GenomeNet

Database: PDB
Entry: 5HXB
LinkDB: 5HXB
Original site: 5HXB 
HEADER    LIGASE                                  30-JAN-16   5HXB              
TITLE     CEREBLON IN COMPLEX WITH DDB1, CC-885, AND GSPT1                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR GTP-BINDING SUBUNIT
COMPND   3 ERF3A;                                                               
COMPND   4 CHAIN: X, A;                                                         
COMPND   5 SYNONYM: ERF3A,G1 TO S PHASE TRANSITION PROTEIN 1 HOMOLOG;           
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA DAMAGE-BINDING PROTEIN 1;                              
COMPND   9 CHAIN: Y, B;                                                         
COMPND  10 SYNONYM: DDB P127 SUBUNIT,DNA DAMAGE-BINDING PROTEIN A,DDBA,DAMAGE-  
COMPND  11 SPECIFIC DNA-BINDING PROTEIN 1,HBV X-ASSOCIATED PROTEIN 1,XAP-1,UV-  
COMPND  12 DAMAGED DNA-BINDING FACTOR,UV-DAMAGED DNA-BINDING PROTEIN 1,UV-DDB 1,
COMPND  13 XPE-BINDING FACTOR,XPE-BF,XERODERMA PIGMENTOSUM GROUP E-COMPLEMENTING
COMPND  14 PROTEIN,XPCE;                                                        
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: PROTEIN CEREBLON;                                          
COMPND  18 CHAIN: Z, C;                                                         
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: GSPT1, ERF3A;                                                  
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: DDB1, XAP1;                                                    
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: CRBN, AD-006;                                                  
SOURCE  20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    E3, LIGASE, UBIQUITIN, DCAF, CEREBLON, DDB1, CRL4, CULLIN, IMID,      
KEYWDS   2 GSPT1, CRBN                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.P.CHAMBERLAIN,M.MATYSKIELA,B.PAGARIGAN                              
REVDAT   4   01-NOV-17 5HXB    1       JRNL   REMARK                            
REVDAT   3   27-JUL-16 5HXB    1       JRNL                                     
REVDAT   2   06-JUL-16 5HXB    1       JRNL                                     
REVDAT   1   29-JUN-16 5HXB    0                                                
JRNL        AUTH   M.E.MATYSKIELA,G.LU,T.ITO,B.PAGARIGAN,C.C.LU,K.MILLER,       
JRNL        AUTH 2 W.FANG,N.Y.WANG,D.NGUYEN,J.HOUSTON,G.CARMEL,T.TRAN,M.RILEY,  
JRNL        AUTH 3 L.NOSAKA,G.C.LANDER,S.GAIDAROVA,S.XU,A.L.RUCHELMAN,H.HANDA,  
JRNL        AUTH 4 J.CARMICHAEL,T.O.DANIEL,B.E.CATHERS,A.LOPEZ-GIRONA,          
JRNL        AUTH 5 P.P.CHAMBERLAIN                                              
JRNL        TITL   A NOVEL CEREBLON MODULATOR RECRUITS GSPT1 TO THE CRL4(CRBN)  
JRNL        TITL 2 UBIQUITIN LIGASE.                                            
JRNL        REF    NATURE                        V. 535   252 2016              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   27338790                                                     
JRNL        DOI    10.1038/NATURE18611                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0107                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 62827                          
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) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3289                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4579                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.87                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3880                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 233                          
REMARK   3   BIN FREE R VALUE                    : 0.4020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 25025                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 64                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 112.3                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.62000                                              
REMARK   3    B22 (A**2) : -8.14000                                             
REMARK   3    B33 (A**2) : 5.16000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.25000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.644         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.536         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 64.833        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.907                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.858                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 25592 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 24215 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 34776 ; 1.796 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 55467 ; 1.012 ; 2.999       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3250 ;12.880 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1035 ;42.516 ;24.551       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  4184 ;24.831 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   115 ;22.380 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4102 ; 0.146 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 28846 ; 0.017 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  5609 ; 0.008 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 13138 ; 9.514 ; 6.525       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 13137 ; 9.512 ; 6.525       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16342 ;14.634 ; 9.783       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 16343 ;14.634 ; 9.783       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 12454 ; 9.217 ; 7.042       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 12453 ; 9.214 ; 7.042       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 18435 ;14.429 ;10.316       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 51500 ;22.277 ;58.115       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 51501 ;22.277 ;58.116       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 3                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     X   440    633       A   440    633   22592  0.11  0.05     
REMARK   3    2     Y     2   1140       B     2   1140  129340  0.05  0.05     
REMARK   3    3     Z    48    442       C    48    442   42544  0.07  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   394        B   672                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.4674 -80.7292 102.4795              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9363 T22:   0.6926                                     
REMARK   3      T33:   0.4144 T12:   0.0250                                     
REMARK   3      T13:   0.0462 T23:  -0.0844                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1669 L22:   1.7476                                     
REMARK   3      L33:   0.8982 L12:  -0.5212                                     
REMARK   3      L13:  -0.0027 L23:   0.3025                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1067 S12:   0.0006 S13:  -0.0702                       
REMARK   3      S21:   0.3257 S22:   0.0918 S23:   0.1779                       
REMARK   3      S31:   0.2799 S32:   0.0694 S33:   0.0149                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Y   394        Y   672                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1104  -4.7754  75.5159              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0017 T22:   0.6860                                     
REMARK   3      T33:   0.4254 T12:  -0.0323                                     
REMARK   3      T13:   0.0853 T23:  -0.0844                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4158 L22:   2.5671                                     
REMARK   3      L33:   1.0240 L12:   0.7972                                     
REMARK   3      L13:   0.0712 L23:   1.1472                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0522 S12:  -0.0301 S13:   0.1022                       
REMARK   3      S21:  -0.4549 S22:   0.0915 S23:   0.1168                       
REMARK   3      S31:  -0.3132 S32:   0.0059 S33:  -0.0394                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    11        B   355                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.8190 -37.9069 134.6649              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5911 T22:   1.0610                                     
REMARK   3      T33:   0.6555 T12:   0.2377                                     
REMARK   3      T13:  -0.1852 T23:  -0.2628                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7332 L22:   1.4065                                     
REMARK   3      L33:   0.9159 L12:   0.3015                                     
REMARK   3      L13:  -0.5004 L23:  -0.2964                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0538 S12:  -0.2971 S13:   0.0774                       
REMARK   3      S21:   0.3252 S22:   0.0718 S23:  -0.6934                       
REMARK   3      S31:   0.2632 S32:   0.4855 S33:  -0.1256                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Y    11        Y   355                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.3600 -47.0441  50.1205              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5320 T22:   1.0248                                     
REMARK   3      T33:   0.5817 T12:  -0.1914                                     
REMARK   3      T13:   0.1741 T23:  -0.2207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8227 L22:   0.9281                                     
REMARK   3      L33:   1.2015 L12:  -0.0223                                     
REMARK   3      L13:   0.1723 L23:  -0.4164                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0083 S12:   0.1339 S13:  -0.0372                       
REMARK   3      S21:  -0.1003 S22:  -0.0077 S23:  -0.4126                       
REMARK   3      S31:  -0.1642 S32:   0.4544 S33:   0.0160                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   713        B  1081                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.5444 -31.3976 116.7175              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7739 T22:   0.7601                                     
REMARK   3      T33:   0.2777 T12:   0.0692                                     
REMARK   3      T13:   0.0322 T23:  -0.0685                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4153 L22:   1.1105                                     
REMARK   3      L33:   1.0000 L12:   0.0113                                     
REMARK   3      L13:  -0.5153 L23:  -0.1850                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0036 S12:  -0.0950 S13:   0.1153                       
REMARK   3      S21:  -0.0870 S22:   0.1229 S23:  -0.0882                       
REMARK   3      S31:  -0.0132 S32:   0.0048 S33:  -0.1265                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Y   713        Y  1081                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0754 -54.1212  61.7448              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7733 T22:   0.7512                                     
REMARK   3      T33:   0.2634 T12:  -0.0484                                     
REMARK   3      T13:   0.0611 T23:  -0.0708                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3318 L22:   1.0848                                     
REMARK   3      L33:   0.8280 L12:   0.0865                                     
REMARK   3      L13:   0.0954 L23:  -0.0562                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0132 S12:   0.0725 S13:  -0.0412                       
REMARK   3      S21:   0.0377 S22:   0.1559 S23:  -0.0490                       
REMARK   3      S31:  -0.0125 S32:   0.0552 S33:  -0.1427                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    60        C   186                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.8159  -2.7506 155.7365              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7994 T22:   0.6645                                     
REMARK   3      T33:   0.3562 T12:   0.1250                                     
REMARK   3      T13:   0.0149 T23:  -0.0281                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3350 L22:   1.0405                                     
REMARK   3      L33:   3.5667 L12:  -0.0519                                     
REMARK   3      L13:  -0.4174 L23:   1.4687                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1643 S12:  -0.0590 S13:  -0.2581                       
REMARK   3      S21:   0.2115 S22:   0.2056 S23:  -0.0976                       
REMARK   3      S31:  -0.1121 S32:   0.1831 S33:  -0.0413                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Z    60        Z   186                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.5574 -82.4773  22.2360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8382 T22:   0.6778                                     
REMARK   3      T33:   0.2965 T12:  -0.1506                                     
REMARK   3      T13:   0.0609 T23:  -0.0448                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1656 L22:   1.7604                                     
REMARK   3      L33:   3.1635 L12:  -0.9251                                     
REMARK   3      L13:   0.9899 L23:   0.9013                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0723 S12:   0.0023 S13:   0.1558                       
REMARK   3      S21:   0.0072 S22:   0.1940 S23:  -0.0872                       
REMARK   3      S31:   0.1381 S32:   0.0282 S33:  -0.1217                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   319        C   442                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.9425  12.9862 134.8985              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2130 T22:   0.7682                                     
REMARK   3      T33:   0.3218 T12:  -0.0663                                     
REMARK   3      T13:   0.2116 T23:  -0.0578                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1325 L22:   2.7962                                     
REMARK   3      L33:   0.3688 L12:  -0.9212                                     
REMARK   3      L13:   0.3958 L23:   0.3188                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0722 S12:  -0.0244 S13:   0.0240                       
REMARK   3      S21:  -0.6011 S22:   0.2751 S23:  -0.3557                       
