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Database: PDB
Entry: 6M91
LinkDB: 6M91
Original site: 6M91 
HEADER    LIGASE                                  22-AUG-18   6M91              
TITLE     MONOPHOSPHORYLATED PSER33 B-CATENIN PEPTIDE, B-TRCP/SKP1, NRX-103094  
TITLE    2 TERNARY COMPLEX                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: F-BOX/WD REPEAT-CONTAINING PROTEIN 1A;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: E3RSIKAPPAB,EPIDIDYMIS TISSUE PROTEIN LI 2A,F-BOX AND WD    
COMPND   5 REPEATS PROTEIN BETA-TRCP,PIKAPPABALPHA-E3 RECEPTOR SUBUNIT;         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: S-PHASE KINASE-ASSOCIATED PROTEIN 1;                       
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: CYCLIN-A/CDK2-ASSOCIATED PROTEIN P19,P19A,ORGAN OF CORTI    
COMPND  11 PROTEIN 2,OCP-2,ORGAN OF CORTI PROTEIN II,OCP-II,RNA POLYMERASE II   
COMPND  12 ELONGATION FACTOR-LIKE PROTEIN,SIII,TRANSCRIPTION ELONGATION FACTOR B
COMPND  13 POLYPEPTIDE 1-LIKE,P19SKP1;                                          
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: CATENIN BETA-1;                                            
COMPND  17 CHAIN: C;                                                            
COMPND  18 SYNONYM: BETA-CATENIN;                                               
COMPND  19 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: BTRC, BTRCP, FBW1A, FBXW1A;                                    
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: SKP1, EMC19, OCP2, SKP1A, TCEB1L;                              
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606                                                 
KEYWDS    UBIQUITIN MOLECULAR GLUE ENHANCER, LIGASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.R.SIMONETTA,M.C.CLIFTON,R.L.WALTER,G.M.RANIERI,J.J.CARTER           
REVDAT   2   10-APR-19 6M91    1       JRNL                                     
REVDAT   1   03-APR-19 6M91    0                                                
JRNL        AUTH   K.R.SIMONETTA,J.TAYGERLY,K.BOYLE,S.E.BASHAM,C.PADOVANI,      
JRNL        AUTH 2 Y.LOU,T.J.CUMMINS,S.L.YUNG,S.K.VON SOLY,F.KAYSER,J.KURIYAN,  
JRNL        AUTH 3 M.RAPE,M.CARDOZO,M.A.GALLOP,N.F.BENCE,P.A.BARSANTI,A.SAHA    
JRNL        TITL   PROSPECTIVE DISCOVERY OF SMALL MOLECULE ENHANCERS OF AN E3   
JRNL        TITL 2 LIGASE-SUBSTRATE INTERACTION.                                
JRNL        REF    NAT COMMUN                    V.  10  1402 2019              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   30926793                                                     
JRNL        DOI    10.1038/S41467-019-09358-9                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.13_2998                                     
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.06                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 33155                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.760                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1245                            
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 44.0705 -  4.9902    0.99     3533   135  0.1713 0.2008        
REMARK   3     2  4.9902 -  3.9616    1.00     3533   142  0.1577 0.1717        
REMARK   3     3  3.9616 -  3.4611    1.00     3573   127  0.1898 0.2140        
REMARK   3     4  3.4611 -  3.1447    1.00     3578   131  0.2104 0.2285        
REMARK   3     5  3.1447 -  2.9194    1.00     3536   140  0.2291 0.2791        
REMARK   3     6  2.9194 -  2.7473    1.00     3536   144  0.2370 0.2754        
REMARK   3     7  2.7473 -  2.6097    1.00     3560   140  0.2589 0.3018        
REMARK   3     8  2.6097 -  2.4961    0.99     3519   140  0.2716 0.3113        
REMARK   3     9  2.4961 -  2.4000    0.99     3542   146  0.3156 0.3325        
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)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.770           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 68.42                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 84.33                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 138 THROUGH 252 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  33.5083 -43.5830 -11.5324              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0527 T22:   0.7475                                     
REMARK   3      T33:   0.9171 T12:   0.3794                                     
REMARK   3      T13:   0.0560 T23:  -0.0382                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3314 L22:   1.9275                                     
