GenomeNet

Database: PDB
Entry: 5D0A
LinkDB: 5D0A
Original site: 5D0A 
HEADER    OXIDOREDUCTASE/RNA                      03-AUG-15   5D0A              
TITLE     CRYSTAL STRUCTURE OF EPOXYQUEUOSINE REDUCTASE WITH CLEAVED RNA STEM   
TITLE    2 LOOP                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPOXYQUEUOSINE REDUCTASE;                                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: QUEUOSINE BIOSYNTHESIS PROTEIN QUEG;                        
COMPND   5 EC: 1.17.99.6;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RNA (5'-                                                   
COMPND   9 R(*G*CP*AP*GP*AP*CP*UP*GP*UP*AP*AP*AP*UP*CP*UP*GP*C)-3');            
COMPND  10 CHAIN: E, F;                                                         
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS (STRAIN 168);                 
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: QUEG, YGAP, YHBA, BSU08910;                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PASK-IBA43PLUS;                           
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  14 ORGANISM_TAXID: 562;                                                 
SOURCE  15 OTHER_DETAILS: SYNTHESIZED BY IDT                                    
KEYWDS    B12, TRNA MODIFICATION, HEAT-DOMAIN, QUEUOSINE, OXIDOREDUCTASE-RNA    
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.P.DOWLING,Z.D.MILES,C.KOHRER,V.BANDARIAN,C.L.DRENNAN                
REVDAT   4   20-SEP-17 5D0A    1       REMARK                                   
REVDAT   3   14-DEC-16 5D0A    1       JRNL                                     
REVDAT   2   05-OCT-16 5D0A    1       JRNL   REMARK                            
REVDAT   1   28-SEP-16 5D0A    0                                                
JRNL        AUTH   D.P.DOWLING,Z.D.MILES,C.KOHRER,S.J.MAIOCCO,S.J.ELLIOTT,      
JRNL        AUTH 2 V.BANDARIAN,C.L.DRENNAN                                      
JRNL        TITL   MOLECULAR BASIS OF COBALAMIN-DEPENDENT RNA MODIFICATION.     
JRNL        REF    NUCLEIC ACIDS RES.            V.  44  9965 2016              
JRNL        REFN                   ESSN 1362-4962                               
JRNL        PMID   27638883                                                     
JRNL        DOI    10.1093/NAR/GKW806                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.39                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 103951                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.910                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5106                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.4021 -  6.5194    0.95     3304   174  0.1720 0.1805        
REMARK   3     2  6.5194 -  5.1768    0.99     3396   194  0.1638 0.1967        
REMARK   3     3  5.1768 -  4.5231    0.97     3299   162  0.1404 0.1906        
REMARK   3     4  4.5231 -  4.1098    0.99     3417   137  0.1406 0.1600        
REMARK   3     5  4.1098 -  3.8154    0.99     3394   180  0.1564 0.1672        
REMARK   3     6  3.8154 -  3.5905    1.00     3370   183  0.1606 0.2069        
REMARK   3     7  3.5905 -  3.4108    0.98     3344   154  0.1776 0.2427        
REMARK   3     8  3.4108 -  3.2623    0.97     3266   177  0.2015 0.2448        
REMARK   3     9  3.2623 -  3.1368    0.99     3357   170  0.2010 0.2519        
REMARK   3    10  3.1368 -  3.0285    0.99     3340   196  0.2085 0.2378        
REMARK   3    11  3.0285 -  2.9339    0.99     3362   149  0.1962 0.2560        
REMARK   3    12  2.9339 -  2.8500    0.99     3356   184  0.1973 0.2423        
REMARK   3    13  2.8500 -  2.7750    0.99     3351   195  0.1878 0.2114        
REMARK   3    14  2.7750 -  2.7073    0.99     3367   165  0.1847 0.2558        
REMARK   3    15  2.7073 -  2.6458    0.98     3337   174  0.1816 0.2334        
REMARK   3    16  2.6458 -  2.5895    0.96     3252   161  0.1865 0.2306        
REMARK   3    17  2.5895 -  2.5377    0.98     3338   168  0.1923 0.2735        
REMARK   3    18  2.5377 -  2.4898    0.98     3322   180  0.1938 0.2582        
REMARK   3    19  2.4898 -  2.4453    0.99     3245   208  0.2061 0.2702        
REMARK   3    20  2.4453 -  2.4039    0.99     3351   192  0.2014 0.2888        
REMARK   3    21  2.4039 -  2.3651    0.99     3324   192  0.2096 0.2649        
REMARK   3    22  2.3651 -  2.3287    0.99     3317   171  0.2036 0.2461        
REMARK   3    23  2.3287 -  2.2945    0.99     3337   197  0.2060 0.2474        
REMARK   3    24  2.2945 -  2.2621    0.99     3306   162  0.2218 0.2543        
REMARK   3    25  2.2621 -  2.2316    0.98     3348   161  0.2292 0.3128        
REMARK   3    26  2.2316 -  2.2026    0.97     3302   152  0.2361 0.2862        
REMARK   3    27  2.2026 -  2.1751    0.94     3138   163  0.2465 0.2896        
REMARK   3    28  2.1751 -  2.1489    0.91     3108   129  0.2564 0.3045        
REMARK   3    29  2.1489 -  2.1239    0.90     3099   139  0.2716 0.3128        
REMARK   3    30  2.1239 -  2.1000    0.84     2798   137  0.2727 0.3444        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.850           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.15                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009          13259                                  
REMARK   3   ANGLE     :  1.088          18146                                  
REMARK   3   CHIRALITY :  0.044           2001                                  
REMARK   3   PLANARITY :  0.006           2300                                  
REMARK   3   DIHEDRAL  : 13.472           5355                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5D0A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212463.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-APR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 104237                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5D08                                                 
REMARK 200                                                                      
REMARK 200 REMARK: SQUARE PYRAMIDAL                                             
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: (0.1 M ACETATE, 0.4 M (NH4)H2PO4, 12%    
REMARK 280  (W/V) PEG 3350, PH 4.5, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 294K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       55.55900            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -27                                                      
REMARK 465     ALA A   -26                                                      
REMARK 465     SER A   -25                                                      
REMARK 465     ARG A   -24                                                      
REMARK 465     GLY A   -23                                                      
REMARK 465     SER A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     GLY A   -15                                                      
REMARK 465     ALA A   -14                                                      
REMARK 465     GLY A   -13                                                      
REMARK 465     ASP A   -12                                                      
REMARK 465     ARG A   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     PRO A    -9                                                      
REMARK 465     GLU A    -8                                                      
REMARK 465     PHE A    -7                                                      
REMARK 465     GLU A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     THR A    -3                                                      
REMARK 465     ARG A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLU A   125                                                      
REMARK 465     LYS A   382                                                      
REMARK 465     GLN A   383                                                      
REMARK 465     GLY A   384                                                      
REMARK 465     LEU A   385                                                      
REMARK 465     SER A   386                                                      
REMARK 465     GLY A   387                                                      
REMARK 465     SER A   388                                                      
REMARK 465     LEU A   389                                                      
REMARK 465     GLU A   390                                                      
REMARK 465     VAL A   391                                                      
REMARK 465     ASP A   392                                                      
REMARK 465     LEU A   393                                                      
REMARK 465     GLN A   394                                                      
REMARK 465     GLY A   395                                                      
REMARK 465     ASP A   396                                                      
REMARK 465     HIS A   397                                                      
REMARK 465     GLY A   398                                                      
REMARK 465     LEU A   399                                                      
REMARK 465     SER A   400                                                      
REMARK 465     ALA A   401                                                      
REMARK 465     TRP A   402                                                      
REMARK 465     SER A   403                                                      
REMARK 465     HIS A   404                                                      
REMARK 465     PRO A   405                                                      
REMARK 465     GLN A   406                                                      
REMARK 465     PHE A   407                                                      
REMARK 465     GLU A   408                                                      
REMARK 465     LYS A   409                                                      
REMARK 465     MET B   -27                                                      
REMARK 465     ALA B   -26                                                      
REMARK 465     SER B   -25                                                      
REMARK 465     ARG B   -24                                                      
REMARK 465     GLY B   -23                                                      
REMARK 465     SER B   -22                                                      
REMARK 465     HIS B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     GLY B   -15                                                      
REMARK 465     ALA B   -14                                                      
REMARK 465     GLY B   -13                                                      
REMARK 465     ASP B   -12                                                      
REMARK 465     ARG B   -11                                                      
REMARK 465     GLY B   -10                                                      
