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Database: PDB
Entry: 5DCA
LinkDB: 5DCA
Original site: 5DCA 
HEADER    HYDROLASE                               23-AUG-15   5DCA              
TITLE     CRYSTAL STRUCTURE OF YEAST FULL LENGTH BRR2 IN COMPLEX WITH PRP8 JAB1 
TITLE    2 DOMAIN                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PRE-MRNA-SPLICING HELICASE BRR2;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PROTEIN SNU246;                                             
COMPND   5 EC: 3.6.4.13;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PRE-MRNA-SPLICING FACTOR 8;                                
COMPND   9 CHAIN: J;                                                            
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE   3 S288C);                                                              
SOURCE   4 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   5 ORGANISM_TAXID: 559292;                                              
SOURCE   6 GENE: BRR2, RSS1, SNU246, YER172C, SYGP-ORF66;                       
SOURCE   7 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   8 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  12 S288C);                                                              
SOURCE  13 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  14 ORGANISM_TAXID: 559292;                                              
SOURCE  15 GENE: PRP8, DBF3, DNA39, RNA8, SLT21, USA2, YHR165C;                 
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN COMPLEX, HELICASE, RNP REMODELING, SPLICEOSOME ACTIVATION,    
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.ABSMEIER,J.WOLLENHAUPT,K.F.SANTOS,M.C.WAHL                          
REVDAT   3   07-MAR-18 5DCA    1       REMARK                                   
REVDAT   2   30-DEC-15 5DCA    1       JRNL                                     
REVDAT   1   16-DEC-15 5DCA    0                                                
JRNL        AUTH   E.ABSMEIER,J.WOLLENHAUPT,S.MOZAFFARI-JOVIN,C.BECKE,C.T.LEE,  
JRNL        AUTH 2 M.PREUSSNER,F.HEYD,H.URLAUB,R.LUHRMANN,K.F.SANTOS,M.C.WAHL   
JRNL        TITL   THE LARGE N-TERMINAL REGION OF THE BRR2 RNA HELICASE GUIDES  
JRNL        TITL 2 PRODUCTIVE SPLICEOSOME ACTIVATION.                           
JRNL        REF    GENES DEV.                    V.  29  2576 2015              
JRNL        REFN                   ISSN 0890-9369                               
JRNL        PMID   26637280                                                     
JRNL        DOI    10.1101/GAD.271528.115                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 81271                          
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4257                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5472                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.15                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 276                          
REMARK   3   BIN FREE R VALUE                    : 0.4550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 17651                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 191                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 101.2                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.03000                                              
REMARK   3    B22 (A**2) : -4.14000                                             
REMARK   3    B33 (A**2) : 2.10000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.777         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.342         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.359         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.310        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 18020 ; 0.006 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 17309 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 24414 ; 0.994 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 39920 ; 0.706 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2191 ; 5.690 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   841 ;35.717 ;24.994       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3253 ;15.634 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    82 ;17.691 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2766 ; 0.056 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 20188 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  4042 ; 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):  8788 ; 3.763 ;10.097       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  8787 ; 3.759 ;10.096       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10971 ; 6.350 ;15.137       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 10972 ; 6.351 ;15.138       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  9232 ; 3.355 ;10.333       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  9233 ; 3.355 ;10.334       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 13444 ; 5.871 ;15.370       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 20528 ;10.000 ;79.200       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 20514 ; 9.998 ;79.215       
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                                                           
REMARK   4                                                                      
REMARK   4 5DCA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212998.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-AUG-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III, EMBL C/O DESY           
REMARK 200  BEAMLINE                       : P14 (MX2)                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 85520                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 4BGD                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES-NAOH, PH 6.5, 9 % (W/V) PEG    
