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Database: PDB
Entry: 2WAQ
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Original site: 2WAQ 
HEADER    TRANSCRIPTION                           11-FEB-09   2WAQ              
TITLE     THE COMPLETE STRUCTURE OF THE ARCHAEAL 13-SUBUNIT DNA-DIRECTED RNA    
TITLE    2 POLYMERASE                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO1N SUBUNIT;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO2 SUBUNIT;                  
COMPND   6 CHAIN: B;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO1C SUBUNIT;                 
COMPND   9 CHAIN: C;                                                            
COMPND  10 MOL_ID: 4;                                                           
COMPND  11 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO3 SUBUNIT;                  
COMPND  12 CHAIN: D;                                                            
COMPND  13 MOL_ID: 5;                                                           
COMPND  14 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO7 SUBUNIT;                  
COMPND  15 CHAIN: E;                                                            
COMPND  16 MOL_ID: 6;                                                           
COMPND  17 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO4 SUBUNIT;                  
COMPND  18 CHAIN: F;                                                            
COMPND  19 MOL_ID: 7;                                                           
COMPND  20 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO8 SUBUNIT;                  
COMPND  21 CHAIN: G;                                                            
COMPND  22 MOL_ID: 8;                                                           
COMPND  23 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO5 SUBUNIT;                  
COMPND  24 CHAIN: H;                                                            
COMPND  25 MOL_ID: 9;                                                           
COMPND  26 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO6 SUBUNIT;                  
COMPND  27 CHAIN: K;                                                            
COMPND  28 MOL_ID: 10;                                                          
COMPND  29 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO11 SUBUNIT;                 
COMPND  30 CHAIN: L;                                                            
COMPND  31 MOL_ID: 11;                                                          
COMPND  32 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO10 SUBUNIT;                 
COMPND  33 CHAIN: N;                                                            
COMPND  34 MOL_ID: 12;                                                          
COMPND  35 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO12 SUBUNIT;                 
COMPND  36 CHAIN: P;                                                            
COMPND  37 MOL_ID: 13;                                                          
COMPND  38 MOLECULE: DNA-DIRECTED RNA POLYMERASE RPO13 SUBUNIT;                 
COMPND  39 CHAIN: Q                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;                            
SOURCE   3 ORGANISM_TAXID: 2286;                                                
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;                            
SOURCE   6 ORGANISM_TAXID: 2286;                                                
SOURCE   7 MOL_ID: 3;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;                            
SOURCE   9 ORGANISM_TAXID: 2286;                                                
SOURCE  10 MOL_ID: 4;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;                            
SOURCE  12 ORGANISM_TAXID: 2286;                                                
SOURCE  13 MOL_ID: 5;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;                            
SOURCE  15 ORGANISM_TAXID: 2286;                                                
SOURCE  16 MOL_ID: 6;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;                            
SOURCE  18 ORGANISM_TAXID: 2286;                                                
SOURCE  19 MOL_ID: 7;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;                            
SOURCE  21 ORGANISM_TAXID: 2286;                                                
SOURCE  22 MOL_ID: 8;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;                            
SOURCE  24 ORGANISM_TAXID: 2286;                                                
SOURCE  25 MOL_ID: 9;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;                            
SOURCE  27 ORGANISM_TAXID: 2286;                                                
SOURCE  28 MOL_ID: 10;                                                          
SOURCE  29 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;                            
SOURCE  30 ORGANISM_TAXID: 2286;                                                
SOURCE  31 MOL_ID: 11;                                                          
SOURCE  32 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;                            
SOURCE  33 ORGANISM_TAXID: 2286;                                                
SOURCE  34 MOL_ID: 12;                                                          
SOURCE  35 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;                            
SOURCE  36 ORGANISM_TAXID: 2286;                                                
SOURCE  37 MOL_ID: 13;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: SULFOLOBUS SHIBATAE;                            
SOURCE  39 ORGANISM_TAXID: 2286                                                 
KEYWDS    MULTI-SUBUNIT, RNA POLYMERASE, TRANSCRIPTION                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.KORKHIN,U.M.UNLIGIL,O.LITTLEFIELD,P.J.NELSON,D.I.STUART,P.B.SIGLER, 
AUTHOR   2 S.D.BELL,N.G.A.ABRESCIA                                              
REVDAT   5   13-DEC-23 2WAQ    1       REMARK                                   
REVDAT   4   28-APR-21 2WAQ    1       REMARK LINK                              
REVDAT   3   28-AUG-19 2WAQ    1       JRNL   REMARK                            
REVDAT   2   30-JAN-19 2WAQ    1       JRNL   REMARK                            
REVDAT   1   19-MAY-09 2WAQ    0                                                
JRNL        AUTH   Y.KORKHIN,U.M.UNLIGIL,O.LITTLEFIELD,P.J.NELSON,D.I.STUART,   
JRNL        AUTH 2 P.B.SIGLER,S.D.BELL,N.G.ABRESCIA                             
JRNL        TITL   EVOLUTION OF COMPLEX RNA POLYMERASES: THE COMPLETE ARCHAEAL  
JRNL        TITL 2 RNA POLYMERASE STRUCTURE.                                    
JRNL        REF    PLOS BIOL.                    V.   7 00102 2009              
JRNL        REFN                   ESSN 1545-7885                               
JRNL        PMID   19419240                                                     
JRNL        DOI    10.1371/JOURNAL.PBIO.1000102                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 77.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 56389                          
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) : 0.274                           
REMARK   3   R VALUE            (WORKING SET) : 0.271                           
REMARK   3   FREE R VALUE                     : 0.341                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3012                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.44                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2580                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 129                          
REMARK   3   BIN FREE R VALUE                    : 0.3420                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 26454                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 17                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 88.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.94000                                              
REMARK   3    B22 (A**2) : -0.90000                                             
REMARK   3    B33 (A**2) : -0.04000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.869         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.652         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 87.522        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.857                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.769                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 26946 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 36436 ; 1.027 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3313 ; 4.881 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1189 ;36.250 ;23.743       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5003 ;17.898 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   220 ;13.904 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4160 ; 0.066 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 19918 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 12722 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 18153 ; 0.296 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   656 ; 0.123 ; 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):    48 ; 0.114 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     1 ; 0.005 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. THE REFINEMENT HAS ALSO BEEN CARRIED OUT USING NORMAL-   
REMARK   3  MODE TO ANISOTROPICALLY REFINE THE OVERALL THERMAL MOTIONS.         
REMARK   3  PLEASE SEE ARTICLE FOR MORE DETAILS.                                
REMARK   4                                                                      
REMARK   4 2WAQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-FEB-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290038536.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59401                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 77.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 44.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: GLRF, MOLREP, SOLVE                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1EN0                                       
REMARK 200                                                                      
REMARK 200 REMARK: THE STATISTICS FOR THIS DATA ARE DERIVED FROM MERGED IOBS    
REMARK 200  AND SIGMAIOBS PRESENT IN THE ONLY MTZ AVAILABLE. RAW IMAGES         
REMARK 200  COLLECTED IN 2001-2002 AND PROCESSING LOG-FILES HAVE BEEN LOST.     
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 7MG/ML ENZYME, 150MM KCL, 100MM SRCL2,   
REMARK 280  1MM ZNCL2, 100MM CACODYLATE PH 6.5, 12% PEG MME 5K, 5% GLYCEROL,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       96.75050            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      106.31000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       96.75050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      106.31000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: TRIDECAMERIC                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIDECAMERIC               
