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Database: PDB
Entry: 3E1Y
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HEADER    TRANSLATION                             05-AUG-08   3E1Y              
TITLE     CRYSTAL STRUCTURE OF HUMAN ERF1/ERF3 COMPLEX                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR SUBUNIT 1;         
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: ERF1, EUKARYOTIC RELEASE FACTOR 1, TB3-1, PROTEIN CL1;      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR GTP-BINDING SUBUNIT
COMPND   8 ERF3A;                                                               
COMPND   9 CHAIN: E, F, G, H;                                                   
COMPND  10 FRAGMENT: UNP RESIDUES 301-499;                                      
COMPND  11 SYNONYM: EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR SUBUNIT 3A, ERF3A,  
COMPND  12 G1 TO S PHASE TRANSITION PROTEIN 1 HOMOLOG;                          
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ETF1, ERF1, RF1, SUP45L1;                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL-21 (DE3);                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRC-NIV-N;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: GSPT1, ERF3A;                                                  
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL-21 (DE3);                               
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1                                 
KEYWDS    TRANSLATION TERMINATION, ERF1, ERF3, PEPTIDE RELEASE, PTC, PROTEIN    
KEYWDS   2 BIOSYNTHESIS, GTP-BINDING, NUCLEOTIDE-BINDING, TRANSLATION           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.CHENG,M.LIM,C.KONG,H.SONG                                           
REVDAT   2   13-JUL-11 3E1Y    1       VERSN                                    
REVDAT   1   19-MAY-09 3E1Y    0                                                
JRNL        AUTH   Z.CHENG,K.SAITO,A.V.PISAREV,M.WADA,V.P.PISAREVA,T.V.PESTOVA, 
JRNL        AUTH 2 M.GAJDA,A.ROUND,C.KONG,M.LIM,Y.NAKAMURA,D.I.SVERGUN,K.ITO,   
JRNL        AUTH 3 H.SONG                                                       
JRNL        TITL   STRUCTURAL INSIGHTS INTO ERF3 AND STOP CODON RECOGNITION BY  
JRNL        TITL 2 ERF1                                                         
JRNL        REF    GENES DEV.                    V.  23  1106 2009              
JRNL        REFN                   ISSN 0890-9369                               
JRNL        PMID   19417105                                                     
JRNL        DOI    10.1101/GAD.1770109                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0077                                      
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) : 3.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 33542                          
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) : 0.262                           
REMARK   3   R VALUE            (WORKING SET) : 0.260                           
REMARK   3   FREE R VALUE                     : 0.304                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1777                            
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) : 3.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2423                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3500                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 129                          
REMARK   3   BIN FREE R VALUE                    : 0.4240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 17048                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 62                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 87.89                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.99000                                              
REMARK   3    B22 (A**2) : 0.99000                                              
REMARK   3    B33 (A**2) : -1.98000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.838         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.713         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 112.939       
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.915                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.895                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 17360 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 23364 ; 1.469 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2146 ;13.457 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   734 ;37.192 ;24.632       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3304 ;22.750 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    98 ;17.655 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2714 ; 0.103 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12540 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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): 10744 ; 0.618 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 17360 ; 1.195 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6616 ; 1.019 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6004 ; 1.654 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 4                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      8       A     412      1                      
REMARK   3           1     B      8       B     412      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   2905 ; 0.010 ; 0.050           
REMARK   3   TIGHT THERMAL      1    A (A**2):   2905 ; 0.020 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : E F                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     E    440       E     634      1                      
REMARK   3           1     F    440       F     634      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    E    (A):   1513 ; 0.030 ; 0.050           
REMARK   3   TIGHT THERMAL      2    E (A**2):   1513 ; 0.020 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : G H                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     G    440       G     634      1                      
REMARK   3           1     H    440       H     634      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    G    (A):   1513 ; 0.010 ; 0.050           
REMARK   3   TIGHT THERMAL      3    G (A**2):   1513 ; 0.020 ; 0.500           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C      8       C     412      1                      
REMARK   3           1     D      8       D     412      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    C    (A):   2449 ; 0.010 ; 0.050           
REMARK   3   TIGHT THERMAL      4    C (A**2):   2449 ; 0.010 ; 0.500           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 16                                         
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 :   A     8        A   141                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.4417 106.3734  -0.5756              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3454 T22:   0.3725                                     
REMARK   3      T33:   0.4059 T12:   0.0200                                     
REMARK   3      T13:   0.0807 T23:   0.0498                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.5056 L22:   6.9813                                     
REMARK   3      L33:   3.2957 L12:   1.7554                                     
REMARK   3      L13:  -0.5063 L23:  -1.1299                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1590 S12:   0.6135 S13:   0.3370                       
REMARK   3      S21:  -0.2374 S22:  -0.0436 S23:  -0.3596                       
REMARK   3      S31:   0.5101 S32:  -0.3536 S33:   0.2026                       
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 :   A   144        A   271                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.2582  79.8641  39.4160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6941 T22:   0.5032                                     
REMARK   3      T33:   0.6845 T12:  -0.0289                                     
REMARK   3      T13:   0.1465 T23:  -0.1161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5720 L22:   3.4035                                     
REMARK   3      L33:   8.6473 L12:  -0.6242                                     
REMARK   3      L13:   1.9670 L23:  -1.6442                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0115 S12:  -0.4909 S13:  -0.1749                       
REMARK   3      S21:  -0.0030 S22:   0.0001 S23:   0.1008                       
REMARK   3      S31:   0.2583 S32:  -0.0371 S33:  -0.0117                       
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 :   A   274        A   412                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.4999  74.6641  -3.1640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9249 T22:   0.5759                                     
REMARK   3      T33:   0.2126 T12:  -0.0601                                     
REMARK   3      T13:   0.0451 T23:  -0.3498                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4960 L22:   6.8086                                     
REMARK   3      L33:   9.0153 L12:  -0.2798                                     
REMARK   3      L13:   3.5132 L23:  -0.8721                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1435 S12:   0.5100 S13:  -0.4783                       
REMARK   3      S21:  -0.2341 S22:  -0.1116 S23:   1.3042                       
REMARK   3      S31:   0.6181 S32:  -0.5142 S33:   0.2551                       
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 :   B     8        B   141                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.3708 112.4308  18.9921              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3846 T22:   0.3568                                     
REMARK   3      T33:   0.3739 T12:   0.0224                                     
REMARK   3      T13:   0.0610 T23:   0.0923                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7077 L22:   9.5014                                     
REMARK   3      L33:   3.2451 L12:   1.7170                                     
REMARK   3      L13:  -1.1408 L23:  -0.1075                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0720 S12:  -0.2639 S13:  -0.3082                       
REMARK   3      S21:   0.5550 S22:  -0.1346 S23:   0.2781                       
REMARK   3      S31:  -0.2967 S32:   0.4726 S33:   0.2066                       
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   144        B   271                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.1189 111.2391 -21.0437              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4837 T22:   0.6872                                     
REMARK   3      T33:   0.6845 T12:  -0.0344                                     
REMARK   3      T13:  -0.1101 T23:   0.1503                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3302 L22:   3.9044                                     
REMARK   3      L33:   8.8549 L12:  -0.5377                                     
REMARK   3      L13:  -1.5529 L23:   1.8055                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0083 S12:   0.0283 S13:   0.0983                       
REMARK   3      S21:  -0.4231 S22:   0.0496 S23:  -0.1660                       
REMARK   3      S31:  -0.0001 S32:   0.2581 S33:  -0.0580                       
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 :   B   274        B   412                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3199 117.5595  21.5020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5814 T22:   0.9783                                     
REMARK   3      T33:   0.2137 T12:  -0.0745                                     
REMARK   3      T13:  -0.3435 T23:   0.0426                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5989 L22:   8.5110                                     
REMARK   3      L33:   7.9115 L12:  -0.3694                                     
REMARK   3      L13:   0.3812 L23:   2.2545                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1500 S12:  -0.2113 S13:   1.2943                       
REMARK   3      S21:   0.5717 S22:  -0.1312 S23:  -0.4590                       
REMARK   3      S31:  -0.5170 S32:   0.5276 S33:   0.2812                       
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 :   E   440        E   634                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.5118  89.8077   6.2830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4542 T22:   0.8646                                     
REMARK   3      T33:   0.4034 T12:   0.0711                                     
REMARK   3      T13:  -0.2033 T23:   0.3598                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2705 L22:   8.3813                                     
