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Database: PDB
Entry: 4BGD
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Original site: 4BGD 
HEADER    TRANSCRIPTION                           25-MAR-13   4BGD              
TITLE     CRYSTAL STRUCTURE OF BRR2 IN COMPLEX WITH THE JAB1/MPN DOMAIN OF PRP8 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PRE-MRNA-SPLICING HELICASE BRR2;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 442-2163;                                         
COMPND   5 SYNONYM: PROTEIN SNU246;                                             
COMPND   6 EC: 3.6.4.13;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PRE-MRNA-SPLICING FACTOR 8;                                
COMPND  10 CHAIN: C;                                                            
COMPND  11 FRAGMENT: RESIDUES 2148-2395;                                        
COMPND  12 SYNONYM: PRP8, JAB1/MPN;                                             
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 STRAIN: S288C;                                                       
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  11 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  12 ORGANISM_TAXID: 4932;                                                
SOURCE  13 STRAIN: S288C;                                                       
SOURCE  14 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  15 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 4932                                        
KEYWDS    TRANSCRIPTION, SPLICEOSOME, RNA HELICASE, U5 SNRNP, RETINITIS         
KEYWDS   2 PIGMENTOSA                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.H.D.NGUYEN,J.LI,K.NAGAI                                             
REVDAT   3   14-AUG-13 4BGD    1       JRNL                                     
REVDAT   2   12-JUN-13 4BGD    1       JRNL                                     
REVDAT   1   29-MAY-13 4BGD    0                                                
JRNL        AUTH   T.H.D.NGUYEN,J.LI,W.P.GALEJ,H.OSHIKANE,A.J.NEWMAN,K.NAGAI    
JRNL        TITL   STRUCTURAL BASIS OF BRR2-PRP8 INTERACTIONS AND IMPLICATIONS  
JRNL        TITL 2 FOR U5 SNRNP BIOGENESIS AND THE SPLICEOSOME ACTIVE SITE      
JRNL        REF    STRUCTURE                     V.  21   910 2013              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   23727230                                                     
JRNL        DOI    10.1016/J.STR.2013.04.017                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 92.37                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.35                          
REMARK   3   NUMBER OF REFLECTIONS             : 60299                          
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 + TEST SET) : 0.21664                         
REMARK   3   R VALUE            (WORKING SET) : 0.21373                         
REMARK   3   FREE R VALUE                     : 0.26993                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3206                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.100                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.180                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4224                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.23                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.306                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 231                          
REMARK   3   BIN FREE R VALUE                    : 0.409                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15663                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 55                                      
REMARK   3   SOLVENT ATOMS            : 15                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 121.282                        
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.73                                                 
REMARK   3    B22 (A**2) : -7.84                                                
REMARK   3    B33 (A**2) : 2.11                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.436         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.347         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.956        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 16074 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 15378 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 21795 ; 1.477 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 35451 ; 0.798 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1954 ; 7.085 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   740 ;35.919 ;24.770       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2848 ;17.349 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    74 ;18.729 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2457 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 17993 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3646 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  7819 ; 8.549 ;11.874       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  7818 ; 8.548 ;11.874       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9769 ;12.739 ;17.808       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  8255 ; 8.782 ;12.469       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3   POSITIONS. U VALUES REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 4BGD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-APR-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-56282.