REMARK 280  3350, 0.2 M MGCL2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  291K                                                                
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       53.92500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       90.55500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       89.42500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       90.55500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       53.92500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       89.42500            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 99230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, J                                  
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 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    MET A  1609     O    HOH A  2201              2.15            
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    LEU A 131      -70.69    -75.77                                   
REMARK 500    LYS A 152      105.71    -57.80                                   
REMARK 500    ASN A 154      -20.70     74.05                                   
REMARK 500    ILE A 162      -40.54   -145.70                                   
REMARK 500    GLU A 163      -77.91    -82.95                                   
REMARK 500    GLU A 172     -103.06     83.19                                   
REMARK 500    ILE A 265       87.50     65.53                                   
REMARK 500    ILE A 270      106.03     19.86                                   
REMARK 500    ASP A 274     -166.55     59.50                                   
REMARK 500    SER A 275     -165.07     61.85                                   
REMARK 500    LYS A 276     -155.82    -81.75                                   
REMARK 500    GLU A 281      -63.12     64.09                                   
REMARK 500    SER A 282     -146.92   -134.86                                   
REMARK 500    VAL A 283      122.49     78.79                                   
REMARK 500    PHE A 291       56.93    -99.89                                   
REMARK 500    ILE A 320       68.41   -101.72                                   
REMARK 500    GLU A 321      -62.93    175.13                                   
REMARK 500    LYS A 339      -78.61     82.44                                   
REMARK 500    ARG A 361     -115.98     55.62                                   
REMARK 500    LYS A 364      -68.71   -148.72                                   
REMARK 500    GLU A 367      -76.24     68.96                                   
REMARK 500    ALA A 422       53.22     83.46                                   
REMARK 500    ASP A 435      156.06     70.73                                   
REMARK 500    GLU A 436      173.27     73.55                                   
REMARK 500    VAL A 443       71.53    -62.50                                   
REMARK 500    LYS A 445      143.41     71.09                                   
REMARK 500    THR A 496      -62.55   -104.04                                   
REMARK 500    SER A 498      149.86    125.20                                   
REMARK 500    ASP A 591       77.75    -67.66                                   
REMARK 500    SER A 592       17.15     82.72                                   
REMARK 500    SER A 595       33.24    -91.23                                   
REMARK 500    GLU A 764      -66.22   -137.52                                   
REMARK 500    THR A 767      -62.33     34.64                                   
REMARK 500    ARG A 932      -36.57    -38.81                                   
REMARK 500    SER A 951       59.11   -147.34                                   
REMARK 500    ASP A 994       61.32     61.27                                   
REMARK 500    PRO A1064      139.11    -39.14                                   
REMARK 500    LYS A1190      -41.90     84.97                                   
REMARK 500    ASP A1225       78.12   -105.34                                   
REMARK 500    ASP A1245     -178.93    -66.97                                   
REMARK 500    ASN A1336      132.54   -173.01                                   
REMARK 500    LYS A1392      -73.66    -66.23                                   
REMARK 500    ALA A1420      -12.44     93.40                                   
REMARK 500    ASN A1430      -61.32     52.20                                   
REMARK 500    ARG A1458       30.35    -92.81                                   
REMARK 500    GLU A1478        3.46    -69.83                                   
REMARK 500    GLU A1606       38.73    -93.76                                   
REMARK 500    MET A1609      157.61    167.94                                   
REMARK 500    ASN A1611        1.43     96.21                                   
REMARK 500    MET A1644      142.32     62.29                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      63 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5DCA A  113  2163  UNP    P32639   BRR2_YEAST     113   2163             
DBREF  5DCA J 2148  2398  UNP    P33334   PRP8_YEAST    2148   2398             
SEQADV 5DCA     A       UNP  P32639    THR   193 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASP   194 DELETION                       
SEQADV 5DCA     A       UNP  P32639    TYR   195 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLU   196 DELETION                       
SEQADV 5DCA     A       UNP  P32639    THR   197 DELETION                       
SEQADV 5DCA     A       UNP  P32639    HIS   198 DELETION                       