REMARK   3      L33:   8.5115 L12:  -1.3557                                     
REMARK   3      L13:  -1.2985 L23:   5.3951                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0507 S12:  -1.1239 S13:  -0.2319                       
REMARK   3      S21:   0.5883 S22:   0.1353 S23:  -0.4527                       
REMARK   3      S31:   0.5615 S32:   0.4389 S33:  -0.0846                       
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 :   F   440        F   634                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.8368  53.4705  12.0906              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8654 T22:   0.4813                                     
REMARK   3      T33:   0.3974 T12:   0.0899                                     
REMARK   3      T13:   0.3584 T23:  -0.2060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1663 L22:   3.2415                                     
REMARK   3      L33:   8.4660 L12:  -1.2259                                     
REMARK   3      L13:   5.3347 L23:  -1.3812                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1397 S12:   0.6085 S13:  -0.4560                       
REMARK   3      S21:  -1.1240 S22:  -0.0511 S23:  -0.2071                       
REMARK   3      S31:   0.5183 S32:   0.5641 S33:  -0.0886                       
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 :   G   440        G   634                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.7738  28.7564  20.2482              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9802 T22:   0.4274                                     
REMARK   3      T33:   1.0585 T12:   0.1584                                     
REMARK   3      T13:   0.0760 T23:  -0.1918                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0224 L22:   2.0818                                     
REMARK   3      L33:   8.4355 L12:   0.2975                                     
REMARK   3      L13:   2.8173 L23:   0.1079                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0622 S12:   0.0212 S13:  -0.4571                       
REMARK   3      S21:  -0.8453 S22:   0.0228 S23:  -0.0609                       
REMARK   3      S31:   0.2087 S32:   0.0175 S33:  -0.0850                       
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 :   H   440        H   634                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.2097  94.7510  -1.8651              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4274 T22:   0.9759                                     
REMARK   3      T33:   1.0647 T12:   0.1864                                     
REMARK   3      T13:  -0.1822 T23:   0.0755                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2229 L22:   4.9544                                     
REMARK   3      L33:   8.6054 L12:   0.4338                                     
REMARK   3      L13:   0.1342 L23:   2.8851                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0167 S12:  -0.8500 S13:  -0.0817                       
REMARK   3      S21:   0.0258 S22:   0.1064 S23:  -0.4630                       
REMARK   3      S31:  -0.0060 S32:   0.2269 S33:  -0.0897                       
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 :   C   274        C   412                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.8650  18.3066  56.1210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3151 T22:   1.2797                                     
REMARK   3      T33:   0.9488 T12:  -0.0900                                     
REMARK   3      T13:  -0.0978 T23:  -0.0812                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8547 L22:   7.8278                                     
REMARK   3      L33:   8.1702 L12:  -3.0170                                     
REMARK   3      L13:  -0.2516 L23:  -1.4583                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4547 S12:  -1.0472 S13:  -0.4007                       
REMARK   3      S21:   0.3664 S22:   0.0137 S23:  -0.6248                       
REMARK   3      S31:   0.1773 S32:   0.1352 S33:  -0.4684                       
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 :   D   274        D   412                          
REMARK   3    ORIGIN FOR THE GROUP (A):  68.6618  97.8433 -37.7616              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2796 T22:   0.2769                                     
REMARK   3      T33:   1.0153 T12:  -0.0912                                     
REMARK   3      T13:  -0.0820 T23:  -0.0973                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6992 L22:   4.3142                                     
REMARK   3      L33:   7.9539 L12:  -2.4296                                     
REMARK   3      L13:  -0.5571 L23:  -1.2144                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0371 S12:   0.3793 S13:  -0.6571                       
REMARK   3      S21:  -0.9102 S22:   0.4739 S23:  -0.3795                       
REMARK   3      S31:   0.0253 S32:   0.2200 S33:  -0.5110                       
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 :   C     8        C   141                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.1084  -2.9385  62.2240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1689 T22:   1.7639                                     
REMARK   3      T33:   1.2568 T12:   0.0885                                     
REMARK   3      T13:   0.1292 T23:   0.4560                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5608 L22:   9.1379                                     
REMARK   3      L33:   0.5886 L12:   2.9296                                     
REMARK   3      L13:   1.5869 L23:   0.5054                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1879 S12:  -0.9424 S13:  -0.6085                       
REMARK   3      S21:   0.5835 S22:  -0.3929 S23:   1.3750                       
REMARK   3      S31:   0.4738 S32:   0.3624 S33:   0.2050                       
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 :   D     8        D   141                          
REMARK   3    ORIGIN FOR THE GROUP (A):  89.9141 119.0832 -43.8386              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6790 T22:   1.1628                                     
REMARK   3      T33:   1.2951 T12:   0.0949                                     
REMARK   3      T13:   0.3888 T23:   0.1329                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.1423 L22:   3.6530                                     
REMARK   3      L33:   0.9658 L12:   3.2101                                     
REMARK   3      L13:  -0.0842 L23:   1.5316                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5383 S12:   0.8236 S13:   1.1445                       
REMARK   3      S21:  -0.8928 S22:   0.2391 S23:  -0.6085                       
REMARK   3      S31:   0.2736 S32:   0.4926 S33:   0.2992                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   144        C   270                          
REMARK   3    ORIGIN FOR THE GROUP (A): -37.0166  39.5383  56.8917              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7036 T22:   1.0496                                     
REMARK   3      T33:   1.1236 T12:  -0.1193                                     
REMARK   3      T13:  -0.1315 T23:  -0.0534                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9087 L22:   8.6705                                     
REMARK   3      L33:   2.2582 L12:  -0.0422                                     
REMARK   3      L13:  -2.1707 L23:   1.8908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1084 S12:   0.2589 S13:   0.5712                       
REMARK   3      S21:   0.0774 S22:   0.0868 S23:  -0.2050                       
REMARK   3      S31:  -0.7113 S32:   0.0689 S33:   0.0216                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   144        D   270                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.4378 123.9896 -38.5319              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0492 T22:   0.6838                                     
REMARK   3      T33:   1.0842 T12:  -0.1203                                     
REMARK   3      T13:  -0.0614 T23:  -0.0919                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1413 L22:   3.5074                                     
REMARK   3      L33:   1.9970 L12:   0.2833                                     
REMARK   3      L13:   1.7259 L23:  -1.6246                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1389 S12:   0.0704 S13:  -0.1541                       
REMARK   3      S21:   0.2494 S22:  -0.1052 S23:   0.5045                       
REMARK   3      S31:   0.0952 S32:  -0.6630 S33:  -0.0337                       
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 3E1Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-AUG-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB048772.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35459                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1DT9, 1R5B                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES, PH5.6, 20-22% ETHYLENE         
REMARK 280  GLYCOL, 2MM DTT, 2MM ATP, EVAPORATION, TEMPERATURE 288K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
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       59.91200            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       89.86800            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       29.95600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G                                  
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -13                                                      
REMARK 465     ARG A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     MET A    -2                                                      
REMARK 465     ALA A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     TYR A   331                                                      
REMARK 465     VAL A   332                                                      
REMARK 465     LEU A   333                                                      
REMARK 465     HIS A   334                                                      
REMARK 465     CYS A   335                                                      
REMARK 465     GLN A   336                                                      
REMARK 465     GLY A   337                                                      
REMARK 465     THR A   338                                                      
REMARK 465     GLU A   339                                                      
REMARK 465     GLU A   340                                                      
REMARK 465     GLU A   341                                                      
REMARK 465     LYS A   342                                                      
REMARK 465     ILE A   343                                                      
REMARK 465     GLU A   351                                                      
REMARK 465     LYS A   352                                                      
REMARK 465     ASP A   353                                                      
REMARK 465     LYS A   354                                                      
REMARK 465     SER A   355                                                      
REMARK 465     HIS A   356                                                      
REMARK 465     PHE A   357                                                      
REMARK 465     THR A   358                                                      
REMARK 465     ASP A   359                                                      
REMARK 465     LYS A   360                                                      
REMARK 465     GLU A   361                                                      
REMARK 465     THR A   362                                                      
REMARK 465     GLY A   363                                                      
REMARK 465     GLN A   364                                                      
REMARK 465     GLU A   365                                                      
REMARK 465     HIS A   366                                                      
REMARK 465     GLU A   367                                                      
REMARK 465     LEU A   368                                                      
REMARK 465     ILE A   369                                                      
REMARK 465     GLU A   370                                                      
REMARK 465     SER A   371                                                      
REMARK 465     GLY A   421                                                      
REMARK 465     MET A   422                                                      