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 71970 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 172810 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -446.1 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, K, L,         
REMARK 350                    AND CHAINS: N, P, Q                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     ASP A    31                                                      
REMARK 465     VAL A    32                                                      
REMARK 465     TYR A    33                                                      
REMARK 465     ASP A    34                                                      
REMARK 465     GLU A    35                                                      
REMARK 465     ASP A    36                                                      
REMARK 465     GLY A    37                                                      
REMARK 465     THR A    38                                                      
REMARK 465     PRO A    39                                                      
REMARK 465     ILE A    40                                                      
REMARK 465     GLU A    41                                                      
REMARK 465     LYS A   157                                                      
REMARK 465     LEU A   158                                                      
REMARK 465     GLU A   159                                                      
REMARK 465     LYS A   160                                                      
REMARK 465     PRO A   161                                                      
REMARK 465     TYR A   162                                                      
REMARK 465     ASN A   163                                                      
REMARK 465     PHE A   164                                                      
REMARK 465     TYR A   165                                                      
REMARK 465     GLU A   166                                                      
REMARK 465     GLU A   167                                                      
REMARK 465     ARG A   168                                                      
REMARK 465     LYS A   169                                                      
REMARK 465     GLU A   170                                                      
REMARK 465     GLY A   171                                                      
REMARK 465     VAL A   172                                                      
REMARK 465     ALA A   173                                                      
REMARK 465     LYS A   174                                                      
REMARK 465     ILE A   225                                                      
REMARK 465     GLU A   226                                                      
REMARK 465     SER A   227                                                      
REMARK 465     GLY A   228                                                      
REMARK 465     ILE A   229                                                      
REMARK 465     ARG A   230                                                      
REMARK 465     THR A   880                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     GLY B   198                                                      
REMARK 465     TYR B   199                                                      
REMARK 465     GLU B   509                                                      
REMARK 465     GLY B   510                                                      
REMARK 465     GLY B   511                                                      
REMARK 465     GLU B   512                                                      
REMARK 465     ASP B   513                                                      
REMARK 465     GLN B   514                                                      
REMARK 465     ASN B   515                                                      
REMARK 465     GLU B   516                                                      
REMARK 465     TYR B   517                                                      
REMARK 465     LEU B   518                                                      
REMARK 465     ARG B   821                                                      
REMARK 465     PHE B   822                                                      
REMARK 465     LEU B   823                                                      
REMARK 465     GLN B   824                                                      
REMARK 465     GLU B   825                                                      
REMARK 465     PHE B   826                                                      
REMARK 465     LYS B   827                                                      
REMARK 465     GLU B   828                                                      
REMARK 465     LEU B   829                                                      
REMARK 465     SER B   830                                                      
REMARK 465     PRO B   831                                                      
REMARK 465     GLU B   832                                                      
REMARK 465     GLN B   833                                                      
REMARK 465     GLY B  1123                                                      
REMARK 465     LEU B  1124                                                      
REMARK 465     SER B  1125                                                      
REMARK 465     GLY B  1126                                                      
REMARK 465     GLY B  1127                                                      
REMARK 465     LYS B  1128                                                      
REMARK 465     GLY B  1129                                                      
REMARK 465     ASN B  1130                                                      
REMARK 465     GLU B  1131                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     ASN C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     ILE C     5                                                      
REMARK 465     ASP C     6                                                      
REMARK 465     GLU C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     ASP C     9                                                      
REMARK 465     LYS C    10                                                      
REMARK 465     MET C    85                                                      
REMARK 465     THR C    86                                                      
REMARK 465     LEU C    87                                                      
REMARK 465     ARG C    88                                                      
REMARK 465     THR C    89                                                      
REMARK 465     PHE C    90                                                      
REMARK 465     HIS C    91                                                      
REMARK 465     PHE C    92                                                      
REMARK 465     ALA C    93                                                      
REMARK 465     GLY C    94                                                      
REMARK 465     ILE C    95                                                      
REMARK 465     ARG C    96                                                      
REMARK 465     GLU C    97                                                      
REMARK 465     LEU C    98                                                      
REMARK 465     ASN C    99                                                      
REMARK 465     VAL C   100                                                      
REMARK 465     THR C   101                                                      
REMARK 465     ARG C   395                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D    86                                                      
REMARK 465     GLU D    87                                                      
REMARK 465     ASN D    88                                                      
REMARK 465     LYS D   265                                                      
REMARK 465     THR E   154                                                      
REMARK 465     GLY E   155                                                      
REMARK 465     ARG E   156                                                      
REMARK 465     ALA E   178                                                      
REMARK 465     LYS E   179                                                      
REMARK 465     LYS E   180                                                      
REMARK 465     MET F     1                                                      
REMARK 465     SER F     2                                                      
REMARK 465     ARG F    93                                                      
REMARK 465     THR F    94                                                      
REMARK 465     TYR F    95                                                      
REMARK 465     THR F    96                                                      
REMARK 465     SER F    97                                                      
REMARK 465     GLU F    98                                                      
REMARK 465     ASP F    99                                                      
REMARK 465     ILE F   100                                                      
REMARK 465     GLN F   101                                                      
REMARK 465     LYS F   102                                                      
REMARK 465     ILE F   103                                                      
REMARK 465     ILE F   104                                                      
REMARK 465     ASP F   105                                                      
REMARK 465     ILE F   106                                                      
REMARK 465     ILE F   107                                                      
REMARK 465     ARG F   108                                                      
REMARK 465     LYS F   109                                                      
REMARK 465     TYR F   110                                                      
REMARK 465     ILE F   111                                                      
REMARK 465     LYS F   112                                                      
REMARK 465     SER F   113                                                      
REMARK 465     MET G     1                                                      
REMARK 465     MET G     2                                                      
REMARK 465     GLU G     3                                                      
REMARK 465     SER G     4                                                      
REMARK 465     LEU G   118                                                      