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAY-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97950                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63788                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.10                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 92.20                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 6.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.2                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.80                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.0                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.88                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.40                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: PDB ENTRIES 3HIB AND 2OG4                            
REMARK 200                                                                      
REMARK 200 REMARK: THE TWO KNOWN FRAGMENTS COULD ALSO BE FOUND BY               
REMARK 200  MOLECULAR REPLACEMENT, BUT IT WAS NOT SUFFICIENT FOR                
REMARK 200  STRUCTURE DETERMINATION. THE STRUCTURE WAS SOLVED BY SIRAS.         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPESNA PH 7.5, 200 MM            
REMARK 280  MGCL2, 32-40% PEG400                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       53.82000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       90.20000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       89.32000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       90.20000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       53.82000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       89.32000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 83910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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     GLU A  1826                                                      
REMARK 465     ALA A  1827                                                      
REMARK 465     GLU A  1828                                                      
REMARK 465     VAL A  1829                                                      
REMARK 465     THR A  1830                                                      
REMARK 465     ALA A  1831                                                      
REMARK 465     GLU A  1832                                                      
REMARK 465     VAL A  1833                                                      
REMARK 465     ASN A  1834                                                      
REMARK 465     GLY A  1835                                                      
REMARK 465     GLY A  1836                                                      
REMARK 465     ASP A  1837                                                      
REMARK 465     ASP A  1838                                                      
REMARK 465     GLU A  1839                                                      
REMARK 465     ALA A  1840                                                      
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   NZ   LYS A   556     O    THR A   602              2.14            
REMARK 500   NH2  ARG A   699     O    ALA A   875              2.17            
REMARK 500   OD2B ASP A  1023     O    HOH A  3002              2.08            
REMARK 500   OD2B ASP A  1023     O    HOH A  3003              2.08            
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    TYR A 460      136.28   -170.46                                   
REMARK 500    PRO A 484      153.46    -41.61                                   
REMARK 500    GLN A 488      -36.40    -37.78                                   
REMARK 500    PRO A 492      -76.80    -60.16                                   
REMARK 500    ASP A 591      -50.89   -125.64                                   
REMARK 500    ILE A 599        1.71    -62.30                                   
REMARK 500    ASP A 600       25.92    -78.66                                   
REMARK 500    LEU A 622      -33.00    -37.07                                   
REMARK 500    LYS A 659     -121.58     53.31                                   
REMARK 500    GLN A 662      -10.15     68.83                                   
REMARK 500    CYS A 701       74.62     57.93                                   
REMARK 500    ASN A 765      -62.41   -128.19                                   
REMARK 500    ILE A 766       -7.08     68.54                                   
REMARK 500    PRO A 791     -156.64    -79.33                                   
REMARK 500    ASN A 839       70.08   -117.80                                   
REMARK 500    LYS A 848       96.54    -68.69                                   
REMARK 500    THR A 850       18.85     49.71                                   
REMARK 500    ASN A 921      -37.32    -38.90                                   