REMARK 465     GLU A   423                                                      
REMARK 465     TYR A   424                                                      
REMARK 465     GLN A   425                                                      
REMARK 465     GLY A   426                                                      
REMARK 465     GLY A   427                                                      
REMARK 465     ASP A   428                                                      
REMARK 465     ASP A   429                                                      
REMARK 465     GLU A   430                                                      
REMARK 465     PHE A   431                                                      
REMARK 465     PHE A   432                                                      
REMARK 465     ASP A   433                                                      
REMARK 465     LEU A   434                                                      
REMARK 465     ASP A   435                                                      
REMARK 465     ASP A   436                                                      
REMARK 465     TYR A   437                                                      
REMARK 465     MET B   -13                                                      
REMARK 465     ARG B   -12                                                      
REMARK 465     GLY B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     MET B    -2                                                      
REMARK 465     ALA B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     TYR B   331                                                      
REMARK 465     VAL B   332                                                      
REMARK 465     LEU B   333                                                      
REMARK 465     HIS B   334                                                      
REMARK 465     CYS B   335                                                      
REMARK 465     GLN B   336                                                      
REMARK 465     GLY B   337                                                      
REMARK 465     THR B   338                                                      
REMARK 465     GLU B   339                                                      
REMARK 465     GLU B   340                                                      
REMARK 465     GLU B   341                                                      
REMARK 465     LYS B   342                                                      
REMARK 465     ILE B   343                                                      
REMARK 465     GLU B   351                                                      
REMARK 465     LYS B   352                                                      
REMARK 465     ASP B   353                                                      
REMARK 465     LYS B   354                                                      
REMARK 465     SER B   355                                                      
REMARK 465     HIS B   356                                                      
REMARK 465     PHE B   357                                                      
REMARK 465     THR B   358                                                      
REMARK 465     ASP B   359                                                      
REMARK 465     LYS B   360                                                      
REMARK 465     GLU B   361                                                      
REMARK 465     THR B   362                                                      
REMARK 465     GLY B   363                                                      
REMARK 465     GLN B   364                                                      
REMARK 465     GLU B   365                                                      
REMARK 465     HIS B   366                                                      
REMARK 465     GLU B   367                                                      
REMARK 465     LEU B   368                                                      
REMARK 465     ILE B   369                                                      
REMARK 465     GLU B   370                                                      
REMARK 465     SER B   371                                                      
REMARK 465     GLY B   421                                                      
REMARK 465     MET B   422                                                      
REMARK 465     GLU B   423                                                      
REMARK 465     TYR B   424                                                      
REMARK 465     GLN B   425                                                      
REMARK 465     GLY B   426                                                      
REMARK 465     GLY B   427                                                      
REMARK 465     ASP B   428                                                      
REMARK 465     ASP B   429                                                      
REMARK 465     GLU B   430                                                      
REMARK 465     PHE B   431                                                      
REMARK 465     PHE B   432                                                      
REMARK 465     ASP B   433                                                      
REMARK 465     LEU B   434                                                      
REMARK 465     ASP B   435                                                      
REMARK 465     ASP B   436                                                      
REMARK 465     TYR B   437                                                      
REMARK 465     MET C   -13                                                      
REMARK 465     ARG C   -12                                                      
REMARK 465     GLY C   -11                                                      
REMARK 465     SER C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     HIS C    -8                                                      
REMARK 465     HIS C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     MET C    -2                                                      
REMARK 465     ALA C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     ASP C     3                                                      
REMARK 465     ASP C     4                                                      
REMARK 465     PRO C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     ALA C    27                                                      
REMARK 465     ARG C    28                                                      
REMARK 465     GLY C    29                                                      
REMARK 465     ASN C    30                                                      
REMARK 465     GLY C    31                                                      
REMARK 465     THR C    32                                                      
REMARK 465     LYS C    42                                                      
REMARK 465     ASP C    43                                                      
REMARK 465     GLN C    44                                                      
REMARK 465     ILE C    45                                                      
REMARK 465     ALA C    59                                                      
REMARK 465     SER C    60                                                      
REMARK 465     ASN C    61                                                      
REMARK 465     ILE C    62                                                      
REMARK 465     LYS C    63                                                      
REMARK 465     SER C    64                                                      
REMARK 465     TYR C    85                                                      
REMARK 465     ASN C    86                                                      
REMARK 465     LYS C    87                                                      
REMARK 465     VAL C    88                                                      
REMARK 465     PRO C    89                                                      
REMARK 465     PRO C    90                                                      
REMARK 465     ASN C    91                                                      
REMARK 465     GLY C    92                                                      
REMARK 465     GLY C    98                                                      
REMARK 465     THR C    99                                                      
REMARK 465     ILE C   100                                                      
REMARK 465     VAL C   101                                                      
REMARK 465     THR C   102                                                      
REMARK 465     GLU C   103                                                      
REMARK 465     GLU C   104                                                      
REMARK 465     GLY C   105                                                      
REMARK 465     LYS C   106                                                      
REMARK 465     GLU C   107                                                      
REMARK 465     LYS C   108                                                      
REMARK 465     LYS C   109                                                      
REMARK 465     VAL C   110                                                      
REMARK 465     ASN C   111                                                      
REMARK 465     ASP C   128                                                      
REMARK 465     ASN C   129                                                      
REMARK 465     LYS C   130                                                      
REMARK 465     VAL C   174                                                      
REMARK 465     ASP C   175                                                      
REMARK 465     LEU C   176                                                      
REMARK 465     PRO C   177                                                      
REMARK 465     LYS C   178                                                      
REMARK 465     LYS C   179                                                      
REMARK 465     HIS C   180                                                      
REMARK 465     GLY C   181                                                      
REMARK 465     ARG C   182                                                      
REMARK 465     GLY C   183                                                      
REMARK 465     GLY C   184                                                      
REMARK 465     GLN C   185                                                      
REMARK 465     SER C   186                                                      
REMARK 465     ALA C   187                                                      
REMARK 465     LEU C   188                                                      
REMARK 465     ARG C   189                                                      
REMARK 465     PHE C   190                                                      
REMARK 465     ALA C   191                                                      
REMARK 465     ARG C   192                                                      
REMARK 465     LEU C   193                                                      
REMARK 465     ARG C   194                                                      
REMARK 465     VAL C   332                                                      
REMARK 465     LEU C   333                                                      
REMARK 465     HIS C   334                                                      
REMARK 465     CYS C   335                                                      
REMARK 465     GLN C   336                                                      
REMARK 465     GLY C   337                                                      
REMARK 465     THR C   338                                                      
REMARK 465     GLU C   339                                                      
REMARK 465     GLU C   340                                                      
REMARK 465     GLU C   341                                                      
REMARK 465     LYS C   342                                                      
REMARK 465     ILE C   343                                                      
REMARK 465     GLU C   351                                                      
REMARK 465     LYS C   352                                                      
REMARK 465     ASP C   353                                                      
REMARK 465     LYS C   354                                                      
REMARK 465     SER C   355                                                      
REMARK 465     HIS C   356                                                      
