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Database: PDB
Entry: 2ID0
LinkDB: 2ID0
Original site: 2ID0 
HEADER    HYDROLASE                               13-SEP-06   2ID0              
TITLE     ESCHERICHIA COLI RNASE II                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EXORIBONUCLEASE 2;                                         
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: EXORIBONUCLEASE II, RIBONUCLEASE II, RNASE II;              
COMPND   5 EC: 3.1.13.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: RNB;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    RNASE, EXORIBONUCLEASE, RIBONUCLEASE, EXONUCLEASE, NUCLEASE,          
KEYWDS   2 HYDROLYASE, MRNA DECAY, RNR FAMILY, HYDROLASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZUO,J.ZHANG,Y.WANG,A.MALHOTRA                                       
REVDAT   5   18-OCT-17 2ID0    1       REMARK                                   
REVDAT   4   13-JUL-11 2ID0    1       VERSN                                    
REVDAT   3   24-FEB-09 2ID0    1       VERSN                                    
REVDAT   2   17-OCT-06 2ID0    1       JRNL                                     
REVDAT   1   03-OCT-06 2ID0    0                                                
JRNL        AUTH   Y.ZUO,H.A.VINCENT,J.ZHANG,Y.WANG,M.P.DEUTSCHER,A.MALHOTRA    
JRNL        TITL   STRUCTURAL BASIS FOR PROCESSIVITY AND SINGLE-STRAND          
JRNL        TITL 2 SPECIFICITY OF RNASE II.                                     
JRNL        REF    MOL.CELL                      V.  24   149 2006              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   16996291                                                     
JRNL        DOI    10.1016/J.MOLCEL.2006.09.004                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 17.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 82.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 100806                         
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) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5045                            
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) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.41                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4151                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 48.70                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 181                          
REMARK   3   BIN FREE R VALUE                    : 0.3350                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 19529                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 287                                     
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) : 54.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.29000                                             
REMARK   3    B22 (A**2) : -0.30000                                             
REMARK   3    B33 (A**2) : 0.16000                                              
REMARK   3    B12 (A**2) : -0.16000                                             
REMARK   3    B13 (A**2) : -0.24000                                             
REMARK   3    B23 (A**2) : -0.59000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.586         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.311         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.240         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.628        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
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): 19935 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 27089 ; 1.564 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2536 ; 6.405 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   887 ;35.222 ;23.224       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3220 ;17.610 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   173 ;21.067 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3084 ; 0.097 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 15214 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  8681 ; 0.232 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 13396 ; 0.311 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   769 ; 0.173 ; 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):   145 ; 0.216 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.181 ; 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): 12993 ; 1.021 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 20284 ; 1.565 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7786 ; 2.415 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6805 ; 3.683 ; 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 : NULL                              
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     5        A   644                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.1470  56.7912  72.0626              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1449 T22:   0.0800                                     
REMARK   3      T33:  -0.1159 T12:   0.0932                                     
REMARK   3      T13:  -0.0240 T23:  -0.0566                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6703 L22:   1.7549                                     
REMARK   3      L33:   0.5331 L12:  -0.2676                                     
REMARK   3      L13:  -0.7886 L23:  -0.1588                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0184 S12:  -0.6514 S13:   0.2419                       
REMARK   3      S21:   0.7780 S22:   0.1346 S23:   0.0042                       
REMARK   3      S31:   0.0340 S32:   0.2905 S33:  -0.1162                       
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     5        B   644                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.0849  28.4806  14.2179              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0435 T22:  -0.0766                                     
REMARK   3      T33:  -0.1714 T12:   0.0041                                     
REMARK   3      T13:  -0.0145 T23:  -0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5422 L22:   0.9031                                     
REMARK   3      L33:   0.5286 L12:   0.0241                                     
REMARK   3      L13:   0.1315 L23:  -0.1350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0172 S12:   0.4559 S13:  -0.2096                       
REMARK   3      S21:  -0.4773 S22:   0.0150 S23:   0.1170                       
REMARK   3      S31:   0.1063 S32:   0.0568 S33:   0.0022                       
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     5        C   644                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.3549  -0.0445  73.7113              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1419 T22:  -0.1411                                     
REMARK   3      T33:  -0.2128 T12:   0.0112                                     
REMARK   3      T13:   0.0098 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3038 L22:   0.5072                                     
REMARK   3      L33:   0.9264 L12:  -0.0800                                     
REMARK   3      L13:  -0.1185 L23:   0.0388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0592 S12:  -0.3029 S13:   0.1039                       
REMARK   3      S21:   0.2604 S22:  -0.0070 S23:   0.0499                       
REMARK   3      S31:  -0.0874 S32:   0.0686 S33:  -0.0522                       
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     5        D   644                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.2289  89.1888  16.4794              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1408 T22:  -0.0254                                     
REMARK   3      T33:  -0.1433 T12:  -0.0181                                     
REMARK   3      T13:  -0.0092 T23:  -0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4980 L22:   1.7748                                     
REMARK   3      L33:   0.5296 L12:   0.3566                                     
REMARK   3      L13:   0.3875 L23:   0.2282                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0400 S12:   0.5294 S13:  -0.0844                       
REMARK   3      S21:  -0.8807 S22:   0.1263 S23:   0.0909                       
REMARK   3      S31:  -0.1862 S32:   0.1217 S33:  -0.0863                       
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 2ID0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-SEP-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000039429.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-NOV-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 8-BM                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9790                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 117653                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.340                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 17.950                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.7                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 69.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SNB                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25.5% PEG 2000 MME, 0.36 M MGCL2, 0.5    
REMARK 280  MM MNCL2, 5 MM DTT, 2 MM 3',5'-ADP, 0.1 M TRIS-CL, PH 7.5, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
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     PHE A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     GLU A   518                                                      
REMARK 465     THR A   519                                                      
REMARK 465     ALA A   520                                                      
REMARK 465     THR A   521                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     PHE B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     GLU B   518                                                      
REMARK 465     THR B   519                                                      
REMARK 465     ALA B   520                                                      
REMARK 465     THR B   521                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     PHE C     2                                                      
REMARK 465     GLN C     3                                                      
REMARK 465     ASP C     4                                                      
REMARK 465     GLU C   518                                                      
REMARK 465     THR C   519                                                      
REMARK 465     ALA C   520                                                      
