GenomeNet

Database: PDB
Entry: 4WQO
LinkDB: 4WQO
Original site: 4WQO 
HEADER    TRANSCRIPTION                           22-OCT-14   4WQO              
TITLE     STRUCTURE OF VHL-ELOB-ELOC-CUL2                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VON HIPPEL-LINDAU DISEASE TUMOR SUPPRESSOR;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PROTEIN G7,PVHL;                                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 2;           
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: ELONGIN 18 KDA SUBUNIT,ELONGIN-B,ELOB,RNA POLYMERASE II     
COMPND  10 TRANSCRIPTION FACTOR SIII SUBUNIT B,SIII P18;                        
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 1;           
COMPND  14 CHAIN: C;                                                            
COMPND  15 FRAGMENT: UNP RESIDUES 17-112;                                       
COMPND  16 SYNONYM: ELONGIN 15 KDA SUBUNIT,ELONGIN-C,ELOC,RNA POLYMERASE II     
COMPND  17 TRANSCRIPTION FACTOR SIII SUBUNIT C,SIII P15;                        
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: CULLIN-2;                                                  
COMPND  21 CHAIN: D;                                                            
COMPND  22 FRAGMENT: UNP RESIDUES 20-122;                                       
COMPND  23 SYNONYM: CUL-2;                                                      
COMPND  24 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: VHL;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: TCEB2;                                                         
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: TCEB1;                                                         
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 GENE: CUL2;                                                          
SOURCE  27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    E3 LIGASE COMPLEX, TRANSCRIPTION                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.C.NGUYEN,Y.XIONG                                                    
REVDAT   3   22-NOV-17 4WQO    1       SOURCE JRNL   REMARK                     
REVDAT   2   11-MAR-15 4WQO    1       JRNL                                     
REVDAT   1   04-MAR-15 4WQO    0                                                
JRNL        AUTH   H.C.NGUYEN,H.YANG,J.L.FRIBOURGH,L.S.WOLFE,Y.XIONG            
JRNL        TITL   INSIGHTS INTO CULLIN-RING E3 UBIQUITIN LIGASE RECRUITMENT:   
JRNL        TITL 2 STRUCTURE OF THE VHL-ELOBC-CUL2 COMPLEX.                     
JRNL        REF    STRUCTURE                     V.  23   441 2015              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   25661653                                                     
JRNL        DOI    10.1016/J.STR.2014.12.014                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.30                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 24319                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.780                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1163                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.3022 -  6.3958    0.99     3059   170  0.1776 0.2024        
REMARK   3     2  6.3958 -  5.0783    1.00     2949   152  0.2195 0.2478        
REMARK   3     3  5.0783 -  4.4369    0.98     2903   130  0.1914 0.2294        
REMARK   3     4  4.4369 -  4.0315    0.98     2843   140  0.2136 0.2485        
REMARK   3     5  4.0315 -  3.7426    0.98     2833   132  0.2693 0.3174        
REMARK   3     6  3.7426 -  3.5220    0.99     2866   157  0.3050 0.3408        
REMARK   3     7  3.5220 -  3.3457    0.99     2843   140  0.3287 0.3385        
REMARK   3     8  3.3457 -  3.2001    1.00     2860   142  0.3556 0.3979        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.450            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.700           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 122.9                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011           3993                                  
REMARK   3   ANGLE     :  1.774           5421                                  
REMARK   3   CHIRALITY :  0.076            610                                  
REMARK   3   PLANARITY :  0.011            695                                  
REMARK   3   DIHEDRAL  : 15.250           1493                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -50.8489  -7.0025 -38.0830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4000 T22:   0.7384                                     
REMARK   3      T33:   1.0771 T12:   0.8964                                     
REMARK   3      T13:  -0.3513 T23:  -0.2005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0559 L22:   0.1544                                     
REMARK   3      L33:   0.2171 L12:  -0.0656                                     
REMARK   3      L13:   0.0927 L23:  -0.1431                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0064 S12:  -0.1378 S13:  -0.0408                       
