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Database: PDB
Entry: 2FRX
LinkDB: 2FRX
Original site: 2FRX 
HEADER    TRANSFERASE                             20-JAN-06   2FRX              
TITLE     CRYSTAL STRUCTURE OF YEBU, A M5C RNA METHYLTRANSFERASE FROM E.COLI    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYPOTHETICAL PROTEIN YEBU;                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: RNA M5C METHYLTRANSFERASE;                                  
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: YEBU;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PT73.3HISGW                               
KEYWDS    ROSSMANN-TYPE S-ADENOSYLMETHIONINE-DEPENDENT METHYLTRANSFERASE        
KEYWDS   2 DOMAIN, C-TERMINAL PUA (PSEUDOURIDINE SYNTHASES AND ARCHAEOSINE-     
KEYWDS   3 SPECIFIC TRANSGLYCOSYLASES) DOMAIN, TRANSFERASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.ERLANDSEN,P.NORDLUND,B.M.HALLBERG,K.A.JOHNSON,U.B.ERICSSON          
REVDAT   4   23-MAY-18 2FRX    1       REMARK                                   
REVDAT   3   13-JUL-11 2FRX    1       VERSN                                    
REVDAT   2   24-FEB-09 2FRX    1       VERSN                                    
REVDAT   1   29-AUG-06 2FRX    0                                                
JRNL        AUTH   B.M.HALLBERG,U.B.ERICSSON,K.A.JOHNSON,N.M.ANDERSEN,          
JRNL        AUTH 2 S.DOUTHWAITE,P.NORDLUND,A.E.BEUSCHER IV,H.ERLANDSEN          
JRNL        TITL   THE STRUCTURE OF THE RNA M5C METHYLTRANSFERASE YEBU FROM     
JRNL        TITL 2 ESCHERICHIA COLI REVEALS A C-TERMINAL RNA-RECRUITING PUA     
JRNL        TITL 3 DOMAIN                                                       
JRNL        REF    J.MOL.BIOL.                   V. 360   774 2006              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   16793063                                                     
JRNL        DOI    10.1016/J.JMB.2006.05.047                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0003                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
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) : 29.03                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 45743                          
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) : 0.234                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2314                            
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) : 3188                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.52                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2980                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 159                          
REMARK   3   BIN FREE R VALUE                    : 0.3610                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14266                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.07000                                              
REMARK   3    B22 (A**2) : 0.03000                                              
REMARK   3    B33 (A**2) : -0.11000                                             
REMARK   3    B12 (A**2) : 0.01000                                              
REMARK   3    B13 (A**2) : 0.04000                                              
REMARK   3    B23 (A**2) : -0.05000                                             
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): 0.480         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.415         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 49.191        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.892                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 14636 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 19901 ; 1.758 ; 1.936       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1806 ; 7.613 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   693 ;39.807 ;23.709       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2319 ;22.484 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   111 ;18.281 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2150 ; 0.124 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11375 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  7353 ; 0.264 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  9870 ; 0.326 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   426 ; 0.196 ; 0.200       
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):    83 ; 0.201 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.264 ; 0.200       
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):  9264 ; 0.532 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14587 ; 0.798 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6107 ; 1.661 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5314 ; 2.524 ; 4.500       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : C A B D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C      8       C     474      3                      
REMARK   3           1     A      8       A     474      3                      
REMARK   3           1     B      8       B     474      3                      
REMARK   3           1     D      8       D     474      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    C    (A):   1812 ; 0.060 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    A    (A):   1812 ; 0.060 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   1812 ; 0.060 ; 0.050           
REMARK   3   TIGHT POSITIONAL   1    D    (A):   1812 ; 0.060 ; 0.050           
REMARK   3   LOOSE POSITIONAL   1    C    (A):   1739 ; 0.820 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    A    (A):   1739 ; 0.780 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   1739 ; 0.760 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    D    (A):   1739 ; 0.740 ; 5.000           
REMARK   3   TIGHT THERMAL      1    C (A**2):   1812 ; 0.100 ; 0.500           
REMARK   3   TIGHT THERMAL      1    A (A**2):   1812 ; 0.090 ; 0.500           
REMARK   3   TIGHT THERMAL      1    B (A**2):   1812 ; 0.110 ; 0.500           
REMARK   3   TIGHT THERMAL      1    D (A**2):   1812 ; 0.090 ; 0.500           
REMARK   3   LOOSE THERMAL      1    C (A**2):   1739 ; 1.590 ;10.000           
REMARK   3   LOOSE THERMAL      1    A (A**2):   1739 ; 1.650 ;10.000           
REMARK   3   LOOSE THERMAL      1    B (A**2):   1739 ; 1.850 ;10.000           
REMARK   3   LOOSE THERMAL      1    D (A**2):   1739 ; 1.490 ;10.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     8        A   474                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.7270   8.6830  76.6220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0680 T22:  -0.1847                                     
REMARK   3      T33:  -0.1430 T12:   0.2645                                     
REMARK   3      T13:   0.0570 T23:  -0.0215                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9944 L22:   2.6787                                     
REMARK   3      L33:   2.1126 L12:  -1.8184                                     
REMARK   3      L13:  -1.1410 L23:   0.5126                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2743 S12:   0.3578 S13:   0.0257                       
REMARK   3      S21:  -0.7060 S22:  -0.3099 S23:  -0.4123                       
REMARK   3      S31:   0.2088 S32:  -0.0469 S33:   0.0355                       
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     8        B   474                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3070  54.6060  67.0110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3715 T22:  -0.2458                                     
REMARK   3      T33:  -0.3273 T12:   0.1090                                     
REMARK   3      T13:  -0.0283 T23:  -0.0694                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8442 L22:   2.4195                                     
REMARK   3      L33:   2.0409 L12:   0.5456                                     
REMARK   3      L13:  -0.6522 L23:  -0.8433                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0100 S12:   0.4839 S13:  -0.0915                       
REMARK   3      S21:  -0.3075 S22:  -0.0677 S23:  -0.1097                       
REMARK   3      S31:   0.4215 S32:   0.1229 S33:   0.0576                       
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     8        C   474                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.0350   7.8980  25.6440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2472 T22:  -0.2235                                     