REMARK 465     THR C   521                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     PHE D     2                                                      
REMARK 465     GLN D     3                                                      
REMARK 465     ASP D     4                                                      
REMARK 465     GLU D   518                                                      
REMARK 465     THR D   519                                                      
REMARK 465     ALA D   520                                                      
REMARK 465     THR D   521                                                      
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     LYS A  27    CG   CD   CE   NZ                                   
REMARK 470     GLU A  69    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 116    CD   NE   CZ   NH1  NH2                             
REMARK 470     THR A 180    OG1  CG2                                            
REMARK 470     GLU A 181    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 185    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 189    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 196    CG   OD1  OD2                                       
REMARK 470     ASP A 207    CG   OD1  OD2                                       
REMARK 470     LYS A 243    CG   CD   CE   NZ                                   
REMARK 470     LYS A 246    CG   CD   CE   NZ                                   
REMARK 470     ARG A 264    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 265    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 268    CG   OD1  OD2                                       
REMARK 470     ASP A 269    CG   OD1  OD2                                       
REMARK 470     ASN A 276    CG   OD1  ND2                                       
REMARK 470     GLU A 277    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 295    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 296    CG   OD1  OD2                                       
REMARK 470     GLU A 299    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 306    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 310    CG   CD   CE   NZ                                   
REMARK 470     GLU A 321    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 322    CG   OD1  ND2                                       
REMARK 470     GLU A 331    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 335    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 339    CG   CD1  CD2                                       
REMARK 470     ARG A 346    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 349    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 360    CG   OD1  OD2                                       
REMARK 470     GLU A 380    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 382    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 390    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 420    CG   OD1  OD2                                       
REMARK 470     LYS A 432    CG   CD   CE   NZ                                   
REMARK 470     ASP A 447    CG   OD1  OD2                                       
REMARK 470     LYS A 451    CG   CD   CE                                        
REMARK 470     ARG A 454    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 459    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 464    CG   CD1  CD2                                       
REMARK 470     ARG A 469    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 480    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 489    CG   CD1  CD2                                       
REMARK 470     GLU A 490    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 516    CG   CD   CE   NZ                                   
REMARK 470     ARG A 522    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 524    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 526    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 573    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 606    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  69    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  95    CG   OD1  OD2                                       
REMARK 470     GLU B 121    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 123    CG   CD   CE   NZ                                   
REMARK 470     GLU B 181    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 206    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 215    CG   CD   CE   NZ                                   
REMARK 470     ASP B 220    CG   OD1  OD2                                       
REMARK 470     LYS B 240    CG   CD   CE   NZ                                   
REMARK 470     LYS B 243    CG   CD   CE   NZ                                   
REMARK 470     LYS B 246    CG   CD   CE   NZ                                   
REMARK 470     ARG B 264    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 299    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 306    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 321    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 322    CG   OD1  ND2                                       
REMARK 470     GLU B 370    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 407    CG   CD   CE   NZ                                   
REMARK 470     LYS B 432    CG   CD   CE   NZ                                   
REMARK 470     ASP B 439    CG   OD1  OD2                                       
REMARK 470     GLU B 480    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 516    CG   CD   CE   NZ                                   
REMARK 470     ARG B 522    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 526    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 573    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C  41    CG   CD   OE1  NE2                                  
REMARK 470     GLU C  67    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  69    CG   CD   OE1  OE2                                  
REMARK 470     ASP C  95    CG   OD1  OD2                                       
REMARK 470     GLU C 121    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 155    CG   OD1  OD2                                       
REMARK 470     GLU C 181    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 240    CG   CD   CE   NZ                                   
REMARK 470     GLU C 265    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 269    CG   OD1  OD2                                       
REMARK 470     GLU C 306    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 310    CG   CD   CE   NZ                                   
REMARK 470     GLU C 321    CG   CD   OE1  OE2                                  
REMARK 470     ASN C 322    CG   OD1  ND2                                       
REMARK 470     GLU C 335    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 338    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 349    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 361    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 365    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 382    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 407    CG   CD   CE   NZ                                   
REMARK 470     GLU C 441    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 447    CG   OD1  OD2                                       
REMARK 470     LYS C 451    CG   CD   CE   NZ                                   
REMARK 470     ARG C 522    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 526    CG   CD   OE1  OE2                                  
REMARK 470     GLN D  18    CG   CD   OE1  NE2                                  
REMARK 470     GLU D  30    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  31    CG   CD   CE   NZ                                   
REMARK 470     ASP D  39    CG   OD1  OD2                                       
REMARK 470     GLN D  41    CG   CD   OE1  NE2                                  
REMARK 470     GLU D  67    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  68    CG   CD   CE   NZ                                   
REMARK 470     GLU D  69    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  80    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  96    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN D 119    CG   OD1  ND2                                       
REMARK 470     GLU D 124    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 141    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 181    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 184    CG   OD1  OD2                                       
REMARK 470     GLU D 185    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 190    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 206    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 207    CG   OD1  OD2                                       
REMARK 470     LYS D 215    CG   CD   CE   NZ                                   
REMARK 470     ASP D 219    CG   OD1  OD2                                       
REMARK 470     ASP D 220    CG   OD1  OD2                                       
REMARK 470     LYS D 246    CG   CD   CE   NZ                                   
REMARK 470     ARG D 264    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 268    CG   OD1  OD2                                       
REMARK 470     ASP D 269    CG   OD1  OD2                                       
REMARK 470     ARG D 274    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 299    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 306    CG   CD   OE1  OE2                                  
REMARK 470     ASN D 322    CG   OD1  ND2                                       
REMARK 470     GLU D 335    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 359    CG   CD   CE   NZ                                   
REMARK 470     ARG D 361    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 380    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 387    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 405    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 432    CG   CD   CE   NZ                                   
REMARK 470     GLU D 441    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 447    CG   OD1  OD2                                       
REMARK 470     LYS D 451    CG   CD   CE   NZ                                   
REMARK 470     GLN D 459    CG   CD   OE1  NE2                                  
REMARK 470     PHE D 474    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU D 476    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 480    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 516    CG   CD   CE   NZ                                   
