GenomeNet

Database: PDB
Entry: 4CI3
LinkDB: 4CI3
Original site: 4CI3 
HEADER    DNA BINDING PROTEIN                     05-DEC-13   4CI3              
TITLE     STRUCTURE OF THE DDB1-CRBN E3 UBIQUITIN LIGASE BOUND TO POMALIDOMIDE  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA DAMAGE-BINDING PROTEIN 1;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DDB P127 SUBUNIT, DNA DAMAGE-BINDING PROTEIN A, DDBA,       
COMPND   5 DAMAGE-SPECIFIC DNA-BINDING PROTEIN 1, HBV X-ASSOCIATED PROTEIN 1,   
COMPND   6 XAP- 1, UV-DAMAGED DNA-BINDING FACTOR, UV-DAMAGED DNA-BINDING PROTEIN
COMPND   7 1, UV-DDB 1, XPE-BINDING FACTOR, XPE-BF, XERODERMA PIGMENTOSUM GROUP 
COMPND   8 E-COMPLEMENTING PROTEIN, XPCE, DNA DAMAGE BINDING PROTEIN 1;         
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: PROTEIN CEREBLON;                                          
COMPND  12 CHAIN: B;                                                            
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DUAL;                            
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE  13 ORGANISM_COMMON: CHICKEN;                                            
SOURCE  14 ORGANISM_TAXID: 9031;                                                
SOURCE  15 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  16 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PFASTBAC DUAL                             
KEYWDS    DNA BINDING PROTEIN, DDB1, CRBN, CULLIN, E3 LIGASE, UBIQUITIN,        
KEYWDS   2 THALIDOMIDE, CONTERGAN                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.S.FISCHER,K.BOEHM,N.H.THOMA                                         
REVDAT   5   20-DEC-23 4CI3    1       REMARK LINK                              
REVDAT   4   27-MAR-19 4CI3    1       SOURCE                                   
REVDAT   3   13-AUG-14 4CI3    1       JRNL                                     
REVDAT   2   30-JUL-14 4CI3    1       JRNL                                     
REVDAT   1   16-JUL-14 4CI3    0                                                
JRNL        AUTH   E.S.FISCHER,K.BOHM,J.R.LYDEARD,H.YANG,M.B.STADLER,           
JRNL        AUTH 2 S.CAVADINI,J.NAGEL,F.SERLUCA,V.ACKER,G.M.LINGARAJU,          
JRNL        AUTH 3 R.B.TICHKULE,M.SCHEBESTA,W.C.FORRESTER,M.SCHIRLE,            
JRNL        AUTH 4 U.HASSIEPEN,J.OTTL,M.HILD,R.E.J.BECKWITH,J.W.HARPER,         
JRNL        AUTH 5 J.L.JENKINS,N.H.THOMA                                        
JRNL        TITL   STRUCTURE OF THE DDB1-CRBN E3 UBIQUITIN LIGASE IN COMPLEX    
JRNL        TITL 2 WITH THALIDOMIDE.                                            
JRNL        REF    NATURE                        V. 512    49 2014              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   25043012                                                     
JRNL        DOI    10.1038/NATURE13527                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.4                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.63                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 25108                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.212                          
REMARK   3   R VALUE            (WORKING SET)  : 0.211                          
REMARK   3   FREE R VALUE                      : 0.235                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1256                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 13                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.50                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.64                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 84.52                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2778                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2403                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2639                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2402                   
REMARK   3   BIN FREE R VALUE                        : 0.2423                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.00                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 139                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11389                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 88.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 139.2                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 10.70410                                             
REMARK   3    B22 (A**2) : 10.70410                                             
REMARK   3    B33 (A**2) : -21.40820                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.921               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.567               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.925                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 11640  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 15803  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 4005   ; 4.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 289    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1679   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 11640  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 2      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1553   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 12762  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.16                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.69                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.70                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -72.8209  -29.3981   -4.3369           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1836 T22:   -0.0740                                    
REMARK   3     T33:   -0.3040 T12:    0.1177                                    
REMARK   3     T13:   -0.0316 T23:   -0.1937                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2000 L22:    1.5445                                    
REMARK   3     L33:    0.9342 L12:    0.9528                                    
REMARK   3     L13:   -0.0998 L23:    0.1407                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0646 S12:   -0.3325 S13:   -0.0915                     
REMARK   3     S21:    0.0651 S22:   -0.0446 S23:    0.1756                     
REMARK   3     S31:   -0.1405 S32:   -0.3444 S33:   -0.0200                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -24.6365   -5.2858   -9.7386           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0235 T22:    0.0333                                    