REMARK   3      T33:  -0.2559 T12:  -0.1291                                     
REMARK   3      T13:   0.0082 T23:   0.0494                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3852 L22:   2.5212                                     
REMARK   3      L33:   2.1703 L12:  -0.6592                                     
REMARK   3      L13:  -0.7989 L23:   0.7925                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0763 S12:  -0.5283 S13:  -0.2569                       
REMARK   3      S21:   0.4517 S22:  -0.1726 S23:   0.3057                       
REMARK   3      S31:   0.4979 S32:  -0.1536 S33:   0.0963                       
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     8        D   474                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.2050  49.2670  15.9740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1892 T22:  -0.1886                                     
REMARK   3      T33:  -0.1745 T12:  -0.2396                                     
REMARK   3      T13:   0.1058 T23:  -0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8795 L22:   3.0957                                     
REMARK   3      L33:   2.5828 L12:   1.7689                                     
REMARK   3      L13:  -1.3205 L23:  -0.5548                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2214 S12:  -0.2689 S13:   0.1614                       
REMARK   3      S21:   0.8064 S22:  -0.2331 S23:   0.5128                       
REMARK   3      S31:   0.2775 S32:  -0.0191 S33:   0.0117                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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: NULL                                      
REMARK   4                                                                      
REMARK   4 2FRX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JAN-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000036237.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-SEP-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I711                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.962                              
REMARK 200  MONOCHROMATOR                  : MIRROR FOLLOWED BY                 
REMARK 200                                   ASYMMETRICALLY CUT SI-111          
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : MIRROR FOLLOWED BY                 
REMARK 200                                   ASYMMETRICALLY CUT SI-111          
REMARK 200                                   MONOCHROMATOR                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45870                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 3.220                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1300                             
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) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.55100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.140                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXD, SOLVE                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15%(W/V) PEG 8000, 50MM MONO-POTASSIUM   
REMARK 280  DIHYDROGEN PHOSPHATE, 10MM BACL2 OR 15% PEG 5000 MME, SODIUM        
REMARK 280  ACETATE PH 4.6, 0.2M AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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     MSE A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     SER A    22                                                      
REMARK 465     THR A    23                                                      
REMARK 465     LEU A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     ILE A    76                                                      
REMARK 465     GLU A    77                                                      
REMARK 465     ARG A    78                                                      
REMARK 465     ASP A    79                                                      
REMARK 465     ASN A    80                                                      
REMARK 465     GLU A    81                                                      
REMARK 465     ASP A    82                                                      
REMARK 465     ALA A    83                                                      
REMARK 465     LEU A    84                                                      
REMARK 465     PHE A   475                                                      
REMARK 465     THR A   476                                                      
REMARK 465     GLY A   477                                                      
REMARK 465     ASN A   478                                                      
REMARK 465     ALA A   479                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     VAL B     6                                                      
REMARK 465     TYR B     7                                                      
REMARK 465     SER B    22                                                      
REMARK 465     THR B    23                                                      
REMARK 465     LEU B    24                                                      
REMARK 465     SER B    25                                                      
REMARK 465     ILE B    76                                                      
REMARK 465     GLU B    77                                                      
REMARK 465     ARG B    78                                                      
REMARK 465     ASP B    79                                                      
REMARK 465     ASN B    80                                                      
REMARK 465     GLU B    81                                                      
REMARK 465     ASP B    82                                                      
REMARK 465     ALA B    83                                                      
REMARK 465     LEU B    84                                                      
REMARK 465     PHE B   475                                                      
REMARK 465     THR B   476                                                      
REMARK 465     GLY B   477                                                      
REMARK 465     ASN B   478                                                      
REMARK 465     ALA B   479                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     GLN C     3                                                      
REMARK 465     HIS C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     VAL C     6                                                      
REMARK 465     TYR C     7                                                      
REMARK 465     SER C    22                                                      
REMARK 465     THR C    23                                                      
REMARK 465     LEU C    24                                                      
REMARK 465     SER C    25                                                      
REMARK 465     ILE C    76                                                      
REMARK 465     GLU C    77                                                      
REMARK 465     ARG C    78                                                      
REMARK 465     ASP C    79                                                      
REMARK 465     ASN C    80                                                      
REMARK 465     GLU C    81                                                      
REMARK 465     ASP C    82                                                      
REMARK 465     ALA C    83                                                      
REMARK 465     LEU C    84                                                      
REMARK 465     PHE C   475                                                      
REMARK 465     THR C   476                                                      
REMARK 465     GLY C   477                                                      
REMARK 465     ASN C   478                                                      
REMARK 465     ALA C   479                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     GLN D     3                                                      
REMARK 465     HIS D     4                                                      
REMARK 465     THR D     5                                                      
REMARK 465     VAL D     6                                                      
REMARK 465     SER D    22                                                      
REMARK 465     THR D    23                                                      
REMARK 465     LEU D    24                                                      