REMARK 470     ARG D 522    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN D 524    CG   CD   OE1  NE2                                  
REMARK 470     ASP D 525    CG   OD1  OD2                                       
REMARK 470     GLU D 526    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 539    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 573    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   OD2  ASP B   582     O    HOH B  1044              1.96            
REMARK 500   O    ALA A   115     O    HOH A  1051              1.99            
REMARK 500   OD1  ASP C   561     O    HOH C  1048              2.15            
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    VAL A 188   C     VAL A 188   O       0.116                       
REMARK 500    ARG A 285   CZ    ARG A 285   NH1     0.210                       
REMARK 500    ARG A 285   CZ    ARG A 285   NH2     0.091                       
REMARK 500    PHE A 301   CG    PHE A 301   CD2     0.104                       
REMARK 500    PHE A 301   CZ    PHE A 301   CE2     0.155                       
REMARK 500    GLU B 190   CD    GLU B 190   OE1     0.175                       
REMARK 500    GLU B 190   CD    GLU B 190   OE2     0.166                       
REMARK 500    ASN D   5   N     ASN D   5   CA      0.124                       
REMARK 500    ASN D   5   CG    ASN D   5   ND2     0.370                       
REMARK 500    GLN D  13   CD    GLN D  13   OE1     0.140                       
REMARK 500    GLN D  14   C     GLN D  14   O       0.243                       
REMARK 500    GLN D  14   C     LEU D  15   N       0.140                       
REMARK 500    ARG D 285   NE    ARG D 285   CZ      0.170                       
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 285   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    LEU B   8   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500    LEU B   8   CB  -  CG  -  CD2 ANGL. DEV. = -11.6 DEGREES          
REMARK 500    ASP B  58   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG C 535   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG D 285   NE  -  CZ  -  NH1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG D 285   NE  -  CZ  -  NH2 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  29     -166.55   -129.70                                   
REMARK 500    GLU A  30        9.32    -65.46                                   
REMARK 500    ASP A  39     -141.75   -169.33                                   
REMARK 500    GLU A  69      -90.35   -122.29                                   
REMARK 500    GLU A  76      -51.89   -125.21                                   
REMARK 500    THR A  84      -91.88   -133.85                                   
REMARK 500    ASN A  94      -71.62     -1.88                                   
REMARK 500    ARG A 113      132.99    177.20                                   
REMARK 500    ALA A 115     -163.55    -59.69                                   
REMARK 500    PHE A 122       96.59    -65.86                                   
REMARK 500    LYS A 123     -173.53    -57.79                                   
REMARK 500    ILE A 151      -66.36    -93.52                                   
REMARK 500    VAL A 159      -55.76    -28.50                                   
REMARK 500    GLU A 185      -62.50   -126.79                                   
REMARK 500    LEU A 187       88.96    -59.37                                   
REMARK 500    GLU A 190     -149.47    -74.46                                   
REMARK 500    THR A 193      -76.49    -55.67                                   
REMARK 500    ALA A 216       90.02    -67.29                                   
REMARK 500    PRO A 218      -82.53    -74.49                                   
REMARK 500    ASP A 220        6.23     55.95                                   
REMARK 500    ASP A 230       72.19   -101.96                                   
REMARK 500    SER A 239      145.64    -33.90                                   
REMARK 500    ALA A 249      -50.40     70.71                                   
REMARK 500    PRO A 255      105.65    -51.46                                   
REMARK 500    ASP A 269      -87.61   -117.83                                   
REMARK 500    LEU A 273       79.68   -106.68                                   
REMARK 500    ARG A 274     -135.54    -68.74                                   
REMARK 500    SER A 289     -136.89   -131.97                                   
REMARK 500    GLU A 295     -135.59   -107.02                                   
REMARK 500    ASP A 296       36.53    -67.37                                   
REMARK 500    SER A 307      136.04    -34.56                                   
REMARK 500    ALA A 309      128.39   -172.95                                   
REMARK 500    TYR A 313      -36.75    -39.48                                   
REMARK 500    GLU A 321      -46.76   -139.71                                   
REMARK 500    ASN A 322      142.25    118.22                                   
REMARK 500    THR A 323     -149.96   -163.02                                   
REMARK 500    ASP A 325      -82.59    176.21                                   
REMARK 500    HIS A 354       10.47   -144.08                                   
REMARK 500    ALA A 355     -136.95   -149.61                                   
REMARK 500    ARG A 361      129.96    -20.46                                   
REMARK 500    ARG A 383     -153.36    -87.73                                   
REMARK 500    HIS A 437       86.35    -54.24                                   
REMARK 500    GLU A 441      -79.40    -57.05                                   
REMARK 500    VAL A 443      -66.96     -3.72                                   
REMARK 500    SER A 497       69.18   -154.17                                   
REMARK 500    LYS A 516      -86.08   -108.48                                   
REMARK 500    THR A 621      -28.66    102.50                                   
REMARK 500    LEU B  15      -78.41    -31.79                                   
REMARK 500    GLU B  30      -26.69    -39.75                                   
REMARK 500    LYS B  31     -153.18    -82.57                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     154 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 ASN A    5     PRO A    6                  147.55                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A1001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 201   OD1                                                    
REMARK 620 2 ASP A 210   OD1 103.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B1002  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 210   OD1                                                    
REMARK 620 2 ASP B 201   OD1 101.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C1003  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 201   OD1                                                    
REMARK 620 2 ASP C 210   OD1 164.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D1004  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 201   OD1                                                    
REMARK 620 2 ASP D 210   OD1 163.4                                              
REMARK 620 3 ASP D 209   OD1 109.6  85.8                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 1004                 
DBREF  2ID0 A    1   644  UNP    P30850   RNB_ECOLI        1    644             
DBREF  2ID0 B    1   644  UNP    P30850   RNB_ECOLI        1    644             
DBREF  2ID0 C    1   644  UNP    P30850   RNB_ECOLI        1    644             
DBREF  2ID0 D    1   644  UNP    P30850   RNB_ECOLI        1    644             
SEQADV 2ID0 MSE A    1  UNP  P30850    MET     1 MODIFIED RESIDUE               
SEQADV 2ID0 MSE A   51  UNP  P30850    MET    51 MODIFIED RESIDUE               
SEQADV 2ID0 MSE A   55  UNP  P30850    MET    55 MODIFIED RESIDUE               
SEQADV 2ID0 MSE A  132  UNP  P30850    MET   132 MODIFIED RESIDUE               
SEQADV 2ID0 MSE A  182  UNP  P30850    MET   182 MODIFIED RESIDUE               
SEQADV 2ID0 MSE A  208  UNP  P30850    MET   208 MODIFIED RESIDUE               
SEQADV 2ID0 MSE A  261  UNP  P30850    MET   261 MODIFIED RESIDUE               
SEQADV 2ID0 MSE A  286  UNP  P30850    MET   286 MODIFIED RESIDUE               
SEQADV 2ID0 MSE A  393  UNP  P30850    MET   393 MODIFIED RESIDUE               
SEQADV 2ID0 MSE A  417  UNP  P30850    MET   417 MODIFIED RESIDUE               
SEQADV 2ID0 MSE A  505  UNP  P30850    MET   505 MODIFIED RESIDUE               
SEQADV 2ID0 MSE A  531  UNP  P30850    MET   531 MODIFIED RESIDUE               
SEQADV 2ID0 MSE A  540  UNP  P30850    MET   540 MODIFIED RESIDUE               
SEQADV 2ID0 MSE A  576  UNP  P30850    MET   576 MODIFIED RESIDUE               
SEQADV 2ID0 MSE A  633  UNP  P30850    MET   633 MODIFIED RESIDUE               
SEQADV 2ID0 MSE B    1  UNP  P30850    MET     1 MODIFIED RESIDUE               
SEQADV 2ID0 MSE B   51  UNP  P30850    MET    51 MODIFIED RESIDUE               
SEQADV 2ID0 MSE B   55  UNP  P30850    MET    55 MODIFIED RESIDUE               
SEQADV 2ID0 MSE B  132  UNP  P30850    MET   132 MODIFIED RESIDUE               
SEQADV 2ID0 MSE B  182  UNP  P30850    MET   182 MODIFIED RESIDUE               
SEQADV 2ID0 MSE B  208  UNP  P30850    MET   208 MODIFIED RESIDUE               
SEQADV 2ID0 MSE B  261  UNP  P30850    MET   261 MODIFIED RESIDUE               
SEQADV 2ID0 MSE B  286  UNP  P30850    MET   286 MODIFIED RESIDUE               
SEQADV 2ID0 MSE B  393  UNP  P30850    MET   393 MODIFIED RESIDUE               
SEQADV 2ID0 MSE B  417  UNP  P30850    MET   417 MODIFIED RESIDUE               
SEQADV 2ID0 MSE B  505  UNP  P30850    MET   505 MODIFIED RESIDUE               
SEQADV 2ID0 MSE B  531  UNP  P30850    MET   531 MODIFIED RESIDUE               
SEQADV 2ID0 MSE B  540  UNP  P30850    MET   540 MODIFIED RESIDUE               
SEQADV 2ID0 MSE B  576  UNP  P30850    MET   576 MODIFIED RESIDUE               
SEQADV 2ID0 MSE B  633  UNP  P30850    MET   633 MODIFIED RESIDUE               
SEQADV 2ID0 MSE C    1  UNP  P30850    MET     1 MODIFIED RESIDUE               
SEQADV 2ID0 MSE C   51  UNP  P30850    MET    51 MODIFIED RESIDUE               
SEQADV 2ID0 MSE C   55  UNP  P30850    MET    55 MODIFIED RESIDUE               
SEQADV 2ID0 MSE C  132  UNP  P30850    MET   132 MODIFIED RESIDUE               
SEQADV 2ID0 MSE C  182  UNP  P30850    MET   182 MODIFIED RESIDUE               
SEQADV 2ID0 MSE C  208  UNP  P30850    MET   208 MODIFIED RESIDUE               