REMARK 465     ASN G   119                                                      
REMARK 465     VAL G   120                                                      
REMARK 465     MET G   121                                                      
REMARK 465     ASP G   122                                                      
REMARK 465     HIS G   123                                                      
REMARK 465     ILE G   124                                                      
REMARK 465     TYR G   125                                                      
REMARK 465     PHE G   126                                                      
REMARK 465     CYS G   127                                                      
REMARK 465     VAL G   128                                                      
REMARK 465     LYS G   129                                                      
REMARK 465     LYS G   130                                                      
REMARK 465     ASN G   131                                                      
REMARK 465     THR G   132                                                      
REMARK 465     MET H     1                                                      
REMARK 465     ARG H     2                                                      
REMARK 465     GLY H     3                                                      
REMARK 465     SER H     4                                                      
REMARK 465     SER H     5                                                      
REMARK 465     ASN H     6                                                      
REMARK 465     ARG H     7                                                      
REMARK 465     LYS H     8                                                      
REMARK 465     SER H    83                                                      
REMARK 465     GLY H    84                                                      
REMARK 465     MET K     1                                                      
REMARK 465     GLY K     2                                                      
REMARK 465     LEU K     3                                                      
REMARK 465     GLU K     4                                                      
REMARK 465     ARG K     5                                                      
REMARK 465     ASP K     6                                                      
REMARK 465     GLY K     7                                                      
REMARK 465     ILE K     8                                                      
REMARK 465     LEU K     9                                                      
REMARK 465     SER K    10                                                      
REMARK 465     ARG K    93                                                      
REMARK 465     LYS K    94                                                      
REMARK 465     SER K    95                                                      
REMARK 465     LYS L    92                                                      
REMARK 465     PRO N    65                                                      
REMARK 465     ILE N    66                                                      
REMARK 465     MET P     1                                                      
REMARK 465     ALA P     2                                                      
REMARK 465     VAL P     3                                                      
REMARK 465     TYR P     4                                                      
REMARK 465     ARG P     5                                                      
REMARK 465     MET Q     1                                                      
REMARK 465     VAL Q     2                                                      
REMARK 465     SER Q     3                                                      
REMARK 465     GLY Q     4                                                      
REMARK 465     MET Q     5                                                      
REMARK 465     SER Q     6                                                      
REMARK 465     THR Q     7                                                      
REMARK 465     GLU Q     8                                                      
REMARK 465     GLU Q     9                                                      
REMARK 465     GLU Q    10                                                      
REMARK 465     LYS Q    11                                                      
REMARK 465     GLU Q    12                                                      
REMARK 465     GLY Q    13                                                      
REMARK 465     THR Q    14                                                      
REMARK 465     ASN Q    15                                                      
REMARK 465     ASP Q    16                                                      
REMARK 465     GLU Q    17                                                      
REMARK 465     GLU Q    18                                                      
REMARK 465     VAL Q    19                                                      
REMARK 465     SER Q    20                                                      
REMARK 465     GLU Q    21                                                      
REMARK 465     GLU Q    22                                                      
REMARK 465     ARG Q    23                                                      
REMARK 465     GLU Q    24                                                      
REMARK 465     VAL Q    25                                                      
REMARK 465     GLU Q    26                                                      
REMARK 465     GLU Q    27                                                      
REMARK 465     THR Q    28                                                      
REMARK 465     SER Q    29                                                      
REMARK 465     GLU Q    30                                                      
REMARK 465     GLU Q    31                                                      
REMARK 465     GLU Q    32                                                      
REMARK 465     PHE Q    33                                                      
REMARK 465     PRO Q    34                                                      
REMARK 465     LYS Q    35                                                      
REMARK 465     LEU Q    36                                                      
REMARK 465     SER Q    37                                                      
REMARK 465     LYS Q    83                                                      
REMARK 465     ALA Q    84                                                      
REMARK 465     LYS Q    85                                                      
REMARK 465     LYS Q    86                                                      
REMARK 465     ALA Q    87                                                      
REMARK 465     ALA Q    88                                                      
REMARK 465     SER Q    89                                                      
REMARK 465     LYS Q    90                                                      
REMARK 465     LYS Q    91                                                      
REMARK 465     VAL Q    92                                                      
REMARK 465     LYS Q    93                                                      
REMARK 465     LYS Q    94                                                      
REMARK 465     THR Q    95                                                      
REMARK 465     LYS Q    96                                                      
REMARK 465     LYS Q    97                                                      
REMARK 465     LYS Q    98                                                      
REMARK 465     GLU Q    99                                                      
REMARK 465     LYS Q   100                                                      
REMARK 465     SER Q   101                                                      
REMARK 465     VAL Q   102                                                      
REMARK 465     GLU Q   103                                                      
REMARK 465     GLY Q   104                                                      
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     ILE A 223    CG1  CG2  CD1                                       
REMARK 470     MET A 224    CG   SD   CE                                        
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    MET A  22      -38.56     63.80                                   
REMARK 500    ILE A  27      -47.06   -134.17                                   
REMARK 500    VAL A  44       73.19   -100.04                                   
REMARK 500    MET A  45      -40.46   -170.76                                   
REMARK 500    ASP A  46      -68.29   -108.73                                   
REMARK 500    ARG A  48        0.13     88.40                                   
REMARK 500    GLU A  53      152.66     66.39                                   
REMARK 500    GLN A  56     -147.90   -118.89                                   
REMARK 500    CYS A  61      -91.19   -142.35                                   
REMARK 500    LEU A  65     -172.48     63.69                                   
REMARK 500    ARG A  79       95.51     86.56                                   
REMARK 500    PRO A  80      150.76    -49.48                                   
REMARK 500    ARG A  99      -33.34     82.23                                   
REMARK 500    CYS A 101     -120.31   -129.05                                   
REMARK 500    ARG A 103      -63.15     50.18                                   
REMARK 500    ILE A 106     -108.69   -110.71                                   
REMARK 500    TYR A 118       47.76    -96.82                                   
REMARK 500    LYS A 142      -58.66   -122.38                                   
REMARK 500    ALA A 143     -106.88     56.30                                   
REMARK 500    VAL A 145       83.51   -152.82                                   
REMARK 500    PRO A 147       59.44    -94.98                                   
REMARK 500    HIS A 148      177.23     62.85                                   
REMARK 500    GLU A 151     -107.26   -142.75                                   
REMARK 500    LYS A 155      148.16    -37.33                                   
REMARK 500    THR A 200      -62.71   -107.97                                   
REMARK 500    SER A 252       38.56    -98.47                                   
REMARK 500    ALA A 257       99.54     66.81                                   
REMARK 500    PHE A 277      -72.07    -75.54                                   
REMARK 500    GLU A 280      -45.35   -173.17                                   
REMARK 500    PRO A 282      177.11    -57.07                                   
REMARK 500    LEU A 284       66.99     39.93                                   