SEQADV 5DCA     A       UNP  P32639    PRO   199 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASP   200 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASN   201 DELETION                       
SEQADV 5DCA     A       UNP  P32639    SER   202 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASN   203 DELETION                       
SEQADV 5DCA     A       UNP  P32639    LYS   204 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLN   205 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ALA   206 DELETION                       
SEQADV 5DCA     A       UNP  P32639    VAL   207 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ALA   208 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ILE   209 DELETION                       
SEQADV 5DCA     A       UNP  P32639    LEU   210 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ALA   211 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASP   212 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASP   213 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLU   214 DELETION                       
SEQADV 5DCA     A       UNP  P32639    LYS   215 DELETION                       
SEQADV 5DCA     A       UNP  P32639    SER   216 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASP   217 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLU   218 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLU   219 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLU   220 DELETION                       
SEQADV 5DCA     A       UNP  P32639    VAL   221 DELETION                       
SEQADV 5DCA     A       UNP  P32639    THR   222 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLU   223 DELETION                       
SEQADV 5DCA     A       UNP  P32639    MET   224 DELETION                       
SEQADV 5DCA     A       UNP  P32639    SER   225 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASN   226 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASN   227 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ALA   228 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASN   229 DELETION                       
SEQADV 5DCA     A       UNP  P32639    VAL   230 DELETION                       
SEQADV 5DCA     A       UNP  P32639    LEU   231 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLY   232 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLY   233 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLU   234 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ILE   235 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASN   236 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASP   237 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASN   238 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLU   239 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASP   240 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASP   241 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASP   242 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLU   243 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLU   244 DELETION                       
SEQADV 5DCA     A       UNP  P32639    TYR   245 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASP   246 DELETION                       
SEQADV 5DCA     A       UNP  P32639    TYR   247 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASN   248 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASP   249 DELETION                       
SEQADV 5DCA     A       UNP  P32639    VAL   250 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLU   251 DELETION                       
SEQADV 5DCA     A       UNP  P32639    VAL   252 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASN   253 DELETION                       
SEQADV 5DCA     A       UNP  P32639    SER   254 DELETION                       
SEQADV 5DCA     A       UNP  P32639    LYS   255 DELETION                       
SEQADV 5DCA     A       UNP  P32639    LYS   256 DELETION                       
SEQADV 5DCA     A       UNP  P32639    LYS   257 DELETION                       
SEQADV 5DCA     A       UNP  P32639    THR   394 DELETION                       
SEQADV 5DCA     A       UNP  P32639    THR   395 DELETION                       
SEQADV 5DCA     A       UNP  P32639    HIS   396 DELETION                       
SEQADV 5DCA     A       UNP  P32639    SER   397 DELETION                       
SEQADV 5DCA     A       UNP  P32639    LYS   398 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ARG   399 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLU   400 DELETION                       
SEQADV 5DCA     A       UNP  P32639    LEU   401 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASP   402 DELETION                       
SEQADV 5DCA     A       UNP  P32639    SER   403 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLY   404 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASP   405 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASP   406 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLN   407 DELETION                       
SEQADV 5DCA     A       UNP  P32639    PRO   408 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLN   409 DELETION                       
SEQADV 5DCA     A       UNP  P32639    SER   410 DELETION                       
SEQADV 5DCA     A       UNP  P32639    SER   411 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLU   412 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ALA   413 DELETION                       
SEQADV 5DCA     A       UNP  P32639    LYS   414 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ARG   415 DELETION                       
SEQADV 5DCA     A       UNP  P32639    THR   416 DELETION                       
SEQADV 5DCA     A       UNP  P32639    LYS   417 DELETION                       