REMARK 500    SER A 951       57.19   -144.15                                   
REMARK 500    GLN A 965       45.95    -97.64                                   
REMARK 500    ASP A 994       58.82     73.25                                   
REMARK 500    THR A1164       -3.74     62.42                                   
REMARK 500    ARG A1184       12.16     81.80                                   
REMARK 500    THR A1212     -168.73   -116.51                                   
REMARK 500    ASP A1225       66.68   -115.63                                   
REMARK 500    SER A1300       72.71   -108.46                                   
REMARK 500    GLU A1344        1.38     55.57                                   
REMARK 500    ALA A1420        9.21   -157.07                                   
REMARK 500    ARG A1458       42.87   -102.00                                   
REMARK 500    GLU A1555      -38.30    -32.83                                   
REMARK 500    ALA A1604       35.52    -89.14                                   
REMARK 500    TRP A1607       98.17    -68.92                                   
REMARK 500    ASN A1611       12.99     81.22                                   
REMARK 500    CYS A1670        1.87    -69.54                                   
REMARK 500    ALA A1674       94.94    -67.56                                   
REMARK 500    HIS A1693       29.53     36.10                                   
REMARK 500    ASP A1714     -122.89     59.84                                   
REMARK 500    SER A1761       18.15     58.69                                   
REMARK 500    ASN A1785       66.22   -150.77                                   
REMARK 500    ARG A1936       40.14     33.35                                   
REMARK 500    ASN A1968       20.83    -69.61                                   
REMARK 500    SER A2056      118.30   -161.21                                   
REMARK 500    SER A2062       42.64   -105.47                                   
REMARK 500    PRO C2216       -8.51    -57.16                                   
REMARK 500    ASP C2249       14.91     53.32                                   
REMARK 500    SER C2326       44.09     38.12                                   
REMARK 500    ASN C2355      -21.23     90.25                                   
REMARK 500    TYR C2359       36.42    -95.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLN A 662        24.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3165  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A3009   O                                                      
REMARK 620 2 HOH A3011   O    92.8                                              
REMARK 620 3 HOH A3012   O    89.2  89.5                                        
REMARK 620 4 ADP A3164   O3B 102.4 164.4  87.2                                  
REMARK 620 5 HOH A3007   O   177.7  88.4  88.8  76.3                            
REMARK 620 6 HOH A3008   O    93.1  90.9 177.6  91.8  88.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A3164                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A3165                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE5 A3166                 
DBREF  4BGD A  442  2163  UNP    P32639   BRR2_YEAST     442   2163             
DBREF  4BGD C 2148  2395  UNP    P33334   PRP8_YEAST    2148   2395             
SEQRES   1 A 1722  THR VAL THR LYS VAL SER LEU PRO GLU GLY SER PHE LYS          
SEQRES   2 A 1722  ARG VAL LYS PRO GLN TYR ASP GLU ILE HIS ILE PRO ALA          
SEQRES   3 A 1722  PRO SER LYS PRO VAL ILE ASP TYR GLU LEU LYS GLU ILE          
SEQRES   4 A 1722  THR SER LEU PRO ASP TRP CYS GLN GLU ALA PHE PRO SER          
SEQRES   5 A 1722  SER GLU THR THR SER LEU ASN PRO ILE GLN SER LYS VAL          
SEQRES   6 A 1722  PHE HIS ALA ALA PHE GLU GLY ASP SER ASN MET LEU ILE          
SEQRES   7 A 1722  CYS ALA PRO THR GLY SER GLY LYS THR ASN ILE ALA LEU          
SEQRES   8 A 1722  LEU THR VAL LEU LYS ALA LEU SER HIS HIS TYR ASN PRO          
SEQRES   9 A 1722  LYS THR LYS LYS LEU ASN LEU SER ALA PHE LYS ILE VAL          
SEQRES  10 A 1722  TYR ILE ALA PRO LEU LYS ALA LEU VAL GLN GLU GLN VAL          
SEQRES  11 A 1722  ARG GLU PHE GLN ARG ARG LEU ALA PHE LEU GLY ILE LYS          
SEQRES  12 A 1722  VAL ALA GLU LEU THR GLY ASP SER ARG LEU SER ARG LYS          
SEQRES  13 A 1722  GLN ILE ASP GLU THR GLN VAL LEU VAL SER THR PRO GLU          
SEQRES  14 A 1722  LYS TRP ASP ILE THR THR ARG ASN SER ASN ASN LEU ALA          
SEQRES  15 A 1722  ILE VAL GLU LEU VAL ARG LEU LEU ILE ILE ASP GLU ILE          
SEQRES  16 A 1722  HIS LEU LEU HIS ASP ASP ARG GLY PRO VAL LEU GLU SER          
SEQRES  17 A 1722  ILE VAL ALA ARG THR PHE TRP ALA SER LYS TYR GLY GLN          
SEQRES  18 A 1722  GLU TYR PRO ARG ILE ILE GLY LEU SER ALA THR LEU PRO          
SEQRES  19 A 1722  ASN TYR GLU ASP VAL GLY ARG PHE LEU ARG VAL PRO LYS          
SEQRES  20 A 1722  GLU GLY LEU PHE TYR PHE ASP SER SER PHE ARG PRO CYS          
SEQRES  21 A 1722  PRO LEU SER GLN GLN PHE CYS GLY ILE LYS GLU ARG ASN          
SEQRES  22 A 1722  SER LEU LYS LYS LEU LYS ALA MET ASN ASP ALA CYS TYR          
SEQRES  23 A 1722  GLU LYS VAL LEU GLU SER ILE ASN GLU GLY ASN GLN ILE          
SEQRES  24 A 1722  ILE VAL PHE VAL HIS SER ARG LYS GLU THR SER ARG THR          