SEQADV 2ID0 MSE C  261  UNP  P30850    MET   261 MODIFIED RESIDUE               
SEQADV 2ID0 MSE C  286  UNP  P30850    MET   286 MODIFIED RESIDUE               
SEQADV 2ID0 MSE C  393  UNP  P30850    MET   393 MODIFIED RESIDUE               
SEQADV 2ID0 MSE C  417  UNP  P30850    MET   417 MODIFIED RESIDUE               
SEQADV 2ID0 MSE C  505  UNP  P30850    MET   505 MODIFIED RESIDUE               
SEQADV 2ID0 MSE C  531  UNP  P30850    MET   531 MODIFIED RESIDUE               
SEQADV 2ID0 MSE C  540  UNP  P30850    MET   540 MODIFIED RESIDUE               
SEQADV 2ID0 MSE C  576  UNP  P30850    MET   576 MODIFIED RESIDUE               
SEQADV 2ID0 MSE C  633  UNP  P30850    MET   633 MODIFIED RESIDUE               
SEQADV 2ID0 MSE D    1  UNP  P30850    MET     1 MODIFIED RESIDUE               
SEQADV 2ID0 MSE D   51  UNP  P30850    MET    51 MODIFIED RESIDUE               
SEQADV 2ID0 MSE D   55  UNP  P30850    MET    55 MODIFIED RESIDUE               
SEQADV 2ID0 MSE D  132  UNP  P30850    MET   132 MODIFIED RESIDUE               
SEQADV 2ID0 MSE D  182  UNP  P30850    MET   182 MODIFIED RESIDUE               
SEQADV 2ID0 MSE D  208  UNP  P30850    MET   208 MODIFIED RESIDUE               
SEQADV 2ID0 MSE D  261  UNP  P30850    MET   261 MODIFIED RESIDUE               
SEQADV 2ID0 MSE D  286  UNP  P30850    MET   286 MODIFIED RESIDUE               
SEQADV 2ID0 MSE D  393  UNP  P30850    MET   393 MODIFIED RESIDUE               
SEQADV 2ID0 MSE D  417  UNP  P30850    MET   417 MODIFIED RESIDUE               
SEQADV 2ID0 MSE D  505  UNP  P30850    MET   505 MODIFIED RESIDUE               
SEQADV 2ID0 MSE D  531  UNP  P30850    MET   531 MODIFIED RESIDUE               
SEQADV 2ID0 MSE D  540  UNP  P30850    MET   540 MODIFIED RESIDUE               
SEQADV 2ID0 MSE D  576  UNP  P30850    MET   576 MODIFIED RESIDUE               
SEQADV 2ID0 MSE D  633  UNP  P30850    MET   633 MODIFIED RESIDUE               
SEQRES   1 A  644  MSE PHE GLN ASP ASN PRO LEU LEU ALA GLN LEU LYS GLN          
SEQRES   2 A  644  GLN LEU HIS SER GLN THR PRO ARG ALA GLU GLY VAL VAL          
SEQRES   3 A  644  LYS ALA THR GLU LYS GLY PHE GLY PHE LEU GLU VAL ASP          
SEQRES   4 A  644  ALA GLN LYS SER TYR PHE ILE PRO PRO PRO GLN MSE LYS          
SEQRES   5 A  644  LYS VAL MSE HIS GLY ASP ARG ILE ILE ALA VAL ILE HIS          
SEQRES   6 A  644  SER GLU LYS GLU ARG GLU SER ALA GLU PRO GLU GLU LEU          
SEQRES   7 A  644  VAL GLU PRO PHE LEU THR ARG PHE VAL GLY LYS VAL GLN          
SEQRES   8 A  644  GLY LYS ASN ASP ARG LEU ALA ILE VAL PRO ASP HIS PRO          
SEQRES   9 A  644  LEU LEU LYS ASP ALA ILE PRO CYS ARG ALA ALA ARG GLY          
SEQRES  10 A  644  LEU ASN HIS GLU PHE LYS GLU GLY ASP TRP ALA VAL ALA          
SEQRES  11 A  644  GLU MSE ARG ARG HIS PRO LEU LYS GLY ASP ARG SER PHE          
SEQRES  12 A  644  TYR ALA GLU LEU THR GLN TYR ILE THR PHE GLY ASP ASP          
SEQRES  13 A  644  HIS PHE VAL PRO TRP TRP VAL THR LEU ALA ARG HIS ASN          
SEQRES  14 A  644  LEU GLU LYS GLU ALA PRO ASP GLY VAL ALA THR GLU MSE          
SEQRES  15 A  644  LEU ASP GLU GLY LEU VAL ARG GLU ASP LEU THR ALA LEU          
SEQRES  16 A  644  ASP PHE VAL THR ILE ASP SER ALA SER THR GLU ASP MSE          
SEQRES  17 A  644  ASP ASP ALA LEU PHE ALA LYS ALA LEU PRO ASP ASP LYS          
SEQRES  18 A  644  LEU GLN LEU ILE VAL ALA ILE ALA ASP PRO THR ALA TRP          
SEQRES  19 A  644  ILE ALA GLU GLY SER LYS LEU ASP LYS ALA ALA LYS ILE          
SEQRES  20 A  644  ARG ALA PHE THR ASN TYR LEU PRO GLY PHE ASN ILE PRO          
SEQRES  21 A  644  MSE LEU PRO ARG GLU LEU SER ASP ASP LEU CYS SER LEU          
SEQRES  22 A  644  ARG ALA ASN GLU VAL ARG PRO VAL LEU ALA CYS ARG MSE          
SEQRES  23 A  644  THR LEU SER ALA ASP GLY THR ILE GLU ASP ASN ILE GLU          
SEQRES  24 A  644  PHE PHE ALA ALA THR ILE GLU SER LYS ALA LYS LEU VAL          
SEQRES  25 A  644  TYR ASP GLN VAL SER ASP TRP LEU GLU ASN THR GLY ASP          
SEQRES  26 A  644  TRP GLN PRO GLU SER GLU ALA ILE ALA GLU GLN VAL ARG          
SEQRES  27 A  644  LEU LEU ALA GLN ILE CYS GLN ARG ARG GLY GLU TRP ARG          
SEQRES  28 A  644  HIS ASN HIS ALA LEU VAL PHE LYS ASP ARG PRO ASP TYR          
SEQRES  29 A  644  ARG PHE ILE LEU GLY GLU LYS GLY GLU VAL LEU ASP ILE          
SEQRES  30 A  644  VAL ALA GLU PRO ARG ARG ILE ALA ASN ARG ILE VAL GLU          
SEQRES  31 A  644  GLU ALA MSE ILE ALA ALA ASN ILE CYS ALA ALA ARG VAL          
SEQRES  32 A  644  LEU ARG ASP LYS LEU GLY PHE GLY ILE TYR ASN VAL HIS          
SEQRES  33 A  644  MSE GLY PHE ASP PRO ALA ASN ALA ASP ALA LEU ALA ALA          
SEQRES  34 A  644  LEU LEU LYS THR HIS GLY LEU HIS VAL ASP ALA GLU GLU          
SEQRES  35 A  644  VAL LEU THR LEU ASP GLY PHE CYS LYS LEU ARG ARG GLU          
SEQRES  36 A  644  LEU ASP ALA GLN PRO THR GLY PHE LEU ASP SER ARG ILE          
SEQRES  37 A  644  ARG ARG PHE GLN SER PHE ALA GLU ILE SER THR GLU PRO          
SEQRES  38 A  644  GLY PRO HIS PHE GLY LEU GLY LEU GLU ALA TYR ALA THR          
SEQRES  39 A  644  TRP THR SER PRO ILE ARG LYS TYR GLY ASP MSE ILE ASN          
SEQRES  40 A  644  HIS ARG LEU LEU LYS ALA VAL ILE LYS GLY GLU THR ALA          
SEQRES  41 A  644  THR ARG PRO GLN ASP GLU ILE THR VAL GLN MSE ALA GLU          
SEQRES  42 A  644  ARG ARG ARG LEU ASN ARG MSE ALA GLU ARG ASP VAL GLY          
SEQRES  43 A  644  ASP TRP LEU TYR ALA ARG PHE LEU LYS ASP LYS ALA GLY          
SEQRES  44 A  644  THR ASP THR ARG PHE ALA ALA GLU ILE VAL ASP ILE SER          
SEQRES  45 A  644  ARG GLY GLY MSE ARG VAL ARG LEU VAL ASP ASN GLY ALA          
SEQRES  46 A  644  ILE ALA PHE ILE PRO ALA PRO PHE LEU HIS ALA VAL ARG          
SEQRES  47 A  644  ASP GLU LEU VAL CYS SER GLN GLU ASN GLY THR VAL GLN          
SEQRES  48 A  644  ILE LYS GLY GLU THR VAL TYR LYS VAL THR ASP VAL ILE          
SEQRES  49 A  644  ASP VAL THR ILE ALA GLU VAL ARG MSE GLU THR ARG SER          
SEQRES  50 A  644  ILE ILE ALA ARG PRO VAL ALA                                  
SEQRES   1 B  644  MSE PHE GLN ASP ASN PRO LEU LEU ALA GLN LEU LYS GLN          
SEQRES   2 B  644  GLN LEU HIS SER GLN THR PRO ARG ALA GLU GLY VAL VAL          
SEQRES   3 B  644  LYS ALA THR GLU LYS GLY PHE GLY PHE LEU GLU VAL ASP          
SEQRES   4 B  644  ALA GLN LYS SER TYR PHE ILE PRO PRO PRO GLN MSE LYS          
SEQRES   5 B  644  LYS VAL MSE HIS GLY ASP ARG ILE ILE ALA VAL ILE HIS          
SEQRES   6 B  644  SER GLU LYS GLU ARG GLU SER ALA GLU PRO GLU GLU LEU          
SEQRES   7 B  644  VAL GLU PRO PHE LEU THR ARG PHE VAL GLY LYS VAL GLN          
SEQRES   8 B  644  GLY LYS ASN ASP ARG LEU ALA ILE VAL PRO ASP HIS PRO          
SEQRES   9 B  644  LEU LEU LYS ASP ALA ILE PRO CYS ARG ALA ALA ARG GLY          
SEQRES  10 B  644  LEU ASN HIS GLU PHE LYS GLU GLY ASP TRP ALA VAL ALA          
SEQRES  11 B  644  GLU MSE ARG ARG HIS PRO LEU LYS GLY ASP ARG SER PHE          
SEQRES  12 B  644  TYR ALA GLU LEU THR GLN TYR ILE THR PHE GLY ASP ASP          
SEQRES  13 B  644  HIS PHE VAL PRO TRP TRP VAL THR LEU ALA ARG HIS ASN          
SEQRES  14 B  644  LEU GLU LYS GLU ALA PRO ASP GLY VAL ALA THR GLU MSE          
SEQRES  15 B  644  LEU ASP GLU GLY LEU VAL ARG GLU ASP LEU THR ALA LEU          
SEQRES  16 B  644  ASP PHE VAL THR ILE ASP SER ALA SER THR GLU ASP MSE          
SEQRES  17 B  644  ASP ASP ALA LEU PHE ALA LYS ALA LEU PRO ASP ASP LYS          
SEQRES  18 B  644  LEU GLN LEU ILE VAL ALA ILE ALA ASP PRO THR ALA TRP          
SEQRES  19 B  644  ILE ALA GLU GLY SER LYS LEU ASP LYS ALA ALA LYS ILE          
SEQRES  20 B  644  ARG ALA PHE THR ASN TYR LEU PRO GLY PHE ASN ILE PRO          
SEQRES  21 B  644  MSE LEU PRO ARG GLU LEU SER ASP ASP LEU CYS SER LEU          
SEQRES  22 B  644  ARG ALA ASN GLU VAL ARG PRO VAL LEU ALA CYS ARG MSE          
SEQRES  23 B  644  THR LEU SER ALA ASP GLY THR ILE GLU ASP ASN ILE GLU          
SEQRES  24 B  644  PHE PHE ALA ALA THR ILE GLU SER LYS ALA LYS LEU VAL          
SEQRES  25 B  644  TYR ASP GLN VAL SER ASP TRP LEU GLU ASN THR GLY ASP          
SEQRES  26 B  644  TRP GLN PRO GLU SER GLU ALA ILE ALA GLU GLN VAL ARG          
SEQRES  27 B  644  LEU LEU ALA GLN ILE CYS GLN ARG ARG GLY GLU TRP ARG          
SEQRES  28 B  644  HIS ASN HIS ALA LEU VAL PHE LYS ASP ARG PRO ASP TYR          
SEQRES  29 B  644  ARG PHE ILE LEU GLY GLU LYS GLY GLU VAL LEU ASP ILE          
SEQRES  30 B  644  VAL ALA GLU PRO ARG ARG ILE ALA ASN ARG ILE VAL GLU          
SEQRES  31 B  644  GLU ALA MSE ILE ALA ALA ASN ILE CYS ALA ALA ARG VAL          
SEQRES  32 B  644  LEU ARG ASP LYS LEU GLY PHE GLY ILE TYR ASN VAL HIS          
SEQRES  33 B  644  MSE GLY PHE ASP PRO ALA ASN ALA ASP ALA LEU ALA ALA          
SEQRES  34 B  644  LEU LEU LYS THR HIS GLY LEU HIS VAL ASP ALA GLU GLU          
SEQRES  35 B  644  VAL LEU THR LEU ASP GLY PHE CYS LYS LEU ARG ARG GLU          
SEQRES  36 B  644  LEU ASP ALA GLN PRO THR GLY PHE LEU ASP SER ARG ILE          
SEQRES  37 B  644  ARG ARG PHE GLN SER PHE ALA GLU ILE SER THR GLU PRO          
SEQRES  38 B  644  GLY PRO HIS PHE GLY LEU GLY LEU GLU ALA TYR ALA THR          
SEQRES  39 B  644  TRP THR SER PRO ILE ARG LYS TYR GLY ASP MSE ILE ASN          
SEQRES  40 B  644  HIS ARG LEU LEU LYS ALA VAL ILE LYS GLY GLU THR ALA          
SEQRES  41 B  644  THR ARG PRO GLN ASP GLU ILE THR VAL GLN MSE ALA GLU          
SEQRES  42 B  644  ARG ARG ARG LEU ASN ARG MSE ALA GLU ARG ASP VAL GLY          
SEQRES  43 B  644  ASP TRP LEU TYR ALA ARG PHE LEU LYS ASP LYS ALA GLY          
SEQRES  44 B  644  THR ASP THR ARG PHE ALA ALA GLU ILE VAL ASP ILE SER          
SEQRES  45 B  644  ARG GLY GLY MSE ARG VAL ARG LEU VAL ASP ASN GLY ALA          
SEQRES  46 B  644  ILE ALA PHE ILE PRO ALA PRO PHE LEU HIS ALA VAL ARG          
SEQRES  47 B  644  ASP GLU LEU VAL CYS SER GLN GLU ASN GLY THR VAL GLN          
SEQRES  48 B  644  ILE LYS GLY GLU THR VAL TYR LYS VAL THR ASP VAL ILE          
SEQRES  49 B  644  ASP VAL THR ILE ALA GLU VAL ARG MSE GLU THR ARG SER          
SEQRES  50 B  644  ILE ILE ALA ARG PRO VAL ALA                                  
SEQRES   1 C  644  MSE PHE GLN ASP ASN PRO LEU LEU ALA GLN LEU LYS GLN          
SEQRES   2 C  644  GLN LEU HIS SER GLN THR PRO ARG ALA GLU GLY VAL VAL          
SEQRES   3 C  644  LYS ALA THR GLU LYS GLY PHE GLY PHE LEU GLU VAL ASP          
SEQRES   4 C  644  ALA GLN LYS SER TYR PHE ILE PRO PRO PRO GLN MSE LYS          
SEQRES   5 C  644  LYS VAL MSE HIS GLY ASP ARG ILE ILE ALA VAL ILE HIS          
SEQRES   6 C  644  SER GLU LYS GLU ARG GLU SER ALA GLU PRO GLU GLU LEU          
SEQRES   7 C  644  VAL GLU PRO PHE LEU THR ARG PHE VAL GLY LYS VAL GLN          
SEQRES   8 C  644  GLY LYS ASN ASP ARG LEU ALA ILE VAL PRO ASP HIS PRO          
SEQRES   9 C  644  LEU LEU LYS ASP ALA ILE PRO CYS ARG ALA ALA ARG GLY          
SEQRES  10 C  644  LEU ASN HIS GLU PHE LYS GLU GLY ASP TRP ALA VAL ALA          