SEQADV 5DCA     A       UNP  P32639    PHE   418 DELETION                       
SEQADV 5DCA     A       UNP  P32639    SER   419 DELETION                       
SEQADV 5DCA     A       UNP  P32639    VAL  1829 DELETION                       
SEQADV 5DCA     A       UNP  P32639    THR  1830 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ALA  1831 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLU  1832 DELETION                       
SEQADV 5DCA     A       UNP  P32639    VAL  1833 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASN  1834 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLY  1835 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLY  1836 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASP  1837 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ASP  1838 DELETION                       
SEQADV 5DCA     A       UNP  P32639    GLU  1839 DELETION                       
SEQADV 5DCA     A       UNP  P32639    ALA  1840 DELETION                       
SEQRES   1 A 1948  ASP PRO SER ASN VAL GLU THR TYR GLU GLN ILE LEU GLN          
SEQRES   2 A 1948  TRP VAL THR GLU VAL LEU GLY ASN ASP ILE PRO HIS ASP          
SEQRES   3 A 1948  LEU ILE ILE GLY THR ALA ASP ILE PHE ILE ARG GLN LEU          
SEQRES   4 A 1948  LYS GLU ASN GLU GLU ASN GLU ASP GLY ASN ILE GLU GLU          
SEQRES   5 A 1948  ARG LYS GLU LYS ILE GLN HIS GLU LEU GLY ILE ASN ILE          
SEQRES   6 A 1948  ASP SER LEU LYS PHE ASN GLU LEU VAL LYS LEU MET LYS          
SEQRES   7 A 1948  ASN ILE ASN LYS ARG ALA LEU PRO ASN ILE GLU ASN ASP          
SEQRES   8 A 1948  ILE ILE LYS LEU SER ASP SER LYS THR SER ASN ILE GLU          
SEQRES   9 A 1948  SER VAL PRO ILE TYR SER ILE ASP GLU PHE PHE LEU GLN          
SEQRES  10 A 1948  ARG LYS LEU ARG SER GLU LEU GLY TYR LYS ASP THR SER          
SEQRES  11 A 1948  VAL ILE GLN ASP LEU SER GLU LYS ILE LEU ASN ASP ILE          
SEQRES  12 A 1948  GLU THR LEU GLU HIS ASN PRO VAL ALA LEU GLU GLN LYS          
SEQRES  13 A 1948  LEU VAL ASP LEU LEU LYS PHE GLU ASN ILE SER LEU ALA          
SEQRES  14 A 1948  GLU PHE ILE LEU LYS ASN ARG SER THR ILE PHE TRP GLY          
SEQRES  15 A 1948  ILE ARG LEU ALA LYS SER THR GLU ASN GLU ILE PRO ASN          
SEQRES  16 A 1948  LEU ILE GLU LYS MET VAL ALA LYS GLY LEU ASN ASP LEU          
SEQRES  17 A 1948  VAL GLU GLN TYR LYS PHE ARG GLU ASN PRO ALA ILE PRO          
SEQRES  18 A 1948  PRO VAL ILE ASP LEU GLU LYS ILE LYS PHE ASP GLU SER          
SEQRES  19 A 1948  SER LYS LEU MET THR VAL THR LYS VAL SER LEU PRO GLU          
SEQRES  20 A 1948  GLY SER PHE LYS ARG VAL LYS PRO GLN TYR ASP GLU ILE          
SEQRES  21 A 1948  HIS ILE PRO ALA PRO SER LYS PRO VAL ILE ASP TYR GLU          
SEQRES  22 A 1948  LEU LYS GLU ILE THR SER LEU PRO ASP TRP CYS GLN GLU          
SEQRES  23 A 1948  ALA PHE PRO SER SER GLU THR THR SER LEU ASN PRO ILE          
SEQRES  24 A 1948  GLN SER LYS VAL PHE HIS ALA ALA PHE GLU GLY ASP SER          
SEQRES  25 A 1948  ASN MET LEU ILE CYS ALA PRO THR GLY SER GLY LYS THR          
SEQRES  26 A 1948  ASN ILE ALA LEU LEU THR VAL LEU LYS ALA LEU SER HIS          
SEQRES  27 A 1948  HIS TYR ASN PRO LYS THR LYS LYS LEU ASN LEU SER ALA          
SEQRES  28 A 1948  PHE LYS ILE VAL TYR ILE ALA PRO LEU LYS ALA LEU VAL          
SEQRES  29 A 1948  GLN GLU GLN VAL ARG GLU PHE GLN ARG ARG LEU ALA PHE          
SEQRES  30 A 1948  LEU GLY ILE LYS VAL ALA GLU LEU THR GLY ASP SER ARG          
SEQRES  31 A 1948  LEU SER ARG LYS GLN ILE ASP GLU THR GLN VAL LEU VAL          
SEQRES  32 A 1948  SER THR PRO GLU LYS TRP ASP ILE THR THR ARG ASN SER          
SEQRES  33 A 1948  ASN ASN LEU ALA ILE VAL GLU LEU VAL ARG LEU LEU ILE          
SEQRES  34 A 1948  ILE ASP GLU ILE HIS LEU LEU HIS ASP ASP ARG GLY PRO          
SEQRES  35 A 1948  VAL LEU GLU SER ILE VAL ALA ARG THR PHE TRP ALA SER          
SEQRES  36 A 1948  LYS TYR GLY GLN GLU TYR PRO ARG ILE ILE GLY LEU SER          
SEQRES  37 A 1948  ALA THR LEU PRO ASN TYR GLU ASP VAL GLY ARG PHE LEU          
SEQRES  38 A 1948  ARG VAL PRO LYS GLU GLY LEU PHE TYR PHE ASP SER SER          
SEQRES  39 A 1948  PHE ARG PRO CYS PRO LEU SER GLN GLN PHE CYS GLY ILE          
SEQRES  40 A 1948  LYS GLU ARG ASN SER LEU LYS LYS LEU LYS ALA MET ASN          
SEQRES  41 A 1948  ASP ALA CYS TYR GLU LYS VAL LEU GLU SER ILE ASN GLU          
SEQRES  42 A 1948  GLY ASN GLN ILE ILE VAL PHE VAL HIS SER ARG LYS GLU          
SEQRES  43 A 1948  THR SER ARG THR ALA THR TRP LEU LYS ASN LYS PHE ALA          
SEQRES  44 A 1948  GLU GLU ASN ILE THR HIS LYS LEU THR LYS ASN ASP ALA          
SEQRES  45 A 1948  GLY SER LYS GLN ILE LEU LYS THR GLU ALA ALA ASN VAL          
SEQRES  46 A 1948  LEU ASP PRO SER LEU ARG LYS LEU ILE GLU SER GLY ILE          
SEQRES  47 A 1948  GLY THR HIS HIS ALA GLY LEU THR ARG SER ASP ARG SER          
SEQRES  48 A 1948  LEU SER GLU ASP LEU PHE ALA ASP GLY LEU LEU GLN VAL          
SEQRES  49 A 1948  LEU VAL CYS THR ALA THR LEU ALA TRP GLY VAL ASN LEU          
SEQRES  50 A 1948  PRO ALA HIS THR VAL ILE ILE LYS GLY THR ASP VAL TYR          
SEQRES  51 A 1948  SER PRO GLU LYS GLY SER TRP GLU GLN LEU SER PRO GLN          
SEQRES  52 A 1948  ASP VAL LEU GLN MET LEU GLY ARG ALA GLY ARG PRO ARG          
SEQRES  53 A 1948  TYR ASP THR PHE GLY GLU GLY ILE ILE ILE THR ASP GLN          
SEQRES  54 A 1948  SER ASN VAL GLN TYR TYR LEU SER VAL LEU ASN GLN GLN          
SEQRES  55 A 1948  LEU PRO ILE GLU SER GLN PHE VAL SER LYS LEU VAL ASP          
SEQRES  56 A 1948  ASN LEU ASN ALA GLU VAL VAL ALA GLY ASN ILE LYS CYS          
SEQRES  57 A 1948  ARG ASN ASP ALA VAL ASN TRP LEU ALA TYR THR TYR LEU          
SEQRES  58 A 1948  TYR VAL ARG MET LEU ALA SER PRO MET LEU TYR LYS VAL          
SEQRES  59 A 1948  PRO ASP ILE SER SER ASP GLY GLN LEU LYS LYS PHE ARG          
SEQRES  60 A 1948  GLU SER LEU VAL HIS SER ALA LEU CYS ILE LEU LYS GLU          