REMARK   3     T33:   -0.2944 T12:   -0.0142                                    
REMARK   3     T13:    0.0001 T23:   -0.1266                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.4794 L22:    1.6136                                    
REMARK   3     L33:    0.5110 L12:    1.0780                                    
REMARK   3     L13:   -0.2246 L23:   -0.5907                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1828 S12:    0.3799 S13:   -0.0040                     
REMARK   3     S21:   -0.0612 S22:   -0.0382 S23:    0.3228                     
REMARK   3     S31:    0.0565 S32:   -0.2342 S33:    0.2210                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4CI3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-DEC-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290059151.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-NOV-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99997                            
REMARK 200  MONOCHROMATOR                  : SI(111) MONOCHROMATOR              
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25109                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.4                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.0500                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.31000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.910                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3EI3, CHAIN A                              
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 100 MM     
REMARK 280  NA-CACOCYLATE, 80 MM NAH2PO4, 120 MM K2HPO4, 700 MM TRI-NA          
REMARK 280  CITRATE., PH 6.5                                                    
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       91.95333            
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       45.97667            
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       45.97667            
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       91.95333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 59880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.1 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   -17                                                      
REMARK 465     HIS 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     ARG A   -10                                                      
REMARK 465     ARG A    -9                                                      
REMARK 465     LEU A    -8                                                      
REMARK 465     VAL A    -7                                                      
REMARK 465     PRO A    -6                                                      
REMARK 465     ARG A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ARG A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASP A   146                                                      
REMARK 465     ARG A   147                                                      
REMARK 465     ASP A   148                                                      
REMARK 465     ASN A   149                                                      
REMARK 465     GLU A   286                                                      
REMARK 465     LYS A   287                                                      
REMARK 465     GLU A   288                                                      
REMARK 465     GLU A   289                                                      
REMARK 465     GLN A   290                                                      
REMARK 465     MET A   291                                                      
REMARK 465     ASP A   292                                                      
REMARK 465     GLY A   293                                                      
REMARK 465     THR A   294                                                      
REMARK 465     VAL A   295                                                      
REMARK 465     THR A   296                                                      
REMARK 465     LEU A   297                                                      
REMARK 465     LYS A   298                                                      
REMARK 465     ASP A   299                                                      
REMARK 465     SER A   772                                                      
REMARK 465     SER A   773                                                      
REMARK 465     SER A   774                                                      
REMARK 465     THR A   775                                                      
REMARK 465     ALA A   776                                                      
REMARK 465     PRO A   777                                                      
REMARK 465     HIS A   778                                                      
REMARK 465     GLU A   779                                                      
REMARK 465     THR A   780                                                      
REMARK 465     SER A   781                                                      
REMARK 465     PHE A   782                                                      
REMARK 465     GLY A   783                                                      
REMARK 465     ASP A   980                                                      
REMARK 465     SER A   981                                                      
REMARK 465     ALA A   982                                                      
REMARK 465     ALA A   983                                                      
REMARK 465     GLN A  1015                                                      
REMARK 465     ASN A  1016                                                      
REMARK 465     LEU A  1017                                                      
REMARK 465     GLY A  1018                                                      
REMARK 465     GLU A  1019                                                      
REMARK 465     THR A  1020                                                      
REMARK 465     SER A  1021                                                      
REMARK 465     TYR A  1114                                                      
REMARK 465     ASP A  1115                                                      
REMARK 465     ASP A  1116                                                      
REMARK 465     GLY A  1117                                                      
REMARK 465     SER A  1118                                                      
REMARK 465     GLY A  1119                                                      
REMARK 465     MET A  1120                                                      