REMARK 500    SER A 287      111.13     65.78                                   
REMARK 500    ARG A 290      -86.68     61.97                                   
REMARK 500    ARG A 308      -76.58     65.76                                   
REMARK 500    ILE A 332      136.12     66.65                                   
REMARK 500    PRO A 355        3.77    -61.29                                   
REMARK 500    ASP A 393      108.48     63.92                                   
REMARK 500    ASP A 413      100.97    -57.50                                   
REMARK 500    VAL A 449       46.39   -100.16                                   
REMARK 500    PHE A 457       77.00   -113.41                                   
REMARK 500    ASP A 458       17.74   -142.46                                   
REMARK 500    LYS A 477      -34.38   -132.25                                   
REMARK 500    ALA A 499      -77.90    -77.34                                   
REMARK 500    GLN A 500      -50.12   -144.76                                   
REMARK 500    LYS A 531       41.07    -99.12                                   
REMARK 500    GLU A 536      114.16     64.07                                   
REMARK 500    ALA A 541      -81.96    -68.04                                   
REMARK 500    ALA A 554       44.37    -83.11                                   
REMARK 500    PHE A 555      -25.17   -140.79                                   
REMARK 500    LYS A 558       20.76    -78.46                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     339 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  58   SG                                                     
REMARK 620 2 CYS A  68   SG  118.8                                              
REMARK 620 3 HIS A  71   NE2 101.0 136.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1400  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 456   OD1                                                    
REMARK 620 2 ASP A 458   OD1  71.0                                              
REMARK 620 3 ASP A 460   OD1  62.1  75.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B1064   SG                                                     
REMARK 620 2 CYS B1067   SG  109.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S D1001  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 203   SG                                                     
REMARK 620 2 F3S D1001   S1  128.3                                              
REMARK 620 3 F3S D1001   S3  103.2 108.6                                        
REMARK 620 4 F3S D1001   S4  121.6  85.7 108.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S D1001  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 206   SG                                                     
REMARK 620 2 F3S D1001   S2   94.3                                              
REMARK 620 3 F3S D1001   S3  114.2 108.3                                        
REMARK 620 4 F3S D1001   S4  134.2  88.5 108.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S D1001  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 209   SG                                                     
REMARK 620 2 F3S D1001   S1  122.4                                              
REMARK 620 3 F3S D1001   S2  107.5  84.0                                        
REMARK 620 4 F3S D1001   S3  119.4 108.6 108.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN N 100  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N   7   SG                                                     
REMARK 620 2 CYS N  10   SG  100.4                                              
REMARK 620 3 CYS N  45   SG  131.6  54.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN P  50  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS P   9   SG                                                     
REMARK 620 2 THR P  12   OG1 118.6                                              
REMARK 620 3 CYS P  29   SG  127.4 113.2                                        
REMARK 620 N                    1     2                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEETS PRESENTED AS "BJ" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1350                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1360                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1400                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1400                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C1000                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S D1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN N 100                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN P 50                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WB1   RELATED DB: PDB                                   
REMARK 900 THE COMPLETE STRUCTURE OF THE ARCHAEAL 13- SUBUNIT DNA-DIRECTED RNA  
REMARK 900 POLYMERASE                                                           
DBREF  2WAQ A    1   880  PDB    2WAQ     2WAQ             1    880             
DBREF  2WAQ B    1  1131  PDB    2WAQ     2WAQ             1   1131             
DBREF  2WAQ C    1   395  PDB    2WAQ     2WAQ             1    395             
DBREF  2WAQ D    1   265  PDB    2WAQ     2WAQ             1    265             
DBREF  2WAQ E    1   180  PDB    2WAQ     2WAQ             1    180             
DBREF  2WAQ F    1   113  PDB    2WAQ     2WAQ             1    113             
DBREF  2WAQ G    1   132  PDB    2WAQ     2WAQ             1    132             
DBREF  2WAQ H    1    84  PDB    2WAQ     2WAQ             1     84             
DBREF  2WAQ K    1    95  PDB    2WAQ     2WAQ             1     95             
DBREF  2WAQ L    1    92  PDB    2WAQ     2WAQ             1     92             
DBREF  2WAQ N    1    66  PDB    2WAQ     2WAQ             1     66             
DBREF  2WAQ P    1    48  PDB    2WAQ     2WAQ             1     48             
DBREF  2WAQ Q    1   104  PDB    2WAQ     2WAQ             1    104             
SEQRES   1 A  880  MET SER GLU LYS ASN ILE LYS GLY ILE LYS PHE GLY ILE          
SEQRES   2 A  880  LEU SER PRO ASP GLU ILE ARG LYS MET SER VAL THR ALA          
SEQRES   3 A  880  ILE ILE THR PRO ASP VAL TYR ASP GLU ASP GLY THR PRO          
SEQRES   4 A  880  ILE GLU GLY SER VAL MET ASP PRO ARG LEU GLY VAL ILE          
SEQRES   5 A  880  GLU PRO GLY GLN LYS CYS PRO THR CYS GLY ASN THR LEU          
SEQRES   6 A  880  GLY ASN CYS PRO GLY HIS PHE GLY HIS ILE GLU LEU VAL          
SEQRES   7 A  880  ARG PRO VAL ILE HIS VAL GLY PHE VAL LYS HIS VAL TYR          
SEQRES   8 A  880  GLU PHE LEU LYS ALA THR CYS ARG ARG CYS GLY ARG VAL          
SEQRES   9 A  880  LYS ILE SER GLU ASP GLU ILE GLU LYS TYR SER ARG ILE          
SEQRES  10 A  880  TYR ASN ALA ILE LYS LYS ARG TRP PRO SER ALA ALA ARG          
SEQRES  11 A  880  ARG LEU THR GLU TYR VAL LYS LYS THR ALA MET LYS ALA          
SEQRES  12 A  880  GLN VAL CYS PRO HIS CYS GLY GLU LYS GLN PHE LYS ILE          
SEQRES  13 A  880  LYS LEU GLU LYS PRO TYR ASN PHE TYR GLU GLU ARG LYS          
SEQRES  14 A  880  GLU GLY VAL ALA LYS LEU THR PRO SER ASP ILE ARG GLU          
SEQRES  15 A  880  ARG LEU GLU LYS VAL PRO GLU SER ASP VAL GLU ILE LEU          
SEQRES  16 A  880  GLY TYR ASP PRO THR THR SER ARG PRO GLU TRP MET ILE          
SEQRES  17 A  880  LEU THR VAL LEU PRO VAL PRO PRO ILE THR ILE ARG PRO          
SEQRES  18 A  880  SER ILE MET ILE GLU SER GLY ILE ARG ALA GLU ASP ASP          
SEQRES  19 A  880  LEU THR HIS LYS LEU VAL ASP ILE VAL ARG ILE ASN GLU          
SEQRES  20 A  880  ARG LEU LYS GLU SER ILE ASP ALA GLY ALA PRO GLN LEU          
SEQRES  21 A  880  ILE ILE GLU ASP LEU TRP ASP LEU LEU GLN TYR HIS VAL          
SEQRES  22 A  880  ALA THR TYR PHE ASP ASN GLU ILE PRO GLY LEU PRO PRO          
SEQRES  23 A  880  SER LYS HIS ARG SER GLY ARG PRO LEU ARG THR LEU ALA          
SEQRES  24 A  880  GLN ARG LEU LYS GLY LYS GLU GLY ARG PHE ARG GLY ASN          
SEQRES  25 A  880  LEU SER GLY LYS ARG VAL ASP PHE SER SER ARG THR VAL          
SEQRES  26 A  880  ILE SER PRO ASP PRO ASN ILE SER ILE ASP GLU VAL GLY          
SEQRES  27 A  880  VAL PRO GLU ILE ILE ALA ARG THR LEU THR VAL PRO GLU          
SEQRES  28 A  880  ARG ILE THR PRO TRP ASN ILE GLU LYS LEU ARG GLN PHE          
SEQRES  29 A  880  VAL ILE ASN GLY PRO ASP LYS TRP PRO GLY ALA ASN TYR          
SEQRES  30 A  880  VAL ILE ARG PRO ASP GLY ARG ARG ILE ASP LEU ARG TYR          
SEQRES  31 A  880  VAL LYS ASP ARG LYS GLU LEU ALA SER THR LEU ALA PRO          
SEQRES  32 A  880  GLY TYR VAL VAL GLU ARG HIS LEU THR ASP GLY ASP VAL          
SEQRES  33 A  880  VAL LEU PHE ASN ARG GLN PRO SER LEU HIS ARG ILE SER          
SEQRES  34 A  880  MET MET ALA HIS ARG VAL ARG VAL LEU LYS GLY LEU THR          
SEQRES  35 A  880  PHE ARG LEU ASN LEU LEU VAL CYS PRO PRO TYR ASN ALA          
SEQRES  36 A  880  ASP PHE ASP GLY ASP GLU MET ASN LEU HIS VAL PRO GLN          
SEQRES  37 A  880  SER GLU GLU ALA ILE ALA GLU ALA LYS GLU ILE MET LEU          
SEQRES  38 A  880  VAL HIS LYS ASN ILE ILE THR PRO ARG TYR GLY GLY PRO          
SEQRES  39 A  880  ILE ILE GLY ALA ALA GLN ASP TYR ILE SER GLY ALA TYR          
SEQRES  40 A  880  LEU LEU THR VAL LYS THR THR LEU LEU THR LYS GLU GLU          
SEQRES  41 A  880  ALA GLN GLN ILE LEU GLY VAL ALA ASP VAL LYS ILE ASP          
SEQRES  42 A  880  LEU GLY GLU PRO ALA ILE LEU ALA PRO ARG GLU TYR TYR          
SEQRES  43 A  880  THR GLY LYS GLN VAL VAL SER ALA PHE LEU PRO LYS ASP          
SEQRES  44 A  880  PHE ASN PHE HIS GLY GLN ALA ASN VAL SER SER GLY PRO          
SEQRES  45 A  880  ARG LEU CYS LYS ASN GLU ASP CYS PRO HIS ASP SER TYR          
SEQRES  46 A  880  VAL VAL ILE LYS ASN GLY ILE LEU LEU GLU GLY VAL PHE          
SEQRES  47 A  880  ASP LYS LYS ALA ILE GLY ASN GLN GLN PRO GLU SER ILE          
SEQRES  48 A  880  LEU HIS TRP LEU ILE LYS GLU TYR SER ASP GLU TYR GLY          
SEQRES  49 A  880  LYS TRP LEU MET ASP ASN LEU PHE ARG VAL PHE ILE ARG          
SEQRES  50 A  880  PHE VAL GLU LEU GLN GLY PHE THR MET ARG LEU GLU ASP          
SEQRES  51 A  880  VAL SER LEU GLY ASP ASP VAL LYS LYS GLU ILE TYR ASN          
SEQRES  52 A  880  GLU ILE ASP ARG ALA LYS VAL GLU VAL ASP ASN LEU ILE          
SEQRES  53 A  880  GLN LYS TYR LYS ASN GLY GLU LEU GLU PRO ILE PRO GLY          
SEQRES  54 A  880  ARG THR LEU GLU GLU SER LEU GLU ASN TYR ILE LEU ASP          
SEQRES  55 A  880  THR LEU ASP LYS LEU ARG SER THR ALA GLY ASP ILE ALA          
SEQRES  56 A  880  SER LYS TYR LEU ASP PRO PHE ASN PHE ALA TYR VAL MET          
SEQRES  57 A  880  ALA ARG THR GLY ALA ARG GLY SER VAL LEU ASN ILE THR          
SEQRES  58 A  880  GLN MET ALA ALA MET LEU GLY GLN GLN SER VAL ARG GLY          
SEQRES  59 A  880  GLU ARG ILE LYS ARG GLY TYR MET THR ARG THR LEU PRO          
SEQRES  60 A  880  HIS PHE LYS PRO TYR ASP ILE SER PRO GLU ALA ARG GLY          
SEQRES  61 A  880  PHE ILE TYR SER SER PHE ARG THR GLY LEU LYS PRO THR          
SEQRES  62 A  880  GLU LEU PHE PHE HIS ALA ALA GLY GLY ARG GLU GLY LEU          
SEQRES  63 A  880  VAL ASP THR ALA VAL ARG THR SER GLN SER GLY TYR MET          