SEQRES  61 A 1948  GLN GLU LEU VAL LEU TYR ASP ALA GLU ASN ASP VAL ILE          
SEQRES  62 A 1948  GLU ALA THR ASP LEU GLY ASN ILE ALA SER SER PHE TYR          
SEQRES  63 A 1948  ILE ASN HIS ALA SER MET ASP VAL TYR ASN ARG GLU LEU          
SEQRES  64 A 1948  ASP GLU HIS THR THR GLN ILE ASP LEU PHE ARG ILE PHE          
SEQRES  65 A 1948  SER MET SER GLU GLU PHE LYS TYR VAL SER VAL ARG TYR          
SEQRES  66 A 1948  GLU GLU LYS ARG GLU LEU LYS GLN LEU LEU GLU LYS ALA          
SEQRES  67 A 1948  PRO ILE PRO ILE ARG GLU ASP ILE ASP ASP PRO LEU ALA          
SEQRES  68 A 1948  LYS VAL ASN VAL LEU LEU GLN SER TYR PHE SER GLN LEU          
SEQRES  69 A 1948  LYS PHE GLU GLY PHE ALA LEU ASN SER ASP ILE VAL PHE          
SEQRES  70 A 1948  ILE HIS GLN ASN ALA GLY ARG LEU LEU ARG ALA MET PHE          
SEQRES  71 A 1948  GLU ILE CYS LEU LYS ARG GLY TRP GLY HIS PRO THR ARG          
SEQRES  72 A 1948  MET LEU LEU ASN LEU CYS LYS SER ALA THR THR LYS MET          
SEQRES  73 A 1948  TRP PRO THR ASN CYS PRO LEU ARG GLN PHE LYS THR CYS          
SEQRES  74 A 1948  PRO VAL GLU VAL ILE LYS ARG LEU GLU ALA SER THR VAL          
SEQRES  75 A 1948  PRO TRP GLY ASP TYR LEU GLN LEU GLU THR PRO ALA GLU          
SEQRES  76 A 1948  VAL GLY ARG ALA ILE ARG SER GLU LYS TYR GLY LYS GLN          
SEQRES  77 A 1948  VAL TYR ASP LEU LEU LYS ARG PHE PRO LYS MET SER VAL          
SEQRES  78 A 1948  THR CYS ASN ALA GLN PRO ILE THR ARG SER VAL MET ARG          
SEQRES  79 A 1948  PHE ASN ILE GLU ILE ILE ALA ASP TRP ILE TRP ASP MET          
SEQRES  80 A 1948  ASN VAL HIS GLY SER LEU GLU PRO PHE LEU LEU MET LEU          
SEQRES  81 A 1948  GLU ASP THR ASP GLY ASP SER ILE LEU TYR TYR ASP VAL          
SEQRES  82 A 1948  LEU PHE ILE THR PRO ASP ILE VAL GLY HIS GLU PHE THR          
SEQRES  83 A 1948  LEU SER PHE THR TYR GLU LEU LYS GLN HIS ASN GLN ASN          
SEQRES  84 A 1948  ASN LEU PRO PRO ASN PHE PHE LEU THR LEU ILE SER GLU          
SEQRES  85 A 1948  ASN TRP TRP HIS SER GLU PHE GLU ILE PRO VAL SER PHE          
SEQRES  86 A 1948  ASN GLY PHE LYS LEU PRO LYS LYS PHE PRO PRO PRO THR          
SEQRES  87 A 1948  PRO LEU LEU GLU ASN ILE SER ILE SER THR SER GLU LEU          
SEQRES  88 A 1948  GLY ASN ASP ASP PHE SER GLU VAL PHE GLU PHE LYS THR          
SEQRES  89 A 1948  PHE ASN LYS ILE GLN SER GLN VAL PHE GLU SER LEU TYR          
SEQRES  90 A 1948  ASN SER ASN ASP SER VAL PHE VAL GLY SER GLY LYS GLY          
SEQRES  91 A 1948  THR GLY LYS THR ALA MET ALA GLU LEU ALA LEU LEU ASN          
SEQRES  92 A 1948  HIS TRP ARG GLN ASN LYS GLY ARG ALA VAL TYR ILE ASN          
SEQRES  93 A 1948  PRO SER GLY GLU LYS ILE ASP PHE LEU LEU SER ASP TRP          
SEQRES  94 A 1948  ASN LYS ARG PHE SER HIS LEU ALA GLY GLY LYS ILE ILE          
SEQRES  95 A 1948  ASN LYS LEU GLY ASN ASP PRO SER LEU ASN LEU LYS LEU          
SEQRES  96 A 1948  LEU ALA LYS SER HIS VAL LEU LEU ALA THR PRO VAL GLN          
SEQRES  97 A 1948  PHE GLU LEU LEU SER ARG ARG TRP ARG GLN ARG LYS ASN          
SEQRES  98 A 1948  ILE GLN SER LEU GLU LEU MET ILE TYR ASP ASP ALA HIS          
SEQRES  99 A 1948  GLU ILE SER GLN GLY VAL TYR GLY ALA VAL TYR GLU THR          
SEQRES 100 A 1948  LEU ILE SER ARG MET ILE PHE ILE ALA THR GLN LEU GLU          
SEQRES 101 A 1948  LYS LYS ILE ARG PHE VAL CYS LEU SER ASN CYS LEU ALA          
SEQRES 102 A 1948  ASN ALA ARG ASP PHE GLY GLU TRP ALA GLY MET THR LYS          
SEQRES 103 A 1948  SER ASN ILE TYR ASN PHE SER PRO SER GLU ARG ILE GLU          
SEQRES 104 A 1948  PRO LEU GLU ILE ASN ILE GLN SER PHE LYS ASP VAL GLU          
SEQRES 105 A 1948  HIS ILE SER PHE ASN PHE SER MET LEU GLN MET ALA PHE          
SEQRES 106 A 1948  GLU ALA SER ALA ALA ALA ALA GLY ASN ARG ASN SER SER          
SEQRES 107 A 1948  SER VAL PHE LEU PRO SER ARG LYS ASP CYS MET GLU VAL          
SEQRES 108 A 1948  ALA SER ALA PHE MET LYS PHE SER LYS ALA ILE GLU TRP          
SEQRES 109 A 1948  ASP MET LEU ASN VAL GLU GLU GLU GLN ILE VAL PRO TYR          
SEQRES 110 A 1948  ILE GLU LYS LEU THR ASP GLY HIS LEU ARG ALA PRO LEU          
SEQRES 111 A 1948  LYS HIS GLY VAL GLY ILE LEU TYR LYS GLY MET ALA SER          
SEQRES 112 A 1948  ASN ASP GLU ARG ILE VAL LYS ARG LEU TYR GLU TYR GLY          
SEQRES 113 A 1948  ALA VAL SER VAL LEU LEU ILE SER LYS ASP CYS SER ALA          
SEQRES 114 A 1948  PHE ALA CYS LYS THR ASP GLU VAL ILE ILE LEU GLY THR          
SEQRES 115 A 1948  ASN LEU TYR ASP GLY ALA GLU HIS LYS TYR MET PRO TYR          
SEQRES 116 A 1948  THR ILE ASN GLU LEU LEU GLU MET VAL GLY LEU ALA SER          
SEQRES 117 A 1948  GLY ASN ASP SER MET ALA GLY LYS VAL LEU ILE LEU THR          
SEQRES 118 A 1948  SER HIS ASN MET LYS ALA TYR TYR LYS LYS PHE LEU ILE          
SEQRES 119 A 1948  GLU PRO LEU PRO THR GLU SER TYR LEU GLN TYR ILE ILE          
SEQRES 120 A 1948  HIS ASP THR LEU ASN ASN GLU ILE ALA ASN SER ILE ILE          
SEQRES 121 A 1948  GLN SER LYS GLN ASP CYS VAL ASP TRP PHE THR TYR SER          
SEQRES 122 A 1948  TYR PHE TYR ARG ARG ILE HIS VAL ASN PRO SER TYR TYR          
SEQRES 123 A 1948  GLY VAL ARG ASP THR SER PRO HIS GLY ILE SER VAL PHE          
SEQRES 124 A 1948  LEU SER ASN LEU VAL GLU THR CYS LEU ASN ASP LEU VAL          
SEQRES 125 A 1948  GLU SER SER PHE ILE GLU ILE ASP ASP THR GLU ALA GLU          
SEQRES 126 A 1948  THR GLU ILE ILE SER THR LEU SER ASN GLY LEU ILE ALA          
SEQRES 127 A 1948  SER HIS TYR GLY VAL SER PHE PHE THR ILE GLN SER PHE          
SEQRES 128 A 1948  VAL SER SER LEU SER ASN THR SER THR LEU LYS ASN MET          
SEQRES 129 A 1948  LEU TYR VAL LEU SER THR ALA VAL GLU PHE GLU SER VAL          
SEQRES 130 A 1948  PRO LEU ARG LYS GLY ASP ARG ALA LEU LEU VAL LYS LEU          
SEQRES 131 A 1948  SER LYS ARG LEU PRO LEU ARG PHE PRO GLU HIS THR SER          
SEQRES 132 A 1948  SER GLY SER VAL SER PHE LYS VAL PHE LEU LEU LEU GLN          