REMARK 465     PRO B    -9                                                      
REMARK 465     GLU B    -8                                                      
REMARK 465     PHE B    -7                                                      
REMARK 465     GLU B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     THR B    -3                                                      
REMARK 465     ARG B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B   125                                                      
REMARK 465     LYS B   382                                                      
REMARK 465     GLN B   383                                                      
REMARK 465     GLY B   384                                                      
REMARK 465     LEU B   385                                                      
REMARK 465     SER B   386                                                      
REMARK 465     GLY B   387                                                      
REMARK 465     SER B   388                                                      
REMARK 465     LEU B   389                                                      
REMARK 465     GLU B   390                                                      
REMARK 465     VAL B   391                                                      
REMARK 465     ASP B   392                                                      
REMARK 465     LEU B   393                                                      
REMARK 465     GLN B   394                                                      
REMARK 465     GLY B   395                                                      
REMARK 465     ASP B   396                                                      
REMARK 465     HIS B   397                                                      
REMARK 465     GLY B   398                                                      
REMARK 465     LEU B   399                                                      
REMARK 465     SER B   400                                                      
REMARK 465     ALA B   401                                                      
REMARK 465     TRP B   402                                                      
REMARK 465     SER B   403                                                      
REMARK 465     HIS B   404                                                      
REMARK 465     PRO B   405                                                      
REMARK 465     GLN B   406                                                      
REMARK 465     PHE B   407                                                      
REMARK 465     GLU B   408                                                      
REMARK 465     LYS B   409                                                      
REMARK 465     MET C   -27                                                      
REMARK 465     ALA C   -26                                                      
REMARK 465     SER C   -25                                                      
REMARK 465     ARG C   -24                                                      
REMARK 465     GLY C   -23                                                      
REMARK 465     SER C   -22                                                      
REMARK 465     HIS C   -21                                                      
REMARK 465     HIS C   -20                                                      
REMARK 465     HIS C   -19                                                      
REMARK 465     HIS C   -18                                                      
REMARK 465     HIS C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     GLY C   -15                                                      
REMARK 465     ALA C   -14                                                      
REMARK 465     GLY C   -13                                                      
REMARK 465     ASP C   -12                                                      
REMARK 465     ARG C   -11                                                      
REMARK 465     GLY C   -10                                                      
REMARK 465     PRO C    -9                                                      
REMARK 465     GLU C    -8                                                      
REMARK 465     PHE C    -7                                                      
REMARK 465     GLU C    -6                                                      
REMARK 465     LEU C    -5                                                      
REMARK 465     GLY C    -4                                                      
REMARK 465     THR C    -3                                                      
REMARK 465     ARG C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C   125                                                      
REMARK 465     GLY C   379                                                      
REMARK 465     MET C   380                                                      
REMARK 465     THR C   381                                                      
REMARK 465     LYS C   382                                                      
REMARK 465     GLN C   383                                                      
REMARK 465     GLY C   384                                                      
REMARK 465     LEU C   385                                                      
REMARK 465     SER C   386                                                      
REMARK 465     GLY C   387                                                      
REMARK 465     SER C   388                                                      
REMARK 465     LEU C   389                                                      
REMARK 465     GLU C   390                                                      
REMARK 465     VAL C   391                                                      
REMARK 465     ASP C   392                                                      
REMARK 465     LEU C   393                                                      
REMARK 465     GLN C   394                                                      
REMARK 465     GLY C   395                                                      
REMARK 465     ASP C   396                                                      
REMARK 465     HIS C   397                                                      
REMARK 465     GLY C   398                                                      
REMARK 465     LEU C   399                                                      
REMARK 465     SER C   400                                                      
REMARK 465     ALA C   401                                                      
REMARK 465     TRP C   402                                                      
REMARK 465     SER C   403                                                      
REMARK 465     HIS C   404                                                      
REMARK 465     PRO C   405                                                      
REMARK 465     GLN C   406                                                      
REMARK 465     PHE C   407                                                      
REMARK 465     GLU C   408                                                      
REMARK 465     LYS C   409                                                      
REMARK 465     MET D   -27                                                      
REMARK 465     ALA D   -26                                                      
REMARK 465     SER D   -25                                                      
REMARK 465     ARG D   -24                                                      
REMARK 465     GLY D   -23                                                      
REMARK 465     SER D   -22                                                      
REMARK 465     HIS D   -21                                                      
REMARK 465     HIS D   -20                                                      
REMARK 465     HIS D   -19                                                      
REMARK 465     HIS D   -18                                                      
REMARK 465     HIS D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     GLY D   -15                                                      
REMARK 465     ALA D   -14                                                      
REMARK 465     GLY D   -13                                                      
REMARK 465     ASP D   -12                                                      
REMARK 465     ARG D   -11                                                      
REMARK 465     GLY D   -10                                                      
REMARK 465     PRO D    -9                                                      
REMARK 465     GLU D    -8                                                      
REMARK 465     PHE D    -7                                                      
REMARK 465     GLU D    -6                                                      
REMARK 465     LEU D    -5                                                      
REMARK 465     GLY D    -4                                                      
REMARK 465     THR D    -3                                                      
REMARK 465     ARG D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLU D   125                                                      
REMARK 465     SER D   378                                                      
REMARK 465     GLY D   379                                                      
REMARK 465     MET D   380                                                      
REMARK 465     THR D   381                                                      
REMARK 465     LYS D   382                                                      
REMARK 465     GLN D   383                                                      
REMARK 465     GLY D   384                                                      
REMARK 465     LEU D   385                                                      
REMARK 465     SER D   386                                                      
REMARK 465     GLY D   387                                                      
REMARK 465     SER D   388                                                      
REMARK 465     LEU D   389                                                      
REMARK 465     GLU D   390                                                      
REMARK 465     VAL D   391                                                      
REMARK 465     ASP D   392                                                      
REMARK 465     LEU D   393                                                      
REMARK 465     GLN D   394                                                      
REMARK 465     GLY D   395                                                      
REMARK 465     ASP D   396                                                      
REMARK 465     HIS D   397                                                      
REMARK 465     GLY D   398                                                      
REMARK 465     LEU D   399                                                      