REMARK 465     PHE C   357                                                      
REMARK 465     THR C   358                                                      
REMARK 465     ASP C   359                                                      
REMARK 465     LYS C   360                                                      
REMARK 465     GLU C   361                                                      
REMARK 465     THR C   362                                                      
REMARK 465     GLY C   363                                                      
REMARK 465     GLN C   364                                                      
REMARK 465     GLU C   365                                                      
REMARK 465     HIS C   366                                                      
REMARK 465     GLU C   367                                                      
REMARK 465     LEU C   368                                                      
REMARK 465     ILE C   369                                                      
REMARK 465     GLU C   370                                                      
REMARK 465     PHE C   419                                                      
REMARK 465     GLN C   420                                                      
REMARK 465     GLY C   421                                                      
REMARK 465     MET C   422                                                      
REMARK 465     GLU C   423                                                      
REMARK 465     TYR C   424                                                      
REMARK 465     GLN C   425                                                      
REMARK 465     GLY C   426                                                      
REMARK 465     GLY C   427                                                      
REMARK 465     ASP C   428                                                      
REMARK 465     ASP C   429                                                      
REMARK 465     GLU C   430                                                      
REMARK 465     PHE C   431                                                      
REMARK 465     PHE C   432                                                      
REMARK 465     ASP C   433                                                      
REMARK 465     LEU C   434                                                      
REMARK 465     ASP C   435                                                      
REMARK 465     ASP C   436                                                      
REMARK 465     TYR C   437                                                      
REMARK 465     MET D   -13                                                      
REMARK 465     ARG D   -12                                                      
REMARK 465     GLY D   -11                                                      
REMARK 465     SER D   -10                                                      
REMARK 465     HIS D    -9                                                      
REMARK 465     HIS D    -8                                                      
REMARK 465     HIS D    -7                                                      
REMARK 465     HIS D    -6                                                      
REMARK 465     HIS D    -5                                                      
REMARK 465     HIS D    -4                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     MET D    -2                                                      
REMARK 465     ALA D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     ASP D     3                                                      
REMARK 465     ASP D     4                                                      
REMARK 465     PRO D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     ALA D    27                                                      
REMARK 465     ARG D    28                                                      
REMARK 465     GLY D    29                                                      
REMARK 465     ASN D    30                                                      
REMARK 465     GLY D    31                                                      
REMARK 465     THR D    32                                                      
REMARK 465     LYS D    42                                                      
REMARK 465     ASP D    43                                                      
REMARK 465     GLN D    44                                                      
REMARK 465     ILE D    45                                                      
REMARK 465     ALA D    59                                                      
REMARK 465     SER D    60                                                      
REMARK 465     ASN D    61                                                      
REMARK 465     ILE D    62                                                      
REMARK 465     LYS D    63                                                      
REMARK 465     SER D    64                                                      
REMARK 465     TYR D    85                                                      
REMARK 465     ASN D    86                                                      
REMARK 465     LYS D    87                                                      
REMARK 465     VAL D    88                                                      
REMARK 465     PRO D    89                                                      
REMARK 465     PRO D    90                                                      
REMARK 465     ASN D    91                                                      
REMARK 465     GLY D    92                                                      
REMARK 465     GLY D    98                                                      
REMARK 465     THR D    99                                                      
REMARK 465     ILE D   100                                                      
REMARK 465     VAL D   101                                                      
REMARK 465     THR D   102                                                      
REMARK 465     GLU D   103                                                      
REMARK 465     GLU D   104                                                      
REMARK 465     GLY D   105                                                      
REMARK 465     LYS D   106                                                      
REMARK 465     GLU D   107                                                      
REMARK 465     LYS D   108                                                      
REMARK 465     LYS D   109                                                      
REMARK 465     VAL D   110                                                      
REMARK 465     ASN D   111                                                      
REMARK 465     ASP D   128                                                      
REMARK 465     ASN D   129                                                      
REMARK 465     LYS D   130                                                      
REMARK 465     VAL D   174                                                      
REMARK 465     ASP D   175                                                      
REMARK 465     LEU D   176                                                      
REMARK 465     PRO D   177                                                      
REMARK 465     LYS D   178                                                      
REMARK 465     LYS D   179                                                      
REMARK 465     HIS D   180                                                      
REMARK 465     GLY D   181                                                      
REMARK 465     ARG D   182                                                      
REMARK 465     GLY D   183                                                      
REMARK 465     GLY D   184                                                      
REMARK 465     GLN D   185                                                      
REMARK 465     SER D   186                                                      
REMARK 465     ALA D   187                                                      
REMARK 465     LEU D   188                                                      
REMARK 465     ARG D   189                                                      
REMARK 465     PHE D   190                                                      
REMARK 465     ALA D   191                                                      
REMARK 465     ARG D   192                                                      
REMARK 465     LEU D   193                                                      
REMARK 465     ARG D   194                                                      
REMARK 465     VAL D   332                                                      
REMARK 465     LEU D   333                                                      
REMARK 465     HIS D   334                                                      
REMARK 465     CYS D   335                                                      
REMARK 465     GLN D   336                                                      
REMARK 465     GLY D   337                                                      
REMARK 465     THR D   338                                                      
REMARK 465     GLU D   339                                                      
REMARK 465     GLU D   340                                                      
REMARK 465     GLU D   341                                                      
REMARK 465     LYS D   342                                                      
REMARK 465     ILE D   343                                                      
REMARK 465     GLU D   351                                                      
REMARK 465     LYS D   352                                                      
REMARK 465     ASP D   353                                                      
REMARK 465     LYS D   354                                                      
REMARK 465     SER D   355                                                      
REMARK 465     HIS D   356                                                      
REMARK 465     PHE D   357                                                      
REMARK 465     THR D   358                                                      
REMARK 465     ASP D   359                                                      
REMARK 465     LYS D   360                                                      
REMARK 465     GLU D   361                                                      
REMARK 465     THR D   362                                                      
REMARK 465     GLY D   363                                                      
REMARK 465     GLN D   364                                                      
REMARK 465     GLU D   365                                                      
REMARK 465     HIS D   366                                                      
REMARK 465     GLU D   367                                                      
REMARK 465     LEU D   368                                                      
REMARK 465     ILE D   369                                                      
REMARK 465     GLU D   370                                                      
REMARK 465     PHE D   419                                                      
REMARK 465     GLN D   420                                                      
REMARK 465     GLY D   421                                                      
REMARK 465     MET D   422                                                      
REMARK 465     GLU D   423                                                      
REMARK 465     TYR D   424                                                      
REMARK 465     GLN D   425                                                      
REMARK 465     GLY D   426                                                      
REMARK 465     GLY D   427                                                      
REMARK 465     ASP D   428                                                      
REMARK 465     ASP D   429                                                      
REMARK 465     GLU D   430                                                      
REMARK 465     PHE D   431                                                      
REMARK 465     PHE D   432                                                      
REMARK 465     ASP D   433                                                      
REMARK 465     LEU D   434                                                      
REMARK 465     ASP D   435                                                      
REMARK 465     ASP D   436                                                      
REMARK 465     TYR D   437                                                      