SEQRES 133 A 1948  ALA TYR PHE SER ARG LEU GLU LEU PRO VAL ASP PHE GLN          
SEQRES 134 A 1948  ASN ASP LEU LYS ASP ILE LEU GLU LYS VAL VAL PRO LEU          
SEQRES 135 A 1948  ILE ASN VAL VAL VAL ASP ILE LEU SER ALA ASN GLY TYR          
SEQRES 136 A 1948  LEU ASN ALA THR THR ALA MET ASP LEU ALA GLN MET LEU          
SEQRES 137 A 1948  ILE GLN GLY VAL TRP ASP VAL ASP ASN PRO LEU ARG GLN          
SEQRES 138 A 1948  ILE PRO HIS PHE ASN ASN LYS ILE LEU GLU LYS CYS LYS          
SEQRES 139 A 1948  GLU ILE ASN VAL GLU THR VAL TYR ASP ILE MET ALA LEU          
SEQRES 140 A 1948  GLU ASP GLU GLU ARG ASP GLU ILE LEU THR LEU THR ASP          
SEQRES 141 A 1948  SER GLN LEU ALA GLN VAL ALA ALA PHE VAL ASN ASN TYR          
SEQRES 142 A 1948  PRO ASN VAL GLU LEU THR TYR SER LEU ASN ASN SER ASP          
SEQRES 143 A 1948  SER LEU ILE SER GLY VAL LYS GLN LYS ILE THR ILE GLN          
SEQRES 144 A 1948  LEU THR ARG ASP VAL GLU PRO GLU ASN LEU GLN VAL THR          
SEQRES 145 A 1948  SER GLU LYS TYR PRO PHE ASP LYS LEU GLU SER TRP TRP          
SEQRES 146 A 1948  LEU VAL LEU GLY GLU VAL SER LYS LYS GLU LEU TYR ALA          
SEQRES 147 A 1948  ILE LYS LYS VAL THR LEU ASN LYS GLU THR GLN GLN TYR          
SEQRES 148 A 1948  GLU LEU GLU PHE ASP THR PRO THR SER GLY LYS HIS ASN          
SEQRES 149 A 1948  LEU THR ILE TRP CYS VAL CYS ASP SER TYR LEU ASP ALA          
SEQRES 150 A 1948  ASP LYS GLU LEU SER PHE GLU ILE ASN VAL LYS                  
SEQRES   1 J  251  SER LYS ASN GLU TRP ARG LYS SER ALA ILE ALA ASN THR          
SEQRES   2 J  251  LEU LEU TYR LEU ARG LEU LYS ASN ILE TYR VAL SER ALA          
SEQRES   3 J  251  ASP ASP PHE VAL GLU GLU GLN ASN VAL TYR VAL LEU PRO          
SEQRES   4 J  251  LYS ASN LEU LEU LYS LYS PHE ILE GLU ILE SER ASP VAL          
SEQRES   5 J  251  LYS ILE GLN VAL ALA ALA PHE ILE TYR GLY MET SER ALA          
SEQRES   6 J  251  LYS ASP HIS PRO LYS VAL LYS GLU ILE LYS THR VAL VAL          
SEQRES   7 J  251  LEU VAL PRO GLN LEU GLY HIS VAL GLY SER VAL GLN ILE          
SEQRES   8 J  251  SER ASN ILE PRO ASP ILE GLY ASP LEU PRO ASP THR GLU          
SEQRES   9 J  251  GLY LEU GLU LEU LEU GLY TRP ILE HIS THR GLN THR GLU          
SEQRES  10 J  251  GLU LEU LYS PHE MET ALA ALA SER GLU VAL ALA THR HIS          
SEQRES  11 J  251  SER LYS LEU PHE ALA ASP LYS LYS ARG ASP CYS ILE ASP          
SEQRES  12 J  251  ILE SER ILE PHE SER THR PRO GLY SER VAL SER LEU SER          
SEQRES  13 J  251  ALA TYR ASN LEU THR ASP GLU GLY TYR GLN TRP GLY GLU          
SEQRES  14 J  251  GLU ASN LYS ASP ILE MET ASN VAL LEU SER GLU GLY PHE          
SEQRES  15 J  251  GLU PRO THR PHE SER THR HIS ALA GLN LEU LEU LEU SER          
SEQRES  16 J  251  ASP ARG ILE THR GLY ASN PHE ILE ILE PRO SER GLY ASN          
SEQRES  17 J  251  VAL TRP ASN TYR THR PHE MET GLY THR ALA PHE ASN GLN          
SEQRES  18 J  251  GLU GLY ASP TYR ASN PHE LYS TYR GLY ILE PRO LEU GLU          
SEQRES  19 J  251  PHE TYR ASN GLU MET HIS ARG PRO VAL HIS PHE LEU GLN          
SEQRES  20 J  251  PHE SER GLU LEU                                              
FORMUL   3  HOH   *191(H2 O)                                                    
HELIX    1 AA1 ASP A  113  LEU A  131  1                                  19    
HELIX    2 AA2 PRO A  136  GLN A  150  1                                  15    
HELIX    3 AA3 GLU A  163  GLN A  170  1                                   8    
HELIX    4 AA4 ILE A  175  LYS A  187  1                                  13    
HELIX    5 AA5 PHE A  291  LEU A  301  1                                  11    
HELIX    6 AA6 ASP A  305  ILE A  320  1                                  16    
HELIX    7 AA7 ALA A  329  LYS A  339  1                                  11    
HELIX    8 AA8 ALA A  346  LYS A  351  1                                   6    
HELIX    9 AA9 ASN A  352  GLY A  359  1                                   8    
HELIX   10 AB1 GLU A  369  VAL A  378  1                                  10    
HELIX   11 AB2 GLU A  387  GLU A  393  1                                   7    
HELIX   12 AB3 ASP A  428  LYS A  433  1                                   6    
HELIX   13 AB4 GLU A  479  LEU A  483  5                                   5    
HELIX   14 AB5 PRO A  484  PHE A  491  5                                   8    
HELIX   15 AB6 ASN A  500  GLU A  512  1                                  13    
HELIX   16 AB7 GLY A  526  HIS A  541  1                                  16    
HELIX   17 AB8 LEU A  563  LEU A  578  1                                  16    
HELIX   18 AB9 SER A  595  THR A  602  1                                   8    
HELIX   19 AC1 THR A  608  ASN A  618  1                                  11    
HELIX   20 AC2 ASN A  621  GLU A  626  1                                   6    
HELIX   21 AC3 GLU A  635  ASP A  641  5                                   7    
HELIX   22 AC4 ARG A  643  ALA A  657  1                                  15    
HELIX   23 AC5 ASN A  676  LEU A  684  1                                   9    
HELIX   24 AC6 PRO A  687  GLU A  689  5                                   3    
HELIX   25 AC7 ASP A  695  ARG A  699  5                                   5    
HELIX   26 AC8 ASN A  714  GLU A  736  1                                  23    
HELIX   27 AC9 SER A  746  GLU A  763  1                                  18    
HELIX   28 AD1 ALA A  775  ALA A  786  1                                  12    
HELIX   29 AD2 ASP A  790  SER A  799  1                                  10    
HELIX   30 AD3 THR A  809  ASP A  822  1                                  14    
HELIX   31 AD4 ALA A  832  GLY A  837  1                                   6    
HELIX   32 AD5 PRO A  855  GLY A  858  5                                   4    