REMARK 465     SER D   400                                                      
REMARK 465     ALA D   401                                                      
REMARK 465     TRP D   402                                                      
REMARK 465     SER D   403                                                      
REMARK 465     HIS D   404                                                      
REMARK 465     PRO D   405                                                      
REMARK 465     GLN D   406                                                      
REMARK 465     PHE D   407                                                      
REMARK 465     GLU D   408                                                      
REMARK 465     LYS D   409                                                      
REMARK 465       G E    27                                                      
REMARK 465       G E    34                                                      
REMARK 465       U E    35                                                      
REMARK 465       A E    36                                                      
REMARK 465       C E    43                                                      
REMARK 465       G F    34                                                      
REMARK 465       U F    35                                                      
REMARK 465       A F    36                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  86    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  86    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470       C E  28    P    OP1  OP2  O5'  C5'  C4'  O4'                   
REMARK 470       C E  28    C3'  C2'  O2'  C1'  N1   C2   O2                    
REMARK 470       C E  28    N3   C4   N4   C5   C6                              
REMARK 470       G F  27    O5'                                                 
REMARK 470       A F  37    P    OP1  OP2  O5'  C5'  C4'  O4'                   
REMARK 470       A F  37    C3'  C2'  O2'  C1'  N9   C8   N7                    
REMARK 470       A F  37    C5   C6   N6   N1   C2   N3   C4                    
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   758     O    HOH B   768              2.12            
REMARK 500   O    HOH D   733     O    HOH D   762              2.15            
REMARK 500   OE1  GLU D    41     O    HOH D   601              2.17            
REMARK 500   O    HOH C   758     O    HOH C   774              2.18            
REMARK 500   O    HOH B   799     O    HOH B   802              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  91       72.85   -112.23                                   
REMARK 500    ASP A 104      118.07    -28.71                                   
REMARK 500    LYS A 123      -86.58    -77.56                                   
REMARK 500    ASP A 134      -42.09     66.46                                   
REMARK 500    CYS A 156       -7.21     83.31                                   
REMARK 500    HIS A 256       70.32   -119.32                                   
REMARK 500    MET A 380       48.49    -98.46                                   
REMARK 500    GLU B  91       74.68   -119.63                                   
REMARK 500    ASP B 104      115.41    -38.46                                   
REMARK 500    LYS B 123      -95.72    -82.70                                   
REMARK 500    ASP B 134      -42.63     68.66                                   
REMARK 500    CYS B 156       -8.33     75.68                                   
REMARK 500    MET B 380       34.22    -82.75                                   
REMARK 500    LYS C 123      -89.51    -84.78                                   
REMARK 500    ASP C 134      -47.43     68.41                                   
REMARK 500    CYS C 156       -4.85     75.71                                   
REMARK 500    THR C 192       26.70   -146.98                                   
REMARK 500    TYR C 238      122.51   -171.53                                   
REMARK 500    HIS C 256       72.30   -119.35                                   
REMARK 500    LYS D 123      -80.82    -94.30                                   
REMARK 500    ASP D 134      -42.26     67.57                                   
REMARK 500    CYS D 156       -6.19     73.13                                   
REMARK 500    THR D 192       22.54   -142.53                                   
REMARK 500    HIS D 256       67.23   -119.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 803        DISTANCE =  6.38 ANGSTROMS                       
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                             SF4 A 501  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 188   SG                                                     
REMARK 620 2 SF4 A 501   S1  116.8                                              
REMARK 620 3 SF4 A 501   S2  111.0 104.8                                        
REMARK 620 4 SF4 A 501   S3  114.5 104.3 104.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 501  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 191   SG                                                     
REMARK 620 2 SF4 A 501   S1  117.4                                              
REMARK 620 3 SF4 A 501   S3  111.5 103.8                                        
REMARK 620 4 SF4 A 501   S4  114.0 104.3 104.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 501  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 194   SG                                                     
REMARK 620 2 SF4 A 501   S2  119.7                                              
REMARK 620 3 SF4 A 501   S3  111.2 103.6                                        
REMARK 620 4 SF4 A 501   S4  113.1 103.8 103.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 502  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 198   SG                                                     
REMARK 620 2 SF4 A 502   S2  112.1                                              
REMARK 620 3 SF4 A 502   S3  112.6 104.5                                        
REMARK 620 4 SF4 A 502   S4  119.4 102.3 104.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 502  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 214   SG                                                     
REMARK 620 2 SF4 A 502   S1  105.8                                              
REMARK 620 3 SF4 A 502   S2  113.2 104.9                                        
REMARK 620 4 SF4 A 502   S3  123.5 102.8 104.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 502  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 240   SG                                                     
REMARK 620 2 SF4 A 502   S1  106.4                                              
REMARK 620 3 SF4 A 502   S2  120.5 104.5                                        
REMARK 620 4 SF4 A 502   S4  116.2 104.2 103.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 502  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 243   SG                                                     
REMARK 620 2 SF4 A 502   S1  111.0                                              
REMARK 620 3 SF4 A 502   S3  122.1 103.7                                        
REMARK 620 4 SF4 A 502   S4  109.7 104.3 104.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A 501  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 247   SG                                                     
REMARK 620 2 SF4 A 501   S1  108.4                                              
REMARK 620 3 SF4 A 501   S2  117.2 104.6                                        
REMARK 620 4 SF4 A 501   S4  117.1 104.2 103.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 501  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 188   SG                                                     
REMARK 620 2 SF4 B 501   S1  118.0                                              
REMARK 620 3 SF4 B 501   S2  111.3 104.2                                        
REMARK 620 4 SF4 B 501   S3  113.9 104.2 103.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 501  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 191   SG                                                     
REMARK 620 2 SF4 B 501   S1  120.1                                              
REMARK 620 3 SF4 B 501   S3  111.4 103.8                                        
REMARK 620 4 SF4 B 501   S4  111.1 104.5 104.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 501  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 194   SG                                                     
REMARK 620 2 SF4 B 501   S2  118.6                                              
REMARK 620 3 SF4 B 501   S3  112.5 103.7                                        
REMARK 620 4 SF4 B 501   S4  112.9 103.5 104.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 502  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 198   SG                                                     
REMARK 620 2 SF4 B 502   S2  110.0                                              
REMARK 620 3 SF4 B 502   S3  115.2 105.7                                        
REMARK 620 4 SF4 B 502   S4  117.1 103.5 104.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 502  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 214   SG                                                     
REMARK 620 2 SF4 B 502   S1  104.4                                              
REMARK 620 3 SF4 B 502   S2  114.4 104.4                                        
REMARK 620 4 SF4 B 502   S3  123.3 103.0 105.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 502  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 240   SG                                                     
REMARK 620 2 SF4 B 502   S1  106.9                                              
REMARK 620 3 SF4 B 502   S2  118.9 104.3                                        
REMARK 620 4 SF4 B 502   S4  117.7 104.7 102.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 502  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 243   SG                                                     
REMARK 620 2 SF4 B 502   S1  115.4                                              
REMARK 620 3 SF4 B 502   S3  122.8 102.2                                        
REMARK 620 4 SF4 B 502   S4  105.7 105.5 103.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 501  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 247   SG                                                     
REMARK 620 2 SF4 B 501   S1  106.9                                              
REMARK 620 3 SF4 B 501   S2  117.4 104.5                                        
REMARK 620 4 SF4 B 501   S4  118.0 104.5 104.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 501  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 188   SG                                                     
REMARK 620 2 SF4 C 501   S1  118.2                                              
REMARK 620 3 SF4 C 501   S2  107.0 105.1                                        