REMARK   3      S31:  -0.2425 S32:   0.0484 S33:  -0.2029                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Z   319        Z   442                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.4798 -98.1525  43.1082              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2429 T22:   0.7348                                     
REMARK   3      T33:   0.2455 T12:   0.0400                                     
REMARK   3      T13:  -0.0665 T23:  -0.0257                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7020 L22:   2.0108                                     
REMARK   3      L33:   0.7212 L12:   0.3725                                     
REMARK   3      L13:   0.1039 L23:   1.1795                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0062 S12:   0.0789 S13:   0.0155                       
REMARK   3      S21:   0.5574 S22:   0.2343 S23:  -0.2702                       
REMARK   3      S31:   0.3033 S32:   0.1099 S33:  -0.2405                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   437        A   523                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7093  37.9356 176.0349              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8919 T22:   0.8660                                     
REMARK   3      T33:   0.4323 T12:  -0.1877                                     
REMARK   3      T13:   0.1531 T23:  -0.0973                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2282 L22:   5.2409                                     
REMARK   3      L33:   2.9811 L12:  -0.8281                                     
REMARK   3      L13:   0.9413 L23:  -0.5564                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1887 S12:  -0.0965 S13:   0.2131                       
REMARK   3      S21:   0.1950 S22:  -0.0543 S23:  -0.5038                       
REMARK   3      S31:   0.0364 S32:   0.4353 S33:   0.2430                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   X   437        X   523                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8786-123.5713   4.2636              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9148 T22:   0.8093                                     
REMARK   3      T33:   0.3233 T12:   0.1711                                     
REMARK   3      T13:  -0.0191 T23:  -0.0439                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3244 L22:   3.0612                                     
REMARK   3      L33:   1.7296 L12:   0.1333                                     
REMARK   3      L13:  -0.3976 L23:  -0.8294                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0344 S12:  -0.2382 S13:  -0.0997                       
REMARK   3      S21:  -0.3857 S22:  -0.0149 S23:  -0.0073                       
REMARK   3      S31:   0.5516 S32:   0.5807 S33:   0.0493                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   526        A   634                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.4663  27.9491 158.6586              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5270 T22:   0.3965                                     
REMARK   3      T33:   0.0363 T12:   0.0385                                     
REMARK   3      T13:   0.0960 T23:   0.0265                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6765 L22:   0.6171                                     
REMARK   3      L33:   0.5130 L12:   0.4321                                     
REMARK   3      L13:   0.3556 L23:   0.5335                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1093 S12:   0.0742 S13:   0.0410                       
REMARK   3      S21:   0.1363 S22:  -0.0418 S23:  -0.0405                       
REMARK   3      S31:  -0.0102 S32:  -0.1301 S33:  -0.0675                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   X   526        X   634                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.1093-113.3883  17.5169              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0171 T22:   0.7851                                     
REMARK   3      T33:   0.3318 T12:  -0.0863                                     
REMARK   3      T13:  -0.0155 T23:  -0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7963 L22:   0.6823                                     
REMARK   3      L33:   2.7649 L12:  -0.6633                                     
REMARK   3      L13:  -0.6980 L23:   1.0856                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0679 S12:  -0.1655 S13:  -0.0114                       
REMARK   3      S21:   0.0577 S22:   0.1342 S23:  -0.0558                       
REMARK   3      S31:   0.2306 S32:  -0.1212 S33:  -0.0663                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3   POSITIONS                                                          
REMARK   4                                                                      
REMARK   4 5HXB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000215861.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUL-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.4 - 8.6                          
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66582                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.19800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.79600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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: 4TZ4, 3E1Y                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM SODIUM CITRATE, TRIS PH 8.5, 18%   
REMARK 280  PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 280K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 300 REMARK: TRIMERIC AS DETERMINED BY ELECTRON MICROSCOPY                
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 APPLY THE FOLLOWING TO CHAINS: X, Y, Z                               
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, A                               
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     GLY X   436                                                      
REMARK 465     SER X   437                                                      
REMARK 465     GLY X   438                                                      
REMARK 465     PRO X   439                                                      
REMARK 465     MET Y     1                                                      
REMARK 465     GLU Y    47                                                      
REMARK 465     GLY Y    48                                                      
REMARK 465     SER Y    94                                                      
REMARK 465     GLY Y    95                                                      
REMARK 465     GLU Y    96                                                      
REMARK 465     GLU Y   210                                                      
REMARK 465     GLU Y   288                                                      
REMARK 465     GLU Y   289                                                      
REMARK 465     GLN Y   290                                                      
REMARK 465     MET Y   291                                                      
REMARK 465     ASP Y   292                                                      
REMARK 465     GLY Y   293                                                      
REMARK 465     THR Y   294                                                      
REMARK 465     VAL Y   295                                                      
REMARK 465     LEU Y   367                                                      
REMARK 465     GLU Y   368                                                      
REMARK 465     ARG Y   369                                                      
REMARK 465     ASN Y   418                                                      
REMARK 465     ARG Y   419                                                      
REMARK 465     GLY Y   547                                                      
REMARK 465     ASP Y   548                                                      
REMARK 465     SER Y   549                                                      
REMARK 465     GLU Y   585                                                      
REMARK 465     LEU Y   644                                                      
REMARK 465     SER Y   662                                                      
REMARK 465     THR Y   745                                                      
REMARK 465     SER Y   746                                                      
REMARK 465     GLY Y   747                                                      
REMARK 465     GLY Y   748                                                      
REMARK 465     PHE Y   771                                                      
REMARK 465     SER Y   772                                                      
REMARK 465     SER Y   773                                                      
REMARK 465     SER Y   774                                                      
REMARK 465     THR Y   775                                                      
REMARK 465     ALA Y   776                                                      
REMARK 465     PRO Y   777                                                      
REMARK 465     HIS Y   778                                                      
REMARK 465     GLU Y   779                                                      
REMARK 465     THR Y   780                                                      
REMARK 465     SER Y   781                                                      
REMARK 465     PHE Y   782                                                      
REMARK 465     GLY Y   783                                                      
REMARK 465     SER Y   981                                                      
REMARK 465     ALA Y   982                                                      
REMARK 465     ALA Y   983                                                      
REMARK 465     THR Y   984                                                      
REMARK 465     THR Y   985                                                      
REMARK 465     ASP Y   986                                                      
REMARK 465     LEU Y  1017                                                      
REMARK 465     GLY Y  1018                                                      
REMARK 465     GLU Y  1019                                                      
REMARK 465     THR Y  1020                                                      
REMARK 465     SER Y  1021                                                      
REMARK 465     THR Y  1022                                                      
REMARK 465     GLU Y  1079                                                      
REMARK 465     ARG Y  1080                                                      
REMARK 465     SER Y  1118                                                      
REMARK 465     GLY Y  1119                                                      
REMARK 465     MET Y  1120                                                      
REMARK 465     GLY Z    37                                                      
REMARK 465     SER Z    38                                                      
REMARK 465     MET Z    39                                                      
REMARK 465     GLU Z    40                                                      
REMARK 465     ALA Z    41                                                      
REMARK 465     LYS Z    42                                                      
REMARK 465     LYS Z    43                                                      
REMARK 465     PRO Z    44                                                      
REMARK 465     ASN Z    45                                                      
REMARK 465     ILE Z    46                                                      
REMARK 465     ILE Z    47                                                      
REMARK 465     SER Z   214                                                      
REMARK 465     ARG Z   215                                                      
REMARK 465     GLU Z   216                                                      
REMARK 465     ASP Z   217                                                      
REMARK 465     GLN Z   218                                                      
REMARK 465     CYS Z   219                                                      
REMARK 465     LEU Z   268                                                      
REMARK 465     LYS Z   269                                                      
REMARK 465     ASP Z   270                                                      
REMARK 465     ASP Z   271                                                      
REMARK 465     ILE Z   433                                                      
REMARK 465     SER Z   434                                                      
REMARK 465     PRO Z   435                                                      
REMARK 465     ASP Z   436                                                      
REMARK 465     LYS Z   437                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B    47                                                      
REMARK 465     GLY B    48                                                      
REMARK 465     SER B    94                                                      
REMARK 465     GLY B    95                                                      
REMARK 465     GLU B    96                                                      
REMARK 465     GLU B   288                                                      
REMARK 465     GLU B   289                                                      
REMARK 465     GLN B   290                                                      
REMARK 465     MET B   291                                                      
REMARK 465     ASP B   292                                                      
REMARK 465     GLY B   293                                                      
REMARK 465     THR B   294                                                      
REMARK 465     VAL B   295                                                      
REMARK 465     VAL B   338                                                      
REMARK 465     ASP B   339                                                      
REMARK 465     SER B   340                                                      
REMARK 465     ASN B   341                                                      
REMARK 465     GLU B   342                                                      
REMARK 465     LEU B   367                                                      
REMARK 465     GLU B   368                                                      
REMARK 465     ARG B   369                                                      
REMARK 465     ASN B   418                                                      
REMARK 465     ARG B   419                                                      