REMARK   3      S21:   0.4054 S22:   0.1373 S23:   0.2014                       
REMARK   3      S31:  -0.0536 S32:   0.1396 S33:   0.1017                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -32.2460  15.3825 -65.0636              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2993 T22:   1.2922                                     
REMARK   3      T33:   1.1541 T12:   0.0138                                     
REMARK   3      T13:   0.0388 T23:  -0.1907                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0687 L22:   0.0561                                     
REMARK   3      L33:   0.0378 L12:  -0.0238                                     
REMARK   3      L13:   0.0552 L23:  -0.0435                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1775 S12:   0.3136 S13:   0.2736                       
REMARK   3      S21:   0.1188 S22:   0.3366 S23:  -0.2822                       
REMARK   3      S31:  -0.4759 S32:   0.3112 S33:   0.0003                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'C'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -49.1261  12.5729 -58.7693              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2079 T22:   0.7388                                     
REMARK   3      T33:   0.8988 T12:   0.2743                                     
REMARK   3      T13:  -0.1707 T23:  -0.0941                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0723 L22:   0.0733                                     
REMARK   3      L33:   0.0676 L12:   0.0655                                     
REMARK   3      L13:  -0.0544 L23:  -0.0028                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1809 S12:   0.1125 S13:  -0.1252                       
REMARK   3      S21:  -0.0518 S22:   0.3877 S23:  -0.3050                       
REMARK   3      S31:  -0.2957 S32:   0.0684 S33:   0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'D'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -75.9941  15.2847 -60.7844              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4524 T22:   1.1231                                     
REMARK   3      T33:   0.7060 T12:   0.4710                                     
REMARK   3      T13:  -0.1485 T23:  -0.1482                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6390 L22:   0.0593                                     
REMARK   3      L33:   0.1675 L12:   0.2151                                     
REMARK   3      L13:  -0.1514 L23:  -0.0001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4640 S12:   0.7333 S13:   0.4047                       
REMARK   3      S21:   0.1453 S22:   0.1930 S23:  -0.1727                       
REMARK   3      S31:  -0.2886 S32:  -0.3367 S33:  -0.0373                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4WQO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-OCT-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204322.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-SEP-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24321                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 1LM8 AND 2WZK                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 75.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 4M NA FORMATE, MICROBATCH, TEMPERATURE   
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      142.51200            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       71.25600            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       71.25600            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      142.51200            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     TRP A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     GLU A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     VAL A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     GLU A    16                                                      
REMARK 465     GLU A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     GLY A    19                                                      
REMARK 465     VAL A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     GLU A    22                                                      
REMARK 465     TYR A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     GLU A    26                                                      
REMARK 465     GLU A    27                                                      
REMARK 465     ASP A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     GLY A    30                                                      
REMARK 465     GLU A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     SER A    33                                                      
REMARK 465     GLY A    34                                                      
REMARK 465     ALA A    35                                                      
REMARK 465     GLU A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     SER A    38                                                      