REMARK 465     GLY E   434                                                      
REMARK 465     PRO E   435                                                      
REMARK 465     LEU E   436                                                      
REMARK 465     GLY E   437                                                      
REMARK 465     SER E   438                                                      
REMARK 465     PRO E   439                                                      
REMARK 465     GLU E   635                                                      
REMARK 465     LYS E   636                                                      
REMARK 465     ASP E   637                                                      
REMARK 465     GLY F   434                                                      
REMARK 465     PRO F   435                                                      
REMARK 465     LEU F   436                                                      
REMARK 465     GLY F   437                                                      
REMARK 465     SER F   438                                                      
REMARK 465     PRO F   439                                                      
REMARK 465     GLU F   635                                                      
REMARK 465     LYS F   636                                                      
REMARK 465     ASP F   637                                                      
REMARK 465     GLY G   434                                                      
REMARK 465     PRO G   435                                                      
REMARK 465     LEU G   436                                                      
REMARK 465     GLY G   437                                                      
REMARK 465     SER G   438                                                      
REMARK 465     PRO G   439                                                      
REMARK 465     GLU G   635                                                      
REMARK 465     LYS G   636                                                      
REMARK 465     ASP G   637                                                      
REMARK 465     GLY H   434                                                      
REMARK 465     PRO H   435                                                      
REMARK 465     LEU H   436                                                      
REMARK 465     GLY H   437                                                      
REMARK 465     SER H   438                                                      
REMARK 465     PRO H   439                                                      
REMARK 465     GLU H   635                                                      
REMARK 465     LYS H   636                                                      
REMARK 465     ASP H   637                                                      
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    GLY B   223     O    LYS B   249              1.90            
REMARK 500   O    GLY A   223     O    LYS A   249              1.91            
REMARK 500   CB   LYS G   541     OE1  GLN G   587              1.97            
REMARK 500   O    GLY C   223     O    LYS C   249              1.99            
REMARK 500   O    GLY D   223     O    LYS D   249              1.99            
REMARK 500   CE   MET F   473     O    CYS F   525              2.03            
REMARK 500   CB   LYS H   541     OE1  GLN H   587              2.03            
REMARK 500   CB   LYS E   541     OE1  GLN E   587              2.05            
REMARK 500   CG   LYS E   541     NE2  GLN E   587              2.05            
REMARK 500   CB   LYS F   541     OE1  GLN F   587              2.06            
REMARK 500   CG   LYS H   541     NE2  GLN H   587              2.08            
REMARK 500   CG   LYS F   541     NE2  GLN F   587              2.09            
REMARK 500   CG   LYS G   541     NE2  GLN G   587              2.09            
REMARK 500   OD1  ASP C   152     O    TYR C   258              2.10            
REMARK 500   OD1  ASP D   152     O    TYR D   258              2.11            
REMARK 500   O    LYS B   300     N    LEU B   413              2.11            
REMARK 500   O    ASN A    91     CG2  ILE A   120              2.12            
REMARK 500   O    ASN B    91     CG2  ILE B   120              2.13            
REMARK 500   NE2  HIS E   540     O    ILE E   543              2.14            
REMARK 500   O    LEU A   176     N    LYS A   178              2.15            
REMARK 500   NE2  HIS F   540     O    ILE F   543              2.15            
REMARK 500   O    LEU B   176     N    LYS B   178              2.15            
REMARK 500   O    LYS A   300     N    LEU A   413              2.16            
REMARK 500   NE2  HIS H   540     O    ILE H   543              2.17            
REMARK 500   O    LEU A   275     N    ASN A   277              2.18            
REMARK 500   NE2  HIS G   540     O    ILE G   543              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    ARG A 416   CD    ARG A 416   NE      0.111                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 116   C   -  N   -  CD  ANGL. DEV. = -19.7 DEGREES          
REMARK 500    LEU A 176   CA  -  CB  -  CG  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    PRO B 116   C   -  N   -  CD  ANGL. DEV. = -19.2 DEGREES          
REMARK 500    LEU B 176   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500    GLY B 299   N   -  CA  -  C   ANGL. DEV. = -24.6 DEGREES          
REMARK 500    LEU E 518   N   -  CA  -  C   ANGL. DEV. =  16.3 DEGREES          
REMARK 500    ILE E 537   N   -  CA  -  C   ANGL. DEV. = -20.2 DEGREES          
REMARK 500    GLU E 539   N   -  CA  -  C   ANGL. DEV. = -26.9 DEGREES          
REMARK 500    HIS E 540   N   -  CA  -  C   ANGL. DEV. =  18.1 DEGREES          
REMARK 500    ILE F 537   N   -  CA  -  C   ANGL. DEV. = -19.9 DEGREES          
REMARK 500    HIS F 540   N   -  CA  -  C   ANGL. DEV. =  19.7 DEGREES          
REMARK 500    LEU G 518   N   -  CA  -  C   ANGL. DEV. =  16.8 DEGREES          
REMARK 500    GLU G 539   N   -  CA  -  C   ANGL. DEV. = -28.6 DEGREES          
REMARK 500    HIS G 540   N   -  CA  -  C   ANGL. DEV. =  16.2 DEGREES          
REMARK 500    LEU H 518   N   -  CA  -  C   ANGL. DEV. =  17.5 DEGREES          
REMARK 500    GLU H 539   N   -  CA  -  C   ANGL. DEV. = -27.7 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    SER A  23       27.23    -71.15                                   
REMARK 500    LYS A  42       -2.06     75.42                                   
REMARK 500    ASN A  61      -79.69   -101.65                                   
REMARK 500    ILE A  62      -42.34     71.03                                   
REMARK 500    SER A  64       47.27   -161.69                                   
REMARK 500    ARG A  65      -86.72     18.26                                   
REMARK 500    ARG A  68      -71.56    -49.00                                   
REMARK 500    PRO A  90      -35.31    -23.89                                   
REMARK 500    THR A 102     -156.89   -130.42                                   
REMARK 500    GLU A 104      -16.67     71.78                                   
REMARK 500    GLU A 107     -141.25   -118.04                                   
REMARK 500    LYS A 108       99.24    154.65                                   
REMARK 500    GLU A 115     -156.44    -77.63                                   
REMARK 500    PHE A 117       -6.60    -46.01                                   
REMARK 500    LYS A 118     -149.10   -132.55                                   
REMARK 500    PRO A 119       66.26   -110.99                                   
REMARK 500    ILE A 120      140.82    -17.85                                   
REMARK 500    THR A 122      153.85    149.82                                   
REMARK 500    LEU A 124      120.46   -172.82                                   
REMARK 500    ASP A 128     -154.04    -98.21                                   
REMARK 500    ASP A 142       55.90    -41.28                                   
REMARK 500    HIS A 170      143.81   -177.49                                   
REMARK 500    LYS A 171      139.21   -172.75                                   
REMARK 500    PRO A 177       67.88    -32.60                                   
REMARK 500    HIS A 180     -166.66   -105.86                                   
REMARK 500    ARG A 182       15.76   -158.41                                   
REMARK 500    PHE A 190      -73.49    -46.52                                   
REMARK 500    ASP A 217      -24.45     71.37                                   
REMARK 500    VAL A 221     -148.51    -98.69                                   
REMARK 500    ALA A 222       14.77   -177.45                                   
REMARK 500    LEU A 224       98.27     64.55                                   
REMARK 500    SER A 229     -179.04    -56.39                                   
REMARK 500    ASP A 231       -1.28     77.53                                   
REMARK 500    ASP A 240       16.44    -67.09                                   
REMARK 500    ASP A 243     -135.28   -137.61                                   
REMARK 500    GLN A 244     -154.03     69.22                                   
REMARK 500    TYR A 258     -112.24    -80.66                                   
REMARK 500    THR A 272      -42.03    -27.36                                   
REMARK 500    SER A 276       23.63    -53.53                                   
REMARK 500    THR A 298      -63.54    -95.50                                   
REMARK 500    LYS A 300       46.22    -95.22                                   
REMARK 500    MET A 314     -146.66   -109.57                                   
REMARK 500    THR A 347     -154.08    -86.96                                   
REMARK 500    PRO A 348       54.92    -60.80                                   
REMARK 500    ASN A 381       50.06    177.37                                   
REMARK 500    ALA A 387      176.49     70.18                                   
REMARK 500    THR A 388      160.61    -41.57                                   
REMARK 500    ASP A 394       58.87   -119.13                                   
REMARK 500    TYR A 415     -155.12   -152.73                                   
REMARK 500    SER B  23       27.97    -70.21                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     321 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 THR B  298     GLY B  299                   92.13                    
REMARK 500 GLN E  469     LEU E  470                  126.97                    
REMARK 500 MET E  473     PRO E  474                  -51.40                    
REMARK 500 ILE E  517     LEU E  518                  116.90                    
REMARK 500 PRO E  521     ASN E  522                   35.73                    
REMARK 500 GLY E  528     ARG E  529                  125.70                    
REMARK 500 VAL E  536     ILE E  537                 -117.76                    
REMARK 500 ILE E  538     GLU E  539                 -128.56                    
REMARK 500 GLU E  539     HIS E  540                  137.80                    
REMARK 500 ILE E  543     ILE E  544                  146.76                    
REMARK 500 ILE E  544     CYS E  545                  149.16                    
REMARK 500 GLN F  469     LEU F  470                  127.55                    
REMARK 500 MET F  473     PRO F  474                  -50.46                    
REMARK 500 ILE F  517     LEU F  518                  116.98                    
REMARK 500 PRO F  521     ASN F  522                   36.88                    
REMARK 500 LEU F  524     CYS F  525                 -117.78                    
REMARK 500 GLY F  528     ARG F  529                   69.95                    
REMARK 500 VAL F  536     ILE F  537                 -116.61                    
REMARK 500 GLU F  539     HIS F  540                  129.86                    
REMARK 500 ILE F  543     ILE F  544                  146.97                    
REMARK 500 ILE F  544     CYS F  545                  148.97                    
REMARK 500 GLN G  469     LEU G  470                  -97.86                    
REMARK 500 ILE G  517     LEU G  518                  101.12                    
REMARK 500 PRO G  521     ASN G  522                   39.90                    
REMARK 500 ILE G  538     GLU G  539                 -121.06                    
REMARK 500 GLU G  539     HIS G  540                  140.45                    
REMARK 500 GLN H  469     LEU H  470                  -96.81                    
REMARK 500 ILE H  517     LEU H  518                   99.83                    
REMARK 500 PRO H  521     ASN H  522                   40.44                    
REMARK 500 ILE H  538     GLU H  539                 -120.72                    
