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Database: PDB
Entry: 5ZCT
LinkDB: 5ZCT
Original site: 5ZCT 
HEADER    LIGASE                                  20-FEB-18   5ZCT              
TITLE     THE CRYSTAL STRUCTURE OF THE POLY-ALPHA-L-GLUTAMATE PEPTIDES          
TITLE    2 SYNTHETASE RIMK AT 2.05 ANGSTROM RESOLUTION.                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBOSOMAL PROTEIN S6--L-GLUTAMATE LIGASE;                  
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: POLYGLUTAMATE SYNTHASE,RIBOSOMAL PROTEIN S6 MODIFICATION    
COMPND   5 PROTEIN;                                                             
COMPND   6 EC: 6.3.2.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);                  
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: RIMK, B0852, JW0836;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    L-AMINO ACID LIGASE, LIGASE                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ARIMURA,T.KONO,K.KINO,H.KURUMIZAKA                                  
REVDAT   1   25-JUL-18 5ZCT    0                                                
JRNL        AUTH   Y.ARIMURA,T.KONO,K.KINO,H.KURUMIZAKA                         
JRNL        TITL   STRUCTURAL POLYMORPHISM OF THE ESCHERICHIA COLI              
JRNL        TITL 2 POLY-ALPHA-L-GLUTAMATE SYNTHETASE RIMK                       
JRNL        REF    ACTA CRYSTALLOGR F STRUCT     V.  74   385 2018              
JRNL        REF  2 BIOL COMMUN                                                  
JRNL        REFN                   ESSN 2053-230X                               
JRNL        PMID   29969101                                                     
JRNL        DOI    10.1107/S2053230X18007689                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.21                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 164146                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.140                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8436                            
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 48.2266 -  6.3652    1.00     5426   267  0.1519 0.1663        
REMARK   3     2  6.3652 -  5.0540    1.00     5360   260  0.1734 0.1975        
REMARK   3     3  5.0540 -  4.4157    1.00     5360   264  0.1461 0.1783        
REMARK   3     4  4.4157 -  4.0122    1.00     5281   314  0.1497 0.1768        
REMARK   3     5  4.0122 -  3.7247    1.00     5278   282  0.1713 0.1943        
REMARK   3     6  3.7247 -  3.5052    0.99     5239   286  0.1895 0.2503        
REMARK   3     7  3.5052 -  3.3297    1.00     5264   304  0.1905 0.2300        
REMARK   3     8  3.3297 -  3.1848    1.00     5253   317  0.2016 0.2516        
REMARK   3     9  3.1848 -  3.0622    1.00     5251   305  0.2065 0.2641        
REMARK   3    10  3.0622 -  2.9565    1.00     5295   287  0.2073 0.2735        
REMARK   3    11  2.9565 -  2.8641    1.00     5303   269  0.2152 0.2863        
REMARK   3    12  2.8641 -  2.7822    1.00     5223   265  0.2183 0.2544        
REMARK   3    13  2.7822 -  2.7090    1.00     5276   294  0.2026 0.2587        
REMARK   3    14  2.7090 -  2.6429    1.00     5299   284  0.1971 0.2455        
REMARK   3    15  2.6429 -  2.5828    1.00     5245   315  0.2043 0.2667        
REMARK   3    16  2.5828 -  2.5279    1.00     5296   273  0.2044 0.2521        
REMARK   3    17  2.5279 -  2.4773    1.00     5193   290  0.2050 0.2596        
REMARK   3    18  2.4773 -  2.4306    1.00     5259   260  0.2113 0.2762        
REMARK   3    19  2.4306 -  2.3871    1.00     5298   273  0.2153 0.2788        
REMARK   3    20  2.3871 -  2.3467    1.00     5231   275  0.2177 0.2890        
REMARK   3    21  2.3467 -  2.3088    0.99     5243   293  0.2221 0.2620        
REMARK   3    22  2.3088 -  2.2733    0.99     5248   281  0.2250 0.2846        
REMARK   3    23  2.2733 -  2.2399    0.77     4078   219  0.5102 0.5695        
REMARK   3    24  2.2399 -  2.2083    0.85     4399   276  0.3895 0.4874        
REMARK   3    25  2.2083 -  2.1785    1.00     5219   279  0.2415 0.2754        
REMARK   3    26  2.1785 -  2.1502    1.00     5253   270  0.2439 0.2972        
REMARK   3    27  2.1502 -  2.1233    0.99     5287   288  0.2452 0.2823        
REMARK   3    28  2.1233 -  2.0977    0.99     5195   292  0.2658 0.3106        
REMARK   3    29  2.0977 -  2.0733    0.99     5201   282  0.2835 0.3209        
REMARK   3    30  2.0733 -  2.0500    0.94     4957   272  0.2871 0.3305        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.730           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.65                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.38                          
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      :  0.008          18265                                  
REMARK   3   ANGLE     :  1.067          24750                                  
REMARK   3   CHIRALITY :  0.056           2892                                  
REMARK   3   PLANARITY :  0.006           3173                                  
REMARK   3   DIHEDRAL  : 10.776          11111                                  
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 5ZCT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300006861.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-MAY-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 164792                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
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     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55000                            
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 2.5.6                                          
REMARK 200 STARTING MODEL: 4IWX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BIS-TRIS PROPANE (PH 7.0), 210    
REMARK 280  MM NA2SO4, AND 16% PEG3350, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      106.30900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.81400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      106.30900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       60.81400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17380 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -258.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16840 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42960 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -261.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
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     GLU A   293                                                      
REMARK 465     TYR A   294                                                      
REMARK 465     CYS A   295                                                      
REMARK 465     LEU A   296                                                      
REMARK 465     LYS A   297                                                      
REMARK 465     THR A   298                                                      
REMARK 465     GLY A   299                                                      
REMARK 465     GLY A   300                                                      
REMARK 465     GLY A   301                                                      
REMARK 465     THR A   302                                                      
REMARK 465     LEU A   303                                                      
REMARK 465     VAL A   304                                                      
REMARK 465     PRO A   305                                                      
REMARK 465     ARG A   306                                                      
REMARK 465     GLU B   293                                                      
REMARK 465     TYR B   294                                                      
REMARK 465     CYS B   295                                                      
REMARK 465     LEU B   296                                                      
REMARK 465     LYS B   297                                                      
REMARK 465     THR B   298                                                      
REMARK 465     GLY B   299                                                      
REMARK 465     GLY B   300                                                      
REMARK 465     GLY B   301                                                      
REMARK 465     THR B   302                                                      
REMARK 465     LEU B   303                                                      
REMARK 465     VAL B   304                                                      
REMARK 465     PRO B   305                                                      
REMARK 465     ARG B   306                                                      
REMARK 465     THR C   291                                                      
REMARK 465     THR C   292                                                      
REMARK 465     GLU C   293                                                      
REMARK 465     TYR C   294                                                      
REMARK 465     CYS C   295                                                      
REMARK 465     LEU C   296                                                      
REMARK 465     LYS C   297                                                      
REMARK 465     THR C   298                                                      
REMARK 465     GLY C   299                                                      
REMARK 465     GLY C   300                                                      
REMARK 465     GLY C   301                                                      
REMARK 465     THR C   302                                                      
REMARK 465     LEU C   303                                                      
REMARK 465     VAL C   304                                                      