REMARK 465     GLY A    39                                                      
REMARK 465     PRO A    40                                                      
REMARK 465     GLU A    41                                                      
REMARK 465     GLU A    42                                                      
REMARK 465     SER A    43                                                      
REMARK 465     GLY A    44                                                      
REMARK 465     PRO A    45                                                      
REMARK 465     GLU A    46                                                      
REMARK 465     GLU A    47                                                      
REMARK 465     LEU A    48                                                      
REMARK 465     GLY A    49                                                      
REMARK 465     ALA A    50                                                      
REMARK 465     GLU A    51                                                      
REMARK 465     GLU A    52                                                      
REMARK 465     GLU A    53                                                      
REMARK 465     MET A    54                                                      
REMARK 465     GLU A    55                                                      
REMARK 465     ALA A    56                                                      
REMARK 465     GLY A    57                                                      
REMARK 465     ARG A    58                                                      
REMARK 465     PRO A    59                                                      
REMARK 465     HIS A   208                                                      
REMARK 465     GLN A   209                                                      
REMARK 465     ARG A   210                                                      
REMARK 465     MET A   211                                                      
REMARK 465     GLY A   212                                                      
REMARK 465     ASP A   213                                                      
REMARK 465     PRO B   105                                                      
REMARK 465     GLN B   106                                                      
REMARK 465     ASP B   107                                                      
REMARK 465     SER B   108                                                      
REMARK 465     GLY B   109                                                      
REMARK 465     SER B   110                                                      
REMARK 465     SER B   111                                                      
REMARK 465     ALA B   112                                                      
REMARK 465     ASN B   113                                                      
REMARK 465     GLU B   114                                                      
REMARK 465     GLN B   115                                                      
REMARK 465     ALA B   116                                                      
REMARK 465     VAL B   117                                                      
REMARK 465     GLN B   118                                                      
REMARK 465     MET D   -22                                                      
REMARK 465     GLY D   -21                                                      
REMARK 465     SER D   -20                                                      
REMARK 465     SER D   -19                                                      
REMARK 465     HIS D   -18                                                      
REMARK 465     HIS D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     SER D   -12                                                      
REMARK 465     GLN D   -11                                                      
REMARK 465     ASP D   -10                                                      
REMARK 465     PRO D    -9                                                      
REMARK 465     THR D    -8                                                      
REMARK 465     THR D    -7                                                      
REMARK 465     VAL D    -6                                                      
REMARK 465     LYS D    -5                                                      
REMARK 465     LEU D    -4                                                      
REMARK 465     GLN D    -3                                                      
REMARK 465     ALA D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     PHE D     0                                                      
REMARK 465     LYS D   117                                                      
REMARK 465     LEU D   118                                                      
REMARK 465     THR D   119                                                      