REMARK 500 GLU H  539     HIS H  540                  142.08                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR B 298        23.3      L          L   OUTSIDE RANGE           
REMARK 500    LEU E 518        19.4      L          L   OUTSIDE RANGE           
REMARK 500    GLU E 539        48.5      L          L   OUTSIDE RANGE           
REMARK 500    HIS E 540        24.1      L          L   OUTSIDE RANGE           
REMARK 500    LEU F 518        19.3      L          L   OUTSIDE RANGE           
REMARK 500    HIS F 540        22.6      L          L   OUTSIDE RANGE           
REMARK 500    LEU G 518        14.8      L          L   OUTSIDE RANGE           
REMARK 500    GLU G 539        48.5      L          L   OUTSIDE RANGE           
REMARK 500    HIS G 540        23.2      L          L   OUTSIDE RANGE           
REMARK 500    LEU H 518        15.5      L          L   OUTSIDE RANGE           
REMARK 500    GLU H 539        47.7      L          L   OUTSIDE RANGE           
REMARK 500    HIS H 540        23.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 1526                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 1526                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3E20   RELATED DB: PDB                                   
DBREF  3E1Y A    1   437  UNP    P62495   ERF1_HUMAN       1    437             
DBREF  3E1Y B    1   437  UNP    P62495   ERF1_HUMAN       1    437             
DBREF  3E1Y C    1   437  UNP    P62495   ERF1_HUMAN       1    437             
DBREF  3E1Y D    1   437  UNP    P62495   ERF1_HUMAN       1    437             
DBREF  3E1Y E  439   637  UNP    P15170   ERF3A_HUMAN    301    499             
DBREF  3E1Y F  439   637  UNP    P15170   ERF3A_HUMAN    301    499             
DBREF  3E1Y G  439   637  UNP    P15170   ERF3A_HUMAN    301    499             
DBREF  3E1Y H  439   637  UNP    P15170   ERF3A_HUMAN    301    499             
SEQADV 3E1Y MET A  -13  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y ARG A  -12  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y GLY A  -11  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y SER A  -10  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS A   -9  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS A   -8  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS A   -7  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS A   -6  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS A   -5  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS A   -4  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y GLY A   -3  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y MET A   -2  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y ALA A   -1  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y SER A    0  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y MET B  -13  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y ARG B  -12  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y GLY B  -11  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y SER B  -10  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS B   -9  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS B   -8  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS B   -7  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS B   -6  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS B   -5  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS B   -4  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y GLY B   -3  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y MET B   -2  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y ALA B   -1  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y SER B    0  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y MET C  -13  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y ARG C  -12  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y GLY C  -11  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y SER C  -10  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS C   -9  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS C   -8  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS C   -7  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS C   -6  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS C   -5  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS C   -4  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y GLY C   -3  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y MET C   -2  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y ALA C   -1  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y SER C    0  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y MET D  -13  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y ARG D  -12  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y GLY D  -11  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y SER D  -10  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS D   -9  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS D   -8  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS D   -7  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS D   -6  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS D   -5  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y HIS D   -4  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y GLY D   -3  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y MET D   -2  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y ALA D   -1  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y SER D    0  UNP  P62495              EXPRESSION TAG                 
SEQADV 3E1Y GLY E  434  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y PRO E  435  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y LEU E  436  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y GLY E  437  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y SER E  438  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y GLY F  434  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y PRO F  435  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y LEU F  436  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y GLY F  437  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y SER F  438  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y GLY G  434  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y PRO G  435  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y LEU G  436  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y GLY G  437  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y SER G  438  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y GLY H  434  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y PRO H  435  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y LEU H  436  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y GLY H  437  UNP  P15170              EXPRESSION TAG                 
SEQADV 3E1Y SER H  438  UNP  P15170              EXPRESSION TAG                 
SEQRES   1 A  451  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA          
SEQRES   2 A  451  SER MET ALA ASP ASP PRO SER ALA ALA ASP ARG ASN VAL          
SEQRES   3 A  451  GLU ILE TRP LYS ILE LYS LYS LEU ILE LYS SER LEU GLU          
SEQRES   4 A  451  ALA ALA ARG GLY ASN GLY THR SER MET ILE SER LEU ILE          
SEQRES   5 A  451  ILE PRO PRO LYS ASP GLN ILE SER ARG VAL ALA LYS MET          
SEQRES   6 A  451  LEU ALA ASP GLU PHE GLY THR ALA SER ASN ILE LYS SER          
SEQRES   7 A  451  ARG VAL ASN ARG LEU SER VAL LEU GLY ALA ILE THR SER          
SEQRES   8 A  451  VAL GLN GLN ARG LEU LYS LEU TYR ASN LYS VAL PRO PRO          
SEQRES   9 A  451  ASN GLY LEU VAL VAL TYR CYS GLY THR ILE VAL THR GLU          
SEQRES  10 A  451  GLU GLY LYS GLU LYS LYS VAL ASN ILE ASP PHE GLU PRO          
SEQRES  11 A  451  PHE LYS PRO ILE ASN THR SER LEU TYR LEU CYS ASP ASN          
SEQRES  12 A  451  LYS PHE HIS THR GLU ALA LEU THR ALA LEU LEU SER ASP          
SEQRES  13 A  451  ASP SER LYS PHE GLY PHE ILE VAL ILE ASP GLY SER GLY          
SEQRES  14 A  451  ALA LEU PHE GLY THR LEU GLN GLY ASN THR ARG GLU VAL          
SEQRES  15 A  451  LEU HIS LYS PHE THR VAL ASP LEU PRO LYS LYS HIS GLY          
SEQRES  16 A  451  ARG GLY GLY GLN SER ALA LEU ARG PHE ALA ARG LEU ARG          
SEQRES  17 A  451  MET GLU LYS ARG HIS ASN TYR VAL ARG LYS VAL ALA GLU          
SEQRES  18 A  451  THR ALA VAL GLN LEU PHE ILE SER GLY ASP LYS VAL ASN          
SEQRES  19 A  451  VAL ALA GLY LEU VAL LEU ALA GLY SER ALA ASP PHE LYS          
SEQRES  20 A  451  THR GLU LEU SER GLN SER ASP MET PHE ASP GLN ARG LEU          
SEQRES  21 A  451  GLN SER LYS VAL LEU LYS LEU VAL ASP ILE SER TYR GLY          
SEQRES  22 A  451  GLY GLU ASN GLY PHE ASN GLN ALA ILE GLU LEU SER THR          
SEQRES  23 A  451  GLU VAL LEU SER ASN VAL LYS PHE ILE GLN GLU LYS LYS          
SEQRES  24 A  451  LEU ILE GLY ARG TYR PHE ASP GLU ILE SER GLN ASP THR          
SEQRES  25 A  451  GLY LYS TYR CYS PHE GLY VAL GLU ASP THR LEU LYS ALA          
SEQRES  26 A  451  LEU GLU MET GLY ALA VAL GLU ILE LEU ILE VAL TYR GLU          
SEQRES  27 A  451  ASN LEU ASP ILE MET ARG TYR VAL LEU HIS CYS GLN GLY          
SEQRES  28 A  451  THR GLU GLU GLU LYS ILE LEU TYR LEU THR PRO GLU GLN          
SEQRES  29 A  451  GLU LYS ASP LYS SER HIS PHE THR ASP LYS GLU THR GLY          
SEQRES  30 A  451  GLN GLU HIS GLU LEU ILE GLU SER MET PRO LEU LEU GLU          
SEQRES  31 A  451  TRP PHE ALA ASN ASN TYR LYS LYS PHE GLY ALA THR LEU          
SEQRES  32 A  451  GLU ILE VAL THR ASP LYS SER GLN GLU GLY SER GLN PHE          
SEQRES  33 A  451  VAL LYS GLY PHE GLY GLY ILE GLY GLY ILE LEU ARG TYR          
SEQRES  34 A  451  ARG VAL ASP PHE GLN GLY MET GLU TYR GLN GLY GLY ASP          
SEQRES  35 A  451  ASP GLU PHE PHE ASP LEU ASP ASP TYR                          
SEQRES   1 B  451  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA          
SEQRES   2 B  451  SER MET ALA ASP ASP PRO SER ALA ALA ASP ARG ASN VAL          
SEQRES   3 B  451  GLU ILE TRP LYS ILE LYS LYS LEU ILE LYS SER LEU GLU          
SEQRES   4 B  451  ALA ALA ARG GLY ASN GLY THR SER MET ILE SER LEU ILE          
SEQRES   5 B  451  ILE PRO PRO LYS ASP GLN ILE SER ARG VAL ALA LYS MET          
SEQRES   6 B  451  LEU ALA ASP GLU PHE GLY THR ALA SER ASN ILE LYS SER          
SEQRES   7 B  451  ARG VAL ASN ARG LEU SER VAL LEU GLY ALA ILE THR SER          
SEQRES   8 B  451  VAL GLN GLN ARG LEU LYS LEU TYR ASN LYS VAL PRO PRO          
SEQRES   9 B  451  ASN GLY LEU VAL VAL TYR CYS GLY THR ILE VAL THR GLU          
SEQRES  10 B  451  GLU GLY LYS GLU LYS LYS VAL ASN ILE ASP PHE GLU PRO          
SEQRES  11 B  451  PHE LYS PRO ILE ASN THR SER LEU TYR LEU CYS ASP ASN          
SEQRES  12 B  451  LYS PHE HIS THR GLU ALA LEU THR ALA LEU LEU SER ASP          
SEQRES  13 B  451  ASP SER LYS PHE GLY PHE ILE VAL ILE ASP GLY SER GLY          
SEQRES  14 B  451  ALA LEU PHE GLY THR LEU GLN GLY ASN THR ARG GLU VAL          
SEQRES  15 B  451  LEU HIS LYS PHE THR VAL ASP LEU PRO LYS LYS HIS GLY          
SEQRES  16 B  451  ARG GLY GLY GLN SER ALA LEU ARG PHE ALA ARG LEU ARG          
SEQRES  17 B  451  MET GLU LYS ARG HIS ASN TYR VAL ARG LYS VAL ALA GLU          
SEQRES  18 B  451  THR ALA VAL GLN LEU PHE ILE SER GLY ASP LYS VAL ASN          
SEQRES  19 B  451  VAL ALA GLY LEU VAL LEU ALA GLY SER ALA ASP PHE LYS          
SEQRES  20 B  451  THR GLU LEU SER GLN SER ASP MET PHE ASP GLN ARG LEU          
SEQRES  21 B  451  GLN SER LYS VAL LEU LYS LEU VAL ASP ILE SER TYR GLY          
SEQRES  22 B  451  GLY GLU ASN GLY PHE ASN GLN ALA ILE GLU LEU SER THR          
SEQRES  23 B  451  GLU VAL LEU SER ASN VAL LYS PHE ILE GLN GLU LYS LYS          
SEQRES  24 B  451  LEU ILE GLY ARG TYR PHE ASP GLU ILE SER GLN ASP THR          
SEQRES  25 B  451  GLY LYS TYR CYS PHE GLY VAL GLU ASP THR LEU LYS ALA          
SEQRES  26 B  451  LEU GLU MET GLY ALA VAL GLU ILE LEU ILE VAL TYR GLU          
SEQRES  27 B  451  ASN LEU ASP ILE MET ARG TYR VAL LEU HIS CYS GLN GLY          
SEQRES  28 B  451  THR GLU GLU GLU LYS ILE LEU TYR LEU THR PRO GLU GLN          
SEQRES  29 B  451  GLU LYS ASP LYS SER HIS PHE THR ASP LYS GLU THR GLY          
SEQRES  30 B  451  GLN GLU HIS GLU LEU ILE GLU SER MET PRO LEU LEU GLU          
SEQRES  31 B  451  TRP PHE ALA ASN ASN TYR LYS LYS PHE GLY ALA THR LEU          
SEQRES  32 B  451  GLU ILE VAL THR ASP LYS SER GLN GLU GLY SER GLN PHE          
SEQRES  33 B  451  VAL LYS GLY PHE GLY GLY ILE GLY GLY ILE LEU ARG TYR          
SEQRES  34 B  451  ARG VAL ASP PHE GLN GLY MET GLU TYR GLN GLY GLY ASP          
SEQRES  35 B  451  ASP GLU PHE PHE ASP LEU ASP ASP TYR                          
SEQRES   1 C  451  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA          
SEQRES   2 C  451  SER MET ALA ASP ASP PRO SER ALA ALA ASP ARG ASN VAL          
SEQRES   3 C  451  GLU ILE TRP LYS ILE LYS LYS LEU ILE LYS SER LEU GLU          
SEQRES   4 C  451  ALA ALA ARG GLY ASN GLY THR SER MET ILE SER LEU ILE          