REMARK 465     PRO C   305                                                      
REMARK 465     ARG C   306                                                      
REMARK 465     GLU D   293                                                      
REMARK 465     TYR D   294                                                      
REMARK 465     CYS D   295                                                      
REMARK 465     LEU D   296                                                      
REMARK 465     LYS D   297                                                      
REMARK 465     THR D   298                                                      
REMARK 465     GLY D   299                                                      
REMARK 465     GLY D   300                                                      
REMARK 465     GLY D   301                                                      
REMARK 465     THR D   302                                                      
REMARK 465     LEU D   303                                                      
REMARK 465     VAL D   304                                                      
REMARK 465     PRO D   305                                                      
REMARK 465     ARG D   306                                                      
REMARK 465     GLU E   293                                                      
REMARK 465     TYR E   294                                                      
REMARK 465     CYS E   295                                                      
REMARK 465     LEU E   296                                                      
REMARK 465     LYS E   297                                                      
REMARK 465     THR E   298                                                      
REMARK 465     GLY E   299                                                      
REMARK 465     GLY E   300                                                      
REMARK 465     GLY E   301                                                      
REMARK 465     THR E   302                                                      
REMARK 465     LEU E   303                                                      
REMARK 465     VAL E   304                                                      
REMARK 465     PRO E   305                                                      
REMARK 465     ARG E   306                                                      
REMARK 465     GLU F   293                                                      
REMARK 465     TYR F   294                                                      
REMARK 465     CYS F   295                                                      
REMARK 465     LEU F   296                                                      
REMARK 465     LYS F   297                                                      
REMARK 465     THR F   298                                                      
REMARK 465     GLY F   299                                                      
REMARK 465     GLY F   300                                                      
REMARK 465     GLY F   301                                                      
REMARK 465     THR F   302                                                      
REMARK 465     LEU F   303                                                      
REMARK 465     VAL F   304                                                      
REMARK 465     PRO F   305                                                      
REMARK 465     ARG F   306                                                      
REMARK 465     GLU G   293                                                      
REMARK 465     TYR G   294                                                      
REMARK 465     CYS G   295                                                      
REMARK 465     LEU G   296                                                      
REMARK 465     LYS G   297                                                      
REMARK 465     THR G   298                                                      
REMARK 465     GLY G   299                                                      
REMARK 465     GLY G   300                                                      
REMARK 465     GLY G   301                                                      
REMARK 465     THR G   302                                                      
REMARK 465     LEU G   303                                                      
REMARK 465     VAL G   304                                                      
REMARK 465     PRO G   305                                                      
REMARK 465     ARG G   306                                                      
REMARK 465     GLU H   293                                                      
REMARK 465     TYR H   294                                                      
REMARK 465     CYS H   295                                                      
REMARK 465     LEU H   296                                                      
REMARK 465     LYS H   297                                                      
REMARK 465     THR H   298                                                      
REMARK 465     GLY H   299                                                      
REMARK 465     GLY H   300                                                      
REMARK 465     GLY H   301                                                      
REMARK 465     THR H   302                                                      
REMARK 465     LEU H   303                                                      
REMARK 465     VAL H   304                                                      
REMARK 465     PRO H   305                                                      
REMARK 465     ARG H   306                                                      
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   CG   ASN H   213     O3G  ANP H   401              1.77            
REMARK 500   NZ   LYS D   206     O    ARG D   211              2.01            
REMARK 500   OD1  ASN H   213     O3G  ANP H   401              2.08            
REMARK 500   ND2  ASN H   213     PG   ANP H   401              2.16            
REMARK 500   CA   GLY E   148     O1B  ANP E   402              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY A 148   C   -  N   -  CA  ANGL. DEV. = -13.8 DEGREES          
REMARK 500    LEU H 142   CA  -  CB  -  CG  ANGL. DEV. = -13.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A   9       52.80    -96.45                                   
REMARK 500    TYR A  50      109.29   -162.81                                   
REMARK 500    ASN A  89      115.39     99.58                                   
REMARK 500    HIS A 121      -63.68   -135.05                                   
REMARK 500    ALA B  44      120.57    -30.52                                   
REMARK 500    TYR B  50      116.40   -160.42                                   
REMARK 500    ASN B  89      116.62     94.12                                   
REMARK 500    HIS B 121      -66.83   -135.46                                   
REMARK 500    SER B 212       11.16    -66.00                                   
REMARK 500    ASN B 213      151.57    -48.44                                   
REMARK 500    ASP C   9       46.73    -96.13                                   
REMARK 500    ASN C  89      117.79     99.49                                   
REMARK 500    HIS C 121      -71.33   -126.76                                   
REMARK 500    SER C 122       73.89   -118.25                                   
REMARK 500    GLU C 144       35.11    -84.93                                   
REMARK 500    ARG C 216       31.06    -91.77                                   
REMARK 500    ASP D   9       47.97    -98.58                                   
REMARK 500    TYR D  50      114.57   -161.28                                   
REMARK 500    ASN D  89      122.05     90.35                                   
REMARK 500    HIS D 121      -68.23   -127.56                                   
REMARK 500    LYS D 206      175.03    -57.46                                   
REMARK 500    HIS D 215        9.10    -66.55                                   
REMARK 500    ASP E   9       53.25   -100.61                                   
REMARK 500    ASN E  89      113.57     95.10                                   
REMARK 500    HIS E 121      -67.54   -124.48                                   
REMARK 500    ASP F   9       59.08   -103.09                                   
REMARK 500    ASN F  89      114.56     92.55                                   
REMARK 500    HIS F 121      -68.33   -130.03                                   
REMARK 500    ASP G   9       50.34   -106.19                                   
REMARK 500    ASN G  89      114.92     94.74                                   
REMARK 500    HIS G 121      -64.22   -126.61                                   
REMARK 500    ASP H   9       57.90   -111.16                                   
REMARK 500    TYR H  50      117.40   -165.89                                   
REMARK 500    ASN H  89      115.18     94.13                                   
REMARK 500    HIS H 121      -65.90   -140.01                                   
REMARK 500    SER H 212       43.16   -152.99                                   
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 G 743        DISTANCE =  6.58 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                              MG B 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 260   OE2                                                    
REMARK 620 2 ANP B 401   O1G 119.0                                              
REMARK 620 3 ANP B 401   O1B  69.9  55.0                                        
REMARK 620 4 ANP B 401   O2A  68.3  60.9  56.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 260   OE1                                                    