REMARK 465     SER D    25                                                      
REMARK 465     ILE D    76                                                      
REMARK 465     GLU D    77                                                      
REMARK 465     ARG D    78                                                      
REMARK 465     ASP D    79                                                      
REMARK 465     ASN D    80                                                      
REMARK 465     GLU D    81                                                      
REMARK 465     ASP D    82                                                      
REMARK 465     ALA D    83                                                      
REMARK 465     LEU D    84                                                      
REMARK 465     PHE D   475                                                      
REMARK 465     THR D   476                                                      
REMARK 465     GLY D   477                                                      
REMARK 465     ASN D   478                                                      
REMARK 465     ALA D   479                                                      
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 D 455    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ASP C   176     N    ARG C   178              2.06            
REMARK 500   OD2  ASP C   230     OH   TYR C   265              2.09            
REMARK 500   O    ASP B   176     N    ARG B   178              2.11            
REMARK 500   O    ASP D   176     N    ARG D   178              2.13            
REMARK 500   O    LEU C   210     N    ASN C   212              2.15            
REMARK 500   O    ASP A   176     N    ARG A   178              2.16            
REMARK 500   OD1  ASN A   410     N    ASN A   412              2.16            
REMARK 500   O    PRO D   318     CD   PRO D   320              2.17            
REMARK 500   O    VAL A   430     O    ARG A   459              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASP A  10   CG    ASP A  10   OD2     0.151                       
REMARK 500    ARG A  17   NE    ARG A  17   CZ      0.093                       
REMARK 500    GLU A  18   CD    GLU A  18   OE1     0.085                       
REMARK 500    ASP A  27   CG    ASP A  27   OD1     0.150                       
REMARK 500    ASP A  27   CG    ASP A  27   OD2     0.155                       
REMARK 500    GLU A 216   CG    GLU A 216   CD      0.091                       
REMARK 500    ARG A 335   NE    ARG A 335   CZ      0.114                       
REMARK 500    ARG A 428   CZ    ARG A 428   NH1     0.083                       
REMARK 500    LYS A 454   CD    LYS A 454   CE      0.187                       
REMARK 500    LYS A 454   CE    LYS A 454   NZ      0.299                       
REMARK 500    GLU B  18   CD    GLU B  18   OE1     0.097                       
REMARK 500    GLU B  18   CD    GLU B  18   OE2     0.068                       
REMARK 500    GLN B  34   CD    GLN B  34   OE1     0.140                       
REMARK 500    ARG C  17   CZ    ARG C  17   NH1     0.160                       
REMARK 500    SER C 214   CB    SER C 214   OG      0.430                       
REMARK 500    GLU C 216   CD    GLU C 216   OE1     0.112                       
REMARK 500    GLU C 216   CD    GLU C 216   OE2     0.117                       
REMARK 500    SER C 217   CB    SER C 217   OG      0.080                       
REMARK 500    ARG C 428   CD    ARG C 428   NE      0.174                       
REMARK 500    ARG C 428   NE    ARG C 428   CZ      0.125                       
REMARK 500    ARG C 428   CZ    ARG C 428   NH1     0.273                       
REMARK 500    ARG C 428   CZ    ARG C 428   NH2     0.152                       
REMARK 500    ASP D  10   CG    ASP D  10   OD1     0.309                       
REMARK 500    ASP D  10   CG    ASP D  10   OD2     0.371                       
REMARK 500    ARG D  17   CD    ARG D  17   NE      0.188                       
REMARK 500    ARG D  17   NE    ARG D  17   CZ      0.174                       
REMARK 500    ARG D  17   CZ    ARG D  17   NH1     0.118                       
REMARK 500    ARG D  17   CZ    ARG D  17   NH2    -0.112                       
REMARK 500    GLU D  18   CD    GLU D  18   OE1     0.117                       
REMARK 500    GLU D  18   CD    GLU D  18   OE2     0.108                       
REMARK 500    PHE D  26   CG    PHE D  26   CD2     0.119                       
REMARK 500    PHE D  26   CG    PHE D  26   CD1     0.103                       
REMARK 500    PHE D  26   CE1   PHE D  26   CZ      0.119                       
REMARK 500    PHE D  26   CZ    PHE D  26   CE2     0.118                       
REMARK 500    ASP D  28   CG    ASP D  28   OD2     0.139                       
REMARK 500    ASP D 208   CG    ASP D 208   OD1     0.211                       
REMARK 500    ASP D 208   CG    ASP D 208   OD2     0.189                       
REMARK 500    SER D 214   CB    SER D 214   OG      0.126                       
REMARK 500    LYS D 283   CD    LYS D 283   CE      0.186                       
REMARK 500    LYS D 333   CE    LYS D 333   NZ      0.156                       
REMARK 500    ARG D 335   NE    ARG D 335   CZ      0.515                       
REMARK 500    GLN D 339   CD    GLN D 339   OE1     0.157                       
REMARK 500    GLU D 420   CD    GLU D 420   OE1     0.426                       
REMARK 500    GLU D 420   CD    GLU D 420   OE2     0.199                       
REMARK 500    ARG D 428   NE    ARG D 428   CZ      0.142                       
REMARK 500    ARG D 428   CZ    ARG D 428   NH1     0.185                       
REMARK 500    ARG D 428   CZ    ARG D 428   NH2     0.092                       
REMARK 500    TYR D 431   CG    TYR D 431   CD2     0.157                       
REMARK 500    TYR D 431   CG    TYR D 431   CD1     0.155                       
REMARK 500    TYR D 431   CE1   TYR D 431   CZ      0.242                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      56 BOND DEVIATIONS.                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  17   NE  -  CZ  -  NH1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    LEU A  30   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    ASP A 206   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 208   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP A 276   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ARG A 428   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    LYS A 454   CD  -  CE  -  NZ  ANGL. DEV. = -16.6 DEGREES          
REMARK 500    LEU B 106   CA  -  CB  -  CG  ANGL. DEV. =  14.8 DEGREES          
REMARK 500    ASP B 230   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ASP B 299   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B 352   CB  -  CA  -  C   ANGL. DEV. = -13.2 DEGREES          
REMARK 500    ASP B 429   CB  -  CG  -  OD2 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ASP C  10   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP C  28   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG C  39   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ASP C  52   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ASP C 123   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG C 138   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG C 164   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP C 189   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP C 206   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ASP C 208   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP C 230   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP C 334   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG C 428   CD  -  NE  -  CZ  ANGL. DEV. = -14.9 DEGREES          
REMARK 500    ARG C 428   NE  -  CZ  -  NH1 ANGL. DEV. =  15.0 DEGREES          
REMARK 500    ARG C 428   NE  -  CZ  -  NH2 ANGL. DEV. = -15.5 DEGREES          
REMARK 500    ASP C 429   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG D  17   NH1 -  CZ  -  NH2 ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    ARG D  17   NE  -  CZ  -  NH2 ANGL. DEV. =  11.4 DEGREES          
REMARK 500    SER D 103   N   -  CA  -  CB  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    ASP D 230   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG D 335   NE  -  CZ  -  NH1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG D 335   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    ASP D 409   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    GLU D 420   OE1 -  CD  -  OE2 ANGL. DEV. =  11.1 DEGREES          