SEQRES  11 C  644  GLU MSE ARG ARG HIS PRO LEU LYS GLY ASP ARG SER PHE          
SEQRES  12 C  644  TYR ALA GLU LEU THR GLN TYR ILE THR PHE GLY ASP ASP          
SEQRES  13 C  644  HIS PHE VAL PRO TRP TRP VAL THR LEU ALA ARG HIS ASN          
SEQRES  14 C  644  LEU GLU LYS GLU ALA PRO ASP GLY VAL ALA THR GLU MSE          
SEQRES  15 C  644  LEU ASP GLU GLY LEU VAL ARG GLU ASP LEU THR ALA LEU          
SEQRES  16 C  644  ASP PHE VAL THR ILE ASP SER ALA SER THR GLU ASP MSE          
SEQRES  17 C  644  ASP ASP ALA LEU PHE ALA LYS ALA LEU PRO ASP ASP LYS          
SEQRES  18 C  644  LEU GLN LEU ILE VAL ALA ILE ALA ASP PRO THR ALA TRP          
SEQRES  19 C  644  ILE ALA GLU GLY SER LYS LEU ASP LYS ALA ALA LYS ILE          
SEQRES  20 C  644  ARG ALA PHE THR ASN TYR LEU PRO GLY PHE ASN ILE PRO          
SEQRES  21 C  644  MSE LEU PRO ARG GLU LEU SER ASP ASP LEU CYS SER LEU          
SEQRES  22 C  644  ARG ALA ASN GLU VAL ARG PRO VAL LEU ALA CYS ARG MSE          
SEQRES  23 C  644  THR LEU SER ALA ASP GLY THR ILE GLU ASP ASN ILE GLU          
SEQRES  24 C  644  PHE PHE ALA ALA THR ILE GLU SER LYS ALA LYS LEU VAL          
SEQRES  25 C  644  TYR ASP GLN VAL SER ASP TRP LEU GLU ASN THR GLY ASP          
SEQRES  26 C  644  TRP GLN PRO GLU SER GLU ALA ILE ALA GLU GLN VAL ARG          
SEQRES  27 C  644  LEU LEU ALA GLN ILE CYS GLN ARG ARG GLY GLU TRP ARG          
SEQRES  28 C  644  HIS ASN HIS ALA LEU VAL PHE LYS ASP ARG PRO ASP TYR          
SEQRES  29 C  644  ARG PHE ILE LEU GLY GLU LYS GLY GLU VAL LEU ASP ILE          
SEQRES  30 C  644  VAL ALA GLU PRO ARG ARG ILE ALA ASN ARG ILE VAL GLU          
SEQRES  31 C  644  GLU ALA MSE ILE ALA ALA ASN ILE CYS ALA ALA ARG VAL          
SEQRES  32 C  644  LEU ARG ASP LYS LEU GLY PHE GLY ILE TYR ASN VAL HIS          
SEQRES  33 C  644  MSE GLY PHE ASP PRO ALA ASN ALA ASP ALA LEU ALA ALA          
SEQRES  34 C  644  LEU LEU LYS THR HIS GLY LEU HIS VAL ASP ALA GLU GLU          
SEQRES  35 C  644  VAL LEU THR LEU ASP GLY PHE CYS LYS LEU ARG ARG GLU          
SEQRES  36 C  644  LEU ASP ALA GLN PRO THR GLY PHE LEU ASP SER ARG ILE          
SEQRES  37 C  644  ARG ARG PHE GLN SER PHE ALA GLU ILE SER THR GLU PRO          
SEQRES  38 C  644  GLY PRO HIS PHE GLY LEU GLY LEU GLU ALA TYR ALA THR          
SEQRES  39 C  644  TRP THR SER PRO ILE ARG LYS TYR GLY ASP MSE ILE ASN          
SEQRES  40 C  644  HIS ARG LEU LEU LYS ALA VAL ILE LYS GLY GLU THR ALA          
SEQRES  41 C  644  THR ARG PRO GLN ASP GLU ILE THR VAL GLN MSE ALA GLU          
SEQRES  42 C  644  ARG ARG ARG LEU ASN ARG MSE ALA GLU ARG ASP VAL GLY          
SEQRES  43 C  644  ASP TRP LEU TYR ALA ARG PHE LEU LYS ASP LYS ALA GLY          
SEQRES  44 C  644  THR ASP THR ARG PHE ALA ALA GLU ILE VAL ASP ILE SER          
SEQRES  45 C  644  ARG GLY GLY MSE ARG VAL ARG LEU VAL ASP ASN GLY ALA          
SEQRES  46 C  644  ILE ALA PHE ILE PRO ALA PRO PHE LEU HIS ALA VAL ARG          
SEQRES  47 C  644  ASP GLU LEU VAL CYS SER GLN GLU ASN GLY THR VAL GLN          
SEQRES  48 C  644  ILE LYS GLY GLU THR VAL TYR LYS VAL THR ASP VAL ILE          
SEQRES  49 C  644  ASP VAL THR ILE ALA GLU VAL ARG MSE GLU THR ARG SER          
SEQRES  50 C  644  ILE ILE ALA ARG PRO VAL ALA                                  
SEQRES   1 D  644  MSE PHE GLN ASP ASN PRO LEU LEU ALA GLN LEU LYS GLN          
SEQRES   2 D  644  GLN LEU HIS SER GLN THR PRO ARG ALA GLU GLY VAL VAL          
SEQRES   3 D  644  LYS ALA THR GLU LYS GLY PHE GLY PHE LEU GLU VAL ASP          
SEQRES   4 D  644  ALA GLN LYS SER TYR PHE ILE PRO PRO PRO GLN MSE LYS          
SEQRES   5 D  644  LYS VAL MSE HIS GLY ASP ARG ILE ILE ALA VAL ILE HIS          
SEQRES   6 D  644  SER GLU LYS GLU ARG GLU SER ALA GLU PRO GLU GLU LEU          
SEQRES   7 D  644  VAL GLU PRO PHE LEU THR ARG PHE VAL GLY LYS VAL GLN          
SEQRES   8 D  644  GLY LYS ASN ASP ARG LEU ALA ILE VAL PRO ASP HIS PRO          
SEQRES   9 D  644  LEU LEU LYS ASP ALA ILE PRO CYS ARG ALA ALA ARG GLY          
SEQRES  10 D  644  LEU ASN HIS GLU PHE LYS GLU GLY ASP TRP ALA VAL ALA          
SEQRES  11 D  644  GLU MSE ARG ARG HIS PRO LEU LYS GLY ASP ARG SER PHE          
SEQRES  12 D  644  TYR ALA GLU LEU THR GLN TYR ILE THR PHE GLY ASP ASP          
SEQRES  13 D  644  HIS PHE VAL PRO TRP TRP VAL THR LEU ALA ARG HIS ASN          
SEQRES  14 D  644  LEU GLU LYS GLU ALA PRO ASP GLY VAL ALA THR GLU MSE          
SEQRES  15 D  644  LEU ASP GLU GLY LEU VAL ARG GLU ASP LEU THR ALA LEU          
SEQRES  16 D  644  ASP PHE VAL THR ILE ASP SER ALA SER THR GLU ASP MSE          
SEQRES  17 D  644  ASP ASP ALA LEU PHE ALA LYS ALA LEU PRO ASP ASP LYS          
SEQRES  18 D  644  LEU GLN LEU ILE VAL ALA ILE ALA ASP PRO THR ALA TRP          
SEQRES  19 D  644  ILE ALA GLU GLY SER LYS LEU ASP LYS ALA ALA LYS ILE          
SEQRES  20 D  644  ARG ALA PHE THR ASN TYR LEU PRO GLY PHE ASN ILE PRO          
SEQRES  21 D  644  MSE LEU PRO ARG GLU LEU SER ASP ASP LEU CYS SER LEU          
SEQRES  22 D  644  ARG ALA ASN GLU VAL ARG PRO VAL LEU ALA CYS ARG MSE          
SEQRES  23 D  644  THR LEU SER ALA ASP GLY THR ILE GLU ASP ASN ILE GLU          
SEQRES  24 D  644  PHE PHE ALA ALA THR ILE GLU SER LYS ALA LYS LEU VAL          
SEQRES  25 D  644  TYR ASP GLN VAL SER ASP TRP LEU GLU ASN THR GLY ASP          
SEQRES  26 D  644  TRP GLN PRO GLU SER GLU ALA ILE ALA GLU GLN VAL ARG          
SEQRES  27 D  644  LEU LEU ALA GLN ILE CYS GLN ARG ARG GLY GLU TRP ARG          
SEQRES  28 D  644  HIS ASN HIS ALA LEU VAL PHE LYS ASP ARG PRO ASP TYR          
SEQRES  29 D  644  ARG PHE ILE LEU GLY GLU LYS GLY GLU VAL LEU ASP ILE          
SEQRES  30 D  644  VAL ALA GLU PRO ARG ARG ILE ALA ASN ARG ILE VAL GLU          
SEQRES  31 D  644  GLU ALA MSE ILE ALA ALA ASN ILE CYS ALA ALA ARG VAL          
SEQRES  32 D  644  LEU ARG ASP LYS LEU GLY PHE GLY ILE TYR ASN VAL HIS          
SEQRES  33 D  644  MSE GLY PHE ASP PRO ALA ASN ALA ASP ALA LEU ALA ALA          
SEQRES  34 D  644  LEU LEU LYS THR HIS GLY LEU HIS VAL ASP ALA GLU GLU          
SEQRES  35 D  644  VAL LEU THR LEU ASP GLY PHE CYS LYS LEU ARG ARG GLU          
SEQRES  36 D  644  LEU ASP ALA GLN PRO THR GLY PHE LEU ASP SER ARG ILE          
SEQRES  37 D  644  ARG ARG PHE GLN SER PHE ALA GLU ILE SER THR GLU PRO          
SEQRES  38 D  644  GLY PRO HIS PHE GLY LEU GLY LEU GLU ALA TYR ALA THR          
SEQRES  39 D  644  TRP THR SER PRO ILE ARG LYS TYR GLY ASP MSE ILE ASN          
SEQRES  40 D  644  HIS ARG LEU LEU LYS ALA VAL ILE LYS GLY GLU THR ALA          
SEQRES  41 D  644  THR ARG PRO GLN ASP GLU ILE THR VAL GLN MSE ALA GLU          
SEQRES  42 D  644  ARG ARG ARG LEU ASN ARG MSE ALA GLU ARG ASP VAL GLY          
SEQRES  43 D  644  ASP TRP LEU TYR ALA ARG PHE LEU LYS ASP LYS ALA GLY          
SEQRES  44 D  644  THR ASP THR ARG PHE ALA ALA GLU ILE VAL ASP ILE SER          
SEQRES  45 D  644  ARG GLY GLY MSE ARG VAL ARG LEU VAL ASP ASN GLY ALA          
SEQRES  46 D  644  ILE ALA PHE ILE PRO ALA PRO PHE LEU HIS ALA VAL ARG          
SEQRES  47 D  644  ASP GLU LEU VAL CYS SER GLN GLU ASN GLY THR VAL GLN          
SEQRES  48 D  644  ILE LYS GLY GLU THR VAL TYR LYS VAL THR ASP VAL ILE          
SEQRES  49 D  644  ASP VAL THR ILE ALA GLU VAL ARG MSE GLU THR ARG SER          
SEQRES  50 D  644  ILE ILE ALA ARG PRO VAL ALA                                  
MODRES 2ID0 MSE A   51  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE A   55  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE A  132  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE A  182  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE A  208  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE A  261  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE A  286  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE A  393  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE A  417  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE A  505  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE A  531  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE A  540  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE A  576  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE A  633  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE B   51  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE B   55  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE B  132  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE B  182  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE B  208  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE B  261  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE B  286  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE B  393  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE B  417  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE B  505  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE B  531  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE B  540  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE B  576  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE B  633  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE C   51  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE C   55  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE C  132  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE C  182  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE C  208  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE C  261  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE C  286  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE C  393  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE C  417  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE C  505  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE C  531  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE C  540  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE C  576  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE C  633  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE D   51  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE D   55  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE D  132  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE D  182  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE D  208  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE D  261  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE D  286  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE D  393  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE D  417  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE D  505  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE D  531  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE D  540  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE D  576  MET  SELENOMETHIONINE                                   
MODRES 2ID0 MSE D  633  MET  SELENOMETHIONINE                                   