REMARK   3      L33:   0.4557 L12:  -0.1409                                     
REMARK   3      L13:   0.4767 L23:   0.5512                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0444 S12:   0.1873 S13:   0.4129                       
REMARK   3      S21:  -0.0958 S22:  -0.1610 S23:   0.0946                       
REMARK   3      S31:   0.0859 S32:   0.1920 S33:   0.1004                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 253 THROUGH 548 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.4421 -13.4314  -1.6466              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7374 T22:   0.3676                                     
REMARK   3      T33:   0.6135 T12:   0.1018                                     
REMARK   3      T13:  -0.0753 T23:   0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2216 L22:   2.2841                                     
REMARK   3      L33:   2.5514 L12:  -0.6705                                     
REMARK   3      L13:  -0.0892 L23:  -0.1586                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2394 S12:   0.1515 S13:  -0.2347                       
REMARK   3      S21:  -0.0171 S22:  -0.1141 S23:  -0.3180                       
REMARK   3      S31:   0.1882 S32:   0.0022 S33:  -0.1131                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 58 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   8.8164 -69.4707  -9.2563              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9732 T22:   1.4715                                     
REMARK   3      T33:   0.9711 T12:   0.1775                                     
REMARK   3      T13:   0.3763 T23:   0.0548                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8469 L22:   1.3975                                     
REMARK   3      L33:   1.5140 L12:  -0.3228                                     
REMARK   3      L13:  -0.5916 L23:   0.6480                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0633 S12:  -0.5873 S13:   0.1188                       
REMARK   3      S21:   0.5921 S22:  -0.3435 S23:   0.7915                       
REMARK   3      S31:   0.0191 S32:  -1.2736 S33:   0.3817                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 59 THROUGH 78 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3344 -59.5611   4.4838              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2485 T22:   1.3238                                     
REMARK   3      T33:   0.8304 T12:   0.1841                                     
REMARK   3      T13:   0.3653 T23:  -0.1548                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1735 L22:   2.2535                                     
REMARK   3      L33:   4.0614 L12:   0.4425                                     
REMARK   3      L13:   1.5588 L23:  -1.4518                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7452 S12:  -0.1302 S13:   0.4563                       
REMARK   3      S21:   0.1995 S22:  -1.3596 S23:   0.3398                       
REMARK   3      S31:  -0.4309 S32:  -0.6669 S33:   0.4504                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 79 THROUGH 139 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  34.0029 -57.5171  -5.9798              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1124 T22:   0.8267                                     
REMARK   3      T33:   0.6264 T12:   0.4440                                     
REMARK   3      T13:   0.1004 T23:   0.0125                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7483 L22:   3.2679                                     
REMARK   3      L33:   1.7221 L12:   1.2966                                     
REMARK   3      L13:   0.5666 L23:   0.0759                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0251 S12:  -0.3329 S13:   0.1556                       
REMARK   3      S21:   0.9104 S22:  -0.0057 S23:  -0.2069                       
REMARK   3      S31:  -0.2824 S32:  -0.3690 S33:   0.1063                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 29 THROUGH 38 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   7.0595  -0.2166   3.9811              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9790 T22:   0.5074                                     
REMARK   3      T33:   0.5238 T12:   0.1247                                     
REMARK   3      T13:  -0.0403 T23:  -0.0343                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0224 L22:   1.5806                                     