REMARK 500    GLU D 420   CG  -  CD  -  OE1 ANGL. DEV. = -14.0 DEGREES          
REMARK 500    ARG D 428   NE  -  CZ  -  NH1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG D 428   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.8 DEGREES          
REMARK 500    TYR D 431   CB  -  CG  -  CD1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    TYR D 431   CZ  -  CE2 -  CD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG D 459   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    ASP D 471   CB  -  CG  -  OD2 ANGL. DEV. =   7.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  14       26.24    -77.07                                   
REMARK 500    GLN A  15      -12.55   -140.79                                   
REMARK 500    ASP A 176       37.12    -83.17                                   
REMARK 500    VAL A 184       53.22   -147.36                                   
REMARK 500    PRO A 185     -117.89    -18.18                                   
REMARK 500    GLU A 186       55.95    -90.60                                   
REMARK 500    ALA A 209      -67.93    -28.49                                   
REMARK 500    LYS A 211      -47.07      9.00                                   
REMARK 500    ASN A 212       34.08    -87.49                                   
REMARK 500    ASN A 254      -87.12   -119.05                                   
REMARK 500    ASP A 299       75.37     60.16                                   
REMARK 500    CYS A 300     -150.03   -175.73                                   
REMARK 500    ALA A 319       63.47   -112.46                                   
REMARK 500    LYS A 323      112.09    -18.13                                   
REMARK 500    ARG A 360      -68.21   -121.34                                   
REMARK 500    ASP A 361     -112.40   -113.77                                   
REMARK 500    ARG A 382      153.96    179.77                                   
REMARK 500    ASN A 392     -145.13     46.97                                   
REMARK 500    ASP A 409       89.77    -52.10                                   
REMARK 500    ALA A 434      -77.64    -49.39                                   
REMARK 500    ALA A 435       73.72     82.26                                   
REMARK 500    PRO A 436      175.25    -52.38                                   
REMARK 500    ILE A 456       80.14     31.70                                   
REMARK 500    LEU A 460       91.26     59.53                                   
REMARK 500    GLU A 467      -12.22    -44.22                                   
REMARK 500    VAL A 469      106.41    -59.27                                   
REMARK 500    THR B  14       26.38    -73.70                                   
REMARK 500    GLN B  15      -12.71   -143.58                                   
REMARK 500    CYS B  70      102.88   -162.68                                   
REMARK 500    ASN B 169       31.43    -99.84                                   
REMARK 500    ASP B 176       46.54    -83.49                                   
REMARK 500    VAL B 184       59.00   -148.86                                   
REMARK 500    PRO B 185     -110.43    -30.77                                   
REMARK 500    PRO B 196      121.36    -39.17                                   
REMARK 500    LYS B 211      -47.70     10.48                                   
REMARK 500    ASN B 212       28.01    -78.46                                   
REMARK 500    ASN B 254      -92.15   -118.01                                   
REMARK 500    PRO B 273      143.40    -39.39                                   
REMARK 500    ASP B 299       86.58     48.31                                   
REMARK 500    CYS B 300     -154.76   -174.59                                   
REMARK 500    PRO B 315      153.16    -45.77                                   
REMARK 500    TYR B 322       39.19    -91.11                                   
REMARK 500    LYS B 323      123.39    -35.97                                   
REMARK 500    ARG B 335      -74.47    -15.83                                   
REMARK 500    ARG B 360      -69.17   -133.87                                   
REMARK 500    ASP B 361     -117.25   -116.38                                   
REMARK 500    ASN B 392     -148.75     53.81                                   
REMARK 500    ASP B 409       97.13    -55.06                                   
REMARK 500    ALA B 434      -77.25    -48.57                                   
REMARK 500    ALA B 435       73.39     76.15                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     110 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO A  318     ALA A  319                  -77.20                    
REMARK 500 PRO B  318     ALA B  319                 -126.29                    
REMARK 500 LYS B  323     VAL B  324                 -149.20                    
REMARK 500 PRO C  318     ALA C  319                 -130.14                    
REMARK 500 PRO D  318     ALA D  319                 -128.64                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG D 459         0.09    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2FRX A    1   479  UNP    P76273   YEBU_ECOLI       1    479             
DBREF  2FRX B    1   479  UNP    P76273   YEBU_ECOLI       1    479             
DBREF  2FRX C    1   479  UNP    P76273   YEBU_ECOLI       1    479             
DBREF  2FRX D    1   479  UNP    P76273   YEBU_ECOLI       1    479             
SEQADV 2FRX MSE A    1  UNP  P76273    MET     1 MODIFIED RESIDUE               
SEQADV 2FRX MSE A   16  UNP  P76273    MET    16 MODIFIED RESIDUE               
SEQADV 2FRX MSE A   20  UNP  P76273    MET    20 MODIFIED RESIDUE               
SEQADV 2FRX MSE A  105  UNP  P76273    MET   105 MODIFIED RESIDUE               
SEQADV 2FRX MSE A  122  UNP  P76273    MET   122 MODIFIED RESIDUE               
SEQADV 2FRX MSE A  139  UNP  P76273    MET   139 MODIFIED RESIDUE               
SEQADV 2FRX MSE A  187  UNP  P76273    MET   187 MODIFIED RESIDUE               
SEQADV 2FRX MSE A  411  UNP  P76273    MET   411 MODIFIED RESIDUE               
SEQADV 2FRX MSE B    1  UNP  P76273    MET     1 MODIFIED RESIDUE               
SEQADV 2FRX MSE B   16  UNP  P76273    MET    16 MODIFIED RESIDUE               
SEQADV 2FRX MSE B   20  UNP  P76273    MET    20 MODIFIED RESIDUE               
SEQADV 2FRX MSE B  105  UNP  P76273    MET   105 MODIFIED RESIDUE               
SEQADV 2FRX MSE B  122  UNP  P76273    MET   122 MODIFIED RESIDUE               
SEQADV 2FRX MSE B  139  UNP  P76273    MET   139 MODIFIED RESIDUE               
SEQADV 2FRX MSE B  187  UNP  P76273    MET   187 MODIFIED RESIDUE               
SEQADV 2FRX MSE B  411  UNP  P76273    MET   411 MODIFIED RESIDUE               
SEQADV 2FRX MSE C    1  UNP  P76273    MET     1 MODIFIED RESIDUE               
SEQADV 2FRX MSE C   16  UNP  P76273    MET    16 MODIFIED RESIDUE               
SEQADV 2FRX MSE C   20  UNP  P76273    MET    20 MODIFIED RESIDUE               
SEQADV 2FRX MSE C  105  UNP  P76273    MET   105 MODIFIED RESIDUE               
SEQADV 2FRX MSE C  122  UNP  P76273    MET   122 MODIFIED RESIDUE               
SEQADV 2FRX MSE C  139  UNP  P76273    MET   139 MODIFIED RESIDUE               
SEQADV 2FRX MSE C  187  UNP  P76273    MET   187 MODIFIED RESIDUE               
SEQADV 2FRX MSE C  411  UNP  P76273    MET   411 MODIFIED RESIDUE               
SEQADV 2FRX MSE D    1  UNP  P76273    MET     1 MODIFIED RESIDUE               
SEQADV 2FRX MSE D   16  UNP  P76273    MET    16 MODIFIED RESIDUE               
SEQADV 2FRX MSE D   20  UNP  P76273    MET    20 MODIFIED RESIDUE               
SEQADV 2FRX MSE D  105  UNP  P76273    MET   105 MODIFIED RESIDUE               
SEQADV 2FRX MSE D  122  UNP  P76273    MET   122 MODIFIED RESIDUE               
SEQADV 2FRX MSE D  139  UNP  P76273    MET   139 MODIFIED RESIDUE               
SEQADV 2FRX MSE D  187  UNP  P76273    MET   187 MODIFIED RESIDUE               
SEQADV 2FRX MSE D  411  UNP  P76273    MET   411 MODIFIED RESIDUE               
SEQRES   1 A  479  MSE ALA GLN HIS THR VAL TYR PHE PRO ASP ALA PHE LEU          
SEQRES   2 A  479  THR GLN MSE ARG GLU ALA MSE PRO SER THR LEU SER PHE          
SEQRES   3 A  479  ASP ASP PHE LEU ALA ALA CYS GLN ARG PRO LEU ARG ARG          
SEQRES   4 A  479  SER ILE ARG VAL ASN THR LEU LYS ILE SER VAL ALA ASP          
SEQRES   5 A  479  PHE LEU GLN LEU THR ALA PRO TYR GLY TRP THR LEU THR          