HET    MSE  A  51       8                                                       
HET    MSE  A  55       8                                                       
HET    MSE  A 132       8                                                       
HET    MSE  A 182       8                                                       
HET    MSE  A 208       8                                                       
HET    MSE  A 261       8                                                       
HET    MSE  A 286       8                                                       
HET    MSE  A 393       8                                                       
HET    MSE  A 417       8                                                       
HET    MSE  A 505       8                                                       
HET    MSE  A 531       8                                                       
HET    MSE  A 540       8                                                       
HET    MSE  A 576       8                                                       
HET    MSE  A 633       8                                                       
HET    MSE  B  51       8                                                       
HET    MSE  B  55       8                                                       
HET    MSE  B 132       8                                                       
HET    MSE  B 182       8                                                       
HET    MSE  B 208       8                                                       
HET    MSE  B 261       8                                                       
HET    MSE  B 286       8                                                       
HET    MSE  B 393       8                                                       
HET    MSE  B 417       8                                                       
HET    MSE  B 505       8                                                       
HET    MSE  B 531       8                                                       
HET    MSE  B 540       8                                                       
HET    MSE  B 576       8                                                       
HET    MSE  B 633       8                                                       
HET    MSE  C  51       8                                                       
HET    MSE  C  55       8                                                       
HET    MSE  C 132       8                                                       
HET    MSE  C 182       8                                                       
HET    MSE  C 208       8                                                       
HET    MSE  C 261       8                                                       
HET    MSE  C 286       8                                                       
HET    MSE  C 393       8                                                       
HET    MSE  C 417       8                                                       
HET    MSE  C 505       8                                                       
HET    MSE  C 531       8                                                       
HET    MSE  C 540       8                                                       
HET    MSE  C 576       8                                                       
HET    MSE  C 633       8                                                       
HET    MSE  D  51       8                                                       
HET    MSE  D  55       8                                                       
HET    MSE  D 132       8                                                       
HET    MSE  D 182       8                                                       
HET    MSE  D 208       8                                                       
HET    MSE  D 261       8                                                       
HET    MSE  D 286       8                                                       
HET    MSE  D 393       8                                                       
HET    MSE  D 417       8                                                       
HET    MSE  D 505       8                                                       
HET    MSE  D 531       8                                                       
HET    MSE  D 540       8                                                       
HET    MSE  D 576       8                                                       
HET    MSE  D 633       8                                                       
HET     MN  A1001       1                                                       
HET     MN  B1002       1                                                       
HET     MN  C1003       1                                                       
HET     MN  D1004       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   1  MSE    56(C5 H11 N O2 SE)                                           
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   9  HOH   *287(H2 O)                                                    
HELIX    1   1 ASN A    5  GLN A   18  1                                  14    
HELIX    2   2 PRO A   47  LYS A   52  1                                   6    
HELIX    3   3 HIS A  135  GLY A  139  5                                   5    
HELIX    4   4 PHE A  158  HIS A  168  1                                  11    
HELIX    5   5 PRO A  231  TRP A  234  5                                   4    
HELIX    6   6 SER A  239  ALA A  249  1                                  11    
HELIX    7   7 PRO A  263  ASP A  268  1                                   6    
HELIX    8   8 TYR A  313  LEU A  320  1                                   8    
HELIX    9   9 SER A  330  ALA A  355  1                                  26    
HELIX   10  10 ARG A  383  LEU A  408  1                                  26    
HELIX   11  11 ASN A  423  GLY A  435  1                                  13    
HELIX   12  12 ASP A  439  LEU A  444  1                                   6    
HELIX   13  13 THR A  445  ALA A  458  1                                  14    
HELIX   14  14 GLY A  462  ARG A  469  1                                   8    
HELIX   15  15 LYS A  501  ILE A  515  1                                  15    
HELIX   16  16 GLU A  526  LYS A  555  1                                  30    
HELIX   17  17 ASP A  556  ALA A  558  5                                   3    
HELIX   18  18 PRO A  592  LEU A  594  5                                   3    
HELIX   19  19 VAL A  597  ASP A  599  5                                   3    
HELIX   20  20 ASN B    5  GLN B   14  1                                  10    
HELIX   21  21 PRO B   47  LYS B   52  1                                   6    
HELIX   22  22 HIS B  135  GLY B  139  5                                   5    
HELIX   23  23 PHE B  158  ASN B  169  1                                  12    
HELIX   24  24 PRO B  231  TRP B  234  5                                   4    
HELIX   25  25 SER B  239  ALA B  249  1                                  11    
HELIX   26  26 PRO B  263  ASP B  268  1                                   6    
HELIX   27  27 TYR B  313  ASN B  322  1                                  10    
HELIX   28  28 SER B  330  ALA B  355  1                                  26    
HELIX   29  29 ARG B  383  LYS B  407  1                                  25    
HELIX   30  30 ASN B  423  THR B  433  1                                  11    
HELIX   31  31 GLU B  441  LEU B  444  5                                   4    
HELIX   32  32 THR B  445  GLN B  459  1                                  15    
HELIX   33  33 GLY B  462  ILE B  468  1                                   7    
HELIX   34  34 ARG B  469  GLN B  472  5                                   4    
HELIX   35  35 LYS B  501  LYS B  516  1                                  16    
HELIX   36  36 GLN B  524  LYS B  555  1                                  32    
HELIX   37  37 ASP B  556  ALA B  558  5                                   3    
HELIX   38  38 PRO B  592  LEU B  594  5                                   3    
HELIX   39  39 VAL B  597  ASP B  599  5                                   3    
HELIX   40  40 ASN C    5  GLN C   18  1                                  14    
HELIX   41  41 PRO C   49  LYS C   53  5                                   5    
HELIX   42  42 HIS C  135  GLY C  139  5                                   5    
HELIX   43  43 PHE C  158  HIS C  168  1                                  11    
HELIX   44  44 PRO C  231  TRP C  234  5                                   4    
HELIX   45  45 SER C  239  ALA C  249  1                                  11    
HELIX   46  46 PRO C  263  ASP C  269  1                                   7    
HELIX   47  47 TYR C  313  ASN C  322  1                                  10    
HELIX   48  48 SER C  330  ALA C  355  1                                  26    
HELIX   49  49 ARG C  383  LYS C  407  1                                  25    
HELIX   50  50 ASP C  420  HIS C  434  1                                  15    
HELIX   51  51 ASP C  439  LEU C  444  1                                   6    
HELIX   52  52 THR C  445  ALA C  458  1                                  14    
HELIX   53  53 GLY C  462  ILE C  468  1                                   7    
HELIX   54  54 ARG C  469  GLN C  472  5                                   4    
HELIX   55  55 LYS C  501  ILE C  515  1                                  15    
HELIX   56  56 GLN C  524  LYS C  555  1                                  32    
HELIX   57  57 ASP C  556  ALA C  558  5                                   3    
HELIX   58  58 PRO C  592  LEU C  594  5                                   3    
HELIX   59  59 VAL C  597  ASP C  599  5                                   3    
HELIX   60  60 ASN D    5  THR D   19  1                                  15    
HELIX   61  61 HIS D  135  ASP D  140  1                                   6    
HELIX   62  62 PHE D  158  HIS D  168  1                                  11    
HELIX   63  63 SER D  239  ALA D  249  1                                  11    
HELIX   64  64 PRO D  263  ASP D  269  1                                   7    
HELIX   65  65 TYR D  313  ASN D  322  1                                  10    
HELIX   66  66 SER D  330  ALA D  355  1                                  26    
HELIX   67  67 ARG D  383  LEU D  408  1                                  26    
HELIX   68  68 ASP D  420  THR D  433  1                                  14    
HELIX   69  69 GLU D  441  LEU D  444  5                                   4    
HELIX   70  70 THR D  445  ASP D  457  1                                  13    
HELIX   71  71 GLY D  462  ARG D  469  1                                   8    
HELIX   72  72 ARG D  470  GLN D  472  5                                   3    