REMARK 465     GLU D   120                                                      
REMARK 465     ALA D   121                                                      
REMARK 465     ASP D   122                                                      
REMARK 465     LEU D   123                                                      
REMARK 465     GLN D   124                                                      
REMARK 465     TYR D   125                                                      
REMARK 465     GLY D   126                                                      
REMARK 465     TYR D   127                                                      
REMARK 465     GLY D   128                                                      
REMARK 465     GLY D   129                                                      
REMARK 465     VAL D   130                                                      
REMARK 465     ASP D   131                                                      
REMARK 465     MET D   132                                                      
REMARK 465     ASN D   133                                                      
REMARK 465     GLU D   134                                                      
REMARK 465     ILE D   160                                                      
REMARK 465     ARG D   161                                                      
REMARK 465     MET D   162                                                      
REMARK 465     LEU D   163                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A 142    CG1  CG2                                            
REMARK 470     ASP A 143    CG   OD1  OD2                                       
REMARK 470     GLN A 145    CG   CD   OE1  NE2                                  
REMARK 470     ILE A 147    CG1  CG2  CD1                                       
REMARK 470     GLN A 203    CG   CD   OE1  NE2                                  
REMARK 470     ARG B  80    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B  82    CG   OD1  OD2                                       
REMARK 470     ASP B  83    CG   OD1  OD2                                       
REMARK 470     THR B  84    OG1  CG2                                            
REMARK 470     PHE B  85    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B  98    CG   CD   OE1  OE2                                  
REMARK 470     GLN C  51    CG   CD   OE1  NE2                                  
REMARK 470     PHE C  52    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU C  54    CG   CD   OE1  OE2                                  
REMARK 470     ASN C  55    CG   OD1  ND2                                       
REMARK 470     GLU C  56    CG   CD   OE1  OE2                                  
REMARK 470     VAL D  30    CG1  CG2                                            
REMARK 470     GLU D  80    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  81    CG   CD   OE1  OE2                                  
REMARK 470     GLN D  82    CG   CD   OE1  NE2                                  
REMARK 470     VAL D  83    CG1  CG2                                            
REMARK 470     LEU D 144    CG   CD1  CD2                                       
REMARK 470     MET D 151    CG   SD   CE                                        
REMARK 470     GLU D 153    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 156    CG   CD   OE1  NE2                                  
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   OG   SER A    68     O    ARG A   113              2.02            
REMARK 500   NH1  ARG A   120     O    HIS A   125              2.11            
REMARK 500   OD2  ASP A   179     NZ   LYS D     4              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 154   C   -  N   -  CA  ANGL. DEV. = -15.0 DEGREES          
REMARK 500    PRO B  39   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
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    ARG A  69       21.82    -67.51                                   
REMARK 500    ARG A  79       47.75   -103.98                                   
REMARK 500    SER A 111     -162.30   -116.96                                   
REMARK 500    HIS B  10       75.06     48.99                                   
REMARK 500    ALA B  71       66.53   -155.21                                   
REMARK 500    ALA B  81     -147.28   -126.85                                   
REMARK 500    GLN D  82       72.18   -150.71                                   
REMARK 500    LEU D  84      -69.22     58.62                                   
REMARK 500    ALA D 157       23.28    -69.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4WQO A    1   213  UNP    P40337   VHL_HUMAN        1    213             
DBREF  4WQO B    1   118  UNP    Q15370   ELOB_HUMAN       1    118             
DBREF  4WQO C   17   112  UNP    Q15369   ELOC_HUMAN      17    112             
DBREF  4WQO D    1   163  UNP    Q13617   CUL2_HUMAN      20    182             