REMARK 465     MET B   -23                                                      
REMARK 465     ASP B   -22                                                      
REMARK 465     TRP B   -21                                                      
REMARK 465     SER B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     PRO B   -18                                                      
REMARK 465     GLN B   -17                                                      
REMARK 465     PHE B   -16                                                      
REMARK 465     GLU B   -15                                                      
REMARK 465     LYS B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     ALA B   -12                                                      
REMARK 465     VAL B   -11                                                      
REMARK 465     ASP B   -10                                                      
REMARK 465     GLU B    -9                                                      
REMARK 465     ASN B    -8                                                      
REMARK 465     LEU B    -7                                                      
REMARK 465     TYR B    -6                                                      
REMARK 465     PHE B    -5                                                      
REMARK 465     GLN B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     ARG B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     ASP B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     ARG B    10                                                      
REMARK 465     ARG B    11                                                      
REMARK 465     ASN B    12                                                      
REMARK 465     MET B    13                                                      
REMARK 465     GLY B    14                                                      
REMARK 465     ASN B    15                                                      
REMARK 465     PRO B    16                                                      
REMARK 465     PRO B    17                                                      
REMARK 465     PRO B    18                                                      
REMARK 465     PRO B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     PRO B    21                                                      
REMARK 465     ALA B    22                                                      
REMARK 465     GLU B    23                                                      
REMARK 465     SER B    24                                                      
REMARK 465     GLU B    25                                                      
REMARK 465     GLU B    26                                                      
REMARK 465     GLU B    27                                                      
REMARK 465     ASP B    28                                                      
REMARK 465     ASP B    29                                                      
REMARK 465     ASN B    30                                                      
REMARK 465     GLU B    31                                                      
REMARK 465     MET B    32                                                      
REMARK 465     GLU B    33                                                      
REMARK 465     VAL B    34                                                      
REMARK 465     GLU B    35                                                      
REMARK 465     ASP B    36                                                      
REMARK 465     GLN B    37                                                      
REMARK 465     ASP B    38                                                      
REMARK 465     GLY B    39                                                      
REMARK 465     LYS B    40                                                      
REMARK 465     GLU B    41                                                      
REMARK 465     ALA B    42                                                      
REMARK 465     GLU B    43                                                      
REMARK 465     LYS B    44                                                      
REMARK 465     PRO B    45                                                      
REMARK 465     ASN B    46                                                      
REMARK 465     PHE B   209                                                      
REMARK 465     PRO B   210                                                      
REMARK 465     SER B   211                                                      
REMARK 465     SER B   212                                                      
REMARK 465     LYS B   213                                                      
REMARK 465     PRO B   214                                                      
REMARK 465     LYS B   215                                                      
REMARK 465     VAL B   216                                                      
REMARK 465     TRP B   217                                                      
REMARK 465     GLN B   218                                                      
REMARK 465     ASP B   219                                                      
REMARK 465     ILE B   428                                                      
REMARK 465     PRO B   429                                                      
REMARK 465     GLU B   430                                                      
REMARK 465     ALA B   431                                                      
REMARK 465     GLU B   432                                                      
REMARK 465     ASP B   433                                                      
REMARK 465     GLU B   434                                                      
REMARK 465     LEU B   435                                                      
REMARK 465     GLY B   436                                                      
REMARK 465     HIS B   437                                                      
REMARK 465     ASP B   438                                                      
REMARK 465     ARG B   439                                                      
REMARK 465     SER B   440                                                      
REMARK 465     PRO B   441                                                      
REMARK 465     LEU B   442                                                      
REMARK 465     LEU B   443                                                      
REMARK 465     CYS B   444                                                      