SEQRES  25 A 1722  ALA THR TRP LEU LYS ASN LYS PHE ALA GLU GLU ASN ILE          
SEQRES  26 A 1722  THR HIS LYS LEU THR LYS ASN ASP ALA GLY SER LYS GLN          
SEQRES  27 A 1722  ILE LEU LYS THR GLU ALA ALA ASN VAL LEU ASP PRO SER          
SEQRES  28 A 1722  LEU ARG LYS LEU ILE GLU SER GLY ILE GLY THR HIS HIS          
SEQRES  29 A 1722  ALA GLY LEU THR ARG SER ASP ARG SER LEU SER GLU ASP          
SEQRES  30 A 1722  LEU PHE ALA ASP GLY LEU LEU GLN VAL LEU VAL CYS THR          
SEQRES  31 A 1722  ALA THR LEU ALA TRP GLY VAL ASN LEU PRO ALA HIS THR          
SEQRES  32 A 1722  VAL ILE ILE LYS GLY THR ASP VAL TYR SER PRO GLU LYS          
SEQRES  33 A 1722  GLY SER TRP GLU GLN LEU SER PRO GLN ASP VAL LEU GLN          
SEQRES  34 A 1722  MET LEU GLY ARG ALA GLY ARG PRO ARG TYR ASP THR PHE          
SEQRES  35 A 1722  GLY GLU GLY ILE ILE ILE THR ASP GLN SER ASN VAL GLN          
SEQRES  36 A 1722  TYR TYR LEU SER VAL LEU ASN GLN GLN LEU PRO ILE GLU          
SEQRES  37 A 1722  SER GLN PHE VAL SER LYS LEU VAL ASP ASN LEU ASN ALA          
SEQRES  38 A 1722  GLU VAL VAL ALA GLY ASN ILE LYS CYS ARG ASN ASP ALA          
SEQRES  39 A 1722  VAL ASN TRP LEU ALA TYR THR TYR LEU TYR VAL ARG MET          
SEQRES  40 A 1722  LEU ALA SER PRO MET LEU TYR LYS VAL PRO ASP ILE SER          
SEQRES  41 A 1722  SER ASP GLY GLN LEU LYS LYS PHE ARG GLU SER LEU VAL          
SEQRES  42 A 1722  HIS SER ALA LEU CYS ILE LEU LYS GLU GLN GLU LEU VAL          
SEQRES  43 A 1722  LEU TYR ASP ALA GLU ASN ASP VAL ILE GLU ALA THR ASP          
SEQRES  44 A 1722  LEU GLY ASN ILE ALA SER SER PHE TYR ILE ASN HIS ALA          
SEQRES  45 A 1722  SER MET ASP VAL TYR ASN ARG GLU LEU ASP GLU HIS THR          
SEQRES  46 A 1722  THR GLN ILE ASP LEU PHE ARG ILE PHE SER MET SER GLU          
SEQRES  47 A 1722  GLU PHE LYS TYR VAL SER VAL ARG TYR GLU GLU LYS ARG          
SEQRES  48 A 1722  GLU LEU LYS GLN LEU LEU GLU LYS ALA PRO ILE PRO ILE          
SEQRES  49 A 1722  ARG GLU ASP ILE ASP ASP PRO LEU ALA LYS VAL ASN VAL          
SEQRES  50 A 1722  LEU LEU GLN SER TYR PHE SER GLN LEU LYS PHE GLU GLY          
SEQRES  51 A 1722  PHE ALA LEU ASN SER ASP ILE VAL PHE ILE HIS GLN ASN          
SEQRES  52 A 1722  ALA GLY ARG LEU LEU ARG ALA MET PHE GLU ILE CYS LEU          
SEQRES  53 A 1722  LYS ARG GLY TRP GLY HIS PRO THR ARG MET LEU LEU ASN          
SEQRES  54 A 1722  LEU CYS LYS SER ALA THR THR LYS MET TRP PRO THR ASN          
SEQRES  55 A 1722  CYS PRO LEU ARG GLN PHE LYS THR CYS PRO VAL GLU VAL          
SEQRES  56 A 1722  ILE LYS ARG LEU GLU ALA SER THR VAL PRO TRP GLY ASP          
SEQRES  57 A 1722  TYR LEU GLN LEU GLU THR PRO ALA GLU VAL GLY ARG ALA          
SEQRES  58 A 1722  ILE ARG SER GLU LYS TYR GLY LYS GLN VAL TYR ASP LEU          
SEQRES  59 A 1722  LEU LYS ARG PHE PRO LYS MET SER VAL THR CYS ASN ALA          
SEQRES  60 A 1722  GLN PRO ILE THR ARG SER VAL MET ARG PHE ASN ILE GLU          
SEQRES  61 A 1722  ILE ILE ALA ASP TRP ILE TRP ASP MET ASN VAL HIS GLY          
SEQRES  62 A 1722  SER LEU GLU PRO PHE LEU LEU MET LEU GLU ASP THR ASP          
SEQRES  63 A 1722  GLY ASP SER ILE LEU TYR TYR ASP VAL LEU PHE ILE THR          
SEQRES  64 A 1722  PRO ASP ILE VAL GLY HIS GLU PHE THR LEU SER PHE THR          
SEQRES  65 A 1722  TYR GLU LEU LYS GLN HIS ASN GLN ASN ASN LEU PRO PRO          
SEQRES  66 A 1722  ASN PHE PHE LEU THR LEU ILE SER GLU ASN TRP TRP HIS          
SEQRES  67 A 1722  SER GLU PHE GLU ILE PRO VAL SER PHE ASN GLY PHE LYS          
SEQRES  68 A 1722  LEU PRO LYS LYS PHE PRO PRO PRO THR PRO LEU LEU GLU          
SEQRES  69 A 1722  ASN ILE SER ILE SER THR SER GLU LEU GLY ASN ASP ASP          
SEQRES  70 A 1722  PHE SER GLU VAL PHE GLU PHE LYS THR PHE ASN LYS ILE          
SEQRES  71 A 1722  GLN SER GLN VAL PHE GLU SER LEU TYR ASN SER ASN ASP          
SEQRES  72 A 1722  SER VAL PHE VAL GLY SER GLY LYS GLY THR GLY LYS THR          
SEQRES  73 A 1722  ALA MET ALA GLU LEU ALA LEU LEU ASN HIS TRP ARG GLN          
SEQRES  74 A 1722  ASN LYS GLY ARG ALA VAL TYR ILE ASN PRO SER GLY GLU          
SEQRES  75 A 1722  LYS ILE ASP PHE LEU LEU SER ASP TRP ASN LYS ARG PHE          
SEQRES  76 A 1722  SER HIS LEU ALA GLY GLY LYS ILE ILE ASN LYS LEU GLY          
SEQRES  77 A 1722  ASN ASP PRO SER LEU ASN LEU LYS LEU LEU ALA LYS SER          
SEQRES  78 A 1722  HIS VAL LEU LEU ALA THR PRO VAL GLN PHE GLU LEU LEU          
SEQRES  79 A 1722  SER ARG ARG TRP ARG GLN ARG LYS ASN ILE GLN SER LEU          
SEQRES  80 A 1722  GLU LEU MET ILE TYR ASP ASP ALA HIS GLU ILE SER GLN          
SEQRES  81 A 1722  GLY VAL TYR GLY ALA VAL TYR GLU THR LEU ILE SER ARG          
SEQRES  82 A 1722  MET ILE PHE ILE ALA THR GLN LEU GLU LYS LYS ILE ARG          
SEQRES  83 A 1722  PHE VAL CYS LEU SER ASN CYS LEU ALA ASN ALA ARG ASP          
SEQRES  84 A 1722  PHE GLY GLU TRP ALA GLY MET THR LYS SER ASN ILE TYR          
SEQRES  85 A 1722  ASN PHE SER PRO SER GLU ARG ILE GLU PRO LEU GLU ILE          
SEQRES  86 A 1722  ASN ILE GLN SER PHE LYS ASP VAL GLU HIS ILE SER PHE          
SEQRES  87 A 1722  ASN PHE SER MET LEU GLN MET ALA PHE GLU ALA SER ALA          
SEQRES  88 A 1722  ALA ALA ALA GLY ASN ARG ASN SER SER SER VAL PHE LEU          
SEQRES  89 A 1722  PRO SER ARG LYS ASP CYS MET GLU VAL ALA SER ALA PHE          
SEQRES  90 A 1722  MET LYS PHE SER LYS ALA ILE GLU TRP ASP MET LEU ASN          