HELIX   73  73 LYS D  501  LYS D  516  1                                  16    
HELIX   74  74 GLU D  526  LYS D  555  1                                  30    
HELIX   75  75 ASP D  556  ALA D  558  5                                   3    
HELIX   76  76 PRO D  592  LEU D  594  5                                   3    
HELIX   77  77 VAL D  597  ASP D  599  5                                   3    
SHEET    1   A 6 ARG A  21  LYS A  27  0                                        
SHEET    2   A 6 GLY A  34  GLU A  37 -1  O  GLU A  37   N  VAL A  25           
SHEET    3   A 6 SER A  43  ILE A  46 -1  O  ILE A  46   N  GLY A  34           
SHEET    4   A 6 SER A  72  GLU A  80  1  O  ALA A  73   N  PHE A  45           
SHEET    5   A 6 ARG A  59  HIS A  65 -1  N  ARG A  59   O  GLU A  80           
SHEET    6   A 6 ARG A  21  LYS A  27 -1  N  ALA A  22   O  ALA A  62           
SHEET    1   B 5 ILE A 110  PRO A 111  0                                        
SHEET    2   B 5 ARG A  96  PRO A 101 -1  N  ILE A  99   O  ILE A 110           
SHEET    3   B 5 ARG A  85  LYS A  93 -1  N  LYS A  93   O  ARG A  96           
SHEET    4   B 5 TRP A 127  ARG A 134 -1  O  ALA A 130   N  PHE A  86           
SHEET    5   B 5 TYR A 144  THR A 152 -1  O  GLU A 146   N  GLU A 131           
SHEET    1   C 2 THR A 199  ASP A 201  0                                        
SHEET    2   C 2 LYS A 310  VAL A 312  1  O  LEU A 311   N  ASP A 201           
SHEET    1   D 4 ASP A 210  ALA A 214  0                                        
SHEET    2   D 4 LEU A 222  ALA A 229 -1  O  ALA A 227   N  ALA A 211           
SHEET    3   D 4 VAL A 278  LEU A 288 -1  O  LEU A 282   N  ILE A 228           
SHEET    4   D 4 PHE A 300  GLU A 306 -1  O  ILE A 305   N  ARG A 279           
SHEET    1   E 2 ASN A 252  LEU A 254  0                                        
SHEET    2   E 2 PHE A 257  ILE A 259 -1  O  ILE A 259   N  ASN A 252           
SHEET    1   F 2 TYR A 364  LEU A 368  0                                        
SHEET    2   F 2 VAL A 374  ALA A 379 -1  O  VAL A 378   N  ARG A 365           
SHEET    1   G 2 TYR A 413  VAL A 415  0                                        
SHEET    2   G 2 GLU A 476  SER A 478 -1  O  SER A 478   N  TYR A 413           
SHEET    1   H 6 PHE A 564  SER A 572  0                                        
SHEET    2   H 6 GLY A 575  LEU A 580 -1  O  ARG A 577   N  ASP A 570           
SHEET    3   H 6 ILE A 586  PRO A 590 -1  O  ALA A 587   N  VAL A 578           
SHEET    4   H 6 SER A 637  PRO A 642  1  O  ILE A 638   N  PHE A 588           
SHEET    5   H 6 VAL A 623  ARG A 632 -1  N  ARG A 632   O  SER A 637           
SHEET    6   H 6 PHE A 564  SER A 572 -1  N  ALA A 566   O  ILE A 624           
SHEET    1   I 3 LEU A 601  SER A 604  0                                        
SHEET    2   I 3 THR A 609  ILE A 612 -1  O  GLN A 611   N  VAL A 602           
SHEET    3   I 3 GLU A 615  LYS A 619 -1  O  VAL A 617   N  VAL A 610           
SHEET    1   J 6 ARG B  21  LYS B  27  0                                        
SHEET    2   J 6 GLY B  34  GLU B  37 -1  O  PHE B  35   N  LYS B  27           
SHEET    3   J 6 SER B  43  ILE B  46 -1  O  ILE B  46   N  GLY B  34           
SHEET    4   J 6 GLU B  71  GLU B  80  1  O  ALA B  73   N  PHE B  45           
SHEET    5   J 6 ARG B  59  SER B  66 -1  N  ARG B  59   O  VAL B  79           
SHEET    6   J 6 ARG B  21  LYS B  27 -1  N  GLY B  24   O  ILE B  60           
SHEET    1   K 6 ARG B  85  LYS B  93  0                                        
SHEET    2   K 6 ARG B  96  PRO B 101 -1  O  ALA B  98   N  GLN B  91           
SHEET    3   K 6 ILE B 110  ALA B 114 -1  O  ILE B 110   N  ILE B  99           
SHEET    4   K 6 TYR B 144  THR B 152  1  O  LEU B 147   N  ARG B 113           
SHEET    5   K 6 TRP B 127  ARG B 134 -1  N  ARG B 133   O  TYR B 144           
SHEET    6   K 6 ARG B  85  LYS B  93 -1  N  PHE B  86   O  ALA B 130           
SHEET    1   L 5 GLU B 190  ASP B 191  0                                        
SHEET    2   L 5 GLU B 299  GLU B 306  1  N  THR B 304   O  GLU B 190           
SHEET    3   L 5 VAL B 278  LEU B 288 -1  N  ARG B 279   O  ILE B 305           
SHEET    4   L 5 LYS B 221  ALA B 229 -1  N  ILE B 228   O  LEU B 282           
SHEET    5   L 5 ASP B 210  LEU B 217 -1  N  ALA B 211   O  ALA B 227           
SHEET    1   M 2 THR B 199  ASP B 201  0                                        
SHEET    2   M 2 LYS B 310  VAL B 312  1  O  LEU B 311   N  THR B 199           
SHEET    1   N 2 ASN B 252  LEU B 254  0                                        
SHEET    2   N 2 PHE B 257  ILE B 259 -1  O  PHE B 257   N  LEU B 254           
SHEET    1   O 2 ASP B 363  LEU B 368  0                                        
SHEET    2   O 2 VAL B 374  GLU B 380 -1  O  VAL B 378   N  ARG B 365           
SHEET    1   P 2 TYR B 413  VAL B 415  0                                        
SHEET    2   P 2 GLU B 476  SER B 478 -1  O  GLU B 476   N  VAL B 415           
SHEET    1   Q 6 ARG B 563  SER B 572  0                                        
SHEET    2   Q 6 GLY B 575  LEU B 580 -1  O  ARG B 579   N  GLU B 567           
SHEET    3   Q 6 ILE B 586  PRO B 590 -1  O  ILE B 589   N  MSE B 576           
SHEET    4   Q 6 SER B 637  PRO B 642  1  O  ILE B 638   N  PHE B 588           
SHEET    5   Q 6 VAL B 623  ARG B 632 -1  N  ARG B 632   O  SER B 637           
SHEET    6   Q 6 ARG B 563  SER B 572 -1  N  ALA B 566   O  ILE B 624           
SHEET    1   R 3 LEU B 601  SER B 604  0                                        
SHEET    2   R 3 THR B 609  ILE B 612 -1  O  THR B 609   N  SER B 604           
SHEET    3   R 3 GLU B 615  LYS B 619 -1  O  VAL B 617   N  VAL B 610           
SHEET    1   S 6 ARG C  21  LYS C  27  0                                        
SHEET    2   S 6 GLY C  34  ASP C  39 -1  O  PHE C  35   N  LYS C  27           
SHEET    3   S 6 LYS C  42  ILE C  46 -1  O  TYR C  44   N  LEU C  36           
SHEET    4   S 6 SER C  72  GLU C  80  1  O  ALA C  73   N  PHE C  45           
SHEET    5   S 6 ARG C  59  HIS C  65 -1  N  ILE C  61   O  GLU C  76           
SHEET    6   S 6 ARG C  21  LYS C  27 -1  N  ALA C  22   O  ALA C  62           
SHEET    1   T 6 ARG C  85  LYS C  93  0                                        
SHEET    2   T 6 ARG C  96  PRO C 101 -1  O  ALA C  98   N  GLN C  91           
SHEET    3   T 6 ILE C 110  ALA C 114 -1  O  ILE C 110   N  ILE C  99           
SHEET    4   T 6 TYR C 144  THR C 152  1  O  ALA C 145   N  PRO C 111           
SHEET    5   T 6 TRP C 127  ARG C 134 -1  N  TRP C 127   O  THR C 152           
SHEET    6   T 6 ARG C  85  LYS C  93 -1  N  GLY C  88   O  ALA C 128           
SHEET    1   U 5 GLU C 190  ASP C 191  0                                        
SHEET    2   U 5 GLU C 299  ILE C 305  1  O  ALA C 302   N  GLU C 190           
SHEET    3   U 5 ARG C 279  LEU C 288 -1  N  ARG C 279   O  ILE C 305           
SHEET    4   U 5 LYS C 221  ALA C 229 -1  N  ILE C 228   O  LEU C 282           
SHEET    5   U 5 ASP C 210  LEU C 217 -1  N  ALA C 211   O  ALA C 227           
SHEET    1   V 2 VAL C 198  ASP C 201  0                                        
SHEET    2   V 2 ALA C 309  VAL C 312  1  O  LEU C 311   N  THR C 199           
SHEET    1   W 2 ASN C 252  LEU C 254  0                                        
SHEET    2   W 2 PHE C 257  ILE C 259 -1  O  PHE C 257   N  LEU C 254           
SHEET    1   X 2 ASP C 363  LEU C 368  0                                        
SHEET    2   X 2 VAL C 374  GLU C 380 -1  O  LEU C 375   N  ILE C 367           
SHEET    1   Y 2 TYR C 413  VAL C 415  0                                        
SHEET    2   Y 2 GLU C 476  SER C 478 -1  O  SER C 478   N  TYR C 413           
SHEET    1   Z 6 ARG C 563  SER C 572  0                                        
SHEET    2   Z 6 GLY C 575  LEU C 580 -1  O  GLY C 575   N  SER C 572           
SHEET    3   Z 6 ILE C 586  PRO C 590 -1  O  ALA C 587   N  VAL C 578           
SHEET    4   Z 6 SER C 637  PRO C 642  1  O  ILE C 638   N  PHE C 588           
SHEET    5   Z 6 VAL C 623  ARG C 632 -1  N  GLU C 630   O  ILE C 639           
SHEET    6   Z 6 ARG C 563  SER C 572 -1  N  ALA C 566   O  ILE C 624           
SHEET    1  AA 3 LEU C 601  SER C 604  0                                        
SHEET    2  AA 3 THR C 609  ILE C 612 -1  O  GLN C 611   N  VAL C 602           
SHEET    3  AA 3 GLU C 615  LYS C 619 -1  O  VAL C 617   N  VAL C 610           
SHEET    1  AB 6 ARG D  21  ALA D  28  0                                        
SHEET    2  AB 6 GLY D  34  GLU D  37 -1  O  PHE D  35   N  LYS D  27           
SHEET    3  AB 6 SER D  43  ILE D  46 -1  O  ILE D  46   N  GLY D  34           
SHEET    4  AB 6 SER D  72  GLU D  80  1  O  ALA D  73   N  PHE D  45           
SHEET    5  AB 6 ARG D  59  HIS D  65 -1  N  HIS D  65   O  SER D  72           
SHEET    6  AB 6 ARG D  21  ALA D  28 -1  N  GLY D  24   O  ILE D  60           
SHEET    1  AC 6 ARG D  85  GLY D  92  0                                        
SHEET    2  AC 6 LEU D  97  PRO D 101 -1  O  ALA D  98   N  GLN D  91           
SHEET    3  AC 6 ILE D 110  ALA D 114 -1  O  CYS D 112   N  LEU D  97           
SHEET    4  AC 6 TYR D 144  THR D 152  1  O  ALA D 145   N  PRO D 111           
SHEET    5  AC 6 TRP D 127  ARG D 134 -1  N  TRP D 127   O  THR D 152           
SHEET    6  AC 6 ARG D  85  GLY D  92 -1  N  PHE D  86   O  ALA D 130           
SHEET    1  AD 6 GLU D 190  ASP D 201  0                                        
SHEET    2  AD 6 ASP D 210  ALA D 216 -1  O  LEU D 212   N  VAL D 198           
SHEET    3  AD 6 LEU D 222  ALA D 229 -1  O  GLN D 223   N  LYS D 215           
SHEET    4  AD 6 VAL D 278  LEU D 288 -1  O  LEU D 282   N  ILE D 228           
SHEET    5  AD 6 ILE D 294  VAL D 312 -1  O  GLU D 299   N  ARG D 285           
SHEET    6  AD 6 GLU D 190  ASP D 201  1  N  PHE D 197   O  LYS D 308           
SHEET    1  AE 2 ASN D 252  LEU D 254  0                                        
SHEET    2  AE 2 PHE D 257  ILE D 259 -1  O  ILE D 259   N  ASN D 252           
SHEET    1  AF 2 ASP D 363  LEU D 368  0                                        
SHEET    2  AF 2 VAL D 374  GLU D 380 -1  O  ASP D 376   N  ILE D 367           
SHEET    1  AG 2 TYR D 413  VAL D 415  0                                        
SHEET    2  AG 2 GLU D 476  SER D 478 -1  O  SER D 478   N  TYR D 413           
SHEET    1  AH 6 PHE D 564  SER D 572  0                                        
SHEET    2  AH 6 GLY D 575  LEU D 580 -1  O  ARG D 577   N  ASP D 570           
SHEET    3  AH 6 ILE D 586  PRO D 590 -1  O  ALA D 587   N  VAL D 578           
SHEET    4  AH 6 SER D 637  PRO D 642  1  O  ALA D 640   N  PHE D 588           
SHEET    5  AH 6 VAL D 623  ARG D 632 -1  N  GLU D 630   O  ILE D 639           