REMARK 465     GLY B   547                                                      
REMARK 465     ASP B   548                                                      
REMARK 465     LEU B   577                                                      
REMARK 465     GLU B   585                                                      
REMARK 465     LEU B   644                                                      
REMARK 465     SER B   662                                                      
REMARK 465     THR B   745                                                      
REMARK 465     SER B   746                                                      
REMARK 465     GLY B   747                                                      
REMARK 465     GLY B   748                                                      
REMARK 465     PHE B   771                                                      
REMARK 465     SER B   772                                                      
REMARK 465     SER B   773                                                      
REMARK 465     SER B   774                                                      
REMARK 465     THR B   775                                                      
REMARK 465     ALA B   776                                                      
REMARK 465     PRO B   777                                                      
REMARK 465     HIS B   778                                                      
REMARK 465     GLU B   779                                                      
REMARK 465     THR B   780                                                      
REMARK 465     SER B   781                                                      
REMARK 465     PHE B   782                                                      
REMARK 465     GLY B   783                                                      
REMARK 465     SER B   981                                                      
REMARK 465     ALA B   982                                                      
REMARK 465     ALA B   983                                                      
REMARK 465     THR B   984                                                      
REMARK 465     THR B   985                                                      
REMARK 465     ASP B   986                                                      
REMARK 465     LEU B  1017                                                      
REMARK 465     GLY B  1018                                                      
REMARK 465     GLU B  1019                                                      
REMARK 465     THR B  1020                                                      
REMARK 465     SER B  1021                                                      
REMARK 465     THR B  1022                                                      
REMARK 465     PRO B  1023                                                      
REMARK 465     GLU B  1079                                                      
REMARK 465     ARG B  1080                                                      
REMARK 465     SER B  1118                                                      
REMARK 465     GLY B  1119                                                      
REMARK 465     MET B  1120                                                      
REMARK 465     GLY C    37                                                      
REMARK 465     SER C    38                                                      
REMARK 465     MET C    39                                                      
REMARK 465     GLU C    40                                                      
REMARK 465     ALA C    41                                                      
REMARK 465     LYS C    42                                                      
REMARK 465     LYS C    43                                                      
REMARK 465     PRO C    44                                                      
REMARK 465     ASN C    45                                                      
REMARK 465     ILE C    46                                                      
REMARK 465     ILE C    47                                                      
REMARK 465     GLN C   129                                                      
REMARK 465     GLU C   130                                                      
REMARK 465     ARG C   131                                                      
REMARK 465     VAL C   213                                                      
REMARK 465     SER C   214                                                      
REMARK 465     ARG C   215                                                      
REMARK 465     GLU C   216                                                      
REMARK 465     ASP C   217                                                      
REMARK 465     GLN C   218                                                      
REMARK 465     CYS C   219                                                      
REMARK 465     GLU C   266                                                      
REMARK 465     ASN C   267                                                      
REMARK 465     LEU C   268                                                      
REMARK 465     LYS C   269                                                      
REMARK 465     ASP C   270                                                      
REMARK 465     ASP C   271                                                      
REMARK 465     GLU C   430                                                      
REMARK 465     ASP C   431                                                      
REMARK 465     GLU C   432                                                      
REMARK 465     ILE C   433                                                      
REMARK 465     SER C   434                                                      
REMARK 465     PRO C   435                                                      
REMARK 465     ASP C   436                                                      
REMARK 465     LYS C   437                                                      
REMARK 465     VAL C   438                                                      
REMARK 465     GLY A   436                                                      
REMARK 465     SER A   437                                                      
REMARK 465     GLY A   438                                                      
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     MET X 451    CG   SD   CE                                        
REMARK 470     LYS X 466    CG   CD   CE   NZ                                   
REMARK 470     GLN X 468    CG   CD   OE1  NE2                                  
REMARK 470     GLU X 480    CG   CD   OE1  OE2                                  
REMARK 470     ASP X 488    CG   OD1  OD2                                       
REMARK 470     LYS X 541    CG   CD   CE   NZ                                   
REMARK 470     ARG X 583    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS X 607    CG   CD   CE   NZ                                   
REMARK 470     GLU Y  27    CG   CD   OE1  OE2                                  
REMARK 470     ARG Y 111    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE Y 112    CG1  CG2  CD1                                       
REMARK 470     ARG Y 114    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP Y 148    CG   OD1  OD2                                       
REMARK 470     LYS Y 150    CG   CD   CE   NZ                                   
REMARK 470     LYS Y 153    CG   CD   CE   NZ                                   
REMARK 470     ARG Y 158    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN Y 174    CG   CD   OE1  NE2                                  
REMARK 470     GLN Y 186    CG   CD   OE1  NE2                                  
REMARK 470     ASN Y 211    CG   OD1  ND2                                       
REMARK 470     LYS Y 254    CG   CD   CE   NZ                                   
REMARK 470     ARG Y 301    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN Y 319    CG   OD1  ND2                                       
REMARK 470     VAL Y 338    CG1  CG2                                            
REMARK 470     ASP Y 339    CG   OD1  OD2                                       
REMARK 470     ASN Y 341    CG   OD1  ND2                                       
REMARK 470     GLU Y 342    CG   CD   OE1  OE2                                  
REMARK 470     GLN Y 343    CG   CD   OE1  NE2                                  
REMARK 470     SER Y 345    OG                                                  
REMARK 470     TYR Y 346    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN Y 370    CG   CD   OE1  NE2                                  
REMARK 470     GLN Y 372    CB   CG   CD   OE1  NE2                             
REMARK 470     ARG Y 391    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER Y 415    OG                                                  
REMARK 470     GLU Y 441    CG   CD   OE1  OE2                                  
REMARK 470     GLU Y 447    CG   CD   OE1  OE2                                  
REMARK 470     HIS Y 465    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU Y 482    CG   CD   OE1  OE2                                  
REMARK 470     GLN Y 494    CG   CD   OE1  NE2                                  
REMARK 470     GLU Y 525    CG   CD   OE1  OE2                                  
REMARK 470     ARG Y 527    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU Y 535    CG   CD   OE1  OE2                                  
REMARK 470     ASN Y 550    CG   OD1  ND2                                       
REMARK 470     LEU Y 552    CG   CD1  CD2                                       
REMARK 470     LYS Y 570    CG   CD   CE   NZ                                   
REMARK 470     PHE Y 574    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU Y 575    CG   CD   OE1  OE2                                  
REMARK 470     LEU Y 577    CG   CD1  CD2                                       
REMARK 470     HIS Y 578    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS Y 579    CG   CD   CE   NZ                                   
REMARK 470     GLU Y 580    CG   CD   OE1  OE2                                  
REMARK 470     MET Y 581    CG   SD   CE                                        
REMARK 470     ARG Y 589    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER Y 590    OG                                                  
REMARK 470     GLU Y 597    CG   CD   OE1  OE2                                  
REMARK 470     ASN Y 617    CG   OD1  ND2                                       
REMARK 470     GLU Y 619    CG   CD   OE1  OE2                                  
REMARK 470     THR Y 620    OG1  CG2                                            
REMARK 470     LEU Y 622    CG   CD1  CD2                                       
REMARK 470     LEU Y 623    CG   CD1  CD2                                       
REMARK 470     LYS Y 627    CG   CD   CE   NZ                                   
REMARK 470     GLN Y 634    CG   CD   OE1  NE2                                  
REMARK 470     SER Y 643    OG                                                  
REMARK 470     SER Y 645    OG                                                  
REMARK 470     ARG Y 655    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS Y 665    CG   CD   CE   NZ                                   
REMARK 470     LEU Y 666    CG   CD1  CD2                                       
REMARK 470     SER Y 669    OG                                                  
REMARK 470     LYS Y 674    CG   CD   CE   NZ                                   
REMARK 470     THR Y 703    OG1  CG2                                            
REMARK 470     GLU Y 706    CG   CD   OE1  OE2                                  
REMARK 470     ILE Y 707    CG1  CG2  CD1                                       
REMARK 470     ARG Y 713    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN Y 743    CG   CD   OE1  NE2                                  
REMARK 470     ASP Y 744    CG   OD1  OD2                                       
REMARK 470     SER Y 762    OG                                                  
REMARK 470     SER Y 768    OG                                                  
REMARK 470     LYS Y 769    CG   CD   CE   NZ                                   
REMARK 470     GLU Y 784    CG   CD   OE1  OE2                                  
REMARK 470     GLN Y 809    CG   CD   OE1  NE2                                  
REMARK 470     ASP Y 855    CG   OD1  OD2                                       
REMARK 470     LYS Y 857    CG   CD   CE   NZ                                   
REMARK 470     LYS Y 867    CG   CD   CE   NZ                                   
REMARK 470     GLU Y 896    CG   CD   OE1  OE2                                  
REMARK 470     MET Y1014    CG   SD   CE                                        
REMARK 470     GLN Y1015    CG   CD   OE1  NE2                                  
REMARK 470     ASN Y1016    CG   OD1  ND2                                       
REMARK 470     LYS Y1081    CG   CD   CE   NZ                                   
REMARK 470     GLN Y1113    CG   CD   OE1  NE2                                  
REMARK 470     LYS Y1121    CG   CD   CE   NZ                                   
REMARK 470     GLU Y1123    CG   CD   OE1  OE2                                  
REMARK 470     LEU Z  53    CG   CD1  CD2                                       
REMARK 470     ASP Z  63    CG   OD1  OD2                                       
REMARK 470     GLU Z  65    CG   CD   OE1  OE2                                  
REMARK 470     HIS Z  68    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS Z 116    CG   CD   CE   NZ                                   
REMARK 470     ASN Z 127    CG   OD1  ND2                                       
REMARK 470     VAL Z 128    CG1  CG2                                            
REMARK 470     GLN Z 129    CG   CD   OE1  NE2                                  
REMARK 470     GLU Z 130    CG   CD   OE1  OE2                                  
REMARK 470     ARG Z 131    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU Z 132    CG   CD   OE1  OE2                                  
REMARK 470     GLU Z 146    CG   CD   OE1  OE2                                  
REMARK 470     GLN Z 173    CG   CD   OE1  NE2                                  
REMARK 470     LYS Z 226    CG   CD   CE   NZ                                   
REMARK 470     LYS Z 229    CG   CD   CE   NZ                                   
REMARK 470     ARG Z 230    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN Z 267    CG   OD1  ND2                                       
REMARK 470     ASP Z 292    CG   OD1  OD2                                       