SEQRES  91 A 1722  VAL GLU GLU GLU GLN ILE VAL PRO TYR ILE GLU LYS LEU          
SEQRES  92 A 1722  THR ASP GLY HIS LEU ARG ALA PRO LEU LYS HIS GLY VAL          
SEQRES  93 A 1722  GLY ILE LEU TYR LYS GLY MET ALA SER ASN ASP GLU ARG          
SEQRES  94 A 1722  ILE VAL LYS ARG LEU TYR GLU TYR GLY ALA VAL SER VAL          
SEQRES  95 A 1722  LEU LEU ILE SER LYS ASP CYS SER ALA PHE ALA CYS LYS          
SEQRES  96 A 1722  THR ASP GLU VAL ILE ILE LEU GLY THR ASN LEU TYR ASP          
SEQRES  97 A 1722  GLY ALA GLU HIS LYS TYR MET PRO TYR THR ILE ASN GLU          
SEQRES  98 A 1722  LEU LEU GLU MET VAL GLY LEU ALA SER GLY ASN ASP SER          
SEQRES  99 A 1722  MET ALA GLY LYS VAL LEU ILE LEU THR SER HIS ASN MET          
SEQRES 100 A 1722  LYS ALA TYR TYR LYS LYS PHE LEU ILE GLU PRO LEU PRO          
SEQRES 101 A 1722  THR GLU SER TYR LEU GLN TYR ILE ILE HIS ASP THR LEU          
SEQRES 102 A 1722  ASN ASN GLU ILE ALA ASN SER ILE ILE GLN SER LYS GLN          
SEQRES 103 A 1722  ASP CYS VAL ASP TRP PHE THR TYR SER TYR PHE TYR ARG          
SEQRES 104 A 1722  ARG ILE HIS VAL ASN PRO SER TYR TYR GLY VAL ARG ASP          
SEQRES 105 A 1722  THR SER PRO HIS GLY ILE SER VAL PHE LEU SER ASN LEU          
SEQRES 106 A 1722  VAL GLU THR CYS LEU ASN ASP LEU VAL GLU SER SER PHE          
SEQRES 107 A 1722  ILE GLU ILE ASP ASP THR GLU ALA GLU VAL THR ALA GLU          
SEQRES 108 A 1722  VAL ASN GLY GLY ASP ASP GLU ALA THR GLU ILE ILE SER          
SEQRES 109 A 1722  THR LEU SER ASN GLY LEU ILE ALA SER HIS TYR GLY VAL          
SEQRES 110 A 1722  SER PHE PHE THR ILE GLN SER PHE VAL SER SER LEU SER          
SEQRES 111 A 1722  ASN THR SER THR LEU LYS ASN MET LEU TYR VAL LEU SER          
SEQRES 112 A 1722  THR ALA VAL GLU PHE GLU SER VAL PRO LEU ARG LYS GLY          
SEQRES 113 A 1722  ASP ARG ALA LEU LEU VAL LYS LEU SER LYS ARG LEU PRO          
SEQRES 114 A 1722  LEU ARG PHE PRO GLU HIS THR SER SER GLY SER VAL SER          
SEQRES 115 A 1722  PHE LYS VAL PHE LEU LEU LEU GLN ALA TYR PHE SER ARG          
SEQRES 116 A 1722  LEU GLU LEU PRO VAL ASP PHE GLN ASN ASP LEU LYS ASP          
SEQRES 117 A 1722  ILE LEU GLU LYS VAL VAL PRO LEU ILE ASN VAL VAL VAL          
SEQRES 118 A 1722  ASP ILE LEU SER ALA ASN GLY TYR LEU ASN ALA THR THR          
SEQRES 119 A 1722  ALA MET ASP LEU ALA GLN MET LEU ILE GLN GLY VAL TRP          
SEQRES 120 A 1722  ASP VAL ASP ASN PRO LEU ARG GLN ILE PRO HIS PHE ASN          
SEQRES 121 A 1722  ASN LYS ILE LEU GLU LYS CYS LYS GLU ILE ASN VAL GLU          
SEQRES 122 A 1722  THR VAL TYR ASP ILE MET ALA LEU GLU ASP GLU GLU ARG          
SEQRES 123 A 1722  ASP GLU ILE LEU THR LEU THR ASP SER GLN LEU ALA GLN          
SEQRES 124 A 1722  VAL ALA ALA PHE VAL ASN ASN TYR PRO ASN VAL GLU LEU          
SEQRES 125 A 1722  THR TYR SER LEU ASN ASN SER ASP SER LEU ILE SER GLY          
SEQRES 126 A 1722  VAL LYS GLN LYS ILE THR ILE GLN LEU THR ARG ASP VAL          
SEQRES 127 A 1722  GLU PRO GLU ASN LEU GLN VAL THR SER GLU LYS TYR PRO          
SEQRES 128 A 1722  PHE ASP LYS LEU GLU SER TRP TRP LEU VAL LEU GLY GLU          
SEQRES 129 A 1722  VAL SER LYS LYS GLU LEU TYR ALA ILE LYS LYS VAL THR          
SEQRES 130 A 1722  LEU ASN LYS GLU THR GLN GLN TYR GLU LEU GLU PHE ASP          
SEQRES 131 A 1722  THR PRO THR SER GLY LYS HIS ASN LEU THR ILE TRP CYS          
SEQRES 132 A 1722  VAL CYS ASP SER TYR LEU ASP ALA ASP LYS GLU LEU SER          
SEQRES 133 A 1722  PHE GLU ILE ASN VAL LYS                                      
SEQRES   1 C  248  SER LYS ASN GLU TRP ARG LYS SER ALA ILE ALA ASN THR          
SEQRES   2 C  248  LEU LEU TYR LEU ARG LEU LYS ASN ILE TYR VAL SER ALA          
SEQRES   3 C  248  ASP ASP PHE VAL GLU GLU GLN ASN VAL TYR VAL LEU PRO          
SEQRES   4 C  248  LYS ASN LEU LEU LYS LYS PHE ILE GLU ILE SER ASP VAL          
SEQRES   5 C  248  LYS ILE GLN VAL ALA ALA PHE ILE TYR GLY MET SER ALA          
SEQRES   6 C  248  LYS ASP HIS PRO LYS VAL LYS GLU ILE LYS THR VAL VAL          
SEQRES   7 C  248  LEU VAL PRO GLN LEU GLY HIS VAL GLY SER VAL GLN ILE          
SEQRES   8 C  248  SER ASN ILE PRO ASP ILE GLY ASP LEU PRO ASP THR GLU          
SEQRES   9 C  248  GLY LEU GLU LEU LEU GLY TRP ILE HIS THR GLN THR GLU          
SEQRES  10 C  248  GLU LEU LYS PHE MET ALA ALA SER GLU VAL ALA THR HIS          
SEQRES  11 C  248  SER LYS LEU PHE ALA ASP LYS LYS ARG ASP CYS ILE ASP          
SEQRES  12 C  248  ILE SER ILE PHE SER THR PRO GLY SER VAL SER LEU SER          
SEQRES  13 C  248  ALA TYR ASN LEU THR ASP GLU GLY TYR GLN TRP GLY GLU          
SEQRES  14 C  248  GLU ASN LYS ASP ILE MET ASN VAL LEU SER GLU GLY PHE          
SEQRES  15 C  248  GLU PRO THR PHE SER THR HIS ALA GLN LEU LEU LEU SER          
SEQRES  16 C  248  ASP ARG ILE THR GLY ASN PHE ILE ILE PRO SER GLY ASN          
SEQRES  17 C  248  VAL TRP ASN TYR THR PHE MET GLY THR ALA PHE ASN GLN          
SEQRES  18 C  248  GLU GLY ASP TYR ASN PHE LYS TYR GLY ILE PRO LEU GLU          
SEQRES  19 C  248  PHE TYR ASN GLU MET HIS ARG PRO VAL HIS PHE LEU GLN          
SEQRES  20 C  248  PHE                                                          
HET    ADP  A3164      27                                                       
HET     MG  A3165       1                                                       