REMARK 620 4 SF4 C 501   S3  117.3 104.0 103.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 501  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 191   SG                                                     
REMARK 620 2 SF4 C 501   S1  116.2                                              
REMARK 620 3 SF4 C 501   S3  107.0 103.9                                        
REMARK 620 4 SF4 C 501   S4  119.9 103.9 104.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 501  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 194   SG                                                     
REMARK 620 2 SF4 C 501   S2  117.5                                              
REMARK 620 3 SF4 C 501   S3  113.5 103.9                                        
REMARK 620 4 SF4 C 501   S4  112.9 103.6 104.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 502  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 198   SG                                                     
REMARK 620 2 SF4 C 502   S2  112.3                                              
REMARK 620 3 SF4 C 502   S3  113.3 106.3                                        
REMARK 620 4 SF4 C 502   S4  115.6 103.1 105.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 502  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 214   SG                                                     
REMARK 620 2 SF4 C 502   S1  106.6                                              
REMARK 620 3 SF4 C 502   S2  113.3 104.3                                        
REMARK 620 4 SF4 C 502   S3  122.6 102.6 105.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 502  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 240   SG                                                     
REMARK 620 2 SF4 C 502   S1  106.5                                              
REMARK 620 3 SF4 C 502   S2  120.0 103.9                                        
REMARK 620 4 SF4 C 502   S4  117.4 105.4 102.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 502  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 243   SG                                                     
REMARK 620 2 SF4 C 502   S1  111.4                                              
REMARK 620 3 SF4 C 502   S3  124.6 102.1                                        
REMARK 620 4 SF4 C 502   S4  108.2 104.9 103.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 501  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 247   SG                                                     
REMARK 620 2 SF4 C 501   S1  110.5                                              
REMARK 620 3 SF4 C 501   S2  117.0 105.1                                        
REMARK 620 4 SF4 C 501   S4  115.2 104.1 103.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D 501  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 188   SG                                                     
REMARK 620 2 SF4 D 501   S1  120.3                                              
REMARK 620 3 SF4 D 501   S2  107.4 105.4                                        
REMARK 620 4 SF4 D 501   S3  114.1 104.4 103.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D 501  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 191   SG                                                     
REMARK 620 2 SF4 D 501   S1  117.0                                              
REMARK 620 3 SF4 D 501   S3  111.7 104.6                                        
REMARK 620 4 SF4 D 501   S4  113.9 104.1 104.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D 501  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 194   SG                                                     
REMARK 620 2 SF4 D 501   S2  119.9                                              
REMARK 620 3 SF4 D 501   S3  111.3 103.4                                        
REMARK 620 4 SF4 D 501   S4  113.7 103.5 103.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D 502  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 198   SG                                                     
REMARK 620 2 SF4 D 502   S2  111.2                                              
REMARK 620 3 SF4 D 502   S3  114.7 104.5                                        
REMARK 620 4 SF4 D 502   S4  117.5 102.5 104.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D 502  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 214   SG                                                     
REMARK 620 2 SF4 D 502   S1  109.0                                              
REMARK 620 3 SF4 D 502   S2  111.5 104.0                                        
REMARK 620 4 SF4 D 502   S3  123.5 102.6 104.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D 502  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 240   SG                                                     
REMARK 620 2 SF4 D 502   S1  106.5                                              
REMARK 620 3 SF4 D 502   S2  119.9 104.7                                        
REMARK 620 4 SF4 D 502   S4  116.5 105.0 102.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D 502  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 243   SG                                                     
REMARK 620 2 SF4 D 502   S1  111.3                                              
REMARK 620 3 SF4 D 502   S3  125.0 102.8                                        
REMARK 620 4 SF4 D 502   S4  107.7 104.0 104.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D 501  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 247   SG                                                     
REMARK 620 2 SF4 D 501   S1  111.6                                              
REMARK 620 3 SF4 D 501   S2  112.5 105.2                                        
REMARK 620 4 SF4 D 501   S4  117.2 104.5 104.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             B12 A 503  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 652   O                                                      
REMARK 620 2 B12 A 503   N21  93.0                                              
REMARK 620 3 B12 A 503   N22  89.5  88.2                                        
REMARK 620 4 B12 A 503   N23 100.5 165.9  95.9                                  
REMARK 620 5 B12 A 503   N24  98.6  83.6 168.8  90.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             B12 B 503  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 677   O                                                      
REMARK 620 2 B12 B 503   N21  92.8                                              
REMARK 620 3 B12 B 503   N22  89.8  88.9                                        
REMARK 620 4 B12 B 503   N23  95.4 170.6  95.8                                  
REMARK 620 5 B12 B 503   N24  92.9  83.9 172.4  91.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             B12 C 503  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 678   O                                                      
REMARK 620 2 B12 C 503   N21  89.2                                              
REMARK 620 3 B12 C 503   N22  87.4  89.3                                        
REMARK 620 4 B12 C 503   N23  98.0 171.4  95.7                                  
REMARK 620 5 B12 C 503   N24  96.9  83.9 171.9  90.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             B12 D 503  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 693   O                                                      
REMARK 620 2 B12 D 503   N21  95.2                                              
REMARK 620 3 B12 D 503   N22  85.0  88.8                                        
REMARK 620 4 B12 D 503   N23  97.1 167.1  96.1                                  
REMARK 620 5 B12 D 503   N24 100.5  83.3 170.8  90.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue B12 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue B12 B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue B12 C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue B12 D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 505                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5D08   RELATED DB: PDB                                   
REMARK 900 5D08 IS THE SAME PROTEIN, SELENOMETHIONINE LABELED, WITHOUT RNA      
REMARK 900 SUBSTRATE.                                                           
REMARK 900 RELATED ID: 5D0B   RELATED DB: PDB                                   
DBREF  5D0A A    1   386  UNP    P97030   QUEG_BACSU       1    386             
DBREF  5D0A B    1   386  UNP    P97030   QUEG_BACSU       1    386             
DBREF  5D0A C    1   386  UNP    P97030   QUEG_BACSU       1    386             
DBREF  5D0A D    1   386  UNP    P97030   QUEG_BACSU       1    386             
DBREF  5D0A E   27    43  PDB    5D0A     5D0A            27     43             
DBREF  5D0A F   27    43  PDB    5D0A     5D0A            27     43             
SEQADV 5D0A MET A  -27  UNP  P97030              INITIATING METHIONINE          
SEQADV 5D0A ALA A  -26  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER A  -25  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ARG A  -24  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY A  -23  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER A  -22  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS A  -21  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS A  -20  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS A  -19  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS A  -18  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS A  -17  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS A  -16  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY A  -15  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ALA A  -14  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY A  -13  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ASP A  -12  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ARG A  -11  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY A  -10  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A PRO A   -9  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLU A   -8  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A PHE A   -7  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLU A   -6  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LEU A   -5  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY A   -4  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A THR A   -3  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ARG A   -2  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY A   -1  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER A    0  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY A  387  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER A  388  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LEU A  389  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLU A  390  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A VAL A  391  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ASP A  392  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LEU A  393  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLN A  394  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY A  395  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ASP A  396  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS A  397  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY A  398  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LEU A  399  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER A  400  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ALA A  401  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A TRP A  402  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER A  403  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS A  404  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A PRO A  405  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLN A  406  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A PHE A  407  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLU A  408  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LYS A  409  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A MET B  -27  UNP  P97030              INITIATING METHIONINE          