REMARK 470     LYS Z 317    CG   CD   CE   NZ                                   
REMARK 470     LYS Z 364    CG   CD   CE   NZ                                   
REMARK 470     LYS Z 392    CG   CD   CE   NZ                                   
REMARK 470     LYS Z 413    CG   CD   CE   NZ                                   
REMARK 470     GLU Z 432    CG   CD   OE1  OE2                                  
REMARK 470     VAL Z 438    CG1  CG2                                            
REMARK 470     ILE Z 439    CG1  CG2  CD1                                       
REMARK 470     LEU Z 440    CG   CD1  CD2                                       
REMARK 470     CYS Z 441    SG                                                  
REMARK 470     LEU Z 442    CG   CD1  CD2                                       
REMARK 470     GLU B  27    CG   CD   OE1  OE2                                  
REMARK 470     LEU B  49    CG   CD1  CD2                                       
REMARK 470     ARG B  68    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  92    CG   CD   CE   NZ                                   
REMARK 470     ARG B 111    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 112    CG1  CG2  CD1                                       
REMARK 470     ARG B 114    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 147    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 148    CG   OD1  OD2                                       
REMARK 470     LYS B 150    CG   CD   CE   NZ                                   
REMARK 470     LYS B 153    CG   CD   CE   NZ                                   
REMARK 470     ARG B 158    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 160    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 174    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 186    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 188    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS B 189    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 191    CG   CD   CE   NZ                                   
REMARK 470     ARG B 198    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 204    CG   CD   CE   NZ                                   
REMARK 470     LYS B 208    CG   CD   CE   NZ                                   
REMARK 470     GLN B 209    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 210    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 211    CG   OD1  ND2                                       
REMARK 470     GLU B 213    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 215    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 235    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 254    CG   CD   CE   NZ                                   
REMARK 470     GLU B 277    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 301    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 307    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 319    CG   OD1  ND2                                       
REMARK 470     GLN B 343    CG   CD   OE1  NE2                                  
REMARK 470     TYR B 346    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN B 370    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 372    CB   CG   CD   OE1  NE2                             
REMARK 470     LYS B 383    CG   CD   CE   NZ                                   
REMARK 470     ARG B 391    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 415    OG                                                  
REMARK 470     GLU B 447    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 494    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 535    CG   CD   OE1  OE2                                  
REMARK 470     SER B 549    OG                                                  
REMARK 470     ASN B 550    CG   OD1  ND2                                       
REMARK 470     LEU B 552    CG   CD1  CD2                                       
REMARK 470     LYS B 570    CG   CD   CE   NZ                                   
REMARK 470     GLU B 575    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 576    CG   CD1  CD2                                       
REMARK 470     HIS B 578    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU B 580    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 589    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 590    OG                                                  
REMARK 470     GLU B 597    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 617    CG   OD1  ND2                                       
REMARK 470     GLU B 619    CG   CD   OE1  OE2                                  
REMARK 470     THR B 620    OG1  CG2                                            
REMARK 470     LEU B 622    CG   CD1  CD2                                       
REMARK 470     LEU B 623    CG   CD1  CD2                                       
REMARK 470     ARG B 626    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 627    CG   CD   CE   NZ                                   
REMARK 470     GLN B 634    CG   CD   OE1  NE2                                  
REMARK 470     SER B 643    OG                                                  
REMARK 470     SER B 645    OG                                                  
REMARK 470     ARG B 655    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 665    CG   CD   CE   NZ                                   
REMARK 470     LEU B 666    CG   CD1  CD2                                       
REMARK 470     SER B 669    OG                                                  
REMARK 470     LYS B 674    CG   CD   CE   NZ                                   
REMARK 470     LEU B 699    CG   CD1  CD2                                       
REMARK 470     THR B 703    OG1  CG2                                            
REMARK 470     GLU B 706    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 743    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 744    CG   OD1  OD2                                       
REMARK 470     THR B 749    OG1  CG2                                            
REMARK 470     SER B 762    OG                                                  
REMARK 470     LYS B 769    CG   CD   CE   NZ                                   
REMARK 470     LEU B 770    CG   CD1  CD2                                       
REMARK 470     GLU B 784    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 809    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 811    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 855    CG   OD1  OD2                                       
REMARK 470     LYS B 857    CG   CD   CE   NZ                                   
REMARK 470     LYS B 867    CG   CD   CE   NZ                                   
REMARK 470     GLU B 896    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 906    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET B1014    CG   SD   CE                                        
REMARK 470     ASN B1016    CG   OD1  ND2                                       
REMARK 470     LYS B1081    CG   CD   CE   NZ                                   
REMARK 470     GLN B1113    CG   CD   OE1  NE2                                  
REMARK 470     LYS B1121    CG   CD   CE   NZ                                   
REMARK 470     GLU B1123    CG   CD   OE1  OE2                                  
REMARK 470     LEU C  53    CG   CD1  CD2                                       
REMARK 470     ASP C  63    CG   OD1  OD2                                       
REMARK 470     GLU C  65    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  66    CG   CD   OE1  OE2                                  
REMARK 470     HIS C  68    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG C  70    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 116    CG   CD   CE   NZ                                   
REMARK 470     SER C 126    OG                                                  
REMARK 470     GLU C 132    CG   CD   OE1  OE2                                  
REMARK 470     PHE C 135    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU C 146    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 173    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 211    CG   CD   CE   NZ                                   
REMARK 470     LYS C 222    CG   CD   CE   NZ                                   
REMARK 470     GLN C 225    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 226    CG   CD   CE   NZ                                   
REMARK 470     LYS C 229    CG   CD   CE   NZ                                   
REMARK 470     ARG C 230    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 258    CG   CD   CE   NZ                                   
REMARK 470     LYS C 259    CG   CD   CE   NZ                                   
REMARK 470     ASP C 292    CG   OD1  OD2                                       
REMARK 470     LYS C 334    CG   CD   CE   NZ                                   
REMARK 470     LEU C 360    CG   CD1  CD2                                       
REMARK 470     LYS C 364    CG   CD   CE   NZ                                   
REMARK 470     LYS C 392    CG   CD   CE   NZ                                   
REMARK 470     LYS C 413    CG   CD   CE   NZ                                   
REMARK 470     LEU C 440    CG   CD1  CD2                                       
REMARK 470     CYS C 441    SG                                                  
REMARK 470     ARG A 441    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 461    OG                                                  
REMARK 470     GLN A 468    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 469    CG   CD   OE1  NE2                                  
REMARK 470     MET A 473    CG   SD   CE                                        
REMARK 470     LYS A 476    CG   CD   CE   NZ                                   
REMARK 470     GLU A 480    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 490    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 498    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 501    CG   CD   CE   NZ                                   
REMARK 470     ILE A 507    CG1  CG2  CD1                                       
REMARK 470     CYS A 519    SG                                                  
REMARK 470     ASN A 523    CG   OD1  ND2                                       
REMARK 470     GLU A 539    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 541    CG   CD   CE   NZ                                   
REMARK 470     LYS A 577    CG   CD   CE   NZ                                   
REMARK 470     ARG A 581    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 583    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 588    CG   OD1  OD2                                       
REMARK 470     LEU A 603    CG   CD1  CD2                                       
REMARK 470     LYS A 607    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ILE Y   568     CB   LEU Y   576              1.55            
REMARK 500   SG   CYS C   394    ZN     ZN C   501              1.69            
REMARK 500   N    LEU Y   569     CB   LEU Y   576              1.84            
REMARK 500   C    ILE Y   568     CB   LEU Y   576              1.87            
REMARK 500   O    SER X   486     O    VAL X   489              1.93            
REMARK 500   NZ   LYS X   449     OE2  GLU X   510              1.96            
REMARK 500   OG1  THR Y   595     ND1  HIS Y   600              1.98            
REMARK 500   O    TYR Y   660     N    VAL Y   667              2.04            
REMARK 500   OD2  ASP C   313     O    CYS C   441              2.06            
REMARK 500   O    TYR B   660     N    VAL B   667              2.06            
REMARK 500   O    ASP Y   403     OG   SER B   768              2.09            
REMARK 500   CD2  PHE X   606     CG   LYS X   628              2.15            
REMARK 500   O    LEU B   546     N    SER B   549              2.17            
REMARK 500   CG   PRO Z   352     ND1  HIS Z   378              2.17            
REMARK 500   OG   SER Y   955     O    VAL Y  1004              2.18            
REMARK 500   CD2  PHE A   606     CG   LYS A   628              2.19            
REMARK 500   OG1  THR Y   595     CE1  HIS Y   600              2.19            
REMARK 500   OG1  THR Y    13     OD1  ASN Y   355              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   CD2  HIS Z   103     OG   SER A   542     2546     2.05            
REMARK 500   CB   LYS Z   116     CB   TYR A   448     1544     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU Y 489   CG    GLU Y 489   CD      0.115                       
REMARK 500    TYR Y 853   CB    TYR Y 853   CG     -0.103                       
REMARK 500    GLU Y1134   CG    GLU Y1134   CD      0.093                       
REMARK 500    GLU B 489   CG    GLU B 489   CD      0.109                       
REMARK 500    GLU B1134   CG    GLU B1134   CD      0.098                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO X 474   C   -  N   -  CA  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    PRO X 474   C   -  N   -  CD  ANGL. DEV. = -18.8 DEGREES          
REMARK 500    LEU X 485   CA  -  CB  -  CG  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    GLU X 510   N   -  CA  -  C   ANGL. DEV. = -18.7 DEGREES          
REMARK 500    VAL X 536   CG1 -  CB  -  CG2 ANGL. DEV. =  11.2 DEGREES          
REMARK 500    PRO Y 225   C   -  N   -  CA  ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    PRO Y 358   C   -  N   -  CA  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    PRO Y 358   C   -  N   -  CD  ANGL. DEV. = -23.8 DEGREES          
REMARK 500    ARG Y 434   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    PRO Y 483   C   -  N   -  CD  ANGL. DEV. = -14.1 DEGREES          
REMARK 500    PRO Y 572   C   -  N   -  CD  ANGL. DEV. = -14.5 DEGREES          
REMARK 500    GLU Y 597   N   -  CA  -  C   ANGL. DEV. = -18.9 DEGREES          
REMARK 500    CYS Y 977   CA  -  CB  -  SG  ANGL. DEV. =   8.9 DEGREES          
REMARK 500    ASP Z 265   N   -  CA  -  C   ANGL. DEV. =  17.5 DEGREES          
REMARK 500    ILE Z 296   CB  -  CA  -  C   ANGL. DEV. = -12.2 DEGREES          
REMARK 500    PRO Z 411   C   -  N   -  CD  ANGL. DEV. = -20.4 DEGREES          
REMARK 500    PRO B 225   C   -  N   -  CA  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    PRO B 358   C   -  N   -  CA  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    PRO B 358   C   -  N   -  CD  ANGL. DEV. = -23.9 DEGREES          
REMARK 500    PRO B 572   C   -  N   -  CD  ANGL. DEV. = -14.5 DEGREES          
REMARK 500    LEU B 623   N   -  CA  -  C   ANGL. DEV. = -16.7 DEGREES          
REMARK 500    LEU C 199   CB  -  CG  -  CD1 ANGL. DEV. =  11.2 DEGREES          