HELIX   33 AD6 SER A  864  ARG A  874  1                                  11    
HELIX   34 AD7 ASN A  894  LEU A  902  1                                   9    
HELIX   35 AD8 GLN A  911  SER A  914  5                                   4    
HELIX   36 AD9 LYS A  915  ALA A  926  1                                  12    
HELIX   37 AE1 CYS A  931  ALA A  940  1                                  10    
HELIX   38 AE2 THR A  942  SER A  951  1                                  10    
HELIX   39 AE3 ASP A  959  GLY A  964  1                                   6    
HELIX   40 AE4 LEU A  966  GLN A  984  1                                  19    
HELIX   41 AE5 THR A  999  TYR A 1009  1                                  11    
HELIX   42 AE6 ASN A 1011  LEU A 1022  1                                  12    
HELIX   43 AE7 THR A 1027  MET A 1037  1                                  11    
HELIX   44 AE8 SER A 1038  LYS A 1042  5                                   5    
HELIX   45 AE9 GLU A 1050  LYS A 1060  1                                  11    
HELIX   46 AF1 ASP A 1071  SER A 1085  1                                  15    
HELIX   47 AF2 GLY A 1091  GLY A 1120  1                                  30    
HELIX   48 AF3 TRP A 1121  LYS A 1138  1                                  18    
HELIX   49 AF4 CYS A 1144  PHE A 1149  5                                   6    
HELIX   50 AF5 PRO A 1153  THR A 1164  1                                  12    
HELIX   51 AF6 TRP A 1167  GLN A 1172  1                                   6    
HELIX   52 AF7 ALA A 1177  ILE A 1183  1                                   7    
HELIX   53 AF8 LYS A 1190  LYS A 1197  1                                   8    
HELIX   54 AF9 ASP A 1229  GLY A 1234  1                                   6    
HELIX   55 AG1 LYS A 1277  ASN A 1283  1                                   7    
HELIX   56 AG2 SER A 1330  LEU A 1334  5                                   5    
HELIX   57 AG3 ASN A 1336  GLU A 1341  1                                   6    
HELIX   58 AG4 ASN A 1349  VAL A 1355  1                                   7    
HELIX   59 AG5 VAL A 1355  ASN A 1361  1                                   7    
HELIX   60 AG6 GLY A 1375  GLN A 1390  1                                  16    
HELIX   61 AG7 SER A 1401  SER A 1417  1                                  17    
HELIX   62 AG8 ASP A 1431  SER A 1442  1                                  12    
HELIX   63 AG9 THR A 1448  SER A 1456  1                                   9    
HELIX   64 AH1 ARG A 1457  GLN A 1461  5                                   5    
HELIX   65 AH2 ARG A 1462  SER A 1467  1                                   6    
HELIX   66 AH3 ALA A 1476  SER A 1480  5                                   5    
HELIX   67 AH4 GLN A 1481  GLU A 1503  1                                  23    
HELIX   68 AH5 ALA A 1518  GLY A 1526  1                                   9    
HELIX   69 AH6 THR A 1528  SER A 1530  5                                   3    
HELIX   70 AH7 ASN A 1560  ASN A 1577  1                                  18    
HELIX   71 AH8 SER A 1587  ALA A 1604  1                                  18    
HELIX   72 AH9 GLU A 1613  LYS A 1623  1                                  11    
HELIX   73 AI1 ASP A 1626  HIS A 1628  5                                   3    
HELIX   74 AI2 LEU A 1629  HIS A 1635  1                                   7    
HELIX   75 AI3 ALA A 1645  TYR A 1658  1                                  14    
HELIX   76 AI4 ASP A 1669  SER A 1671  5                                   3    
HELIX   77 AI5 THR A 1699  GLY A 1708  1                                  10    
HELIX   78 AI6 HIS A 1726  GLU A 1738  1                                  13    
HELIX   79 AI7 TYR A 1745  TYR A 1748  5                                   4    
HELIX   80 AI8 ILE A 1749  ASN A 1760  1                                  12    
HELIX   81 AI9 SER A 1765  THR A 1774  1                                  10    
HELIX   82 AJ1 SER A 1776  HIS A 1783  1                                   8    
HELIX   83 AJ2 ASN A 1785  GLY A 1790  5                                   6    
HELIX   84 AJ3 SER A 1795  SER A 1817  1                                  23    
HELIX   85 AJ4 LEU A 1847  GLY A 1857  1                                  11    
HELIX   86 AJ5 SER A 1859  LEU A 1870  1                                  12    
HELIX   87 AJ6 THR A 1875  THR A 1885  1                                  11    
HELIX   88 AJ7 ALA A 1886  VAL A 1892  5                                   7    
HELIX   89 AJ8 GLY A 1897  LYS A 1907  1                                  11    
HELIX   90 AJ9 SER A 1921  ARG A 1936  1                                  16    
HELIX   91 AK1 PRO A 1940  ASN A 1968  1                                  29    
HELIX   92 AK2 ASN A 1972  GLY A 1986  1                                  15    
HELIX   93 AK3 ASN A 2001  ILE A 2011  1                                  11    
HELIX   94 AK4 THR A 2015  ALA A 2021  1                                   7    
HELIX   95 AK5 GLU A 2023  LEU A 2031  1                                   9    
HELIX   96 AK6 THR A 2034  TYR A 2048  1                                  15    
HELIX   97 AK7 GLU J 2151  THR J 2160  1                                  10    
HELIX   98 AK8 LEU J 2161  LYS J 2167  5                                   7    
HELIX   99 AK9 LYS J 2187  ILE J 2196  1                                  10    
HELIX  100 AL1 ALA J 2270  ALA J 2282  1                                  13    
HELIX  101 AL2 THR J 2308  ASN J 2318  1                                  11    
HELIX  102 AL3 MET J 2362  PHE J 2366  5                                   5    
HELIX  103 AL4 ASN J 2384  HIS J 2387  5                                   4    
HELIX  104 AL5 ARG J 2388  GLU J 2397  1                                  10    
