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Database: PDB
Entry: 5BO4
LinkDB: 5BO4
Original site: 5BO4 
HEADER    SIGNALING PROTEIN                       27-MAY-15   5BO4              
TITLE     STRUCTURE OF SOCS2:ELONGIN C:ELONGIN B FROM DMSO-TREATED CRYSTALS     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPPRESSOR OF CYTOKINE SIGNALING 2;                        
COMPND   3 CHAIN: A, D, G, J, M, P;                                             
COMPND   4 SYNONYM: SOCS-2,CYTOKINE-INDUCIBLE SH2 PROTEIN 2,CIS-2,STAT-INDUCED  
COMPND   5 STAT INHIBITOR 2,SSI-2;                                              
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 2;           
COMPND   9 CHAIN: B, E, H, K, N, Q;                                             
COMPND  10 SYNONYM: ELONGIN 18 KDA SUBUNIT,ELONGIN-B,ELOB,RNA POLYMERASE II     
COMPND  11 TRANSCRIPTION FACTOR SIII SUBUNIT B,SIII P18;                        
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: TRANSCRIPTION ELONGATION FACTOR B POLYPEPTIDE 1;           
COMPND  15 CHAIN: C, F, I, L, O, R;                                             
COMPND  16 SYNONYM: ELONGIN 15 KDA SUBUNIT,ELONGIN-C,ELOC,RNA POLYMERASE II     
COMPND  17 TRANSCRIPTION FACTOR SIII SUBUNIT C,SIII P15;                        
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOCS2, CIS2, SSI2, STATI2;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PLIC;                                     
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: TCEB2;                                                         
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PCDFDUET-1;                               
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 GENE: TCEB1;                                                         
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  27 EXPRESSION_SYSTEM_PLASMID: PCDFDUET-1                                
KEYWDS    SIGNALING PROTEIN, UBIQUITIN LIGASE, SUPPRESSOR OF CYTOKINE           
KEYWDS   2 SIGNALLING                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.S.GADD,E.BULATOV,A.CIULLI                                           
REVDAT   2   18-OCT-17 5BO4    1       REMARK                                   
REVDAT   1   08-JUL-15 5BO4    0                                                
JRNL        AUTH   M.S.GADD,E.BULATOV,A.CIULLI                                  
JRNL        TITL   SERENDIPITOUS SAD SOLUTION FOR DMSO-SOAKED                   
JRNL        TITL 2 SOCS2-ELONGINC-ELONGINB CRYSTALS USING COVALENTLY            
JRNL        TITL 3 INCORPORATED DIMETHYLARSENIC: INSIGHTS INTO SUBSTRATE        
JRNL        TITL 4 RECEPTOR CONFORMATIONAL FLEXIBILITY IN CULLIN RING LIGASES.  
JRNL        REF    PLOS ONE                      V.  10 31218 2015              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   26121586                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0131218                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 53812                          
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) : 0.232                           
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.287                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2862                            
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4013                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.67                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 203                          
REMARK   3   BIN FREE R VALUE                    : 0.4140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14871                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 33                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 59.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 77.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.05000                                              
REMARK   3    B22 (A**2) : 2.05000                                              
REMARK   3    B33 (A**2) : -6.65000                                             
REMARK   3    B12 (A**2) : 1.02000                                              
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): 0.447         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.423         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 50.951        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.909                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.867                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15180 ; 0.006 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 14103 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20696 ; 1.014 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 32258 ; 0.712 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1957 ; 5.450 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   526 ;33.589 ;23.574       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2276 ;15.005 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    57 ;16.238 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2493 ; 0.052 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 16933 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3258 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  7939 ; 4.066 ; 4.580       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  7938 ; 4.066 ; 4.580       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9859 ; 6.491 ; 7.704       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : 3                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A D G J M P                     
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     32       A     198      4                      
REMARK   3           1     D     32       D     198      4                      
REMARK   3           1     G     32       G     198      4                      
REMARK   3           1     J     32       J     198      4                      
REMARK   3           1     M     32       M     198      4                      
REMARK   3           1     P     32       P     198      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2169 ; 0.410 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   2169 ; 0.460 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    G    (A):   2169 ; 0.490 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    J    (A):   2169 ; 0.440 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    M    (A):   2169 ; 0.490 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    P    (A):   2169 ; 0.490 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   2169 ; 8.080 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   2169 ;19.160 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    G (A**2):   2169 ;10.020 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    J (A**2):   2169 ;13.940 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    M (A**2):   2169 ; 8.400 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    P (A**2):   2169 ; 9.950 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B E H K N Q                     
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      1       B     104      4                      
REMARK   3           1     E      1       E     104      4                      
REMARK   3           1     H      1       H     104      4                      
REMARK   3           1     K      1       K     104      4                      
REMARK   3           1     N      1       N     104      4                      
REMARK   3           1     Q      1       Q     104      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    B    (A):    757 ; 0.270 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    E    (A):    757 ; 0.270 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    H    (A):    757 ; 0.220 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    K    (A):    757 ; 0.230 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    N    (A):    757 ; 0.320 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    Q    (A):    757 ; 0.300 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    B (A**2):    757 ;11.060 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    E (A**2):    757 ;11.810 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    H (A**2):    757 ;14.940 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    K (A**2):    757 ;10.090 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    N (A**2):    757 ;12.500 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    Q (A**2):    757 ;13.330 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : C F I L O R                     
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C     17       C     112      4                      
REMARK   3           1     F     17       F     112      4                      
REMARK   3           1     I     17       I     112      4                      
REMARK   3           1     L     17       L     112      4                      
REMARK   3           1     O     17       O     112      4                      
REMARK   3           1     R     17       R     112      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    C    (A):   1008 ; 0.310 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  3    F    (A):   1008 ; 0.380 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  3    I    (A):   1008 ; 0.300 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  3    L    (A):   1008 ; 0.300 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  3    O    (A):   1008 ; 0.380 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  3    R    (A):   1008 ; 0.460 ; 0.500           
REMARK   3   MEDIUM THERMAL     3    C (A**2):   1008 ; 9.310 ; 2.000           
REMARK   3   MEDIUM THERMAL     3    F (A**2):   1008 ;18.820 ; 2.000           
REMARK   3   MEDIUM THERMAL     3    I (A**2):   1008 ;13.440 ; 2.000           
REMARK   3   MEDIUM THERMAL     3    L (A**2):   1008 ; 9.690 ; 2.000           
REMARK   3   MEDIUM THERMAL     3    O (A**2):   1008 ;10.130 ; 2.000           
REMARK   3   MEDIUM THERMAL     3    R (A**2):   1008 ;12.530 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
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    31        A  2054                          
REMARK   3    ORIGIN FOR THE GROUP (A):  80.1336 142.6257   6.0033              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3474 T22:   0.5469                                     
REMARK   3      T33:   0.7167 T12:   0.1000                                     
REMARK   3      T13:   0.0652 T23:  -0.0639                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2407 L22:   0.8847                                     
REMARK   3      L33:   3.2739 L12:  -0.2042                                     
REMARK   3      L13:   0.8041 L23:  -0.0782                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0041 S12:  -0.0366 S13:   0.0090                       
REMARK   3      S21:   0.2105 S22:  -0.0506 S23:   0.1471                       
REMARK   3      S31:   0.1891 S32:  -0.3360 S33:   0.0547                       
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 :   B     2        B   104                          
REMARK   3    ORIGIN FOR THE GROUP (A):  77.9184 107.3378 -10.0738              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0449 T22:   0.2744                                     
REMARK   3      T33:   0.7998 T12:  -0.0641                                     
REMARK   3      T13:  -0.2895 T23:   0.0103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6360 L22:   2.5936                                     
REMARK   3      L33:   2.7998 L12:   0.0770                                     
REMARK   3      L13:   0.9079 L23:   2.0025                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6725 S12:  -0.0378 S13:  -0.2852                       
REMARK   3      S21:  -0.0663 S22:  -0.2061 S23:   0.1173                       
REMARK   3      S31:   0.7673 S32:  -0.0750 S33:  -0.4664                       
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 :   C    17        C   112                          
REMARK   3    ORIGIN FOR THE GROUP (A):  83.8746 116.0520   3.2982              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7248 T22:   0.2544                                     
REMARK   3      T33:   0.5805 T12:  -0.0204                                     
REMARK   3      T13:  -0.1231 T23:  -0.0797                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5893 L22:   4.5792                                     
REMARK   3      L33:   2.4265 L12:  -3.1315                                     
REMARK   3      L13:   2.7061 L23:  -1.5934                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3605 S12:   0.1904 S13:  -0.0931                       
REMARK   3      S21:  -0.1556 S22:  -0.1027 S23:   0.1127                       
REMARK   3      S31:   0.3860 S32:   0.1911 S33:  -0.2578                       
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 :   D    32        D  2054                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.3646  54.0974  44.1047              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0657 T22:   0.6036                                     
REMARK   3      T33:   0.8049 T12:   0.0509                                     
REMARK   3      T13:  -0.0355 T23:  -0.4105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1602 L22:   1.8652                                     
REMARK   3      L33:   3.1724 L12:  -0.9494                                     
REMARK   3      L13:   0.4770 L23:  -2.1796                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0084 S12:   0.2890 S13:  -0.2242                       