REMARK 500    PRO C 411   C   -  N   -  CD  ANGL. DEV. = -19.8 DEGREES          
REMARK 500    PRO C 427   C   -  N   -  CD  ANGL. DEV. = -16.5 DEGREES          
REMARK 500    LEU C 442   CA  -  CB  -  CG  ANGL. DEV. =  16.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG X 441      117.46   -168.92                                   
REMARK 500    MET X 451     -139.08     51.98                                   
REMARK 500    MET X 473     -155.95    -91.18                                   
REMARK 500    PRO X 474      -19.31     -2.42                                   
REMARK 500    VAL X 479      136.55   -177.75                                   
REMARK 500    LEU X 482      -64.45    -91.89                                   
REMARK 500    LEU X 485       38.31    -96.02                                   
REMARK 500    ASP X 487     -150.31     59.42                                   
REMARK 500    PRO X 496      161.98    -47.83                                   
REMARK 500    GLU X 498      170.77    -58.75                                   
REMARK 500    GLU X 511       14.78     89.85                                   
REMARK 500    ASN X 522      -81.11    -77.87                                   
REMARK 500    SER X 527     -150.84   -166.14                                   
REMARK 500    SER X 542     -111.02   -134.31                                   
REMARK 500    CYS X 545      134.53   -176.66                                   
REMARK 500    HIS X 555     -132.58     45.46                                   
REMARK 500    ILE X 567      -75.94   -120.86                                   
REMARK 500    LEU X 569      161.38    -49.25                                   
REMARK 500    SER X 574      -65.87    -90.77                                   
REMARK 500    PHE X 584      164.53    169.23                                   
REMARK 500    ALA X 598        7.61    -60.10                                   
REMARK 500    LYS X 607      -57.46     74.60                                   
REMARK 500    LEU X 630      -67.43   -108.94                                   
REMARK 500    LYS X 631     -169.12   -110.05                                   
REMARK 500    ASN Y  36     -120.85     58.27                                   
REMARK 500    VAL Y 108       30.60    -93.86                                   
REMARK 500    ASP Y 148       30.68    -92.88                                   
REMARK 500    ASN Y 149       55.57   -108.24                                   
REMARK 500    SER Y 217       -8.53   -148.19                                   
REMARK 500    GLU Y 224       48.67    -93.06                                   
REMARK 500    PRO Y 225      -60.24    -95.51                                   
REMARK 500    SER Y 256     -157.36   -156.20                                   
REMARK 500    LEU Y 317      -81.31    -96.66                                   
REMARK 500    ASP Y 339      102.18    -59.34                                   
REMARK 500    PRO Y 358      101.67     15.80                                   
REMARK 500    PHE Y 382     -128.44     47.28                                   
REMARK 500    LEU Y 404       83.38   -155.88                                   
REMARK 500    SER Y 415        0.31    -66.52                                   
REMARK 500    ASP Y 423       -6.29   -141.08                                   
REMARK 500    PRO Y 483       98.70     18.45                                   
REMARK 500    ALA Y 485      160.58    179.07                                   
REMARK 500    ASN Y 504     -154.43   -120.44                                   
REMARK 500    GLN Y 524       -8.15     76.26                                   
REMARK 500    ILE Y 529      -55.56   -138.18                                   
REMARK 500    ILE Y 543       19.82   -156.28                                   
REMARK 500    PRO Y 572      -50.89     15.83                                   
REMARK 500    PHE Y 574        0.65     80.76                                   
REMARK 500    LEU Y 577     -173.59     74.39                                   
REMARK 500    LYS Y 579       78.47   -100.84                                   
REMARK 500    LEU Y 582      175.69    -58.81                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     180 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 MET X  472     MET X  473                 -141.76                    
REMARK 500 MET X  473     PRO X  474                 -105.44                    
REMARK 500 LEU X  500     LYS X  501                  143.84                    
REMARK 500 GLU X  509     GLU X  510                  132.96                    
REMARK 500 GLY X  515     PHE X  516                  132.41                    
REMARK 500 GLN X  534     ILE X  535                 -149.25                    
REMARK 500 ILE X  544     CYS X  545                 -147.74                    
REMARK 500 CYS X  545     PRO X  546                 -140.32                    
REMARK 500 THR X  564     ALA X  565                  129.72                    
REMARK 500 LEU X  566     ILE X  567                 -146.95                    
REMARK 500 SER X  574     GLY X  575                 -148.54                    
REMARK 500 GLN X  587     ASP X  588                  147.80                    
REMARK 500 ILE X  601     CYS X  602                  147.87                    
REMARK 500 LEU X  603     GLU X  604                  145.80                    
REMARK 500 VAL X  633     PRO X  634                 -122.16                    
REMARK 500 GLU Y  224     PRO Y  225                  141.09                    
REMARK 500 GLN Y  332     LEU Y  333                  148.24                    
REMARK 500 VAL Y  338     ASP Y  339                  137.55                    
REMARK 500 GLU Y  342     GLN Y  343                  142.01                    
REMARK 500 SER Y  345     TYR Y  346                 -138.52                    
REMARK 500 GLY Y  357     PRO Y  358                 -113.27                    
REMARK 500 ASN Y  392     GLY Y  393                 -147.78                    
REMARK 500 GLU Y  482     PRO Y  483                 -142.19                    
REMARK 500 LEU Y  571     PRO Y  572                 -128.30                    
REMARK 500 TYR Y  660     SER Y  661                   61.67                    
REMARK 500 HIS Y  664     LYS Y  665                  145.50                    
REMARK 500 GLU Y  706     ILE Y  707                  -44.67                    
REMARK 500 ASN Y  950     PRO Y  951                 -148.17                    
REMARK 500 MET Y 1014     GLN Y 1015                 -147.58                    
REMARK 500 GLY Z   69     ARG Z   70                  -71.69                    
REMARK 500 TYR Z  125     SER Z  126                  146.91                    
REMARK 500 GLY Z  151     ILE Z  152                  135.96                    
REMARK 500 SER Z  410     PRO Z  411                 -119.18                    
REMARK 500 GLU Z  430     ASP Z  431                  136.30                    
REMARK 500 GLN B  209     GLU B  210                 -143.44                    
REMARK 500 GLU B  224     PRO B  225                  141.08                    
REMARK 500 GLN B  332     LEU B  333                  149.61                    
REMARK 500 SER B  345     TYR B  346                 -127.74                    
REMARK 500 GLY B  357     PRO B  358                 -113.71                    
REMARK 500 VAL B  476     ARG B  477                 -148.99                    
REMARK 500 GLU B  482     PRO B  483                 -143.61                    
REMARK 500 LEU B  571     PRO B  572                 -128.80                    
REMARK 500 TYR B  660     SER B  661                   61.80                    
REMARK 500 HIS B  664     LYS B  665                  145.48                    
REMARK 500 GLN B 1015     ASN B 1016                 -139.89                    
REMARK 500 ASP B 1116     GLY B 1117                  138.26                    
REMARK 500 LYS C  181     VAL C  182                 -149.65                    
REMARK 500 SER C  410     PRO C  411                 -118.75                    
REMARK 500 ILE C  426     PRO C  427                  -84.22                    
REMARK 500 CYS C  441     LEU C  442                 -149.01                    
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      63 NON CIS, NON-TRANS OMEGA OUTLIERS.            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    HIS Y 805         0.07    SIDE CHAIN                              
REMARK 500    TYR Y 891         0.07    SIDE CHAIN                              
REMARK 500    PHE Y 965         0.08    SIDE CHAIN                              
REMARK 500    HIS B 465         0.07    SIDE CHAIN                              
REMARK 500    HIS B 805         0.07    SIDE CHAIN                              
REMARK 500    TYR B 853         0.08    SIDE CHAIN                              
REMARK 500    PHE B 965         0.06    SIDE CHAIN                              
REMARK 500    HIS C 103         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ILE X 543        -10.40                                           
REMARK 500    ASN Y 337         10.14                                           
REMARK 500    TYR Y 660         13.23                                           
REMARK 500    TYR B 660         14.41                                           
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 Z 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS Z 323   SG                                                     
REMARK 620 2 CYS Z 326   SG   88.4                                              
REMARK 620 3 CYS Z 391   SG   97.5 114.1                                        
REMARK 620 4 CYS Z 394   SG  112.0 136.9 100.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 323   SG                                                     
REMARK 620 2 CYS C 326   SG   81.1                                              
REMARK 620 3 CYS C 391   SG   82.2  96.8                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN Z 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 85C Z 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 85C C 502                 
DBREF  5HXB X  438   634  UNP    P15170   ERF3A_HUMAN    437    633             
DBREF  5HXB Y    1  1140  UNP    Q16531   DDB1_HUMAN       1   1140             
DBREF  5HXB Z   40   442  UNP    Q96SW2   CRBN_HUMAN      39    441             
DBREF  5HXB B    1  1140  UNP    Q16531   DDB1_HUMAN       1   1140             
DBREF  5HXB C   40   442  UNP    Q96SW2   CRBN_HUMAN      39    441             
DBREF  5HXB A  438   634  UNP    P15170   ERF3A_HUMAN    437    633             
SEQADV 5HXB GLY X  436  UNP  P15170              EXPRESSION TAG                 
SEQADV 5HXB SER X  437  UNP  P15170              EXPRESSION TAG                 
SEQADV 5HXB GLY Z   37  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 5HXB SER Z   38  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 5HXB MET Z   39  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 5HXB GLY C   37  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 5HXB SER C   38  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 5HXB MET C   39  UNP  Q96SW2              EXPRESSION TAG                 
SEQADV 5HXB GLY A  436  UNP  P15170              EXPRESSION TAG                 
SEQADV 5HXB SER A  437  UNP  P15170              EXPRESSION TAG                 
SEQRES   1 X  199  GLY SER GLY PRO ILE ARG LEU PRO ILE VAL ASP LYS TYR          
SEQRES   2 X  199  LYS ASP MET GLY THR VAL VAL LEU GLY LYS LEU GLU SER          
SEQRES   3 X  199  GLY SER ILE CYS LYS GLY GLN GLN LEU VAL MET MET PRO          
SEQRES   4 X  199  ASN LYS HIS ASN VAL GLU VAL LEU GLY ILE LEU SER ASP          
SEQRES   5 X  199  ASP VAL GLU THR ASP THR VAL ALA PRO GLY GLU ASN LEU          
SEQRES   6 X  199  LYS ILE ARG LEU LYS GLY ILE GLU GLU GLU GLU ILE LEU          
SEQRES   7 X  199  PRO GLY PHE ILE LEU CYS ASP PRO ASN ASN LEU CYS HIS          
SEQRES   8 X  199  SER GLY ARG THR PHE ASP ALA GLN ILE VAL ILE ILE GLU          
SEQRES   9 X  199  HIS LYS SER ILE ILE CYS PRO GLY TYR ASN ALA VAL LEU          
SEQRES  10 X  199  HIS ILE HIS THR CYS ILE GLU GLU VAL GLU ILE THR ALA          
SEQRES  11 X  199  LEU ILE CYS LEU VAL ASP LYS LYS SER GLY GLU LYS SER          
SEQRES  12 X  199  LYS THR ARG PRO ARG PHE VAL LYS GLN ASP GLN VAL CYS          
SEQRES  13 X  199  ILE ALA ARG LEU ARG THR ALA GLY THR ILE CYS LEU GLU          
SEQRES  14 X  199  THR PHE LYS ASP PHE PRO GLN MET GLY ARG PHE THR LEU          
SEQRES  15 X  199  ARG ASP GLU GLY LYS THR ILE ALA ILE GLY LYS VAL LEU          
SEQRES  16 X  199  LYS LEU VAL PRO                                              
SEQRES   1 Y 1140  MET SER TYR ASN TYR VAL VAL THR ALA GLN LYS PRO THR          
SEQRES   2 Y 1140  ALA VAL ASN GLY CYS VAL THR GLY HIS PHE THR SER ALA          
SEQRES   3 Y 1140  GLU ASP LEU ASN LEU LEU ILE ALA LYS ASN THR ARG LEU          
SEQRES   4 Y 1140  GLU ILE TYR VAL VAL THR ALA GLU GLY LEU ARG PRO VAL          
SEQRES   5 Y 1140  LYS GLU VAL GLY MET TYR GLY LYS ILE ALA VAL MET GLU          
SEQRES   6 Y 1140  LEU PHE ARG PRO LYS GLY GLU SER LYS ASP LEU LEU PHE          
SEQRES   7 Y 1140  ILE LEU THR ALA LYS TYR ASN ALA CYS ILE LEU GLU TYR          
SEQRES   8 Y 1140  LYS GLN SER GLY GLU SER ILE ASP ILE ILE THR ARG ALA          
SEQRES   9 Y 1140  HIS GLY ASN VAL GLN ASP ARG ILE GLY ARG PRO SER GLU          
SEQRES  10 Y 1140  THR GLY ILE ILE GLY ILE ILE ASP PRO GLU CYS ARG MET          
SEQRES  11 Y 1140  ILE GLY LEU ARG LEU TYR ASP GLY LEU PHE LYS VAL ILE          
SEQRES  12 Y 1140  PRO LEU ASP ARG ASP ASN LYS GLU LEU LYS ALA PHE ASN          
SEQRES  13 Y 1140  ILE ARG LEU GLU GLU LEU HIS VAL ILE ASP VAL LYS PHE          
SEQRES  14 Y 1140  LEU TYR GLY CYS GLN ALA PRO THR ILE CYS PHE VAL TYR          
SEQRES  15 Y 1140  GLN ASP PRO GLN GLY ARG HIS VAL LYS THR TYR GLU VAL          
SEQRES  16 Y 1140  SER LEU ARG GLU LYS GLU PHE ASN LYS GLY PRO TRP LYS          
SEQRES  17 Y 1140  GLN GLU ASN VAL GLU ALA GLU ALA SER MET VAL ILE ALA          
SEQRES  18 Y 1140  VAL PRO GLU PRO PHE GLY GLY ALA ILE ILE ILE GLY GLN          
SEQRES  19 Y 1140  GLU SER ILE THR TYR HIS ASN GLY ASP LYS TYR LEU ALA          
SEQRES  20 Y 1140  ILE ALA PRO PRO ILE ILE LYS GLN SER THR ILE VAL CYS          
SEQRES  21 Y 1140  HIS ASN ARG VAL ASP PRO ASN GLY SER ARG TYR LEU LEU          
SEQRES  22 Y 1140  GLY ASP MET GLU GLY ARG LEU PHE MET LEU LEU LEU GLU          
SEQRES  23 Y 1140  LYS GLU GLU GLN MET ASP GLY THR VAL THR LEU LYS ASP          
SEQRES  24 Y 1140  LEU ARG VAL GLU LEU LEU GLY GLU THR SER ILE ALA GLU          
SEQRES  25 Y 1140  CYS LEU THR TYR LEU ASP ASN GLY VAL VAL PHE VAL GLY          
SEQRES  26 Y 1140  SER ARG LEU GLY ASP SER GLN LEU VAL LYS LEU ASN VAL          