REMARK 465     LEU B   445                                                      
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     GLU A  27    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  70    CG   CD   CE   NZ                                   
REMARK 470     LYS A  74    CG   CD   CE   NZ                                   
REMARK 470     GLU A  96    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 114    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 127    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 145    CG   CD1  CD2                                       
REMARK 470     LYS A 150    CG   CD   CE   NZ                                   
REMARK 470     LYS A 153    CG   CD   CE   NZ                                   
REMARK 470     ARG A 158    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 174    CG   CD   OE1  NE2                                  
REMARK 470     VAL A 195    CG1  CG2                                            
REMARK 470     ARG A 198    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 199    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 200    CG   CD   CE   NZ                                   
REMARK 470     LYS A 208    CG   CD   CE   NZ                                   
REMARK 470     GLU A 224    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 243    CG   OD1  OD2                                       
REMARK 470     LYS A 254    CG   CD   CE   NZ                                   
REMARK 470     ASP A 318    CG   OD1  OD2                                       
REMARK 470     VAL A 338    CG1  CG2                                            
REMARK 470     GLU A 420    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 589    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 769    CG   CD   CE   NZ                                   
REMARK 470     GLU A 800    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 852    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 855    CG   OD1  OD2                                       
REMARK 470     LYS A 857    CG   CD   CE   NZ                                   
REMARK 470     GLN A 859    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 892    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 936    CG   CD   CE   NZ                                   
REMARK 470     MET A 938    CG   SD   CE                                        
REMARK 470     GLU A 988    CG   CD   OE1  OE2                                  
REMARK 470     ARG A1080    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B  47    CG   SD   CE                                        
REMARK 470     MET B  89    CG   SD   CE                                        
REMARK 470     ARG B 172    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 182    CG   CD   CE   NZ                                   
REMARK 470     ARG B 220    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 271    CG   CD   CE   NZ                                   
REMARK 470     ARG B 427    CG   CD   NE   CZ   NH1  NH2                        
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  24      -74.68    -68.11                                   
REMARK 500    LYS A  35       60.22   -114.79                                   
REMARK 500    ASN A  36      -89.84     67.26                                   
REMARK 500    ALA A  46      -30.69     72.53                                   
REMARK 500    TYR A  58       54.19    -91.62                                   
REMARK 500    LYS A  70     -129.52     54.43                                   
REMARK 500    LYS A  74     -154.25   -154.70                                   
REMARK 500    PRO A 144       99.72    -68.93                                   
REMARK 500    ARG A 158       95.48    -66.86                                   
REMARK 500    LYS A 204      126.93    -25.56                                   
REMARK 500    ASN A 241       59.87   -152.97                                   
REMARK 500    ASP A 318     -138.06     53.80                                   
REMARK 500    MET A 350      -69.86    -97.68                                   
REMARK 500    GLU A 368      -95.62     66.86                                   
REMARK 500    PHE A 382     -132.56     56.50                                   
REMARK 500    VAL A 430      108.52    -59.30                                   
REMARK 500    ALA A 495       19.93     53.95                                   
REMARK 500    ASN A 504     -130.10   -112.88                                   
REMARK 500    THR A 562      -60.06     60.64                                   
REMARK 500    SER A 653     -167.25   -163.81                                   
REMARK 500    GLU A 675      146.85   -174.67                                   
REMARK 500    ASN A 695     -151.92   -118.18                                   
REMARK 500    ASP A 705     -162.32    -71.13                                   
REMARK 500    THR A 745       49.90    -77.61                                   
REMARK 500    GLN A 759       42.80    -94.56                                   
REMARK 500    LYS A 769       -9.56   -141.60                                   
REMARK 500    ASN A 810       -1.91     66.84                                   
REMARK 500    LYS A 867       36.09    -87.90                                   
REMARK 500    ASN A 877       66.32     39.18                                   
REMARK 500    ASN A 885     -109.76     55.05                                   
REMARK 500    GLU A 902      -83.99   -102.11                                   
REMARK 500    ASN A 908      -12.03     70.32                                   
REMARK 500    ALA A 911       58.82    -90.57                                   
REMARK 500    LYS A 917      107.72   -163.20                                   
REMARK 500    ALA A 971       49.58     80.20                                   
REMARK 500    ARG A1080      -84.34    -83.71                                   
REMARK 500    ASP B  77       -1.96     60.91                                   
REMARK 500    LYS B 117     -122.62   -143.97                                   
REMARK 500    ARG B 119       -0.51     64.95                                   
REMARK 500    ARG B 163      -66.63   -124.16                                   
REMARK 500    GLU B 170      134.02   -173.10                                   
REMARK 500    ALA B 221      -28.81     76.37                                   
REMARK 500    CYS B 236        3.72    -69.35                                   
REMARK 500    THR B 321      -73.34   -138.16                                   