REMARK   3      L33:   5.6932 L12:  -1.1730                                     
REMARK   3      L13:   0.1284 L23:  -1.2510                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2254 S12:  -0.4823 S13:   0.6415                       
REMARK   3      S21:   0.4935 S22:  -0.5310 S23:   0.0272                       
REMARK   3      S31:  -0.5421 S32:  -0.2353 S33:   0.1965                       
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 6M91 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000236372.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAY-15                          
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               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33157                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.063                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.232                              
REMARK 200  R MERGE                    (I) : 0.04400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.6900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.25                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.39100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.990                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 4000 0.1M BTP PH 5.5, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290                                                                      
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       37.32000            
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       74.64000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A   218                                                      
REMARK 465     ASN A   219                                                      
REMARK 465     LYS A   220                                                      
REMARK 465     PRO A   221                                                      
REMARK 465     PRO A   222                                                      
REMARK 465     ASP A   223                                                      
REMARK 465     GLY A   224                                                      
REMARK 465     ASN A   225                                                      
REMARK 465     ALA A   226                                                      
REMARK 465     ASP A   549                                                      
REMARK 465     PRO A   550                                                      
REMARK 465     ALA A   551                                                      
REMARK 465     ALA A   552                                                      
REMARK 465     GLN A   553                                                      
REMARK 465     ALA A   554                                                      
REMARK 465     GLU A   555                                                      
REMARK 465     PRO A   556                                                      
REMARK 465     PRO A   557                                                      
REMARK 465     ARG A   558                                                      
REMARK 465     SER A   559                                                      
REMARK 465     PRO A   560                                                      
REMARK 465     SER A   561                                                      
REMARK 465     ARG A   562                                                      
REMARK 465     THR A   563                                                      
REMARK 465     TYR A   564                                                      
REMARK 465     THR A   565                                                      
REMARK 465     TYR A   566                                                      
REMARK 465     ILE A   567                                                      
REMARK 465     SER A   568                                                      
REMARK 465     ARG A   569                                                      
REMARK 465     ASP B    61                                                      
REMARK 465     ASP B    62                                                      
REMARK 465     PRO B    63                                                      
REMARK 465     PRO B    64                                                      
REMARK 465     ASP B    65                                                      
REMARK 465     ASP B    66                                                      