SEQRES  27 Y 1140  ASP SER ASN GLU GLN GLY SER TYR VAL VAL ALA MET GLU          
SEQRES  28 Y 1140  THR PHE THR ASN LEU GLY PRO ILE VAL ASP MET CYS VAL          
SEQRES  29 Y 1140  VAL ASP LEU GLU ARG GLN GLY GLN GLY GLN LEU VAL THR          
SEQRES  30 Y 1140  CYS SER GLY ALA PHE LYS GLU GLY SER LEU ARG ILE ILE          
SEQRES  31 Y 1140  ARG ASN GLY ILE GLY ILE HIS GLU HIS ALA SER ILE ASP          
SEQRES  32 Y 1140  LEU PRO GLY ILE LYS GLY LEU TRP PRO LEU ARG SER ASP          
SEQRES  33 Y 1140  PRO ASN ARG GLU THR ASP ASP THR LEU VAL LEU SER PHE          
SEQRES  34 Y 1140  VAL GLY GLN THR ARG VAL LEU MET LEU ASN GLY GLU GLU          
SEQRES  35 Y 1140  VAL GLU GLU THR GLU LEU MET GLY PHE VAL ASP ASP GLN          
SEQRES  36 Y 1140  GLN THR PHE PHE CYS GLY ASN VAL ALA HIS GLN GLN LEU          
SEQRES  37 Y 1140  ILE GLN ILE THR SER ALA SER VAL ARG LEU VAL SER GLN          
SEQRES  38 Y 1140  GLU PRO LYS ALA LEU VAL SER GLU TRP LYS GLU PRO GLN          
SEQRES  39 Y 1140  ALA LYS ASN ILE SER VAL ALA SER CYS ASN SER SER GLN          
SEQRES  40 Y 1140  VAL VAL VAL ALA VAL GLY ARG ALA LEU TYR TYR LEU GLN          
SEQRES  41 Y 1140  ILE HIS PRO GLN GLU LEU ARG GLN ILE SER HIS THR GLU          
SEQRES  42 Y 1140  MET GLU HIS GLU VAL ALA CYS LEU ASP ILE THR PRO LEU          
SEQRES  43 Y 1140  GLY ASP SER ASN GLY LEU SER PRO LEU CYS ALA ILE GLY          
SEQRES  44 Y 1140  LEU TRP THR ASP ILE SER ALA ARG ILE LEU LYS LEU PRO          
SEQRES  45 Y 1140  SER PHE GLU LEU LEU HIS LYS GLU MET LEU GLY GLY GLU          
SEQRES  46 Y 1140  ILE ILE PRO ARG SER ILE LEU MET THR THR PHE GLU SER          
SEQRES  47 Y 1140  SER HIS TYR LEU LEU CYS ALA LEU GLY ASP GLY ALA LEU          
SEQRES  48 Y 1140  PHE TYR PHE GLY LEU ASN ILE GLU THR GLY LEU LEU SER          
SEQRES  49 Y 1140  ASP ARG LYS LYS VAL THR LEU GLY THR GLN PRO THR VAL          
SEQRES  50 Y 1140  LEU ARG THR PHE ARG SER LEU SER THR THR ASN VAL PHE          
SEQRES  51 Y 1140  ALA CYS SER ASP ARG PRO THR VAL ILE TYR SER SER ASN          
SEQRES  52 Y 1140  HIS LYS LEU VAL PHE SER ASN VAL ASN LEU LYS GLU VAL          
SEQRES  53 Y 1140  ASN TYR MET CYS PRO LEU ASN SER ASP GLY TYR PRO ASP          
SEQRES  54 Y 1140  SER LEU ALA LEU ALA ASN ASN SER THR LEU THR ILE GLY          
SEQRES  55 Y 1140  THR ILE ASP GLU ILE GLN LYS LEU HIS ILE ARG THR VAL          
SEQRES  56 Y 1140  PRO LEU TYR GLU SER PRO ARG LYS ILE CYS TYR GLN GLU          
SEQRES  57 Y 1140  VAL SER GLN CYS PHE GLY VAL LEU SER SER ARG ILE GLU          
SEQRES  58 Y 1140  VAL GLN ASP THR SER GLY GLY THR THR ALA LEU ARG PRO          
SEQRES  59 Y 1140  SER ALA SER THR GLN ALA LEU SER SER SER VAL SER SER          
SEQRES  60 Y 1140  SER LYS LEU PHE SER SER SER THR ALA PRO HIS GLU THR          
SEQRES  61 Y 1140  SER PHE GLY GLU GLU VAL GLU VAL HIS ASN LEU LEU ILE          
SEQRES  62 Y 1140  ILE ASP GLN HIS THR PHE GLU VAL LEU HIS ALA HIS GLN          
SEQRES  63 Y 1140  PHE LEU GLN ASN GLU TYR ALA LEU SER LEU VAL SER CYS          
SEQRES  64 Y 1140  LYS LEU GLY LYS ASP PRO ASN THR TYR PHE ILE VAL GLY          
SEQRES  65 Y 1140  THR ALA MET VAL TYR PRO GLU GLU ALA GLU PRO LYS GLN          
SEQRES  66 Y 1140  GLY ARG ILE VAL VAL PHE GLN TYR SER ASP GLY LYS LEU          
SEQRES  67 Y 1140  GLN THR VAL ALA GLU LYS GLU VAL LYS GLY ALA VAL TYR          
SEQRES  68 Y 1140  SER MET VAL GLU PHE ASN GLY LYS LEU LEU ALA SER ILE          
SEQRES  69 Y 1140  ASN SER THR VAL ARG LEU TYR GLU TRP THR THR GLU LYS          
SEQRES  70 Y 1140  GLU LEU ARG THR GLU CYS ASN HIS TYR ASN ASN ILE MET          
SEQRES  71 Y 1140  ALA LEU TYR LEU LYS THR LYS GLY ASP PHE ILE LEU VAL          
SEQRES  72 Y 1140  GLY ASP LEU MET ARG SER VAL LEU LEU LEU ALA TYR LYS          
SEQRES  73 Y 1140  PRO MET GLU GLY ASN PHE GLU GLU ILE ALA ARG ASP PHE          
SEQRES  74 Y 1140  ASN PRO ASN TRP MET SER ALA VAL GLU ILE LEU ASP ASP          
SEQRES  75 Y 1140  ASP ASN PHE LEU GLY ALA GLU ASN ALA PHE ASN LEU PHE          
SEQRES  76 Y 1140  VAL CYS GLN LYS ASP SER ALA ALA THR THR ASP GLU GLU          
SEQRES  77 Y 1140  ARG GLN HIS LEU GLN GLU VAL GLY LEU PHE HIS LEU GLY          
SEQRES  78 Y 1140  GLU PHE VAL ASN VAL PHE CYS HIS GLY SER LEU VAL MET          
SEQRES  79 Y 1140  GLN ASN LEU GLY GLU THR SER THR PRO THR GLN GLY SER          
SEQRES  80 Y 1140  VAL LEU PHE GLY THR VAL ASN GLY MET ILE GLY LEU VAL          
SEQRES  81 Y 1140  THR SER LEU SER GLU SER TRP TYR ASN LEU LEU LEU ASP          
SEQRES  82 Y 1140  MET GLN ASN ARG LEU ASN LYS VAL ILE LYS SER VAL GLY          
SEQRES  83 Y 1140  LYS ILE GLU HIS SER PHE TRP ARG SER PHE HIS THR GLU          
SEQRES  84 Y 1140  ARG LYS THR GLU PRO ALA THR GLY PHE ILE ASP GLY ASP          
SEQRES  85 Y 1140  LEU ILE GLU SER PHE LEU ASP ILE SER ARG PRO LYS MET          
SEQRES  86 Y 1140  GLN GLU VAL VAL ALA ASN LEU GLN TYR ASP ASP GLY SER          
SEQRES  87 Y 1140  GLY MET LYS ARG GLU ALA THR ALA ASP ASP LEU ILE LYS          
SEQRES  88 Y 1140  VAL VAL GLU GLU LEU THR ARG ILE HIS                          
SEQRES   1 Z  406  GLY SER MET GLU ALA LYS LYS PRO ASN ILE ILE ASN PHE          
SEQRES   2 Z  406  ASP THR SER LEU PRO THR SER HIS THR TYR LEU GLY ALA          
SEQRES   3 Z  406  ASP MET GLU GLU PHE HIS GLY ARG THR LEU HIS ASP ASP          
SEQRES   4 Z  406  ASP SER CYS GLN VAL ILE PRO VAL LEU PRO GLN VAL MET          
SEQRES   5 Z  406  MET ILE LEU ILE PRO GLY GLN THR LEU PRO LEU GLN LEU          
SEQRES   6 Z  406  PHE HIS PRO GLN GLU VAL SER MET VAL ARG ASN LEU ILE          
SEQRES   7 Z  406  GLN LYS ASP ARG THR PHE ALA VAL LEU ALA TYR SER ASN          
SEQRES   8 Z  406  VAL GLN GLU ARG GLU ALA GLN PHE GLY THR THR ALA GLU          
SEQRES   9 Z  406  ILE TYR ALA TYR ARG GLU GLU GLN ASP PHE GLY ILE GLU          
SEQRES  10 Z  406  ILE VAL LYS VAL LYS ALA ILE GLY ARG GLN ARG PHE LYS          
SEQRES  11 Z  406  VAL LEU GLU LEU ARG THR GLN SER ASP GLY ILE GLN GLN          
SEQRES  12 Z  406  ALA LYS VAL GLN ILE LEU PRO GLU CYS VAL LEU PRO SER          
SEQRES  13 Z  406  THR MET SER ALA VAL GLN LEU GLU SER LEU ASN LYS CYS          
SEQRES  14 Z  406  GLN ILE PHE PRO SER LYS PRO VAL SER ARG GLU ASP GLN          
SEQRES  15 Z  406  CYS SER TYR LYS TRP TRP GLN LYS TYR GLN LYS ARG LYS          
SEQRES  16 Z  406  PHE HIS CYS ALA ASN LEU THR SER TRP PRO ARG TRP LEU          
SEQRES  17 Z  406  TYR SER LEU TYR ASP ALA GLU THR LEU MET ASP ARG ILE          
SEQRES  18 Z  406  LYS LYS GLN LEU ARG GLU TRP ASP GLU ASN LEU LYS ASP          
SEQRES  19 Z  406  ASP SER LEU PRO SER ASN PRO ILE ASP PHE SER TYR ARG          
SEQRES  20 Z  406  VAL ALA ALA CYS LEU PRO ILE ASP ASP VAL LEU ARG ILE          
SEQRES  21 Z  406  GLN LEU LEU LYS ILE GLY SER ALA ILE GLN ARG LEU ARG          
SEQRES  22 Z  406  CYS GLU LEU ASP ILE MET ASN LYS CYS THR SER LEU CYS          
SEQRES  23 Z  406  CYS LYS GLN CYS GLN GLU THR GLU ILE THR THR LYS ASN          
SEQRES  24 Z  406  GLU ILE PHE SER LEU SER LEU CYS GLY PRO MET ALA ALA          
SEQRES  25 Z  406  TYR VAL ASN PRO HIS GLY TYR VAL HIS GLU THR LEU THR          
SEQRES  26 Z  406  VAL TYR LYS ALA CYS ASN LEU ASN LEU ILE GLY ARG PRO          
SEQRES  27 Z  406  SER THR GLU HIS SER TRP PHE PRO GLY TYR ALA TRP THR          
SEQRES  28 Z  406  VAL ALA GLN CYS LYS ILE CYS ALA SER HIS ILE GLY TRP          
SEQRES  29 Z  406  LYS PHE THR ALA THR LYS LYS ASP MET SER PRO GLN LYS          
SEQRES  30 Z  406  PHE TRP GLY LEU THR ARG SER ALA LEU LEU PRO THR ILE          
SEQRES  31 Z  406  PRO ASP THR GLU ASP GLU ILE SER PRO ASP LYS VAL ILE          
SEQRES  32 Z  406  LEU CYS LEU                                                  
SEQRES   1 B 1140  MET SER TYR ASN TYR VAL VAL THR ALA GLN LYS PRO THR          
SEQRES   2 B 1140  ALA VAL ASN GLY CYS VAL THR GLY HIS PHE THR SER ALA          
SEQRES   3 B 1140  GLU ASP LEU ASN LEU LEU ILE ALA LYS ASN THR ARG LEU          
SEQRES   4 B 1140  GLU ILE TYR VAL VAL THR ALA GLU GLY LEU ARG PRO VAL          
SEQRES   5 B 1140  LYS GLU VAL GLY MET TYR GLY LYS ILE ALA VAL MET GLU          
SEQRES   6 B 1140  LEU PHE ARG PRO LYS GLY GLU SER LYS ASP LEU LEU PHE          
SEQRES   7 B 1140  ILE LEU THR ALA LYS TYR ASN ALA CYS ILE LEU GLU TYR          
SEQRES   8 B 1140  LYS GLN SER GLY GLU SER ILE ASP ILE ILE THR ARG ALA          
SEQRES   9 B 1140  HIS GLY ASN VAL GLN ASP ARG ILE GLY ARG PRO SER GLU          
SEQRES  10 B 1140  THR GLY ILE ILE GLY ILE ILE ASP PRO GLU CYS ARG MET          
SEQRES  11 B 1140  ILE GLY LEU ARG LEU TYR ASP GLY LEU PHE LYS VAL ILE          
SEQRES  12 B 1140  PRO LEU ASP ARG ASP ASN LYS GLU LEU LYS ALA PHE ASN          
SEQRES  13 B 1140  ILE ARG LEU GLU GLU LEU HIS VAL ILE ASP VAL LYS PHE          
SEQRES  14 B 1140  LEU TYR GLY CYS GLN ALA PRO THR ILE CYS PHE VAL TYR          
SEQRES  15 B 1140  GLN ASP PRO GLN GLY ARG HIS VAL LYS THR TYR GLU VAL          
SEQRES  16 B 1140  SER LEU ARG GLU LYS GLU PHE ASN LYS GLY PRO TRP LYS          
SEQRES  17 B 1140  GLN GLU ASN VAL GLU ALA GLU ALA SER MET VAL ILE ALA          
SEQRES  18 B 1140  VAL PRO GLU PRO PHE GLY GLY ALA ILE ILE ILE GLY GLN          
SEQRES  19 B 1140  GLU SER ILE THR TYR HIS ASN GLY ASP LYS TYR LEU ALA          
SEQRES  20 B 1140  ILE ALA PRO PRO ILE ILE LYS GLN SER THR ILE VAL CYS          
SEQRES  21 B 1140  HIS ASN ARG VAL ASP PRO ASN GLY SER ARG TYR LEU LEU          
SEQRES  22 B 1140  GLY ASP MET GLU GLY ARG LEU PHE MET LEU LEU LEU GLU          
SEQRES  23 B 1140  LYS GLU GLU GLN MET ASP GLY THR VAL THR LEU LYS ASP          
SEQRES  24 B 1140  LEU ARG VAL GLU LEU LEU GLY GLU THR SER ILE ALA GLU          
SEQRES  25 B 1140  CYS LEU THR TYR LEU ASP ASN GLY VAL VAL PHE VAL GLY          
SEQRES  26 B 1140  SER ARG LEU GLY ASP SER GLN LEU VAL LYS LEU ASN VAL          
SEQRES  27 B 1140  ASP SER ASN GLU GLN GLY SER TYR VAL VAL ALA MET GLU          
SEQRES  28 B 1140  THR PHE THR ASN LEU GLY PRO ILE VAL ASP MET CYS VAL          
SEQRES  29 B 1140  VAL ASP LEU GLU ARG GLN GLY GLN GLY GLN LEU VAL THR          
SEQRES  30 B 1140  CYS SER GLY ALA PHE LYS GLU GLY SER LEU ARG ILE ILE          
SEQRES  31 B 1140  ARG ASN GLY ILE GLY ILE HIS GLU HIS ALA SER ILE ASP          
SEQRES  32 B 1140  LEU PRO GLY ILE LYS GLY LEU TRP PRO LEU ARG SER ASP          
SEQRES  33 B 1140  PRO ASN ARG GLU THR ASP ASP THR LEU VAL LEU SER PHE          
SEQRES  34 B 1140  VAL GLY GLN THR ARG VAL LEU MET LEU ASN GLY GLU GLU          
SEQRES  35 B 1140  VAL GLU GLU THR GLU LEU MET GLY PHE VAL ASP ASP GLN          
SEQRES  36 B 1140  GLN THR PHE PHE CYS GLY ASN VAL ALA HIS GLN GLN LEU          
SEQRES  37 B 1140  ILE GLN ILE THR SER ALA SER VAL ARG LEU VAL SER GLN          
SEQRES  38 B 1140  GLU PRO LYS ALA LEU VAL SER GLU TRP LYS GLU PRO GLN          
SEQRES  39 B 1140  ALA LYS ASN ILE SER VAL ALA SER CYS ASN SER SER GLN          
SEQRES  40 B 1140  VAL VAL VAL ALA VAL GLY ARG ALA LEU TYR TYR LEU GLN          
SEQRES  41 B 1140  ILE HIS PRO GLN GLU LEU ARG GLN ILE SER HIS THR GLU          
SEQRES  42 B 1140  MET GLU HIS GLU VAL ALA CYS LEU ASP ILE THR PRO LEU          
SEQRES  43 B 1140  GLY ASP SER ASN GLY LEU SER PRO LEU CYS ALA ILE GLY          
SEQRES  44 B 1140  LEU TRP THR ASP ILE SER ALA ARG ILE LEU LYS LEU PRO          
SEQRES  45 B 1140  SER PHE GLU LEU LEU HIS LYS GLU MET LEU GLY GLY GLU          
SEQRES  46 B 1140  ILE ILE PRO ARG SER ILE LEU MET THR THR PHE GLU SER          
SEQRES  47 B 1140  SER HIS TYR LEU LEU CYS ALA LEU GLY ASP GLY ALA LEU          
SEQRES  48 B 1140  PHE TYR PHE GLY LEU ASN ILE GLU THR GLY LEU LEU SER          
SEQRES  49 B 1140  ASP ARG LYS LYS VAL THR LEU GLY THR GLN PRO THR VAL          
SEQRES  50 B 1140  LEU ARG THR PHE ARG SER LEU SER THR THR ASN VAL PHE          
SEQRES  51 B 1140  ALA CYS SER ASP ARG PRO THR VAL ILE TYR SER SER ASN          
SEQRES  52 B 1140  HIS LYS LEU VAL PHE SER ASN VAL ASN LEU LYS GLU VAL          
SEQRES  53 B 1140  ASN TYR MET CYS PRO LEU ASN SER ASP GLY TYR PRO ASP          
SEQRES  54 B 1140  SER LEU ALA LEU ALA ASN ASN SER THR LEU THR ILE GLY          
SEQRES  55 B 1140  THR ILE ASP GLU ILE GLN LYS LEU HIS ILE ARG THR VAL          
SEQRES  56 B 1140  PRO LEU TYR GLU SER PRO ARG LYS ILE CYS TYR GLN GLU          
SEQRES  57 B 1140  VAL SER GLN CYS PHE GLY VAL LEU SER SER ARG ILE GLU          
SEQRES  58 B 1140  VAL GLN ASP THR SER GLY GLY THR THR ALA LEU ARG PRO          
SEQRES  59 B 1140  SER ALA SER THR GLN ALA LEU SER SER SER VAL SER SER          
SEQRES  60 B 1140  SER LYS LEU PHE SER SER SER THR ALA PRO HIS GLU THR          
SEQRES  61 B 1140  SER PHE GLY GLU GLU VAL GLU VAL HIS ASN LEU LEU ILE          
SEQRES  62 B 1140  ILE ASP GLN HIS THR PHE GLU VAL LEU HIS ALA HIS GLN          
SEQRES  63 B 1140  PHE LEU GLN ASN GLU TYR ALA LEU SER LEU VAL SER CYS          
SEQRES  64 B 1140  LYS LEU GLY LYS ASP PRO ASN THR TYR PHE ILE VAL GLY          
SEQRES  65 B 1140  THR ALA MET VAL TYR PRO GLU GLU ALA GLU PRO LYS GLN          
SEQRES  66 B 1140  GLY ARG ILE VAL VAL PHE GLN TYR SER ASP GLY LYS LEU          
SEQRES  67 B 1140  GLN THR VAL ALA GLU LYS GLU VAL LYS GLY ALA VAL TYR          
SEQRES  68 B 1140  SER MET VAL GLU PHE ASN GLY LYS LEU LEU ALA SER ILE          
SEQRES  69 B 1140  ASN SER THR VAL ARG LEU TYR GLU TRP THR THR GLU LYS          
SEQRES  70 B 1140  GLU LEU ARG THR GLU CYS ASN HIS TYR ASN ASN ILE MET          
SEQRES  71 B 1140  ALA LEU TYR LEU LYS THR LYS GLY ASP PHE ILE LEU VAL          
SEQRES  72 B 1140  GLY ASP LEU MET ARG SER VAL LEU LEU LEU ALA TYR LYS          
SEQRES  73 B 1140  PRO MET GLU GLY ASN PHE GLU GLU ILE ALA ARG ASP PHE          
SEQRES  74 B 1140  ASN PRO ASN TRP MET SER ALA VAL GLU ILE LEU ASP ASP          
SEQRES  75 B 1140  ASP ASN PHE LEU GLY ALA GLU ASN ALA PHE ASN LEU PHE          
SEQRES  76 B 1140  VAL CYS GLN LYS ASP SER ALA ALA THR THR ASP GLU GLU          
SEQRES  77 B 1140  ARG GLN HIS LEU GLN GLU VAL GLY LEU PHE HIS LEU GLY          
SEQRES  78 B 1140  GLU PHE VAL ASN VAL PHE CYS HIS GLY SER LEU VAL MET          
SEQRES  79 B 1140  GLN ASN LEU GLY GLU THR SER THR PRO THR GLN GLY SER          
SEQRES  80 B 1140  VAL LEU PHE GLY THR VAL ASN GLY MET ILE GLY LEU VAL          
SEQRES  81 B 1140  THR SER LEU SER GLU SER TRP TYR ASN LEU LEU LEU ASP          
SEQRES  82 B 1140  MET GLN ASN ARG LEU ASN LYS VAL ILE LYS SER VAL GLY          
SEQRES  83 B 1140  LYS ILE GLU HIS SER PHE TRP ARG SER PHE HIS THR GLU          
SEQRES  84 B 1140  ARG LYS THR GLU PRO ALA THR GLY PHE ILE ASP GLY ASP          
SEQRES  85 B 1140  LEU ILE GLU SER PHE LEU ASP ILE SER ARG PRO LYS MET          
SEQRES  86 B 1140  GLN GLU VAL VAL ALA ASN LEU GLN TYR ASP ASP GLY SER          
SEQRES  87 B 1140  GLY MET LYS ARG GLU ALA THR ALA ASP ASP LEU ILE LYS          
SEQRES  88 B 1140  VAL VAL GLU GLU LEU THR ARG ILE HIS                          
SEQRES   1 C  406  GLY SER MET GLU ALA LYS LYS PRO ASN ILE ILE ASN PHE          
SEQRES   2 C  406  ASP THR SER LEU PRO THR SER HIS THR TYR LEU GLY ALA          
SEQRES   3 C  406  ASP MET GLU GLU PHE HIS GLY ARG THR LEU HIS ASP ASP          