SEQRES   6 A  479  PRO ILE PRO TRP CYS GLU GLU GLY PHE TRP ILE GLU ARG          
SEQRES   7 A  479  ASP ASN GLU ASP ALA LEU PRO LEU GLY SER THR ALA GLU          
SEQRES   8 A  479  HIS LEU SER GLY LEU PHE TYR ILE GLN GLU ALA SER SER          
SEQRES   9 A  479  MSE LEU PRO VAL ALA ALA LEU PHE ALA ASP GLY ASN ALA          
SEQRES  10 A  479  PRO GLN ARG VAL MSE ASP VAL ALA ALA ALA PRO GLY SER          
SEQRES  11 A  479  LYS THR THR GLN ILE SER ALA ARG MSE ASN ASN GLU GLY          
SEQRES  12 A  479  ALA ILE LEU ALA ASN GLU PHE SER ALA SER ARG VAL LYS          
SEQRES  13 A  479  VAL LEU HIS ALA ASN ILE SER ARG CYS GLY ILE SER ASN          
SEQRES  14 A  479  VAL ALA LEU THR HIS PHE ASP GLY ARG VAL PHE GLY ALA          
SEQRES  15 A  479  ALA VAL PRO GLU MSE PHE ASP ALA ILE LEU LEU ASP ALA          
SEQRES  16 A  479  PRO CYS SER GLY GLU GLY VAL VAL ARG LYS ASP PRO ASP          
SEQRES  17 A  479  ALA LEU LYS ASN TRP SER PRO GLU SER ASN GLN GLU ILE          
SEQRES  18 A  479  ALA ALA THR GLN ARG GLU LEU ILE ASP SER ALA PHE HIS          
SEQRES  19 A  479  ALA LEU ARG PRO GLY GLY THR LEU VAL TYR SER THR CYS          
SEQRES  20 A  479  THR LEU ASN GLN GLU GLU ASN GLU ALA VAL CYS LEU TRP          
SEQRES  21 A  479  LEU LYS GLU THR TYR PRO ASP ALA VAL GLU PHE LEU PRO          
SEQRES  22 A  479  LEU GLY ASP LEU PHE PRO GLY ALA ASN LYS ALA LEU THR          
SEQRES  23 A  479  GLU GLU GLY PHE LEU HIS VAL PHE PRO GLN ILE TYR ASP          
SEQRES  24 A  479  CYS GLU GLY PHE PHE VAL ALA ARG LEU ARG LYS THR GLN          
SEQRES  25 A  479  ALA ILE PRO ALA LEU PRO ALA PRO LYS TYR LYS VAL GLY          
SEQRES  26 A  479  ASN PHE PRO PHE SER PRO VAL LYS ASP ARG GLU ALA GLY          
SEQRES  27 A  479  GLN ILE ARG GLN ALA ALA THR GLY VAL GLY LEU ASN TRP          
SEQRES  28 A  479  ASP GLU ASN LEU ARG LEU TRP GLN ARG ASP LYS GLU LEU          
SEQRES  29 A  479  TRP LEU PHE PRO VAL GLY ILE GLU ALA LEU ILE GLY LYS          
SEQRES  30 A  479  VAL ARG PHE SER ARG LEU GLY ILE LYS LEU ALA GLU THR          
SEQRES  31 A  479  HIS ASN LYS GLY TYR ARG TRP GLN HIS GLU ALA VAL ILE          
SEQRES  32 A  479  ALA LEU ALA SER PRO ASP ASN MSE ASN ALA PHE GLU LEU          
SEQRES  33 A  479  THR PRO GLN GLU ALA GLU GLU TRP TYR ARG GLY ARG ASP          
SEQRES  34 A  479  VAL TYR PRO GLN ALA ALA PRO VAL ALA ASP ASP VAL LEU          
SEQRES  35 A  479  VAL THR PHE GLN HIS GLN PRO ILE GLY LEU ALA LYS ARG          
SEQRES  36 A  479  ILE GLY SER ARG LEU LYS ASN SER TYR PRO ARG GLU LEU          
SEQRES  37 A  479  VAL ARG ASP GLY LYS LEU PHE THR GLY ASN ALA                  
SEQRES   1 B  479  MSE ALA GLN HIS THR VAL TYR PHE PRO ASP ALA PHE LEU          
SEQRES   2 B  479  THR GLN MSE ARG GLU ALA MSE PRO SER THR LEU SER PHE          
SEQRES   3 B  479  ASP ASP PHE LEU ALA ALA CYS GLN ARG PRO LEU ARG ARG          
SEQRES   4 B  479  SER ILE ARG VAL ASN THR LEU LYS ILE SER VAL ALA ASP          
SEQRES   5 B  479  PHE LEU GLN LEU THR ALA PRO TYR GLY TRP THR LEU THR          
SEQRES   6 B  479  PRO ILE PRO TRP CYS GLU GLU GLY PHE TRP ILE GLU ARG          
SEQRES   7 B  479  ASP ASN GLU ASP ALA LEU PRO LEU GLY SER THR ALA GLU          
SEQRES   8 B  479  HIS LEU SER GLY LEU PHE TYR ILE GLN GLU ALA SER SER          
SEQRES   9 B  479  MSE LEU PRO VAL ALA ALA LEU PHE ALA ASP GLY ASN ALA          
SEQRES  10 B  479  PRO GLN ARG VAL MSE ASP VAL ALA ALA ALA PRO GLY SER          
SEQRES  11 B  479  LYS THR THR GLN ILE SER ALA ARG MSE ASN ASN GLU GLY          
SEQRES  12 B  479  ALA ILE LEU ALA ASN GLU PHE SER ALA SER ARG VAL LYS          
SEQRES  13 B  479  VAL LEU HIS ALA ASN ILE SER ARG CYS GLY ILE SER ASN          
SEQRES  14 B  479  VAL ALA LEU THR HIS PHE ASP GLY ARG VAL PHE GLY ALA          
SEQRES  15 B  479  ALA VAL PRO GLU MSE PHE ASP ALA ILE LEU LEU ASP ALA          
SEQRES  16 B  479  PRO CYS SER GLY GLU GLY VAL VAL ARG LYS ASP PRO ASP          
SEQRES  17 B  479  ALA LEU LYS ASN TRP SER PRO GLU SER ASN GLN GLU ILE          
SEQRES  18 B  479  ALA ALA THR GLN ARG GLU LEU ILE ASP SER ALA PHE HIS          
SEQRES  19 B  479  ALA LEU ARG PRO GLY GLY THR LEU VAL TYR SER THR CYS          
SEQRES  20 B  479  THR LEU ASN GLN GLU GLU ASN GLU ALA VAL CYS LEU TRP          
SEQRES  21 B  479  LEU LYS GLU THR TYR PRO ASP ALA VAL GLU PHE LEU PRO          
SEQRES  22 B  479  LEU GLY ASP LEU PHE PRO GLY ALA ASN LYS ALA LEU THR          
SEQRES  23 B  479  GLU GLU GLY PHE LEU HIS VAL PHE PRO GLN ILE TYR ASP          
SEQRES  24 B  479  CYS GLU GLY PHE PHE VAL ALA ARG LEU ARG LYS THR GLN          
SEQRES  25 B  479  ALA ILE PRO ALA LEU PRO ALA PRO LYS TYR LYS VAL GLY          
SEQRES  26 B  479  ASN PHE PRO PHE SER PRO VAL LYS ASP ARG GLU ALA GLY          
SEQRES  27 B  479  GLN ILE ARG GLN ALA ALA THR GLY VAL GLY LEU ASN TRP          
SEQRES  28 B  479  ASP GLU ASN LEU ARG LEU TRP GLN ARG ASP LYS GLU LEU          
SEQRES  29 B  479  TRP LEU PHE PRO VAL GLY ILE GLU ALA LEU ILE GLY LYS          
SEQRES  30 B  479  VAL ARG PHE SER ARG LEU GLY ILE LYS LEU ALA GLU THR          
SEQRES  31 B  479  HIS ASN LYS GLY TYR ARG TRP GLN HIS GLU ALA VAL ILE          
SEQRES  32 B  479  ALA LEU ALA SER PRO ASP ASN MSE ASN ALA PHE GLU LEU          
SEQRES  33 B  479  THR PRO GLN GLU ALA GLU GLU TRP TYR ARG GLY ARG ASP          
SEQRES  34 B  479  VAL TYR PRO GLN ALA ALA PRO VAL ALA ASP ASP VAL LEU          
SEQRES  35 B  479  VAL THR PHE GLN HIS GLN PRO ILE GLY LEU ALA LYS ARG          
SEQRES  36 B  479  ILE GLY SER ARG LEU LYS ASN SER TYR PRO ARG GLU LEU          
SEQRES  37 B  479  VAL ARG ASP GLY LYS LEU PHE THR GLY ASN ALA                  
SEQRES   1 C  479  MSE ALA GLN HIS THR VAL TYR PHE PRO ASP ALA PHE LEU          
SEQRES   2 C  479  THR GLN MSE ARG GLU ALA MSE PRO SER THR LEU SER PHE          
SEQRES   3 C  479  ASP ASP PHE LEU ALA ALA CYS GLN ARG PRO LEU ARG ARG          
SEQRES   4 C  479  SER ILE ARG VAL ASN THR LEU LYS ILE SER VAL ALA ASP          
SEQRES   5 C  479  PHE LEU GLN LEU THR ALA PRO TYR GLY TRP THR LEU THR          
SEQRES   6 C  479  PRO ILE PRO TRP CYS GLU GLU GLY PHE TRP ILE GLU ARG          
SEQRES   7 C  479  ASP ASN GLU ASP ALA LEU PRO LEU GLY SER THR ALA GLU          
SEQRES   8 C  479  HIS LEU SER GLY LEU PHE TYR ILE GLN GLU ALA SER SER          
SEQRES   9 C  479  MSE LEU PRO VAL ALA ALA LEU PHE ALA ASP GLY ASN ALA          
SEQRES  10 C  479  PRO GLN ARG VAL MSE ASP VAL ALA ALA ALA PRO GLY SER          
SEQRES  11 C  479  LYS THR THR GLN ILE SER ALA ARG MSE ASN ASN GLU GLY          
SEQRES  12 C  479  ALA ILE LEU ALA ASN GLU PHE SER ALA SER ARG VAL LYS          
SEQRES  13 C  479  VAL LEU HIS ALA ASN ILE SER ARG CYS GLY ILE SER ASN          
SEQRES  14 C  479  VAL ALA LEU THR HIS PHE ASP GLY ARG VAL PHE GLY ALA          
SEQRES  15 C  479  ALA VAL PRO GLU MSE PHE ASP ALA ILE LEU LEU ASP ALA          
SEQRES  16 C  479  PRO CYS SER GLY GLU GLY VAL VAL ARG LYS ASP PRO ASP          
SEQRES  17 C  479  ALA LEU LYS ASN TRP SER PRO GLU SER ASN GLN GLU ILE          
SEQRES  18 C  479  ALA ALA THR GLN ARG GLU LEU ILE ASP SER ALA PHE HIS          
SEQRES  19 C  479  ALA LEU ARG PRO GLY GLY THR LEU VAL TYR SER THR CYS          
SEQRES  20 C  479  THR LEU ASN GLN GLU GLU ASN GLU ALA VAL CYS LEU TRP          
SEQRES  21 C  479  LEU LYS GLU THR TYR PRO ASP ALA VAL GLU PHE LEU PRO          
SEQRES  22 C  479  LEU GLY ASP LEU PHE PRO GLY ALA ASN LYS ALA LEU THR          
SEQRES  23 C  479  GLU GLU GLY PHE LEU HIS VAL PHE PRO GLN ILE TYR ASP          
SEQRES  24 C  479  CYS GLU GLY PHE PHE VAL ALA ARG LEU ARG LYS THR GLN          
SEQRES  25 C  479  ALA ILE PRO ALA LEU PRO ALA PRO LYS TYR LYS VAL GLY          
SEQRES  26 C  479  ASN PHE PRO PHE SER PRO VAL LYS ASP ARG GLU ALA GLY          
SEQRES  27 C  479  GLN ILE ARG GLN ALA ALA THR GLY VAL GLY LEU ASN TRP          
SEQRES  28 C  479  ASP GLU ASN LEU ARG LEU TRP GLN ARG ASP LYS GLU LEU          
SEQRES  29 C  479  TRP LEU PHE PRO VAL GLY ILE GLU ALA LEU ILE GLY LYS          
SEQRES  30 C  479  VAL ARG PHE SER ARG LEU GLY ILE LYS LEU ALA GLU THR          
SEQRES  31 C  479  HIS ASN LYS GLY TYR ARG TRP GLN HIS GLU ALA VAL ILE          
SEQRES  32 C  479  ALA LEU ALA SER PRO ASP ASN MSE ASN ALA PHE GLU LEU          
SEQRES  33 C  479  THR PRO GLN GLU ALA GLU GLU TRP TYR ARG GLY ARG ASP          
SEQRES  34 C  479  VAL TYR PRO GLN ALA ALA PRO VAL ALA ASP ASP VAL LEU          
SEQRES  35 C  479  VAL THR PHE GLN HIS GLN PRO ILE GLY LEU ALA LYS ARG          
SEQRES  36 C  479  ILE GLY SER ARG LEU LYS ASN SER TYR PRO ARG GLU LEU          
SEQRES  37 C  479  VAL ARG ASP GLY LYS LEU PHE THR GLY ASN ALA                  
SEQRES   1 D  479  MSE ALA GLN HIS THR VAL TYR PHE PRO ASP ALA PHE LEU          
SEQRES   2 D  479  THR GLN MSE ARG GLU ALA MSE PRO SER THR LEU SER PHE          