SEQRES   5 C  451  ILE PRO PRO LYS ASP GLN ILE SER ARG VAL ALA LYS MET          
SEQRES   6 C  451  LEU ALA ASP GLU PHE GLY THR ALA SER ASN ILE LYS SER          
SEQRES   7 C  451  ARG VAL ASN ARG LEU SER VAL LEU GLY ALA ILE THR SER          
SEQRES   8 C  451  VAL GLN GLN ARG LEU LYS LEU TYR ASN LYS VAL PRO PRO          
SEQRES   9 C  451  ASN GLY LEU VAL VAL TYR CYS GLY THR ILE VAL THR GLU          
SEQRES  10 C  451  GLU GLY LYS GLU LYS LYS VAL ASN ILE ASP PHE GLU PRO          
SEQRES  11 C  451  PHE LYS PRO ILE ASN THR SER LEU TYR LEU CYS ASP ASN          
SEQRES  12 C  451  LYS PHE HIS THR GLU ALA LEU THR ALA LEU LEU SER ASP          
SEQRES  13 C  451  ASP SER LYS PHE GLY PHE ILE VAL ILE ASP GLY SER GLY          
SEQRES  14 C  451  ALA LEU PHE GLY THR LEU GLN GLY ASN THR ARG GLU VAL          
SEQRES  15 C  451  LEU HIS LYS PHE THR VAL ASP LEU PRO LYS LYS HIS GLY          
SEQRES  16 C  451  ARG GLY GLY GLN SER ALA LEU ARG PHE ALA ARG LEU ARG          
SEQRES  17 C  451  MET GLU LYS ARG HIS ASN TYR VAL ARG LYS VAL ALA GLU          
SEQRES  18 C  451  THR ALA VAL GLN LEU PHE ILE SER GLY ASP LYS VAL ASN          
SEQRES  19 C  451  VAL ALA GLY LEU VAL LEU ALA GLY SER ALA ASP PHE LYS          
SEQRES  20 C  451  THR GLU LEU SER GLN SER ASP MET PHE ASP GLN ARG LEU          
SEQRES  21 C  451  GLN SER LYS VAL LEU LYS LEU VAL ASP ILE SER TYR GLY          
SEQRES  22 C  451  GLY GLU ASN GLY PHE ASN GLN ALA ILE GLU LEU SER THR          
SEQRES  23 C  451  GLU VAL LEU SER ASN VAL LYS PHE ILE GLN GLU LYS LYS          
SEQRES  24 C  451  LEU ILE GLY ARG TYR PHE ASP GLU ILE SER GLN ASP THR          
SEQRES  25 C  451  GLY LYS TYR CYS PHE GLY VAL GLU ASP THR LEU LYS ALA          
SEQRES  26 C  451  LEU GLU MET GLY ALA VAL GLU ILE LEU ILE VAL TYR GLU          
SEQRES  27 C  451  ASN LEU ASP ILE MET ARG TYR VAL LEU HIS CYS GLN GLY          
SEQRES  28 C  451  THR GLU GLU GLU LYS ILE LEU TYR LEU THR PRO GLU GLN          
SEQRES  29 C  451  GLU LYS ASP LYS SER HIS PHE THR ASP LYS GLU THR GLY          
SEQRES  30 C  451  GLN GLU HIS GLU LEU ILE GLU SER MET PRO LEU LEU GLU          
SEQRES  31 C  451  TRP PHE ALA ASN ASN TYR LYS LYS PHE GLY ALA THR LEU          
SEQRES  32 C  451  GLU ILE VAL THR ASP LYS SER GLN GLU GLY SER GLN PHE          
SEQRES  33 C  451  VAL LYS GLY PHE GLY GLY ILE GLY GLY ILE LEU ARG TYR          
SEQRES  34 C  451  ARG VAL ASP PHE GLN GLY MET GLU TYR GLN GLY GLY ASP          
SEQRES  35 C  451  ASP GLU PHE PHE ASP LEU ASP ASP TYR                          
SEQRES   1 D  451  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA          
SEQRES   2 D  451  SER MET ALA ASP ASP PRO SER ALA ALA ASP ARG ASN VAL          
SEQRES   3 D  451  GLU ILE TRP LYS ILE LYS LYS LEU ILE LYS SER LEU GLU          
SEQRES   4 D  451  ALA ALA ARG GLY ASN GLY THR SER MET ILE SER LEU ILE          
SEQRES   5 D  451  ILE PRO PRO LYS ASP GLN ILE SER ARG VAL ALA LYS MET          
SEQRES   6 D  451  LEU ALA ASP GLU PHE GLY THR ALA SER ASN ILE LYS SER          
SEQRES   7 D  451  ARG VAL ASN ARG LEU SER VAL LEU GLY ALA ILE THR SER          
SEQRES   8 D  451  VAL GLN GLN ARG LEU LYS LEU TYR ASN LYS VAL PRO PRO          
SEQRES   9 D  451  ASN GLY LEU VAL VAL TYR CYS GLY THR ILE VAL THR GLU          
SEQRES  10 D  451  GLU GLY LYS GLU LYS LYS VAL ASN ILE ASP PHE GLU PRO          
SEQRES  11 D  451  PHE LYS PRO ILE ASN THR SER LEU TYR LEU CYS ASP ASN          
SEQRES  12 D  451  LYS PHE HIS THR GLU ALA LEU THR ALA LEU LEU SER ASP          
SEQRES  13 D  451  ASP SER LYS PHE GLY PHE ILE VAL ILE ASP GLY SER GLY          
SEQRES  14 D  451  ALA LEU PHE GLY THR LEU GLN GLY ASN THR ARG GLU VAL          
SEQRES  15 D  451  LEU HIS LYS PHE THR VAL ASP LEU PRO LYS LYS HIS GLY          
SEQRES  16 D  451  ARG GLY GLY GLN SER ALA LEU ARG PHE ALA ARG LEU ARG          
SEQRES  17 D  451  MET GLU LYS ARG HIS ASN TYR VAL ARG LYS VAL ALA GLU          
SEQRES  18 D  451  THR ALA VAL GLN LEU PHE ILE SER GLY ASP LYS VAL ASN          
SEQRES  19 D  451  VAL ALA GLY LEU VAL LEU ALA GLY SER ALA ASP PHE LYS          
SEQRES  20 D  451  THR GLU LEU SER GLN SER ASP MET PHE ASP GLN ARG LEU          
SEQRES  21 D  451  GLN SER LYS VAL LEU LYS LEU VAL ASP ILE SER TYR GLY          
SEQRES  22 D  451  GLY GLU ASN GLY PHE ASN GLN ALA ILE GLU LEU SER THR          
SEQRES  23 D  451  GLU VAL LEU SER ASN VAL LYS PHE ILE GLN GLU LYS LYS          
SEQRES  24 D  451  LEU ILE GLY ARG TYR PHE ASP GLU ILE SER GLN ASP THR          
SEQRES  25 D  451  GLY LYS TYR CYS PHE GLY VAL GLU ASP THR LEU LYS ALA          
SEQRES  26 D  451  LEU GLU MET GLY ALA VAL GLU ILE LEU ILE VAL TYR GLU          
SEQRES  27 D  451  ASN LEU ASP ILE MET ARG TYR VAL LEU HIS CYS GLN GLY          
SEQRES  28 D  451  THR GLU GLU GLU LYS ILE LEU TYR LEU THR PRO GLU GLN          
SEQRES  29 D  451  GLU LYS ASP LYS SER HIS PHE THR ASP LYS GLU THR GLY          
SEQRES  30 D  451  GLN GLU HIS GLU LEU ILE GLU SER MET PRO LEU LEU GLU          
SEQRES  31 D  451  TRP PHE ALA ASN ASN TYR LYS LYS PHE GLY ALA THR LEU          
SEQRES  32 D  451  GLU ILE VAL THR ASP LYS SER GLN GLU GLY SER GLN PHE          
SEQRES  33 D  451  VAL LYS GLY PHE GLY GLY ILE GLY GLY ILE LEU ARG TYR          
SEQRES  34 D  451  ARG VAL ASP PHE GLN GLY MET GLU TYR GLN GLY GLY ASP          
SEQRES  35 D  451  ASP GLU PHE PHE ASP LEU ASP ASP TYR                          
SEQRES   1 E  204  GLY PRO LEU GLY SER PRO ILE ARG LEU PRO ILE VAL ASP          
SEQRES   2 E  204  LYS TYR LYS ASP MET GLY THR VAL VAL LEU GLY LYS LEU          
SEQRES   3 E  204  GLU SER GLY SER ILE CYS LYS GLY GLN GLN LEU VAL MET          
SEQRES   4 E  204  MET PRO ASN LYS HIS ASN VAL GLU VAL LEU GLY ILE LEU          
SEQRES   5 E  204  SER ASP ASP VAL GLU THR ASP THR VAL ALA PRO GLY GLU          
SEQRES   6 E  204  ASN LEU LYS ILE ARG LEU LYS GLY ILE GLU GLU GLU GLU          
SEQRES   7 E  204  ILE LEU PRO GLY PHE ILE LEU CYS ASP PRO ASN ASN LEU          
SEQRES   8 E  204  CYS HIS SER GLY ARG THR PHE ASP ALA GLN ILE VAL ILE          
SEQRES   9 E  204  ILE GLU HIS LYS SER ILE ILE CYS PRO GLY TYR ASN ALA          
SEQRES  10 E  204  VAL LEU HIS ILE HIS THR CYS ILE GLU GLU VAL GLU ILE          
SEQRES  11 E  204  THR ALA LEU ILE CYS LEU VAL ASP LYS LYS SER GLY GLU          
SEQRES  12 E  204  LYS SER LYS THR ARG PRO ARG PHE VAL LYS GLN ASP GLN          
SEQRES  13 E  204  VAL CYS ILE ALA ARG LEU ARG THR ALA GLY THR ILE CYS          
SEQRES  14 E  204  LEU GLU THR PHE LYS ASP PHE PRO GLN MET GLY ARG PHE          
SEQRES  15 E  204  THR LEU ARG ASP GLU GLY LYS THR ILE ALA ILE GLY LYS          
SEQRES  16 E  204  VAL LEU LYS LEU VAL PRO GLU LYS ASP                          
SEQRES   1 F  204  GLY PRO LEU GLY SER PRO ILE ARG LEU PRO ILE VAL ASP          
SEQRES   2 F  204  LYS TYR LYS ASP MET GLY THR VAL VAL LEU GLY LYS LEU          
SEQRES   3 F  204  GLU SER GLY SER ILE CYS LYS GLY GLN GLN LEU VAL MET          
SEQRES   4 F  204  MET PRO ASN LYS HIS ASN VAL GLU VAL LEU GLY ILE LEU          
SEQRES   5 F  204  SER ASP ASP VAL GLU THR ASP THR VAL ALA PRO GLY GLU          
SEQRES   6 F  204  ASN LEU LYS ILE ARG LEU LYS GLY ILE GLU GLU GLU GLU          
SEQRES   7 F  204  ILE LEU PRO GLY PHE ILE LEU CYS ASP PRO ASN ASN LEU          
SEQRES   8 F  204  CYS HIS SER GLY ARG THR PHE ASP ALA GLN ILE VAL ILE          
SEQRES   9 F  204  ILE GLU HIS LYS SER ILE ILE CYS PRO GLY TYR ASN ALA          
SEQRES  10 F  204  VAL LEU HIS ILE HIS THR CYS ILE GLU GLU VAL GLU ILE          
SEQRES  11 F  204  THR ALA LEU ILE CYS LEU VAL ASP LYS LYS SER GLY GLU          
SEQRES  12 F  204  LYS SER LYS THR ARG PRO ARG PHE VAL LYS GLN ASP GLN          
SEQRES  13 F  204  VAL CYS ILE ALA ARG LEU ARG THR ALA GLY THR ILE CYS          
SEQRES  14 F  204  LEU GLU THR PHE LYS ASP PHE PRO GLN MET GLY ARG PHE          
SEQRES  15 F  204  THR LEU ARG ASP GLU GLY LYS THR ILE ALA ILE GLY LYS          
SEQRES  16 F  204  VAL LEU LYS LEU VAL PRO GLU LYS ASP                          
SEQRES   1 G  204  GLY PRO LEU GLY SER PRO ILE ARG LEU PRO ILE VAL ASP          
SEQRES   2 G  204  LYS TYR LYS ASP MET GLY THR VAL VAL LEU GLY LYS LEU          
SEQRES   3 G  204  GLU SER GLY SER ILE CYS LYS GLY GLN GLN LEU VAL MET          
SEQRES   4 G  204  MET PRO ASN LYS HIS ASN VAL GLU VAL LEU GLY ILE LEU          
SEQRES   5 G  204  SER ASP ASP VAL GLU THR ASP THR VAL ALA PRO GLY GLU          
SEQRES   6 G  204  ASN LEU LYS ILE ARG LEU LYS GLY ILE GLU GLU GLU GLU          
SEQRES   7 G  204  ILE LEU PRO GLY PHE ILE LEU CYS ASP PRO ASN ASN LEU          
SEQRES   8 G  204  CYS HIS SER GLY ARG THR PHE ASP ALA GLN ILE VAL ILE          
SEQRES   9 G  204  ILE GLU HIS LYS SER ILE ILE CYS PRO GLY TYR ASN ALA          
SEQRES  10 G  204  VAL LEU HIS ILE HIS THR CYS ILE GLU GLU VAL GLU ILE          
SEQRES  11 G  204  THR ALA LEU ILE CYS LEU VAL ASP LYS LYS SER GLY GLU          
SEQRES  12 G  204  LYS SER LYS THR ARG PRO ARG PHE VAL LYS GLN ASP GLN          
SEQRES  13 G  204  VAL CYS ILE ALA ARG LEU ARG THR ALA GLY THR ILE CYS          
SEQRES  14 G  204  LEU GLU THR PHE LYS ASP PHE PRO GLN MET GLY ARG PHE          
SEQRES  15 G  204  THR LEU ARG ASP GLU GLY LYS THR ILE ALA ILE GLY LYS          
SEQRES  16 G  204  VAL LEU LYS LEU VAL PRO GLU LYS ASP                          
SEQRES   1 H  204  GLY PRO LEU GLY SER PRO ILE ARG LEU PRO ILE VAL ASP          
SEQRES   2 H  204  LYS TYR LYS ASP MET GLY THR VAL VAL LEU GLY LYS LEU          
SEQRES   3 H  204  GLU SER GLY SER ILE CYS LYS GLY GLN GLN LEU VAL MET          
SEQRES   4 H  204  MET PRO ASN LYS HIS ASN VAL GLU VAL LEU GLY ILE LEU          
SEQRES   5 H  204  SER ASP ASP VAL GLU THR ASP THR VAL ALA PRO GLY GLU          
SEQRES   6 H  204  ASN LEU LYS ILE ARG LEU LYS GLY ILE GLU GLU GLU GLU          
SEQRES   7 H  204  ILE LEU PRO GLY PHE ILE LEU CYS ASP PRO ASN ASN LEU          
SEQRES   8 H  204  CYS HIS SER GLY ARG THR PHE ASP ALA GLN ILE VAL ILE          
SEQRES   9 H  204  ILE GLU HIS LYS SER ILE ILE CYS PRO GLY TYR ASN ALA          
SEQRES  10 H  204  VAL LEU HIS ILE HIS THR CYS ILE GLU GLU VAL GLU ILE          
SEQRES  11 H  204  THR ALA LEU ILE CYS LEU VAL ASP LYS LYS SER GLY GLU          
SEQRES  12 H  204  LYS SER LYS THR ARG PRO ARG PHE VAL LYS GLN ASP GLN          
SEQRES  13 H  204  VAL CYS ILE ALA ARG LEU ARG THR ALA GLY THR ILE CYS          
SEQRES  14 H  204  LEU GLU THR PHE LYS ASP PHE PRO GLN MET GLY ARG PHE          
SEQRES  15 H  204  THR LEU ARG ASP GLU GLY LYS THR ILE ALA ILE GLY LYS          
SEQRES  16 H  204  VAL LEU LYS LEU VAL PRO GLU LYS ASP                          
HET    ATP  B1526      31                                                       
HET    ATP  A1526      31                                                       
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   9  ATP    2(C10 H16 N5 O13 P3)                                         
HELIX    1   1 ALA A    7  SER A   23  1                                  17    
HELIX    2   2 GLN A   44  ALA A   59  1                                  16    
HELIX    3   3 SER A   64  LYS A   83  1                                  20    
HELIX    4   4 THR A  102  LYS A  106  5                                   5    
HELIX    5   5 ALA A  135  LEU A  140  5                                   6    
HELIX    6   6 SER A  186  PHE A  213  1                                  28    
HELIX    7   7 PHE A  232  SER A  237  1                                   6    
HELIX    8   8 ASP A  243  LYS A  249  5                                   7    
HELIX    9   9 GLY A  259  LEU A  270  1                                  12    
HELIX   10  10 SER A  271  SER A  276  1                                   6    
HELIX   11  11 ASN A  277  SER A  295  1                                  19    
HELIX   12  12 VAL A  305  MET A  314  1                                  10    
HELIX   13  13 PRO A  373  ASN A  380  1                                   8    
HELIX   14  14 TYR A  382  GLY A  386  5                                   5    
HELIX   15  15 SER A  396  GLY A  405  1                                  10    
HELIX   16  16 ALA B    7  SER B   23  1                                  17    
HELIX   17  17 GLN B   44  ALA B   59  1                                  16    
HELIX   18  18 SER B   64  LYS B   83  1                                  20    
HELIX   19  19 THR B  102  LYS B  106  5                                   5    
HELIX   20  20 ALA B  135  LEU B  140  5                                   6    
HELIX   21  21 SER B  186  PHE B  213  1                                  28    
HELIX   22  22 PHE B  232  SER B  237  1                                   6    
HELIX   23  23 ASP B  243  LYS B  249  5                                   7    
HELIX   24  24 GLY B  259  LEU B  270  1                                  12    
HELIX   25  25 SER B  271  SER B  276  1                                   6    
HELIX   26  26 ASN B  277  SER B  295  1                                  19    
HELIX   27  27 VAL B  305  MET B  314  1                                  10    