REMARK   3      S21:  -0.2253 S22:   0.0237 S23:   0.1442                       
REMARK   3      S31:   0.3302 S32:  -0.4218 S33:  -0.0321                       
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 :   E     2        E    98                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.5817  70.2562  64.0375              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2017 T22:   0.6649                                     
REMARK   3      T33:   0.6433 T12:   0.2699                                     
REMARK   3      T13:   0.1316 T23:  -0.0593                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2304 L22:   2.3504                                     
REMARK   3      L33:   3.9650 L12:   0.2191                                     
REMARK   3      L13:  -2.2296 L23:  -0.8208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1117 S12:  -0.0378 S13:  -0.0345                       
REMARK   3      S21:   0.3914 S22:   0.2439 S23:   0.1655                       
REMARK   3      S31:  -0.2339 S32:  -0.1209 S33:  -0.1321                       
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 :   F    17        F  2021                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.4671  71.1610  47.6510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0759 T22:   0.7369                                     
REMARK   3      T33:   0.5806 T12:   0.2037                                     
REMARK   3      T13:   0.0263 T23:  -0.0412                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6588 L22:   3.7156                                     
REMARK   3      L33:   1.0111 L12:  -2.1693                                     
REMARK   3      L13:  -1.0476 L23:  -0.0659                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1550 S12:   0.5412 S13:  -0.2033                       
REMARK   3      S21:   0.0899 S22:   0.0766 S23:   0.2212                       
REMARK   3      S31:  -0.1531 S32:  -0.3636 S33:  -0.2316                       
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 :   G    31        G  2054                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.4836  89.9133  23.8164              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1681 T22:   0.2285                                     
REMARK   3      T33:   0.7975 T12:   0.1279                                     
REMARK   3      T13:   0.0979 T23:  -0.0081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1017 L22:   1.8169                                     
REMARK   3      L33:   2.4468 L12:   0.1738                                     
REMARK   3      L13:   0.4252 L23:  -0.1225                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0158 S12:   0.0207 S13:  -0.0079                       
REMARK   3      S21:  -0.1664 S22:   0.0333 S23:  -0.1910                       
REMARK   3      S31:   0.1630 S32:   0.2833 S33:  -0.0175                       
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 :   H     1        H   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.9487  54.6995  39.9493              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6534 T22:   0.2776                                     
REMARK   3      T33:   0.7615 T12:  -0.0587                                     
REMARK   3      T13:   0.0614 T23:   0.1252                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8106 L22:   3.8362                                     
REMARK   3      L33:   4.7870 L12:  -1.3607                                     
REMARK   3      L13:   0.5354 L23:  -1.1664                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1598 S12:  -0.1336 S13:  -0.1665                       
REMARK   3      S21:   0.3600 S22:  -0.2756 S23:   0.0798                       
REMARK   3      S31:   0.3053 S32:   0.3639 S33:   0.1158                       
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 :   I    17        I  2019                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.5774  62.6572  26.0460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4567 T22:   0.0999                                     
REMARK   3      T33:   0.5672 T12:   0.1859                                     
REMARK   3      T13:   0.0209 T23:   0.0286                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0137 L22:   3.5725                                     
REMARK   3      L33:   2.7622 L12:  -0.2605                                     
REMARK   3      L13:   1.2446 L23:   0.8291                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1642 S12:  -0.0070 S13:  -0.2344                       
REMARK   3      S21:  -0.1539 S22:  -0.0377 S23:   0.1333                       
REMARK   3      S31:   0.4770 S32:  -0.0095 S33:  -0.1265                       
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 :   J    32        J  2054                          
REMARK   3    ORIGIN FOR THE GROUP (A):  84.3863  72.7378  28.2621              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4862 T22:   0.1418                                     
REMARK   3      T33:   0.9306 T12:   0.2069                                     
REMARK   3      T13:  -0.4476 T23:  -0.1952                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6342 L22:   0.7666                                     
REMARK   3      L33:   3.4725 L12:  -0.8059                                     
REMARK   3      L13:  -1.9788 L23:   0.3626                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1962 S12:  -0.1447 S13:   0.1723                       
REMARK   3      S21:   0.2721 S22:   0.0131 S23:  -0.2554                       
REMARK   3      S31:  -0.2167 S32:   0.1755 S33:   0.1831                       
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 :   K     2        K   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.9504  95.6208  12.2414              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3444 T22:   0.3910                                     
REMARK   3      T33:   0.6958 T12:   0.3233                                     
REMARK   3      T13:  -0.2556 T23:  -0.0913                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3567 L22:   1.7645                                     
REMARK   3      L33:   1.4203 L12:  -1.6105                                     
REMARK   3      L13:   0.9556 L23:  -1.5214                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0024 S12:   0.3485 S13:  -0.0699                       
REMARK   3      S21:   0.1419 S22:   0.0304 S23:  -0.0238                       
REMARK   3      S31:  -0.1515 S32:  -0.1346 S33:  -0.0280                       
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 :   L    16        L   112                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.1358  85.0680  26.0614              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5337 T22:   0.3395                                     
REMARK   3      T33:   0.6915 T12:   0.3187                                     
REMARK   3      T13:  -0.2764 T23:  -0.0267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4138 L22:   3.3482                                     
REMARK   3      L33:   0.8841 L12:  -0.0099                                     
REMARK   3      L13:   0.2686 L23:  -1.2409                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1622 S12:  -0.2467 S13:  -0.1273                       
REMARK   3      S21:   0.4594 S22:   0.4753 S23:   0.1718                       
REMARK   3      S31:  -0.0884 S32:  -0.3680 S33:  -0.3131                       
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 :   M    32        M  2054                          
REMARK   3    ORIGIN FOR THE GROUP (A): 104.1946 139.8581  21.1418              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3495 T22:   0.4553                                     
REMARK   3      T33:   0.8256 T12:   0.3110                                     
REMARK   3      T13:   0.1229 T23:  -0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7743 L22:   1.3207                                     
REMARK   3      L33:   2.2536 L12:   0.9863                                     
REMARK   3      L13:   1.2819 L23:   1.5733                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0672 S12:   0.0454 S13:  -0.0942                       
REMARK   3      S21:  -0.0636 S22:   0.1582 S23:  -0.2424                       
REMARK   3      S31:  -0.0223 S32:   0.1023 S33:  -0.0910                       
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 :   N     2        N   104                          
REMARK   3    ORIGIN FOR THE GROUP (A): 110.0841 109.4974  39.7255              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2165 T22:   0.3948                                     
REMARK   3      T33:   0.8050 T12:   0.2289                                     
REMARK   3      T13:  -0.1123 T23:   0.1487                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6769 L22:   1.1977                                     
REMARK   3      L33:   7.9447 L12:  -0.7405                                     
REMARK   3      L13:   2.1994 L23:  -2.2234                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2096 S12:   0.0635 S13:   0.1162                       
REMARK   3      S21:   0.1846 S22:  -0.1496 S23:  -0.5883                       
REMARK   3      S31:   0.1236 S32:  -0.2375 S33:  -0.0600                       
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 :   O    17        O   112                          
REMARK   3    ORIGIN FOR THE GROUP (A): 102.4063 112.4195  24.3992              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7471 T22:   0.3587                                     
REMARK   3      T33:   0.5419 T12:   0.3012                                     
REMARK   3      T13:  -0.1344 T23:   0.0459                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6334 L22:   7.4298                                     
REMARK   3      L33:   1.8107 L12:   3.7443                                     
REMARK   3      L13:   0.1913 L23:   0.1730                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3817 S12:  -0.3125 S13:  -0.2944                       
REMARK   3      S21:   0.3579 S22:  -0.1320 S23:  -0.1075                       
REMARK   3      S31:   0.6115 S32:   0.0262 S33:  -0.2497                       
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 :   P    32        P  2054                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.5339 106.9618  53.4047              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0690 T22:   0.3461                                     
REMARK   3      T33:   0.7622 T12:   0.0088                                     
REMARK   3      T13:  -0.0472 T23:   0.0905                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3211 L22:   0.6927                                     
REMARK   3      L33:   2.2728 L12:   0.6945                                     
REMARK   3      L13:   0.4734 L23:   1.0415                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1083 S12:   0.0222 S13:  -0.1226                       
REMARK   3      S21:   0.0921 S22:   0.0483 S23:  -0.0623                       
REMARK   3      S31:   0.2171 S32:   0.1881 S33:  -0.1566                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   Q     2        Q   103                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.7734 121.0285  34.2444              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5899 T22:   0.9191                                     
REMARK   3      T33:   0.7976 T12:  -0.2988                                     
REMARK   3      T13:   0.2031 T23:  -0.0676                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4649 L22:   0.4181                                     
REMARK   3      L33:   3.3238 L12:   0.2268                                     
REMARK   3      L13:  -0.2300 L23:  -0.8371                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2504 S12:  -0.1454 S13:  -0.0852                       
REMARK   3      S21:  -0.3226 S22:   0.1745 S23:  -0.1750                       
REMARK   3      S31:  -0.0031 S32:   0.4927 S33:   0.0759                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   R    17        R  2021                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.7434 123.6115  49.5665              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1419 T22:   0.7327                                     
REMARK   3      T33:   0.6166 T12:  -0.2266                                     
REMARK   3      T13:   0.1018 T23:  -0.0184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1177 L22:   1.3465                                     
REMARK   3      L33:   2.9943 L12:   1.7832                                     
REMARK   3      L13:  -0.0983 L23:  -0.7170                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0837 S12:   0.0090 S13:   0.0265                       
REMARK   3      S21:  -0.0968 S22:   0.2234 S23:  -0.0320                       
REMARK   3      S31:  -0.3539 S32:   0.4380 S33:  -0.1397                       
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 U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 5BO4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210263.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-JAN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0432, 0.9537                     