SEQRES   3 D  479  ASP ASP PHE LEU ALA ALA CYS GLN ARG PRO LEU ARG ARG          
SEQRES   4 D  479  SER ILE ARG VAL ASN THR LEU LYS ILE SER VAL ALA ASP          
SEQRES   5 D  479  PHE LEU GLN LEU THR ALA PRO TYR GLY TRP THR LEU THR          
SEQRES   6 D  479  PRO ILE PRO TRP CYS GLU GLU GLY PHE TRP ILE GLU ARG          
SEQRES   7 D  479  ASP ASN GLU ASP ALA LEU PRO LEU GLY SER THR ALA GLU          
SEQRES   8 D  479  HIS LEU SER GLY LEU PHE TYR ILE GLN GLU ALA SER SER          
SEQRES   9 D  479  MSE LEU PRO VAL ALA ALA LEU PHE ALA ASP GLY ASN ALA          
SEQRES  10 D  479  PRO GLN ARG VAL MSE ASP VAL ALA ALA ALA PRO GLY SER          
SEQRES  11 D  479  LYS THR THR GLN ILE SER ALA ARG MSE ASN ASN GLU GLY          
SEQRES  12 D  479  ALA ILE LEU ALA ASN GLU PHE SER ALA SER ARG VAL LYS          
SEQRES  13 D  479  VAL LEU HIS ALA ASN ILE SER ARG CYS GLY ILE SER ASN          
SEQRES  14 D  479  VAL ALA LEU THR HIS PHE ASP GLY ARG VAL PHE GLY ALA          
SEQRES  15 D  479  ALA VAL PRO GLU MSE PHE ASP ALA ILE LEU LEU ASP ALA          
SEQRES  16 D  479  PRO CYS SER GLY GLU GLY VAL VAL ARG LYS ASP PRO ASP          
SEQRES  17 D  479  ALA LEU LYS ASN TRP SER PRO GLU SER ASN GLN GLU ILE          
SEQRES  18 D  479  ALA ALA THR GLN ARG GLU LEU ILE ASP SER ALA PHE HIS          
SEQRES  19 D  479  ALA LEU ARG PRO GLY GLY THR LEU VAL TYR SER THR CYS          
SEQRES  20 D  479  THR LEU ASN GLN GLU GLU ASN GLU ALA VAL CYS LEU TRP          
SEQRES  21 D  479  LEU LYS GLU THR TYR PRO ASP ALA VAL GLU PHE LEU PRO          
SEQRES  22 D  479  LEU GLY ASP LEU PHE PRO GLY ALA ASN LYS ALA LEU THR          
SEQRES  23 D  479  GLU GLU GLY PHE LEU HIS VAL PHE PRO GLN ILE TYR ASP          
SEQRES  24 D  479  CYS GLU GLY PHE PHE VAL ALA ARG LEU ARG LYS THR GLN          
SEQRES  25 D  479  ALA ILE PRO ALA LEU PRO ALA PRO LYS TYR LYS VAL GLY          
SEQRES  26 D  479  ASN PHE PRO PHE SER PRO VAL LYS ASP ARG GLU ALA GLY          
SEQRES  27 D  479  GLN ILE ARG GLN ALA ALA THR GLY VAL GLY LEU ASN TRP          
SEQRES  28 D  479  ASP GLU ASN LEU ARG LEU TRP GLN ARG ASP LYS GLU LEU          
SEQRES  29 D  479  TRP LEU PHE PRO VAL GLY ILE GLU ALA LEU ILE GLY LYS          
SEQRES  30 D  479  VAL ARG PHE SER ARG LEU GLY ILE LYS LEU ALA GLU THR          
SEQRES  31 D  479  HIS ASN LYS GLY TYR ARG TRP GLN HIS GLU ALA VAL ILE          
SEQRES  32 D  479  ALA LEU ALA SER PRO ASP ASN MSE ASN ALA PHE GLU LEU          
SEQRES  33 D  479  THR PRO GLN GLU ALA GLU GLU TRP TYR ARG GLY ARG ASP          
SEQRES  34 D  479  VAL TYR PRO GLN ALA ALA PRO VAL ALA ASP ASP VAL LEU          
SEQRES  35 D  479  VAL THR PHE GLN HIS GLN PRO ILE GLY LEU ALA LYS ARG          
SEQRES  36 D  479  ILE GLY SER ARG LEU LYS ASN SER TYR PRO ARG GLU LEU          
SEQRES  37 D  479  VAL ARG ASP GLY LYS LEU PHE THR GLY ASN ALA                  
MODRES 2FRX MSE A   16  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE A   20  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE A  105  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE A  122  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE A  139  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE A  187  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE A  411  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE B   16  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE B   20  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE B  105  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE B  122  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE B  139  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE B  187  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE B  411  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE C   16  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE C   20  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE C  105  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE C  122  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE C  139  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE C  187  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE C  411  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE D   16  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE D   20  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE D  105  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE D  122  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE D  139  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE D  187  MET  SELENOMETHIONINE                                   
MODRES 2FRX MSE D  411  MET  SELENOMETHIONINE                                   
HET    MSE  A  16       8                                                       
HET    MSE  A  20       8                                                       
HET    MSE  A 105       8                                                       
HET    MSE  A 122       8                                                       
HET    MSE  A 139       8                                                       
HET    MSE  A 187       8                                                       
HET    MSE  A 411       8                                                       
HET    MSE  B  16       8                                                       
HET    MSE  B  20       8                                                       
HET    MSE  B 105       8                                                       
HET    MSE  B 122       8                                                       
HET    MSE  B 139       8                                                       
HET    MSE  B 187       8                                                       
HET    MSE  B 411       8                                                       
HET    MSE  C  16       8                                                       
HET    MSE  C  20       8                                                       
HET    MSE  C 105       8                                                       
HET    MSE  C 122       8                                                       
HET    MSE  C 139       8                                                       
HET    MSE  C 187       8                                                       
HET    MSE  C 411       8                                                       
HET    MSE  D  16       8                                                       
HET    MSE  D  20       8                                                       
HET    MSE  D 105       8                                                       
HET    MSE  D 122       8                                                       
HET    MSE  D 139       8                                                       
HET    MSE  D 187       8                                                       
HET    MSE  D 411       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    28(C5 H11 N O2 SE)                                           
HELIX    1   1 PRO A    9  ARG A   17  1                                   9    
HELIX    2   2 GLU A   18  MSE A   20  5                                   3    
HELIX    3   3 PHE A   26  GLN A   34  1                                   9    
HELIX    4   4 SER A   49  ALA A   58  1                                  10    
HELIX    5   5 PRO A   59  GLY A   61  5                                   3    
HELIX    6   6 PRO A   85  SER A   88  5                                   4    
HELIX    7   7 THR A   89  SER A   94  1                                   6    
HELIX    8   8 GLU A  101  PHE A  112  1                                  12    
HELIX    9   9 GLY A  129  MSE A  139  1                                  11    
HELIX   10  10 SER A  151  GLY A  166  1                                  16    
HELIX   11  11 VAL A  179  VAL A  184  1                                   6    
HELIX   12  12 GLY A  199  LYS A  205  5                                   7    
HELIX   13  13 SER A  214  ALA A  235  1                                  22    
HELIX   14  14 ASN A  254  TYR A  265  1                                  12    
HELIX   15  15 GLY A  280  LEU A  285  5                                   6    
HELIX   16  16 LYS A  333  GLY A  346  1                                  14    
HELIX   17  17 GLY A  370  ILE A  375  5                                   6    
HELIX   18  18 GLN A  398  ALA A  406  1                                   9    
HELIX   19  19 THR A  417  ARG A  426  1                                  10    
HELIX   20  20 PRO A  465  VAL A  469  5                                   5    
HELIX   21  21 PRO B    9  ARG B   17  1                                   9    