SEQADV 5D0A ALA B  -26  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER B  -25  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ARG B  -24  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY B  -23  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER B  -22  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS B  -21  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS B  -20  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS B  -19  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS B  -18  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS B  -17  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS B  -16  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY B  -15  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ALA B  -14  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY B  -13  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ASP B  -12  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ARG B  -11  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY B  -10  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A PRO B   -9  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLU B   -8  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A PHE B   -7  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLU B   -6  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LEU B   -5  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY B   -4  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A THR B   -3  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ARG B   -2  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY B   -1  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER B    0  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY B  387  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER B  388  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LEU B  389  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLU B  390  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A VAL B  391  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ASP B  392  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LEU B  393  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLN B  394  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY B  395  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ASP B  396  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS B  397  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY B  398  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LEU B  399  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER B  400  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ALA B  401  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A TRP B  402  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER B  403  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS B  404  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A PRO B  405  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLN B  406  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A PHE B  407  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLU B  408  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LYS B  409  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A MET C  -27  UNP  P97030              INITIATING METHIONINE          
SEQADV 5D0A ALA C  -26  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER C  -25  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ARG C  -24  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY C  -23  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER C  -22  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS C  -21  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS C  -20  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS C  -19  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS C  -18  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS C  -17  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS C  -16  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY C  -15  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ALA C  -14  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY C  -13  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ASP C  -12  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ARG C  -11  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY C  -10  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A PRO C   -9  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLU C   -8  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A PHE C   -7  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLU C   -6  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LEU C   -5  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY C   -4  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A THR C   -3  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ARG C   -2  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY C   -1  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER C    0  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY C  387  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER C  388  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LEU C  389  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLU C  390  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A VAL C  391  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ASP C  392  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LEU C  393  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLN C  394  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY C  395  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ASP C  396  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS C  397  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY C  398  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LEU C  399  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER C  400  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ALA C  401  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A TRP C  402  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER C  403  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS C  404  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A PRO C  405  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLN C  406  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A PHE C  407  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLU C  408  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LYS C  409  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A MET D  -27  UNP  P97030              INITIATING METHIONINE          
SEQADV 5D0A ALA D  -26  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER D  -25  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ARG D  -24  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY D  -23  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER D  -22  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS D  -21  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS D  -20  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS D  -19  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS D  -18  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS D  -17  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS D  -16  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY D  -15  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ALA D  -14  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY D  -13  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ASP D  -12  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ARG D  -11  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY D  -10  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A PRO D   -9  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLU D   -8  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A PHE D   -7  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLU D   -6  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LEU D   -5  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY D   -4  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A THR D   -3  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ARG D   -2  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY D   -1  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER D    0  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY D  387  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER D  388  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LEU D  389  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLU D  390  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A VAL D  391  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ASP D  392  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LEU D  393  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLN D  394  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY D  395  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ASP D  396  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS D  397  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLY D  398  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LEU D  399  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER D  400  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A ALA D  401  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A TRP D  402  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A SER D  403  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A HIS D  404  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A PRO D  405  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLN D  406  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A PHE D  407  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A GLU D  408  UNP  P97030              EXPRESSION TAG                 
SEQADV 5D0A LYS D  409  UNP  P97030              EXPRESSION TAG                 
SEQRES   1 A  437  MET ALA SER ARG GLY SER HIS HIS HIS HIS HIS HIS GLY          
SEQRES   2 A  437  ALA GLY ASP ARG GLY PRO GLU PHE GLU LEU GLY THR ARG          
SEQRES   3 A  437  GLY SER MET ASN VAL TYR GLN LEU LYS GLU GLU LEU ILE          