SEQADV 4WQO MET A  -19  UNP  P40337              INITIATING METHIONINE          
SEQADV 4WQO GLY A  -18  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO SER A  -17  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO SER A  -16  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO HIS A  -15  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO HIS A  -14  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO HIS A  -13  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO HIS A  -12  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO HIS A  -11  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO HIS A  -10  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO SER A   -9  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO SER A   -8  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO GLY A   -7  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO LEU A   -6  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO VAL A   -5  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO PRO A   -4  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO ARG A   -3  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO GLY A   -2  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO SER A   -1  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO HIS A    0  UNP  P40337              EXPRESSION TAG                 
SEQADV 4WQO MET D  -22  UNP  Q13617              INITIATING METHIONINE          
SEQADV 4WQO GLY D  -21  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO SER D  -20  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO SER D  -19  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO HIS D  -18  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO HIS D  -17  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO HIS D  -16  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO HIS D  -15  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO HIS D  -14  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO HIS D  -13  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO SER D  -12  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO GLN D  -11  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO ASP D  -10  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO PRO D   -9  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO THR D   -8  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO THR D   -7  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO VAL D   -6  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO LYS D   -5  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO LEU D   -4  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO GLN D   -3  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO ALA D   -2  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO GLY D   -1  UNP  Q13617              EXPRESSION TAG                 
SEQADV 4WQO PHE D    0  UNP  Q13617              EXPRESSION TAG                 
SEQRES   1 A  233  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  233  LEU VAL PRO ARG GLY SER HIS MET PRO ARG ARG ALA GLU          
SEQRES   3 A  233  ASN TRP ASP GLU ALA GLU VAL GLY ALA GLU GLU ALA GLY          
SEQRES   4 A  233  VAL GLU GLU TYR GLY PRO GLU GLU ASP GLY GLY GLU GLU          
SEQRES   5 A  233  SER GLY ALA GLU GLU SER GLY PRO GLU GLU SER GLY PRO          
SEQRES   6 A  233  GLU GLU LEU GLY ALA GLU GLU GLU MET GLU ALA GLY ARG          
SEQRES   7 A  233  PRO ARG PRO VAL LEU ARG SER VAL ASN SER ARG GLU PRO          
SEQRES   8 A  233  SER GLN VAL ILE PHE CYS ASN ARG SER PRO ARG VAL VAL          
SEQRES   9 A  233  LEU PRO VAL TRP LEU ASN PHE ASP GLY GLU PRO GLN PRO          
SEQRES  10 A  233  TYR PRO THR LEU PRO PRO GLY THR GLY ARG ARG ILE HIS          
SEQRES  11 A  233  SER TYR ARG GLY HIS LEU TRP LEU PHE ARG ASP ALA GLY          
SEQRES  12 A  233  THR HIS ASP GLY LEU LEU VAL ASN GLN THR GLU LEU PHE          
SEQRES  13 A  233  VAL PRO SER LEU ASN VAL ASP GLY GLN PRO ILE PHE ALA          
SEQRES  14 A  233  ASN ILE THR LEU PRO VAL TYR THR LEU LYS GLU ARG CYS          
SEQRES  15 A  233  LEU GLN VAL VAL ARG SER LEU VAL LYS PRO GLU ASN TYR          
SEQRES  16 A  233  ARG ARG LEU ASP ILE VAL ARG SER LEU TYR GLU ASP LEU          
SEQRES  17 A  233  GLU ASP HIS PRO ASN VAL GLN LYS ASP LEU GLU ARG LEU          
SEQRES  18 A  233  THR GLN GLU ARG ILE ALA HIS GLN ARG MET GLY ASP              
SEQRES   1 B  118  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 B  118  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 B  118  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 B  118  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 B  118  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 B  118  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 B  118  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CYS ILE GLU          
SEQRES   8 B  118  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
SEQRES   9 B  118  PRO GLN ASP SER GLY SER SER ALA ASN GLU GLN ALA VAL          
SEQRES  10 B  118  GLN                                                          