REMARK 620 2 GLU D 260   OE2  51.0                                              
REMARK 620 3 ANP D 401   O3G  91.7  69.3                                        
REMARK 620 4 ANP D 401   O2B 158.0 129.3  71.3                                  
REMARK 620 5 ANP D 401   O2A 120.3  71.0  78.7  71.2                            
REMARK 620 6 HOH D 523   O    99.8  94.6 147.4 102.0  69.1                      
REMARK 620 7 HOH D 506   O    62.2 109.9  95.8 104.5 173.8 116.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F 260   OE2                                                    
REMARK 620 2 ANP F 401   O2G 136.7                                              
REMARK 620 3 ANP F 401   O2B  78.1  67.9                                        
REMARK 620 4 ANP F 401   O2A  95.7  96.6  69.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H 248   OD2                                                    
REMARK 620 2 GLU H 260   OE2  94.0                                              
REMARK 620 3 ANP H 401   O2G 147.3  66.8                                        
REMARK 620 4 ANP H 401   O1A 143.9  75.4  59.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP A 401   O1G                                                    
REMARK 620 2 ANP A 401   O1B  84.6                                              
REMARK 620 3 ANP A 401   O1A  96.2  79.5                                        
REMARK 620 4 HOH A 520   O    91.7 170.2  91.9                                  
REMARK 620 5 HOH A 508   O   174.0  90.7  79.3  92.3                            
REMARK 620 6 HOH A 586   O    86.9  91.1 169.8  97.8  96.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP C 401   O3G                                                    
REMARK 620 2 ANP C 401   O2B  78.6                                              
REMARK 620 3 ANP C 401   O1A  76.0  81.3                                        
REMARK 620 4 HOH C 513   O   167.9  96.3  92.4                                  
REMARK 620 5 HOH C 623   O    87.6  93.5 163.5 103.8                            
REMARK 620 6 HOH C 514   O    82.4 160.8  91.4 101.8  88.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 403  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP E 402   O3G                                                    
REMARK 620 2 ANP E 402   O2B  79.3                                              
REMARK 620 3 ANP E 402   O1A  91.3  88.5                                        
REMARK 620 4 HOH E 559   O    83.6  89.1 174.7                                  
REMARK 620 5 HOH E 502   O    93.6 166.3 103.4  78.4                            
REMARK 620 6 HOH E 564   O   168.0  93.9  98.5  86.4  90.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP G 401   O1G                                                    
REMARK 620 2 ANP G 401   O1B  89.6                                              
REMARK 620 3 ANP G 401   O2A  97.7  85.4                                        
REMARK 620 4 HOH G 505   O    97.9 169.8  86.7                                  
REMARK 620 5 HOH G 576   O   178.7  90.0  83.5  82.7                            
REMARK 620 6 HOH G 532   O    95.5  86.2 164.3  99.9  83.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP F 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG F 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP G 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG G 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ANP B 401 and ASN B    
REMARK 800  213                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide SO4 B 403 and ARG B    
REMARK 800  102                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide SO4 E 401 and ARG E    
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ANP E 402 and GLY E    
REMARK 800  148                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide SO4 G 403 and ARG G    
REMARK 800  203                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ANP H 401 and ASN H    
REMARK 800  213                                                                 
DBREF  5ZCT A    1   292  UNP    P0C0U4   RIMK_ECOLI       1    292             
DBREF  5ZCT B    1   292  UNP    P0C0U4   RIMK_ECOLI       1    292             
DBREF  5ZCT C    1   292  UNP    P0C0U4   RIMK_ECOLI       1    292             
DBREF  5ZCT D    1   292  UNP    P0C0U4   RIMK_ECOLI       1    292             
DBREF  5ZCT E    1   292  UNP    P0C0U4   RIMK_ECOLI       1    292             
DBREF  5ZCT F    1   292  UNP    P0C0U4   RIMK_ECOLI       1    292             
DBREF  5ZCT G    1   292  UNP    P0C0U4   RIMK_ECOLI       1    292             
DBREF  5ZCT H    1   292  UNP    P0C0U4   RIMK_ECOLI       1    292             
SEQADV 5ZCT GLU A  293  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT TYR A  294  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT CYS A  295  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LEU A  296  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LYS A  297  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT THR A  298  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY A  299  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY A  300  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY A  301  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT THR A  302  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LEU A  303  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT VAL A  304  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT PRO A  305  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT ARG A  306  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLU B  293  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT TYR B  294  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT CYS B  295  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LEU B  296  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LYS B  297  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT THR B  298  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY B  299  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY B  300  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY B  301  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT THR B  302  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LEU B  303  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT VAL B  304  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT PRO B  305  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT ARG B  306  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLU C  293  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT TYR C  294  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT CYS C  295  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LEU C  296  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LYS C  297  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT THR C  298  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY C  299  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY C  300  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY C  301  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT THR C  302  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LEU C  303  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT VAL C  304  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT PRO C  305  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT ARG C  306  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLU D  293  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT TYR D  294  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT CYS D  295  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LEU D  296  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LYS D  297  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT THR D  298  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY D  299  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY D  300  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY D  301  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT THR D  302  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LEU D  303  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT VAL D  304  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT PRO D  305  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT ARG D  306  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLU E  293  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT TYR E  294  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT CYS E  295  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LEU E  296  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LYS E  297  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT THR E  298  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY E  299  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY E  300  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY E  301  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT THR E  302  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LEU E  303  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT VAL E  304  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT PRO E  305  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT ARG E  306  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLU F  293  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT TYR F  294  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT CYS F  295  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LEU F  296  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LYS F  297  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT THR F  298  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY F  299  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY F  300  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY F  301  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT THR F  302  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LEU F  303  