REMARK 500    GLN B 329      -39.06     66.93                                   
REMARK 500    CYS B 368      -74.39   -113.16                                   
REMARK 500    PRO B 426        1.93    -67.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1428  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 325   SG                                                     
REMARK 620 2 CYS B 328   SG  105.3                                              
REMARK 620 3 CYS B 393   SG  103.3 107.3                                        
REMARK 620 4 CYS B 396   SG  102.1 125.7 110.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1428                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Y70 B 1429                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CI1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4CI2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EI1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EI2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EI3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EI4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2B5M   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2B5L   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3E0C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4A11   RELATED DB: PDB                                   
DBREF  4CI3 A    1  1140  UNP    Q16531   DDB1_HUMAN       1   1140             
DBREF  4CI3 B    1   445  UNP    P0CF65   CRBN_CHICK       1    445             
SEQADV 4CI3 MET A  -17  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 HIS A  -16  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 HIS A  -15  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 HIS A  -14  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 HIS A  -13  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 HIS A  -12  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 HIS A  -11  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 ARG A  -10  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 ARG A   -9  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 LEU A   -8  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 VAL A   -7  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 PRO A   -6  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 ARG A   -5  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 GLY A   -4  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 SER A   -3  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 GLY A   -2  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 GLY A   -1  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 ARG A    0  UNP  Q16531              EXPRESSION TAG                 
SEQADV 4CI3 MET B  -23  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 ASP B  -22  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 TRP B  -21  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 SER B  -20  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 HIS B  -19  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 PRO B  -18  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 GLN B  -17  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 PHE B  -16  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 GLU B  -15  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 LYS B  -14  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 SER B  -13  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 ALA B  -12  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 VAL B  -11  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 ASP B  -10  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 GLU B   -9  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 ASN B   -8  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 LEU B   -7  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 TYR B   -6  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 PHE B   -5  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 GLN B   -4  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 GLY B   -3  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 GLY B   -2  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 GLY B   -1  UNP  P0CF65              EXPRESSION TAG                 
SEQADV 4CI3 ARG B    0  UNP  P0CF65              EXPRESSION TAG                 
SEQRES   1 A 1158  MET HIS HIS HIS HIS HIS HIS ARG ARG LEU VAL PRO ARG          
SEQRES   2 A 1158  GLY SER GLY GLY ARG MET SER TYR ASN TYR VAL VAL THR          
SEQRES   3 A 1158  ALA GLN LYS PRO THR ALA VAL ASN GLY CYS VAL THR GLY          
SEQRES   4 A 1158  HIS PHE THR SER ALA GLU ASP LEU ASN LEU LEU ILE ALA          
SEQRES   5 A 1158  LYS ASN THR ARG LEU GLU ILE TYR VAL VAL THR ALA GLU          
SEQRES   6 A 1158  GLY LEU ARG PRO VAL LYS GLU VAL GLY MET TYR GLY LYS          
SEQRES   7 A 1158  ILE ALA VAL MET GLU LEU PHE ARG PRO LYS GLY GLU SER          
SEQRES   8 A 1158  LYS ASP LEU LEU PHE ILE LEU THR ALA LYS TYR ASN ALA          
SEQRES   9 A 1158  CYS ILE LEU GLU TYR LYS GLN SER GLY GLU SER ILE ASP          
SEQRES  10 A 1158  ILE ILE THR ARG ALA HIS GLY ASN VAL GLN ASP ARG ILE          
SEQRES  11 A 1158  GLY ARG PRO SER GLU THR GLY ILE ILE GLY ILE ILE ASP          
SEQRES  12 A 1158  PRO GLU CYS ARG MET ILE GLY LEU ARG LEU TYR ASP GLY          
SEQRES  13 A 1158  LEU PHE LYS VAL ILE PRO LEU ASP ARG ASP ASN LYS GLU          
SEQRES  14 A 1158  LEU LYS ALA PHE ASN ILE ARG LEU GLU GLU LEU HIS VAL          
SEQRES  15 A 1158  ILE ASP VAL LYS PHE LEU TYR GLY CYS GLN ALA PRO THR          
SEQRES  16 A 1158  ILE CYS PHE VAL TYR GLN ASP PRO GLN GLY ARG HIS VAL          
SEQRES  17 A 1158  LYS THR TYR GLU VAL SER LEU ARG GLU LYS GLU PHE ASN          
SEQRES  18 A 1158  LYS GLY PRO TRP LYS GLN GLU ASN VAL GLU ALA GLU ALA          
SEQRES  19 A 1158  SER MET VAL ILE ALA VAL PRO GLU PRO PHE GLY GLY ALA          
SEQRES  20 A 1158  ILE ILE ILE GLY GLN GLU SER ILE THR TYR HIS ASN GLY          
SEQRES  21 A 1158  ASP LYS TYR LEU ALA ILE ALA PRO PRO ILE ILE LYS GLN          
SEQRES  22 A 1158  SER THR ILE VAL CYS HIS ASN ARG VAL ASP PRO ASN GLY          
SEQRES  23 A 1158  SER ARG TYR LEU LEU GLY ASP MET GLU GLY ARG LEU PHE          
SEQRES  24 A 1158  MET LEU LEU LEU GLU LYS GLU GLU GLN MET ASP GLY THR          
SEQRES  25 A 1158  VAL THR LEU LYS ASP LEU ARG VAL GLU LEU LEU GLY GLU          
SEQRES  26 A 1158  THR SER ILE ALA GLU CYS LEU THR TYR LEU ASP ASN GLY          
SEQRES  27 A 1158  VAL VAL PHE VAL GLY SER ARG LEU GLY ASP SER GLN LEU          
SEQRES  28 A 1158  VAL LYS LEU ASN VAL ASP SER ASN GLU GLN GLY SER TYR          
SEQRES  29 A 1158  VAL VAL ALA MET GLU THR PHE THR ASN LEU GLY PRO ILE          