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.3.11                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56676                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : 0.12000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.04500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, CAOAC, SODIUM CACODYLATE,      
REMARK 280  GLYCEROL, PH 7.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.80267            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       22.40133            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, 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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I                               
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, L                               
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: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O                               
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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, Q, R                               
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     SER A    30                                                      
REMARK 465     ASP A   135                                                      
REMARK 465     LYS A   136                                                      
REMARK 465     ARG A   137                                                      
REMARK 465     THR A   138                                                      
REMARK 465     GLY A   139                                                      
REMARK 465     PRO A   140                                                      
REMARK 465     GLU A   141                                                      
REMARK 465     ALA A   142                                                      
REMARK 465     PRO A   143                                                      
REMARK 465     ARG A   144                                                      
REMARK 465     ASN A   145                                                      
REMARK 465     GLY A   146                                                      
REMARK 465     THR A   147                                                      
REMARK 465     VAL A   148                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LEU C    46                                                      
REMARK 465     SER C    47                                                      
REMARK 465     GLY C    48                                                      
REMARK 465     PRO C    49                                                      
REMARK 465     GLY C    50                                                      
REMARK 465     GLN C    51                                                      
REMARK 465     PHE C    52                                                      
REMARK 465     ALA C    53                                                      
REMARK 465     GLU C    54                                                      
REMARK 465     ASN C    55                                                      
REMARK 465     GLU C    56                                                      
REMARK 465     THR C    57                                                      
REMARK 465     SER D    30                                                      
REMARK 465     ASP D   135                                                      
REMARK 465     LYS D   136                                                      
REMARK 465     ARG D   137                                                      
REMARK 465     THR D   138                                                      
REMARK 465     GLY D   139                                                      
REMARK 465     PRO D   140                                                      
REMARK 465     GLU D   141                                                      
REMARK 465     ALA D   142                                                      
REMARK 465     PRO D   143                                                      
REMARK 465     ARG D   144                                                      
REMARK 465     ASN D   145                                                      
REMARK 465     GLY D   146                                                      
REMARK 465     THR D   147                                                      
REMARK 465     VAL D   148                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ALA E    18                                                      
REMARK 465     LYS E    19                                                      
REMARK 465     LEU E    99                                                      
REMARK 465     PRO E   100                                                      
REMARK 465     ASP E   101                                                      
REMARK 465     VAL E   102                                                      
REMARK 465     MET E   103                                                      
REMARK 465     LYS E   104                                                      
REMARK 465     MET F    16                                                      
REMARK 465     LEU F    46                                                      
REMARK 465     SER F    47                                                      
REMARK 465     GLY F    48                                                      
REMARK 465     PRO F    49                                                      
REMARK 465     GLY F    50                                                      
REMARK 465     GLN F    51                                                      
REMARK 465     PHE F    52                                                      
REMARK 465     ALA F    53                                                      
REMARK 465     GLU F    54                                                      
REMARK 465     ASN F    55                                                      
REMARK 465     GLU F    56                                                      
REMARK 465     THR F    57                                                      
REMARK 465     THR F    84                                                      
REMARK 465     ASN F    85                                                      
REMARK 465     SER F    86                                                      
REMARK 465     SER F    87                                                      
REMARK 465     THR F    88                                                      
REMARK 465     SER G    30                                                      
REMARK 465     ASP G   135                                                      
REMARK 465     LYS G   136                                                      
REMARK 465     ARG G   137                                                      
REMARK 465     THR G   138                                                      
REMARK 465     GLY G   139                                                      
REMARK 465     PRO G   140                                                      
REMARK 465     GLU G   141                                                      
REMARK 465     ALA G   142                                                      
REMARK 465     PRO G   143                                                      
REMARK 465     ARG G   144                                                      
REMARK 465     ASN G   145                                                      
REMARK 465     GLY G   146                                                      
REMARK 465     THR G   147                                                      
REMARK 465     VAL G   148                                                      
REMARK 465     LYS H   104                                                      
REMARK 465     PRO I    49                                                      
REMARK 465     GLY I    50                                                      
REMARK 465     GLN I    51                                                      
REMARK 465     PHE I    52                                                      
REMARK 465     ALA I    53                                                      
REMARK 465     GLU I    54                                                      
REMARK 465     ASN I    55                                                      
REMARK 465     GLU I    56                                                      
REMARK 465     THR I    57                                                      
REMARK 465     SER J    30                                                      
REMARK 465     ASP J   135                                                      
REMARK 465     LYS J   136                                                      
REMARK 465     ARG J   137                                                      
REMARK 465     THR J   138                                                      
REMARK 465     GLY J   139                                                      
REMARK 465     PRO J   140                                                      
REMARK 465     GLU J   141                                                      
REMARK 465     ALA J   142                                                      
REMARK 465     PRO J   143                                                      
REMARK 465     ARG J   144                                                      
REMARK 465     ASN J   145                                                      
REMARK 465     GLY J   146                                                      
REMARK 465     THR J   147                                                      
REMARK 465     VAL J   148                                                      
REMARK 465     MET K     1                                                      
REMARK 465     LYS K   104                                                      
REMARK 465     LEU L    46                                                      
REMARK 465     SER L    47                                                      
REMARK 465     GLY L    48                                                      
REMARK 465     PRO L    49                                                      
REMARK 465     GLY L    50                                                      
REMARK 465     GLN L    51                                                      
REMARK 465     PHE L    52                                                      
REMARK 465     ALA L    53                                                      
REMARK 465     GLU L    54                                                      
REMARK 465     ASN L    55                                                      
REMARK 465     GLU L    56                                                      
REMARK 465     THR L    57                                                      
REMARK 465     ASN L    58                                                      
REMARK 465     SER M    30                                                      
REMARK 465     MET M    31                                                      
REMARK 465     ASP M   135                                                      
REMARK 465     LYS M   136                                                      
REMARK 465     ARG M   137                                                      
REMARK 465     THR M   138                                                      
REMARK 465     GLY M   139                                                      
REMARK 465     PRO M   140                                                      
REMARK 465     GLU M   141                                                      
REMARK 465     ALA M   142                                                      
REMARK 465     PRO M   143                                                      
REMARK 465     ARG M   144                                                      
REMARK 465     ASN M   145                                                      
REMARK 465     GLY M   146                                                      
REMARK 465     THR M   147                                                      
REMARK 465     VAL M   148                                                      
REMARK 465     MET N     1                                                      
REMARK 465     PHE N    15                                                      
REMARK 465     THR N    16                                                      
REMARK 465     ASP N    17                                                      
REMARK 465     ALA N    18                                                      
REMARK 465     LYS N    19                                                      
REMARK 465     VAL N    31                                                      
REMARK 465     GLU N    32                                                      
REMARK 465     GLY N    33                                                      
REMARK 465     ILE N    34                                                      
REMARK 465     LEU N    35                                                      
REMARK 465     LYS N    36                                                      
REMARK 465     ARG N    37                                                      
REMARK 465     ALA N    78                                                      
REMARK 465     PHE N    79                                                      
REMARK 465     ARG N    80                                                      
REMARK 465     ALA N    81                                                      
REMARK 465     ASP N    82                                                      
REMARK 465     ASP N    83                                                      
REMARK 465     THR N    84                                                      