HET    PE5  A3166      27                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     PE5 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL                       
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     PE5 2-(2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]                    
HETSYN   2 PE5  -ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-                       
HETSYN   3 PE5  ETHANOL, POLYETHYLENE GLYCOL PEG400                             
FORMUL   3  ADP    C10 H15 N5 O10 P2                                            
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  PE5    C18 H38 O9                                                   
FORMUL   6  HOH   *15(H2 O)                                                     
HELIX    1   1 ILE A  480  LEU A  483  5                                   4    
HELIX    2   2 TRP A  486  PHE A  491  5                                   6    
HELIX    3   3 ASN A  500  GLU A  512  1                                  13    
HELIX    4   4 GLY A  526  HIS A  541  1                                  16    
HELIX    5   5 LEU A  563  ALA A  579  1                                  17    
HELIX    6   6 ARG A  593  LYS A  597  5                                   5    
HELIX    7   7 THR A  608  ASN A  618  1                                  11    
HELIX    8   8 ASN A  621  GLU A  626  1                                   6    
HELIX    9   9 GLU A  635  ASP A  641  5                                   7    
HELIX   10  10 GLY A  644  ALA A  657  1                                  14    
HELIX   11  11 SER A  658  GLN A  662  5                                   5    
HELIX   12  12 ASN A  676  LEU A  684  1                                   9    
HELIX   13  13 PRO A  687  GLU A  689  5                                   3    
HELIX   14  14 ASP A  695  ARG A  699  5                                   5    
HELIX   15  15 ASN A  714  GLU A  736  1                                  23    
HELIX   16  16 SER A  746  ASN A  765  1                                  20    
HELIX   17  17 ILE A  766  THR A  771  1                                   6    
HELIX   18  18 SER A  777  VAL A  788  1                                  12    
HELIX   19  19 SER A  792  SER A  799  1                                   8    
HELIX   20  20 THR A  809  ASP A  822  1                                  14    
HELIX   21  21 ALA A  832  VAL A  838  1                                   7    
HELIX   22  22 SER A  864  LEU A  872  1                                   9    
HELIX   23  23 GLN A  892  ASN A  903  1                                  12    
HELIX   24  24 LYS A  915  ALA A  926  1                                  12    
HELIX   25  25 CYS A  931  LEU A  939  1                                   9    
HELIX   26  26 THR A  942  SER A  951  1                                  10    
HELIX   27  27 ASP A  959  GLY A  964  1                                   6    
HELIX   28  28 LEU A  966  GLN A  984  1                                  19    
HELIX   29  29 THR A  999  PHE A 1008  1                                  10    
HELIX   30  30 ASN A 1011  LEU A 1022  1                                  12    
HELIX   31  31 THR A 1027  MET A 1037  1                                  11    
HELIX   32  32 SER A 1038  LYS A 1042  5                                   5    
HELIX   33  33 GLU A 1050  LYS A 1060  1                                  11    
HELIX   34  34 ASP A 1071  GLN A 1086  1                                  16    
HELIX   35  35 GLY A 1091  GLY A 1120  1                                  30    
HELIX   36  36 TRP A 1121  THR A 1137  1                                  17    
HELIX   37  37 CYS A 1144  GLN A 1148  5                                   5    
HELIX   38  38 PRO A 1153  SER A 1163  1                                  11    
HELIX   39  39 PRO A 1166  LEU A 1173  1                                   8    
HELIX   40  40 THR A 1175  ARG A 1184  1                                  10    
HELIX   41  41 SER A 1185  ARG A 1198  1                                  14    
HELIX   42  42 ASP A 1229  GLY A 1234  1                                   6    
HELIX   43  43 LYS A 1277  ASN A 1283  1                                   7    
HELIX   44  44 THR A 1331  LEU A 1334  5                                   4    
HELIX   45  45 ASN A 1336  GLU A 1344  1                                   9    
HELIX   46  46 ASN A 1349  ASN A 1361  1                                  13    
HELIX   47  47 GLY A 1375  ARG A 1389  1                                  15    
HELIX   48  48 SER A 1401  SER A 1417  1                                  17    
HELIX   49  49 ASP A 1431  SER A 1442  1                                  12    
HELIX   50  50 THR A 1448  ARG A 1457  1                                  10    
HELIX   51  51 ARG A 1462  SER A 1467  1                                   6    
HELIX   52  52 ASP A 1475  GLN A 1481  5                                   7    
HELIX   53  53 GLY A 1482  GLU A 1503  1                                  22    
HELIX   54  54 ASN A 1517  ALA A 1525  1                                   9    
HELIX   55  55 THR A 1528  SER A 1530  5                                   3    
HELIX   56  56 SER A 1536  ARG A 1540  5                                   5    