SEQRES  30 A 1158  VAL ASP MET CYS VAL VAL ASP LEU GLU ARG GLN GLY GLN          
SEQRES  31 A 1158  GLY GLN LEU VAL THR CYS SER GLY ALA PHE LYS GLU GLY          
SEQRES  32 A 1158  SER LEU ARG ILE ILE ARG ASN GLY ILE GLY ILE HIS GLU          
SEQRES  33 A 1158  HIS ALA SER ILE ASP LEU PRO GLY ILE LYS GLY LEU TRP          
SEQRES  34 A 1158  PRO LEU ARG SER ASP PRO ASN ARG GLU THR ASP ASP THR          
SEQRES  35 A 1158  LEU VAL LEU SER PHE VAL GLY GLN THR ARG VAL LEU MET          
SEQRES  36 A 1158  LEU ASN GLY GLU GLU VAL GLU GLU THR GLU LEU MET GLY          
SEQRES  37 A 1158  PHE VAL ASP ASP GLN GLN THR PHE PHE CYS GLY ASN VAL          
SEQRES  38 A 1158  ALA HIS GLN GLN LEU ILE GLN ILE THR SER ALA SER VAL          
SEQRES  39 A 1158  ARG LEU VAL SER GLN GLU PRO LYS ALA LEU VAL SER GLU          
SEQRES  40 A 1158  TRP LYS GLU PRO GLN ALA LYS ASN ILE SER VAL ALA SER          
SEQRES  41 A 1158  CYS ASN SER SER GLN VAL VAL VAL ALA VAL GLY ARG ALA          
SEQRES  42 A 1158  LEU TYR TYR LEU GLN ILE HIS PRO GLN GLU LEU ARG GLN          
SEQRES  43 A 1158  ILE SER HIS THR GLU MET GLU HIS GLU VAL ALA CYS LEU          
SEQRES  44 A 1158  ASP ILE THR PRO LEU GLY ASP SER ASN GLY LEU SER PRO          
SEQRES  45 A 1158  LEU CYS ALA ILE GLY LEU TRP THR ASP ILE SER ALA ARG          
SEQRES  46 A 1158  ILE LEU LYS LEU PRO SER PHE GLU LEU LEU HIS LYS GLU          
SEQRES  47 A 1158  MET LEU GLY GLY GLU ILE ILE PRO ARG SER ILE LEU MET          
SEQRES  48 A 1158  THR THR PHE GLU SER SER HIS TYR LEU LEU CYS ALA LEU          
SEQRES  49 A 1158  GLY ASP GLY ALA LEU PHE TYR PHE GLY LEU ASN ILE GLU          
SEQRES  50 A 1158  THR GLY LEU LEU SER ASP ARG LYS LYS VAL THR LEU GLY          
SEQRES  51 A 1158  THR GLN PRO THR VAL LEU ARG THR PHE ARG SER LEU SER          
SEQRES  52 A 1158  THR THR ASN VAL PHE ALA CYS SER ASP ARG PRO THR VAL          
SEQRES  53 A 1158  ILE TYR SER SER ASN HIS LYS LEU VAL PHE SER ASN VAL          
SEQRES  54 A 1158  ASN LEU LYS GLU VAL ASN TYR MET CYS PRO LEU ASN SER          
SEQRES  55 A 1158  ASP GLY TYR PRO ASP SER LEU ALA LEU ALA ASN ASN SER          
SEQRES  56 A 1158  THR LEU THR ILE GLY THR ILE ASP GLU ILE GLN LYS LEU          
SEQRES  57 A 1158  HIS ILE ARG THR VAL PRO LEU TYR GLU SER PRO ARG LYS          
SEQRES  58 A 1158  ILE CYS TYR GLN GLU VAL SER GLN CYS PHE GLY VAL LEU          
SEQRES  59 A 1158  SER SER ARG ILE GLU VAL GLN ASP THR SER GLY GLY THR          
SEQRES  60 A 1158  THR ALA LEU ARG PRO SER ALA SER THR GLN ALA LEU SER          
SEQRES  61 A 1158  SER SER VAL SER SER SER LYS LEU PHE SER SER SER THR          
SEQRES  62 A 1158  ALA PRO HIS GLU THR SER PHE GLY GLU GLU VAL GLU VAL          
SEQRES  63 A 1158  HIS ASN LEU LEU ILE ILE ASP GLN HIS THR PHE GLU VAL          
SEQRES  64 A 1158  LEU HIS ALA HIS GLN PHE LEU GLN ASN GLU TYR ALA LEU          
SEQRES  65 A 1158  SER LEU VAL SER CYS LYS LEU GLY LYS ASP PRO ASN THR          
SEQRES  66 A 1158  TYR PHE ILE VAL GLY THR ALA MET VAL TYR PRO GLU GLU          
SEQRES  67 A 1158  ALA GLU PRO LYS GLN GLY ARG ILE VAL VAL PHE GLN TYR          
SEQRES  68 A 1158  SER ASP GLY LYS LEU GLN THR VAL ALA GLU LYS GLU VAL          
SEQRES  69 A 1158  LYS GLY ALA VAL TYR SER MET VAL GLU PHE ASN GLY LYS          
SEQRES  70 A 1158  LEU LEU ALA SER ILE ASN SER THR VAL ARG LEU TYR GLU          
SEQRES  71 A 1158  TRP THR THR GLU LYS GLU LEU ARG THR GLU CYS ASN HIS          
SEQRES  72 A 1158  TYR ASN ASN ILE MET ALA LEU TYR LEU LYS THR LYS GLY          
SEQRES  73 A 1158  ASP PHE ILE LEU VAL GLY ASP LEU MET ARG SER VAL LEU          
SEQRES  74 A 1158  LEU LEU ALA TYR LYS PRO MET GLU GLY ASN PHE GLU GLU          
SEQRES  75 A 1158  ILE ALA ARG ASP PHE ASN PRO ASN TRP MET SER ALA VAL          
SEQRES  76 A 1158  GLU ILE LEU ASP ASP ASP ASN PHE LEU GLY ALA GLU ASN          
SEQRES  77 A 1158  ALA PHE ASN LEU PHE VAL CYS GLN LYS ASP SER ALA ALA          
SEQRES  78 A 1158  THR THR ASP GLU GLU ARG GLN HIS LEU GLN GLU VAL GLY          
SEQRES  79 A 1158  LEU PHE HIS LEU GLY GLU PHE VAL ASN VAL PHE CYS HIS          
SEQRES  80 A 1158  GLY SER LEU VAL MET GLN ASN LEU GLY GLU THR SER THR          
SEQRES  81 A 1158  PRO THR GLN GLY SER VAL LEU PHE GLY THR VAL ASN GLY          
SEQRES  82 A 1158  MET ILE GLY LEU VAL THR SER LEU SER GLU SER TRP TYR          
SEQRES  83 A 1158  ASN LEU LEU LEU ASP MET GLN ASN ARG LEU ASN LYS VAL          
SEQRES  84 A 1158  ILE LYS SER VAL GLY LYS ILE GLU HIS SER PHE TRP ARG          
SEQRES  85 A 1158  SER PHE HIS THR GLU ARG LYS THR GLU PRO ALA THR GLY          
SEQRES  86 A 1158  PHE ILE ASP GLY ASP LEU ILE GLU SER PHE LEU ASP ILE          
SEQRES  87 A 1158  SER ARG PRO LYS MET GLN GLU VAL VAL ALA ASN LEU GLN          
SEQRES  88 A 1158  TYR ASP ASP GLY SER GLY MET LYS ARG GLU ALA THR ALA          
SEQRES  89 A 1158  ASP ASP LEU ILE LYS VAL VAL GLU GLU LEU THR ARG ILE          
SEQRES  90 A 1158  HIS                                                          
SEQRES   1 B  469  MET ASP TRP SER HIS PRO GLN PHE GLU LYS SER ALA VAL          
SEQRES   2 B  469  ASP GLU ASN LEU TYR PHE GLN GLY GLY GLY ARG MET ALA          
SEQRES   3 B  469  ALA GLU GLU GLY GLY ASP GLY ARG ARG ASN MET GLY ASN          
SEQRES   4 B  469  PRO PRO PRO PRO ALA PRO ALA GLU SER GLU GLU GLU ASP          
SEQRES   5 B  469  ASP ASN GLU MET GLU VAL GLU ASP GLN ASP GLY LYS GLU          
SEQRES   6 B  469  ALA GLU LYS PRO ASN MET ILE ASN PHE ASP THR SER LEU          
SEQRES   7 B  469  PRO THR SER HIS MET TYR LEU GLY SER ASP MET GLU GLU          
SEQRES   8 B  469  PHE HIS GLY ARG THR LEU HIS ASP ASP ASP SER CYS GLN          
SEQRES   9 B  469  VAL ILE PRO VAL LEU PRO HIS VAL MET VAL MET LEU ILE          
SEQRES  10 B  469  PRO GLY GLN THR LEU PRO LEU GLN LEU PHE HIS PRO GLN          
SEQRES  11 B  469  GLU VAL SER MET VAL ARG ASN LEU ILE GLN LYS ASP ARG          
SEQRES  12 B  469  THR PHE ALA VAL LEU ALA TYR SER ASN VAL ARG GLU ARG          
SEQRES  13 B  469  GLU ALA HIS PHE GLY THR THR ALA GLU ILE TYR ALA TYR          
SEQRES  14 B  469  ARG GLU GLU GLN GLU TYR GLY ILE GLU THR VAL LYS VAL          
SEQRES  15 B  469  LYS ALA ILE GLY ARG GLN ARG PHE LYS VAL LEU GLU ILE          
SEQRES  16 B  469  ARG THR GLN SER ASP GLY ILE GLN GLN ALA LYS VAL GLN          
SEQRES  17 B  469  ILE LEU PRO GLU ARG VAL LEU PRO SER THR MET SER ALA          
SEQRES  18 B  469  VAL GLN LEU GLN SER LEU SER ARG ARG HIS ILE PHE PRO          
SEQRES  19 B  469  SER SER LYS PRO LYS VAL TRP GLN ASP ARG ALA PHE ARG          
SEQRES  20 B  469  GLN TRP TRP GLN LYS TYR GLN LYS ARG LYS PHE HIS CYS          
SEQRES  21 B  469  ALA SER LEU THR SER TRP PRO PRO TRP LEU TYR SER LEU          
SEQRES  22 B  469  TYR ASP ALA GLU THR LEU MET GLU ARG VAL LYS ARG GLN          