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT VAL F  304  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT PRO F  305  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT ARG F  306  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLU G  293  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT TYR G  294  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT CYS G  295  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LEU G  296  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LYS G  297  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT THR G  298  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY G  299  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY G  300  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY G  301  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT THR G  302  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LEU G  303  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT VAL G  304  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT PRO G  305  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT ARG G  306  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLU H  293  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT TYR H  294  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT CYS H  295  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LEU H  296  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LYS H  297  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT THR H  298  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY H  299  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY H  300  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT GLY H  301  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT THR H  302  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT LEU H  303  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT VAL H  304  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT PRO H  305  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 5ZCT ARG H  306  UNP  P0C0U4              EXPRESSION TAG                 
SEQRES   1 A  306  MET LYS ILE ALA ILE LEU SER ARG ASP GLY THR LEU TYR          
SEQRES   2 A  306  SER CYS LYS ARG LEU ARG GLU ALA ALA ILE GLN ARG GLY          
SEQRES   3 A  306  HIS LEU VAL GLU ILE LEU ASP PRO LEU SER CYS TYR MET          
SEQRES   4 A  306  ASN ILE ASN PRO ALA ALA SER SER ILE HIS TYR LYS GLY          
SEQRES   5 A  306  ARG LYS LEU PRO HIS PHE ASP ALA VAL ILE PRO ARG ILE          
SEQRES   6 A  306  GLY THR ALA ILE THR PHE TYR GLY THR ALA ALA LEU ARG          
SEQRES   7 A  306  GLN PHE GLU MET LEU GLY SER TYR PRO LEU ASN GLU SER          
SEQRES   8 A  306  VAL ALA ILE ALA ARG ALA ARG ASP LYS LEU ARG SER MET          
SEQRES   9 A  306  GLN LEU LEU ALA ARG GLN GLY ILE ASP LEU PRO VAL THR          
SEQRES  10 A  306  GLY ILE ALA HIS SER PRO ASP ASP THR SER ASP LEU ILE          
SEQRES  11 A  306  ASP MET VAL GLY GLY ALA PRO LEU VAL VAL LYS LEU VAL          
SEQRES  12 A  306  GLU GLY THR GLN GLY ILE GLY VAL VAL LEU ALA GLU THR          
SEQRES  13 A  306  ARG GLN ALA ALA GLU SER VAL ILE ASP ALA PHE ARG GLY          
SEQRES  14 A  306  LEU ASN ALA HIS ILE LEU VAL GLN GLU TYR ILE LYS GLU          
SEQRES  15 A  306  ALA GLN GLY CYS ASP ILE ARG CYS LEU VAL VAL GLY ASP          
SEQRES  16 A  306  GLU VAL VAL ALA ALA ILE GLU ARG ARG ALA LYS GLU GLY          
SEQRES  17 A  306  ASP PHE ARG SER ASN LEU HIS ARG GLY GLY ALA ALA SER          
SEQRES  18 A  306  VAL ALA SER ILE THR PRO GLN GLU ARG GLU ILE ALA ILE          
SEQRES  19 A  306  LYS ALA ALA ARG THR MET ALA LEU ASP VAL ALA GLY VAL          
SEQRES  20 A  306  ASP ILE LEU ARG ALA ASN ARG GLY PRO LEU VAL MET GLU          
SEQRES  21 A  306  VAL ASN ALA SER PRO GLY LEU GLU GLY ILE GLU LYS THR          
SEQRES  22 A  306  THR GLY ILE ASP ILE ALA GLY LYS MET ILE ARG TRP ILE          
SEQRES  23 A  306  GLU ARG HIS ALA THR THR GLU TYR CYS LEU LYS THR GLY          
SEQRES  24 A  306  GLY GLY THR LEU VAL PRO ARG                                  
SEQRES   1 B  306  MET LYS ILE ALA ILE LEU SER ARG ASP GLY THR LEU TYR          
SEQRES   2 B  306  SER CYS LYS ARG LEU ARG GLU ALA ALA ILE GLN ARG GLY          
SEQRES   3 B  306  HIS LEU VAL GLU ILE LEU ASP PRO LEU SER CYS TYR MET          
SEQRES   4 B  306  ASN ILE ASN PRO ALA ALA SER SER ILE HIS TYR LYS GLY          
SEQRES   5 B  306  ARG LYS LEU PRO HIS PHE ASP ALA VAL ILE PRO ARG ILE          
SEQRES   6 B  306  GLY THR ALA ILE THR PHE TYR GLY THR ALA ALA LEU ARG          
SEQRES   7 B  306  GLN PHE GLU MET LEU GLY SER TYR PRO LEU ASN GLU SER          
SEQRES   8 B  306  VAL ALA ILE ALA ARG ALA ARG ASP LYS LEU ARG SER MET          
SEQRES   9 B  306  GLN LEU LEU ALA ARG GLN GLY ILE ASP LEU PRO VAL THR          
SEQRES  10 B  306  GLY ILE ALA HIS SER PRO ASP ASP THR SER ASP LEU ILE          
SEQRES  11 B  306  ASP MET VAL GLY GLY ALA PRO LEU VAL VAL LYS LEU VAL          
SEQRES  12 B  306  GLU GLY THR GLN GLY ILE GLY VAL VAL LEU ALA GLU THR          
SEQRES  13 B  306  ARG GLN ALA ALA GLU SER VAL ILE ASP ALA PHE ARG GLY          
SEQRES  14 B  306  LEU ASN ALA HIS ILE LEU VAL GLN GLU TYR ILE LYS GLU          
SEQRES  15 B  306  ALA GLN GLY CYS ASP ILE ARG CYS LEU VAL VAL GLY ASP          
SEQRES  16 B  306  GLU VAL VAL ALA ALA ILE GLU ARG ARG ALA LYS GLU GLY          
SEQRES  17 B  306  ASP PHE ARG SER ASN LEU HIS ARG GLY GLY ALA ALA SER          
SEQRES  18 B  306  VAL ALA SER ILE THR PRO GLN GLU ARG GLU ILE ALA ILE          
SEQRES  19 B  306  LYS ALA ALA ARG THR MET ALA LEU ASP VAL ALA GLY VAL          
SEQRES  20 B  306  ASP ILE LEU ARG ALA ASN ARG GLY PRO LEU VAL MET GLU          
SEQRES  21 B  306  VAL ASN ALA SER PRO GLY LEU GLU GLY ILE GLU LYS THR          
SEQRES  22 B  306  THR GLY ILE ASP ILE ALA GLY LYS MET ILE ARG TRP ILE          
SEQRES  23 B  306  GLU ARG HIS ALA THR THR GLU TYR CYS LEU LYS THR GLY          
SEQRES  24 B  306  GLY GLY THR LEU VAL PRO ARG                                  
SEQRES   1 C  306  MET LYS ILE ALA ILE LEU SER ARG ASP GLY THR LEU TYR          
SEQRES   2 C  306  SER CYS LYS ARG LEU ARG GLU ALA ALA ILE GLN ARG GLY          
SEQRES   3 C  306  HIS LEU VAL GLU ILE LEU ASP PRO LEU SER CYS TYR MET          
SEQRES   4 C  306  ASN ILE ASN PRO ALA ALA SER SER ILE HIS TYR LYS GLY          
SEQRES   5 C  306  ARG LYS LEU PRO HIS PHE ASP ALA VAL ILE PRO ARG ILE          
SEQRES   6 C  306  GLY THR ALA ILE THR PHE TYR GLY THR ALA ALA LEU ARG          
SEQRES   7 C  306  GLN PHE GLU MET LEU GLY SER TYR PRO LEU ASN GLU SER          
SEQRES   8 C  306  VAL ALA ILE ALA ARG ALA ARG ASP LYS LEU ARG SER MET          
SEQRES   9 C  306  GLN LEU LEU ALA ARG GLN GLY ILE ASP LEU PRO VAL THR          
SEQRES  10 C  306  GLY ILE ALA HIS SER PRO ASP ASP THR SER ASP LEU ILE          
SEQRES  11 C  306  ASP MET VAL GLY GLY ALA PRO LEU VAL VAL LYS LEU VAL          
SEQRES  12 C  306  GLU GLY THR GLN GLY ILE GLY VAL VAL LEU ALA GLU THR          
SEQRES  13 C  306  ARG GLN ALA ALA GLU SER VAL ILE ASP ALA PHE ARG GLY          
SEQRES  14 C  306  LEU ASN ALA HIS ILE LEU VAL GLN GLU TYR ILE LYS GLU          
SEQRES  15 C  306  ALA GLN GLY CYS ASP ILE ARG CYS LEU VAL VAL GLY ASP          
SEQRES  16 C  306  GLU VAL VAL ALA ALA ILE GLU ARG ARG ALA LYS GLU GLY          
SEQRES  17 C  306  ASP PHE ARG SER ASN LEU HIS ARG GLY GLY ALA ALA SER          
SEQRES  18 C  306  VAL ALA SER ILE THR PRO GLN GLU ARG GLU ILE ALA ILE          
SEQRES  19 C  306  LYS ALA ALA ARG THR MET ALA LEU ASP VAL ALA GLY VAL          
SEQRES  20 C  306  ASP ILE LEU ARG ALA ASN ARG GLY PRO LEU VAL MET GLU          
SEQRES  21 C  306  VAL ASN ALA SER PRO GLY LEU GLU GLY ILE GLU LYS THR          
SEQRES  22 C  306  THR GLY ILE ASP ILE ALA GLY LYS MET ILE ARG TRP ILE          
SEQRES  23 C  306  GLU ARG HIS ALA THR THR GLU TYR CYS LEU LYS THR GLY          
SEQRES  24 C  306  GLY GLY THR LEU VAL PRO ARG                                  
SEQRES   1 D  306  MET LYS ILE ALA ILE LEU SER ARG ASP GLY THR LEU TYR          
SEQRES   2 D  306  SER CYS LYS ARG LEU ARG GLU ALA ALA ILE GLN ARG GLY          
SEQRES   3 D  306  HIS LEU VAL GLU ILE LEU ASP PRO LEU SER CYS TYR MET          
SEQRES   4 D  306  ASN ILE ASN PRO ALA ALA SER SER ILE HIS TYR LYS GLY          
SEQRES   5 D  306  ARG LYS LEU PRO HIS PHE ASP ALA VAL ILE PRO ARG ILE          
SEQRES   6 D  306  GLY THR ALA ILE THR PHE TYR GLY THR ALA ALA LEU ARG          
SEQRES   7 D  306  GLN PHE GLU MET LEU GLY SER TYR PRO LEU ASN GLU SER          
SEQRES   8 D  306  VAL ALA ILE ALA ARG ALA ARG ASP LYS LEU ARG SER MET          
SEQRES   9 D  306  GLN LEU LEU ALA ARG GLN GLY ILE ASP LEU PRO VAL THR          
SEQRES  10 D  306  GLY ILE ALA HIS SER PRO ASP ASP THR SER ASP LEU ILE          
SEQRES  11 D  306  ASP MET VAL GLY GLY ALA PRO LEU VAL VAL LYS LEU VAL          
SEQRES  12 D  306  GLU GLY THR GLN GLY ILE GLY VAL VAL LEU ALA GLU THR          
SEQRES  13 D  306  ARG GLN ALA ALA GLU SER VAL ILE ASP ALA PHE ARG GLY          
SEQRES  14 D  306  LEU ASN ALA HIS ILE LEU VAL GLN GLU TYR ILE LYS GLU          
SEQRES  15 D  306  ALA GLN GLY CYS ASP ILE ARG CYS LEU VAL VAL GLY ASP          
SEQRES  16 D  306  GLU VAL VAL ALA ALA ILE GLU ARG ARG ALA LYS GLU GLY          
SEQRES  17 D  306  ASP PHE ARG SER ASN LEU HIS ARG GLY GLY ALA ALA SER          
SEQRES  18 D  306  VAL ALA SER ILE THR PRO GLN GLU ARG GLU ILE ALA ILE          
SEQRES  19 D  306  LYS ALA ALA ARG THR MET ALA LEU ASP VAL ALA GLY VAL          
SEQRES  20 D  306  ASP ILE LEU ARG ALA ASN ARG GLY PRO LEU VAL MET GLU          
SEQRES  21 D  306  VAL ASN ALA SER PRO GLY LEU GLU GLY ILE GLU LYS THR          
SEQRES  22 D  306  THR GLY ILE ASP ILE ALA GLY LYS MET ILE ARG TRP ILE          
SEQRES  23 D  306  GLU ARG HIS ALA THR THR GLU TYR CYS LEU LYS THR GLY          
SEQRES  24 D  306  GLY GLY THR LEU VAL PRO ARG                                  
SEQRES   1 E  306  MET LYS ILE ALA ILE LEU SER ARG ASP GLY THR LEU TYR          
SEQRES   2 E  306  SER CYS LYS ARG LEU ARG GLU ALA ALA ILE GLN ARG GLY          