HELIX   57  57 ASN A 1560  ASN A 1577  1                                  18    
HELIX   58  58 SER A 1587  ALA A 1604  1                                  18    
HELIX   59  59 GLN A 1616  GLU A 1622  1                                   7    
HELIX   60  60 ASP A 1626  HIS A 1628  5                                   3    
HELIX   61  61 LEU A 1629  LYS A 1634  1                                   6    
HELIX   62  62 ALA A 1645  GLY A 1659  1                                  15    
HELIX   63  63 ASP A 1669  PHE A 1673  5                                   5    
HELIX   64  64 THR A 1699  GLY A 1708  1                                  10    
HELIX   65  65 SER A 1725  LEU A 1736  1                                  12    
HELIX   66  66 TYR A 1745  TYR A 1748  5                                   4    
HELIX   67  67 ILE A 1749  ASN A 1760  1                                  12    
HELIX   68  68 LYS A 1766  TYR A 1775  1                                  10    
HELIX   69  69 SER A 1776  ASN A 1785  1                                  10    
HELIX   70  70 ASN A 1785  GLY A 1790  1                                   6    
HELIX   71  71 SER A 1795  SER A 1817  1                                  23    
HELIX   72  72 LEU A 1847  GLY A 1857  1                                  11    
HELIX   73  73 SER A 1859  LEU A 1870  1                                  12    
HELIX   74  74 THR A 1875  THR A 1885  1                                  11    
HELIX   75  75 ALA A 1886  VAL A 1892  5                                   7    
HELIX   76  76 GLY A 1897  LEU A 1909  1                                  13    
HELIX   77  77 SER A 1921  SER A 1935  1                                  15    
HELIX   78  78 PRO A 1940  ASN A 1968  1                                  29    
HELIX   79  79 ASN A 1972  GLY A 1986  1                                  15    
HELIX   80  80 ASN A 1992  ILE A 1997  5                                   6    
HELIX   81  81 ASN A 2001  ILE A 2011  1                                  11    
HELIX   82  82 THR A 2015  LEU A 2022  1                                   8    
HELIX   83  83 GLU A 2023  LEU A 2031  1                                   9    
HELIX   84  84 THR A 2034  TYR A 2048  1                                  15    
HELIX   85  85 ASN C 2150  ASN C 2159  1                                  10    
HELIX   86  86 THR C 2160  LYS C 2167  5                                   8    
HELIX   87  87 LYS C 2187  ILE C 2196  1                                  10    
HELIX   88  88 ALA C 2270  ALA C 2282  1                                  13    
HELIX   89  89 THR C 2308  ASN C 2318  1                                  11    
HELIX   90  90 GLU C 2330  THR C 2332  5                                   3    
HELIX   91  91 ASN C 2384  PRO C 2389  5                                   6    
HELIX   92  92 VAL C 2390  PHE C 2395  1                                   6    
SHEET    1  AA 8 PHE A 453  VAL A 456  0                                        
SHEET    2  AA 8 TYR A 460  ILE A 465 -1  O  GLU A 462   N  ARG A 455           
SHEET    3  AA 8 LEU A 703  ILE A 710 -1  O  GLN A 705   N  ILE A 465           
SHEET    4  AA 8 GLY A 884  ASP A 891  1  O  GLY A 884   N  SER A 704           
SHEET    5  AA 8 THR A 844  LYS A 848  1  O  VAL A 845   N  ILE A 887           
SHEET    6  AA 8 ILE A 740  PHE A 743  1  O  ILE A 741   N  ILE A 846           
SHEET    7  AA 8 VAL A 827  CYS A 830  1  O  LEU A 828   N  VAL A 742           
SHEET    8  AA 8 ILE A 801  HIS A 804  1  O  GLY A 802   N  VAL A 829           
SHEET    1  AB 7 VAL A 585  GLU A 587  0                                        
SHEET    2  AB 7 VAL A 604  SER A 607  1  O  VAL A 604   N  ALA A 586           
SHEET    3  AB 7 LYS A 556  ILE A 560  1  O  ILE A 557   N  LEU A 605           
SHEET    4  AB 7 VAL A 628  ILE A 633  1  N  ARG A 629   O  LYS A 556           
SHEET    5  AB 7 ARG A 666  ALA A 672  1  O  ARG A 666   N  LEU A 631           
SHEET    6  AB 7 MET A 517  ALA A 521  1  O  MET A 517   N  GLY A 669           
SHEET    7  AB 7 LEU A 691  TYR A 693  1  O  PHE A 692   N  CYS A 520           
SHEET    1  AC 2 ASP A 851  SER A 854  0                                        
SHEET    2  AC 2 SER A 859  GLN A 862 -1  O  SER A 859   N  SER A 854           
SHEET    1  AD 2 VAL A 987  ASP A 990  0                                        
SHEET    2  AD 2 VAL A 995  ALA A 998 -1  O  VAL A 995   N  ASP A 990           
SHEET    1  AE 3 MET A1202  PRO A1210  0                                        
SHEET    2  AE 3 VAL A1215  ALA A1224 -1  O  ARG A1217   N  GLN A1209           
SHEET    3  AE 3 GLU A1267  GLU A1275 -1  O  PHE A1268   N  ILE A1222           
SHEET    1  AF 4 ILE A1251  ILE A1259  0                                        
SHEET    2  AF 4 GLU A1237  GLU A1244 -1  O  GLU A1237   N  ILE A1259           
SHEET    3  AF 4 ASN A1287  SER A1294 -1  O  PHE A1289   N  GLU A1244           
SHEET    4  AF 4 GLU A1301  SER A1307 -1  O  PHE A1302   N  LEU A1292           
SHEET    1  AG 7 ILE A1424  ASN A1426  0                                        
SHEET    2  AG 7 VAL A1444  ALA A1447  1  O  VAL A1444   N  ILE A1425           
SHEET    3  AG 7 ALA A1395  ILE A1398  1  O  ALA A1395   N  LEU A1445           
SHEET    4  AG 7 LEU A1470  TYR A1473  1  O  LEU A1470   N  VAL A1396           