SEQRES  23 B  469  LEU HIS GLU TRP ASP GLU ASN LEU LYS ASP GLU SER LEU          
SEQRES  24 B  469  PRO THR ASN PRO ILE ASP PHE SER TYR ARG VAL ALA ALA          
SEQRES  25 B  469  CYS LEU PRO ILE ASP ASP ALA LEU ARG ILE GLN LEU LEU          
SEQRES  26 B  469  LYS ILE GLY SER ALA ILE GLN ARG LEU ARG CYS GLU LEU          
SEQRES  27 B  469  ASP ILE MET ASN LYS CYS THR SER LEU CYS CYS LYS GLN          
SEQRES  28 B  469  CYS GLN ASP THR GLU ILE THR THR LYS ASN GLU ILE PHE          
SEQRES  29 B  469  SER LEU SER LEU CYS GLY PRO MET ALA ALA TYR VAL ASN          
SEQRES  30 B  469  PRO HIS GLY TYR ILE HIS GLU THR LEU THR VAL TYR LYS          
SEQRES  31 B  469  ALA CYS ASN LEU ASN LEU SER GLY ARG PRO SER THR GLU          
SEQRES  32 B  469  HIS SER TRP PHE PRO GLY TYR ALA TRP THR ILE ALA GLN          
SEQRES  33 B  469  CYS ARG ILE CYS GLY ASN HIS MET GLY TRP LYS PHE THR          
SEQRES  34 B  469  ALA THR LYS LYS ASP MET SER PRO GLN LYS PHE TRP GLY          
SEQRES  35 B  469  LEU THR ARG SER ALA LEU LEU PRO ARG ILE PRO GLU ALA          
SEQRES  36 B  469  GLU ASP GLU LEU GLY HIS ASP ARG SER PRO LEU LEU CYS          
SEQRES  37 B  469  LEU                                                          
HET     ZN  B1428       1                                                       
HET    Y70  B1429      20                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     Y70 S-POMALIDOMIDE                                                   
FORMUL   3   ZN    ZN 2+                                                        
FORMUL   4  Y70    C13 H11 N3 O4                                                
HELIX    1   1 PRO A  250  LYS A  254  5                                   5    
HELIX    2   2 ALA A  381  GLU A  384  5                                   4    
HELIX    3   3 THR A  985  GLN A  990  1                                   6    
HELIX    4   4 SER A 1044  ILE A 1062  1                                  19    
HELIX    5   5 GLU A 1069  SER A 1075  1                                   7    
HELIX    6   6 GLY A 1091  SER A 1096  1                                   6    
HELIX    7   7 SER A 1101  ALA A 1110  1                                  10    
HELIX    8   8 THR A 1125  ARG A 1138  1                                  14    
HELIX    9   9 THR B   52  SER B   57  1                                   6    
HELIX   10  10 HIS B   58  GLY B   62  5                                   5    
HELIX   11  11 HIS B  104  GLN B  116  1                                  13    
HELIX   12  12 GLN B  201  ARG B  205  5                                   5    
HELIX   13  13 PHE B  222  PHE B  234  1                                  13    
HELIX   14  14 HIS B  235  THR B  240  5                                   6    
HELIX   15  15 PRO B  243  LEU B  249  1                                   7    
HELIX   16  16 ASP B  251  ASP B  267  1                                  17    
HELIX   17  17 LYS B  271  LEU B  275  5                                   5    
HELIX   18  18 ASN B  278  ALA B  288  1                                  11    
HELIX   19  19 ASP B  293  ILE B  303  1                                  11    
HELIX   20  20 SER B  305  CYS B  320  1                                  16    
SHEET    1  AA 5 VAL A1004  HIS A1009  0                                        
SHEET    2  AA 5 GLN A1025  THR A1032 -1  O  LEU A1029   N  CYS A1008           
SHEET    3  AA 5 ILE A1037  LEU A1043 -1  O  GLY A1038   N  PHE A1030           
SHEET    4  AA 5 TYR A   3  GLN A  10 -1  O  TYR A   3   N  LEU A1043           
SHEET    5  AA 5 PHE A1088  ASP A1090  1  O  ILE A1089   N  VAL A   6           
SHEET    1  AB 4 GLY A  17  GLY A  21  0                                        
SHEET    2  AB 4 ASN A  30  LYS A  35 -1  O  ASN A  30   N  GLY A  21           
SHEET    3  AB 4 ARG A  38  VAL A  44 -1  O  ARG A  38   N  LYS A  35           
SHEET    4  AB 4 LEU A  49  GLY A  56 -1  O  ARG A  50   N  VAL A  43           
SHEET    1  AC 4 ILE A  61  PHE A  67  0                                        
SHEET    2  AC 4 LEU A  76  THR A  81 -1  O  LEU A  76   N  PHE A  67           
SHEET    3  AC 4 ASN A  85  SER A  94 -1  O  ASN A  85   N  THR A  81           
SHEET    4  AC 4 SER A  97  ASN A 107 -1  O  SER A  97   N  SER A  94           
SHEET    1  AD 3 ILE A 121  ILE A 124  0                                        
SHEET    2  AD 3 ILE A 131  ARG A 134 -1  O  GLY A 132   N  ILE A 123           
SHEET    3  AD 3 LYS A 141  ILE A 143 -1  O  LYS A 141   N  LEU A 133           
SHEET    1  AE 4 HIS A 163  PHE A 169  0                                        
SHEET    2  AE 4 THR A 177  GLN A 183 -1  O  CYS A 179   N  LYS A 168           
SHEET    3  AE 4 ARG A 188  SER A 196 -1  O  HIS A 189   N  TYR A 182           
SHEET    4  AE 4 GLU A 201  LYS A 204 -1  O  GLU A 201   N  SER A 196           
SHEET    1  AF 4 MET A 218  ALA A 221  0                                        
SHEET    2  AF 4 ALA A 229  ILE A 232 -1  O  ILE A 230   N  ILE A 220           
SHEET    3  AF 4 ILE A 237  ASN A 241 -1  O  THR A 238   N  ILE A 231           
SHEET    4  AF 4 LYS A 244  ILE A 248 -1  O  LYS A 244   N  ASN A 241           
SHEET    1  AG 4 ILE A 258  ARG A 263  0                                        
SHEET    2  AG 4 ARG A 270  ASP A 275 -1  O  LEU A 272   N  ASN A 262           
SHEET    3  AG 4 ARG A 279  LEU A 284 -1  O  ARG A 279   N  ASP A 275           
SHEET    4  AG 4 ARG A 301  GLU A 307 -1  O  ARG A 301   N  LEU A 284           
SHEET    1  AH 4 ALA A 311  TYR A 316  0                                        
SHEET    2  AH 4 VAL A 321  SER A 326 -1  O  PHE A 323   N  THR A 315           
SHEET    3  AH 4 SER A 331  LEU A 336 -1  O  GLN A 332   N  VAL A 324           
SHEET    4  AH 4 VAL A 347  PHE A 353 -1  O  VAL A 348   N  LYS A 335           
SHEET    1  AI 4 ILE A 359  VAL A 365  0                                        
SHEET    2  AI 4 GLN A 374  SER A 379 -1  O  GLN A 374   N  VAL A 365           
SHEET    3  AI 4 SER A 386  ASN A 392 -1  O  SER A 386   N  SER A 379           
SHEET    4  AI 4 LEU A 710  PRO A 716 -1  O  HIS A 711   N  ARG A 391           
SHEET    1  AJ 4 ILE A 396  ASP A 403  0                                        
SHEET    2  AJ 4 THR A 698  ILE A 704 -1  O  LEU A 699   N  ILE A 402           
SHEET    3  AJ 4 SER A 690  ALA A 694 -1  O  LEU A 691   N  GLY A 702           
SHEET    4  AJ 4 TYR A 678  LEU A 682 -1  O  TYR A 678   N  ALA A 694           
SHEET    1  AK 4 GLY A 409  LEU A 413  0                                        
SHEET    2  AK 4 THR A 424  PHE A 429 -1  O  THR A 424   N  LEU A 413           
SHEET    3  AK 4 GLN A 432  ASN A 439 -1  O  GLN A 432   N  PHE A 429           