SEQRES  64 A  880  GLN ARG ARG LEU ILE ASN ALA LEU SER ASP LEU ARG ALA          
SEQRES  65 A  880  GLU TYR ASP GLY THR VAL ARG SER LEU TYR GLY GLU VAL          
SEQRES  66 A  880  ILE GLN VAL ALA TYR GLY ASP ASP GLY VAL PHE PRO MET          
SEQRES  67 A  880  TYR SER ALA HIS GLY LYS THR VAL ASP VAL ASN ARG ILE          
SEQRES  68 A  880  PHE GLU ARG VAL VAL GLY TRP LYS THR                          
SEQRES   1 B 1131  MET ASN GLU LEU SER SER ASN LEU SER ILE ASP GLU ARG          
SEQRES   2 B 1131  TRP LYS VAL ILE GLU ALA TYR PHE LYS SER LYS GLY LEU          
SEQRES   3 B 1131  VAL ARG GLN HIS LEU ASP SER TYR ASN ASP PHE VAL ARG          
SEQRES   4 B 1131  ASN LYS LEU GLN GLU ILE ILE ASP GLU GLN GLY GLU ILE          
SEQRES   5 B 1131  PRO THR GLU ILE PRO GLY LEU LYS VAL ARG LEU GLY LYS          
SEQRES   6 B 1131  ILE ARG ILE GLY LYS PRO ARG VAL ARG GLU SER ASP ARG          
SEQRES   7 B 1131  GLY GLU ARG GLU ILE SER PRO MET GLU ALA ARG LEU ARG          
SEQRES   8 B 1131  ASN LEU THR TYR ALA ALA PRO LEU TRP LEU THR MET ILE          
SEQRES   9 B 1131  PRO VAL GLU ASN ASN ILE GLU ALA GLU PRO GLU GLU VAL          
SEQRES  10 B 1131  TYR ILE GLY ASP LEU PRO ILE MET LEU LYS SER ALA ILE          
SEQRES  11 B 1131  ASP PRO ILE SER GLN TYR THR LEU ASP LYS LEU ILE GLU          
SEQRES  12 B 1131  ILE GLY GLU ASP PRO LYS ASP PRO GLY GLY TYR PHE ILE          
SEQRES  13 B 1131  VAL ASN GLY SER GLU ARG VAL ILE VAL THR GLN GLU ASP          
SEQRES  14 B 1131  LEU ALA PRO ASN ARG VAL LEU VAL ASP THR GLY LYS THR          
SEQRES  15 B 1131  GLY SER ASN ILE THR HIS THR ALA LYS ILE ILE SER SER          
SEQRES  16 B 1131  THR ALA GLY TYR ARG VAL PRO VAL THR ILE GLU ARG LEU          
SEQRES  17 B 1131  LYS ASP GLY THR PHE HIS VAL SER PHE PRO ALA VAL PRO          
SEQRES  18 B 1131  GLY LYS ILE PRO PHE VAL ILE LEU MET ARG ALA LEU GLY          
SEQRES  19 B 1131  ILE LEU THR ASP ARG ASP ILE VAL TYR ALA VAL SER LEU          
SEQRES  20 B 1131  ASP PRO GLU ILE GLN ASN GLU LEU PHE PRO SER LEU GLU          
SEQRES  21 B 1131  GLN ALA SER SER ILE ALA ASN VAL ASP ASP ALA LEU ASP          
SEQRES  22 B 1131  PHE ILE GLY SER ARG VAL ALA ILE GLY GLN LYS ARG GLU          
SEQRES  23 B 1131  ASN ARG ILE GLU LYS ALA GLN GLN ILE ILE ASP LYS TYR          
SEQRES  24 B 1131  PHE LEU PRO HIS LEU GLY THR SER ALA ASP ASP ARG ARG          
SEQRES  25 B 1131  LYS LYS ALA TYR TYR LEU ALA TYR ALA ILE SER LYS VAL          
SEQRES  26 B 1131  ILE GLU LEU TYR LEU GLY ARG ARG GLU PRO ASP ASP LYS          
SEQRES  27 B 1131  ASP HIS TYR ALA ASN LYS ARG LEU ARG LEU ALA GLY ASP          
SEQRES  28 B 1131  LEU PHE ALA SER LEU PHE ARG VAL ALA PHE LYS ALA PHE          
SEQRES  29 B 1131  VAL LYS ASP LEU THR TYR GLN LEU GLU LYS SER LYS VAL          
SEQRES  30 B 1131  ARG GLY ARG LYS LEU ALA LEU LYS ALA LEU VAL ARG PRO          
SEQRES  31 B 1131  ASP ILE VAL THR GLU ARG ILE ARG HIS ALA LEU ALA THR          
SEQRES  32 B 1131  GLY ASN TRP VAL GLY GLY ARG THR GLY VAL SER GLN LEU          
SEQRES  33 B 1131  LEU ASP ARG THR ASN TRP LEU SER MET LEU SER HIS LEU          
SEQRES  34 B 1131  ARG ARG VAL ILE SER SER LEU ALA ARG GLY GLN PRO ASN          
SEQRES  35 B 1131  PHE GLU ALA ARG ASP LEU HIS GLY THR GLN TRP GLY ARG          
SEQRES  36 B 1131  MET CYS PRO PHE GLU THR PRO GLU GLY PRO ASN SER GLY          
SEQRES  37 B 1131  LEU VAL LYS ASN LEU ALA LEU MET ALA GLN ILE ALA VAL          
SEQRES  38 B 1131  GLY ILE ASN GLU LYS ILE VAL GLU LYS THR LEU TYR GLU          
SEQRES  39 B 1131  MET GLY VAL VAL PRO VAL GLU GLU VAL ILE ARG ARG VAL          
SEQRES  40 B 1131  THR GLU GLY GLY GLU ASP GLN ASN GLU TYR LEU LYS TRP          
SEQRES  41 B 1131  SER LYS VAL ILE LEU ASN GLY ARG LEU VAL GLY TYR TYR          
SEQRES  42 B 1131  ARG ASP GLY GLU GLU LEU ALA LYS LYS ILE ARG GLU ARG          
SEQRES  43 B 1131  ARG ARG LYS GLY GLU ILE SER ASP GLU VAL ASN VAL GLY          
SEQRES  44 B 1131  HIS ILE VAL THR ASP PHE ILE ASN GLU VAL HIS VAL ASN          
SEQRES  45 B 1131  CYS ASP SER GLY ARG VAL ARG ARG PRO LEU ILE ILE VAL          
SEQRES  46 B 1131  SER ASN GLY ASN PRO LEU VAL THR ARG GLU ASP ILE GLU          
SEQRES  47 B 1131  LYS LEU ASP SER GLY SER ILE THR PHE ASP ASP LEU VAL          
SEQRES  48 B 1131  ARG GLN GLY LYS ILE GLU TYR LEU ASP ALA GLU GLU GLU          
SEQRES  49 B 1131  GLU ASN ALA TYR VAL ALA LEU GLU PRO SER ASP LEU THR          
SEQRES  50 B 1131  PRO GLU HIS THR HIS LEU GLU ILE TRP SER PRO ALA ILE          
SEQRES  51 B 1131  LEU GLY ILE THR ALA SER ILE ILE PRO TYR PRO GLU HIS          
SEQRES  52 B 1131  ASN GLN SER PRO ARG ASN THR TYR GLN SER ALA MET ALA          
SEQRES  53 B 1131  LYS GLN ALA LEU GLY LEU TYR ALA ALA ASN TYR GLN LEU          
SEQRES  54 B 1131  ARG THR ASP THR ARG ALA HIS LEU LEU HIS TYR PRO GLN          
SEQRES  55 B 1131  ARG PRO LEU VAL GLN THR ARG ALA LEU ASP ILE ILE GLY          
SEQRES  56 B 1131  TYR THR ASN ARG PRO ALA GLY ASN ASN ALA ILE LEU ALA          
SEQRES  57 B 1131  VAL ILE SER PHE THR GLY TYR ASN MET GLU ASP SER ILE          
SEQRES  58 B 1131  ILE MET ASN ARG SER SER VAL GLU ARG GLY MET TYR ARG          
SEQRES  59 B 1131  SER THR PHE PHE ARG LEU TYR SER THR GLU GLU VAL LYS          
SEQRES  60 B 1131  TYR PRO GLY GLY GLN GLU ASP LYS ILE VAL MET PRO GLU          
SEQRES  61 B 1131  PRO GLY VAL ARG GLY TYR LYS GLY LYS GLU TYR TYR ARG          
SEQRES  62 B 1131  LEU LEU GLU ASP ASN GLY VAL VAL SER PRO GLU VAL GLU          
SEQRES  63 B 1131  VAL LYS GLY GLY ASP VAL LEU ILE GLY LYS VAL SER PRO          
SEQRES  64 B 1131  PRO ARG PHE LEU GLN GLU PHE LYS GLU LEU SER PRO GLU          
SEQRES  65 B 1131  GLN ALA LYS ARG ASP THR SER ILE VAL THR ARG HIS GLY          
SEQRES  66 B 1131  GLU MET GLY ILE VAL ASP LEU VAL LEU ILE THR GLU THR          
SEQRES  67 B 1131  ALA GLU GLY ASN LYS LEU VAL LYS VAL ARG VAL ARG ASP          
SEQRES  68 B 1131  LEU ARG ILE PRO SER ILE GLY ASP LYS PHE ALA SER ARG          
SEQRES  69 B 1131  HIS GLY GLN LYS GLY VAL ILE GLY MET LEU ILE PRO GLN          
SEQRES  70 B 1131  VAL ASP MET PRO TYR THR VAL LYS GLY VAL VAL PRO ASP          
SEQRES  71 B 1131  VAL ILE LEU ASN PRO HIS ALA LEU PRO SER ARG MET THR          
SEQRES  72 B 1131  LEU GLY GLN ILE MET GLU GLY ILE ALA GLY LYS TYR ALA          
SEQRES  73 B 1131  ALA LEU SER GLY ASN ILE VAL ASP ALA THR PRO PHE TYR          
SEQRES  74 B 1131  LYS THR PRO ILE GLU GLN LEU GLN ASN GLU ILE LEU LYS          
SEQRES  75 B 1131  TYR GLY TYR LEU PRO ASP ALA THR GLU VAL THR TYR ASP          
SEQRES  76 B 1131  GLY ARG THR GLY GLN LYS ILE LYS SER ARG ILE TYR PHE          
SEQRES  77 B 1131  GLY VAL VAL TYR TYR GLN LYS LEU HIS HIS MET VAL ALA          
SEQRES  78 B 1131  ASP LYS ILE HIS ALA ARG ALA ARG GLY PRO VAL GLN ILE          
SEQRES  79 B 1131  LEU THR ARG GLN PRO THR GLU GLY ARG ALA ARG GLU GLY          
SEQRES  80 B 1131  GLY LEU ARG PHE GLY GLU MET GLU ARG ASP CYS LEU ILE          
SEQRES  81 B 1131  GLY PHE GLY THR ALA MET LEU LEU LYS ASP ARG LEU LEU          
SEQRES  82 B 1131  ASP ASN SER ASP ARG THR THR ILE TYR VAL CYS ASP GLN          
SEQRES  83 B 1131  CYS GLY TYR ILE GLY TRP TYR ASP LYS ASN LYS ASN LYS          
SEQRES  84 B 1131  TYR VAL CYS PRO ILE HIS GLY ASP LYS SER ASN LEU PHE          
SEQRES  85 B 1131  PRO VAL THR VAL SER TYR ALA PHE LYS LEU LEU ILE GLN          
SEQRES  86 B 1131  GLU LEU MET SER MET ILE ILE SER PRO ARG LEU ILE LEU          
SEQRES  87 B 1131  GLU ASP ARG VAL GLY LEU SER GLY GLY LYS GLY ASN GLU          
SEQRES   1 C  395  MET GLU ASN VAL ILE ASP GLU LYS ASP LYS SER TYR LEU          
SEQRES   2 C  395  GLU GLU LYS VAL LYS GLN ALA SER ASN ILE LEU PRO GLN          
SEQRES   3 C  395  LYS ILE VAL GLU ASP LEU LYS ASN LEU ILE SER ASN LYS          
SEQRES   4 C  395  GLU VAL LEU VAL THR ARG ASP GLU ILE ASP LYS ILE PHE          
SEQRES   5 C  395  ASP LEU ALA ILE LYS GLU TYR SER GLU GLY LEU ILE ALA          
SEQRES   6 C  395  PRO GLY GLU ALA ILE GLY ILE VAL ALA ALA GLN SER VAL          
SEQRES   7 C  395  GLY GLU PRO GLY THR GLN MET THR LEU ARG THR PHE HIS          
SEQRES   8 C  395  PHE ALA GLY ILE ARG GLU LEU ASN VAL THR LEU GLY LEU          
SEQRES   9 C  395  PRO ARG LEU ILE GLU ILE VAL ASP ALA LYS LYS VAL PRO          
SEQRES  10 C  395  SER THR PRO MET MET THR ILE TYR LEU THR ASP GLU TYR          
SEQRES  11 C  395  LYS HIS ASP LYS GLU LYS ALA LEU GLU VAL ALA ARG LYS          
SEQRES  12 C  395  LEU GLU TYR THR LYS ILE GLU ASN VAL VAL SER SER THR          
SEQRES  13 C  395  SER ILE ASP ILE ALA SER MET SER ILE ILE LEU GLN LEU          
SEQRES  14 C  395  ASP ASN GLU MET LEU LYS ASP LYS GLY VAL THR VAL ASP          
SEQRES  15 C  395  ASP VAL LYS LYS ALA ILE ASN ARG LEU LYS LEU GLY GLU          
SEQRES  16 C  395  PHE VAL ILE ASP GLU SER GLU GLY THR THR LEU ASN ILE          
SEQRES  17 C  395  SER PHE ALA ASN ILE ASP SER ILE ALA ALA LEU PHE LYS          
SEQRES  18 C  395  LEU ARG ASP LYS ILE LEU ASN THR LYS ILE LYS GLY ILE          
SEQRES  19 C  395  LYS GLY ILE LYS ARG ALA ILE VAL GLN LYS LYS GLY ASP          
SEQRES  20 C  395  GLU TYR ILE ILE LEU THR ASP GLY SER ASN LEU SER GLY          
SEQRES  21 C  395  VAL LEU SER VAL LYS GLY VAL ASP ILE ALA LYS VAL GLU          
SEQRES  22 C  395  THR ASN ASN ILE ARG GLU ILE GLU GLU VAL PHE GLY ILE          
SEQRES  23 C  395  GLU ALA ALA ARG GLU ILE ILE ILE ARG GLU ILE SER LYS          
SEQRES  24 C  395  VAL LEU ALA GLU GLN GLY LEU ASP VAL ASP MET ARG HIS          
SEQRES  25 C  395  ILE LEU LEU VAL ALA ASP VAL MET THR ARG THR GLY VAL          
SEQRES  26 C  395  VAL ARG GLN ILE GLY ARG HIS GLY VAL THR GLY GLU LYS          
SEQRES  27 C  395  ASN SER VAL LEU ALA ARG ALA ALA PHE GLU VAL THR VAL          
SEQRES  28 C  395  LYS HIS LEU LEU ASP ALA ALA ALA ARG GLY ASP VAL GLU          
SEQRES  29 C  395  GLU PHE LYS GLY VAL VAL GLU ASN ILE ILE ILE GLY HIS          
SEQRES  30 C  395  PRO ILE LYS LEU GLY THR GLY MET VAL GLU LEU THR MET          
SEQRES  31 C  395  ARG PRO ILE LEU ARG                                          
SEQRES   1 D  265  MET SER ILE ASN LEU LEU HIS LYS ASP ASP LYS ARG ILE          
SEQRES   2 D  265  ASP LEU VAL PHE GLU GLY TYR PRO LEU GLU PHE VAL ASN          
SEQRES   3 D  265  ALA ILE ARG ARG ALA ALA MET LEU TYR VAL PRO VAL MET          
SEQRES   4 D  265  SER ILE ASP ASP VAL TYR PHE ILE GLU ASN ASN SER PRO          
SEQRES   5 D  265  LEU TYR ASP GLU ILE LEU ALA HIS ARG LEU ALA LEU ILE          
SEQRES   6 D  265  PRO PHE THR SER GLU GLU ALA LEU ASP THR TYR ARG TRP          
SEQRES   7 D  265  PRO GLU GLU CYS ILE ASP CYS THR GLU ASN CYS GLU LYS          
SEQRES   8 D  265  CYS TYR THR LYS ILE TYR ILE GLU ALA GLU ALA LEU ASN          
SEQRES   9 D  265  GLU PRO LYS MET LEU TYR SER LYS ASP ILE LYS SER GLU          
SEQRES  10 D  265  ASP PRO SER ILE VAL PRO ILE SER GLY ASP ILE PRO ILE          
SEQRES  11 D  265  VAL LEU LEU GLY ALA ASN GLN LYS ILE SER LEU GLU ALA          
SEQRES  12 D  265  ARG LEU ARG LEU GLY TYR GLY LYS GLU HIS ALA LYS PHE          
SEQRES  13 D  265  ILE PRO VAL SER LEU ALA ILE VAL ARG TYR TYR PRO LYS          
SEQRES  14 D  265  VAL GLU ILE LEU GLY ASN CYS GLU LYS GLY ALA THR VAL          
SEQRES  15 D  265  CYS PRO GLU GLY VAL PHE GLU LEU LYS ASP GLY LYS LEU          