SEQRES   3 E  306  HIS LEU VAL GLU ILE LEU ASP PRO LEU SER CYS TYR MET          
SEQRES   4 E  306  ASN ILE ASN PRO ALA ALA SER SER ILE HIS TYR LYS GLY          
SEQRES   5 E  306  ARG LYS LEU PRO HIS PHE ASP ALA VAL ILE PRO ARG ILE          
SEQRES   6 E  306  GLY THR ALA ILE THR PHE TYR GLY THR ALA ALA LEU ARG          
SEQRES   7 E  306  GLN PHE GLU MET LEU GLY SER TYR PRO LEU ASN GLU SER          
SEQRES   8 E  306  VAL ALA ILE ALA ARG ALA ARG ASP LYS LEU ARG SER MET          
SEQRES   9 E  306  GLN LEU LEU ALA ARG GLN GLY ILE ASP LEU PRO VAL THR          
SEQRES  10 E  306  GLY ILE ALA HIS SER PRO ASP ASP THR SER ASP LEU ILE          
SEQRES  11 E  306  ASP MET VAL GLY GLY ALA PRO LEU VAL VAL LYS LEU VAL          
SEQRES  12 E  306  GLU GLY THR GLN GLY ILE GLY VAL VAL LEU ALA GLU THR          
SEQRES  13 E  306  ARG GLN ALA ALA GLU SER VAL ILE ASP ALA PHE ARG GLY          
SEQRES  14 E  306  LEU ASN ALA HIS ILE LEU VAL GLN GLU TYR ILE LYS GLU          
SEQRES  15 E  306  ALA GLN GLY CYS ASP ILE ARG CYS LEU VAL VAL GLY ASP          
SEQRES  16 E  306  GLU VAL VAL ALA ALA ILE GLU ARG ARG ALA LYS GLU GLY          
SEQRES  17 E  306  ASP PHE ARG SER ASN LEU HIS ARG GLY GLY ALA ALA SER          
SEQRES  18 E  306  VAL ALA SER ILE THR PRO GLN GLU ARG GLU ILE ALA ILE          
SEQRES  19 E  306  LYS ALA ALA ARG THR MET ALA LEU ASP VAL ALA GLY VAL          
SEQRES  20 E  306  ASP ILE LEU ARG ALA ASN ARG GLY PRO LEU VAL MET GLU          
SEQRES  21 E  306  VAL ASN ALA SER PRO GLY LEU GLU GLY ILE GLU LYS THR          
SEQRES  22 E  306  THR GLY ILE ASP ILE ALA GLY LYS MET ILE ARG TRP ILE          
SEQRES  23 E  306  GLU ARG HIS ALA THR THR GLU TYR CYS LEU LYS THR GLY          
SEQRES  24 E  306  GLY GLY THR LEU VAL PRO ARG                                  
SEQRES   1 F  306  MET LYS ILE ALA ILE LEU SER ARG ASP GLY THR LEU TYR          
SEQRES   2 F  306  SER CYS LYS ARG LEU ARG GLU ALA ALA ILE GLN ARG GLY          
SEQRES   3 F  306  HIS LEU VAL GLU ILE LEU ASP PRO LEU SER CYS TYR MET          
SEQRES   4 F  306  ASN ILE ASN PRO ALA ALA SER SER ILE HIS TYR LYS GLY          
SEQRES   5 F  306  ARG LYS LEU PRO HIS PHE ASP ALA VAL ILE PRO ARG ILE          
SEQRES   6 F  306  GLY THR ALA ILE THR PHE TYR GLY THR ALA ALA LEU ARG          
SEQRES   7 F  306  GLN PHE GLU MET LEU GLY SER TYR PRO LEU ASN GLU SER          
SEQRES   8 F  306  VAL ALA ILE ALA ARG ALA ARG ASP LYS LEU ARG SER MET          
SEQRES   9 F  306  GLN LEU LEU ALA ARG GLN GLY ILE ASP LEU PRO VAL THR          
SEQRES  10 F  306  GLY ILE ALA HIS SER PRO ASP ASP THR SER ASP LEU ILE          
SEQRES  11 F  306  ASP MET VAL GLY GLY ALA PRO LEU VAL VAL LYS LEU VAL          
SEQRES  12 F  306  GLU GLY THR GLN GLY ILE GLY VAL VAL LEU ALA GLU THR          
SEQRES  13 F  306  ARG GLN ALA ALA GLU SER VAL ILE ASP ALA PHE ARG GLY          
SEQRES  14 F  306  LEU ASN ALA HIS ILE LEU VAL GLN GLU TYR ILE LYS GLU          
SEQRES  15 F  306  ALA GLN GLY CYS ASP ILE ARG CYS LEU VAL VAL GLY ASP          
SEQRES  16 F  306  GLU VAL VAL ALA ALA ILE GLU ARG ARG ALA LYS GLU GLY          
SEQRES  17 F  306  ASP PHE ARG SER ASN LEU HIS ARG GLY GLY ALA ALA SER          
SEQRES  18 F  306  VAL ALA SER ILE THR PRO GLN GLU ARG GLU ILE ALA ILE          
SEQRES  19 F  306  LYS ALA ALA ARG THR MET ALA LEU ASP VAL ALA GLY VAL          
SEQRES  20 F  306  ASP ILE LEU ARG ALA ASN ARG GLY PRO LEU VAL MET GLU          
SEQRES  21 F  306  VAL ASN ALA SER PRO GLY LEU GLU GLY ILE GLU LYS THR          
SEQRES  22 F  306  THR GLY ILE ASP ILE ALA GLY LYS MET ILE ARG TRP ILE          
SEQRES  23 F  306  GLU ARG HIS ALA THR THR GLU TYR CYS LEU LYS THR GLY          
SEQRES  24 F  306  GLY GLY THR LEU VAL PRO ARG                                  
SEQRES   1 G  306  MET LYS ILE ALA ILE LEU SER ARG ASP GLY THR LEU TYR          
SEQRES   2 G  306  SER CYS LYS ARG LEU ARG GLU ALA ALA ILE GLN ARG GLY          
SEQRES   3 G  306  HIS LEU VAL GLU ILE LEU ASP PRO LEU SER CYS TYR MET          
SEQRES   4 G  306  ASN ILE ASN PRO ALA ALA SER SER ILE HIS TYR LYS GLY          
SEQRES   5 G  306  ARG LYS LEU PRO HIS PHE ASP ALA VAL ILE PRO ARG ILE          
SEQRES   6 G  306  GLY THR ALA ILE THR PHE TYR GLY THR ALA ALA LEU ARG          
SEQRES   7 G  306  GLN PHE GLU MET LEU GLY SER TYR PRO LEU ASN GLU SER          
SEQRES   8 G  306  VAL ALA ILE ALA ARG ALA ARG ASP LYS LEU ARG SER MET          
SEQRES   9 G  306  GLN LEU LEU ALA ARG GLN GLY ILE ASP LEU PRO VAL THR          
SEQRES  10 G  306  GLY ILE ALA HIS SER PRO ASP ASP THR SER ASP LEU ILE          
SEQRES  11 G  306  ASP MET VAL GLY GLY ALA PRO LEU VAL VAL LYS LEU VAL          
SEQRES  12 G  306  GLU GLY THR GLN GLY ILE GLY VAL VAL LEU ALA GLU THR          
SEQRES  13 G  306  ARG GLN ALA ALA GLU SER VAL ILE ASP ALA PHE ARG GLY          
SEQRES  14 G  306  LEU ASN ALA HIS ILE LEU VAL GLN GLU TYR ILE LYS GLU          
SEQRES  15 G  306  ALA GLN GLY CYS ASP ILE ARG CYS LEU VAL VAL GLY ASP          
SEQRES  16 G  306  GLU VAL VAL ALA ALA ILE GLU ARG ARG ALA LYS GLU GLY          
SEQRES  17 G  306  ASP PHE ARG SER ASN LEU HIS ARG GLY GLY ALA ALA SER          
SEQRES  18 G  306  VAL ALA SER ILE THR PRO GLN GLU ARG GLU ILE ALA ILE          
SEQRES  19 G  306  LYS ALA ALA ARG THR MET ALA LEU ASP VAL ALA GLY VAL          
SEQRES  20 G  306  ASP ILE LEU ARG ALA ASN ARG GLY PRO LEU VAL MET GLU          
SEQRES  21 G  306  VAL ASN ALA SER PRO GLY LEU GLU GLY ILE GLU LYS THR          
SEQRES  22 G  306  THR GLY ILE ASP ILE ALA GLY LYS MET ILE ARG TRP ILE          
SEQRES  23 G  306  GLU ARG HIS ALA THR THR GLU TYR CYS LEU LYS THR GLY          
SEQRES  24 G  306  GLY GLY THR LEU VAL PRO ARG                                  
SEQRES   1 H  306  MET LYS ILE ALA ILE LEU SER ARG ASP GLY THR LEU TYR          
SEQRES   2 H  306  SER CYS LYS ARG LEU ARG GLU ALA ALA ILE GLN ARG GLY          
SEQRES   3 H  306  HIS LEU VAL GLU ILE LEU ASP PRO LEU SER CYS TYR MET          
SEQRES   4 H  306  ASN ILE ASN PRO ALA ALA SER SER ILE HIS TYR LYS GLY          
SEQRES   5 H  306  ARG LYS LEU PRO HIS PHE ASP ALA VAL ILE PRO ARG ILE          
SEQRES   6 H  306  GLY THR ALA ILE THR PHE TYR GLY THR ALA ALA LEU ARG          
SEQRES   7 H  306  GLN PHE GLU MET LEU GLY SER TYR PRO LEU ASN GLU SER          
SEQRES   8 H  306  VAL ALA ILE ALA ARG ALA ARG ASP LYS LEU ARG SER MET          
SEQRES   9 H  306  GLN LEU LEU ALA ARG GLN GLY ILE ASP LEU PRO VAL THR          
SEQRES  10 H  306  GLY ILE ALA HIS SER PRO ASP ASP THR SER ASP LEU ILE          
SEQRES  11 H  306  ASP MET VAL GLY GLY ALA PRO LEU VAL VAL LYS LEU VAL          
SEQRES  12 H  306  GLU GLY THR GLN GLY ILE GLY VAL VAL LEU ALA GLU THR          
SEQRES  13 H  306  ARG GLN ALA ALA GLU SER VAL ILE ASP ALA PHE ARG GLY          
SEQRES  14 H  306  LEU ASN ALA HIS ILE LEU VAL GLN GLU TYR ILE LYS GLU          
SEQRES  15 H  306  ALA GLN GLY CYS ASP ILE ARG CYS LEU VAL VAL GLY ASP          
SEQRES  16 H  306  GLU VAL VAL ALA ALA ILE GLU ARG ARG ALA LYS GLU GLY          
SEQRES  17 H  306  ASP PHE ARG SER ASN LEU HIS ARG GLY GLY ALA ALA SER          
SEQRES  18 H  306  VAL ALA SER ILE THR PRO GLN GLU ARG GLU ILE ALA ILE          
SEQRES  19 H  306  LYS ALA ALA ARG THR MET ALA LEU ASP VAL ALA GLY VAL          
SEQRES  20 H  306  ASP ILE LEU ARG ALA ASN ARG GLY PRO LEU VAL MET GLU          
SEQRES  21 H  306  VAL ASN ALA SER PRO GLY LEU GLU GLY ILE GLU LYS THR          
SEQRES  22 H  306  THR GLY ILE ASP ILE ALA GLY LYS MET ILE ARG TRP ILE          
SEQRES  23 H  306  GLU ARG HIS ALA THR THR GLU TYR CYS LEU LYS THR GLY          
SEQRES  24 H  306  GLY GLY THR LEU VAL PRO ARG                                  
HET    ANP  A 401      31                                                       
HET     MG  A 402       1                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    SO4  A 405       5                                                       
HET    ANP  B 401      31                                                       
HET     MG  B 402       1                                                       
HET    SO4  B 403       5                                                       
HET    ANP  C 401      31                                                       
HET     MG  C 402       1                                                       
HET    SO4  C 403       5                                                       
HET    SO4  C 404       5                                                       
HET    SO4  C 405       5                                                       
HET    ANP  D 401      31                                                       
HET     MG  D 402       1                                                       
HET    SO4  D 403       5                                                       
HET    SO4  E 401       5                                                       
HET    ANP  E 402      31                                                       
HET     MG  E 403       1                                                       
HET    SO4  E 404       5                                                       
HET    ANP  F 401      31                                                       
HET     MG  F 402       1                                                       
HET    SO4  F 403       5                                                       
HET    ANP  G 401      31                                                       
HET     MG  G 402       1                                                       
HET    SO4  G 403       5                                                       
HET    SO4  G 404       5                                                       
HET    ANP  H 401      31                                                       
HET     MG  H 402       1                                                       
HET    SO4  H 403       5                                                       
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SO4 SULFATE ION                                                      