SEQRES   4 A  437  GLU TYR ALA LYS SER ILE GLY VAL ASP LYS ILE GLY PHE          
SEQRES   5 A  437  THR THR ALA ASP THR PHE ASP SER LEU LYS ASP ARG LEU          
SEQRES   6 A  437  ILE LEU GLN GLU SER LEU GLY TYR LEU SER GLY PHE GLU          
SEQRES   7 A  437  GLU PRO ASP ILE GLU LYS ARG VAL THR PRO LYS LEU LEU          
SEQRES   8 A  437  LEU PRO LYS ALA LYS SER ILE VAL ALA ILE ALA LEU ALA          
SEQRES   9 A  437  TYR PRO SER ARG MET LYS ASP ALA PRO ARG SER THR ARG          
SEQRES  10 A  437  THR GLU ARG ARG GLY ILE PHE CYS ARG ALA SER TRP GLY          
SEQRES  11 A  437  LYS ASP TYR HIS ASP VAL LEU ARG GLU LYS LEU ASP LEU          
SEQRES  12 A  437  LEU GLU ASP PHE LEU LYS SER LYS HIS GLU ASP ILE ARG          
SEQRES  13 A  437  THR LYS SER MET VAL ASP THR GLY GLU LEU SER ASP ARG          
SEQRES  14 A  437  ALA VAL ALA GLU ARG ALA GLY ILE GLY PHE SER ALA LYS          
SEQRES  15 A  437  ASN CYS MET ILE THR THR PRO GLU TYR GLY SER TYR VAL          
SEQRES  16 A  437  TYR LEU ALA GLU MET ILE THR ASN ILE PRO PHE GLU PRO          
SEQRES  17 A  437  ASP VAL PRO ILE GLU ASP MET CYS GLY SER CYS THR LYS          
SEQRES  18 A  437  CYS LEU ASP ALA CYS PRO THR GLY ALA LEU VAL ASN PRO          
SEQRES  19 A  437  GLY GLN LEU ASN ALA GLN ARG CYS ILE SER PHE LEU THR          
SEQRES  20 A  437  GLN THR LYS GLY PHE LEU PRO ASP GLU PHE ARG THR LYS          
SEQRES  21 A  437  ILE GLY ASN ARG LEU TYR GLY CYS ASP THR CYS GLN THR          
SEQRES  22 A  437  VAL CYS PRO LEU ASN LYS GLY LYS ASP PHE HIS LEU HIS          
SEQRES  23 A  437  PRO GLU MET GLU PRO ASP PRO GLU ILE ALA LYS PRO LEU          
SEQRES  24 A  437  LEU LYS PRO LEU LEU ALA ILE SER ASN ARG GLU PHE LYS          
SEQRES  25 A  437  GLU LYS PHE GLY HIS VAL SER GLY SER TRP ARG GLY LYS          
SEQRES  26 A  437  LYS PRO ILE GLN ARG ASN ALA ILE LEU ALA LEU ALA HIS          
SEQRES  27 A  437  PHE LYS ASP ALA SER ALA LEU PRO GLU LEU THR GLU LEU          
SEQRES  28 A  437  MET HIS LYS ASP PRO ARG PRO VAL ILE ARG GLY THR ALA          
SEQRES  29 A  437  ALA TRP ALA ILE GLY LYS ILE GLY ASP PRO ALA TYR ALA          
SEQRES  30 A  437  GLU GLU LEU GLU LYS ALA LEU GLU LYS GLU LYS ASP GLU          
SEQRES  31 A  437  GLU ALA LYS LEU GLU ILE GLU LYS GLY ILE GLU LEU LEU          
SEQRES  32 A  437  LYS ALA SER GLY MET THR LYS GLN GLY LEU SER GLY SER          
SEQRES  33 A  437  LEU GLU VAL ASP LEU GLN GLY ASP HIS GLY LEU SER ALA          
SEQRES  34 A  437  TRP SER HIS PRO GLN PHE GLU LYS                              
SEQRES   1 B  437  MET ALA SER ARG GLY SER HIS HIS HIS HIS HIS HIS GLY          
SEQRES   2 B  437  ALA GLY ASP ARG GLY PRO GLU PHE GLU LEU GLY THR ARG          
SEQRES   3 B  437  GLY SER MET ASN VAL TYR GLN LEU LYS GLU GLU LEU ILE          
SEQRES   4 B  437  GLU TYR ALA LYS SER ILE GLY VAL ASP LYS ILE GLY PHE          
SEQRES   5 B  437  THR THR ALA ASP THR PHE ASP SER LEU LYS ASP ARG LEU          
SEQRES   6 B  437  ILE LEU GLN GLU SER LEU GLY TYR LEU SER GLY PHE GLU          
SEQRES   7 B  437  GLU PRO ASP ILE GLU LYS ARG VAL THR PRO LYS LEU LEU          
SEQRES   8 B  437  LEU PRO LYS ALA LYS SER ILE VAL ALA ILE ALA LEU ALA          
SEQRES   9 B  437  TYR PRO SER ARG MET LYS ASP ALA PRO ARG SER THR ARG          
SEQRES  10 B  437  THR GLU ARG ARG GLY ILE PHE CYS ARG ALA SER TRP GLY          
SEQRES  11 B  437  LYS ASP TYR HIS ASP VAL LEU ARG GLU LYS LEU ASP LEU          
SEQRES  12 B  437  LEU GLU ASP PHE LEU LYS SER LYS HIS GLU ASP ILE ARG          
SEQRES  13 B  437  THR LYS SER MET VAL ASP THR GLY GLU LEU SER ASP ARG          
SEQRES  14 B  437  ALA VAL ALA GLU ARG ALA GLY ILE GLY PHE SER ALA LYS          
SEQRES  15 B  437  ASN CYS MET ILE THR THR PRO GLU TYR GLY SER TYR VAL          
SEQRES  16 B  437  TYR LEU ALA GLU MET ILE THR ASN ILE PRO PHE GLU PRO          
SEQRES  17 B  437  ASP VAL PRO ILE GLU ASP MET CYS GLY SER CYS THR LYS          
SEQRES  18 B  437  CYS LEU ASP ALA CYS PRO THR GLY ALA LEU VAL ASN PRO          
SEQRES  19 B  437  GLY GLN LEU ASN ALA GLN ARG CYS ILE SER PHE LEU THR          
SEQRES  20 B  437  GLN THR LYS GLY PHE LEU PRO ASP GLU PHE ARG THR LYS          
SEQRES  21 B  437  ILE GLY ASN ARG LEU TYR GLY CYS ASP THR CYS GLN THR          
SEQRES  22 B  437  VAL CYS PRO LEU ASN LYS GLY LYS ASP PHE HIS LEU HIS          
SEQRES  23 B  437  PRO GLU MET GLU PRO ASP PRO GLU ILE ALA LYS PRO LEU          
SEQRES  24 B  437  LEU LYS PRO LEU LEU ALA ILE SER ASN ARG GLU PHE LYS          
SEQRES  25 B  437  GLU LYS PHE GLY HIS VAL SER GLY SER TRP ARG GLY LYS          
SEQRES  26 B  437  LYS PRO ILE GLN ARG ASN ALA ILE LEU ALA LEU ALA HIS          
SEQRES  27 B  437  PHE LYS ASP ALA SER ALA LEU PRO GLU LEU THR GLU LEU          
SEQRES  28 B  437  MET HIS LYS ASP PRO ARG PRO VAL ILE ARG GLY THR ALA          
SEQRES  29 B  437  ALA TRP ALA ILE GLY LYS ILE GLY ASP PRO ALA TYR ALA          
SEQRES  30 B  437  GLU GLU LEU GLU LYS ALA LEU GLU LYS GLU LYS ASP GLU          
SEQRES  31 B  437  GLU ALA LYS LEU GLU ILE GLU LYS GLY ILE GLU LEU LEU          
SEQRES  32 B  437  LYS ALA SER GLY MET THR LYS GLN GLY LEU SER GLY SER          
SEQRES  33 B  437  LEU GLU VAL ASP LEU GLN GLY ASP HIS GLY LEU SER ALA          
SEQRES  34 B  437  TRP SER HIS PRO GLN PHE GLU LYS                              
SEQRES   1 C  437  MET ALA SER ARG GLY SER HIS HIS HIS HIS HIS HIS GLY          
SEQRES   2 C  437  ALA GLY ASP ARG GLY PRO GLU PHE GLU LEU GLY THR ARG          
SEQRES   3 C  437  GLY SER MET ASN VAL TYR GLN LEU LYS GLU GLU LEU ILE          
SEQRES   4 C  437  GLU TYR ALA LYS SER ILE GLY VAL ASP LYS ILE GLY PHE          
SEQRES   5 C  437  THR THR ALA ASP THR PHE ASP SER LEU LYS ASP ARG LEU          
SEQRES   6 C  437  ILE LEU GLN GLU SER LEU GLY TYR LEU SER GLY PHE GLU          
SEQRES   7 C  437  GLU PRO ASP ILE GLU LYS ARG VAL THR PRO LYS LEU LEU          
SEQRES   8 C  437  LEU PRO LYS ALA LYS SER ILE VAL ALA ILE ALA LEU ALA          
SEQRES   9 C  437  TYR PRO SER ARG MET LYS ASP ALA PRO ARG SER THR ARG          
SEQRES  10 C  437  THR GLU ARG ARG GLY ILE PHE CYS ARG ALA SER TRP GLY          
SEQRES  11 C  437  LYS ASP TYR HIS ASP VAL LEU ARG GLU LYS LEU ASP LEU          
SEQRES  12 C  437  LEU GLU ASP PHE LEU LYS SER LYS HIS GLU ASP ILE ARG          
SEQRES  13 C  437  THR LYS SER MET VAL ASP THR GLY GLU LEU SER ASP ARG          
SEQRES  14 C  437  ALA VAL ALA GLU ARG ALA GLY ILE GLY PHE SER ALA LYS          
SEQRES  15 C  437  ASN CYS MET ILE THR THR PRO GLU TYR GLY SER TYR VAL          
SEQRES  16 C  437  TYR LEU ALA GLU MET ILE THR ASN ILE PRO PHE GLU PRO          
SEQRES  17 C  437  ASP VAL PRO ILE GLU ASP MET CYS GLY SER CYS THR LYS          
SEQRES  18 C  437  CYS LEU ASP ALA CYS PRO THR GLY ALA LEU VAL ASN PRO          
SEQRES  19 C  437  GLY GLN LEU ASN ALA GLN ARG CYS ILE SER PHE LEU THR          
SEQRES  20 C  437  GLN THR LYS GLY PHE LEU PRO ASP GLU PHE ARG THR LYS          
SEQRES  21 C  437  ILE GLY ASN ARG LEU TYR GLY CYS ASP THR CYS GLN THR          
SEQRES  22 C  437  VAL CYS PRO LEU ASN LYS GLY LYS ASP PHE HIS LEU HIS          
SEQRES  23 C  437  PRO GLU MET GLU PRO ASP PRO GLU ILE ALA LYS PRO LEU          
SEQRES  24 C  437  LEU LYS PRO LEU LEU ALA ILE SER ASN ARG GLU PHE LYS          
SEQRES  25 C  437  GLU LYS PHE GLY HIS VAL SER GLY SER TRP ARG GLY LYS          
SEQRES  26 C  437  LYS PRO ILE GLN ARG ASN ALA ILE LEU ALA LEU ALA HIS          
SEQRES  27 C  437  PHE LYS ASP ALA SER ALA LEU PRO GLU LEU THR GLU LEU          
SEQRES  28 C  437  MET HIS LYS ASP PRO ARG PRO VAL ILE ARG GLY THR ALA          
SEQRES  29 C  437  ALA TRP ALA ILE GLY LYS ILE GLY ASP PRO ALA TYR ALA          
SEQRES  30 C  437  GLU GLU LEU GLU LYS ALA LEU GLU LYS GLU LYS ASP GLU          
SEQRES  31 C  437  GLU ALA LYS LEU GLU ILE GLU LYS GLY ILE GLU LEU LEU          
SEQRES  32 C  437  LYS ALA SER GLY MET THR LYS GLN GLY LEU SER GLY SER          
SEQRES  33 C  437  LEU GLU VAL ASP LEU GLN GLY ASP HIS GLY LEU SER ALA          
SEQRES  34 C  437  TRP SER HIS PRO GLN PHE GLU LYS                              
SEQRES   1 D  437  MET ALA SER ARG GLY SER HIS HIS HIS HIS HIS HIS GLY          
SEQRES   2 D  437  ALA GLY ASP ARG GLY PRO GLU PHE GLU LEU GLY THR ARG          
SEQRES   3 D  437  GLY SER MET ASN VAL TYR GLN LEU LYS GLU GLU LEU ILE          
SEQRES   4 D  437  GLU TYR ALA LYS SER ILE GLY VAL ASP LYS ILE GLY PHE          
SEQRES   5 D  437  THR THR ALA ASP THR PHE ASP SER LEU LYS ASP ARG LEU          
SEQRES   6 D  437  ILE LEU GLN GLU SER LEU GLY TYR LEU SER GLY PHE GLU          
SEQRES   7 D  437  GLU PRO ASP ILE GLU LYS ARG VAL THR PRO LYS LEU LEU          
SEQRES   8 D  437  LEU PRO LYS ALA LYS SER ILE VAL ALA ILE ALA LEU ALA          
SEQRES   9 D  437  TYR PRO SER ARG MET LYS ASP ALA PRO ARG SER THR ARG          
SEQRES  10 D  437  THR GLU ARG ARG GLY ILE PHE CYS ARG ALA SER TRP GLY          
SEQRES  11 D  437  LYS ASP TYR HIS ASP VAL LEU ARG GLU LYS LEU ASP LEU          
SEQRES  12 D  437  LEU GLU ASP PHE LEU LYS SER LYS HIS GLU ASP ILE ARG          
SEQRES  13 D  437  THR LYS SER MET VAL ASP THR GLY GLU LEU SER ASP ARG          
SEQRES  14 D  437  ALA VAL ALA GLU ARG ALA GLY ILE GLY PHE SER ALA LYS          
SEQRES  15 D  437  ASN CYS MET ILE THR THR PRO GLU TYR GLY SER TYR VAL          
SEQRES  16 D  437  TYR LEU ALA GLU MET ILE THR ASN ILE PRO PHE GLU PRO          
SEQRES  17 D  437  ASP VAL PRO ILE GLU ASP MET CYS GLY SER CYS THR LYS          
SEQRES  18 D  437  CYS LEU ASP ALA CYS PRO THR GLY ALA LEU VAL ASN PRO          
SEQRES  19 D  437  GLY GLN LEU ASN ALA GLN ARG CYS ILE SER PHE LEU THR          
SEQRES  20 D  437  GLN THR LYS GLY PHE LEU PRO ASP GLU PHE ARG THR LYS          
SEQRES  21 D  437  ILE GLY ASN ARG LEU TYR GLY CYS ASP THR CYS GLN THR          
SEQRES  22 D  437  VAL CYS PRO LEU ASN LYS GLY LYS ASP PHE HIS LEU HIS          
SEQRES  23 D  437  PRO GLU MET GLU PRO ASP PRO GLU ILE ALA LYS PRO LEU          
SEQRES  24 D  437  LEU LYS PRO LEU LEU ALA ILE SER ASN ARG GLU PHE LYS          
SEQRES  25 D  437  GLU LYS PHE GLY HIS VAL SER GLY SER TRP ARG GLY LYS          
SEQRES  26 D  437  LYS PRO ILE GLN ARG ASN ALA ILE LEU ALA LEU ALA HIS          
SEQRES  27 D  437  PHE LYS ASP ALA SER ALA LEU PRO GLU LEU THR GLU LEU          
SEQRES  28 D  437  MET HIS LYS ASP PRO ARG PRO VAL ILE ARG GLY THR ALA          
SEQRES  29 D  437  ALA TRP ALA ILE GLY LYS ILE GLY ASP PRO ALA TYR ALA          
SEQRES  30 D  437  GLU GLU LEU GLU LYS ALA LEU GLU LYS GLU LYS ASP GLU          
SEQRES  31 D  437  GLU ALA LYS LEU GLU ILE GLU LYS GLY ILE GLU LEU LEU          
SEQRES  32 D  437  LYS ALA SER GLY MET THR LYS GLN GLY LEU SER GLY SER          
SEQRES  33 D  437  LEU GLU VAL ASP LEU GLN GLY ASP HIS GLY LEU SER ALA          
SEQRES  34 D  437  TRP SER HIS PRO GLN PHE GLU LYS                              
SEQRES   1 E   17    G   C   A   G   A   C   U   G   U   A   A   A   U          
SEQRES   2 E   17    C   U   G   C                                              
SEQRES   1 F   17    G   C   A   G   A   C   U   G   U   A   A   A   U          
SEQRES   2 F   17    C   U   G   C                                              
HET    SF4  A 501       8                                                       