REMARK 465     GLN B   140                                                      
REMARK 465     TRP B   141                                                      
REMARK 465     CYS B   142                                                      
REMARK 465     GLU B   143                                                      
REMARK 465     GLU B   144                                                      
REMARK 465     LYS B   145                                                      
REMARK 465     CYS C    16                                                      
REMARK 465     ASP C    17                                                      
REMARK 465     ARG C    18                                                      
REMARK 465     LYS C    19                                                      
REMARK 465     ALA C    20                                                      
REMARK 465     ALA C    21                                                      
REMARK 465     VAL C    22                                                      
REMARK 465     SER C    23                                                      
REMARK 465     HIS C    24                                                      
REMARK 465     TRP C    25                                                      
REMARK 465     GLN C    26                                                      
REMARK 465     GLN C    27                                                      
REMARK 465     GLN C    28                                                      
REMARK 465     ALA C    39                                                      
REMARK 465     THR C    40                                                      
REMARK 465     THR C    41                                                      
REMARK 465     THR C    42                                                      
REMARK 465     ALA C    43                                                      
REMARK 465     PRO C    44                                                      
REMARK 465     SER C    45                                                      
REMARK 465     LEU C    46                                                      
REMARK 465     SER C    47                                                      
REMARK 465     GLY C    48                                                      
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     SER A 138    OG                                                  
REMARK 470     LYS A 167    CG   CD   CE   NZ                                   
REMARK 470     GLU A 208    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 214    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 244    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 251    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 254    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 298    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 300    CG   CD   CE   NZ                                   
REMARK 470     ASN A 357    CG   OD1  ND2                                       
REMARK 470     LYS A 430    CG   CD   CE   NZ                                   
REMARK 470     GLU A 471    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 504    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO B   2    CG   CD                                             
REMARK 470     ILE B   4    CG1  CG2  CD1                                       
REMARK 470     LYS B   5    CG   CD   CE   NZ                                   
REMARK 470     GLU B  15    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  17    CG   OD1  OD2                                       
REMARK 470     GLU B  19    CG   CD   OE1  OE2                                  
REMARK 470     ILE B  20    CG1  CG2  CD1                                       
REMARK 470     LYS B  28    CG   CD   CE   NZ                                   
REMARK 470     LYS B  50    CG   CD   CE   NZ                                   
REMARK 470     LYS B  51    CG   CD   CE   NZ                                   
REMARK 470     LYS B  60    CG   CD   CE   NZ                                   
REMARK 470     LYS B  76    CG   CD   CE   NZ                                   
REMARK 470     LYS B  95    CG   CD   CE   NZ                                   
REMARK 470     LYS B 103    CG   CD   CE   NZ                                   
REMARK 470     LYS B 110    CG   CD   CE   NZ                                   
REMARK 470     GLU B 115    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 119    CG   CD   CE   NZ                                   