FORMUL   9  ANP    8(C10 H17 N6 O12 P3)                                         
FORMUL  10   MG    8(MG 2+)                                                     
FORMUL  11  SO4    14(O4 S 2-)                                                  
FORMUL  39  HOH   *1186(H2 O)                                                   
HELIX    1 AA1 LEU A   12  ARG A   25  1                                  14    
HELIX    2 AA2 ASP A   33  LEU A   35  5                                   3    
HELIX    3 AA3 GLY A   66  ALA A   68  5                                   3    
HELIX    4 AA4 ILE A   69  LEU A   83  1                                  15    
HELIX    5 AA5 GLU A   90  ASP A   99  1                                  10    
HELIX    6 AA6 ASP A   99  GLN A  110  1                                  12    
HELIX    7 AA7 ASP A  125  GLY A  134  1                                  10    
HELIX    8 AA8 THR A  156  GLY A  169  1                                  14    
HELIX    9 AA9 ILE A  180  GLN A  184  5                                   5    
HELIX   10 AB1 ASN A  213  GLY A  217  5                                   5    
HELIX   11 AB2 THR A  226  MET A  240  1                                  15    
HELIX   12 AB3 LEU A  267  GLY A  275  1                                   9    
HELIX   13 AB4 ASP A  277  ALA A  290  1                                  14    
HELIX   14 AB5 LEU B   12  ARG B   25  1                                  14    
HELIX   15 AB6 ASP B   33  LEU B   35  5                                   3    
HELIX   16 AB7 GLY B   66  ALA B   68  5                                   3    
HELIX   17 AB8 ILE B   69  LEU B   83  1                                  15    
HELIX   18 AB9 GLU B   90  ASP B   99  1                                  10    
HELIX   19 AC1 ASP B   99  GLN B  110  1                                  12    
HELIX   20 AC2 ASP B  125  VAL B  133  1                                   9    
HELIX   21 AC3 THR B  156  ARG B  168  1                                  13    
HELIX   22 AC4 THR B  226  MET B  240  1                                  15    
HELIX   23 AC5 LEU B  267  GLY B  275  1                                   9    
HELIX   24 AC6 ASP B  277  ALA B  290  1                                  14    
HELIX   25 AC7 LEU C   12  ARG C   25  1                                  14    
HELIX   26 AC8 ASP C   33  LEU C   35  5                                   3    
HELIX   27 AC9 GLY C   66  ALA C   68  5                                   3    
HELIX   28 AD1 ILE C   69  LEU C   83  1                                  15    
HELIX   29 AD2 GLU C   90  ASP C   99  1                                  10    
HELIX   30 AD3 ASP C   99  GLN C  110  1                                  12    
HELIX   31 AD4 ASP C  125  GLY C  134  1                                  10    
HELIX   32 AD5 THR C  156  GLY C  169  1                                  14    
HELIX   33 AD6 ILE C  180  GLN C  184  5                                   5    
HELIX   34 AD7 ASN C  213  GLY C  217  5                                   5    
HELIX   35 AD8 THR C  226  MET C  240  1                                  15    
HELIX   36 AD9 LEU C  267  GLY C  275  1                                   9    
HELIX   37 AE1 ASP C  277  ALA C  290  1                                  14    
HELIX   38 AE2 LEU D   12  ARG D   25  1                                  14    
HELIX   39 AE3 ASP D   33  LEU D   35  5                                   3    
HELIX   40 AE4 GLY D   66  ALA D   68  5                                   3    
HELIX   41 AE5 ILE D   69  LEU D   83  1                                  15    
HELIX   42 AE6 GLU D   90  ASP D   99  1                                  10    
HELIX   43 AE7 ASP D   99  GLN D  110  1                                  12    
HELIX   44 AE8 ASP D  125  VAL D  133  1                                   9    
HELIX   45 AE9 THR D  156  ARG D  168  1                                  13    
HELIX   46 AF1 ILE D  180  GLN D  184  5                                   5    
HELIX   47 AF2 ASN D  213  GLY D  217  5                                   5    
HELIX   48 AF3 THR D  226  MET D  240  1                                  15    
HELIX   49 AF4 LEU D  267  GLY D  275  1                                   9    
HELIX   50 AF5 ASP D  277  ALA D  290  1                                  14    
HELIX   51 AF6 LEU E   12  ARG E   25  1                                  14    
HELIX   52 AF7 ASP E   33  LEU E   35  5                                   3    
HELIX   53 AF8 GLY E   66  ALA E   68  5                                   3    
HELIX   54 AF9 ILE E   69  LEU E   83  1                                  15    
HELIX   55 AG1 GLU E   90  ASP E   99  1                                  10    
HELIX   56 AG2 ASP E   99  GLN E  110  1                                  12    
HELIX   57 AG3 ASP E  125  VAL E  133  1                                   9    
HELIX   58 AG4 THR E  156  GLY E  169  1                                  14    
HELIX   59 AG5 ILE E  180  GLN E  184  5                                   5    
HELIX   60 AG6 ASN E  213  GLY E  217  5                                   5    
HELIX   61 AG7 THR E  226  MET E  240  1                                  15    
HELIX   62 AG8 LEU E  267  GLY E  275  1                                   9    
HELIX   63 AG9 ASP E  277  ALA E  290  1                                  14    
HELIX   64 AH1 LEU F   12  ARG F   25  1                                  14    
HELIX   65 AH2 ASP F   33  LEU F   35  5                                   3    
HELIX   66 AH3 GLY F   66  ALA F   68  5                                   3    
HELIX   67 AH4 ILE F   69  LEU F   83  1                                  15    
HELIX   68 AH5 GLU F   90  ASP F   99  1                                  10    
HELIX   69 AH6 ASP F   99  GLN F  110  1                                  12    
HELIX   70 AH7 ASP F  125  VAL F  133  1                                   9    
HELIX   71 AH8 THR F  156  PHE F  167  1                                  12    
HELIX   72 AH9 ILE F  180  GLN F  184  5                                   5    
HELIX   73 AI1 ASN F  213  GLY F  217  5                                   5    
HELIX   74 AI2 THR F  226  MET F  240  1                                  15    
HELIX   75 AI3 LEU F  267  GLY F  275  1                                   9    
HELIX   76 AI4 ASP F  277  ALA F  290  1                                  14    
HELIX   77 AI5 LEU G   12  ARG G   25  1                                  14    
HELIX   78 AI6 ASP G   33  LEU G   35  5                                   3    
HELIX   79 AI7 GLY G   66  ALA G   68  5                                   3    
HELIX   80 AI8 ILE G   69  LEU G   83  1                                  15    
HELIX   81 AI9 GLU G   90  ASP G   99  1                                  10    
HELIX   82 AJ1 ASP G   99  GLN G  110  1                                  12    
HELIX   83 AJ2 ASP G  125  GLY G  134  1                                  10    
HELIX   84 AJ3 THR G  156  GLY G  169  1                                  14    
HELIX   85 AJ4 ILE G  180  GLN G  184  5                                   5    
HELIX   86 AJ5 ASN G  213  GLY G  217  5                                   5    
HELIX   87 AJ6 THR G  226  MET G  240  1                                  15    
HELIX   88 AJ7 LEU G  267  GLY G  275  1                                   9    
HELIX   89 AJ8 ASP G  277  ALA G  290  1                                  14    
HELIX   90 AJ9 LEU H   12  ARG H   25  1                                  14    
HELIX   91 AK1 ASP H   33  LEU H   35  5                                   3    
HELIX   92 AK2 GLY H   66  ALA H   68  5                                   3    
HELIX   93 AK3 ILE H   69  LEU H   83  1                                  15    
HELIX   94 AK4 GLU H   90  ARG H   98  1                                   9    
HELIX   95 AK5 ASP H   99  GLN H  110  1                                  12    
HELIX   96 AK6 ASP H  125  GLY H  134  1                                  10    
HELIX   97 AK7 THR H  156  ARG H  168  1                                  13    
HELIX   98 AK8 ILE H  180  GLN H  184  5                                   5    
HELIX   99 AK9 THR H  226  MET H  240  1                                  15    
HELIX  100 AL1 LEU H  267  GLY H  275  1                                   9    
HELIX  101 AL2 ASP H  277  ALA H  290  1                                  14    
SHEET    1 AA1 4 LEU A  28  LEU A  32  0                                        
SHEET    2 AA1 4 LYS A   2  SER A   7  1  N  ILE A   3   O  LEU A  28           
SHEET    3 AA1 4 ALA A  60  ARG A  64  1  O  ILE A  62   N  ALA A   4           
SHEET    4 AA1 4 TYR A  86  PRO A  87  1  O  TYR A  86   N  VAL A  61           
SHEET    1 AA2 7 ARG A  53  LYS A  54  0                                        
SHEET    2 AA2 7 ILE A  48  TYR A  50 -1  N  TYR A  50   O  ARG A  53           
SHEET    3 AA2 7 CYS A  37  ASN A  42 -1  N  TYR A  38   O  HIS A  49           
SHEET    4 AA2 7 THR B 117  ALA B 120 -1  O  ILE B 119   N  MET A  39           
SHEET    5 AA2 7 HIS B 173  GLU B 178 -1  O  ILE B 174   N  ALA B 120           
SHEET    6 AA2 7 LEU B 138  GLU B 144 -1  N  VAL B 139   O  GLN B 177           
SHEET    7 AA2 7 GLN B 147  ALA B 154 -1  O  ILE B 149   N  LEU B 142           
SHEET    1 AA3 7 VAL A 151  ALA A 154  0                                        
SHEET    2 AA3 7 LEU A 138  LEU A 142 -1  N  LEU A 138   O  ALA A 154           
SHEET    3 AA3 7 ILE A 174  GLU A 178 -1  O  GLN A 177   N  VAL A 139           
SHEET    4 AA3 7 THR A 117  ALA A 120 -1  N  GLY A 118   O  VAL A 176           
SHEET    5 AA3 7 CYS B  37  ASN B  42 -1  O  MET B  39   N  ILE A 119           
SHEET    6 AA3 7 ILE B  48  TYR B  50 -1  O  HIS B  49   N  TYR B  38           
SHEET    7 AA3 7 ARG B  53  LYS B  54 -1  O  ARG B  53   N  TYR B  50           