REMARK 465     PHE N    85                                                      
REMARK 465     GLU N    86                                                      
REMARK 465     ALA N    87                                                      
REMARK 465     LEU N    88                                                      
REMARK 465     CAS N    89                                                      
REMARK 465     ILE N    90                                                      
REMARK 465     GLU N    91                                                      
REMARK 465     PRO N    92                                                      
REMARK 465     PHE N    93                                                      
REMARK 465     SER N    94                                                      
REMARK 465     SER N    95                                                      
REMARK 465     PRO N    96                                                      
REMARK 465     MET O    16                                                      
REMARK 465     SER O    47                                                      
REMARK 465     GLY O    48                                                      
REMARK 465     PRO O    49                                                      
REMARK 465     GLY O    50                                                      
REMARK 465     GLN O    51                                                      
REMARK 465     PHE O    52                                                      
REMARK 465     ALA O    53                                                      
REMARK 465     GLU O    54                                                      
REMARK 465     ASN O    55                                                      
REMARK 465     GLU O    56                                                      
REMARK 465     THR O    57                                                      
REMARK 465     THR O    84                                                      
REMARK 465     ASN O    85                                                      
REMARK 465     SER O    86                                                      
REMARK 465     SER O    87                                                      
REMARK 465     THR O    88                                                      
REMARK 465     GLU O    89                                                      
REMARK 465     SER P    30                                                      
REMARK 465     MET P    31                                                      
REMARK 465     ASP P   135                                                      
REMARK 465     LYS P   136                                                      
REMARK 465     ARG P   137                                                      
REMARK 465     THR P   138                                                      
REMARK 465     GLY P   139                                                      
REMARK 465     PRO P   140                                                      
REMARK 465     GLU P   141                                                      
REMARK 465     ALA P   142                                                      
REMARK 465     PRO P   143                                                      
REMARK 465     ARG P   144                                                      
REMARK 465     ASN P   145                                                      
REMARK 465     GLY P   146                                                      
REMARK 465     THR P   147                                                      
REMARK 465     VAL P   148                                                      
REMARK 465     MET Q     1                                                      
REMARK 465     LYS Q   104                                                      
REMARK 465     MET R    16                                                      
REMARK 465     SER R    47                                                      
REMARK 465     GLY R    48                                                      
REMARK 465     PRO R    49                                                      
REMARK 465     GLY R    50                                                      
REMARK 465     GLN R    51                                                      
REMARK 465     PHE R    52                                                      
REMARK 465     ALA R    53                                                      
REMARK 465     GLU R    54                                                      
REMARK 465     ASN R    55                                                      
REMARK 465     GLU R    56                                                      
REMARK 465     THR R    57                                                      
REMARK 465     THR R    84                                                      
REMARK 465     ASN R    85                                                      
REMARK 465     SER R    86                                                      
REMARK 465     SER R    87                                                      
REMARK 465     THR R    88                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  41    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  59    CG   CD   CE   NZ                                   
REMARK 470     GLU A  60    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  64    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 100    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 101    CG   OD1  OD2                                       
REMARK 470     LYS A 113    CG   CD   CE   NZ                                   
REMARK 470     SER A 114    OG                                                  
REMARK 470     LYS A 115    CG   CD   CE   NZ                                   
REMARK 470     LYS A 154    CE   NZ                                             
REMARK 470     LYS A 188    CG   CD   CE   NZ                                   
REMARK 470     LYS A 195    CD   CE   NZ                                        
REMARK 470     LYS B  11    CG   CD   CE   NZ                                   
REMARK 470     LYS B  19    CG   CD   CE   NZ                                   
REMARK 470     PHE B  25    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B  29    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  32    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  36    CG   CD   CE   NZ                                   
REMARK 470     ARG B  37    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  41    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  42    CG   CD   OE1  NE2                                  
REMARK 470     ARG B  43    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B  45    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS B  46    CG   CD   CE   NZ                                   
REMARK 470     ASP B  47    CG   OD1  OD2                                       
REMARK 470     ASP B  48    CG   OD1  OD2                                       
REMARK 470     GLN B  49    CG   CD   OE1  NE2                                  
REMARK 470     LEU B  50    CG   CD1  CD2                                       
REMARK 470     LYS B  55    CG   CD   CE   NZ                                   
REMARK 470     GLU B  59    CG   CD   OE1  OE2                                  
REMARK 470     PHE B  62    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN B  65    CD   OE1  NE2                                       
REMARK 470     ARG B  68    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B  79    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B  80    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B  82    CG   OD1  OD2                                       
REMARK 470     ASP B  83    CG   OD1  OD2                                       
REMARK 470     GLU B  98    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 101    CG   OD1  OD2                                       
REMARK 470     LYS B 104    CG   CD   CE   NZ                                   
REMARK 470     MET C  16    CG   SD   CE                                        
REMARK 470     LYS C  20    CG   CD   CE   NZ                                   
REMARK 470     GLU C  28    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  32    CG   CD   CE   NZ                                   
REMARK 470     ARG C  33    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  43    CG   CD   CE   NZ                                   
REMARK 470     ASN C  58    CG   OD1  ND2                                       
REMARK 470     GLU C  59    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  63    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU C  64    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  92    CG   CD   OE1  OE2                                  
REMARK 470     MET C 105    CG   SD   CE                                        
REMARK 470     MET D  31    CG   SD   CE                                        
REMARK 470     ARG D  35    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  38    CG   CD   CE   NZ                                   
REMARK 470     ARG D  41    NE   CZ   NH1  NH2                                  
REMARK 470     LYS D  59    CD   CE   NZ                                        
REMARK 470     GLU D  60    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  64    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 100    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 103    CG   CD   CE   NZ                                   
REMARK 470     LYS D 113    CG   CD   CE   NZ                                   
REMARK 470     SER D 114    OG                                                  
REMARK 470     LYS D 115    CG   CD   CE   NZ                                   
REMARK 470     LYS D 117    CD   CE   NZ                                        
REMARK 470     MET D 132    CG   SD   CE                                        
REMARK 470     HIS D 149    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS D 154    CE   NZ                                             
REMARK 470     LYS D 173    CG   CD   CE   NZ                                   
REMARK 470     ILE D 178    CG1  CG2  CD1                                       
REMARK 470     ARG D 186    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 188    CG   CD   CE   NZ                                   
REMARK 470     GLU D 192    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 195    CG   CD   CE   NZ                                   
REMARK 470     GLU E  20    CG   CD   OE1  OE2                                  
REMARK 470     LYS E  36    CG   CD   CE   NZ                                   
REMARK 470     ARG E  37    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E  41    CG   CD   OE1  OE2                                  
REMARK 470     LYS E  46    CG   CD   CE   NZ                                   
REMARK 470     ASP E  48    CG   OD1  OD2                                       
REMARK 470     LEU E  51    CG   CD1  CD2                                       
REMARK 470     LYS E  55    CE   NZ                                             
REMARK 470     GLU E  59    CG   CD   OE1  OE2                                  
REMARK 470     PHE E  62    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN E  65    CD   OE1  NE2                                       
REMARK 470     GLU E  98    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  20    CG   CD   CE   NZ                                   
REMARK 470     ARG F  33    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F  43    NZ                                                  
REMARK 470     ASN F  58    CG   OD1  ND2                                       
REMARK 470     GLU F  59    CG   CD   OE1  OE2                                  
REMARK 470     ARG F  63    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU F  64    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  80    CG   CD   CE   NZ                                   
REMARK 470     ARG F  82    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU F  89    CD   OE1  OE2                                       
REMARK 470     GLU F  92    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 102    CG   CD   OE1  OE2                                  
REMARK 470     MET F 105    CG   SD   CE                                        
REMARK 470     PHE F 109    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP F 111    CG   OD1  OD2                                       
REMARK 470     LYS G  38    CG   CD   CE   NZ                                   
REMARK 470     ARG G  41    NE   CZ   NH1  NH2                                  
REMARK 470     LYS G  59    CD   CE   NZ                                        
REMARK 470     GLU G  60    CG   CD   OE1  OE2                                  
REMARK 470     GLU G  64    CG   CD   OE1  OE2                                  
REMARK 470     GLN G 100    CG   CD   OE1  NE2                                  
REMARK 470     ASP G 101    CG   OD1  OD2                                       
REMARK 470     LYS G 113    CG   CD   CE   NZ                                   
REMARK 470     SER G 114    OG                                                  
REMARK 470     LYS G 115    CG   CD   CE   NZ                                   
REMARK 470     MET G 132    CG   SD   CE                                        
REMARK 470     LYS G 134    CE   NZ                                             
REMARK 470     HIS G 149    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS G 154    CG   CD   CE   NZ                                   