SHEET    1 AA1 7 LYS A 271  LEU A 272  0                                        
SHEET    2 AA1 7 LEU A1544  PHE A1551 -1  O  LEU A1544   N  LEU A 272           
SHEET    3 AA1 7 GLY A1718  SER A1725  1  O  ILE A1722   N  GLN A1549           
SHEET    4 AA1 7 GLU A1679  LEU A1683  1  N  ILE A1682   O  LEU A1721           
SHEET    5 AA1 7 SER A1581  LEU A1585  1  N  PHE A1584   O  ILE A1681           
SHEET    6 AA1 7 VAL A1663  SER A1667  1  O  LEU A1664   N  VAL A1583           
SHEET    7 AA1 7 VAL A1637  LEU A1640  1  N  GLY A1638   O  LEU A1665           
SHEET    1 AA2 8 PHE A 453  VAL A 456  0                                        
SHEET    2 AA2 8 TYR A 460  ILE A 465 -1  O  HIS A 464   N  PHE A 453           
SHEET    3 AA2 8 LEU A 703  ILE A 710 -1  O  GLY A 709   N  ASP A 461           
SHEET    4 AA2 8 GLY A 884  ASP A 891  1  O  THR A 890   N  ILE A 710           
SHEET    5 AA2 8 THR A 844  LYS A 848  1  N  ILE A 847   O  ILE A 887           
SHEET    6 AA2 8 ILE A 740  PHE A 743  1  N  PHE A 743   O  ILE A 846           
SHEET    7 AA2 8 VAL A 827  CYS A 830  1  O  CYS A 830   N  VAL A 742           
SHEET    8 AA2 8 ILE A 801  HIS A 804  1  N  GLY A 802   O  VAL A 827           
SHEET    1 AA3 7 VAL A 585  GLU A 587  0                                        
SHEET    2 AA3 7 VAL A 604  SER A 607  1  O  VAL A 604   N  ALA A 586           
SHEET    3 AA3 7 LYS A 556  ILE A 560  1  N  TYR A 559   O  LEU A 605           
SHEET    4 AA3 7 VAL A 628  ILE A 633  1  O  ILE A 632   N  VAL A 558           
SHEET    5 AA3 7 ARG A 666  ALA A 672  1  O  ARG A 666   N  LEU A 631           
SHEET    6 AA3 7 MET A 517  ALA A 521  1  N  MET A 517   O  GLY A 669           
SHEET    7 AA3 7 LEU A 691  TYR A 693  1  O  PHE A 692   N  CYS A 520           
SHEET    1 AA4 2 ASP A 851  SER A 854  0                                        
SHEET    2 AA4 2 SER A 859  GLN A 862 -1  O  GLU A 861   N  VAL A 852           
SHEET    1 AA5 2 VAL A 987  ASP A 990  0                                        
SHEET    2 AA5 2 VAL A 995  ALA A 998 -1  O  GLU A 997   N  LEU A 988           
SHEET    1 AA6 3 MET A1202  PRO A1210  0                                        
SHEET    2 AA6 3 VAL A1215  ALA A1224 -1  O  ARG A1217   N  GLN A1209           
SHEET    3 AA6 3 GLU A1267  GLU A1275 -1  O  PHE A1272   N  PHE A1218           
SHEET    1 AA7 4 ILE A1251  ILE A1259  0                                        
SHEET    2 AA7 4 GLU A1237  GLU A1244 -1  N  LEU A1241   O  ASP A1255           
SHEET    3 AA7 4 ASN A1287  SER A1294 -1  O  ILE A1293   N  LEU A1240           
SHEET    4 AA7 4 GLU A1301  SER A1307 -1  O  ILE A1304   N  LEU A1290           
SHEET    1 AA8 7 ILE A1424  ASN A1426  0                                        
SHEET    2 AA8 7 VAL A1444  ALA A1447  1  O  VAL A1444   N  ILE A1425           
SHEET    3 AA8 7 ALA A1395  ILE A1398  1  N  TYR A1397   O  LEU A1445           
SHEET    4 AA8 7 LEU A1470  ASP A1474  1  O  ILE A1472   N  VAL A1396           
SHEET    5 AA8 7 ARG A1507  SER A1512  1  O  VAL A1509   N  TYR A1473           
SHEET    6 AA8 7 VAL A1366  GLY A1369  1  N  VAL A1368   O  SER A1512           
SHEET    7 AA8 7 ILE A1532  ASN A1534  1  O  TYR A1533   N  GLY A1369           
SHEET    1 AA9 2 ASN A1686  ASP A1689  0                                        
SHEET    2 AA9 2 LYS A1694  PRO A1697 -1  O  MET A1696   N  LEU A1687           
SHEET    1 AB1 2 ILE A1820  ASP A1823  0                                        
SHEET    2 AB1 2 ILE A1843  THR A1846 -1  O  ILE A1843   N  ASP A1823           
SHEET    1 AB2 3 GLU A2052  LEU A2057  0                                        
SHEET    2 AB2 3 LYS A2068  THR A2076 -1  O  GLN A2074   N  THR A2054           
SHEET    3 AB2 3 THR A2123  ASP A2131 -1  O  LEU A2128   N  ILE A2071           
SHEET    1 AB3 4 GLU A2110  VAL A2117  0                                        
SHEET    2 AB3 4 TRP A2099  GLU A2105 -1  N  LEU A2101   O  LYS A2115           
SHEET    3 AB3 4 GLY A2136  CYS A2146 -1  O  TRP A2143   N  VAL A2102           
SHEET    4 AB3 4 LYS A2154  VAL A2162 -1  O  VAL A2162   N  GLY A2136           
SHEET    1 AB4 8 ILE J2169  VAL J2171  0                                        
SHEET    2 AB4 8 SER J2299  LEU J2307  1  O  LEU J2302   N  TYR J2170           
SHEET    3 AB4 8 ILE J2289  THR J2296 -1  N  PHE J2294   O  SER J2301           
SHEET    4 AB4 8 GLU J2254  GLN J2262  1  N  HIS J2260   O  ILE J2293           
SHEET    5 AB4 8 ALA J2204  SER J2211 -1  N  ALA J2205   O  ILE J2259           
SHEET    6 AB4 8 VAL J2218  VAL J2225 -1  O  VAL J2225   N  PHE J2206           
SHEET    7 AB4 8 ASN J2348  PRO J2352  1  O  ASN J2348   N  VAL J2224           
SHEET    8 AB4 8 PHE J2374  TYR J2376 -1  O  LYS J2375   N  ILE J2351           
SHEET    1 AB5 7 ILE J2169  VAL J2171  0                                        
SHEET    2 AB5 7 SER J2299  LEU J2307  1  O  LEU J2302   N  TYR J2170           
SHEET    3 AB5 7 SER J2334  SER J2342 -1  O  ALA J2337   N  ALA J2304           
SHEET    4 AB5 7 VAL J2182  PRO J2186  1  N  TYR J2183   O  LEU J2340           
SHEET    5 AB5 7 VAL J2218  VAL J2225  1  O  LYS J2219   N  VAL J2182           
SHEET    6 AB5 7 ASN J2348  PRO J2352  1  O  ASN J2348   N  VAL J2224           
SHEET    7 AB5 7 PHE J2374  TYR J2376 -1  O  LYS J2375   N  ILE J2351           
SHEET    1 AB6 2 GLN J2229  HIS J2232  0                                        
SHEET    2 AB6 2 SER J2235  ILE J2238 -1  O  GLN J2237   N  LEU J2230           
CRYST1  107.850  178.850  181.110  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      0.009272  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005591  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005522        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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