SHEET    1 AA4 5 ALA A 219  VAL A 222  0                                        
SHEET    2 AA4 5 GLU A 196  ARG A 204 -1  N  ARG A 204   O  ALA A 219           
SHEET    3 AA4 5 CYS A 186  VAL A 193 -1  N  ARG A 189   O  ILE A 201           
SHEET    4 AA4 5 VAL A 244  ALA A 252 -1  O  ALA A 245   N  VAL A 192           
SHEET    5 AA4 5 GLY A 255  ASN A 262 -1  O  MET A 259   N  ASP A 248           
SHEET    1 AA5 4 LEU B  28  LEU B  32  0                                        
SHEET    2 AA5 4 LYS B   2  SER B   7  1  N  ILE B   5   O  LEU B  32           
SHEET    3 AA5 4 ALA B  60  ARG B  64  1  O  ILE B  62   N  ALA B   4           
SHEET    4 AA5 4 TYR B  86  PRO B  87  1  O  TYR B  86   N  VAL B  61           
SHEET    1 AA6 5 GLY B 218  VAL B 222  0                                        
SHEET    2 AA6 5 GLU B 196  ALA B 205 -1  N  ARG B 204   O  ALA B 219           
SHEET    3 AA6 5 CYS B 186  VAL B 193 -1  N  LEU B 191   O  ALA B 199           
SHEET    4 AA6 5 VAL B 244  ALA B 252 -1  O  ALA B 245   N  VAL B 192           
SHEET    5 AA6 5 GLY B 255  ASN B 262 -1  O  MET B 259   N  ASP B 248           
SHEET    1 AA7 4 LEU C  28  LEU C  32  0                                        
SHEET    2 AA7 4 LYS C   2  LEU C   6  1  N  ILE C   3   O  LEU C  28           
SHEET    3 AA7 4 ALA C  60  PRO C  63  1  O  ILE C  62   N  ALA C   4           
SHEET    4 AA7 4 TYR C  86  PRO C  87  1  O  TYR C  86   N  VAL C  61           
SHEET    1 AA8 7 ARG C  53  LYS C  54  0                                        
SHEET    2 AA8 7 ILE C  48  TYR C  50 -1  N  TYR C  50   O  ARG C  53           
SHEET    3 AA8 7 CYS C  37  ASN C  42 -1  N  TYR C  38   O  HIS C  49           
SHEET    4 AA8 7 THR D 117  ALA D 120 -1  O  THR D 117   N  ILE C  41           
SHEET    5 AA8 7 HIS D 173  GLU D 178 -1  O  VAL D 176   N  GLY D 118           
SHEET    6 AA8 7 LEU D 138  GLU D 144 -1  N  VAL D 139   O  GLN D 177           
SHEET    7 AA8 7 GLN D 147  ALA D 154 -1  O  ILE D 149   N  LEU D 142           
SHEET    1 AA9 7 VAL C 151  ALA C 154  0                                        
SHEET    2 AA9 7 LEU C 138  LEU C 142 -1  N  LEU C 138   O  ALA C 154           
SHEET    3 AA9 7 ILE C 174  GLU C 178 -1  O  GLN C 177   N  VAL C 139           
SHEET    4 AA9 7 THR C 117  ALA C 120 -1  N  GLY C 118   O  VAL C 176           
SHEET    5 AA9 7 CYS D  37  ASN D  42 -1  O  MET D  39   N  ILE C 119           
SHEET    6 AA9 7 ILE D  48  TYR D  50 -1  O  HIS D  49   N  TYR D  38           
SHEET    7 AA9 7 ARG D  53  LYS D  54 -1  O  ARG D  53   N  TYR D  50           
SHEET    1 AB1 5 ALA C 219  VAL C 222  0                                        
SHEET    2 AB1 5 GLU C 196  ARG C 204 -1  N  GLU C 202   O  SER C 221           
SHEET    3 AB1 5 CYS C 186  VAL C 193 -1  N  ARG C 189   O  ILE C 201           
SHEET    4 AB1 5 VAL C 244  ALA C 252 -1  O  ALA C 245   N  VAL C 192           
SHEET    5 AB1 5 GLY C 255  ASN C 262 -1  O  MET C 259   N  ASP C 248           
SHEET    1 AB2 4 LEU D  28  LEU D  32  0                                        
SHEET    2 AB2 4 LYS D   2  LEU D   6  1  N  ILE D   3   O  LEU D  28           
SHEET    3 AB2 4 ALA D  60  PRO D  63  1  O  ILE D  62   N  ALA D   4           
SHEET    4 AB2 4 TYR D  86  PRO D  87  1  O  TYR D  86   N  VAL D  61           
SHEET    1 AB3 5 ALA D 219  VAL D 222  0                                        
SHEET    2 AB3 5 GLU D 196  ARG D 204 -1  N  ARG D 204   O  ALA D 219           
SHEET    3 AB3 5 CYS D 186  VAL D 193 -1  N  LEU D 191   O  ALA D 199           
SHEET    4 AB3 5 VAL D 244  ALA D 252 -1  O  ALA D 245   N  VAL D 192           
SHEET    5 AB3 5 GLY D 255  ASN D 262 -1  O  LEU D 257   N  LEU D 250           
SHEET    1 AB4 4 LEU E  28  LEU E  32  0                                        
SHEET    2 AB4 4 LYS E   2  LEU E   6  1  N  ILE E   5   O  LEU E  32           
SHEET    3 AB4 4 ALA E  60  PRO E  63  1  O  ILE E  62   N  ALA E   4           
SHEET    4 AB4 4 TYR E  86  PRO E  87  1  O  TYR E  86   N  VAL E  61           
SHEET    1 AB5 7 ARG E  53  LYS E  54  0                                        
SHEET    2 AB5 7 ILE E  48  TYR E  50 -1  N  TYR E  50   O  ARG E  53           
SHEET    3 AB5 7 CYS E  37  ASN E  40 -1  N  TYR E  38   O  HIS E  49           
SHEET    4 AB5 7 THR F 117  ALA F 120 -1  O  ILE F 119   N  MET E  39           
SHEET    5 AB5 7 HIS F 173  GLU F 178 -1  O  VAL F 176   N  GLY F 118           
SHEET    6 AB5 7 LEU F 138  GLU F 144 -1  N  VAL F 139   O  GLN F 177           
SHEET    7 AB5 7 GLN F 147  ALA F 154 -1  O  ILE F 149   N  LEU F 142           
SHEET    1 AB6 7 VAL E 151  ALA E 154  0                                        
SHEET    2 AB6 7 LEU E 138  LEU E 142 -1  N  LEU E 138   O  ALA E 154           
SHEET    3 AB6 7 ILE E 174  GLU E 178 -1  O  GLN E 177   N  VAL E 139           
SHEET    4 AB6 7 THR E 117  ALA E 120 -1  N  GLY E 118   O  VAL E 176           
SHEET    5 AB6 7 CYS F  37  ASN F  40 -1  O  MET F  39   N  ILE E 119           
SHEET    6 AB6 7 ILE F  48  TYR F  50 -1  O  HIS F  49   N  TYR F  38           
SHEET    7 AB6 7 ARG F  53  LYS F  54 -1  O  ARG F  53   N  TYR F  50           
SHEET    1 AB7 5 ALA E 219  VAL E 222  0                                        
SHEET    2 AB7 5 GLU E 196  ARG E 204 -1  N  GLU E 202   O  SER E 221           
SHEET    3 AB7 5 CYS E 186  VAL E 193 -1  N  ASP E 187   O  ARG E 203           
SHEET    4 AB7 5 VAL E 244  ALA E 252 -1  O  ALA E 245   N  VAL E 192           
SHEET    5 AB7 5 GLY E 255  ASN E 262 -1  O  MET E 259   N  ASP E 248           
SHEET    1 AB8 4 LEU F  28  LEU F  32  0                                        
SHEET    2 AB8 4 LYS F   2  LEU F   6  1  N  ILE F   3   O  LEU F  28           
SHEET    3 AB8 4 ALA F  60  PRO F  63  1  O  ILE F  62   N  ALA F   4           
SHEET    4 AB8 4 TYR F  86  PRO F  87  1  O  TYR F  86   N  VAL F  61           
SHEET    1 AB9 5 ALA F 219  VAL F 222  0                                        
SHEET    2 AB9 5 GLU F 196  ARG F 204 -1  N  ARG F 204   O  ALA F 219           
SHEET    3 AB9 5 CYS F 186  VAL F 193 -1  N  LEU F 191   O  ALA F 199           
SHEET    4 AB9 5 VAL F 244  ALA F 252 -1  O  VAL F 247   N  CYS F 190           
SHEET    5 AB9 5 GLY F 255  ASN F 262 -1  O  MET F 259   N  ASP F 248           
SHEET    1 AC1 4 LEU G  28  LEU G  32  0                                        
SHEET    2 AC1 4 LYS G   2  LEU G   6  1  N  ILE G   3   O  LEU G  28           
SHEET    3 AC1 4 ALA G  60  PRO G  63  1  O  ILE G  62   N  ALA G   4           
SHEET    4 AC1 4 TYR G  86  PRO G  87  1  O  TYR G  86   N  VAL G  61           
SHEET    1 AC2 7 ARG G  53  LYS G  54  0                                        
SHEET    2 AC2 7 ILE G  48  TYR G  50 -1  N  TYR G  50   O  ARG G  53           
SHEET    3 AC2 7 CYS G  37  ASN G  42 -1  N  TYR G  38   O  HIS G  49           
SHEET    4 AC2 7 THR H 117  ALA H 120 -1  O  ILE H 119   N  MET G  39           
SHEET    5 AC2 7 HIS H 173  GLU H 178 -1  O  VAL H 176   N  GLY H 118           
SHEET    6 AC2 7 LEU H 138  GLU H 144 -1  N  VAL H 143   O  HIS H 173           
SHEET    7 AC2 7 GLN H 147  ALA H 154 -1  O  VAL H 152   N  VAL H 140           
SHEET    1 AC3 7 VAL G 151  ALA G 154  0                                        
SHEET    2 AC3 7 LEU G 138  LEU G 142 -1  N  LEU G 138   O  ALA G 154           
SHEET    3 AC3 7 ILE G 174  GLU G 178 -1  O  GLN G 177   N  VAL G 139           
SHEET    4 AC3 7 THR G 117  ALA G 120 -1  N  GLY G 118   O  VAL G 176           
SHEET    5 AC3 7 CYS H  37  ASN H  42 -1  O  MET H  39   N  ILE G 119           
SHEET    6 AC3 7 ILE H  48  TYR H  50 -1  O  HIS H  49   N  TYR H  38           
SHEET    7 AC3 7 ARG H  53  LYS H  54 -1  O  ARG H  53   N  TYR H  50           
SHEET    1 AC4 5 ALA G 219  VAL G 222  0                                        
SHEET    2 AC4 5 GLU G 196  ARG G 204 -1  N  GLU G 202   O  SER G 221           
SHEET    3 AC4 5 CYS G 186  VAL G 193 -1  N  LEU G 191   O  ALA G 199           
SHEET    4 AC4 5 VAL G 244  ALA G 252 -1  O  VAL G 247   N  CYS G 190           
SHEET    5 AC4 5 GLY G 255  ASN G 262 -1  O  MET G 259   N  ASP G 248           
SHEET    1 AC5 4 LEU H  28  LEU H  32  0                                        
SHEET    2 AC5 4 LYS H   2  LEU H   6  1  N  ILE H   3   O  LEU H  28           
SHEET    3 AC5 4 ALA H  60  PRO H  63  1  O  ILE H  62   N  ALA H   4           
SHEET    4 AC5 4 TYR H  86  PRO H  87  1  O  TYR H  86   N  VAL H  61           
SHEET    1 AC6 5 GLY H 218  VAL H 222  0                                        
SHEET    2 AC6 5 GLU H 196  ALA H 205 -1  N  GLU H 202   O  SER H 221           
SHEET    3 AC6 5 CYS H 186  VAL H 193 -1  N  ASP H 187   O  ARG H 203           
SHEET    4 AC6 5 VAL H 244  ALA H 252 -1  O  ALA H 245   N  VAL H 192           
SHEET    5 AC6 5 GLY H 255  ASN H 262 -1  O  MET H 259   N  ASP H 248           
LINK         N   GLY A 148                 O2B ANP A 401     1555   1555  1.33  
LINK         NH2 ARG A 203                 O2  SO4 A 404     1555   1555  1.30  
LINK         NH2 ARG B 102                 O3  SO4 B 403     1555   1555  1.30  
LINK         ND2 ASN B 213                 O2G ANP B 401     1555   1555  1.30  
LINK         OE2 GLU B 260                MG    MG B 402     1555   1555  2.45  
LINK         OE1 GLU D 260                MG    MG D 402     1555   1555  2.70  
LINK         OE2 GLU D 260                MG    MG D 402     1555   1555  2.35  
LINK         N   GLY E 148                 O1B ANP E 402     1555   1555  1.32  
LINK         NH2 ARG E 203                 O3  SO4 E 401     1555   1555  1.30  
LINK         OE2 GLU F 260                MG    MG F 402     1555   1555  2.03  
LINK         NH1 ARG G 203                 O1  SO4 G 403     1555   1555  1.30  
LINK         ND2 ASN H 213                 O3G ANP H 401     1555   1555  1.30  
LINK         OD2 ASP H 248                MG    MG H 402     1555   1555  2.71  