SEQRES   4 C  406  ASP SER CYS GLN VAL ILE PRO VAL LEU PRO GLN VAL MET          
SEQRES   5 C  406  MET ILE LEU ILE PRO GLY GLN THR LEU PRO LEU GLN LEU          
SEQRES   6 C  406  PHE HIS PRO GLN GLU VAL SER MET VAL ARG ASN LEU ILE          
SEQRES   7 C  406  GLN LYS ASP ARG THR PHE ALA VAL LEU ALA TYR SER ASN          
SEQRES   8 C  406  VAL GLN GLU ARG GLU ALA GLN PHE GLY THR THR ALA GLU          
SEQRES   9 C  406  ILE TYR ALA TYR ARG GLU GLU GLN ASP PHE GLY ILE GLU          
SEQRES  10 C  406  ILE VAL LYS VAL LYS ALA ILE GLY ARG GLN ARG PHE LYS          
SEQRES  11 C  406  VAL LEU GLU LEU ARG THR GLN SER ASP GLY ILE GLN GLN          
SEQRES  12 C  406  ALA LYS VAL GLN ILE LEU PRO GLU CYS VAL LEU PRO SER          
SEQRES  13 C  406  THR MET SER ALA VAL GLN LEU GLU SER LEU ASN LYS CYS          
SEQRES  14 C  406  GLN ILE PHE PRO SER LYS PRO VAL SER ARG GLU ASP GLN          
SEQRES  15 C  406  CYS SER TYR LYS TRP TRP GLN LYS TYR GLN LYS ARG LYS          
SEQRES  16 C  406  PHE HIS CYS ALA ASN LEU THR SER TRP PRO ARG TRP LEU          
SEQRES  17 C  406  TYR SER LEU TYR ASP ALA GLU THR LEU MET ASP ARG ILE          
SEQRES  18 C  406  LYS LYS GLN LEU ARG GLU TRP ASP GLU ASN LEU LYS ASP          
SEQRES  19 C  406  ASP SER LEU PRO SER ASN PRO ILE ASP PHE SER TYR ARG          
SEQRES  20 C  406  VAL ALA ALA CYS LEU PRO ILE ASP ASP VAL LEU ARG ILE          
SEQRES  21 C  406  GLN LEU LEU LYS ILE GLY SER ALA ILE GLN ARG LEU ARG          
SEQRES  22 C  406  CYS GLU LEU ASP ILE MET ASN LYS CYS THR SER LEU CYS          
SEQRES  23 C  406  CYS LYS GLN CYS GLN GLU THR GLU ILE THR THR LYS ASN          
SEQRES  24 C  406  GLU ILE PHE SER LEU SER LEU CYS GLY PRO MET ALA ALA          
SEQRES  25 C  406  TYR VAL ASN PRO HIS GLY TYR VAL HIS GLU THR LEU THR          
SEQRES  26 C  406  VAL TYR LYS ALA CYS ASN LEU ASN LEU ILE GLY ARG PRO          
SEQRES  27 C  406  SER THR GLU HIS SER TRP PHE PRO GLY TYR ALA TRP THR          
SEQRES  28 C  406  VAL ALA GLN CYS LYS ILE CYS ALA SER HIS ILE GLY TRP          
SEQRES  29 C  406  LYS PHE THR ALA THR LYS LYS ASP MET SER PRO GLN LYS          
SEQRES  30 C  406  PHE TRP GLY LEU THR ARG SER ALA LEU LEU PRO THR ILE          
SEQRES  31 C  406  PRO ASP THR GLU ASP GLU ILE SER PRO ASP LYS VAL ILE          
SEQRES  32 C  406  LEU CYS LEU                                                  
SEQRES   1 A  199  GLY SER GLY PRO ILE ARG LEU PRO ILE VAL ASP LYS TYR          
SEQRES   2 A  199  LYS ASP MET GLY THR VAL VAL LEU GLY LYS LEU GLU SER          
SEQRES   3 A  199  GLY SER ILE CYS LYS GLY GLN GLN LEU VAL MET MET PRO          
SEQRES   4 A  199  ASN LYS HIS ASN VAL GLU VAL LEU GLY ILE LEU SER ASP          
SEQRES   5 A  199  ASP VAL GLU THR ASP THR VAL ALA PRO GLY GLU ASN LEU          
SEQRES   6 A  199  LYS ILE ARG LEU LYS GLY ILE GLU GLU GLU GLU ILE LEU          
SEQRES   7 A  199  PRO GLY PHE ILE LEU CYS ASP PRO ASN ASN LEU CYS HIS          
SEQRES   8 A  199  SER GLY ARG THR PHE ASP ALA GLN ILE VAL ILE ILE GLU          
SEQRES   9 A  199  HIS LYS SER ILE ILE CYS PRO GLY TYR ASN ALA VAL LEU          
SEQRES  10 A  199  HIS ILE HIS THR CYS ILE GLU GLU VAL GLU ILE THR ALA          
SEQRES  11 A  199  LEU ILE CYS LEU VAL ASP LYS LYS SER GLY GLU LYS SER          
SEQRES  12 A  199  LYS THR ARG PRO ARG PHE VAL LYS GLN ASP GLN VAL CYS          
SEQRES  13 A  199  ILE ALA ARG LEU ARG THR ALA GLY THR ILE CYS LEU GLU          
SEQRES  14 A  199  THR PHE LYS ASP PHE PRO GLN MET GLY ARG PHE THR LEU          
SEQRES  15 A  199  ARG ASP GLU GLY LYS THR ILE ALA ILE GLY LYS VAL LEU          
SEQRES  16 A  199  LYS LEU VAL PRO                                              
HET     ZN  Z 501       1                                                       
HET    85C  Z 502      31                                                       
HET     ZN  C 501       1                                                       
HET    85C  C 502      31                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     85C 1-(3-CHLORO-4-METHYLPHENYL)-3-({2-[(3S)-2,6-                     
HETNAM   2 85C  DIOXOPIPERIDIN-3-YL]-1-OXO-2,3-DIHYDRO-1H-ISOINDOL-5-           
HETNAM   3 85C  YL}METHYL)UREA                                                  
FORMUL   7   ZN    2(ZN 2+)                                                     
FORMUL   8  85C    2(C22 H21 CL N4 O4)                                          
HELIX    1 AA1 PRO Y  250  LYS Y  254  5                                   5    
HELIX    2 AA2 ALA Y  381  GLU Y  384  5                                   4    
HELIX    3 AA3 SER Y  755  GLN Y  759  5                                   5    
HELIX    4 AA4 SER Y 1044  ILE Y 1062  1                                  19    
HELIX    5 AA5 GLU Y 1069  SER Y 1075  1                                   7    
HELIX    6 AA6 GLY Y 1091  SER Y 1096  1                                   6    
HELIX    7 AA7 PHE Y 1097  ILE Y 1100  5                                   4    
HELIX    8 AA8 SER Y 1101  VAL Y 1109  1                                   9    
HELIX    9 AA9 THR Y 1125  ARG Y 1138  1                                  14    
HELIX   10 AB1 LEU Z   53  GLY Z   61  5                                   9    
HELIX   11 AB2 HIS Z  103  LYS Z  116  1                                  14    
HELIX   12 AB3 SER Z  126  GLU Z  130  5                                   5    
HELIX   13 AB4 LEU Z  199  GLN Z  206  5                                   8    
HELIX   14 AB5 TYR Z  221  PHE Z  232  1                                  12    
HELIX   15 AB6 HIS Z  233  THR Z  238  5                                   6    
HELIX   16 AB7 PRO Z  241  SER Z  246  1                                   6    
HELIX   17 AB8 ASP Z  249  TRP Z  264  1                                  16    
HELIX   18 AB9 ASN Z  276  LEU Z  288  1                                  13    
HELIX   19 AC1 ASP Z  291  ILE Z  301  1                                  11    
HELIX   20 AC2 SER Z  303  CYS Z  318  1                                  16    
HELIX   21 AC3 ASN Z  335  ILE Z  337  5                                   3    
HELIX   22 AC4 PRO B  250  LYS B  254  5                                   5    
HELIX   23 AC5 ALA B  381  GLU B  384  5                                   4    
HELIX   24 AC6 SER B  755  GLN B  759  5                                   5    
HELIX   25 AC7 SER B 1044  ILE B 1062  1                                  19    
HELIX   26 AC8 GLU B 1069  SER B 1075  1                                   7    
HELIX   27 AC9 GLY B 1091  SER B 1096  1                                   6    
HELIX   28 AD1 PHE B 1097  ILE B 1100  5                                   4    
HELIX   29 AD2 SER B 1101  VAL B 1109  1                                   9    
HELIX   30 AD3 THR B 1125  ARG B 1138  1                                  14    
HELIX   31 AD4 LEU C   53  GLY C   61  5                                   9    
HELIX   32 AD5 HIS C  103  LYS C  116  1                                  14    
HELIX   33 AD6 LEU C  199  GLN C  206  5                                   8    
HELIX   34 AD7 TYR C  221  PHE C  232  1                                  12    
HELIX   35 AD8 HIS C  233  THR C  238  5                                   6    
HELIX   36 AD9 PRO C  241  SER C  246  1                                   6    
HELIX   37 AE1 ASP C  249  GLU C  263  1                                  15    
HELIX   38 AE2 ASN C  276  LEU C  288  1                                  13    
HELIX   39 AE3 ASP C  291  ILE C  301  1                                  11    
HELIX   40 AE4 SER C  303  CYS C  318  1                                  16    
HELIX   41 AE5 ASN C  335  ILE C  337  5                                   3    
SHEET    1 AA1 7 ARG X 441  LYS X 447  0                                        
SHEET    2 AA1 7 VAL X 455  GLY X 457 -1  O  LEU X 456   N  VAL X 445           
SHEET    3 AA1 7 LYS X 501  LYS X 505 -1  O  ILE X 502   N  VAL X 455           
SHEET    4 AA1 7 HIS X 477  ILE X 484 -1  N  GLY X 483   O  ARG X 503           
SHEET    5 AA1 7 LEU X 470  MET X 472 -1  N  LEU X 470   O  VAL X 479           
SHEET    6 AA1 7 ILE X 517  CYS X 519 -1  O  CYS X 519   N  VAL X 471           
SHEET    7 AA1 7 ARG X 441  LYS X 447 -1  N  LEU X 442   O  LEU X 518           
SHEET    1 AA2 2 ILE X 464  CYS X 465  0                                        
SHEET    2 AA2 2 THR X 493  VAL X 494 -1  O  VAL X 494   N  ILE X 464           
SHEET    1 AA3 7 GLY X 528  VAL X 536  0                                        
SHEET    2 AA3 7 ILE X 592  ILE X 601 -1  O  ALA X 593   N  ALA X 533           
SHEET    3 AA3 7 CYS X 557  LEU X 566 -1  N  ALA X 565   O  ARG X 594           
SHEET    4 AA3 7 TYR X 548  ILE X 554 -1  N  ALA X 550   O  VAL X 561           
SHEET    5 AA3 7 ARG X 614  ASP X 619 -1  O  THR X 616   N  HIS X 553           
SHEET    6 AA3 7 LYS X 622  VAL X 629 -1  O  GLY X 627   N  PHE X 615           
SHEET    7 AA3 7 GLY X 528  VAL X 536 -1  N  VAL X 536   O  ILE X 626           
SHEET    1 AA4 5 VAL Y1004  HIS Y1009  0                                        
SHEET    2 AA4 5 GLN Y1025  THR Y1032 -1  O  LEU Y1029   N  CYS Y1008           
SHEET    3 AA4 5 ILE Y1037  LEU Y1043 -1  O  VAL Y1040   N  VAL Y1028           
SHEET    4 AA4 5 TYR Y   3  GLN Y  10 -1  N  TYR Y   5   O  THR Y1041           
SHEET    5 AA4 5 PHE Y1088  ASP Y1090  1  O  ILE Y1089   N  VAL Y   6           
SHEET    1 AA5 4 GLY Y  17  GLY Y  21  0                                        
SHEET    2 AA5 4 ASN Y  30  LYS Y  35 -1  O  LEU Y  32   N  VAL Y  19           
SHEET    3 AA5 4 ARG Y  38  VAL Y  43 -1  O  GLU Y  40   N  ILE Y  33           
SHEET    4 AA5 4 ARG Y  50  GLY Y  56 -1  O  ARG Y  50   N  VAL Y  43           
SHEET    1 AA6 4 ILE Y  61  PHE Y  67  0                                        
SHEET    2 AA6 4 LEU Y  76  THR Y  81 -1  O  PHE Y  78   N  GLU Y  65           
SHEET    3 AA6 4 ASN Y  85  LYS Y  92 -1  O  LEU Y  89   N  LEU Y  77           
SHEET    4 AA6 4 ASP Y  99  ASN Y 107 -1  O  ILE Y 101   N  GLU Y  90           
SHEET    1 AA7 4 ILE Y 121  ILE Y 124  0                                        
SHEET    2 AA7 4 MET Y 130  ARG Y 134 -1  O  GLY Y 132   N  ILE Y 123           
SHEET    3 AA7 4 LEU Y 139  PRO Y 144 -1  O  LYS Y 141   N  LEU Y 133           
SHEET    4 AA7 4 PHE Y 155  ARG Y 158 -1  O  PHE Y 155   N  VAL Y 142           
SHEET    1 AA8 4 VAL Y 164  PHE Y 169  0                                        
SHEET    2 AA8 4 THR Y 177  ASP Y 184 -1  O  CYS Y 179   N  LYS Y 168           
SHEET    3 AA8 4 GLY Y 187  SER Y 196 -1  O  HIS Y 189   N  TYR Y 182           
SHEET    4 AA8 4 GLU Y 201  LYS Y 208 -1  O  ASN Y 203   N  GLU Y 194           
SHEET    1 AA9 4 MET Y 218  ALA Y 221  0                                        
SHEET    2 AA9 4 ALA Y 229  ILE Y 232 -1  O  ILE Y 230   N  ILE Y 220           
SHEET    3 AA9 4 ILE Y 237  ASN Y 241 -1  O  THR Y 238   N  ILE Y 231           
SHEET    4 AA9 4 LYS Y 244  ILE Y 248 -1  O  LYS Y 244   N  ASN Y 241           
SHEET    1 AB1 4 ILE Y 258  ARG Y 263  0                                        
SHEET    2 AB1 4 ARG Y 270  ASP Y 275 -1  O  LEU Y 272   N  ASN Y 262           
SHEET    3 AB1 4 ARG Y 279  GLU Y 286 -1  O  PHE Y 281   N  LEU Y 273           
SHEET    4 AB1 4 ASP Y 299  GLU Y 307 -1  O  ASP Y 299   N  GLU Y 286           
SHEET    1 AB2 4 ALA Y 311  TYR Y 316  0                                        
SHEET    2 AB2 4 VAL Y 321  SER Y 326 -1  O  GLY Y 325   N  GLU Y 312           
SHEET    3 AB2 4 SER Y 331  LEU Y 336 -1  O  VAL Y 334   N  VAL Y 322           
SHEET    4 AB2 4 VAL Y 347  PHE Y 353 -1  O  MET Y 350   N  LEU Y 333           
SHEET    1 AB3 4 ILE Y 359  VAL Y 365  0                                        
SHEET    2 AB3 4 GLN Y 374  SER Y 379 -1  O  CYS Y 378   N  ASP Y 361           
SHEET    3 AB3 4 SER Y 386  GLY Y 393 -1  O  SER Y 386   N  SER Y 379           
SHEET    4 AB3 4 LYS Y 709  PRO Y 716 -1  O  VAL Y 715   N  LEU Y 387           
SHEET    1 AB4 4 ILE Y 396  ASP Y 403  0                                        
SHEET    2 AB4 4 THR Y 698  ILE Y 704 -1  O  LEU Y 699   N  ILE Y 402           
SHEET    3 AB4 4 SER Y 690  ALA Y 694 -1  N  LEU Y 693   O  THR Y 700           
SHEET    4 AB4 4 TYR Y 678  LEU Y 682 -1  N  TYR Y 678   O  ALA Y 694           
SHEET    1 AB5 4 GLY Y 409  LEU Y 413  0                                        
SHEET    2 AB5 4 THR Y 424  PHE Y 429 -1  O  VAL Y 426   N  TRP Y 411           
SHEET    3 AB5 4 GLN Y 432  ASN Y 439 -1  O  LEU Y 436   N  LEU Y 425           
SHEET    4 AB5 4 GLU Y 442  THR Y 446 -1  O  GLU Y 444   N  MET Y 437           
SHEET    1 AB6 4 THR Y 457  VAL Y 463  0                                        
SHEET    2 AB6 4 GLN Y 467  THR Y 472 -1  O  ILE Y 471   N  PHE Y 459           
SHEET    3 AB6 4 VAL Y 476  SER Y 480 -1  O  VAL Y 479   N  LEU Y 468           
SHEET    4 AB6 4 LEU Y 486  TRP Y 490 -1  O  SER Y 488   N  LEU Y 478           
SHEET    1 AB7 4 VAL Y 500  CYS Y 503  0                                        
SHEET    2 AB7 4 GLN Y 507  VAL Y 512 -1  O  ALA Y 511   N  VAL Y 500           
SHEET    3 AB7 4 ALA Y 515  GLN Y 520 -1  O  LEU Y 519   N  VAL Y 508           
SHEET    4 AB7 4 GLN Y 528  HIS Y 531 -1  O  SER Y 530   N  TYR Y 518           
SHEET    1 AB8 3 VAL Y 538  ASP Y 542  0                                        
SHEET    2 AB8 3 LEU Y 555  LEU Y 560 -1  O  GLY Y 559   N  ALA Y 539           
SHEET    3 AB8 3 ALA Y 566  LYS Y 570 -1  O  ARG Y 567   N  ILE Y 558           
SHEET    1 AB9 4 PRO Y 588  PHE Y 596  0                                        
SHEET    2 AB9 4 SER Y 599  LEU Y 606 -1  O  LEU Y 603   N  LEU Y 592           
SHEET    3 AB9 4 ALA Y 610  LEU Y 616 -1  O  ALA Y 610   N  LEU Y 606           
SHEET    4 AB9 4 LEU Y 623  THR Y 630 -1  O  SER Y 624   N  GLY Y 615           
SHEET    1 AC1 4 VAL Y 637  ARG Y 642  0                                        
SHEET    2 AC1 4 THR Y 647  CYS Y 652 -1  O  ASN Y 648   N  PHE Y 641           
SHEET    3 AC1 4 THR Y 657  TYR Y 660 -1  O  THR Y 657   N  ALA Y 651           
SHEET    4 AC1 4 VAL Y 667  ASN Y 670 -1  O  VAL Y 667   N  TYR Y 660           
SHEET    1 AC2 3 SER Y 720  GLN Y 727  0                                        
SHEET    2 AC2 3 CYS Y 732  VAL Y 742 -1  O  LEU Y 736   N  ARG Y 722           
SHEET    3 AC2 3 THR Y 750  ALA Y 751 -1  O  THR Y 750   N  VAL Y 742           
SHEET    1 AC3 5 SER Y 720  GLN Y 727  0                                        
SHEET    2 AC3 5 CYS Y 732  VAL Y 742 -1  O  LEU Y 736   N  ARG Y 722           
SHEET    3 AC3 5 GLU Y 785  ASP Y 795 -1  O  ASN Y 790   N  SER Y 737           
SHEET    4 AC3 5 VAL Y 801  GLN Y 806 -1  O  HIS Y 803   N  ILE Y 793           
SHEET    5 AC3 5 SER Y 762  VAL Y 765  1  N  SER Y 764   O  ALA Y 804           
SHEET    1 AC4 4 GLU Y 811  CYS Y 819  0                                        
SHEET    2 AC4 4 TYR Y 828  MET Y 835 -1  O  GLY Y 832   N  LEU Y 814           