HELIX   22  22 GLU B   18  MSE B   20  5                                   3    
HELIX   23  23 PHE B   26  GLN B   34  1                                   9    
HELIX   24  24 SER B   49  ALA B   58  1                                  10    
HELIX   25  25 PRO B   59  GLY B   61  5                                   3    
HELIX   26  26 PRO B   85  SER B   88  5                                   4    
HELIX   27  27 THR B   89  SER B   94  1                                   6    
HELIX   28  28 GLU B  101  PHE B  112  1                                  12    
HELIX   29  29 GLY B  129  MSE B  139  1                                  11    
HELIX   30  30 SER B  151  CYS B  165  1                                  15    
HELIX   31  31 VAL B  179  VAL B  184  1                                   6    
HELIX   32  32 GLY B  199  LYS B  205  5                                   7    
HELIX   33  33 SER B  214  ALA B  235  1                                  22    
HELIX   34  34 ASN B  254  TYR B  265  1                                  12    
HELIX   35  35 GLY B  280  LEU B  285  5                                   6    
HELIX   36  36 LYS B  333  GLY B  346  1                                  14    
HELIX   37  37 GLY B  370  ILE B  375  5                                   6    
HELIX   38  38 GLN B  398  ALA B  406  1                                   9    
HELIX   39  39 THR B  417  ARG B  426  1                                  10    
HELIX   40  40 PRO B  465  VAL B  469  5                                   5    
HELIX   41  41 PRO C    9  ARG C   17  1                                   9    
HELIX   42  42 GLU C   18  MSE C   20  5                                   3    
HELIX   43  43 PHE C   26  GLN C   34  1                                   9    
HELIX   44  44 SER C   49  ALA C   58  1                                  10    
HELIX   45  45 PRO C   59  GLY C   61  5                                   3    
HELIX   46  46 PRO C   85  SER C   88  5                                   4    
HELIX   47  47 THR C   89  SER C   94  1                                   6    
HELIX   48  48 GLU C  101  PHE C  112  1                                  12    
HELIX   49  49 GLY C  129  MSE C  139  1                                  11    
HELIX   50  50 SER C  151  CYS C  165  1                                  15    
HELIX   51  51 VAL C  179  VAL C  184  1                                   6    
HELIX   52  52 GLY C  199  LYS C  205  5                                   7    
HELIX   53  53 SER C  214  ALA C  235  1                                  22    
HELIX   54  54 ASN C  254  TYR C  265  1                                  12    
HELIX   55  55 GLY C  280  LEU C  285  5                                   6    
HELIX   56  56 LYS C  333  GLY C  346  1                                  14    
HELIX   57  57 VAL C  369  ALA C  373  1                                   5    
HELIX   58  58 GLN C  398  ALA C  406  1                                   9    
HELIX   59  59 THR C  417  ARG C  426  1                                  10    
HELIX   60  60 PRO C  465  VAL C  469  5                                   5    
HELIX   61  61 PRO D    9  ARG D   17  1                                   9    
HELIX   62  62 PHE D   26  GLN D   34  1                                   9    
HELIX   63  63 SER D   49  ALA D   58  1                                  10    
HELIX   64  64 PRO D   59  GLY D   61  5                                   3    
HELIX   65  65 PRO D   85  SER D   88  5                                   4    
HELIX   66  66 THR D   89  SER D   94  1                                   6    
HELIX   67  67 GLU D  101  ALA D  113  1                                  13    
HELIX   68  68 GLY D  129  MSE D  139  1                                  11    
HELIX   69  69 SER D  151  GLY D  166  1                                  16    
HELIX   70  70 VAL D  179  VAL D  184  1                                   6    
HELIX   71  71 GLY D  199  LYS D  205  5                                   7    
HELIX   72  72 SER D  214  ALA D  235  1                                  22    
HELIX   73  73 ASN D  254  TYR D  265  1                                  12    
HELIX   74  74 GLY D  280  LEU D  285  5                                   6    
HELIX   75  75 LYS D  333  GLY D  346  1                                  14    
HELIX   76  76 GLY D  370  ILE D  375  5                                   6    
HELIX   77  77 GLN D  398  ALA D  406  1                                   9    
HELIX   78  78 THR D  417  ARG D  426  1                                  10    
HELIX   79  79 PRO D  465  VAL D  469  5                                   5    
SHEET    1   A 4 PRO A  66  ILE A  67  0                                        
SHEET    2   A 4 CYS A  70  PHE A  74 -1  O  GLY A  73   N  ILE A  67           
SHEET    3   A 4 ILE A  41  VAL A  43 -1  N  ILE A  41   O  PHE A  74           
SHEET    4   A 4 PHE A  97  ILE A  99 -1  O  TYR A  98   N  ARG A  42           
SHEET    1   B 3 VAL A 269  PHE A 271  0                                        
SHEET    2   B 3 PHE A 303  LYS A 310 -1  O  ARG A 309   N  GLU A 270           
SHEET    3   B 3 LEU A 291  VAL A 293 -1  N  VAL A 293   O  PHE A 303           
SHEET    1   C 8 VAL A 269  PHE A 271  0                                        
SHEET    2   C 8 PHE A 303  LYS A 310 -1  O  ARG A 309   N  GLU A 270           
SHEET    3   C 8 LEU A 236  THR A 246 -1  N  GLY A 239   O  LYS A 310           
SHEET    4   C 8 PHE A 188  ASP A 194  1  N  LEU A 193   O  VAL A 243           
SHEET    5   C 8 ARG A 120  ASP A 123  1  N  MSE A 122   O  LEU A 192           
SHEET    6   C 8 ALA A 144  ASN A 148  1  O  LEU A 146   N  ASP A 123           
SHEET    7   C 8 VAL A 170  THR A 173  1  O  ALA A 171   N  ALA A 147           
SHEET    8   C 8 ARG A 382  LEU A 383 -1  O  ARG A 382   N  LEU A 172           
SHEET    1   D 5 SER A 330  PRO A 331  0                                        
SHEET    2   D 5 LEU A 355  GLN A 359 -1  O  GLN A 359   N  SER A 330           
SHEET    3   D 5 GLU A 363  PRO A 368 -1  O  TRP A 365   N  TRP A 358           
SHEET    4   D 5 ILE A 385  HIS A 391 -1  O  ALA A 388   N  LEU A 364           
SHEET    5   D 5 GLY A 394  TRP A 397 -1  O  ARG A 396   N  GLU A 389           
SHEET    1   E 3 ALA A 413  GLU A 415  0                                        
SHEET    2   E 3 ASP A 440  PHE A 445  1  O  THR A 444   N  PHE A 414           
SHEET    3   E 3 GLN A 448  LYS A 454 -1  O  ALA A 453   N  VAL A 441           
SHEET    1   F 4 PRO B  66  ILE B  67  0                                        
SHEET    2   F 4 CYS B  70  PHE B  74 -1  O  GLY B  73   N  ILE B  67           
SHEET    3   F 4 ILE B  41  VAL B  43 -1  N  ILE B  41   O  PHE B  74           
SHEET    4   F 4 PHE B  97  ILE B  99 -1  O  TYR B  98   N  ARG B  42           
SHEET    1   G 3 VAL B 269  PHE B 271  0                                        
SHEET    2   G 3 PHE B 303  LYS B 310 -1  O  ARG B 309   N  GLU B 270           
SHEET    3   G 3 LEU B 291  VAL B 293 -1  N  VAL B 293   O  PHE B 303           
SHEET    1   H 8 VAL B 269  PHE B 271  0                                        
SHEET    2   H 8 PHE B 303  LYS B 310 -1  O  ARG B 309   N  GLU B 270           
SHEET    3   H 8 LEU B 236  THR B 246 -1  N  TYR B 244   O  ALA B 306           
SHEET    4   H 8 PHE B 188  ASP B 194  1  N  LEU B 193   O  VAL B 243           
SHEET    5   H 8 ARG B 120  ASP B 123  1  N  MSE B 122   O  LEU B 192           
SHEET    6   H 8 ALA B 144  ASN B 148  1  O  LEU B 146   N  ASP B 123           
SHEET    7   H 8 VAL B 170  THR B 173  1  O  ALA B 171   N  ILE B 145           
SHEET    8   H 8 ARG B 382  LEU B 383 -1  O  ARG B 382   N  LEU B 172           
SHEET    1   I 5 SER B 330  PRO B 331  0                                        
SHEET    2   I 5 LEU B 355  GLN B 359 -1  O  GLN B 359   N  SER B 330           
SHEET    3   I 5 GLU B 363  PRO B 368 -1  O  TRP B 365   N  TRP B 358           
SHEET    4   I 5 ILE B 385  HIS B 391 -1  O  LEU B 387   N  LEU B 364           
SHEET    5   I 5 GLY B 394  TRP B 397 -1  O  ARG B 396   N  GLU B 389           
SHEET    1   J 3 ALA B 413  GLU B 415  0                                        
SHEET    2   J 3 ASP B 440  PHE B 445  1  O  THR B 444   N  PHE B 414           
SHEET    3   J 3 GLN B 448  LYS B 454 -1  O  ALA B 453   N  VAL B 441           
SHEET    1   K 4 PRO C  66  ILE C  67  0                                        
SHEET    2   K 4 CYS C  70  PHE C  74 -1  O  GLY C  73   N  ILE C  67           
SHEET    3   K 4 ILE C  41  VAL C  43 -1  N  ILE C  41   O  PHE C  74           
SHEET    4   K 4 PHE C  97  ILE C  99 -1  O  TYR C  98   N  ARG C  42           