HELIX   28  28 PRO B  373  ASN B  380  1                                   8    
HELIX   29  29 TYR B  382  GLY B  386  5                                   5    
HELIX   30  30 SER B  396  GLY B  405  1                                  10    
HELIX   31  31 ARG C   10  ALA C   26  1                                  17    
HELIX   32  32 ARG C   47  GLY C   57  1                                  11    
HELIX   33  33 ASN C   67  LEU C   82  1                                  16    
HELIX   34  34 ALA C  135  LEU C  139  5                                   5    
HELIX   35  35 ARG C  198  PHE C  213  1                                  16    
HELIX   36  36 ASP C  243  SER C  248  1                                   6    
HELIX   37  37 GLY C  259  SER C  276  1                                  18    
HELIX   38  38 ASN C  277  GLU C  293  1                                  17    
HELIX   39  39 GLY C  304  MET C  314  1                                  11    
HELIX   40  40 LEU C  374  ASN C  380  1                                   7    
HELIX   41  41 SER C  396  GLY C  405  1                                  10    
HELIX   42  42 ARG D   10  ALA D   26  1                                  17    
HELIX   43  43 ARG D   47  GLY D   57  1                                  11    
HELIX   44  44 ASN D   67  LEU D   82  1                                  16    
HELIX   45  45 LEU D  136  SER D  141  1                                   6    
HELIX   46  46 ARG D  198  PHE D  213  1                                  16    
HELIX   47  47 ASP D  243  SER D  248  1                                   6    
HELIX   48  48 GLY D  259  SER D  276  1                                  18    
HELIX   49  49 ASN D  277  GLU D  293  1                                  17    
HELIX   50  50 GLY D  304  MET D  314  1                                  11    
HELIX   51  51 LEU D  374  ASN D  380  1                                   7    
HELIX   52  52 SER D  396  GLY D  405  1                                  10    
HELIX   53  53 PHE E  609  MET E  612  5                                   4    
HELIX   54  54 PHE F  609  MET F  612  5                                   4    
HELIX   55  55 PHE G  609  MET G  612  5                                   4    
HELIX   56  56 PHE H  609  MET H  612  5                                   4    
SHEET    1   A 8 LYS A 109  PHE A 114  0                                        
SHEET    2   A 8 LEU A  93  THR A  99 -1  N  TYR A  96   O  ILE A 112           
SHEET    3   A 8 MET A  34  ILE A  39 -1  N  LEU A  37   O  VAL A  95           
SHEET    4   A 8 SER A 123  ASP A 128 -1  O  LEU A 126   N  SER A  36           
SHEET    5   A 8 SER B 123  ASP B 128 -1  O  SER B 123   N  TYR A 125           
SHEET    6   A 8 MET B  34  ILE B  39 -1  N  SER B  36   O  LEU B 126           
SHEET    7   A 8 LEU B  93  THR B  99 -1  O  VAL B  95   N  LEU B  37           
SHEET    8   A 8 LYS B 109  PHE B 114 -1  O  ILE B 112   N  TYR B  96           
SHEET    1   B 5 THR A 165  PHE A 172  0                                        
SHEET    2   B 5 ALA A 156  GLN A 162 -1  N  GLN A 162   O  THR A 165           
SHEET    3   B 5 LYS A 145  ILE A 151 -1  N  PHE A 148   O  GLY A 159           
SHEET    4   B 5 VAL A 225  GLY A 228  1  O  ALA A 227   N  ILE A 149           
SHEET    5   B 5 LYS A 252  ASP A 255  1  O  VAL A 254   N  GLY A 228           
SHEET    1   C 4 TYR A 301  PHE A 303  0                                        
SHEET    2   C 4 ILE A 409  LEU A 413 -1  O  GLY A 411   N  CYS A 302           
SHEET    3   C 4 VAL A 317  TYR A 323 -1  N  ILE A 321   O  GLY A 410           
SHEET    4   C 4 LEU A 389  VAL A 392  1  O  GLU A 390   N  LEU A 320           
SHEET    1   D 5 THR B 165  PHE B 172  0                                        
SHEET    2   D 5 ALA B 156  GLN B 162 -1  N  GLN B 162   O  THR B 165           
SHEET    3   D 5 LYS B 145  ILE B 151 -1  N  PHE B 148   O  GLY B 159           
SHEET    4   D 5 VAL B 225  GLY B 228  1  O  ALA B 227   N  ILE B 149           
SHEET    5   D 5 LYS B 252  ASP B 255  1  O  VAL B 254   N  GLY B 228           
SHEET    1   E 4 TYR B 301  PHE B 303  0                                        
SHEET    2   E 4 ILE B 409  LEU B 413 -1  O  GLY B 411   N  CYS B 302           
SHEET    3   E 4 VAL B 317  TYR B 323 -1  N  ILE B 321   O  GLY B 410           
SHEET    4   E 4 LEU B 389  VAL B 392  1  O  GLU B 390   N  LEU B 320           
SHEET    1   F 4 ASP C 113  PHE C 114  0                                        
SHEET    2   F 4 VAL C  94  CYS C  97 -1  N  VAL C  94   O  PHE C 114           
SHEET    3   F 4 ILE C  35  ILE C  38 -1  N  LEU C  37   O  VAL C  95           
SHEET    4   F 4 LEU C 124  LEU C 126 -1  O  LEU C 126   N  SER C  36           
SHEET    1   G 5 HIS C 170  PHE C 172  0                                        
SHEET    2   G 5 ALA C 156  GLY C 159 -1  N  PHE C 158   O  HIS C 170           
SHEET    3   G 5 PHE C 148  ILE C 151 -1  N  PHE C 148   O  GLY C 159           
SHEET    4   G 5 VAL C 225  GLY C 228  1  O  ALA C 227   N  ILE C 149           
SHEET    5   G 5 LEU C 253  ASP C 255  1  O  VAL C 254   N  GLY C 228           
SHEET    1   H 2 MET C 329  ARG C 330  0                                        
SHEET    2   H 2 MET C 372  PRO C 373 -1  O  MET C 372   N  ARG C 330           
SHEET    1   I 4 ASP D 113  PHE D 114  0                                        
SHEET    2   I 4 VAL D  94  CYS D  97 -1  N  VAL D  94   O  PHE D 114           
SHEET    3   I 4 ILE D  35  ILE D  38 -1  N  LEU D  37   O  VAL D  95           
SHEET    4   I 4 LEU D 124  LEU D 126 -1  O  LEU D 126   N  SER D  36           
SHEET    1   J 5 HIS D 170  PHE D 172  0                                        
SHEET    2   J 5 ALA D 156  GLY D 159 -1  N  PHE D 158   O  HIS D 170           
SHEET    3   J 5 PHE D 148  ILE D 151 -1  N  PHE D 148   O  GLY D 159           
SHEET    4   J 5 VAL D 225  GLY D 228  1  O  ALA D 227   N  ILE D 149           
SHEET    5   J 5 LEU D 253  ASP D 255  1  O  VAL D 254   N  GLY D 228           
SHEET    1   K 2 MET D 329  ARG D 330  0                                        
SHEET    2   K 2 MET D 372  PRO D 373 -1  O  MET D 372   N  ARG D 330           
SHEET    1   L 6 LEU E 470  VAL E 471  0                                        
SHEET    2   L 6 ASN E 478  ILE E 484 -1  O  VAL E 479   N  LEU E 470           
SHEET    3   L 6 ASN E 499  GLY E 506 -1  O  ARG E 503   N  LEU E 482           
SHEET    4   L 6 THR E 453  LYS E 458 -1  N  THR E 453   O  LEU E 504           
SHEET    5   L 6 LEU E 442  LYS E 449 -1  N  VAL E 445   O  LEU E 456           
SHEET    6   L 6 ILE E 517  LEU E 518 -1  O  LEU E 518   N  LEU E 442           
SHEET    1   M 2 ILE E 464  CYS E 465  0                                        
SHEET    2   M 2 THR E 493  VAL E 494 -1  O  VAL E 494   N  ILE E 464           
SHEET    1   N 7 THR E 530  VAL E 536  0                                        
SHEET    2   N 7 VAL E 590  THR E 597 -1  O  CYS E 591   N  ILE E 535           
SHEET    3   N 7 ILE E 558  LEU E 566 -1  N  ALA E 565   O  ARG E 594           
SHEET    4   N 7 TYR E 548  HIS E 553 -1  N  LEU E 552   O  GLU E 559           
SHEET    5   N 7 ARG E 614  ARG E 618 -1  O  THR E 616   N  HIS E 553           
SHEET    6   N 7 ALA E 625  LEU E 632 -1  O  GLY E 627   N  PHE E 615           
SHEET    7   N 7 THR E 530  VAL E 536 -1  N  ASP E 532   O  LYS E 631           
SHEET    1   O 6 LEU F 470  MET F 472  0                                        
SHEET    2   O 6 HIS F 477  ILE F 484 -1  O  VAL F 479   N  LEU F 470           
SHEET    3   O 6 ASN F 499  GLY F 506 -1  O  ARG F 503   N  LEU F 482           
SHEET    4   O 6 THR F 453  LYS F 458 -1  N  THR F 453   O  LEU F 504           
SHEET    5   O 6 LEU F 442  LYS F 449 -1  N  VAL F 445   O  LEU F 456           
SHEET    6   O 6 ILE F 517  LEU F 518 -1  O  LEU F 518   N  LEU F 442           
SHEET    1   P 2 ILE F 464  CYS F 465  0                                        
SHEET    2   P 2 THR F 493  VAL F 494 -1  O  VAL F 494   N  ILE F 464           
SHEET    1   Q 7 THR F 530  VAL F 536  0                                        
SHEET    2   Q 7 VAL F 590  THR F 597 -1  O  CYS F 591   N  ILE F 535           
SHEET    3   Q 7 ILE F 558  LEU F 566 -1  N  ALA F 565   O  ARG F 594           
SHEET    4   Q 7 TYR F 548  HIS F 553 -1  N  LEU F 552   O  GLU F 559           
SHEET    5   Q 7 ARG F 614  ARG F 618 -1  O  THR F 616   N  HIS F 553           
SHEET    6   Q 7 ALA F 625  LEU F 632 -1  O  GLY F 627   N  PHE F 615           
SHEET    7   Q 7 THR F 530  VAL F 536 -1  N  ASP F 532   O  LYS F 631           
SHEET    1   R 7 LEU G 442  PRO G 443  0                                        
SHEET    2   R 7 ILE G 517  CYS G 519 -1  O  LEU G 518   N  LEU G 442           
SHEET    3   R 7 LEU G 470  MET G 472 -1  N  VAL G 471   O  CYS G 519           
SHEET    4   R 7 ASN G 478  GLY G 483 -1  O  VAL G 479   N  LEU G 470           
SHEET    5   R 7 ASN G 499  GLY G 506 -1  O  LYS G 505   N  GLU G 480           
SHEET    6   R 7 THR G 453  LYS G 458 -1  N  THR G 453   O  LEU G 504           
SHEET    7   R 7 ASP G 446  LYS G 449 -1  N  TYR G 448   O  VAL G 454           
SHEET    1   S 2 ILE G 464  CYS G 465  0                                        
SHEET    2   S 2 THR G 493  VAL G 494 -1  O  VAL G 494   N  ILE G 464           
SHEET    1   T 8 LEU G 566  CYS G 568  0                                        
SHEET    2   T 8 CYS G 591  LEU G 603 -1  O  ILE G 592   N  CYS G 568           
SHEET    3   T 8 GLU G 560  ILE G 563 -1  N  GLU G 562   O  ARG G 596           
SHEET    4   T 8 TYR G 548  HIS G 553 -1  N  ALA G 550   O  VAL G 561           
SHEET    5   T 8 ARG G 614  ARG G 618 -1  O  ARG G 618   N  VAL G 551           
SHEET    6   T 8 ALA G 625  LEU G 632 -1  O  ALA G 625   N  LEU G 617           
SHEET    7   T 8 HIS G 526  ILE G 537 -1  N  VAL G 536   O  ILE G 626           
SHEET    8   T 8 CYS G 591  LEU G 603 -1  O  CYS G 591   N  ILE G 535           
SHEET    1   U 7 LEU H 442  PRO H 443  0                                        
SHEET    2   U 7 ILE H 517  CYS H 519 -1  O  LEU H 518   N  LEU H 442           
SHEET    3   U 7 LEU H 470  MET H 472 -1  N  VAL H 471   O  CYS H 519           
SHEET    4   U 7 ASN H 478  GLY H 483 -1  O  VAL H 479   N  LEU H 470           
SHEET    5   U 7 ASN H 499  GLY H 506 -1  O  LYS H 505   N  GLU H 480           
SHEET    6   U 7 THR H 453  LYS H 458 -1  N  THR H 453   O  LEU H 504           
SHEET    7   U 7 ASP H 446  LYS H 449 -1  N  TYR H 448   O  VAL H 454           
SHEET    1   V 2 ILE H 464  CYS H 465  0                                        
SHEET    2   V 2 THR H 493  VAL H 494 -1  O  VAL H 494   N  ILE H 464           
SHEET    1   W 8 LEU H 566  CYS H 568  0                                        
SHEET    2   W 8 CYS H 591  LEU H 603 -1  O  ILE H 592   N  CYS H 568           
SHEET    3   W 8 GLU H 560  ILE H 563 -1  N  GLU H 562   O  ARG H 596           
SHEET    4   W 8 TYR H 548  HIS H 553 -1  N  ALA H 550   O  VAL H 561           
SHEET    5   W 8 ARG H 614  ARG H 618 -1  O  ARG H 618   N  VAL H 551           
SHEET    6   W 8 ALA H 625  LEU H 632 -1  O  ALA H 625   N  LEU H 617           
SHEET    7   W 8 HIS H 526  ILE H 537 -1  N  VAL H 536   O  ILE H 626           
SHEET    8   W 8 CYS H 591  LEU H 603 -1  O  CYS H 591   N  ILE H 535           
SSBOND   1 CYS E  519    CYS E  525                          1555   1555  2.05  
SSBOND   2 CYS F  519    CYS F  525                          1555   1555  2.05  
SSBOND   3 CYS G  519    CYS G  525                          1555   1555  2.03  
SSBOND   4 CYS H  519    CYS H  525                          1555   1555  2.03  
CISPEP   1 HIS E  540    LYS E  541          0         9.60                     
CISPEP   2 VAL E  633    PRO E  634          0       -14.78                     
CISPEP   3 HIS F  540    LYS F  541          0        10.13                     
CISPEP   4 VAL F  633    PRO F  634          0       -15.02                     
CISPEP   5 MET G  473    PRO G  474          0         4.42                     
CISPEP   6 HIS G  540    LYS G  541          0         5.79                     
CISPEP   7 MET H  473    PRO H  474          0         4.34                     
CISPEP   8 HIS H  540    LYS H  541          0         6.55                     
SITE     1 AC1  5 THR A  58  ALA A  59  ILE A  62  LYS B 118                    
SITE     2 AC1  5 ASN B 121                                                     
SITE     1 AC2  5 LYS A 118  ASN A 121  THR B  58  ALA B  59                    
SITE     2 AC2  5 ILE B  62                                                     
CRYST1  173.966  173.966  119.824  90.00  90.00  90.00 P 43         16          
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      0.005748  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005748  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008346        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system