SHEET    3 AC4 4 GLY Y 846  SER Y 854 -1  O  PHE Y 851   N  PHE Y 829           
SHEET    4 AC4 4 LYS Y 857  VAL Y 866 -1  O  ALA Y 862   N  VAL Y 850           
SHEET    1 AC5 4 VAL Y 870  PHE Y 876  0                                        
SHEET    2 AC5 4 LYS Y 879  ILE Y 884 -1  O  LYS Y 879   N  PHE Y 876           
SHEET    3 AC5 4 THR Y 887  TRP Y 893 -1  O  TYR Y 891   N  LEU Y 880           
SHEET    4 AC5 4 LEU Y 899  TYR Y 906 -1  O  ARG Y 900   N  GLU Y 892           
SHEET    1 AC6 4 TYR Y 913  LYS Y 917  0                                        
SHEET    2 AC6 4 PHE Y 920  GLY Y 924 -1  O  LEU Y 922   N  LYS Y 915           
SHEET    3 AC6 4 VAL Y 930  TYR Y 935 -1  O  LEU Y 933   N  ILE Y 921           
SHEET    4 AC6 4 PHE Y 942  ASP Y 948 -1  O  ILE Y 945   N  LEU Y 932           
SHEET    1 AC7 4 MET Y 954  ASP Y 961  0                                        
SHEET    2 AC7 4 ASN Y 964  GLU Y 969 -1  O  LEU Y 966   N  GLU Y 958           
SHEET    3 AC7 4 ASN Y 973  GLN Y 978 -1  O  ASN Y 973   N  GLU Y 969           
SHEET    4 AC7 4 GLN Y 993  HIS Y 999 -1  O  PHE Y 998   N  LEU Y 974           
SHEET    1 AC8 2 GLN Y1113  TYR Y1114  0                                        
SHEET    2 AC8 2 ARG Y1122  GLU Y1123 -1  O  ARG Y1122   N  TYR Y1114           
SHEET    1 AC9 4 GLU Z  65  GLU Z  66  0                                        
SHEET    2 AC9 4 PHE Z 135  GLU Z 147 -1  O  TYR Z 144   N  GLU Z  65           
SHEET    3 AC9 4 ILE Z 154  ARG Z 171 -1  O  ARG Z 162   N  THR Z 138           
SHEET    4 AC9 4 THR Z  96  LEU Z 101 -1  N  LEU Z  97   O  ALA Z 159           
SHEET    1 AD1 5 CYS Z  78  VAL Z  83  0                                        
SHEET    2 AD1 5 GLN Z 178  ILE Z 184 -1  O  VAL Z 182   N  GLN Z  79           
SHEET    3 AD1 5 ILE Z 154  ARG Z 171 -1  N  LEU Z 168   O  LYS Z 181           
SHEET    4 AD1 5 PHE Z 135  GLU Z 147 -1  N  THR Z 138   O  ARG Z 162           
SHEET    5 AD1 5 THR Z 119  ALA Z 124 -1  N  VAL Z 122   O  THR Z 137           
SHEET    1 AD2 3 GLU Z 330  THR Z 333  0                                        
SHEET    2 AD2 3 SER Z 320  CYS Z 323 -1  N  LEU Z 321   O  ILE Z 331           
SHEET    3 AD2 3 LEU Z 422  THR Z 425 -1  O  THR Z 425   N  SER Z 320           
SHEET    1 AD3 6 MET Z 346  VAL Z 350  0                                        
SHEET    2 AD3 6 VAL Z 356  VAL Z 362 -1  O  HIS Z 357   N  TYR Z 349           
SHEET    3 AD3 6 LYS Z 413  THR Z 418 -1  O  TRP Z 415   N  VAL Z 362           
SHEET    4 AD3 6 HIS Z 397  ALA Z 404 -1  N  TRP Z 400   O  GLY Z 416           
SHEET    5 AD3 6 TYR Z 384  CYS Z 391 -1  N  ALA Z 385   O  THR Z 403           
SHEET    6 AD3 6 LEU Z 368  SER Z 375 -1  N  SER Z 375   O  TRP Z 386           
SHEET    1 AD4 5 VAL B1004  HIS B1009  0                                        
SHEET    2 AD4 5 GLN B1025  THR B1032 -1  O  LEU B1029   N  CYS B1008           
SHEET    3 AD4 5 ILE B1037  LEU B1043 -1  O  VAL B1040   N  VAL B1028           
SHEET    4 AD4 5 TYR B   3  GLN B  10 -1  N  TYR B   5   O  THR B1041           
SHEET    5 AD4 5 PHE B1088  ASP B1090  1  O  ILE B1089   N  VAL B   6           
SHEET    1 AD5 4 GLY B  17  GLY B  21  0                                        
SHEET    2 AD5 4 ASN B  30  LYS B  35 -1  O  LEU B  32   N  VAL B  19           
SHEET    3 AD5 4 ARG B  38  VAL B  43 -1  O  GLU B  40   N  ILE B  33           
SHEET    4 AD5 4 ARG B  50  GLY B  56 -1  O  ARG B  50   N  VAL B  43           
SHEET    1 AD6 4 ILE B  61  PHE B  67  0                                        
SHEET    2 AD6 4 LEU B  76  THR B  81 -1  O  PHE B  78   N  GLU B  65           
SHEET    3 AD6 4 ASN B  85  LYS B  92 -1  O  LEU B  89   N  LEU B  77           
SHEET    4 AD6 4 ASP B  99  ASN B 107 -1  O  ILE B 101   N  GLU B  90           
SHEET    1 AD7 4 ILE B 121  ILE B 124  0                                        
SHEET    2 AD7 4 MET B 130  ARG B 134 -1  O  GLY B 132   N  ILE B 123           
SHEET    3 AD7 4 LEU B 139  PRO B 144 -1  O  LYS B 141   N  LEU B 133           
SHEET    4 AD7 4 PHE B 155  ARG B 158 -1  O  PHE B 155   N  VAL B 142           
SHEET    1 AD8 4 VAL B 164  PHE B 169  0                                        
SHEET    2 AD8 4 THR B 177  ASP B 184 -1  O  CYS B 179   N  LYS B 168           
SHEET    3 AD8 4 GLY B 187  SER B 196 -1  O  GLY B 187   N  ASP B 184           
SHEET    4 AD8 4 GLU B 201  GLN B 209 -1  O  ASN B 203   N  GLU B 194           
SHEET    1 AD9 4 MET B 218  ALA B 221  0                                        
SHEET    2 AD9 4 ALA B 229  ILE B 232 -1  O  ILE B 230   N  ILE B 220           
SHEET    3 AD9 4 ILE B 237  ASN B 241 -1  O  THR B 238   N  ILE B 231           
SHEET    4 AD9 4 LYS B 244  ILE B 248 -1  O  LEU B 246   N  TYR B 239           
SHEET    1 AE1 4 ILE B 258  ARG B 263  0                                        
SHEET    2 AE1 4 ARG B 270  ASP B 275 -1  O  LEU B 272   N  ASN B 262           
SHEET    3 AE1 4 ARG B 279  GLU B 286 -1  O  PHE B 281   N  LEU B 273           
SHEET    4 AE1 4 ASP B 299  GLU B 307 -1  O  ASP B 299   N  GLU B 286           
SHEET    1 AE2 4 ALA B 311  TYR B 316  0                                        
SHEET    2 AE2 4 VAL B 321  SER B 326 -1  O  GLY B 325   N  GLU B 312           
SHEET    3 AE2 4 SER B 331  LEU B 336 -1  O  VAL B 334   N  VAL B 322           
SHEET    4 AE2 4 VAL B 347  PHE B 353 -1  O  MET B 350   N  LEU B 333           
SHEET    1 AE3 4 ILE B 359  VAL B 365  0                                        
SHEET    2 AE3 4 GLN B 374  SER B 379 -1  O  CYS B 378   N  ASP B 361           
SHEET    3 AE3 4 SER B 386  GLY B 393 -1  O  SER B 386   N  SER B 379           
SHEET    4 AE3 4 LYS B 709  PRO B 716 -1  O  VAL B 715   N  LEU B 387           
SHEET    1 AE4 4 ILE B 396  ASP B 403  0                                        
SHEET    2 AE4 4 THR B 698  ILE B 704 -1  O  LEU B 699   N  ILE B 402           
SHEET    3 AE4 4 SER B 690  ALA B 694 -1  N  LEU B 693   O  THR B 700           
SHEET    4 AE4 4 TYR B 678  LEU B 682 -1  N  TYR B 678   O  ALA B 694           
SHEET    1 AE5 4 GLY B 409  LEU B 413  0                                        
SHEET    2 AE5 4 THR B 424  PHE B 429 -1  O  VAL B 426   N  TRP B 411           
SHEET    3 AE5 4 GLN B 432  ASN B 439 -1  O  LEU B 436   N  LEU B 425           
SHEET    4 AE5 4 GLU B 442  THR B 446 -1  O  GLU B 444   N  MET B 437           
SHEET    1 AE6 4 THR B 457  VAL B 463  0                                        
SHEET    2 AE6 4 GLN B 467  THR B 472 -1  O  ILE B 471   N  PHE B 459           
SHEET    3 AE6 4 VAL B 476  SER B 480 -1  O  VAL B 479   N  LEU B 468           
SHEET    4 AE6 4 LEU B 486  TRP B 490 -1  O  TRP B 490   N  VAL B 476           
SHEET    1 AE7 4 VAL B 500  CYS B 503  0                                        
SHEET    2 AE7 4 GLN B 507  VAL B 512 -1  O  ALA B 511   N  VAL B 500           
SHEET    3 AE7 4 ALA B 515  GLN B 520 -1  O  LEU B 519   N  VAL B 508           
SHEET    4 AE7 4 GLN B 528  HIS B 531 -1  O  SER B 530   N  TYR B 518           
SHEET    1 AE8 3 VAL B 538  ASP B 542  0                                        
SHEET    2 AE8 3 LEU B 555  LEU B 560 -1  O  GLY B 559   N  ALA B 539           
SHEET    3 AE8 3 ALA B 566  LYS B 570 -1  O  ARG B 567   N  ILE B 558           
SHEET    1 AE9 4 PRO B 588  PHE B 596  0                                        
SHEET    2 AE9 4 SER B 599  LEU B 606 -1  O  LEU B 603   N  LEU B 592           
SHEET    3 AE9 4 ALA B 610  GLY B 615 -1  O  ALA B 610   N  LEU B 606           
SHEET    4 AE9 4 LYS B 628  THR B 630 -1  O  VAL B 629   N  LEU B 611           
SHEET    1 AF1 4 VAL B 637  ARG B 642  0                                        
SHEET    2 AF1 4 THR B 647  CYS B 652 -1  O  ASN B 648   N  PHE B 641           
SHEET    3 AF1 4 THR B 657  TYR B 660 -1  O  THR B 657   N  ALA B 651           
SHEET    4 AF1 4 VAL B 667  ASN B 670 -1  O  VAL B 667   N  TYR B 660           
SHEET    1 AF2 3 SER B 720  GLN B 727  0                                        
SHEET    2 AF2 3 CYS B 732  VAL B 742 -1  O  LEU B 736   N  ARG B 722           
SHEET    3 AF2 3 THR B 750  ALA B 751 -1  O  THR B 750   N  VAL B 742           
SHEET    1 AF3 5 SER B 720  GLN B 727  0                                        
SHEET    2 AF3 5 CYS B 732  VAL B 742 -1  O  LEU B 736   N  ARG B 722           
SHEET    3 AF3 5 GLU B 785  ASP B 795 -1  O  ASN B 790   N  SER B 737           
SHEET    4 AF3 5 VAL B 801  GLN B 806 -1  O  HIS B 803   N  ILE B 793           
SHEET    5 AF3 5 SER B 762  SER B 764  1  N  SER B 764   O  ALA B 804           
SHEET    1 AF4 4 GLU B 811  CYS B 819  0                                        
SHEET    2 AF4 4 TYR B 828  MET B 835 -1  O  GLY B 832   N  LEU B 814           
SHEET    3 AF4 4 GLY B 846  SER B 854 -1  O  PHE B 851   N  PHE B 829           
SHEET    4 AF4 4 LYS B 857  VAL B 866 -1  O  ALA B 862   N  VAL B 850           
SHEET    1 AF5 4 VAL B 870  PHE B 876  0                                        
SHEET    2 AF5 4 LYS B 879  ILE B 884 -1  O  LYS B 879   N  PHE B 876           
SHEET    3 AF5 4 THR B 887  TRP B 893 -1  O  TYR B 891   N  LEU B 880           
SHEET    4 AF5 4 LEU B 899  TYR B 906 -1  O  ARG B 900   N  GLU B 892           
SHEET    1 AF6 4 TYR B 913  LYS B 917  0                                        
SHEET    2 AF6 4 PHE B 920  GLY B 924 -1  O  LEU B 922   N  LYS B 915           
SHEET    3 AF6 4 VAL B 930  TYR B 935 -1  O  LEU B 933   N  ILE B 921           
SHEET    4 AF6 4 PHE B 942  ASP B 948 -1  O  ILE B 945   N  LEU B 932           
SHEET    1 AF7 4 MET B 954  ASP B 961  0                                        
SHEET    2 AF7 4 ASN B 964  GLU B 969 -1  O  LEU B 966   N  GLU B 958           
SHEET    3 AF7 4 ASN B 973  GLN B 978 -1  O  ASN B 973   N  GLU B 969           
SHEET    4 AF7 4 GLN B 993  HIS B 999 -1  O  PHE B 998   N  LEU B 974           
SHEET    1 AF8 2 GLN B1113  TYR B1114  0                                        
SHEET    2 AF8 2 ARG B1122  GLU B1123 -1  O  ARG B1122   N  TYR B1114           
SHEET    1 AF9 4 GLU C  65  GLU C  66  0                                        
SHEET    2 AF9 4 PHE C 135  GLU C 147 -1  O  TYR C 144   N  GLU C  65           
SHEET    3 AF9 4 ILE C 154  THR C 172 -1  O  ARG C 162   N  THR C 138           
SHEET    4 AF9 4 THR C  96  LEU C 101 -1  N  LEU C  97   O  ALA C 159           
SHEET    1 AG1 5 CYS C  78  VAL C  83  0                                        
SHEET    2 AG1 5 GLN C 178  ILE C 184 -1  O  VAL C 182   N  GLN C  79           
SHEET    3 AG1 5 ILE C 154  THR C 172 -1  N  LEU C 168   O  LYS C 181           
SHEET    4 AG1 5 PHE C 135  GLU C 147 -1  N  THR C 138   O  ARG C 162           
SHEET    5 AG1 5 THR C 119  ALA C 124 -1  N  VAL C 122   O  THR C 137           
SHEET    1 AG2 3 GLU C 330  THR C 333  0                                        
SHEET    2 AG2 3 SER C 320  CYS C 323 -1  N  LEU C 321   O  ILE C 331           
SHEET    3 AG2 3 LEU C 422  THR C 425 -1  O  THR C 425   N  SER C 320           
SHEET    1 AG3 6 MET C 346  VAL C 350  0                                        
SHEET    2 AG3 6 VAL C 356  VAL C 362 -1  O  HIS C 357   N  TYR C 349           
SHEET    3 AG3 6 LYS C 413  THR C 418 -1  O  TRP C 415   N  VAL C 362           
SHEET    4 AG3 6 HIS C 397  ALA C 404 -1  N  TRP C 400   O  GLY C 416           
SHEET    5 AG3 6 TYR C 384  CYS C 391 -1  N  THR C 387   O  LYS C 401           
SHEET    6 AG3 6 LEU C 368  SER C 375 -1  N  SER C 375   O  TRP C 386           
SHEET    1 AG4 7 ARG A 441  LYS A 447  0                                        
SHEET    2 AG4 7 THR A 453  GLY A 457 -1  O  LEU A 456   N  VAL A 445           
SHEET    3 AG4 7 LEU A 500  LYS A 505 -1  O  LEU A 504   N  THR A 453           
SHEET    4 AG4 7 HIS A 477  SER A 486 -1  N  GLY A 483   O  ARG A 503           
SHEET    5 AG4 7 LEU A 470  MET A 472 -1  N  LEU A 470   O  VAL A 479           
SHEET    6 AG4 7 ILE A 517  CYS A 519 -1  O  CYS A 519   N  VAL A 471           
SHEET    7 AG4 7 ARG A 441  LYS A 447 -1  N  LEU A 442   O  LEU A 518           
SHEET    1 AG5 2 ILE A 464  CYS A 465  0                                        
SHEET    2 AG5 2 THR A 493  VAL A 494 -1  O  VAL A 494   N  ILE A 464           
SHEET    1 AG6 7 GLY A 528  ILE A 537  0                                        
SHEET    2 AG6 7 ILE A 592  ILE A 601 -1  O  ALA A 593   N  ALA A 533           
SHEET    3 AG6 7 GLU A 559  LEU A 566 -1  N  ALA A 565   O  ARG A 594           
SHEET    4 AG6 7 TYR A 548  ILE A 554 -1  N  ALA A 550   O  VAL A 561           
SHEET    5 AG6 7 ARG A 614  ASP A 619 -1  O  THR A 616   N  HIS A 553           
SHEET    6 AG6 7 LYS A 622  VAL A 629 -1  O  GLY A 627   N  PHE A 615           
SHEET    7 AG6 7 GLY A 528  ILE A 537 -1  N  VAL A 536   O  ILE A 626           
SSBOND   1 CYS X  519    CYS X  525                          1555   1555  2.06  
SSBOND   2 CYS Y   18    CYS Y  313                          1555   1555  2.10  
SSBOND   3 CYS B   18    CYS B  313                          1555   1555  2.11  
LINK         CA  LEU Y 569                 CB  LEU Y 576     1555   1555  1.52  
LINK         SG  CYS Z 323                ZN    ZN Z 501     1555   1555  1.96  
LINK         SG  CYS Z 326                ZN    ZN Z 501     1555   1555  2.43  
LINK         SG  CYS Z 391                ZN    ZN Z 501     1555   1555  2.22  
LINK         SG  CYS Z 394                ZN    ZN Z 501     1555   1555  1.94  
LINK         SG  CYS C 323                ZN    ZN C 501     1555   1555  2.10  
LINK         SG  CYS C 326                ZN    ZN C 501     1555   1555  2.61  
LINK         SG  CYS C 391                ZN    ZN C 501     1555   1555  2.53  
SITE     1 AC1  4 CYS Z 323  CYS Z 326  CYS Z 391  CYS Z 394                    
SITE     1 AC2 19 VAL X 536  VAL X 570  ASP X 571  LYS X 572                    
SITE     2 AC2 19 LYS X 573  SER X 574  GLY X 575  ILE X 626                    
SITE     3 AC2 19 GLY X 627  LYS X 628  ASN Z 351  PRO Z 352                    
SITE     4 AC2 19 HIS Z 353  GLU Z 377  HIS Z 378  SER Z 379                    
SITE     5 AC2 19 TRP Z 380  TRP Z 386  TRP Z 400                               
SITE     1 AC3  4 CYS C 323  CYS C 326  CYS C 391  CYS C 394                    
SITE     1 AC4 17 GLN A 534  VAL A 570  ASP A 571  LYS A 572                    
SITE     2 AC4 17 LYS A 573  SER A 574  GLY A 575  LYS A 628                    
SITE     3 AC4 17 ASN C 351  PRO C 352  HIS C 353  GLU C 377                    
SITE     4 AC4 17 HIS C 378  SER C 379  TRP C 380  TRP C 386                    
SITE     5 AC4 17 TRP C 400                                                     
CRYST1  156.747  111.522  175.057  90.00  95.81  90.00 P 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006380  0.000000  0.000649        0.00000                         
SCALE2      0.000000  0.008967  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005742        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system