SEQRES   1 C   96  MET TYR VAL LYS LEU ILE SER SER ASP GLY HIS GLU PHE          
SEQRES   2 C   96  ILE VAL LYS ARG GLU HIS ALA LEU THR SER GLY THR ILE          
SEQRES   3 C   96  LYS ALA MET LEU SER GLY PRO GLY GLN PHE ALA GLU ASN          
SEQRES   4 C   96  GLU THR ASN GLU VAL ASN PHE ARG GLU ILE PRO SER HIS          
SEQRES   5 C   96  VAL LEU SER LYS VAL CYS MET TYR PHE THR TYR LYS VAL          
SEQRES   6 C   96  ARG TYR THR ASN SER SER THR GLU ILE PRO GLU PHE PRO          
SEQRES   7 C   96  ILE ALA PRO GLU ILE ALA LEU GLU LEU LEU MET ALA ALA          
SEQRES   8 C   96  ASN PHE LEU ASP CYS                                          
SEQRES   1 D  186  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 D  186  PRO THR THR VAL LYS LEU GLN ALA GLY PHE MET SER LEU          
SEQRES   3 D  186  LYS PRO ARG VAL VAL ASP PHE ASP GLU THR TRP ASN LYS          
SEQRES   4 D  186  LEU LEU THR THR ILE LYS ALA VAL VAL MET LEU GLU TYR          
SEQRES   5 D  186  VAL GLU ARG ALA THR TRP ASN ASP ARG PHE SER ASP ILE          
SEQRES   6 D  186  TYR ALA LEU CYS VAL ALA TYR PRO GLU PRO LEU GLY GLU          
SEQRES   7 D  186  ARG LEU TYR THR GLU THR LYS ILE PHE LEU GLU ASN HIS          
SEQRES   8 D  186  VAL ARG HIS LEU HIS LYS ARG VAL LEU GLU SER GLU GLU          
SEQRES   9 D  186  GLN VAL LEU VAL MET TYR HIS ARG TYR TRP GLU GLU TYR          
SEQRES  10 D  186  SER LYS GLY ALA ASP TYR MET ASP CYS LEU TYR ARG TYR          
SEQRES  11 D  186  LEU ASN THR GLN PHE ILE LYS LYS ASN LYS LEU THR GLU          
SEQRES  12 D  186  ALA ASP LEU GLN TYR GLY TYR GLY GLY VAL ASP MET ASN          
SEQRES  13 D  186  GLU PRO LEU MET GLU ILE GLY GLU LEU ALA LEU ASP MET          
SEQRES  14 D  186  TRP ARG LYS LEU MET VAL GLU PRO LEU GLN ALA ILE LEU          
SEQRES  15 D  186  ILE ARG MET LEU                                              
HELIX    1 AA1 THR A  157  VAL A  170  1                                  14    
HELIX    2 AA2 LYS A  171  LEU A  178  5                                   8    
HELIX    3 AA3 SER A  183  ASP A  190  1                                   8    
HELIX    4 AA4 ASN A  193  ALA A  207  1                                  15    
HELIX    5 AA5 THR B   23  LYS B   36  1                                  14    
HELIX    6 AA6 PRO B   38  ASP B   40  5                                   3    
HELIX    7 AA7 PRO B  100  LYS B  104  5                                   5    
HELIX    8 AA8 ARG C   33  LEU C   37  1                                   5    
HELIX    9 AA9 SER C   39  LEU C   46  1                                   8    
HELIX   10 AB1 PRO C   66  THR C   84  1                                  19    
HELIX   11 AB2 ALA C   96  GLU C   98  5                                   3    
HELIX   12 AB3 ILE C   99  ASP C  111  1                                  13    
HELIX   13 AB4 ASP D    9  MET D   26  1                                  18    
HELIX   14 AB5 GLU D   31  ALA D   48  1                                  18    
HELIX   15 AB6 LEU D   53  GLU D   78  1                                  26    
HELIX   16 AB7 LEU D   84  TYR D  105  1                                  22    
HELIX   17 AB8 TYR D  105  ILE D  113  1                                   9    
HELIX   18 AB9 GLU D  138  ALA D  157  1                                  20    
SHEET    1 AA1 4 GLY A 106  TYR A 112  0                                        
SHEET    2 AA1 4 PRO A  71  ARG A  79 -1  N  VAL A  74   O  ILE A 109           
SHEET    3 AA1 4 ILE A 147  THR A 152  1  O  ILE A 151   N  CYS A  77           
SHEET    4 AA1 4 LEU A 129  VAL A 130 -1  N  LEU A 129   O  THR A 152           
SHEET    1 AA2 3 PRO A  95  PRO A  97  0                                        
SHEET    2 AA2 3 VAL A  84  LEU A  89 -1  N  TRP A  88   O  GLN A  96           
SHEET    3 AA2 3 LEU A 116  ASP A 121 -1  O  LEU A 118   N  VAL A  87           
SHEET    1 AA3 7 GLN B  42  TYR B  45  0                                        
SHEET    2 AA3 7 ALA B  73  PHE B  79 -1  O  GLY B  76   N  TYR B  45           
SHEET    3 AA3 7 ASP B   2  ARG B   8  1  N  MET B   6   O  VAL B  75           
SHEET    4 AA3 7 THR B  12  LYS B  19 -1  O  ALA B  18   N  VAL B   3           
SHEET    5 AA3 7 GLU C  28  LYS C  32  1  O  ILE C  30   N  THR B  13           
SHEET    6 AA3 7 TYR C  18  ILE C  22 -1  N  LEU C  21   O  PHE C  29           
SHEET    7 AA3 7 GLU C  59  ASN C  61  1  O  VAL C  60   N  ILE C  22           
CISPEP   1 GLY C   48    PRO C   49          0        -3.41                     
CISPEP   2 PRO C   49    GLY C   50          0        -8.09                     
CISPEP   3 TYR D   49    PRO D   50          0        -5.54                     
CRYST1  108.278  108.278  213.768  90.00  90.00 120.00 P 32 2 1      6          
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      0.009235  0.005332  0.000000        0.00000                         
SCALE2      0.000000  0.010664  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004678        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system