REMARK 470     GLU B 129    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 130    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 136    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 137    CG   CD   CE   NZ                                   
REMARK 470     SER C  29    OG                                                  
REMARK 470     TYR C  30    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD2  ASP A   154     NH2  ARG A   390     3544     2.13            
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    THR A 266      -79.21   -119.00                                   
REMARK 500    ASN A 287        2.95     88.00                                   
REMARK 500    ASP A 316     -159.36   -130.71                                   
REMARK 500    SER A 327        7.22     80.06                                   
REMARK 500    HIS A 345      -54.90   -163.75                                   
REMARK 500    ASN A 356      137.35   -175.63                                   
REMARK 500    ARG A 367        7.34     83.22                                   
REMARK 500    ASP A 440     -113.39     60.30                                   
REMARK 500    ARG A 464      137.22   -172.04                                   
REMARK 500    ASP A 479     -149.26   -123.48                                   
REMARK 500    LEU C  31       13.87    -68.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue J97 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 101                  
DBREF  6M91 A  139   569  UNP    Q9Y297   FBW1A_HUMAN    175    605             
DBREF  6M91 B    2   145  UNP    P63208   SKP1_HUMAN       2    163             
DBREF  6M91 C   17    48  UNP    P35222   CTNB1_HUMAN     17     48             
SEQADV 6M91 SER A  138  UNP  Q9Y297              EXPRESSION TAG                 
SEQADV 6M91     B       UNP  P63208    ASP    37 DELETION                       
SEQADV 6M91     B       UNP  P63208    ASP    38 DELETION                       
SEQADV 6M91     B       UNP  P63208    GLU    39 DELETION                       
SEQADV 6M91     B       UNP  P63208    GLY    40 DELETION                       
SEQADV 6M91     B       UNP  P63208    ASP    41 DELETION                       
SEQADV 6M91     B       UNP  P63208    ASP    42 DELETION                       
SEQADV 6M91     B       UNP  P63208    PRO    71 DELETION                       
SEQADV 6M91     B       UNP  P63208    PRO    72 DELETION                       
SEQADV 6M91     B       UNP  P63208    GLU    73 DELETION                       
SEQADV 6M91     B       UNP  P63208    ASP    74 DELETION                       
SEQADV 6M91     B       UNP  P63208    ASP    75 DELETION                       
SEQADV 6M91     B       UNP  P63208    GLU    76 DELETION                       
SEQADV 6M91     B       UNP  P63208    ASN    77 DELETION                       
SEQADV 6M91     B       UNP  P63208    LYS    78 DELETION                       
SEQADV 6M91     B       UNP  P63208    GLU    79 DELETION                       
SEQADV 6M91     B       UNP  P63208    LYS    80 DELETION                       
SEQADV 6M91     B       UNP  P63208    ARG    81 DELETION                       
SEQADV 6M91     B       UNP  P63208    THR    82 DELETION                       
SEQADV 6M91 CYS C   16  UNP  P35222              EXPRESSION TAG                 
SEQADV 6M91 ALA C   37  UNP  P35222    SER    37 CONFLICT                       
SEQRES   1 A  432  SER MET LEU GLN ARG ASP PHE ILE THR ALA LEU PRO ALA          
SEQRES   2 A  432  ARG GLY LEU ASP HIS ILE ALA GLU ASN ILE LEU SER TYR          
SEQRES   3 A  432  LEU ASP ALA LYS SER LEU CYS ALA ALA GLU LEU VAL CYS          
SEQRES   4 A  432  LYS GLU TRP TYR ARG VAL THR SER ASP GLY MET LEU TRP          
SEQRES   5 A  432  LYS LYS LEU ILE GLU ARG MET VAL ARG THR ASP SER LEU          
SEQRES   6 A  432  TRP ARG GLY LEU ALA GLU ARG ARG GLY TRP GLY GLN TYR          
SEQRES   7 A  432  LEU PHE LYS ASN LYS PRO PRO ASP GLY ASN ALA PRO PRO          
SEQRES   8 A  432  ASN SER PHE TYR ARG ALA LEU TYR PRO LYS ILE ILE GLN          
SEQRES   9 A  432  ASP ILE GLU THR ILE GLU SER ASN TRP ARG CYS GLY ARG          
SEQRES  10 A  432  HIS SER LEU GLN ARG ILE HIS CYS ARG SER GLU THR SER          
SEQRES  11 A  432  LYS GLY VAL TYR CYS LEU GLN TYR ASP ASP GLN LYS ILE          
SEQRES  12 A  432  VAL SER GLY LEU ARG ASP ASN THR ILE LYS ILE TRP ASP          
SEQRES  13 A  432  LYS ASN THR LEU GLU CYS LYS ARG ILE LEU THR GLY HIS          
SEQRES  14 A  432  THR GLY SER VAL LEU CYS LEU GLN TYR ASP GLU ARG VAL          