REMARK 470     ARG G 186    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS G 195    CD   CE   NZ                                        
REMARK 470     MET H   1    CG   SD   CE                                        
REMARK 470     LYS H  11    CG   CD   CE   NZ                                   
REMARK 470     LYS H  28    CG   CD   CE   NZ                                   
REMARK 470     ARG H  29    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU H  32    CG   CD   OE1  OE2                                  
REMARK 470     LYS H  36    CG   CD   CE   NZ                                   
REMARK 470     LYS H  46    CG   CD   CE   NZ                                   
REMARK 470     ASP H  48    CG   OD1  OD2                                       
REMARK 470     GLN H  49    CG   CD   OE1  NE2                                  
REMARK 470     LYS H  55    CG   CD   CE   NZ                                   
REMARK 470     GLU H  59    CG   CD   OE1  OE2                                  
REMARK 470     GLN H  65    CG   CD   OE1  NE2                                  
REMARK 470     ARG H  80    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP H  82    CG   OD1  OD2                                       
REMARK 470     ASP H  83    CG   OD1  OD2                                       
REMARK 470     THR H  84    OG1  CG2                                            
REMARK 470     GLU H  91    CG   CD   OE1  OE2                                  
REMARK 470     GLU H  98    CG   CD   OE1  OE2                                  
REMARK 470     ASP H 101    CG   OD1  OD2                                       
REMARK 470     LYS I  20    CG   CD   CE   NZ                                   
REMARK 470     LYS I  43    CG   CD   CE   NZ                                   
REMARK 470     ASN I  58    CG   OD1  ND2                                       
REMARK 470     ARG I  63    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU I  64    CG   CD   OE1  OE2                                  
REMARK 470     ASN I  85    CG   OD1  ND2                                       
REMARK 470     GLU I  89    CD   OE1  OE2                                       
REMARK 470     GLU I  92    CG   CD   OE1  OE2                                  
REMARK 470     ARG J  35    NE   CZ   NH1  NH2                                  
REMARK 470     LYS J  38    CG   CD   CE   NZ                                   
REMARK 470     ARG J  41    NE   CZ   NH1  NH2                                  
REMARK 470     LYS J  59    CD   CE   NZ                                        
REMARK 470     LYS J  63    CG   CD   CE   NZ                                   
REMARK 470     GLU J  64    CG   CD   OE1  OE2                                  
REMARK 470     GLN J 100    CG   CD   OE1  NE2                                  
REMARK 470     ASP J 101    CG   OD1  OD2                                       
REMARK 470     LYS J 113    CG   CD   CE   NZ                                   
REMARK 470     SER J 114    OG                                                  
REMARK 470     LYS J 115    CG   CD   CE   NZ                                   
REMARK 470     LYS J 117    CD   CE   NZ                                        
REMARK 470     ASP J 120    CG   OD1  OD2                                       
REMARK 470     MET J 132    CG   SD   CE                                        
REMARK 470     HIS J 149    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS J 154    CG   CD   CE   NZ                                   
REMARK 470     ARG J 168    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS J 173    CG   CD   CE   NZ                                   
REMARK 470     ARG J 186    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS J 188    CG   CD   CE   NZ                                   
REMARK 470     LYS J 195    CD   CE   NZ                                        
REMARK 470     LYS K  19    CE   NZ                                             
REMARK 470     GLU K  20    CG   CD   OE1  OE2                                  
REMARK 470     PHE K  25    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG K  29    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS K  36    CG   CD   CE   NZ                                   
REMARK 470     ASP K  48    CG   OD1  OD2                                       
REMARK 470     LYS K  55    CG   CD   CE   NZ                                   
REMARK 470     GLU K  59    CG   CD   OE1  OE2                                  
REMARK 470     GLN K  65    CG   CD   OE1  NE2                                  
REMARK 470     ARG K  68    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP K  83    CG   OD1  OD2                                       
REMARK 470     GLU K  98    CG   CD   OE1  OE2                                  
REMARK 470     ASP K 101    CG   OD1  OD2                                       
REMARK 470     MET L  16    CG   SD   CE                                        
REMARK 470     LYS L  20    CG   CD   CE   NZ                                   
REMARK 470     ASP L  25    CG   OD1  OD2                                       
REMARK 470     ARG L  33    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU L  34    CG   CD   OE1  OE2                                  
REMARK 470     LEU L  37    CG   CD1  CD2                                       
REMARK 470     THR L  41    OG1  CG2                                            
REMARK 470     LYS L  43    CG   CD   CE   NZ                                   
REMARK 470     MET L  45    CG   SD   CE                                        
REMARK 470     GLU L  59    CG   CD   OE1  OE2                                  
REMARK 470     ARG L  63    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS L  80    CG   CD   CE   NZ                                   
REMARK 470     SER L  86    OG                                                  
REMARK 470     SER L  87    OG                                                  
REMARK 470     GLU L  89    CD   OE1  OE2                                       
REMARK 470     GLU L  92    CG   CD   OE1  OE2                                  
REMARK 470     ARG M  35    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG M  41    NE   CZ   NH1  NH2                                  
REMARK 470     LYS M  59    CD   CE   NZ                                        
REMARK 470     GLU M  60    CG   CD   OE1  OE2                                  
REMARK 470     GLU M  64    CG   CD   OE1  OE2                                  
REMARK 470     GLN M 100    CG   CD   OE1  NE2                                  
REMARK 470     ASP M 101    CG   OD1  OD2                                       
REMARK 470     LYS M 113    CG   CD   CE   NZ                                   
REMARK 470     SER M 114    OG                                                  
REMARK 470     LYS M 115    CG   CD   CE   NZ                                   
REMARK 470     LYS M 117    CD   CE   NZ                                        
REMARK 470     GLN M 131    CG   CD   OE1  NE2                                  
REMARK 470     HIS M 149    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS M 154    CG   CD   CE   NZ                                   
REMARK 470     SER M 162    OG                                                  
REMARK 470     LYS M 188    CG   CD   CE   NZ                                   
REMARK 470     LYS M 195    CD   CE   NZ                                        
REMARK 470     LEU N   5    CG   CD1  CD2                                       
REMARK 470     MET N   6    CG   SD   CE                                        
REMARK 470     LYS N  11    CG   CD   CE   NZ                                   
REMARK 470     GLU N  20    CG   CD   OE1  OE2                                  
REMARK 470     PHE N  25    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS N  28    CG   CD   CE   NZ                                   
REMARK 470     ARG N  29    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO N  39    CG   CD                                             
REMARK 470     ASP N  40    CG   OD1  OD2                                       
REMARK 470     GLU N  41    CG   CD   OE1  OE2                                  
REMARK 470     ARG N  43    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR N  45    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP N  48    CG   OD1  OD2                                       
REMARK 470     GLN N  49    CG   CD   OE1  NE2                                  
REMARK 470     LEU N  50    CG   CD1  CD2                                       
REMARK 470     LEU N  51    CG   CD1  CD2                                       
REMARK 470     ASP N  52    CG   OD1  OD2                                       
REMARK 470     LYS N  55    CG   CD   CE   NZ                                   
REMARK 470     GLU N  59    CG   CD   OE1  OE2                                  
REMARK 470     PHE N  62    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN N  65    CD   OE1  NE2                                       
REMARK 470     THR N  66    OG1  CG2                                            
REMARK 470     ARG N  68    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU N  98    CG   CD   OE1  OE2                                  
REMARK 470     LYS N 104    CG   CD   CE   NZ                                   
REMARK 470     TYR O  18    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS O  20    CG   CD   CE   NZ                                   
REMARK 470     GLU O  28    CG   CD   OE1  OE2                                  
REMARK 470     ILE O  30    CG1  CG2  CD1                                       
REMARK 470     LYS O  32    CG   CD   CE   NZ                                   
REMARK 470     ARG O  33    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU O  34    CG   CD   OE1  OE2                                  
REMARK 470     LYS O  43    CG   CD   CE   NZ                                   
REMARK 470     LEU O  46    CG   CD1  CD2                                       
REMARK 470     ASN O  58    CG   OD1  ND2                                       
REMARK 470     GLU O  59    CG   CD   OE1  OE2                                  
REMARK 470     ARG O  63    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG O  82    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU O  92    CG   CD   OE1  OE2                                  
REMARK 470     MET O 105    CG   SD   CE                                        
REMARK 470     ARG P  35    NE   CZ   NH1  NH2                                  
REMARK 470     ARG P  41    NE   CZ   NH1  NH2                                  
REMARK 470     LYS P  59    CD   CE   NZ                                        
REMARK 470     GLU P  60    CG   CD   OE1  OE2                                  
REMARK 470     GLN P 100    CG   CD   OE1  NE2                                  
REMARK 470     LYS P 103    CG   CD   CE   NZ                                   
REMARK 470     LYS P 113    CG   CD   CE   NZ                                   
REMARK 470     LYS P 115    CG   CD   CE   NZ                                   
REMARK 470     HIS P 149    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS P 154    CG   CD   CE   NZ                                   
REMARK 470     GLU P 192    CG   CD   OE1  OE2                                  
REMARK 470     LYS P 195    CD   CE   NZ                                        
REMARK 470     LYS Q  19    CG   CD   CE   NZ                                   
REMARK 470     GLU Q  20    CG   CD   OE1  OE2                                  
REMARK 470     PHE Q  25    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU Q  26    CG   CD   OE1  OE2                                  
REMARK 470     ARG Q  29    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU Q  32    CG   CD   OE1  OE2                                  
REMARK 470     ILE Q  34    CG1  CG2  CD1                                       
REMARK 470     LYS Q  36    CG   CD   CE   NZ                                   
REMARK 470     GLU Q  41    CG   CD   OE1  OE2                                  
REMARK 470     LYS Q  46    CG   CD   CE   NZ                                   
REMARK 470     ASP Q  48    CG   OD1  OD2                                       
REMARK 470     ASP Q  53    CG   OD1  OD2                                       
REMARK 470     LYS Q  55    CE   NZ                                             
REMARK 470     PHE Q  62    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN Q  65    CD   OE1  NE2                                       
REMARK 470     ARG Q  80    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP Q  82    CG   OD1  OD2                                       
REMARK 470     ASP Q  83    CG   OD1  OD2                                       
REMARK 470     GLU Q  98    CG   CD   OE1  OE2                                  
REMARK 470     VAL Q 102    CG1  CG2                                            
REMARK 470     VAL R  31    CG1  CG2                                            
REMARK 470     LYS R  32    CG   CD   CE   NZ                                   
REMARK 470     ARG R  33    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU R  34    CG   CD   OE1  OE2                                  
REMARK 470     LYS R  43    NZ                                                  
REMARK 470     LEU R  46    CG   CD1  CD2                                       
REMARK 470     ASN R  58    CG   OD1  ND2                                       
REMARK 470     ARG R  63    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG R  82    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU R  89    CD   OE1  OE2                                       
REMARK 470     GLU R  92    CG   CD   OE1  OE2                                  
