O  VAL B 132           
SHEET    5   E 6 LEU B   6  HIS B  17 -1  N  LEU B   6   O  LEU B  41           
SHEET    6   E 6 SER B 378  ILE B 379 -1  O  SER B 378   N  SER B   9           
SHEET    1   F 4 SER B 329  LEU B 331  0                                        
SHEET    2   F 4 CYS B 339  LEU B 343 -1  O  ILE B 341   N  LYS B 330           
SHEET    3   F 4 LEU B 230  ASN B 236 -1  N  THR B 235   O  GLY B 340           
SHEET    4   F 4 ASP B 366  LEU B 368 -1  O  ASP B 366   N  ASN B 236           
SHEET    1   G 4 SER B 329  LEU B 331  0                                        
SHEET    2   G 4 CYS B 339  LEU B 343 -1  O  ILE B 341   N  LYS B 330           
SHEET    3   G 4 LEU B 230  ASN B 236 -1  N  THR B 235   O  GLY B 340           
SHEET    4   G 4 SER B 371  ILE B 372 -1  O  ILE B 372   N  LEU B 230           
SHEET    1   H 7 ILE C  58  TRP C  62  0                                        
SHEET    2   H 7 VAL C  49  LEU C  53 -1  N  LEU C  53   O  ILE C  58           
SHEET    3   H 7 LEU C 129  SER C 135  1  O  LEU C 129   N  ASP C  50           
SHEET    4   H 7 ALA C  28  PRO C  43 -1  N  ARG C  40   O  VAL C 132           
SHEET    5   H 7 LEU C   6  HIS C  17 -1  N  VAL C   8   O  LEU C  39           
SHEET    6   H 7 SER C 378  HIS C 380 -1  O  HIS C 380   N  LEU C   7           
SHEET    7   H 7 VAL C 174  ASN C 175 -1  N  ASN C 175   O  ILE C 379           
SHEET    1   I 6 ILE C  58  TRP C  62  0                                        
SHEET    2   I 6 VAL C  49  LEU C  53 -1  N  LEU C  53   O  ILE C  58           
SHEET    3   I 6 LEU C 129  SER C 135  1  O  LEU C 129   N  ASP C  50           
SHEET    4   I 6 ALA C  28  PRO C  43 -1  N  ARG C  40   O  VAL C 132           
SHEET    5   I 6 ALA C 213  TYR C 216 -1  O  TYR C 216   N  ALA C  28           
SHEET    6   I 6 ILE C 221  SER C 223 -1  O  SER C 222   N  ARG C 215           
SHEET    1   J 4 SER C 329  THR C 332  0                                        
SHEET    2   J 4 CYS C 339  LEU C 343 -1  O  ILE C 341   N  LYS C 330           
SHEET    3   J 4 LEU C 230  ASN C 236 -1  N  THR C 235   O  GLY C 340           
SHEET    4   J 4 ASP C 366  ILE C 372 -1  O  THR C 370   N  ILE C 232           
SHEET    1   K 5 LYS D  59  ASP D  63  0                                        
SHEET    2   K 5 LYS D  48  SER D  52 -1  N  LEU D  51   O  ARG D  60           
SHEET    3   K 5 SER D 128  SER D 135  1  O  ILE D 131   N  ASP D  50           
SHEET    4   K 5 ALA D  28  HIS D  44 -1  N  PHE D  38   O  TRP D 134           
SHEET    5   K 5 ALA D 213  TYR D 216 -1  O  LEU D 214   N  ALA D  30           
SHEET    1   L 6 LYS D  59  ASP D  63  0                                        
SHEET    2   L 6 LYS D  48  SER D  52 -1  N  LEU D  51   O  ARG D  60           
SHEET    3   L 6 SER D 128  SER D 135  1  O  ILE D 131   N  ASP D  50           
SHEET    4   L 6 ALA D  28  HIS D  44 -1  N  PHE D  38   O  TRP D 134           
SHEET    5   L 6 LEU D   6  HIS D  17 -1  N  ALA D  10   O  THR D  37           
SHEET    6   L 6 SER D 378  ILE D 379 -1  O  SER D 378   N  SER D   9           
SHEET    1   M 3 GLN D 231  ILE D 232  0                                        
SHEET    2   M 3 CYS D 339  LEU D 344 -1  O  LEU D 344   N  GLN D 231           
SHEET    3   M 3 SER D 329  LEU D 331 -1  N  LYS D 330   O  ILE D 341           
SHEET    1   N 4 GLN D 231  ILE D 232  0                                        
SHEET    2   N 4 CYS D 339  LEU D 344 -1  O  LEU D 344   N  GLN D 231           
SHEET    3   N 4 LEU D 234  ASN D 236 -1  N  THR D 235   O  GLY D 340           
SHEET    4   N 4 ASP D 366  LEU D 368 -1  O  ASP D 366   N  ASN D 236           
CRYST1  102.030   78.200  109.450  90.00 113.33  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009801  0.000000  0.004228        0.00000                         
SCALE2      0.000000  0.012788  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009950        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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