SEQRES  16 D  265  SER VAL LYS ASN GLU LEU ALA CYS THR LEU CYS GLU GLU          
SEQRES  17 D  265  CYS LEU ARG TYR CYS ASN GLY LEU ILE ARG ILE SER SER          
SEQRES  18 D  265  VAL GLU ASP LYS TYR ILE LEU GLU LEU GLU SER VAL GLY          
SEQRES  19 D  265  SER LEU LYS PRO GLU ARG ILE LEU LEU GLU ALA GLY LYS          
SEQRES  20 D  265  SER ILE ILE ARG LYS ILE GLU GLU LEU GLU LYS LYS LEU          
SEQRES  21 D  265  VAL GLU VAL ILE LYS                                          
SEQRES   1 E  180  MET TYR LYS LEU ILE LYS ALA ARG SER ILE VAL ARG ILE          
SEQRES   2 E  180  PRO PRO ASN GLU PHE GLY LYS PRO LEU ASN GLU ILE ALA          
SEQRES   3 E  180  LEU ASN GLU LEU ARG GLN GLN TYR GLN GLU LYS ILE LEU          
SEQRES   4 E  180  LYS ASP LEU GLY LEU VAL LEU ALA ILE LEU ASN VAL LYS          
SEQRES   5 E  180  THR SER GLU GLU GLY ILE LEU VAL PHE GLY ASP GLY ALA          
SEQRES   6 E  180  THR TYR HIS GLU VAL GLU PHE ASP MET ILE THR TYR VAL          
SEQRES   7 E  180  PRO VAL VAL GLN GLU VAL VAL GLU GLY GLU VAL LEU GLN          
SEQRES   8 E  180  VAL ASP ASN TYR GLY ILE PHE VAL ASN LEU GLY PRO MET          
SEQRES   9 E  180  ASP GLY LEU VAL HIS ILE SER GLN ILE THR ASP ASP THR          
SEQRES  10 E  180  LEU LYS TYR ASP ASN VAL ARG GLY ILE ILE PHE GLY GLU          
SEQRES  11 E  180  LYS SER LYS LYS VAL ILE GLN LYS GLY ASP LYS VAL ARG          
SEQRES  12 E  180  ALA ARG VAL ILE SER VAL ALA SER THR VAL THR GLY ARG          
SEQRES  13 E  180  LEU PRO ARG ILE ALA LEU THR MET ARG GLN PRO TYR LEU          
SEQRES  14 E  180  GLY LYS LEU GLU TRP ILE THR GLN ALA LYS LYS                  
SEQRES   1 F  113  MET SER SER VAL TYR ILE VAL GLU GLU HIS TYR ILE PRO          
SEQRES   2 F  113  TYR SER VAL ALA LYS LYS LEU LEU SER ASP VAL ILE LYS          
SEQRES   3 F  113  SER GLY SER SER SER ASN LEU LEU GLN ARG THR TYR ASP          
SEQRES   4 F  113  TYR LEU ASN SER VAL GLU LYS CYS ASP ALA GLU SER ALA          
SEQRES   5 F  113  GLN LYS VAL VAL GLU GLU LEU SER SER ILE ILE SER ARG          
SEQRES   6 F  113  GLU ASP VAL ARG ALA VAL LEU ALA SER ILE CYS PRO ILE          
SEQRES   7 F  113  THR PRO ASP GLU VAL ARG SER ILE LEU ILE MET ASP SER          
SEQRES   8 F  113  ASN ARG THR TYR THR SER GLU ASP ILE GLN LYS ILE ILE          
SEQRES   9 F  113  ASP ILE ILE ARG LYS TYR ILE LYS SER                          
SEQRES   1 G  132  MET MET GLU SER LYS ALA GLN GLU ILE ILE LEU SER CYS          
SEQRES   2 G  132  GLU ILE ASN SER ILE GLU ARG GLY SER LEU LYS ASN LEU          
SEQRES   3 G  132  SER ILE ILE HIS MET SER CYS ASN ASP PHE ASN ILE SER          
SEQRES   4 G  132  PHE ASP ILE ILE ASP SER ILE ASN ILE PHE SER GLN LYS          
SEQRES   5 G  132  GLU LYS VAL LYS ALA PHE ILE SER LYS ASN ARG LEU SER          
SEQRES   6 G  132  TYR THR ASN ASP ASP PHE CYS GLY HIS GLY TYR ILE VAL          
SEQRES   7 G  132  THR GLU LEU LYS ASP SER SER SER ASN ASN GLY ASN ARG          
SEQRES   8 G  132  TYR ILE THR ILE ILE SER LEU PHE GLY LEU LEU VAL LYS          
SEQRES   9 G  132  ILE ILE SER ASN LYS GLU SER PHE LEU LYS ILE HIS GLN          
SEQRES  10 G  132  LEU ASN VAL MET ASP HIS ILE TYR PHE CYS VAL LYS LYS          
SEQRES  11 G  132  ASN THR                                                      
SEQRES   1 H   84  MET ARG GLY SER SER ASN ARG LYS ILE ASP PRO ARG ILE          
SEQRES   2 H   84  HIS TYR LEU VAL PRO LYS HIS GLU VAL LEU SER ILE ASP          
SEQRES   3 H   84  GLU ALA TYR LYS ILE LEU LYS GLU LEU GLY ILE ARG PRO          
SEQRES   4 H   84  GLU GLN LEU PRO TRP ILE ARG ALA SER ASP PRO VAL ALA          
SEQRES   5 H   84  ARG SER ILE ASN ALA LYS PRO GLY ASP ILE ILE ARG ILE          
SEQRES   6 H   84  ILE ARG LYS SER GLN LEU TYR GLY GLU VAL VAL SER TYR          
SEQRES   7 H   84  ARG TYR VAL ILE SER GLY                                      
SEQRES   1 K   95  MET GLY LEU GLU ARG ASP GLY ILE LEU SER GLN ASP LEU          
SEQRES   2 K   95  HIS PHE ASN GLU VAL PHE ILE SER LEU TRP GLN ASN ARG          
SEQRES   3 K   95  LEU THR ARG TYR GLU ILE ALA ARG VAL ILE SER ALA ARG          
SEQRES   4 K   95  ALA LEU GLN LEU ALA MET GLY ALA PRO ALA LEU ILE ASP          
SEQRES   5 K   95  ILE ASN ASN LEU SER SER THR ASP VAL ILE SER ILE ALA          
SEQRES   6 K   95  GLU GLU GLU PHE ARG ARG GLY VAL LEU PRO ILE THR ILE          
SEQRES   7 K   95  ARG ARG ARG LEU PRO ASN GLY LYS ILE ILE LEU LEU SER          
SEQRES   8 K   95  LEU ARG LYS SER                                              
SEQRES   1 L   92  MET GLU ILE LYS ILE LEU LYS SER GLU SER ASN TYR LEU          
SEQRES   2 L   92  GLU LEU GLU ILE GLU GLY GLU ASP HIS THR LEU GLY ASN          
SEQRES   3 L   92  LEU ILE ALA GLY THR LEU ARG LYS ILE SER GLY VAL SER          
SEQRES   4 L   92  PHE ALA SER TYR TYR GLN PRO HIS PRO LEU THR ASP LYS          
SEQRES   5 L   92  ILE ILE VAL LYS ILE LEU THR ASP GLY SER ILE ALA PRO          
SEQRES   6 L   92  LYS ASP ALA LEU LEU LYS ALA ILE GLU THR VAL ARG VAL          
SEQRES   7 L   92  MET ALA SER HIS TYR ILE ASP GLU ILE LYS GLY LEU THR          
SEQRES   8 L   92  LYS                                                          
SEQRES   1 N   66  MET MET ILE PRO ILE ARG CYS PHE THR CYS GLY SER LEU          
SEQRES   2 N   66  ILE ALA ASP LYS TRP GLN PRO PHE ILE THR ARG VAL ASN          
SEQRES   3 N   66  ALA GLY GLU ASN PRO GLY LYS VAL LEU ASP ASP LEU GLY          
SEQRES   4 N   66  VAL LYS ARG TYR CYS CYS ARG ARG MET LEU LEU SER HIS          
SEQRES   5 N   66  ILE ASP ILE ILE SER GLU VAL ILE HIS TYR THR ARG PRO          
SEQRES   6 N   66  ILE                                                          
SEQRES   1 P   48  MET ALA VAL TYR ARG CYS GLY LYS CYS TRP LYS THR PHE          
SEQRES   2 P   48  THR ASP GLU GLN LEU LYS VAL LEU PRO GLY VAL ARG CYS          
SEQRES   3 P   48  PRO TYR CYS GLY TYR LYS ILE ILE PHE MET VAL ARG LYS          
SEQRES   4 P   48  PRO THR ILE LYS ILE VAL LYS ALA ILE                          
SEQRES   1 Q  104  MET VAL SER GLY MET SER THR GLU GLU GLU LYS GLU GLY          
SEQRES   2 Q  104  THR ASN ASP GLU GLU VAL SER GLU GLU ARG GLU VAL GLU          
SEQRES   3 Q  104  GLU THR SER GLU GLU GLU PHE PRO LYS LEU SER ILE GLN          
SEQRES   4 Q  104  ILE ILE GLU LEU LEU MET LYS ASN THR GLU ILE TRP ASP          
SEQRES   5 Q  104  ASN LEU LEU ASN GLY LYS ILE SER VAL ASP GLU ALA LYS          
SEQRES   6 Q  104  ARG LEU PHE GLU ASP ASN TYR LYS ASP TYR GLU LYS ARG          
SEQRES   7 Q  104  ASP SER ARG ARG LYS ALA LYS LYS ALA ALA SER LYS LYS          
SEQRES   8 Q  104  VAL LYS LYS THR LYS LYS LYS GLU LYS SER VAL GLU GLY          
HET     ZN  A1300       1                                                       
HET     ZN  A1350       1                                                       
HET     ZN  A1360       1                                                       
HET     MG  A1400       1                                                       
HET     ZN  B1300       1                                                       
HET     ZN  B1400       1                                                       
HET     ZN  B1500       1                                                       
HET     ZN  C1000       1                                                       
HET    F3S  D1001       7                                                       
HET     ZN  N 100       1                                                       
HET     ZN  P  50       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     F3S FE3-S4 CLUSTER                                                   
FORMUL  14   ZN    9(ZN 2+)                                                     
FORMUL  17   MG    MG 2+                                                        
FORMUL  22  F3S    FE3 S4                                                       
HELIX    1   1 SER A   15  LYS A   21  1                                   7    
HELIX    2   2 PHE A   86  ALA A   96  1                                  11    
HELIX    3   3 LYS A  113  TYR A  118  1                                   6    
HELIX    4   4 TRP A  125  ARG A  130  1                                   6    
HELIX    5   5 THR A  133  LYS A  138  1                                   6    
HELIX    6   6 THR A  176  GLU A  185  1                                  10    
HELIX    7   7 PRO A  188  GLY A  196  1                                   9    
HELIX    8   8 ARG A  203  MET A  207  1                                   5    
HELIX    9   9 PRO A  216  ARG A  220  5                                   5    
HELIX   10  10 ASP A  234  ARG A  244  1                                  11    
HELIX   11  11 ARG A  244  SER A  252  1                                   9    
HELIX   12  12 PRO A  258  ASP A  278  1                                  21    
HELIX   13  13 THR A  297  GLY A  304  1                                   8    
HELIX   14  14 LYS A    4  SER A  314  1                                 276    
HELIX   15  15 PRO A  340  LEU A  347  1                                   8    
HELIX   16  16 ASN A  357  GLY A  368  1                                  12    
HELIX   17  17 GLU A  396  THR A  400  5                                   5    
HELIX   18  18 ASN A  446  CYS A  450  5                                   5    
HELIX   19  19 SER A  469  ILE A  479  1                                  11    
HELIX   20  20 VAL A  482  ASN A  485  5                                   4    
HELIX   21  21 GLN A  500  VAL A  511  1                                  12    
HELIX   22  22 THR A  517  GLY A  526  1                                  10    
HELIX   23  23 GLY A  548  ALA A  554  1                                   7    
HELIX   24  24 SER A  570  LEU A  574  5                                   5    
HELIX   25  25 SER A  610  GLU A  618  1                                   9    
HELIX   26  26 SER A  620  GLY A  643  1                                  24    
HELIX   27  27 ARG A  647  VAL A  651  5                                   5    
HELIX   28  28 VAL A  657  LYS A  680  1                                  24    
HELIX   29  29 THR A  691  TYR A  718  1                                  28    
HELIX   30  30 ASN A  723  ALA A  729  1                                   7    
HELIX   31  31 ASN A  739  ALA A  745  1                                   7    
HELIX   32  32 SER A  775  ARG A  779  5                                   5    
HELIX   33  33 LYS A  791  VAL A  811  1                                  21    
HELIX   34  34 ARG A  812  ASN A  825  1                                  14    
HELIX   35  35 ASN A  869  VAL A  875  1                                   7    
HELIX   36  36 SER B    9  LYS B   24  1                                  16    
HELIX   37  37 HIS B   30  ASN B   40  1                                  11    
HELIX   38  38 LEU B   42  ASP B   47  1                                   6    
HELIX   39  39 SER B   84  ASN B   92  1                                   9    
HELIX   40  40 ASP B  131  GLN B  135  5                                   5    
HELIX   41  41 THR B  137  GLY B  145  1                                   9    
HELIX   42  42 PHE B  226  LEU B  233  1                                   8    