HET    SF4  A 502       8                                                       
HET    B12  A 503      91                                                       
HET    GOL  A 504       6                                                       
HET    PO4  A 505       5                                                       
HET    SF4  B 501       8                                                       
HET    SF4  B 502       8                                                       
HET    B12  B 503      91                                                       
HET    GOL  B 504       6                                                       
HET    PO4  B 505       5                                                       
HET    SF4  C 501       8                                                       
HET    SF4  C 502       8                                                       
HET    B12  C 503      91                                                       
HET    GOL  C 504       6                                                       
HET    PO4  C 505       5                                                       
HET    SF4  D 501       8                                                       
HET    SF4  D 502       8                                                       
HET    B12  D 503      91                                                       
HET    GOL  D 504       6                                                       
HET    PO4  D 505       5                                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     B12 COBALAMIN                                                        
HETNAM     GOL GLYCEROL                                                         
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   7  SF4    8(FE4 S4)                                                    
FORMUL   9  B12    4(C62 H89 CO N13 O14 P 2+)                                   
FORMUL  10  GOL    4(C3 H8 O3)                                                  
FORMUL  11  PO4    4(O4 P 3-)                                                   
FORMUL  27  HOH   *794(H2 O)                                                    
HELIX    1 AA1 ASN A    2  ILE A   17  1                                  16    
HELIX    2 AA2 PHE A   30  LEU A   43  1                                  14    
HELIX    3 AA3 ASP A   53  THR A   59  1                                   7    
HELIX    4 AA4 THR A   59  LEU A   64  1                                   6    
HELIX    5 AA5 ARG A   98  TRP A  101  5                                   4    
HELIX    6 AA6 ASP A  104  SER A  122  1                                  19    
HELIX    7 AA7 SER A  139  ALA A  147  1                                   9    
HELIX    8 AA8 THR A  192  CYS A  198  1                                   7    
HELIX    9 AA9 ALA A  211  ARG A  213  5                                   3    
HELIX   10 AB1 CYS A  214  GLN A  220  1                                   7    
HELIX   11 AB2 PRO A  226  THR A  231  1                                   6    
HELIX   12 AB3 ASP A  241  VAL A  246  1                                   6    
HELIX   13 AB4 CYS A  247  LYS A  251  5                                   5    
HELIX   14 AB5 HIS A  258  GLU A  262  5                                   5    
HELIX   15 AB6 ASP A  264  LYS A  269  1                                   6    
HELIX   16 AB7 LEU A  271  LEU A  276  1                                   6    
HELIX   17 AB8 SER A  279  GLY A  288  1                                  10    
HELIX   18 AB9 VAL A  290  TRP A  294  5                                   5    
HELIX   19 AC1 GLY A  296  PHE A  311  1                                  16    
HELIX   20 AC2 ASP A  313  SER A  315  5                                   3    
HELIX   21 AC3 ALA A  316  ASP A  327  1                                  12    
HELIX   22 AC4 ARG A  329  GLY A  344  1                                  16    
HELIX   23 AC5 ASP A  345  ALA A  347  5                                   3    
HELIX   24 AC6 TYR A  348  GLU A  357  1                                  10    
HELIX   25 AC7 ASP A  361  MET A  380  1                                  20    
HELIX   26 AC8 VAL B    3  ILE B   17  1                                  15    
HELIX   27 AC9 PHE B   30  GLY B   44  1                                  15    
HELIX   28 AD1 ASP B   53  THR B   59  1                                   7    
HELIX   29 AD2 THR B   59  LEU B   64  1                                   6    
HELIX   30 AD3 ARG B   98  TRP B  101  5                                   4    
HELIX   31 AD4 ASP B  104  SER B  122  1                                  19    
HELIX   32 AD5 SER B  139  ALA B  147  1                                   9    
HELIX   33 AD6 THR B  192  CYS B  198  1                                   7    
HELIX   34 AD7 ALA B  211  ARG B  213  5                                   3    
HELIX   35 AD8 CYS B  214  GLN B  220  1                                   7    
HELIX   36 AD9 PRO B  226  THR B  231  1                                   6    
HELIX   37 AE1 ASP B  241  VAL B  246  1                                   6    
HELIX   38 AE2 CYS B  247  LYS B  251  5                                   5    
HELIX   39 AE3 HIS B  258  GLU B  262  5                                   5    
HELIX   40 AE4 ASP B  264  LYS B  269  1                                   6    
HELIX   41 AE5 LEU B  271  LEU B  276  1                                   6    
HELIX   42 AE6 SER B  279  GLY B  288  1                                  10    
HELIX   43 AE7 VAL B  290  TRP B  294  5                                   5    
HELIX   44 AE8 LYS B  297  PHE B  311  1                                  15    
HELIX   45 AE9 ASP B  313  SER B  315  5                                   3    
HELIX   46 AF1 ALA B  316  ASP B  327  1                                  12    
HELIX   47 AF2 ARG B  329  GLY B  344  1                                  16    
HELIX   48 AF3 ASP B  345  ALA B  347  5                                   3    
HELIX   49 AF4 TYR B  348  GLU B  357  1                                  10    
HELIX   50 AF5 ASP B  361  MET B  380  1                                  20    
HELIX   51 AF6 VAL C    3  ILE C   17  1                                  15    
HELIX   52 AF7 PHE C   30  LEU C   43  1                                  14    
HELIX   53 AF8 ASP C   53  THR C   59  1                                   7    
HELIX   54 AF9 THR C   59  LEU C   64  1                                   6    
HELIX   55 AG1 ARG C   98  TRP C  101  5                                   4    
HELIX   56 AG2 ASP C  104  SER C  122  1                                  19    
HELIX   57 AG3 SER C  139  ALA C  147  1                                   9    
HELIX   58 AG4 THR C  192  CYS C  198  1                                   7    
HELIX   59 AG5 ALA C  211  ARG C  213  5                                   3    
HELIX   60 AG6 CYS C  214  GLN C  220  1                                   7    
HELIX   61 AG7 PRO C  226  ARG C  230  5                                   5    
HELIX   62 AG8 ASP C  241  VAL C  246  1                                   6    
HELIX   63 AG9 CYS C  247  LYS C  251  5                                   5    
HELIX   64 AH1 HIS C  258  GLU C  262  5                                   5    
HELIX   65 AH2 ASP C  264  LYS C  269  1                                   6    
HELIX   66 AH3 LEU C  272  ALA C  277  5                                   6    
HELIX   67 AH4 SER C  279  GLY C  288  1                                  10    
HELIX   68 AH5 VAL C  290  TRP C  294  5                                   5    
HELIX   69 AH6 LYS C  297  LYS C  312  1                                  16    
HELIX   70 AH7 ASP C  313  SER C  315  5                                   3    
HELIX   71 AH8 ALA C  316  ASP C  327  1                                  12    
HELIX   72 AH9 ARG C  329  GLY C  344  1                                  16    
HELIX   73 AI1 ASP C  345  ALA C  347  5                                   3    
HELIX   74 AI2 TYR C  348  GLU C  357  1                                  10    
HELIX   75 AI3 ASP C  361  SER C  378  1                                  18    
HELIX   76 AI4 VAL D    3  ILE D   17  1                                  15    
HELIX   77 AI5 PHE D   30  LEU D   43  1                                  14    
HELIX   78 AI6 ASP D   53  THR D   59  1                                   7    
HELIX   79 AI7 THR D   59  LEU D   64  1                                   6    
HELIX   80 AI8 ARG D   98  TRP D  101  5                                   4    
HELIX   81 AI9 ASP D  104  SER D  122  1                                  19    
HELIX   82 AJ1 SER D  139  ALA D  147  1                                   9    
HELIX   83 AJ2 THR D  192  CYS D  198  1                                   7    
HELIX   84 AJ3 ALA D  211  ARG D  213  5                                   3    
HELIX   85 AJ4 CYS D  214  GLN D  220  1                                   7    
HELIX   86 AJ5 PRO D  226  ARG D  230  5                                   5    
HELIX   87 AJ6 ASP D  241  VAL D  246  1                                   6    
HELIX   88 AJ7 CYS D  247  LYS D  251  5                                   5    
HELIX   89 AJ8 HIS D  258  GLU D  262  5                                   5    
HELIX   90 AJ9 ASP D  264  LYS D  269  1                                   6    
HELIX   91 AK1 LEU D  271  ALA D  277  1                                   7    
HELIX   92 AK2 SER D  279  GLY D  288  1                                  10    
HELIX   93 AK3 VAL D  290  TRP D  294  5                                   5    
HELIX   94 AK4 GLY D  296  PHE D  311  1                                  16    
HELIX   95 AK5 ASP D  313  SER D  315  5                                   3    
HELIX   96 AK6 ALA D  316  ASP D  327  1                                  12    
HELIX   97 AK7 ARG D  329  GLY D  344  1                                  16    
HELIX   98 AK8 ASP D  345  ALA D  347  5                                   3    
HELIX   99 AK9 TYR D  348  GLU D  359  1                                  12    
HELIX  100 AL1 ASP D  361  ALA D  377  1                                  17    
SHEET    1 AA1 4 LYS A  21  THR A  26  0                                        
SHEET    2 AA1 4 SER A  69  ALA A  76 -1  O  ILE A  70   N  THR A  25           
SHEET    3 AA1 4 VAL A 167  THR A 174 -1  O  MET A 172   N  VAL A  71           
SHEET    4 AA1 4 THR A 129  MET A 132 -1  N  LYS A 130   O  ILE A 173           
SHEET    1 AA2 2 ILE A  95  PHE A  96  0                                        
SHEET    2 AA2 2 ARG A 236  TYR A 238  1  O  LEU A 237   N  ILE A  95           
SHEET    1 AA3 2 PHE A 151  SER A 152  0                                        
SHEET    2 AA3 2 ILE A 158  THR A 159 -1  O  THR A 159   N  PHE A 151           
SHEET    1 AA4 2 LEU A 203  ASN A 205  0                                        
SHEET    2 AA4 2 GLN A 208  LEU A 209 -1  O  GLN A 208   N  ASN A 205           
SHEET    1 AA5 4 LYS B  21  THR B  26  0                                        