SHEET    4  AK 4 GLU A 442  THR A 446 -1  O  GLU A 442   N  ASN A 439           
SHEET    1  AL 4 THR A 457  VAL A 463  0                                        
SHEET    2  AL 4 GLN A 467  THR A 472 -1  O  GLN A 467   N  VAL A 463           
SHEET    3  AL 4 VAL A 476  SER A 480 -1  O  ARG A 477   N  GLN A 470           
SHEET    4  AL 4 ALA A 485  TRP A 490 -1  O  ALA A 485   N  SER A 480           
SHEET    1  AM 4 VAL A 500  CYS A 503  0                                        
SHEET    2  AM 4 GLN A 507  VAL A 512 -1  O  VAL A 509   N  SER A 502           
SHEET    3  AM 4 ALA A 515  HIS A 522 -1  O  ALA A 515   N  VAL A 512           
SHEET    4  AM 4 GLU A 525  GLU A 533 -1  O  GLU A 525   N  HIS A 522           
SHEET    1  AN 4 VAL A 538  ASP A 542  0                                        
SHEET    2  AN 4 LEU A 555  LEU A 560 -1  O  ALA A 557   N  ASP A 542           
SHEET    3  AN 4 SER A 565  LYS A 570 -1  O  SER A 565   N  LEU A 560           
SHEET    4  AN 4 LEU A 576  MET A 581 -1  N  LEU A 577   O  ILE A 568           
SHEET    1  AO 4 PRO A 588  PHE A 596  0                                        
SHEET    2  AO 4 SER A 599  LEU A 606 -1  O  SER A 599   N  PHE A 596           
SHEET    3  AO 4 ALA A 610  LEU A 616 -1  O  ALA A 610   N  LEU A 606           
SHEET    4  AO 4 LEU A 623  THR A 630 -1  O  SER A 624   N  GLY A 615           
SHEET    1  AP 4 VAL A 637  SER A 643  0                                        
SHEET    2  AP 4 THR A 646  CYS A 652 -1  O  THR A 646   N  SER A 643           
SHEET    3  AP 4 THR A 657  SER A 661 -1  O  THR A 657   N  ALA A 651           
SHEET    4  AP 4 LEU A 666  ASN A 670 -1  O  VAL A 667   N  TYR A 660           
SHEET    1  AQ 2 SER A 720  GLN A 727  0                                        
SHEET    2  AQ 2 CYS A 732  GLN A 743 -1  O  CYS A 732   N  GLN A 727           
SHEET    1  AR 2 THR A 749  ALA A 751  0                                        
SHEET    2  AR 2 CYS A 732  GLN A 743  1  O  VAL A 742   N  THR A 750           
SHEET    1  AS 5 SER A 762  VAL A 765  0                                        
SHEET    2  AS 5 VAL A 801  GLN A 806  1  O  LEU A 802   N  SER A 762           
SHEET    3  AS 5 GLU A 785  ASP A 795 -1  O  LEU A 791   N  HIS A 805           
SHEET    4  AS 5 CYS A 732  GLN A 743 -1  O  PHE A 733   N  ILE A 794           
SHEET    5  AS 5 THR A 749  ALA A 751  1  O  THR A 750   N  VAL A 742           
SHEET    1  AT 5 SER A 762  VAL A 765  0                                        
SHEET    2  AT 5 VAL A 801  GLN A 806  1  O  LEU A 802   N  SER A 762           
SHEET    3  AT 5 GLU A 785  ASP A 795 -1  O  LEU A 791   N  HIS A 805           
SHEET    4  AT 5 CYS A 732  GLN A 743 -1  O  PHE A 733   N  ILE A 794           
SHEET    5  AT 5 SER A 720  GLN A 727 -1  O  SER A 720   N  SER A 738           
SHEET    1  AU 4 GLU A 811  CYS A 819  0                                        
SHEET    2  AU 4 TYR A 828  MET A 835 -1  O  TYR A 828   N  CYS A 819           
SHEET    3  AU 4 GLY A 846  SER A 854 -1  O  ARG A 847   N  THR A 833           
SHEET    4  AU 4 LYS A 857  VAL A 866 -1  O  LYS A 857   N  SER A 854           
SHEET    1  AV 4 MET A 873  PHE A 876  0                                        
SHEET    2  AV 4 LYS A 879  ILE A 884 -1  O  LYS A 879   N  PHE A 876           
SHEET    3  AV 4 THR A 887  TRP A 893 -1  O  THR A 887   N  ILE A 884           
SHEET    4  AV 4 LEU A 899  TYR A 906 -1  O  ARG A 900   N  GLU A 892           
SHEET    1  AW 4 TYR A 913  LYS A 917  0                                        
SHEET    2  AW 4 PHE A 920  GLY A 924 -1  O  PHE A 920   N  LYS A 917           
SHEET    3  AW 4 VAL A 930  LYS A 936 -1  O  LEU A 931   N  VAL A 923           
SHEET    4  AW 4 ASN A 941  ASP A 948 -1  O  ASN A 941   N  LYS A 936           
SHEET    1  AX 4 MET A 954  ILE A 959  0                                        
SHEET    2  AX 4 PHE A 965  GLU A 969 -1  O  LEU A 966   N  GLU A 958           
SHEET    3  AX 4 ASN A 973  GLN A 978 -1  O  ASN A 973   N  GLU A 969           
SHEET    4  AX 4 GLN A 993  HIS A 999 -1  O  GLN A 993   N  GLN A 978           
SHEET    1  AY 2 PHE A1076  HIS A1077  0                                        
SHEET    2  AY 2 THR A1082  GLU A1083 -1  O  GLU A1083   N  PHE A1076           
SHEET    1  BA 2 GLU B  66  GLU B  67  0                                        
SHEET    2  BA 2 GLU B 133  GLU B 150 -1  O  TYR B 145   N  GLU B  66           
SHEET    1  BB 2 THR B  97  LEU B 102  0                                        
SHEET    2  BB 2 ILE B 153  THR B 173 -1  O  VAL B 156   N  LEU B 102           
SHEET    1  BC 3 GLU B 332  THR B 335  0                                        
SHEET    2  BC 3 SER B 322  CYS B 325 -1  O  LEU B 323   N  ILE B 333           
SHEET    3  BC 3 LEU B 424  LEU B 425 -1  O  LEU B 425   N  CYS B 324           
SHEET    1  BD 6 MET B 348  VAL B 352  0                                        
SHEET    2  BD 6 ILE B 358  VAL B 364 -1  O  HIS B 359   N  TYR B 351           
SHEET    3  BD 6 LYS B 415  THR B 420 -1  O  TRP B 417   N  VAL B 364           
SHEET    4  BD 6 HIS B 399  ALA B 406 -1  O  MET B 400   N  THR B 420           
SHEET    5  BD 6 TYR B 386  CYS B 393 -1  O  ALA B 387   N  THR B 405           
SHEET    6  BD 6 LEU B 370  SER B 377 -1  O  ASN B 371   N  GLN B 392           
LINK         SG  CYS B 325                ZN    ZN B1428     1555   1555  2.29  
LINK         SG  CYS B 328                ZN    ZN B1428     1555   1555  2.13  
LINK         SG  CYS B 393                ZN    ZN B1428     1555   1555  2.39  
LINK         SG  CYS B 396                ZN    ZN B1428     1555   1555  2.14  
CISPEP   1 GLU A  224    PRO A  225          0         5.62                     
CISPEP   2 GLY A  357    PRO A  358          0        -2.03                     
CISPEP   3 GLU A  482    PRO A  483          0        -0.16                     
CISPEP   4 LEU A  571    PRO A  572          0         6.26                     
CISPEP   5 SER B  412    PRO B  413          0         1.41                     
SITE     1 AC1  4 CYS B 325  CYS B 328  CYS B 393  CYS B 396                    
SITE     1 AC2 12 GLN B 149  ASN B 353  PRO B 354  HIS B 355                    
SITE     2 AC2 12 GLU B 379  HIS B 380  SER B 381  TRP B 382                    
SITE     3 AC2 12 TRP B 388  ARG B 394  TRP B 402  PHE B 404                    
CRYST1  171.070  171.070  137.930  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      0.005846  0.003375  0.000000        0.00000                         
SCALE2      0.000000  0.006750  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007250        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system