HELIX   43  43 THR B  237  SER B  246  1                                  10    
HELIX   44  44 ASN B  267  ALA B  280  1                                  14    
HELIX   45  45 LYS B  284  PHE B  300  1                                  17    
HELIX   46  46 SER B  307  ARG B  311  5                                   5    
HELIX   47  47 ARG B  311  LYS B  313  5                                   3    
HELIX   48  48 LYS B  314  LEU B  330  1                                  17    
HELIX   49  49 HIS B  340  ALA B  342  5                                   3    
HELIX   50  50 LEU B  348  LYS B  374  1                                  27    
HELIX   51  51 THR B  394  HIS B  399  1                                   6    
HELIX   52  52 ASN B  421  LEU B  429  1                                   9    
HELIX   53  53 HIS B  449  GLN B  452  5                                   4    
HELIX   54  54 ASN B  484  GLU B  489  1                                   6    
HELIX   55  55 LYS B  490  LEU B  492  5                                   3    
HELIX   56  56 PRO B  499  ARG B  505  1                                   7    
HELIX   57  57 ASP B  535  GLY B  550  1                                  16    
HELIX   58  58 LEU B  591  GLU B  595  5                                   5    
HELIX   59  59 THR B  606  GLN B  613  1                                   8    
HELIX   60  60 GLU B  622  ASN B  626  5                                   5    
HELIX   61  61 GLU B  632  LEU B  636  5                                   5    
HELIX   62  62 TRP B  646  LEU B  651  5                                   6    
HELIX   63  63 ILE B  653  ILE B  658  5                                   6    
HELIX   64  64 TYR B  660  ASN B  664  5                                   5    
HELIX   65  65 GLN B  665  ALA B  676  1                                  12    
HELIX   66  66 ARG B  709  GLY B  715  1                                   7    
HELIX   67  67 ARG B  745  GLU B  749  1                                   5    
HELIX   68  68 GLY B  788  ARG B  793  5                                   6    
HELIX   69  69 PRO B  896  MET B  900  5                                   5    
HELIX   70  70 THR B  923  GLY B  940  1                                  18    
HELIX   71  71 PRO B  952  TYR B  963  1                                  12    
HELIX   72  72 MET B  999  LYS B 1003  5                                   5    
HELIX   73  73 GLY B 1022  GLU B 1026  5                                   5    
HELIX   74  74 GLY B 1032  PHE B 1042  1                                  11    
HELIX   75  75 THR B 1044  LEU B 1053  1                                  10    
HELIX   76  76 TYR B 1098  SER B 1109  1                                  12    
HELIX   77  77 LEU C   13  SER C   21  1                                   9    
HELIX   78  78 ASN C   22  LYS C   27  5                                   6    
HELIX   79  79 GLU C   30  LEU C   42  1                                  13    
HELIX   80  80 LYS C   50  ALA C   55  1                                   6    
HELIX   81  81 ALA C   69  GLU C   80  1                                  12    
HELIX   82  82 PRO C   81  GLN C   84  5                                   4    
HELIX   83  83 GLY C  103  VAL C  111  1                                   9    
HELIX   84  84 ASP C  133  GLU C  145  1                                  13    
HELIX   85  85 VAL C  181  ASP C  183  5                                   3    
HELIX   86  86 VAL C  184  ASN C  189  1                                   6    
HELIX   87  87 LEU C  222  LEU C  227  1                                   6    
HELIX   88  88 ASN C  257  LEU C  262  1                                   6    
HELIX   89  89 ASP C  268  VAL C  272  5                                   5    
HELIX   90  90 GLU C  279  PHE C  284  1                                   6    
HELIX   91  91 ILE C  286  GLU C  303  1                                  18    
HELIX   92  92 ASP C  309  ARG C  322  1                                  14    
HELIX   93  93 LEU C  342  PHE C  347  1                                   6    
HELIX   94  94 GLU C  348  THR C  350  5                                   3    
HELIX   95  95 VAL C  351  ARG C  360  1                                  10    
HELIX   96  96 GLY C  368  ILE C  375  1                                   8    
HELIX   97  97 LEU C  381  MET C  385  5                                   5    
HELIX   98  98 PRO D   21  LEU D   34  1                                  14    
HELIX   99  99 TYR D   54  ILE D   65  1                                  12    
HELIX  100 100 GLU D   71  TYR D   76  1                                   6    
HELIX  101 101 LYS D  112  ILE D  114  5                                   3    
HELIX  102 102 TYR D  149  ALA D  154  1                                   6    
HELIX  103 103 GLU D  177  VAL D  182  1                                   6    
HELIX  104 104 GLU D  207  CYS D  213  1                                   7    
HELIX  105 105 LYS D  237  VAL D  263  1                                  27    
HELIX  106 106 PRO E   14  PHE E   18  5                                   5    
HELIX  107 107 PRO E   21  GLN E   32  1                                  12    
HELIX  108 108 LYS E  171  GLN E  177  1                                   7    
HELIX  109 109 ALA F   17  SER F   22  1                                   6    
HELIX  110 110 ASP F   23  ILE F   25  5                                   3    
HELIX  111 111 SER F   31  GLU F   45  1                                  15    
HELIX  112 112 SER F   51  SER F   60  1                                  10    
HELIX  113 113 ARG F   65  CYS F   76  1                                  12    
HELIX  114 114 GLU F   82  ILE F   86  5                                   5    
HELIX  115 115 SER H   24  GLY H   36  1                                  13    
HELIX  116 116 ARG H   38  LEU H   42  5                                   5    
HELIX  117 117 ASP H   49  ASN H   56  1                                   8    
HELIX  118 118 LEU K   13  TRP K   23  1                                  11    
HELIX  119 119 THR K   28  ALA K   44  1                                  17    
HELIX  120 120 ILE K   62  ARG K   71  1                                  10    
HELIX  121 121 ASP L   21  THR L   31  1                                  11    
HELIX  122 122 ALA L   64  GLY L   89  1                                  26    
HELIX  123 123 ILE N   14  ASP N   16  5                                   3    
HELIX  124 124 LYS N   17  ASN N   26  1                                  10    
HELIX  125 125 ASN N   30  LEU N   38  1                                   9    
HELIX  126 126 ARG N   42  SER N   51  1                                  10    
HELIX  127 127 ILE N   55  ILE N   60  1                                   6    
HELIX  128 128 GLU Q   42  ASN Q   53  1                                  12    
HELIX  129 129 SER Q   60  LYS Q   73  1                                  14    
SHEET    1  BA 3 ARG B1115  GLU B1119  0                                        
SHEET    2  BA 3 ASN A   5  LYS A  10 -1  O  ASN A   5   N  GLU B1119           
SHEET    3  BA 3 VAL C 363  GLU C 364 -1  O  GLU C 364   N  ILE A   9           
SHEET    1  AA 2 GLY A  73  ILE A  82  0                                        
SHEET    2  AA 2 ILE A 208  VAL A 214 -1  O  LEU A 209   N  VAL A  81           
SHEET    1  AB 7 SER A 321  PRO A 328  0                                        
SHEET    2  AB 7 GLU A 461  HIS A 465 -1  O  MET A 462   N  THR A 324           
SHEET    3  AB 7 VAL A 416  ASN A 420 -1  O  LEU A 418   N  HIS A 465           
SHEET    4  AB 7 MET A 430  VAL A 437 -1  O  MET A 431   N  PHE A 419           
SHEET    5  AB 7 GLU A 336  VAL A 339  1  O  VAL A 337   N  ARG A 436           
SHEET    6  AB 7 PHE A 443  LEU A 445 -1  O  ARG A 444   N  GLY A 338           
SHEET    7  AB 7 SER A 321  PRO A 328  1  O  VAL A 325   N  PHE A 443           
SHEET    1  AC 4 THR A 348  ARG A 352  0                                        
SHEET    2  AC 4 VAL A 406  HIS A 410 -1  O  VAL A 407   N  GLU A 351           
SHEET    3  AC 4 ALA A 375  ILE A 379 -1  N  ASN A 376   O  GLU A 408           
SHEET    4  AC 4 ARG A 385  ASP A 387 -1  O  ILE A 386   N  VAL A 378           
SHEET    1  AD 2 LEU A 515  LEU A 516  0                                        
SHEET    2  AD 2 TYR A 546  THR A 547 -1  O  TYR A 546   N  LEU A 516           
SHEET    1  AE 3 PHE A 562  GLN A 565  0                                        
SHEET    2  AE 3 TYR A 585  LYS A 589 -1  O  VAL A 586   N  GLY A 564           
SHEET    3  AE 3 ILE A 592  GLU A 595 -1  O  ILE A 592   N  LYS A 589           
SHEET    1  AF 2 GLY A 748  GLN A 749  0                                        
SHEET    2  AF 2 PHE A 781  ILE A 782 -1  O  ILE A 782   N  GLY A 748           
SHEET    1  AG 2 SER A 751  VAL A 752  0                                        
SHEET    2  AG 2 GLU A 755  ARG A 756 -1  O  GLU A 755   N  VAL A 752           
SHEET    1  AH 3 ARG A 831  ALA A 832  0                                        
SHEET    2  AH 3 THR A 837  ARG A 839 -1  O  ARG A 839   N  ARG A 831           
SHEET    3  AH 3 VAL A 845  VAL A 848 -1  N  ILE A 846   O  VAL A 838           
SHEET    1  BB 3 LEU B  59  ILE B  68  0                                        
SHEET    2  BB 3 ALA B  96  GLU B 107 -1  O  TRP B 100   N  ARG B  67           
SHEET    3  BB 3 GLU B 115  PRO B 123 -1  O  GLU B 115   N  MET B 103           
SHEET    1  BC 2 ARG B  72  GLU B  75  0                                        
SHEET    2  BC 2 GLY B  79  GLU B  82 -1  O  GLY B  79   N  GLU B  75           
SHEET    1  BD 3 PHE B 155  VAL B 157  0                                        
SHEET    2  BD 3 SER B 160  ILE B 164 -1  O  SER B 160   N  VAL B 157           
SHEET    3  BD 3 SER B 414  LEU B 416 -1  O  GLN B 415   N  VAL B 163           
SHEET    1  BE 3 LYS B 344  ARG B 347  0                                        
SHEET    2  BE 3 THR B 166  LEU B 170 -1  O  GLN B 167   N  ARG B 347           
SHEET    3  BE 3 VAL B 432  SER B 434  1  O  ILE B 433   N  GLU B 168           
SHEET    1  BF 5 VAL B 175  THR B 179  0                                        
SHEET    2  BF 5 HIS B 188  SER B 194 -1  O  THR B 189   N  ASP B 178           
SHEET    3  BF 5 THR B 204  LYS B 209 -1  O  THR B 204   N  SER B 194           
SHEET    4  BF 5 HIS B 214  SER B 216 -1  O  HIS B 214   N  LYS B 209           
SHEET    5  BF 5 ILE B 224  PRO B 225 -1  O  ILE B 224   N  VAL B 215           
SHEET    1  BG 7 GLN B 478  ILE B 479  0                                        
SHEET    2  BG 7 VAL B 578  ILE B 584 -1  O  ARG B 579   N  GLN B 478           
SHEET    3  BG 7 ILE B 616  LEU B 619 -1  O  GLU B 617   N  LEU B 582           
SHEET    4  BG 7 VAL B 578  ILE B 584 -1  O  ARG B 580   N  LEU B 619           
SHEET    5  BG 7 VAL B 629  ALA B 630  0                                        
SHEET    6  BG 7 HIS B 642  GLU B 644  1  O  HIS B 642   N  ALA B 630           
SHEET    7  BG 7 VAL B 578  ILE B 584 -1  O  ILE B 583   N  LEU B 643           