SEQRES  15 A  432  ILE ILE THR GLY SER SER ASP SER THR VAL ARG VAL TRP          
SEQRES  16 A  432  ASP VAL ASN THR GLY GLU MET LEU ASN THR LEU ILE HIS          
SEQRES  17 A  432  HIS CYS GLU ALA VAL LEU HIS LEU ARG PHE ASN ASN GLY          
SEQRES  18 A  432  MET MET VAL THR CYS SER LYS ASP ARG SER ILE ALA VAL          
SEQRES  19 A  432  TRP ASP MET ALA SER PRO THR ASP ILE THR LEU ARG ARG          
SEQRES  20 A  432  VAL LEU VAL GLY HIS ARG ALA ALA VAL ASN VAL VAL ASP          
SEQRES  21 A  432  PHE ASP ASP LYS TYR ILE VAL SER ALA SER GLY ASP ARG          
SEQRES  22 A  432  THR ILE LYS VAL TRP ASN THR SER THR CYS GLU PHE VAL          
SEQRES  23 A  432  ARG THR LEU ASN GLY HIS LYS ARG GLY ILE ALA CYS LEU          
SEQRES  24 A  432  GLN TYR ARG ASP ARG LEU VAL VAL SER GLY SER SER ASP          
SEQRES  25 A  432  ASN THR ILE ARG LEU TRP ASP ILE GLU CYS GLY ALA CYS          
SEQRES  26 A  432  LEU ARG VAL LEU GLU GLY HIS GLU GLU LEU VAL ARG CYS          
SEQRES  27 A  432  ILE ARG PHE ASP ASN LYS ARG ILE VAL SER GLY ALA TYR          
SEQRES  28 A  432  ASP GLY LYS ILE LYS VAL TRP ASP LEU VAL ALA ALA LEU          
SEQRES  29 A  432  ASP PRO ARG ALA PRO ALA GLY THR LEU CYS LEU ARG THR          
SEQRES  30 A  432  LEU VAL GLU HIS SER GLY ARG VAL PHE ARG LEU GLN PHE          
SEQRES  31 A  432  ASP GLU PHE GLN ILE VAL SER SER SER HIS ASP ASP THR          
SEQRES  32 A  432  ILE LEU ILE TRP ASP PHE LEU ASN ASP PRO ALA ALA GLN          
SEQRES  33 A  432  ALA GLU PRO PRO ARG SER PRO SER ARG THR TYR THR TYR          
SEQRES  34 A  432  ILE SER ARG                                                  
SEQRES   1 B  144  PRO SER ILE LYS LEU GLN SER SER ASP GLY GLU ILE PHE          
SEQRES   2 B  144  GLU VAL ASP VAL GLU ILE ALA LYS GLN SER VAL THR ILE          
SEQRES   3 B  144  LYS THR MET LEU GLU ASP LEU GLY MET ASP PRO VAL PRO          
SEQRES   4 B  144  LEU PRO ASN VAL ASN ALA ALA ILE LEU LYS LYS VAL ILE          
SEQRES   5 B  144  GLN TRP CYS THR HIS HIS LYS ASP ASP PRO PRO ASP ASP          
SEQRES   6 B  144  ILE PRO VAL TRP ASP GLN GLU PHE LEU LYS VAL ASP GLN          
SEQRES   7 B  144  GLY THR LEU PHE GLU LEU ILE LEU ALA ALA ASN TYR LEU          
SEQRES   8 B  144  ASP ILE LYS GLY LEU LEU ASP VAL THR CYS LYS THR VAL          
SEQRES   9 B  144  ALA ASN MET ILE LYS GLY LYS THR PRO GLU GLU ILE ARG          
SEQRES  10 B  144  LYS THR PHE ASN ILE LYS ASN ASP PHE THR GLU GLU GLU          
SEQRES  11 B  144  GLU ALA GLN VAL ARG LYS GLU ASN GLN TRP CYS GLU GLU          
SEQRES  12 B  144  LYS                                                          
SEQRES   1 C   33  CYS ASP ARG LYS ALA ALA VAL SER HIS TRP GLN GLN GLN          
SEQRES   2 C   33  SER TYR LEU ASP SEP GLY ILE HIS ALA GLY ALA THR THR          
SEQRES   3 C   33  THR ALA PRO SER LEU SER GLY                                  
MODRES 6M91 SEP C   33  SER  MODIFIED RESIDUE                                   
HET    SEP  C  33      10                                                       
HET    J97  A 601      32                                                       
HET    PO4  A 602       5                                                       
HET     CL  C 101       1                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     J97 3-({4-[(2,6-DICHLOROPHENYL)SULFANYL]-2-OXO-6-                    
HETNAM   2 J97  (TRIFLUOROMETHYL)-1,2-DIHYDROPYRIDINE-3-                        
HETNAM   3 J97  CARBONYL}AMINO)BENZOIC ACID                                     
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   3  SEP    C3 H8 N O6 P                                                 
FORMUL   4  J97    C20 H11 CL2 F3 N2 O4 S                                       
FORMUL   5  PO4    O4 P 3-                                                      
FORMUL   6   CL    CL 1-                                                        
FORMUL   7  HOH   *25(H2 O)                                                     
HELIX    1 AA1 ASP A  143  ARG A  151  1                                   9    
HELIX    2 AA2 LEU A  153  SER A  162  1                                  10    
HELIX    3 AA3 ASP A  165  LEU A  174  1                                  10    
HELIX    4 AA4 CYS A  176  GLY A  186  1                                  11    
HELIX    5 AA5 MET A  187  ASP A  200  1                                  14    
HELIX    6 AA6 ASP A  200  GLY A  211  1                                  12    
HELIX    7 AA7 TRP A  212  LEU A  216  5                                   5    
HELIX    8 AA8 PRO A  228  GLY A  253  1                                  26    