SHEET    6  AH 6 PHE D 564  SER D 572 -1  N  ALA D 566   O  ILE D 624           
SHEET    1  AI 3 LEU D 601  SER D 604  0                                        
SHEET    2  AI 3 THR D 609  ILE D 612 -1  O  THR D 609   N  SER D 604           
SHEET    3  AI 3 GLU D 615  LYS D 619 -1  O  GLU D 615   N  ILE D 612           
LINK         C   GLN A  50                 N   MSE A  51     1555   1555  1.33  
LINK         C   MSE A  51                 N   LYS A  52     1555   1555  1.33  
LINK         C   VAL A  54                 N   MSE A  55     1555   1555  1.32  
LINK         C   MSE A  55                 N   HIS A  56     1555   1555  1.33  
LINK         C   GLU A 131                 N   MSE A 132     1555   1555  1.35  
LINK         C   MSE A 132                 N   ARG A 133     1555   1555  1.32  
LINK         C   GLU A 181                 N   MSE A 182     1555   1555  1.33  
LINK         C   MSE A 182                 N   LEU A 183     1555   1555  1.34  
LINK         C   ASP A 207                 N   MSE A 208     1555   1555  1.33  
LINK         C   MSE A 208                 N   ASP A 209     1555   1555  1.33  
LINK         C   PRO A 260                 N   MSE A 261     1555   1555  1.33  
LINK         C   MSE A 261                 N   LEU A 262     1555   1555  1.33  
LINK         C   ARG A 285                 N   MSE A 286     1555   1555  1.33  
LINK         C   MSE A 286                 N   THR A 287     1555   1555  1.34  
LINK         C   ALA A 392                 N   MSE A 393     1555   1555  1.33  
LINK         C   MSE A 393                 N   ILE A 394     1555   1555  1.33  
LINK         C   HIS A 416                 N   MSE A 417     1555   1555  1.33  
LINK         C   MSE A 417                 N   GLY A 418     1555   1555  1.33  
LINK         C   ASP A 504                 N   MSE A 505     1555   1555  1.33  
LINK         C   MSE A 505                 N   ILE A 506     1555   1555  1.33  
LINK         C   GLN A 530                 N   MSE A 531     1555   1555  1.33  
LINK         C   MSE A 531                 N   ALA A 532     1555   1555  1.33  
LINK         C   ARG A 539                 N   MSE A 540     1555   1555  1.32  
LINK         C   MSE A 540                 N   ALA A 541     1555   1555  1.32  
LINK         C   GLY A 575                 N   MSE A 576     1555   1555  1.32  
LINK         C   MSE A 576                 N   ARG A 577     1555   1555  1.32  
LINK         C   ARG A 632                 N   MSE A 633     1555   1555  1.32  
LINK         C   MSE A 633                 N   GLU A 634     1555   1555  1.33  
LINK        MN    MN A1001                 OD1 ASP A 201     1555   1555  1.96  
LINK        MN    MN A1001                 OD1 ASP A 210     1555   1555  2.20  
LINK         C   GLN B  50                 N   MSE B  51     1555   1555  1.32  
LINK         C   MSE B  51                 N   LYS B  52     1555   1555  1.33  
LINK         C   VAL B  54                 N   MSE B  55     1555   1555  1.31  
LINK         C   MSE B  55                 N   HIS B  56     1555   1555  1.32  
LINK         C   GLU B 131                 N   MSE B 132     1555   1555  1.33  
LINK         C   MSE B 132                 N   ARG B 133     1555   1555  1.34  
LINK         C   GLU B 181                 N   MSE B 182     1555   1555  1.33  
LINK         C   MSE B 182                 N   LEU B 183     1555   1555  1.33  
LINK         C   ASP B 207                 N   MSE B 208     1555   1555  1.34  
LINK         C   MSE B 208                 N   ASP B 209     1555   1555  1.32  
LINK         C   PRO B 260                 N   MSE B 261     1555   1555  1.33  
LINK         C   MSE B 261                 N   LEU B 262     1555   1555  1.33  
LINK         C   ARG B 285                 N   MSE B 286     1555   1555  1.32  
LINK         C   MSE B 286                 N   THR B 287     1555   1555  1.32  
LINK         C   ALA B 392                 N   MSE B 393     1555   1555  1.32  
LINK         C   MSE B 393                 N   ILE B 394     1555   1555  1.32  
LINK         C   HIS B 416                 N   MSE B 417     1555   1555  1.33  
LINK         C   MSE B 417                 N   GLY B 418     1555   1555  1.33  
LINK         C   ASP B 504                 N   MSE B 505     1555   1555  1.32  
LINK         C   MSE B 505                 N   ILE B 506     1555   1555  1.33  
LINK         C   GLN B 530                 N   MSE B 531     1555   1555  1.33  
LINK         C   MSE B 531                 N   ALA B 532     1555   1555  1.33  
LINK         C   ARG B 539                 N   MSE B 540     1555   1555  1.34  
LINK         C   MSE B 540                 N   ALA B 541     1555   1555  1.34  
LINK         C   GLY B 575                 N   MSE B 576     1555   1555  1.30  
LINK         C   MSE B 576                 N   ARG B 577     1555   1555  1.33  
LINK         C   ARG B 632                 N   MSE B 633     1555   1555  1.32  
LINK         C   MSE B 633                 N   GLU B 634     1555   1555  1.32  
LINK        MN    MN B1002                 OD1 ASP B 210     1555   1555  1.97  
LINK        MN    MN B1002                 OD1 ASP B 201     1555   1555  2.34  
LINK         C   GLN C  50                 N   MSE C  51     1555   1555  1.34  
LINK         C   MSE C  51                 N   LYS C  52     1555   1555  1.34  
LINK         C   VAL C  54                 N   MSE C  55     1555   1555  1.31  
LINK         C   MSE C  55                 N   HIS C  56     1555   1555  1.33  
LINK         C   GLU C 131                 N   MSE C 132     1555   1555  1.33  
LINK         C   MSE C 132                 N   ARG C 133     1555   1555  1.32  
LINK         C   GLU C 181                 N   MSE C 182     1555   1555  1.34  
LINK         C   MSE C 182                 N   LEU C 183     1555   1555  1.33  
LINK         C   ASP C 207                 N   MSE C 208     1555   1555  1.33  
LINK         C   MSE C 208                 N   ASP C 209     1555   1555  1.33  
LINK         C   PRO C 260                 N   MSE C 261     1555   1555  1.33  
LINK         C   MSE C 261                 N   LEU C 262     1555   1555  1.34  
LINK         C   ARG C 285                 N   MSE C 286     1555   1555  1.32  
LINK         C   MSE C 286                 N   THR C 287     1555   1555  1.33  
LINK         C   ALA C 392                 N   MSE C 393     1555   1555  1.33  
LINK         C   MSE C 393                 N   ILE C 394     1555   1555  1.33  
LINK         C   HIS C 416                 N   MSE C 417     1555   1555  1.33  
LINK         C   MSE C 417                 N   GLY C 418     1555   1555  1.33  
LINK         C   ASP C 504                 N   MSE C 505     1555   1555  1.32  
LINK         C   MSE C 505                 N   ILE C 506     1555   1555  1.34  
LINK         C   GLN C 530                 N   MSE C 531     1555   1555  1.34  
LINK         C   MSE C 531                 N   ALA C 532     1555   1555  1.33  
LINK         C   ARG C 539                 N   MSE C 540     1555   1555  1.32  
LINK         C   MSE C 540                 N   ALA C 541     1555   1555  1.34  
LINK         C   GLY C 575                 N   MSE C 576     1555   1555  1.33  
LINK         C   MSE C 576                 N   ARG C 577     1555   1555  1.33  
LINK         C   ARG C 632                 N   MSE C 633     1555   1555  1.33  
LINK         C   MSE C 633                 N   GLU C 634     1555   1555  1.32  
LINK        MN    MN C1003                 OD1 ASP C 201     1555   1555  2.37  
LINK        MN    MN C1003                 OD1 ASP C 210     1555   1555  2.13  
LINK         C   GLN D  50                 N   MSE D  51     1555   1555  1.33  
LINK         C   MSE D  51                 N   LYS D  52     1555   1555  1.33  
LINK         C   VAL D  54                 N   MSE D  55     1555   1555  1.33  
LINK         C   MSE D  55                 N   HIS D  56     1555   1555  1.33  
LINK         C   GLU D 131                 N   MSE D 132     1555   1555  1.33  
LINK         C   MSE D 132                 N   ARG D 133     1555   1555  1.33  
LINK         C   GLU D 181                 N   MSE D 182     1555   1555  1.33  
LINK         C   MSE D 182                 N   LEU D 183     1555   1555  1.33  
LINK         C   ASP D 207                 N   MSE D 208     1555   1555  1.32  
LINK         C   MSE D 208                 N   ASP D 209     1555   1555  1.33  
LINK         C   PRO D 260                 N   MSE D 261     1555   1555  1.32  
LINK         C   MSE D 261                 N   LEU D 262     1555   1555  1.35  
LINK         C   ARG D 285                 N   MSE D 286     1555   1555  1.32  
LINK         C   MSE D 286                 N   THR D 287     1555   1555  1.35  
LINK         C   ALA D 392                 N   MSE D 393     1555   1555  1.34  
LINK         C   MSE D 393                 N   ILE D 394     1555   1555  1.34  
LINK         C   HIS D 416                 N   MSE D 417     1555   1555  1.33  
LINK         C   MSE D 417                 N   GLY D 418     1555   1555  1.33  
LINK         C   ASP D 504                 N   MSE D 505     1555   1555  1.33  
LINK         C   MSE D 505                 N   ILE D 506     1555   1555  1.34  
LINK         C   GLN D 530                 N   MSE D 531     1555   1555  1.34  
LINK         C   MSE D 531                 N   ALA D 532     1555   1555  1.33  
LINK         C   ARG D 539                 N   MSE D 540     1555   1555  1.33  
LINK         C   MSE D 540                 N   ALA D 541     1555   1555  1.32  
LINK         C   GLY D 575                 N   MSE D 576     1555   1555  1.34  
LINK         C   MSE D 576                 N   ARG D 577     1555   1555  1.33  
LINK         C   ARG D 632                 N   MSE D 633     1555   1555  1.33  
LINK         C   MSE D 633                 N   GLU D 634     1555   1555  1.33  
LINK        MN    MN D1004                 OD1 ASP D 201     1555   1555  2.10  
LINK        MN    MN D1004                 OD1 ASP D 210     1555   1555  2.32  
LINK        MN    MN D1004                 OD1 ASP D 209     1555   1555  2.44  
SITE     1 AC1  3 ASP A 201  ASP A 209  ASP A 210                               
SITE     1 AC2  3 ASP B 201  ASP B 209  ASP B 210                               
SITE     1 AC3  3 ASP C 201  ASP C 209  ASP C 210                               
SITE     1 AC4  3 ASP D 201  ASP D 209  ASP D 210                               
CRYST1   55.760  118.430  122.380 107.80  98.36  91.40 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      0.017934  0.000438  0.002919        0.00000                         
SCALE2      0.000000  0.008446  0.002780        0.00000                         
SCALE3      0.000000  0.000000  0.008695        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system