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  52       44.20    -77.43                                   
REMARK 500    GLU A  67      127.47    -33.40                                   
REMARK 500    ASP A 107      102.36    -45.48                                   
REMARK 500    LYS A 115       53.30   -107.15                                   
REMARK 500    THR A 153      -88.49   -126.24                                   
REMARK 500    ALA A 177       98.73    -68.36                                   
REMARK 500    HIS B  10     -113.02     60.91                                   
REMARK 500    ALA B  18     -178.61   -177.29                                   
REMARK 500    GLU B  41       41.44   -107.83                                   
REMARK 500    ASP B  47     -103.64     60.48                                   
REMARK 500    THR B  63      140.99     27.89                                   
REMARK 500    ALA B  67       68.07   -153.05                                   
REMARK 500    ASP B  82     -103.77     56.76                                   
REMARK 500    MET B 103       38.20    -95.94                                   
REMARK 500    TYR C  83       56.82   -115.10                                   
REMARK 500    ASN C  85       67.16     39.24                                   
REMARK 500    ASP C 111       70.84     57.93                                   
REMARK 500    GLN D  32      -77.02   -160.64                                   
REMARK 500    SER D  52       40.67    -83.24                                   
REMARK 500    ASP D 107      107.97    -56.41                                   
REMARK 500    LYS D 115       77.93   -103.99                                   
REMARK 500    THR D 153      -84.36   -136.32                                   
REMARK 500    ALA D 177       91.20    -67.66                                   
REMARK 500    PRO D 182       84.68    -69.59                                   
REMARK 500    HIS E  10     -119.34     52.34                                   
REMARK 500    ASP E  47     -106.67     56.54                                   
REMARK 500    ALA E  67       80.93   -151.35                                   
REMARK 500    ASP E  82     -117.42     51.31                                   
REMARK 500    PRO F  66     -163.86    -75.51                                   
REMARK 500    ASP F 111       74.67     61.57                                   
REMARK 500    THR G 153      -77.54   -130.07                                   
REMARK 500    HIS H  10     -117.18     59.00                                   
REMARK 500    GLU H  41       47.29   -108.51                                   
REMARK 500    ASP H  47     -110.70     56.16                                   
REMARK 500    ALA H  67       78.43   -150.13                                   
REMARK 500    ALA H  81      103.08   -162.54                                   
REMARK 500    ASP H  82     -146.75     68.70                                   
REMARK 500    ASP H  83       35.78    -87.87                                   
REMARK 500    MET I  45       42.68    -98.48                                   
REMARK 500    SER I  47       64.44   -165.78                                   
REMARK 500    SER I  87       51.33    -97.24                                   
REMARK 500    GLU I  89      119.99    -38.41                                   
REMARK 500    SER J  52       45.32    -79.98                                   
REMARK 500    THR J 153      -98.28   -141.84                                   
REMARK 500    HIS K  10     -108.21     56.76                                   
REMARK 500    ASP K  47     -126.53     58.23                                   
REMARK 500    PHE K  62       66.71   -110.67                                   
REMARK 500    ASP K  82     -124.00     60.65                                   
REMARK 500    SER M  52       48.21    -84.56                                   
REMARK 500    LYS M 115       56.38    -96.01                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      68 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5BO4 A   32   198  UNP    O14508   SOCS2_HUMAN     32    198             
DBREF  5BO4 B    1   104  UNP    Q15370   ELOB_HUMAN       1    104             
DBREF  5BO4 C   17   112  UNP    Q15369   ELOC_HUMAN      17    112             
DBREF  5BO4 D   32   198  UNP    O14508   SOCS2_HUMAN     32    198             
DBREF  5BO4 E    1   104  UNP    Q15370   ELOB_HUMAN       1    104             
DBREF  5BO4 F   17   112  UNP    Q15369   ELOC_HUMAN      17    112             
DBREF  5BO4 G   32   198  UNP    O14508   SOCS2_HUMAN     32    198             
DBREF  5BO4 H    1   104  UNP    Q15370   ELOB_HUMAN       1    104             
DBREF  5BO4 I   17   112  UNP    Q15369   ELOC_HUMAN      17    112             
DBREF  5BO4 J   32   198  UNP    O14508   SOCS2_HUMAN     32    198             
DBREF  5BO4 K    1   104  UNP    Q15370   ELOB_HUMAN       1    104             
DBREF  5BO4 L   17   112  UNP    Q15369   ELOC_HUMAN      17    112             
DBREF  5BO4 M   32   198  UNP    O14508   SOCS2_HUMAN     32    198             
DBREF  5BO4 N    1   104  UNP    Q15370   ELOB_HUMAN       1    104             
DBREF  5BO4 O   17   112  UNP    Q15369   ELOC_HUMAN      17    112             
DBREF  5BO4 P   32   198  UNP    O14508   SOCS2_HUMAN     32    198             
DBREF  5BO4 Q    1   104  UNP    Q15370   ELOB_HUMAN       1    104             
DBREF  5BO4 R   17   112  UNP    Q15369   ELOC_HUMAN      17    112             
SEQADV 5BO4 SER A   30  UNP  O14508              EXPRESSION TAG                 
SEQADV 5BO4 MET A   31  UNP  O14508              EXPRESSION TAG                 
SEQADV 5BO4 MET C   16  UNP  Q15369              INITIATING METHIONINE          
SEQADV 5BO4 SER D   30  UNP  O14508              EXPRESSION TAG                 
SEQADV 5BO4 MET D   31  UNP  O14508              EXPRESSION TAG                 
SEQADV 5BO4 MET F   16  UNP  Q15369              INITIATING METHIONINE          
SEQADV 5BO4 SER G   30  UNP  O14508              EXPRESSION TAG                 
SEQADV 5BO4 MET G   31  UNP  O14508              EXPRESSION TAG                 
SEQADV 5BO4 MET I   16  UNP  Q15369              INITIATING METHIONINE          
SEQADV 5BO4 SER J   30  UNP  O14508              EXPRESSION TAG                 
SEQADV 5BO4 MET J   31  UNP  O14508              EXPRESSION TAG                 
SEQADV 5BO4 MET L   16  UNP  Q15369              INITIATING METHIONINE          
SEQADV 5BO4 SER M   30  UNP  O14508              EXPRESSION TAG                 
SEQADV 5BO4 MET M   31  UNP  O14508              EXPRESSION TAG                 
SEQADV 5BO4 MET O   16  UNP  Q15369              INITIATING METHIONINE          
SEQADV 5BO4 SER P   30  UNP  O14508              EXPRESSION TAG                 
SEQADV 5BO4 MET P   31  UNP  O14508              EXPRESSION TAG                 
SEQADV 5BO4 MET R   16  UNP  Q15369              INITIATING METHIONINE          
SEQRES   1 A  169  SER MET GLN ALA ALA ARG LEU ALA LYS ALA LEU ARG GLU          
SEQRES   2 A  169  LEU GLY GLN THR GLY TRP TYR TRP GLY SER MET THR VAL          
SEQRES   3 A  169  ASN GLU ALA LYS GLU LYS LEU LYS GLU ALA PRO GLU GLY          
SEQRES   4 A  169  THR PHE LEU ILE ARG ASP SER SER HIS SER ASP TYR LEU          
SEQRES   5 A  169  LEU THR ILE SER VAL LYS THR SER ALA GLY PRO THR ASN          
SEQRES   6 A  169  LEU ARG ILE GLU TYR GLN ASP GLY LYS PHE ARG LEU ASP          
SEQRES   7 A  169  SER ILE ILE CAS VAL LYS SER LYS LEU LYS GLN PHE ASP          
SEQRES   8 A  169  SER VAL VAL HIS LEU ILE ASP TYR TYR VAL GLN MET CYS          
SEQRES   9 A  169  LYS ASP LYS ARG THR GLY PRO GLU ALA PRO ARG ASN GLY          
SEQRES  10 A  169  THR VAL HIS LEU TYR LEU THR LYS PRO LEU TYR THR SER          
SEQRES  11 A  169  ALA PRO SER LEU GLN HIS LEU CYS ARG LEU THR ILE ASN          
SEQRES  12 A  169  LYS CYS THR GLY ALA ILE TRP GLY LEU PRO LEU PRO THR          
SEQRES  13 A  169  ARG LEU LYS ASP TYR LEU GLU GLU TYR LYS PHE GLN VAL          
SEQRES   1 B  104  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 B  104  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 B  104  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 B  104  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 B  104  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 B  104  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 B  104  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CAS ILE GLU          
SEQRES   8 B  104  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
SEQRES   1 C   97  MET MET TYR VAL LYS LEU ILE SER SER ASP GLY HIS GLU          
SEQRES   2 C   97  PHE ILE VAL LYS ARG GLU HIS ALA LEU THR SER GLY THR          
SEQRES   3 C   97  ILE LYS ALA MET LEU SER GLY PRO GLY GLN PHE ALA GLU          
SEQRES   4 C   97  ASN GLU THR ASN GLU VAL ASN PHE ARG GLU ILE PRO SER          
SEQRES   5 C   97  HIS VAL LEU SER LYS VAL CYS MET TYR PHE THR TYR LYS          
SEQRES   6 C   97  VAL ARG TYR THR ASN SER SER THR GLU ILE PRO GLU PHE          
SEQRES   7 C   97  PRO ILE ALA PRO GLU ILE ALA LEU GLU LEU LEU MET ALA          
SEQRES   8 C   97  ALA ASN PHE LEU ASP CYS                                      
SEQRES   1 D  169  SER MET GLN ALA ALA ARG LEU ALA LYS ALA LEU ARG GLU          
SEQRES   2 D  169  LEU GLY GLN THR GLY TRP TYR TRP GLY SER MET THR VAL          
SEQRES   3 D  169  ASN GLU ALA LYS GLU LYS LEU LYS GLU ALA PRO GLU GLY          
SEQRES   4 D  169  THR PHE LEU ILE ARG ASP SER SER HIS SER ASP TYR LEU          
SEQRES   5 D  169  LEU THR ILE SER VAL LYS THR SER ALA GLY PRO THR ASN          
SEQRES   6 D  169  LEU ARG ILE GLU TYR GLN ASP GLY LYS PHE ARG LEU ASP          
SEQRES   7 D  169  SER ILE ILE CAS VAL LYS SER LYS LEU LYS GLN PHE ASP          
SEQRES   8 D  169  SER VAL VAL HIS LEU ILE ASP TYR TYR VAL GLN MET CYS          
SEQRES   9 D  169  LYS ASP LYS ARG THR GLY PRO GLU ALA PRO ARG ASN GLY          
SEQRES  10 D  169  THR VAL HIS LEU TYR LEU THR LYS PRO LEU TYR THR SER          
SEQRES  11 D  169  ALA PRO SER LEU GLN HIS LEU CYS ARG LEU THR ILE ASN          
SEQRES  12 D  169  LYS CYS THR GLY ALA ILE TRP GLY LEU PRO LEU PRO THR          
SEQRES  13 D  169  ARG LEU LYS ASP TYR LEU GLU GLU TYR LYS PHE GLN VAL          
SEQRES   1 E  104  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 E  104  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 E  104  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 E  104  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 E  104  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 E  104  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 E  104  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CAS ILE GLU          
SEQRES   8 E  104  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
SEQRES   1 F   97  MET MET TYR VAL LYS LEU ILE SER SER ASP GLY HIS GLU          
SEQRES   2 F   97  PHE ILE VAL LYS ARG GLU HIS ALA LEU THR SER GLY THR          
SEQRES   3 F   97  ILE LYS ALA MET LEU SER GLY PRO GLY GLN PHE ALA GLU          
SEQRES   4 F   97  ASN GLU THR ASN GLU VAL ASN PHE ARG GLU ILE PRO SER          
SEQRES   5 F   97  HIS VAL LEU SER LYS VAL CYS MET TYR PHE THR TYR LYS          
SEQRES   6 F   97  VAL ARG TYR THR ASN SER SER THR GLU ILE PRO GLU PHE          
SEQRES   7 F   97  PRO ILE ALA PRO GLU ILE ALA LEU GLU LEU LEU MET ALA          
SEQRES   8 F   97  ALA ASN PHE LEU ASP CYS                                      
SEQRES   1 G  169  SER MET GLN ALA ALA ARG LEU ALA LYS ALA LEU ARG GLU          
SEQRES   2 G  169  LEU GLY GLN THR GLY TRP TYR TRP GLY SER MET THR VAL          
SEQRES   3 G  169  ASN GLU ALA LYS GLU LYS LEU LYS GLU ALA PRO GLU GLY          
SEQRES   4 G  169  THR PHE LEU ILE ARG ASP SER SER HIS SER ASP TYR LEU          
SEQRES   5 G  169  LEU THR ILE SER VAL LYS THR SER ALA GLY PRO THR ASN          
SEQRES   6 G  169  LEU ARG ILE GLU TYR GLN ASP GLY LYS PHE ARG LEU ASP          
SEQRES   7 G  169  SER ILE ILE CAS VAL LYS SER LYS LEU LYS GLN PHE ASP          
SEQRES   8 G  169  SER VAL VAL HIS LEU ILE ASP TYR TYR VAL GLN MET CYS          
SEQRES   9 G  169  LYS ASP LYS ARG THR GLY PRO GLU ALA PRO ARG ASN GLY          
SEQRES  10 G  169  THR VAL HIS LEU TYR LEU THR LYS PRO LEU TYR THR SER          
SEQRES  11 G  169  ALA PRO SER LEU GLN HIS LEU CYS ARG LEU THR ILE ASN          
SEQRES  12 G  169  LYS CYS THR GLY ALA ILE TRP GLY LEU PRO LEU PRO THR          
SEQRES  13 G  169  ARG LEU LYS ASP TYR LEU GLU GLU TYR LYS PHE GLN VAL          
SEQRES   1 H  104  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 H  104  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 H  104  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 H  104  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 H  104  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 H  104  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 H  104  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CAS ILE GLU          
SEQRES   8 H  104  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
SEQRES   1 I   97  MET MET TYR VAL LYS LEU ILE SER SER ASP GLY HIS GLU          
SEQRES   2 I   97  PHE ILE VAL LYS ARG GLU HIS ALA LEU THR SER GLY THR          
SEQRES   3 I   97  ILE LYS ALA MET LEU SER GLY PRO GLY GLN PHE ALA GLU          
SEQRES   4 I   97  ASN GLU THR ASN GLU VAL ASN PHE ARG GLU ILE PRO SER          
SEQRES   5 I   97  HIS VAL LEU SER LYS VAL CYS MET TYR PHE THR TYR LYS          
SEQRES   6 I   97  VAL ARG TYR THR ASN SER SER THR GLU ILE PRO GLU PHE          
SEQRES   7 I   97  PRO ILE ALA PRO GLU ILE ALA LEU GLU LEU LEU MET ALA          
SEQRES   8 I   97  ALA ASN PHE LEU ASP CYS                                      