HELIX    9 AA9 LEU A  497  ASP A  502  1                                   6    
HELIX   10 AB1 PRO A  506  THR A  509  5                                   4    
HELIX   11 AB2 VAL B   18  LYS B   22  1                                   5    
HELIX   12 AB3 SER B   24  ASP B   33  1                                  10    
HELIX   13 AB4 ASN B   45  HIS B   59  1                                  15    
HELIX   14 AB5 PRO B   68  LEU B   75  1                                   8    
HELIX   15 AB6 ASP B   78  ASP B   93  1                                  16    
HELIX   16 AB7 ILE B   94  LYS B  110  1                                  17    
HELIX   17 AB8 THR B  113  ASN B  122  1                                  10    
HELIX   18 AB9 THR B  128  GLU B  138  1                                  11    
SHEET    1 AA1 4 SER A 256  HIS A 261  0                                        
SHEET    2 AA1 4 THR A 540  ASP A 545 -1  O  ILE A 541   N  ILE A 260           
SHEET    3 AA1 4 GLN A 531  SER A 536 -1  N  ILE A 532   O  TRP A 544           
SHEET    4 AA1 4 VAL A 522  PHE A 527 -1  N  GLN A 526   O  VAL A 533           
SHEET    1 AA2 4 VAL A 270  TYR A 275  0                                        
SHEET    2 AA2 4 LYS A 279  LEU A 284 -1  O  VAL A 281   N  GLN A 274           
SHEET    3 AA2 4 ILE A 289  ASP A 293 -1  O  TRP A 292   N  ILE A 280           
SHEET    4 AA2 4 CYS A 299  LEU A 303 -1  O  LEU A 303   N  ILE A 289           
SHEET    1 AA3 4 VAL A 310  TYR A 315  0                                        
SHEET    2 AA3 4 VAL A 319  SER A 324 -1  O  ILE A 321   N  GLN A 314           
SHEET    3 AA3 4 THR A 328  ASP A 333 -1  O  TRP A 332   N  ILE A 320           
SHEET    4 AA3 4 MET A 339  ILE A 344 -1  O  LEU A 340   N  VAL A 331           
SHEET    1 AA4 4 VAL A 350  ASN A 356  0                                        
SHEET    2 AA4 4 MET A 359  SER A 364 -1  O  VAL A 361   N  ARG A 354           
SHEET    3 AA4 4 ILE A 369  SER A 376 -1  O  TRP A 372   N  MET A 360           
SHEET    4 AA4 4 ASP A 379  LEU A 386 -1  O  ARG A 383   N  VAL A 371           
SHEET    1 AA5 4 VAL A 393  PHE A 398  0                                        
SHEET    2 AA5 4 TYR A 402  SER A 407 -1  O  VAL A 404   N  ASP A 397           
SHEET    3 AA5 4 ILE A 412  ASN A 416 -1  O  TRP A 415   N  ILE A 403           
SHEET    4 AA5 4 PHE A 422  LEU A 426 -1  O  LEU A 426   N  ILE A 412           
SHEET    1 AA6 4 ILE A 433  ARG A 439  0                                        
SHEET    2 AA6 4 LEU A 442  SER A 447 -1  O  GLY A 446   N  CYS A 435           
SHEET    3 AA6 4 ILE A 452  ASP A 456 -1  O  TRP A 455   N  VAL A 443           
SHEET    4 AA6 4 CYS A 462  LEU A 466 -1  O  LEU A 466   N  ILE A 452           
SHEET    1 AA7 4 VAL A 473  PHE A 478  0                                        
SHEET    2 AA7 4 ARG A 482  ALA A 487 -1  O  VAL A 484   N  ARG A 477           
SHEET    3 AA7 4 LYS A 491  ASP A 496 -1  O  TRP A 495   N  ILE A 483           
SHEET    4 AA7 4 CYS A 511  VAL A 516 -1  O  LEU A 515   N  ILE A 492           
SHEET    1 AA8 3 ILE B  13  ASP B  17  0                                        
SHEET    2 AA8 3 SER B   3  SER B   8 -1  N  ILE B   4   O  VAL B  16           
SHEET    3 AA8 3 VAL B  39  LEU B  41  1  O  VAL B  39   N  GLN B   7           
LINK         C   ASP C  32                 N   SEP C  33     1555   1555  1.33  
LINK         C   SEP C  33                 N   GLY C  34     1555   1555  1.33  
CISPEP   1 ASP B   37    PRO B   38          0        -5.74                     
SITE     1 AC1 19 ARG A 330  MET A 339  THR A 342  ASN A 394                    
SITE     2 AC1 19 GLY A 408  ARG A 410  ARG A 431  GLY A 432                    
SITE     3 AC1 19 ILE A 433  ALA A 434  SER A 448  LEU A 472                    
SITE     4 AC1 19 TYR A 488  SER C  29  ASP C  32  ILE C  35                    
SITE     5 AC1 19 HIS C  36  ALA C  37   CL C 101                               
SITE     1 AC2  5 GLN A 437  ARG A 477  PHE A 478  GLN A 526                    
SITE     2 AC2  5 PHE A 527                                                     
SITE     1 AC3  1 J97 A 601                                                     
CRYST1   82.490   82.490  111.960  90.00  90.00 120.00 P 31          3          
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      0.012123  0.006999  0.000000        0.00000                         
SCALE2      0.000000  0.013998  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008932        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system