SHEET    5  AG 7 ARG A1507  SER A1512  1  O  ARG A1507   N  MET A1471           
SHEET    6  AG 7 VAL A1366  GLY A1369  1  O  VAL A1366   N  CYS A1510           
SHEET    7  AG 7 ILE A1532  ASN A1534  1  O  TYR A1533   N  GLY A1369           
SHEET    1  AH 6 LEU A1544  GLN A1549  0                                        
SHEET    2  AH 6 GLY A1718  LEU A1723  1  O  GLY A1718   N  GLU A1545           
SHEET    3  AH 6 GLU A1679  LEU A1683  1  O  VAL A1680   N  LEU A1721           
SHEET    4  AH 6 SER A1581  LEU A1585  1  O  SER A1582   N  ILE A1681           
SHEET    5  AH 6 VAL A1663  SER A1667  1  O  LEU A1664   N  VAL A1583           
SHEET    6  AH 6 VAL A1637  LEU A1640  1  O  GLY A1638   N  LEU A1665           
SHEET    1  AI 2 ASN A1686  ASP A1689  0                                        
SHEET    2  AI 2 LYS A1694  PRO A1697 -1  O  LYS A1694   N  ASP A1689           
SHEET    1  AJ 2 ILE A1820  ASP A1823  0                                        
SHEET    2  AJ 2 ILE A1843  THR A1846 -1  O  ILE A1843   N  ASP A1823           
SHEET    1  AK 3 GLU A2052  LEU A2057  0                                        
SHEET    2  AK 3 LYS A2068  THR A2076 -1  O  THR A2072   N  SER A2056           
SHEET    3  AK 3 THR A2123  ASP A2131 -1  O  GLN A2124   N  LEU A2075           
SHEET    1  AL 4 GLU A2110  VAL A2117  0                                        
SHEET    2  AL 4 TRP A2099  GLU A2105 -1  O  TRP A2099   N  VAL A2117           
SHEET    3  AL 4 GLY A2136  CYS A2146 -1  O  THR A2141   N  GLY A2104           
SHEET    4  AL 4 LYS A2154  VAL A2162 -1  O  LYS A2154   N  CYS A2144           
SHEET    1  CA 2 ILE C2169  VAL C2171  0                                        
SHEET    2  CA 2 SER C2299  LEU C2307  1  O  VAL C2300   N  TYR C2170           
SHEET    1  CB 2 SER C2334  HIS C2336  0                                        
SHEET    2  CB 2 SER C2299  LEU C2307  1  O  ASN C2306   N  THR C2335           
SHEET    1  CC 5 GLN C2338  SER C2342  0                                        
SHEET    2  CC 5 VAL C2182  PRO C2186  1  O  TYR C2183   N  LEU C2340           
SHEET    3  CC 5 VAL C2218  LEU C2226  1  O  LYS C2219   N  VAL C2184           
SHEET    4  CC 5 ASN C2348  PRO C2352 -1  O  ASN C2348   N  VAL C2224           
SHEET    5  CC 5 PHE C2374  TYR C2376  1  O  LYS C2375   N  ILE C2351           
SHEET    1  CD 8 GLN C2338  SER C2342  0                                        
SHEET    2  CD 8 VAL C2182  PRO C2186  1  O  TYR C2183   N  LEU C2340           
SHEET    3  CD 8 VAL C2218  LEU C2226  1  O  LYS C2219   N  VAL C2184           
SHEET    4  CD 8 ALA C2204  SER C2211 -1  O  PHE C2206   N  VAL C2225           
SHEET    5  CD 8 GLU C2254  GLN C2262 -1  O  GLU C2254   N  GLY C2209           
SHEET    6  CD 8 ILE C2289  THR C2296  1  O  ILE C2289   N  TRP C2258           
SHEET    7  CD 8 SER C2299  LEU C2307 -1  O  SER C2299   N  THR C2296           
SHEET    8  CD 8 SER C2334  HIS C2336  1  O  THR C2335   N  ASN C2306           
SHEET    1  CE 8 GLN C2338  SER C2342  0                                        
SHEET    2  CE 8 VAL C2182  PRO C2186  1  O  TYR C2183   N  LEU C2340           
SHEET    3  CE 8 VAL C2218  LEU C2226  1  O  LYS C2219   N  VAL C2184           
SHEET    4  CE 8 ALA C2204  SER C2211 -1  O  PHE C2206   N  VAL C2225           
SHEET    5  CE 8 GLU C2254  GLN C2262 -1  O  GLU C2254   N  GLY C2209           
SHEET    6  CE 8 ILE C2289  THR C2296  1  O  ILE C2289   N  TRP C2258           
SHEET    7  CE 8 SER C2299  LEU C2307 -1  O  SER C2299   N  THR C2296           
SHEET    8  CE 8 ILE C2169  VAL C2171  1  O  TYR C2170   N  LEU C2302           
SHEET    1  CF 2 GLN C2229  HIS C2232  0                                        
SHEET    2  CF 2 SER C2235  ILE C2238 -1  O  SER C2235   N  HIS C2232           
LINK        MG    MG A3165                 O   HOH A3009     1555   1555  2.17  
LINK        MG    MG A3165                 O   HOH A3011     1555   1555  2.17  
LINK        MG    MG A3165                 O   HOH A3012     1555   1555  2.16  
LINK        MG    MG A3165                 O3B ADP A3164     1555   1555  2.42  
LINK        MG    MG A3165                 O   HOH A3007     1555   1555  2.16  
LINK        MG    MG A3165                 O   HOH A3008     1555   1555  2.16  
SITE     1 AC1 15 PHE A1345  THR A1347  PHE A1348  ASN A1349                    
SITE     2 AC1 15 GLN A1352  GLY A1371  LYS A1372  GLY A1373                    
SITE     3 AC1 15 THR A1374  GLY A1375  LYS A1376  THR A1377                    
SITE     4 AC1 15 HOH A3007  HOH A3009   MG A3165                               
SITE     1 AC2  6 HOH A3007  HOH A3008  HOH A3009  HOH A3011                    
SITE     2 AC2  6 HOH A3012  ADP A3164                                          
SITE     1 AC3  5 ASP A 474  TYR A 677  LEU A 691  PHE A 692                    
SITE     2 AC3  5 TYR A 693                                                     
CRYST1  107.640  178.640  180.400  90.00  90.00  90.00 P 21 21 21    4          
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      0.009290  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005598  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005543        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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