SEQRES   1 J  169  SER MET GLN ALA ALA ARG LEU ALA LYS ALA LEU ARG GLU          
SEQRES   2 J  169  LEU GLY GLN THR GLY TRP TYR TRP GLY SER MET THR VAL          
SEQRES   3 J  169  ASN GLU ALA LYS GLU LYS LEU LYS GLU ALA PRO GLU GLY          
SEQRES   4 J  169  THR PHE LEU ILE ARG ASP SER SER HIS SER ASP TYR LEU          
SEQRES   5 J  169  LEU THR ILE SER VAL LYS THR SER ALA GLY PRO THR ASN          
SEQRES   6 J  169  LEU ARG ILE GLU TYR GLN ASP GLY LYS PHE ARG LEU ASP          
SEQRES   7 J  169  SER ILE ILE CAS VAL LYS SER LYS LEU LYS GLN PHE ASP          
SEQRES   8 J  169  SER VAL VAL HIS LEU ILE ASP TYR TYR VAL GLN MET CYS          
SEQRES   9 J  169  LYS ASP LYS ARG THR GLY PRO GLU ALA PRO ARG ASN GLY          
SEQRES  10 J  169  THR VAL HIS LEU TYR LEU THR LYS PRO LEU TYR THR SER          
SEQRES  11 J  169  ALA PRO SER LEU GLN HIS LEU CYS ARG LEU THR ILE ASN          
SEQRES  12 J  169  LYS CYS THR GLY ALA ILE TRP GLY LEU PRO LEU PRO THR          
SEQRES  13 J  169  ARG LEU LYS ASP TYR LEU GLU GLU TYR LYS PHE GLN VAL          
SEQRES   1 K  104  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 K  104  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 K  104  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 K  104  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 K  104  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 K  104  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 K  104  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CAS ILE GLU          
SEQRES   8 K  104  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
SEQRES   1 L   97  MET MET TYR VAL LYS LEU ILE SER SER ASP GLY HIS GLU          
SEQRES   2 L   97  PHE ILE VAL LYS ARG GLU HIS ALA LEU THR SER GLY THR          
SEQRES   3 L   97  ILE LYS ALA MET LEU SER GLY PRO GLY GLN PHE ALA GLU          
SEQRES   4 L   97  ASN GLU THR ASN GLU VAL ASN PHE ARG GLU ILE PRO SER          
SEQRES   5 L   97  HIS VAL LEU SER LYS VAL CYS MET TYR PHE THR TYR LYS          
SEQRES   6 L   97  VAL ARG TYR THR ASN SER SER THR GLU ILE PRO GLU PHE          
SEQRES   7 L   97  PRO ILE ALA PRO GLU ILE ALA LEU GLU LEU LEU MET ALA          
SEQRES   8 L   97  ALA ASN PHE LEU ASP CYS                                      
SEQRES   1 M  169  SER MET GLN ALA ALA ARG LEU ALA LYS ALA LEU ARG GLU          
SEQRES   2 M  169  LEU GLY GLN THR GLY TRP TYR TRP GLY SER MET THR VAL          
SEQRES   3 M  169  ASN GLU ALA LYS GLU LYS LEU LYS GLU ALA PRO GLU GLY          
SEQRES   4 M  169  THR PHE LEU ILE ARG ASP SER SER HIS SER ASP TYR LEU          
SEQRES   5 M  169  LEU THR ILE SER VAL LYS THR SER ALA GLY PRO THR ASN          
SEQRES   6 M  169  LEU ARG ILE GLU TYR GLN ASP GLY LYS PHE ARG LEU ASP          
SEQRES   7 M  169  SER ILE ILE CAS VAL LYS SER LYS LEU LYS GLN PHE ASP          
SEQRES   8 M  169  SER VAL VAL HIS LEU ILE ASP TYR TYR VAL GLN MET CYS          
SEQRES   9 M  169  LYS ASP LYS ARG THR GLY PRO GLU ALA PRO ARG ASN GLY          
SEQRES  10 M  169  THR VAL HIS LEU TYR LEU THR LYS PRO LEU TYR THR SER          
SEQRES  11 M  169  ALA PRO SER LEU GLN HIS LEU CYS ARG LEU THR ILE ASN          
SEQRES  12 M  169  LYS CYS THR GLY ALA ILE TRP GLY LEU PRO LEU PRO THR          
SEQRES  13 M  169  ARG LEU LYS ASP TYR LEU GLU GLU TYR LYS PHE GLN VAL          
SEQRES   1 N  104  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 N  104  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 N  104  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 N  104  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 N  104  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 N  104  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 N  104  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CAS ILE GLU          
SEQRES   8 N  104  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
SEQRES   1 O   97  MET MET TYR VAL LYS LEU ILE SER SER ASP GLY HIS GLU          
SEQRES   2 O   97  PHE ILE VAL LYS ARG GLU HIS ALA LEU THR SER GLY THR          
SEQRES   3 O   97  ILE LYS ALA MET LEU SER GLY PRO GLY GLN PHE ALA GLU          
SEQRES   4 O   97  ASN GLU THR ASN GLU VAL ASN PHE ARG GLU ILE PRO SER          
SEQRES   5 O   97  HIS VAL LEU SER LYS VAL CYS MET TYR PHE THR TYR LYS          
SEQRES   6 O   97  VAL ARG TYR THR ASN SER SER THR GLU ILE PRO GLU PHE          
SEQRES   7 O   97  PRO ILE ALA PRO GLU ILE ALA LEU GLU LEU LEU MET ALA          
SEQRES   8 O   97  ALA ASN PHE LEU ASP CYS                                      
SEQRES   1 P  169  SER MET GLN ALA ALA ARG LEU ALA LYS ALA LEU ARG GLU          
SEQRES   2 P  169  LEU GLY GLN THR GLY TRP TYR TRP GLY SER MET THR VAL          
SEQRES   3 P  169  ASN GLU ALA LYS GLU LYS LEU LYS GLU ALA PRO GLU GLY          
SEQRES   4 P  169  THR PHE LEU ILE ARG ASP SER SER HIS SER ASP TYR LEU          
SEQRES   5 P  169  LEU THR ILE SER VAL LYS THR SER ALA GLY PRO THR ASN          
SEQRES   6 P  169  LEU ARG ILE GLU TYR GLN ASP GLY LYS PHE ARG LEU ASP          
SEQRES   7 P  169  SER ILE ILE CAS VAL LYS SER LYS LEU LYS GLN PHE ASP          
SEQRES   8 P  169  SER VAL VAL HIS LEU ILE ASP TYR TYR VAL GLN MET CYS          
SEQRES   9 P  169  LYS ASP LYS ARG THR GLY PRO GLU ALA PRO ARG ASN GLY          
SEQRES  10 P  169  THR VAL HIS LEU TYR LEU THR LYS PRO LEU TYR THR SER          
SEQRES  11 P  169  ALA PRO SER LEU GLN HIS LEU CYS ARG LEU THR ILE ASN          
SEQRES  12 P  169  LYS CYS THR GLY ALA ILE TRP GLY LEU PRO LEU PRO THR          
SEQRES  13 P  169  ARG LEU LYS ASP TYR LEU GLU GLU TYR LYS PHE GLN VAL          
SEQRES   1 Q  104  MET ASP VAL PHE LEU MET ILE ARG ARG HIS LYS THR THR          
SEQRES   2 Q  104  ILE PHE THR ASP ALA LYS GLU SER SER THR VAL PHE GLU          
SEQRES   3 Q  104  LEU LYS ARG ILE VAL GLU GLY ILE LEU LYS ARG PRO PRO          
SEQRES   4 Q  104  ASP GLU GLN ARG LEU TYR LYS ASP ASP GLN LEU LEU ASP          
SEQRES   5 Q  104  ASP GLY LYS THR LEU GLY GLU CYS GLY PHE THR SER GLN          
SEQRES   6 Q  104  THR ALA ARG PRO GLN ALA PRO ALA THR VAL GLY LEU ALA          
SEQRES   7 Q  104  PHE ARG ALA ASP ASP THR PHE GLU ALA LEU CAS ILE GLU          
SEQRES   8 Q  104  PRO PHE SER SER PRO PRO GLU LEU PRO ASP VAL MET LYS          
SEQRES   1 R   97  MET MET TYR VAL LYS LEU ILE SER SER ASP GLY HIS GLU          
SEQRES   2 R   97  PHE ILE VAL LYS ARG GLU HIS ALA LEU THR SER GLY THR          
SEQRES   3 R   97  ILE LYS ALA MET LEU SER GLY PRO GLY GLN PHE ALA GLU          
SEQRES   4 R   97  ASN GLU THR ASN GLU VAL ASN PHE ARG GLU ILE PRO SER          
SEQRES   5 R   97  HIS VAL LEU SER LYS VAL CYS MET TYR PHE THR TYR LYS          
SEQRES   6 R   97  VAL ARG TYR THR ASN SER SER THR GLU ILE PRO GLU PHE          
SEQRES   7 R   97  PRO ILE ALA PRO GLU ILE ALA LEU GLU LEU LEU MET ALA          
SEQRES   8 R   97  ALA ASN PHE LEU ASP CYS                                      
MODRES 5BO4 CAS A  111  CYS  MODIFIED RESIDUE                                   
MODRES 5BO4 CAS B   89  CYS  MODIFIED RESIDUE                                   
MODRES 5BO4 CAS D  111  CYS  MODIFIED RESIDUE                                   
MODRES 5BO4 CAS E   89  CYS  MODIFIED RESIDUE                                   
MODRES 5BO4 CAS G  111  CYS  MODIFIED RESIDUE                                   
MODRES 5BO4 CAS H   89  CYS  MODIFIED RESIDUE                                   
MODRES 5BO4 CAS J  111  CYS  MODIFIED RESIDUE                                   
MODRES 5BO4 CAS K   89  CYS  MODIFIED RESIDUE                                   
MODRES 5BO4 CAS M  111  CYS  MODIFIED RESIDUE                                   
MODRES 5BO4 CAS P  111  CYS  MODIFIED RESIDUE                                   
MODRES 5BO4 CAS Q   89  CYS  MODIFIED RESIDUE                                   
HET    CAS  A 111       9                                                       
HET    CAS  B  89       9                                                       
HET    CAS  D 111       9                                                       
HET    CAS  E  89       9                                                       
HET    CAS  G 111       9                                                       
HET    CAS  H  89       9                                                       
HET    CAS  J 111       9                                                       
HET    CAS  K  89       9                                                       
HET    CAS  M 111       9                                                       
HET    CAS  P 111       9                                                       
HET    CAS  Q  89       9                                                       
HETNAM     CAS S-(DIMETHYLARSENIC)CYSTEINE                                      
FORMUL   1  CAS    11(C5 H12 AS N O2 S)                                         
FORMUL  19  HOH   *33(H2 O)                                                     
HELIX    1 AA1 MET A   31  GLY A   47  1                                  17    
HELIX    2 AA2 THR A   54  LYS A   63  1                                  10    
HELIX    3 AA3 VAL A  112  LEU A  116  5                                   5    
HELIX    4 AA4 SER A  121  CYS A  133  1                                  13    
HELIX    5 AA5 SER A  162  THR A  175  1                                  14    
HELIX    6 AA6 PRO A  184  TYR A  194  1                                  11    
HELIX    7 AA7 THR B   23  LYS B   36  1                                  14    
HELIX    8 AA8 THR B   63  ALA B   67  5                                   5    
HELIX    9 AA9 PRO B  100  LYS B  104  5                                   5    
HELIX   10 AB1 ARG C   33  LEU C   37  1                                   5    
HELIX   11 AB2 SER C   39  ALA C   44  1                                   6    
HELIX   12 AB3 PRO C   66  TYR C   83  1                                  18    
HELIX   13 AB4 ALA C   96  ASP C  111  1                                  16    
HELIX   14 AB5 GLN D   32  GLN D   45  1                                  14    
HELIX   15 AB6 THR D   54  LEU D   62  1                                   9    
HELIX   16 AB7 SER D  121  CYS D  133  1                                  13    
HELIX   17 AB8 SER D  162  THR D  175  1                                  14    
HELIX   18 AB9 PRO D  184  GLU D  193  1                                  10    
HELIX   19 AC1 THR E   23  LYS E   36  1                                  14    
HELIX   20 AC2 PRO E   38  ASP E   40  5                                   3    
HELIX   21 AC3 THR E   56  GLY E   61  1                                   6    
HELIX   22 AC4 ARG F   33  LEU F   37  1                                   5    
HELIX   23 AC5 SER F   39  MET F   45  1                                   7    
HELIX   24 AC6 PRO F   66  TYR F   83  1                                  18    
HELIX   25 AC7 ALA F   96  ASP F  111  1                                  16    
HELIX   26 AC8 GLN G   32  GLY G   47  1                                  16    
HELIX   27 AC9 THR G   54  LYS G   63  1                                  10    
HELIX   28 AD1 VAL G  112  LEU G  116  5                                   5    
HELIX   29 AD2 SER G  121  CYS G  133  1                                  13    
HELIX   30 AD3 SER G  162  LYS G  173  1                                  12    
HELIX   31 AD4 PRO G  184  GLU G  193  1                                  10    
HELIX   32 AD5 THR H   23  LYS H   36  1                                  14    
HELIX   33 AD6 PRO H   38  ASP H   40  5                                   3    
HELIX   34 AD7 THR H   56  GLY H   61  1                                   6    
HELIX   35 AD8 THR H   63  ALA H   67  5                                   5    
HELIX   36 AD9 ARG I   33  LEU I   37  1                                   5    
HELIX   37 AE1 SER I   39  MET I   45  1                                   7    
HELIX   38 AE2 PRO I   66  TYR I   83  1                                  18    
HELIX   39 AE3 ILE I   99  ASP I  111  1                                  13    
HELIX   40 AE4 GLN J   32  GLY J   47  1                                  16    
HELIX   41 AE5 THR J   54  LYS J   63  1                                  10    
HELIX   42 AE6 SER J  121  CYS J  133  1                                  13    
HELIX   43 AE7 SER J  162  THR J  175  1                                  14    
HELIX   44 AE8 ALA J  177  LEU J  181  5                                   5    
HELIX   45 AE9 PRO J  184  GLU J  193  1                                  10    
HELIX   46 AF1 THR K   23  LYS K   36  1                                  14    
HELIX   47 AF2 PRO K   38  ASP K   40  5                                   3    
HELIX   48 AF3 THR K   56  GLY K   61  1                                   6    
HELIX   49 AF4 ARG L   33  LEU L   37  1                                   5    
HELIX   50 AF5 SER L   39  MET L   45  1                                   7    
HELIX   51 AF6 PRO L   66  TYR L   83  1                                  18    
HELIX   52 AF7 ILE L   99  ASP L  111  1                                  13    
HELIX   53 AF8 ALA M   33  GLN M   45  1                                  13    
HELIX   54 AF9 THR M   54  LYS M   63  1                                  10    
HELIX   55 AG1 VAL M  112  LEU M  116  5                                   5    
HELIX   56 AG2 SER M  121  CYS M  133  1                                  13    
HELIX   57 AG3 SER M  162  THR M  175  1                                  14    
HELIX   58 AG4 ALA M  177  LEU M  181  5                                   5    
HELIX   59 AG5 PRO M  184  GLU M  193  1                                  10    
HELIX   60 AG6 THR N   23  ILE N   30  1                                   8    
HELIX   61 AG7 PRO N   38  GLN N   42  5                                   5    
HELIX   62 AG8 ARG O   33  LEU O   37  1                                   5    