SHEET    2 AA5 4 SER B  69  ALA B  76 -1  O  ILE B  70   N  THR B  25           
SHEET    3 AA5 4 VAL B 167  THR B 174 -1  O  TYR B 168   N  LEU B  75           
SHEET    4 AA5 4 THR B 129  MET B 132 -1  N  LYS B 130   O  ILE B 173           
SHEET    1 AA6 2 ILE B  95  PHE B  96  0                                        
SHEET    2 AA6 2 ARG B 236  TYR B 238  1  O  LEU B 237   N  ILE B  95           
SHEET    1 AA7 2 PHE B 151  SER B 152  0                                        
SHEET    2 AA7 2 ILE B 158  THR B 159 -1  O  THR B 159   N  PHE B 151           
SHEET    1 AA8 2 LEU B 203  ASN B 205  0                                        
SHEET    2 AA8 2 GLN B 208  LEU B 209 -1  O  GLN B 208   N  ASN B 205           
SHEET    1 AA9 4 LYS C  21  THR C  26  0                                        
SHEET    2 AA9 4 SER C  69  ALA C  76 -1  O  ILE C  70   N  THR C  25           
SHEET    3 AA9 4 VAL C 167  THR C 174 -1  O  MET C 172   N  VAL C  71           
SHEET    4 AA9 4 THR C 129  MET C 132 -1  N  LYS C 130   O  ILE C 173           
SHEET    1 AB1 2 ILE C  95  PHE C  96  0                                        
SHEET    2 AB1 2 ARG C 236  TYR C 238  1  O  LEU C 237   N  ILE C  95           
SHEET    1 AB2 2 PHE C 151  SER C 152  0                                        
SHEET    2 AB2 2 ILE C 158  THR C 159 -1  O  THR C 159   N  PHE C 151           
SHEET    1 AB3 2 LEU C 203  ASN C 205  0                                        
SHEET    2 AB3 2 GLN C 208  LEU C 209 -1  O  GLN C 208   N  ASN C 205           
SHEET    1 AB4 4 LYS D  21  THR D  26  0                                        
SHEET    2 AB4 4 SER D  69  ALA D  76 -1  O  ILE D  70   N  THR D  25           
SHEET    3 AB4 4 VAL D 167  THR D 174 -1  O  ALA D 170   N  ILE D  73           
SHEET    4 AB4 4 THR D 129  MET D 132 -1  N  LYS D 130   O  ILE D 173           
SHEET    1 AB5 2 ILE D  95  PHE D  96  0                                        
SHEET    2 AB5 2 ARG D 236  TYR D 238  1  O  LEU D 237   N  ILE D  95           
SHEET    1 AB6 2 PHE D 151  SER D 152  0                                        
SHEET    2 AB6 2 ILE D 158  THR D 159 -1  O  THR D 159   N  PHE D 151           
SHEET    1 AB7 2 LEU D 203  ASN D 205  0                                        
SHEET    2 AB7 2 GLN D 208  LEU D 209 -1  O  GLN D 208   N  ASN D 205           
LINK         SG  CYS A 188                FE4  SF4 A 501     1555   1555  2.24  
LINK         SG  CYS A 191                FE2  SF4 A 501     1555   1555  2.29  
LINK         SG  CYS A 194                FE1  SF4 A 501     1555   1555  2.30  
LINK         SG  CYS A 198                FE1  SF4 A 502     1555   1555  2.29  
LINK         SG  CYS A 214                FE4  SF4 A 502     1555   1555  2.28  
LINK         SG  CYS A 240                FE3  SF4 A 502     1555   1555  2.29  
LINK         SG  CYS A 243                FE2  SF4 A 502     1555   1555  2.30  
LINK         SG  CYS A 247                FE3  SF4 A 501     1555   1555  2.28  
LINK         SG  CYS B 188                FE4  SF4 B 501     1555   1555  2.21  
LINK         SG  CYS B 191                FE2  SF4 B 501     1555   1555  2.31  
LINK         SG  CYS B 194                FE1  SF4 B 501     1555   1555  2.33  
LINK         SG  CYS B 198                FE1  SF4 B 502     1555   1555  2.32  
LINK         SG  CYS B 214                FE4  SF4 B 502     1555   1555  2.27  
LINK         SG  CYS B 240                FE3  SF4 B 502     1555   1555  2.31  
LINK         SG  CYS B 243                FE2  SF4 B 502     1555   1555  2.29  
LINK         SG  CYS B 247                FE3  SF4 B 501     1555   1555  2.29  
LINK         SG  CYS C 188                FE4  SF4 C 501     1555   1555  2.29  
LINK         SG  CYS C 191                FE2  SF4 C 501     1555   1555  2.28  
LINK         SG  CYS C 194                FE1  SF4 C 501     1555   1555  2.30  
LINK         SG  CYS C 198                FE1  SF4 C 502     1555   1555  2.29  
LINK         SG  CYS C 214                FE4  SF4 C 502     1555   1555  2.27  
LINK         SG  CYS C 240                FE3  SF4 C 502     1555   1555  2.28  
LINK         SG  CYS C 243                FE2  SF4 C 502     1555   1555  2.30  
LINK         SG  CYS C 247                FE3  SF4 C 501     1555   1555  2.26  
LINK         SG  CYS D 188                FE4  SF4 D 501     1555   1555  2.30  
LINK         SG  CYS D 191                FE2  SF4 D 501     1555   1555  2.26  
LINK         SG  CYS D 194                FE1  SF4 D 501     1555   1555  2.32  
LINK         SG  CYS D 198                FE1  SF4 D 502     1555   1555  2.29  
LINK         SG  CYS D 214                FE4  SF4 D 502     1555   1555  2.28  
LINK         SG  CYS D 240                FE3  SF4 D 502     1555   1555  2.28  
LINK         SG  CYS D 243                FE2  SF4 D 502     1555   1555  2.32  
LINK         SG  CYS D 247                FE3  SF4 D 501     1555   1555  2.28  
LINK        CO   B12 A 503                 O   HOH A 652     1555   1555  2.62  
LINK        CO   B12 B 503                 O   HOH B 677     1555   1555  2.58  
LINK        CO   B12 C 503                 O   HOH C 678     1555   1555  2.54  
LINK        CO   B12 D 503                 O   HOH D 693     1555   1555  2.56  
SITE     1 AC1  8 ALA A 153  LYS A 154  ASN A 155  CYS A 188                    
SITE     2 AC1  8 CYS A 191  CYS A 194  CYS A 247  LEU A 249                    
SITE     1 AC2  8 CYS A 198  PRO A 199  LEU A 209  CYS A 214                    
SITE     2 AC2  8 ILE A 215  CYS A 240  THR A 242  CYS A 243                    
SITE     1 AC3 38 SER A  32  LEU A  33  ARG A  36  SER A  47                    
SITE     2 AC3 38 PHE A  49  GLU A  50  ARG A  57  CYS A  97                    
SITE     3 AC3 38 ASP A 134  LEU A 138  SER A 139  ASP A 140                    
SITE     4 AC3 38 ARG A 141  ALA A 142  SER A 152  ASN A 155                    
SITE     5 AC3 38 CYS A 156  MET A 157  ILE A 158  SER A 165                    
SITE     6 AC3 38 VAL A 167  LEU A 169  PRO A 206  LEU A 209                    
SITE     7 AC3 38 SER A 216  PHE A 217  GLY A 239  CYS A 240                    
SITE     8 AC3 38 ASP A 241  CYS A 243  GLN A 244  HOH A 630                    
SITE     9 AC3 38 HOH A 632  HOH A 635  HOH A 652  HOH A 683                    
SITE    10 AC3 38 HOH A 692  HOH A 747                                          
SITE     1 AC4  7 PHE A  49  ASP A 134  GLN A 220  TYR A 238                    
SITE     2 AC4  7 TRP A 294  HOH A 652  HOH A 653                               
SITE     1 AC5  6 LYS A 112  HIS A 258  PRO A 259  GLU A 260                    
SITE     2 AC5  6 HOH A 639  HOH A 682                                          
SITE     1 AC6  7 ALA B 153  LYS B 154  ASN B 155  CYS B 188                    
SITE     2 AC6  7 CYS B 191  CYS B 194  CYS B 247                               
SITE     1 AC7  8 CYS B 198  LEU B 203  LEU B 209  CYS B 214                    
SITE     2 AC7  8 ILE B 215  CYS B 240  THR B 242  CYS B 243                    
SITE     1 AC8 35 SER B  32  LEU B  33  ARG B  36  SER B  47                    
SITE     2 AC8 35 GLU B  50  ARG B  57  CYS B  97  ASP B 134                    
SITE     3 AC8 35 LEU B 138  SER B 139  ASP B 140  ARG B 141                    
SITE     4 AC8 35 SER B 152  ASN B 155  CYS B 156  MET B 157                    
SITE     5 AC8 35 ILE B 158  SER B 165  VAL B 167  LEU B 169                    
SITE     6 AC8 35 PRO B 206  GLY B 207  LEU B 209  SER B 216                    
SITE     7 AC8 35 GLY B 239  CYS B 240  ASP B 241  CYS B 243                    
SITE     8 AC8 35 GLN B 244  HOH B 616  HOH B 628  HOH B 640                    
SITE     9 AC8 35 HOH B 643  HOH B 668  HOH B 677                               
SITE     1 AC9  6 ASP B 134  GLN B 220  TYR B 238  TRP B 294                    
SITE     2 AC9  6 HOH B 657  HOH B 677                                          
SITE     1 AD1  4 LYS B 112  HIS B 258  PRO B 259  GLU B 260                    
SITE     1 AD2  7 ALA C 153  LYS C 154  ASN C 155  CYS C 188                    
SITE     2 AD2  7 CYS C 191  CYS C 194  CYS C 247                               
SITE     1 AD3  7 CYS C 198  LEU C 209  CYS C 214  ILE C 215                    
SITE     2 AD3  7 CYS C 240  THR C 242  CYS C 243                               
SITE     1 AD4 38 SER C  32  LEU C  33  ARG C  36  SER C  47                    
SITE     2 AD4 38 PHE C  49  GLU C  50  ARG C  57  CYS C  97                    
SITE     3 AD4 38 ASP C 134  LEU C 138  SER C 139  ASP C 140                    
SITE     4 AD4 38 ARG C 141  GLU C 145  SER C 152  ASN C 155                    
SITE     5 AD4 38 CYS C 156  MET C 157  ILE C 158  SER C 165                    
SITE     6 AD4 38 VAL C 167  LEU C 169  PRO C 206  GLY C 207                    
SITE     7 AD4 38 LEU C 209  SER C 216  PHE C 217  GLY C 239                    
SITE     8 AD4 38 CYS C 240  ASP C 241  CYS C 243  GLN C 244                    
SITE     9 AD4 38 HOH C 642  HOH C 648  HOH C 657  HOH C 673                    
SITE    10 AD4 38 HOH C 678  HOH C 692                                          
SITE     1 AD5  7 PHE C  49  ASP C 134  GLN C 220  TYR C 238                    
SITE     2 AD5  7 TRP C 294  HOH C 653  HOH C 678                               
SITE     1 AD6  4 LYS C 112  HIS C 258  PRO C 259  GLU C 260                    
SITE     1 AD7  8 ALA D 153  LYS D 154  ASN D 155  CYS D 188                    
SITE     2 AD7  8 CYS D 191  CYS D 194  CYS D 247  LEU D 249                    
SITE     1 AD8  6 CYS D 198  LEU D 209  CYS D 214  ILE D 215                    
SITE     2 AD8  6 CYS D 240  CYS D 243                                          
SITE     1 AD9 36 SER D  32  LEU D  33  ARG D  36  SER D  47                    
SITE     2 AD9 36 GLU D  50  ARG D  57  CYS D  97  ASP D 134                    
SITE     3 AD9 36 LEU D 138  SER D 139  ASP D 140  ARG D 141                    
SITE     4 AD9 36 ALA D 142  SER D 152  ASN D 155  CYS D 156                    
SITE     5 AD9 36 ILE D 158  SER D 165  VAL D 167  LEU D 169                    
SITE     6 AD9 36 PRO D 206  GLY D 207  LEU D 209  SER D 216                    
SITE     7 AD9 36 GLY D 239  CYS D 240  ASP D 241  CYS D 243                    
SITE     8 AD9 36 GLN D 244  HOH D 614  HOH D 648  HOH D 655                    
SITE     9 AD9 36 HOH D 666  HOH D 678  HOH D 693  HOH D 744                    
SITE     1 AE1  7 PHE D  49  ASP D 134  GLN D 220  TYR D 238                    
SITE     2 AE1  7 TRP D 294  HOH D 628  HOH D 693                               
SITE     1 AE2  5 LYS D 112  HIS D 258  PRO D 259  GLU D 260                    
SITE     2 AE2  5 HOH D 659                                                     
CRYST1   90.587  111.118   96.008  90.00 104.90  90.00 P 1 21 1      8          
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      0.011039  0.000000  0.002936        0.00000                         
SCALE2      0.000000  0.008999  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010778        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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