SHEET    1  BH 4 LEU B 529  GLY B 531  0                                        
SHEET    2  BH 4 LYS B 522  LEU B 525 -1  O  VAL B 523   N  VAL B 530           
SHEET    3  BH 4 GLU B 568  ASN B 572  1  O  VAL B 569   N  ILE B 524           
SHEET    4  BH 4 ASN B 557  ILE B 561 -1  O  ASN B 557   N  ASN B 572           
SHEET    1  BI 8 ARG B 694  ALA B 695  0                                        
SHEET    2  BI 8 SER B 755  GLU B 764 -1  O  PHE B 758   N  ALA B 695           
SHEET    3  BI 8 LYS B 863  ARG B 873 -1  O  VAL B 865   N  THR B 763           
SHEET    4  BI 8 GLY B 848  GLU B 857 -1  O  ILE B 849   N  ARG B 870           
SHEET    5  BI 8 GLU B 806  VAL B 807 -1  O  VAL B 807   N  GLY B 848           
SHEET    6  BI 8 GLY B 848  GLU B 857 -1  O  GLY B 848   N  VAL B 807           
SHEET    7  BI 8 ILE P  34  PHE P  35 -1  O  ILE P  34   N  ILE B 855           
SHEET    8  BI 8 GLY B 848  GLU B 857 -1  O  ILE B 855   N  ILE P  34           
SHEET    1  BJ 7 ASN B 723  VAL B 729  0                                        
SHEET    2  BJ 7 PHE B 988  LYS B 995 -1  O  GLY B 989   N  LEU B 727           
SHEET    3  BJ 7 LYS B 880  SER B 883 -1  O  ALA B 882   N  GLN B 994           
SHEET    4  BJ 7 LYS B 888  ILE B 895 -1  O  GLY B 889   N  PHE B 881           
SHEET    5  BJ 7 ILE B 741  ASN B 744  1  O  ILE B 741   N  GLY B 892           
SHEET    6  BJ 7 VAL B 911  LEU B 913 -1  O  ILE B 912   N  ILE B 742           
SHEET    7  BJ 7 ASN B 723  VAL B 729  1  O  ILE B 726   N  VAL B 911           
SHEET    1  BK 2 VAL B 812  ILE B 814  0                                        
SHEET    2  BK 2 ILE B 840  VAL B 841 -1  O  ILE B 840   N  LEU B 813           
SHEET    1  BL 2 TYR B 902  THR B 903  0                                        
SHEET    2  BL 2 THR B 973  TYR B 974 -1  O  TYR B 974   N  TYR B 902           
SHEET    1  BM 2 ARG B1058  VAL B1063  0                                        
SHEET    2  BM 2 PHE B1092  SER B1097 -1  O  PHE B1092   N  VAL B1063           
SHEET    1  CA 4 ALA C 240  GLN C 243  0                                        
SHEET    2  CA 4 ILE C 250  THR C 253 -1  O  ILE C 250   N  GLN C 243           
SHEET    3  CA 4 MET C 122  ILE C 124 -1  O  MET C 122   N  THR C 253           
SHEET    4  CA 4 GLU C 273  THR C 274 -1  O  GLU C 273   N  THR C 123           
SHEET    1  CB 4 VAL C 153  ILE C 158  0                                        
SHEET    2  CB 4 SER C 164  LEU C 169 -1  O  ILE C 166   N  SER C 157           
SHEET    3  CB 4 THR C 205  ILE C 208 -1  O  THR C 205   N  LEU C 167           
SHEET    4  CB 4 ILE C 198  GLU C 200 -1  O  ASP C 199   N  LEU C 206           
SHEET    1  EA11 ILE E  38  LEU E  39  0                                        
SHEET    2  EA11 GLY E  43  THR E  53 -1  O  GLY E  43   N  LEU E  39           
SHEET    3  EA11 THR E  66  TYR E  77 -1  O  GLU E  71   N  LYS E  52           
SHEET    4  EA11 VAL F   4  ILE F  12  0                                        
SHEET    5  EA11 TYR E   2  ILE E  13 -1  O  TYR E   2   N  ILE F  12           
SHEET    6  EA11 THR E  66  TYR E  77 -1  O  THR E  66   N  ILE E  13           
SHEET    7  EA11 ILE K  87  LEU K  89  0                                        
SHEET    8  EA11 ILE K  76  ARG K  81 -1  O  ARG K  80   N  ILE K  88           
SHEET    9  EA11 GLU C 387  MET C 390 -1  O  GLU C 387   N  ARG K  79           
SHEET   10  EA11 GLY E  57  LEU E  59 -1  O  GLY E  57   N  MET C 390           
SHEET   11  EA11 THR E  66  TYR E  77 -1  O  TYR E  67   N  ILE E  58           
SHEET    1  DA 4 ILE D   3  LYS D   8  0                                        
SHEET    2  DA 4 ARG D  12  GLU D  18 -1  O  ASP D  14   N  LEU D   6           
SHEET    3  DA 4 LYS D 225  GLU D 231 -1  O  TYR D 226   N  PHE D  17           
SHEET    4  DA 4 ILE D 163  TYR D 166 -1  O  ILE D 163   N  GLU D 229           
SHEET    1  DB 4 THR D  94  ALA D 102  0                                        
SHEET    2  DB 4 GLN D 137  GLY D 148 -1  O  GLN D 137   N  ALA D 102           
SHEET    3  DB 4 VAL D  38  ASN D  49 -1  O  VAL D  38   N  GLY D 148           
SHEET    4  DB 4 LYS P  43  LYS P  46 -1  O  LYS P  43   N  PHE D  46           
SHEET    1  DC 2 MET D 108  TYR D 110  0                                        
SHEET    2  DC 2 PRO D 129  LEU D 132 -1  N  ILE D 130   O  LEU D 109           
SHEET    1  DD 2 VAL D 170  ILE D 172  0                                        
SHEET    2  DD 2 ILE D 217  ILE D 219 -1  O  ARG D 218   N  GLU D 171           
SHEET    1  EB 4 VAL E 108  HIS E 109  0                                        
SHEET    2  EB 4 GLY E  96  VAL E  99 -1  O  ILE E  97   N  VAL E 108           
SHEET    3  EB 4 GLY E  87  VAL E  92 -1  N  LEU E  90   O  PHE E  98           
SHEET    4  EB 4 LYS E 141  VAL E 142 -1  O  VAL E 142   N  GLY E  87           
SHEET    1  EC 2 ARG E 145  ALA E 150  0                                        
SHEET    2  EC 2 ARG E 159  THR E 163 -1  O  ARG E 159   N  ALA E 150           
SHEET    1  GA 9 PHE G  71  CYS G  72  0                                        
SHEET    2  GA 9 PHE G 112  ILE G 115 -1  O  ILE G 115   N  PHE G  71           
SHEET    3  GA 9 LYS G  54  SER G  60 -1  O  PHE G  58   N  LYS G 114           
SHEET    4  GA 9 ILE G   9  ARG G  20 -1  O  ILE G   9   N  ILE G  59           
SHEET    5  GA 9 LEU G  26  SER G  32 -1  O  ILE G  28   N  GLU G  19           
SHEET    6  GA 9 ASN G  37  ILE G  43 -1  O  ILE G  38   N  MET G  31           
SHEET    7  GA 9 ASN G  90  ILE G  95 -1  O  ILE G  93   N  SER G  39           
SHEET    8  GA 9 ASP G  83  ASN G  87 -1  O  ASP G  83   N  THR G  94           
SHEET    9  GA 9 TYR G  76  THR G  79 -1  O  TYR G  76   N  SER G  86           
SHEET    1  HA 3 LYS H  19  VAL H  22  0                                        
SHEET    2  HA 3 ILE H  63  SER H  69 -1  O  ARG H  64   N  GLU H  21           
SHEET    3  HA 3 GLY H  73  TYR H  78 -1  O  GLY H  73   N  SER H  69           
SHEET    1  LA 4 GLU L   2  GLU L   9  0                                        
SHEET    2  LA 4 TYR L  12  GLU L  18 -1  O  TYR L  12   N  GLU L   9           
SHEET    3  LA 4 ILE L  53  THR L  59 -1  O  ILE L  53   N  ILE L  17           
SHEET    4  LA 4 VAL L  38  TYR L  44 -1  N  SER L  39   O  LEU L  58           
SSBOND   1 CYS A   98    CYS A  101                          1555   1555  2.04  
SSBOND   2 CYS A  575    CYS A  580                          1555   1555  2.03  
SSBOND   3 CYS D   82    CYS D   92                          1555   1555  2.04  
SSBOND   4 CYS D   85    CYS D   89                          1555   1555  2.03  
SSBOND   5 CYS D  176    CYS D  213                          1555   1555  2.03  
SSBOND   6 CYS G   13    CYS G   33                          1555   1555  2.03  
SSBOND   7 CYS N   10    CYS N   45                          1555   1555  2.04  
SSBOND   8 CYS P   26    CYS P   29                          1555   1555  2.04  
LINK         SG  CYS A  58                ZN    ZN A1300     1555   1555  2.49  
LINK         SG  CYS A  68                ZN    ZN A1300     1555   1555  2.33  
LINK         NE2 HIS A  71                ZN    ZN A1300     1555   1555  2.06  
LINK         SG  CYS A  98                ZN    ZN A1350     1555   1555  2.26  
LINK         OD1 ASP A 456                MG    MG A1400     1555   1555  2.36  
LINK         OD1 ASP A 458                MG    MG A1400     1555   1555  2.46  
LINK         OD1 ASP A 460                MG    MG A1400     1555   1555  2.61  
LINK        ZN    ZN A1360                 OE2 GLU C  80     1555   1555  1.96  
LINK         ND1 HIS B 570                ZN    ZN B1400     1555   1555  2.25  
LINK         SG  CYS B1064                ZN    ZN B1300     1555   1555  2.11  
LINK         SG  CYS B1067                ZN    ZN B1300     1555   1555  2.44  
LINK         NE2 HIS C 353                ZN    ZN C1000     1555   1555  1.89  
LINK         SG  CYS D 203                FE3  F3S D1001     1555   1555  2.32  
LINK         SG  CYS D 206                FE4  F3S D1001     1555   1555  2.65  
LINK         SG  CYS D 209                FE1  F3S D1001     1555   1555  2.22  
LINK         SG  CYS N   7                ZN    ZN N 100     1555   1555  2.35  
LINK         SG  CYS N  10                ZN    ZN N 100     1555   1555  2.08  
LINK         SG  CYS N  45                ZN    ZN N 100     1555   1555  2.36  
LINK         SG  CYS P   9                ZN    ZN P  50     1555   1555  2.37  
LINK         OG1 THR P  12                ZN    ZN P  50     1555   1555  2.51  
LINK         SG  CYS P  29                ZN    ZN P  50     1555   1555  1.63  
CISPEP   1 LYS A  155    ILE A  156          0         3.97                     
CISPEP   2 PRO A  285    PRO A  286          0       -13.32                     
CISPEP   3 GLN A  422    PRO A  423          0         5.49                     
CISPEP   4 SER B   76    ASP B   77          0         5.11                     
CISPEP   5 ILE B  110    GLU B  111          0        -6.87                     
CISPEP   6 GLU B  113    PRO B  114          0        -3.59                     
CISPEP   7 GLY B  734    TYR B  735          0        -7.10                     
CISPEP   8 VAL B  783    ARG B  784          0        -1.23                     
CISPEP   9 TYR B 1069    ILE B 1070          0        -3.89                     
CISPEP  10 ASP B 1074    LYS B 1075          0         1.12                     
CISPEP  11 LYS B 1077    ASN B 1078          0         3.08                     
CISPEP  12 MET C  163    SER C  164          0         4.13                     
CISPEP  13 LYS C  244    LYS C  245          0        -7.26                     
CISPEP  14 LEU P   21    PRO P   22          0        -0.76                     
SITE     1 AC1  4 CYS A  58  CYS A  61  CYS A  68  HIS A  71                    
SITE     1 AC2  4 CYS A  98  CYS A 101  VAL A 145  CYS A 146                    
SITE     1 AC3  2 HIS A 426  GLU C  80                                          
SITE     1 AC4  3 ASP A 456  ASP A 458  ASP A 460                               
SITE     1 AC5  3 CYS B1064  CYS B1067  CYS B1082                               
SITE     1 AC6  3 ARG B 174  HIS B 570  GLU B 622                               
SITE     1 AC7  3 ARG B 694  HIS B 696  HIS B 997                               
SITE     1 AC8  2 GLU C 348  HIS C 353                                          
SITE     1 AC9  8 CYS D 183  PHE D 188  CYS D 203  LEU D 205                    
SITE     2 AC9  8 CYS D 206  GLU D 207  CYS D 209  ILE D 219                    
SITE     1 BC1  4 CYS N   7  CYS N  10  CYS N  44  CYS N  45                    
SITE     1 BC2  4 CYS P   9  THR P  12  CYS P  26  CYS P  29                    
CRYST1  193.501  212.620  128.998  90.00  90.00  90.00 P 21 21 2     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      0.005168  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004703  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007752        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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