SHEET    1   L 3 VAL C 269  PHE C 271  0                                        
SHEET    2   L 3 PHE C 303  LYS C 310 -1  O  ARG C 309   N  GLU C 270           
SHEET    3   L 3 LEU C 291  VAL C 293 -1  N  VAL C 293   O  PHE C 303           
SHEET    1   M 8 VAL C 269  PHE C 271  0                                        
SHEET    2   M 8 PHE C 303  LYS C 310 -1  O  ARG C 309   N  GLU C 270           
SHEET    3   M 8 LEU C 236  THR C 246 -1  N  GLY C 239   O  LYS C 310           
SHEET    4   M 8 PHE C 188  ASP C 194  1  N  ILE C 191   O  VAL C 243           
SHEET    5   M 8 ARG C 120  ASP C 123  1  N  MSE C 122   O  LEU C 192           
SHEET    6   M 8 ALA C 144  ASN C 148  1  O  LEU C 146   N  ASP C 123           
SHEET    7   M 8 VAL C 170  THR C 173  1  O  ALA C 171   N  ALA C 147           
SHEET    8   M 8 ARG C 382  LEU C 383 -1  O  ARG C 382   N  LEU C 172           
SHEET    1   N 5 SER C 330  PRO C 331  0                                        
SHEET    2   N 5 LEU C 355  GLN C 359 -1  O  GLN C 359   N  SER C 330           
SHEET    3   N 5 GLU C 363  PRO C 368 -1  O  TRP C 365   N  TRP C 358           
SHEET    4   N 5 ILE C 385  HIS C 391 -1  O  LEU C 387   N  LEU C 364           
SHEET    5   N 5 GLY C 394  TRP C 397 -1  O  ARG C 396   N  GLU C 389           
SHEET    1   O 3 ALA C 413  GLU C 415  0                                        
SHEET    2   O 3 ASP C 440  THR C 444  1  O  THR C 444   N  PHE C 414           
SHEET    3   O 3 PRO C 449  LYS C 454 -1  O  ILE C 450   N  VAL C 443           
SHEET    1   P 4 PRO D  66  ILE D  67  0                                        
SHEET    2   P 4 CYS D  70  PHE D  74 -1  O  GLY D  73   N  ILE D  67           
SHEET    3   P 4 ILE D  41  VAL D  43 -1  N  ILE D  41   O  PHE D  74           
SHEET    4   P 4 PHE D  97  ILE D  99 -1  O  TYR D  98   N  ARG D  42           
SHEET    1   Q 3 VAL D 269  PHE D 271  0                                        
SHEET    2   Q 3 PHE D 303  LYS D 310 -1  O  ARG D 309   N  GLU D 270           
SHEET    3   Q 3 LEU D 291  VAL D 293 -1  N  VAL D 293   O  PHE D 303           
SHEET    1   R 8 VAL D 269  PHE D 271  0                                        
SHEET    2   R 8 PHE D 303  LYS D 310 -1  O  ARG D 309   N  GLU D 270           
SHEET    3   R 8 LEU D 236  THR D 246 -1  N  GLY D 239   O  LYS D 310           
SHEET    4   R 8 PHE D 188  ASP D 194  1  N  LEU D 193   O  VAL D 243           
SHEET    5   R 8 ARG D 120  ASP D 123  1  N  MSE D 122   O  LEU D 192           
SHEET    6   R 8 ALA D 144  ASN D 148  1  O  LEU D 146   N  ASP D 123           
SHEET    7   R 8 VAL D 170  THR D 173  1  O  ALA D 171   N  ALA D 147           
SHEET    8   R 8 ARG D 382  LEU D 383 -1  O  ARG D 382   N  LEU D 172           
SHEET    1   S 5 SER D 330  PRO D 331  0                                        
SHEET    2   S 5 LEU D 355  GLN D 359 -1  O  GLN D 359   N  SER D 330           
SHEET    3   S 5 GLU D 363  PRO D 368 -1  O  TRP D 365   N  TRP D 358           
SHEET    4   S 5 ILE D 385  HIS D 391 -1  O  ALA D 388   N  LEU D 364           
SHEET    5   S 5 GLY D 394  TRP D 397 -1  O  ARG D 396   N  GLU D 389           
SHEET    1   T 3 ALA D 413  GLU D 415  0                                        
SHEET    2   T 3 VAL D 441  THR D 444  1  O  THR D 444   N  PHE D 414           
SHEET    3   T 3 PRO D 449  ALA D 453 -1  O  ILE D 450   N  VAL D 443           
LINK         C   GLN A  15                 N   MSE A  16     1555   1555  1.34  
LINK         C   MSE A  16                 N   ARG A  17     1555   1555  1.34  
LINK         C   ALA A  19                 N   MSE A  20     1555   1555  1.33  
LINK         C   MSE A  20                 N   PRO A  21     1555   1555  1.34  
LINK         C   SER A 104                 N   MSE A 105     1555   1555  1.33  
LINK         C   MSE A 105                 N   LEU A 106     1555   1555  1.32  
LINK         C   VAL A 121                 N   MSE A 122     1555   1555  1.33  
LINK         C   MSE A 122                 N   ASP A 123     1555   1555  1.33  
LINK         C   ARG A 138                 N   MSE A 139     1555   1555  1.32  
LINK         C   MSE A 139                 N   ASN A 140     1555   1555  1.32  
LINK         C   GLU A 186                 N   MSE A 187     1555   1555  1.33  
LINK         C   MSE A 187                 N   PHE A 188     1555   1555  1.32  
LINK         C   ASN A 410                 N   MSE A 411     1555   1555  1.33  
LINK         C   MSE A 411                 N   ASN A 412     1555   1555  1.34  
LINK         C   GLN B  15                 N   MSE B  16     1555   1555  1.34  
LINK         C   MSE B  16                 N   ARG B  17     1555   1555  1.34  
LINK         C   ALA B  19                 N   MSE B  20     1555   1555  1.34  
LINK         C   MSE B  20                 N   PRO B  21     1555   1555  1.35  
LINK         C   SER B 104                 N   MSE B 105     1555   1555  1.32  
LINK         C   MSE B 105                 N   LEU B 106     1555   1555  1.32  
LINK         C   VAL B 121                 N   MSE B 122     1555   1555  1.34  
LINK         C   MSE B 122                 N   ASP B 123     1555   1555  1.33  
LINK         C   ARG B 138                 N   MSE B 139     1555   1555  1.32  
LINK         C   MSE B 139                 N   ASN B 140     1555   1555  1.33  
LINK         C   GLU B 186                 N   MSE B 187     1555   1555  1.32  
LINK         C   MSE B 187                 N   PHE B 188     1555   1555  1.31  
LINK         C   ASN B 410                 N   MSE B 411     1555   1555  1.33  
LINK         C   MSE B 411                 N   ASN B 412     1555   1555  1.34  
LINK         C   GLN C  15                 N   MSE C  16     1555   1555  1.34  
LINK         C   MSE C  16                 N   ARG C  17     1555   1555  1.34  
LINK         C   ALA C  19                 N   MSE C  20     1555   1555  1.34  
LINK         C   MSE C  20                 N   PRO C  21     1555   1555  1.33  
LINK         C   SER C 104                 N   MSE C 105     1555   1555  1.33  
LINK         C   MSE C 105                 N   LEU C 106     1555   1555  1.34  
LINK         C   VAL C 121                 N   MSE C 122     1555   1555  1.34  
LINK         C   MSE C 122                 N   ASP C 123     1555   1555  1.33  
LINK         C   ARG C 138                 N   MSE C 139     1555   1555  1.33  
LINK         C   MSE C 139                 N   ASN C 140     1555   1555  1.33  
LINK         C   GLU C 186                 N   MSE C 187     1555   1555  1.32  
LINK         C   MSE C 187                 N   PHE C 188     1555   1555  1.33  
LINK         C   ASN C 410                 N   MSE C 411     1555   1555  1.33  
LINK         C   MSE C 411                 N   ASN C 412     1555   1555  1.33  
LINK         C   GLN D  15                 N   MSE D  16     1555   1555  1.34  
LINK         C   MSE D  16                 N   ARG D  17     1555   1555  1.34  
LINK         C   ALA D  19                 N   MSE D  20     1555   1555  1.34  
LINK         C   MSE D  20                 N   PRO D  21     1555   1555  1.34  
LINK         C   SER D 104                 N   MSE D 105     1555   1555  1.34  
LINK         C   MSE D 105                 N   LEU D 106     1555   1555  1.33  
LINK         C   VAL D 121                 N   MSE D 122     1555   1555  1.32  
LINK         C   MSE D 122                 N   ASP D 123     1555   1555  1.33  
LINK         C   ARG D 138                 N   MSE D 139     1555   1555  1.32  
LINK         C   MSE D 139                 N   ASN D 140     1555   1555  1.33  
LINK         C   GLU D 186                 N   MSE D 187     1555   1555  1.32  
LINK         C   MSE D 187                 N   PHE D 188     1555   1555  1.31  
LINK         C   ASN D 410                 N   MSE D 411     1555   1555  1.33  
LINK         C   MSE D 411                 N   ASN D 412     1555   1555  1.33  
CISPEP   1 ALA A  127    PRO A  128          0         5.26                     
CISPEP   2 ALA B  127    PRO B  128          0         1.89                     
CISPEP   3 ALA C  127    PRO C  128          0        -0.85                     
CISPEP   4 ALA D  127    PRO D  128          0         3.05                     
CRYST1   67.706   87.126   95.048  88.33  76.79  90.19 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014770  0.000049 -0.003470        0.00000                         
SCALE2      0.000000  0.011478 -0.000353        0.00000                         
SCALE3      0.000000  0.000000  0.010812        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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