HELIX   63 AG9 SER O   39  MET O   45  1                                   7    
HELIX   64 AH1 PRO O   66  TYR O   83  1                                  18    
HELIX   65 AH2 ILE O   99  ASP O  111  1                                  13    
HELIX   66 AH3 ALA P   33  GLN P   45  1                                  13    
HELIX   67 AH4 THR P   54  LYS P   63  1                                  10    
HELIX   68 AH5 VAL P  112  LEU P  116  5                                   5    
HELIX   69 AH6 SER P  121  CYS P  133  1                                  13    
HELIX   70 AH7 SER P  162  THR P  175  1                                  14    
HELIX   71 AH8 PRO P  184  GLU P  193  1                                  10    
HELIX   72 AH9 THR Q   23  LYS Q   36  1                                  14    
HELIX   73 AI1 PRO Q   38  ASP Q   40  5                                   3    
HELIX   74 AI2 ARG R   33  LEU R   37  1                                   5    
HELIX   75 AI3 SER R   39  MET R   45  1                                   7    
HELIX   76 AI4 PRO R   66  TYR R   83  1                                  18    
HELIX   77 AI5 ALA R   96  ASP R  111  1                                  16    
SHEET    1 AA1 4 PHE A  70  ASP A  74  0                                        
SHEET    2 AA1 4 LEU A  82  LYS A  87 -1  O  SER A  85   N  LEU A  71           
SHEET    3 AA1 4 PRO A  92  GLN A 100 -1  O  LEU A  95   N  ILE A  84           
SHEET    4 AA1 4 LYS A 103  LEU A 106 -1  O  ARG A 105   N  GLU A  98           
SHEET    1 AA2 8 GLN B  49  LEU B  50  0                                        
SHEET    2 AA2 8 GLN B  42  LYS B  46 -1  N  LYS B  46   O  GLN B  49           
SHEET    3 AA2 8 ALA B  73  PHE B  79 -1  O  GLY B  76   N  TYR B  45           
SHEET    4 AA2 8 VAL B   3  ARG B   9  1  N  ARG B   8   O  VAL B  75           
SHEET    5 AA2 8 THR B  12  ALA B  18 -1  O  ILE B  14   N  ILE B   7           
SHEET    6 AA2 8 GLU C  28  LYS C  32  1  O  ILE C  30   N  PHE B  15           
SHEET    7 AA2 8 TYR C  18  ILE C  22 -1  N  LEU C  21   O  PHE C  29           
SHEET    8 AA2 8 GLU C  59  ASN C  61  1  O  VAL C  60   N  ILE C  22           
SHEET    1 AA3 4 PHE D  70  ASP D  74  0                                        
SHEET    2 AA3 4 LEU D  82  THR D  88 -1  O  THR D  83   N  ARG D  73           
SHEET    3 AA3 4 GLY D  91  GLN D 100 -1  O  ILE D  97   N  LEU D  82           
SHEET    4 AA3 4 LYS D 103  LEU D 106 -1  O  ARG D 105   N  GLU D  98           
SHEET    1 AA4 4 GLN E  49  LEU E  50  0                                        
SHEET    2 AA4 4 GLN E  42  LYS E  46 -1  N  LYS E  46   O  GLN E  49           
SHEET    3 AA4 4 ALA E  73  ALA E  81 -1  O  GLY E  76   N  TYR E  45           
SHEET    4 AA4 4 THR E  84  PHE E  85 -1  O  THR E  84   N  ALA E  81           
SHEET    1 AA5 8 GLN E  49  LEU E  50  0                                        
SHEET    2 AA5 8 GLN E  42  LYS E  46 -1  N  LYS E  46   O  GLN E  49           
SHEET    3 AA5 8 ALA E  73  ALA E  81 -1  O  GLY E  76   N  TYR E  45           
SHEET    4 AA5 8 LEU E   5  ARG E   9  1  N  MET E   6   O  VAL E  75           
SHEET    5 AA5 8 THR E  12  THR E  16 -1  O  THR E  12   N  ARG E   9           
SHEET    6 AA5 8 GLU F  28  LYS F  32  1  O  ILE F  30   N  THR E  13           
SHEET    7 AA5 8 TYR F  18  ILE F  22 -1  N  LEU F  21   O  PHE F  29           
SHEET    8 AA5 8 GLU F  59  ASN F  61  1  O  VAL F  60   N  LYS F  20           
SHEET    1 AA6 4 PHE G  70  ASP G  74  0                                        
SHEET    2 AA6 4 LEU G  82  THR G  88 -1  O  THR G  83   N  ARG G  73           
SHEET    3 AA6 4 GLY G  91  GLN G 100 -1  O  GLY G  91   N  THR G  88           
SHEET    4 AA6 4 LYS G 103  LEU G 106 -1  O  ARG G 105   N  GLU G  98           
SHEET    1 AA7 8 GLN H  49  LEU H  50  0                                        
SHEET    2 AA7 8 GLN H  42  LYS H  46 -1  N  LYS H  46   O  GLN H  49           
SHEET    3 AA7 8 ALA H  73  PHE H  79 -1  O  GLY H  76   N  TYR H  45           
SHEET    4 AA7 8 ASP H   2  ARG H   9  1  N  MET H   6   O  VAL H  75           
SHEET    5 AA7 8 THR H  12  LYS H  19 -1  O  ILE H  14   N  ILE H   7           
SHEET    6 AA7 8 GLU I  28  LYS I  32  1  O  ILE I  30   N  PHE H  15           
SHEET    7 AA7 8 TYR I  18  ILE I  22 -1  N  LEU I  21   O  PHE I  29           
SHEET    8 AA7 8 GLU I  59  ASN I  61  1  O  VAL I  60   N  ILE I  22           
SHEET    1 AA8 4 PHE J  70  ASP J  74  0                                        
SHEET    2 AA8 4 LEU J  82  LYS J  87 -1  O  THR J  83   N  ARG J  73           
SHEET    3 AA8 4 PRO J  92  GLN J 100 -1  O  LEU J  95   N  ILE J  84           
SHEET    4 AA8 4 LYS J 103  LEU J 106 -1  O  ARG J 105   N  GLU J  98           
SHEET    1 AA9 4 GLN K  49  LEU K  50  0                                        
SHEET    2 AA9 4 GLN K  42  LYS K  46 -1  N  LYS K  46   O  GLN K  49           
SHEET    3 AA9 4 ALA K  73  ALA K  81 -1  O  GLY K  76   N  TYR K  45           
SHEET    4 AA9 4 THR K  84  PHE K  85 -1  O  THR K  84   N  ALA K  81           
SHEET    1 AB1 8 GLN K  49  LEU K  50  0                                        
SHEET    2 AB1 8 GLN K  42  LYS K  46 -1  N  LYS K  46   O  GLN K  49           
SHEET    3 AB1 8 ALA K  73  ALA K  81 -1  O  GLY K  76   N  TYR K  45           
SHEET    4 AB1 8 VAL K   3  ARG K   9  1  N  ARG K   8   O  VAL K  75           
SHEET    5 AB1 8 THR K  12  ALA K  18 -1  O  ILE K  14   N  ILE K   7           
SHEET    6 AB1 8 GLU L  28  LYS L  32  1  O  ILE L  30   N  PHE K  15           
SHEET    7 AB1 8 TYR L  18  ILE L  22 -1  N  LEU L  21   O  PHE L  29           
SHEET    8 AB1 8 VAL L  60  ASN L  61  1  O  VAL L  60   N  LYS L  20           
SHEET    1 AB2 4 PHE M  70  ASP M  74  0                                        
SHEET    2 AB2 4 LEU M  82  LYS M  87 -1  O  SER M  85   N  LEU M  71           
SHEET    3 AB2 4 PRO M  92  GLN M 100 -1  O  THR M  93   N  VAL M  86           
SHEET    4 AB2 4 LYS M 103  LEU M 106 -1  O  ARG M 105   N  GLU M  98           
SHEET    1 AB3 3 THR N  12  ILE N  14  0                                        
SHEET    2 AB3 3 LEU N   5  ARG N   9 -1  N  ILE N   7   O  ILE N  14           
SHEET    3 AB3 3 ALA N  73  GLY N  76  1  O  VAL N  75   N  ARG N   8           
SHEET    1 AB4 2 TYR N  45  LYS N  46  0                                        
SHEET    2 AB4 2 GLN N  49  LEU N  50 -1  O  GLN N  49   N  LYS N  46           
SHEET    1 AB5 3 GLU O  28  LYS O  32  0                                        
SHEET    2 AB5 3 TYR O  18  ILE O  22 -1  N  LEU O  21   O  PHE O  29           
SHEET    3 AB5 3 GLU O  59  ASN O  61  1  O  VAL O  60   N  LYS O  20           
SHEET    1 AB6 4 PHE P  70  ASP P  74  0                                        
SHEET    2 AB6 4 LEU P  82  THR P  88 -1  O  SER P  85   N  LEU P  71           
SHEET    3 AB6 4 GLY P  91  GLN P 100 -1  O  THR P  93   N  VAL P  86           
SHEET    4 AB6 4 LYS P 103  LEU P 106 -1  O  ARG P 105   N  GLU P  98           
SHEET    1 AB7 8 GLN Q  49  LEU Q  50  0                                        
SHEET    2 AB7 8 GLN Q  42  LYS Q  46 -1  N  LYS Q  46   O  GLN Q  49           
SHEET    3 AB7 8 ALA Q  73  PHE Q  79 -1  O  GLY Q  76   N  TYR Q  45           
SHEET    4 AB7 8 VAL Q   3  ARG Q   9  1  N  MET Q   6   O  VAL Q  75           
SHEET    5 AB7 8 THR Q  12  ALA Q  18 -1  O  THR Q  16   N  LEU Q   5           
SHEET    6 AB7 8 GLU R  28  LYS R  32  1  O  ILE R  30   N  THR Q  13           
SHEET    7 AB7 8 TYR R  18  ILE R  22 -1  N  LEU R  21   O  PHE R  29           
SHEET    8 AB7 8 GLU R  59  ASN R  61  1  O  VAL R  60   N  LYS R  20           
LINK         C   ILE A 110                 N   CAS A 111     1555   1555  1.33  
LINK         C   CAS A 111                 N   VAL A 112     1555   1555  1.33  
LINK         C   LEU B  88                 N   CAS B  89     1555   1555  1.33  
LINK         C   CAS B  89                 N   ILE B  90     1555   1555  1.33  
LINK         C   ILE D 110                 N   CAS D 111     1555   1555  1.34  
LINK         C   CAS D 111                 N   VAL D 112     1555   1555  1.33  
LINK         C   LEU E  88                 N   CAS E  89     1555   1555  1.33  
LINK         C   CAS E  89                 N   ILE E  90     1555   1555  1.33  
LINK         C   ILE G 110                 N   CAS G 111     1555   1555  1.32  
LINK         C   CAS G 111                 N   VAL G 112     1555   1555  1.33  
LINK         C   LEU H  88                 N   CAS H  89     1555   1555  1.33  
LINK         C   CAS H  89                 N   ILE H  90     1555   1555  1.33  
LINK         C   ILE J 110                 N   CAS J 111     1555   1555  1.33  
LINK         C   CAS J 111                 N   VAL J 112     1555   1555  1.33  
LINK         C   LEU K  88                 N   CAS K  89     1555   1555  1.33  
LINK         C   CAS K  89                 N   ILE K  90     1555   1555  1.33  
LINK         C   ILE M 110                 N   CAS M 111     1555   1555  1.33  
LINK         C   CAS M 111                 N   VAL M 112     1555   1555  1.33  
LINK         C   ILE P 110                 N   CAS P 111     1555   1555  1.33  
LINK         C   CAS P 111                 N   VAL P 112     1555   1555  1.33  
LINK         C   LEU Q  88                 N   CAS Q  89     1555   1555  1.33  
LINK         C   CAS Q  89                 N   ILE Q  90     1555   1555  1.33  
CRYST1  185.217  185.217   67.204  90.00  90.00 120.00 P 32         18          
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      0.005399  0.003117  0.000000        0.00000                         
SCALE2      0.000000  0.006234  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014880        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.566268  0.821767 -0.063556       -0.58370    1                    
MTRIX2   2  0.820238 -0.569425 -0.054451      119.32899    1                    
MTRIX3   2 -0.080937 -0.021297 -0.996492       56.06893    1                    
MTRIX1   3 -0.998944 -0.043313  0.015336       96.52274    1                    
MTRIX2   3 -0.043163  0.999018  0.009954       53.27217    1                    
MTRIX3   3 -0.015752  0.009282 -0.999833       29.06266    1                    
MTRIX1   4 -0.548441 -0.836172 -0.005386      188.02098    1                    
MTRIX2   4  0.836188 -0.548438 -0.002080      112.47446    1                    
MTRIX3   4 -0.001214 -0.005645  0.999983      -22.24137    1                    
MTRIX1   5 -0.997727  0.021042 -0.064010      183.16541    1                    
MTRIX2   5  0.024547  0.998213 -0.054481        1.39315    1                    
MTRIX3   5  0.062749 -0.055929 -0.996461       28.03113    1                    
MTRIX1   6 -0.552012  0.830301  0.076705        0.24920    1                    
MTRIX2   6 -0.828796 -0.556448  0.058847      218.96188    1                    
MTRIX3   6  0.091543 -0.031088  0.995316      -46.29263    1                    
MTRIX1   7  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   7  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   7  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   8  0.490237  0.871264  0.023822       -2.55777    1                    
MTRIX2   8  0.869616 -0.487106 -0.080603      112.29782    1                    
MTRIX3   8 -0.058623  0.060231 -0.996462       49.87924    1                    
MTRIX1   9 -0.997753 -0.060461  0.028854       97.39793    1                    
MTRIX2   9 -0.060379  0.998169  0.003729       53.51656    1                    
MTRIX3   9 -0.029026  0.001979 -0.999577       29.52430    1                    
MTRIX1  10 -0.582450 -0.812500 -0.024409      188.82295    1                    
MTRIX2  10  0.812640 -0.582733  0.006100      116.74368    1                    
MTRIX3  10 -0.019180 -0.016283  0.999683      -20.16603    1                    
MTRIX1  11 -0.991361 -0.122077  0.047966      198.44371    1                    
MTRIX2  11 -0.125692  0.988720 -0.081450       18.93620    1                    
MTRIX3  11 -0.037482 -0.086775 -0.995523       42.48910    1                    
MTRIX1  12 -0.481164  0.875576 -0.042990       -0.51914    1                    
MTRIX2  12 -0.874345 -0.475793  0.095611      209.50180    1                    
MTRIX3  12  0.063260  0.083592  0.994490      -58.21887    1                    
MTRIX1  13  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2  13  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3  13  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1  14  0.493554  0.869680  0.007858       -2.01457    1                    
MTRIX2  14  0.866317 -0.490807 -0.092754      113.58715    1                    
MTRIX3  14 -0.076810  0.052586 -0.995658       51.16740    1                    
MTRIX1  15 -0.998466 -0.052271  0.018250       97.08633    1                    
MTRIX2  15 -0.052119  0.998603  0.008702       53.35362    1                    
MTRIX3  15 -0.018679  0.007737 -0.999796       29.14953    1                    
MTRIX1  16 -0.573948 -0.818754 -0.014998      188.62328    1                    
MTRIX2  16  0.818794 -0.574066  0.004876      115.67064    1                    
MTRIX3  16 -0.012602 -0.009482  0.999876      -21.13847    1                    
MTRIX1  17 -0.996819 -0.079039  0.010192      194.64964    1                    
MTRIX2  17 -0.079647  0.992431 -0.093477       14.02297    1                    
MTRIX3  17 -0.002726 -0.093991 -0.995569       39.76540    1                    
MTRIX1  18 -0.480748  0.876794 -0.010669       -2.22743    1                    
MTRIX2  18 -0.873173 -0.477577  0.097414      209.64885    1                    
MTRIX3  18  0.080317  0.056148  0.995187      -55.62812    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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