LINK         OE2 GLU H 260                MG    MG H 402     1555   1555  2.89  
LINK         O1G ANP A 401                MG    MG A 402     1555   1555  2.08  
LINK         O1B ANP A 401                MG    MG A 402     1555   1555  2.15  
LINK         O1A ANP A 401                MG    MG A 402     1555   1555  2.19  
LINK        MG    MG A 402                 O   HOH A 520     1555   1555  2.11  
LINK        MG    MG A 402                 O   HOH A 508     1555   1555  2.06  
LINK        MG    MG A 402                 O   HOH A 586     1555   1555  2.01  
LINK         O1G ANP B 401                MG    MG B 402     1555   1555  1.92  
LINK         O1B ANP B 401                MG    MG B 402     1555   1555  2.68  
LINK         O2A ANP B 401                MG    MG B 402     1555   1555  2.65  
LINK         O3G ANP C 401                MG    MG C 402     1555   1555  2.28  
LINK         O2B ANP C 401                MG    MG C 402     1555   1555  2.27  
LINK         O1A ANP C 401                MG    MG C 402     1555   1555  2.01  
LINK        MG    MG C 402                 O   HOH C 513     1555   1555  2.02  
LINK        MG    MG C 402                 O   HOH C 623     1555   1555  2.08  
LINK        MG    MG C 402                 O   HOH C 514     1555   1555  2.13  
LINK         O3G ANP D 401                MG    MG D 402     1555   1555  2.22  
LINK         O2B ANP D 401                MG    MG D 402     1555   1555  2.44  
LINK         O2A ANP D 401                MG    MG D 402     1555   1555  2.47  
LINK        MG    MG D 402                 O   HOH D 523     1555   1555  2.16  
LINK        MG    MG D 402                 O   HOH D 506     1555   1555  1.96  
LINK         O3G ANP E 402                MG    MG E 403     1555   1555  1.95  
LINK         O2B ANP E 402                MG    MG E 403     1555   1555  2.22  
LINK         O1A ANP E 402                MG    MG E 403     1555   1555  1.97  
LINK        MG    MG E 403                 O   HOH E 559     1555   1555  2.16  
LINK        MG    MG E 403                 O   HOH E 502     1555   1555  2.14  
LINK        MG    MG E 403                 O   HOH E 564     1555   1555  1.97  
LINK         O2G ANP F 401                MG    MG F 402     1555   1555  2.12  
LINK         O2B ANP F 401                MG    MG F 402     1555   1555  2.56  
LINK         O2A ANP F 401                MG    MG F 402     1555   1555  2.05  
LINK         O1G ANP G 401                MG    MG G 402     1555   1555  2.13  
LINK         O1B ANP G 401                MG    MG G 402     1555   1555  2.10  
LINK         O2A ANP G 401                MG    MG G 402     1555   1555  2.08  
LINK        MG    MG G 402                 O   HOH G 505     1555   1555  2.18  
LINK        MG    MG G 402                 O   HOH G 576     1555   1555  2.12  
LINK        MG    MG G 402                 O   HOH G 532     1555   1555  2.19  
LINK         O2G ANP H 401                MG    MG H 402     1555   1555  2.21  
LINK         O1A ANP H 401                MG    MG H 402     1555   1555  2.48  
CISPEP   1 ASN A   42    PRO A   43          0         9.32                     
CISPEP   2 ALA A  136    PRO A  137          0        -1.17                     
CISPEP   3 ASN B   42    PRO B   43          0         2.49                     
CISPEP   4 ALA B  136    PRO B  137          0        -5.00                     
CISPEP   5 ASN C   42    PRO C   43          0         2.79                     
CISPEP   6 ALA C  136    PRO C  137          0        -2.02                     
CISPEP   7 ASN D   42    PRO D   43          0         3.78                     
CISPEP   8 ALA D  136    PRO D  137          0        -1.10                     
CISPEP   9 ALA E  136    PRO E  137          0        -2.66                     
CISPEP  10 ALA F  136    PRO F  137          0        -8.00                     
CISPEP  11 ASN G   42    PRO G   43          0         5.89                     
CISPEP  12 ALA G  136    PRO G  137          0        -3.14                     
CISPEP  13 ASN H   42    PRO H   43          0         0.21                     
CISPEP  14 ALA H  136    PRO H  137          0         2.55                     
SITE     1 AC1 27 LYS A 100  VAL A 139  LYS A 141  GLY A 145                    
SITE     2 AC1 27 THR A 146  GLN A 147  GLY A 148  GLN A 177                    
SITE     3 AC1 27 GLU A 178  TYR A 179  ILE A 180  PHE A 210                    
SITE     4 AC1 27 ARG A 211  SER A 212  ASN A 213  MET A 259                    
SITE     5 AC1 27 GLU A 260   MG A 402  HOH A 508  HOH A 520                    
SITE     6 AC1 27 HOH A 552  HOH A 569  HOH A 584  HOH A 586                    
SITE     7 AC1 27 HOH A 587  HOH A 640  HOH A 668                               
SITE     1 AC2  4 ANP A 401  HOH A 508  HOH A 520  HOH A 586                    
SITE     1 AC3  7 ARG A 284  ARG A 288  HOH A 533  HOH A 583                    
SITE     2 AC3  7 HOH A 599  ARG G 284  ARG G 288                               
SITE     1 AC4  5 ARG A 189  ARG A 203  ASN A 213  LEU A 214                    
SITE     2 AC4  5 HOH A 515                                                     
SITE     1 AC5  3 ARG A  96  ARG A 102  HOH A 526                               
SITE     1 AC6  4 ARG B 189  ASP B 248  GLU B 260  ANP B 401                    
SITE     1 AC7 26 LYS C 100  LYS C 141  GLY C 145  THR C 146                    
SITE     2 AC7 26 GLN C 147  GLY C 148  GLN C 177  GLU C 178                    
SITE     3 AC7 26 TYR C 179  ILE C 180  PHE C 210  ARG C 211                    
SITE     4 AC7 26 SER C 212  ASN C 213  LEU C 250  MET C 259                    
SITE     5 AC7 26 GLU C 260   MG C 402  HOH C 513  HOH C 514                    
SITE     6 AC7 26 HOH C 551  HOH C 557  HOH C 564  HOH C 601                    
SITE     7 AC7 26 HOH C 606  HOH C 623                                          
SITE     1 AC8  4 ANP C 401  HOH C 513  HOH C 514  HOH C 623                    
SITE     1 AC9  6 GLN C 147  ARG C 189  ARG C 203  ASN C 213                    
SITE     2 AC9  6 LEU C 214  HOH C 513                                          
SITE     1 AD1  5 ARG C  96  ARG C 102  ARG C 109  HOH C 537                    
SITE     2 AD1  5 VAL D  92                                                     
SITE     1 AD2  7 ARG C 284  ARG C 288  HOH C 547  HOH C 552                    
SITE     2 AD2  7 HOH C 614  ARG E 284  ARG E 288                               
SITE     1 AD3 20 LYS D 100  VAL D 139  LYS D 141  VAL D 151                    
SITE     2 AD3 20 GLN D 177  GLU D 178  TYR D 179  ILE D 180                    
SITE     3 AD3 20 ASP D 187  ARG D 203  PHE D 210  ARG D 211                    
SITE     4 AD3 20 SER D 212  ASN D 213  MET D 259  GLU D 260                    
SITE     5 AD3 20  MG D 402  HOH D 506  HOH D 523  HOH D 556                    
SITE     1 AD4  5 ASN D 213  GLU D 260  ANP D 401  HOH D 506                    
SITE     2 AD4  5 HOH D 523                                                     
SITE     1 AD5  3 VAL C  92  ARG D 102  HOH D 514                               
SITE     1 AD6  4 ANP E 402  HOH E 502  HOH E 559  HOH E 564                    
SITE     1 AD7  5 ARG E  96  ARG E 102  LEU E 106  HOH E 575                    
SITE     2 AD7  5 VAL F  92                                                     
SITE     1 AD8 18 LYS F 100  LYS F 141  VAL F 151  GLN F 177                    
SITE     2 AD8 18 GLU F 178  TYR F 179  ILE F 180  PHE F 210                    
SITE     3 AD8 18 ARG F 211  SER F 212  ASN F 213  HIS F 215                    
SITE     4 AD8 18 ARG F 216  LEU F 250  MET F 259  GLU F 260                    
SITE     5 AD8 18  MG F 402  HOH F 510                                          
SITE     1 AD9  3 ASN F 213  GLU F 260  ANP F 401                               
SITE     1 AE1  4 ARG F  96  ARG F 102  LEU F 106  HOH F 502                    
SITE     1 AE2 27 LYS G 100  LYS G 141  GLY G 145  THR G 146                    
SITE     2 AE2 27 GLN G 147  GLY G 148  GLN G 177  GLU G 178                    
SITE     3 AE2 27 ILE G 180  ASP G 187  PHE G 210  ARG G 211                    
SITE     4 AE2 27 SER G 212  ASN G 213  LEU G 250  MET G 259                    
SITE     5 AE2 27 GLU G 260   MG G 402  HOH G 505  HOH G 516                    
SITE     6 AE2 27 HOH G 532  HOH G 569  HOH G 576  HOH G 581                    
SITE     7 AE2 27 HOH G 582  HOH G 583  HOH G 638                               
SITE     1 AE3  4 ANP G 401  HOH G 505  HOH G 532  HOH G 576                    
SITE     1 AE4  4 ARG G  96  ARG G 102  LEU G 106  VAL H  92                    
SITE     1 AE5  5 ARG H 203  ASN H 213  ASP H 248  GLU H 260                    
SITE     2 AE5  5 ANP H 401                                                     
SITE     1 AE6  5 VAL G  92  ARG H  96  ARG H 102  ARG H 109                    
SITE     2 AE6  5 HOH H 534                                                     
SITE     1 AE7 20 LYS B 100  VAL B 139  LYS B 141  VAL B 151                    
SITE     2 AE7 20 GLN B 177  GLU B 178  TYR B 179  ILE B 180                    
SITE     3 AE7 20 ASP B 187  ARG B 203  PHE B 210  ARG B 211                    
SITE     4 AE7 20 SER B 212  LEU B 214  HIS B 215  ARG B 216                    
SITE     5 AE7 20 LEU B 250  MET B 259  GLU B 260   MG B 402                    
SITE     1 AE8 11 ARG A  78  ARG B  96  ASP B  99  LYS B 100                    
SITE     2 AE8 11 LEU B 101  SER B 103  MET B 104  GLN B 105                    
SITE     3 AE8 11 LEU B 106  HOH B 509  HOH B 531                               
SITE     1 AE9 10 GLY E 185  CYS E 186  ASP E 187  ARG E 189                    
SITE     2 AE9 10 GLU E 202  ARG E 204  SER E 212  ASN E 213                    
SITE     3 AE9 10 LEU E 214  ALA E 219                                          
SITE     1 AF1 26 LYS E 141  GLY E 145  THR E 146  GLN E 147                    
SITE     2 AF1 26 ILE E 149  GLY E 150  VAL E 151  GLN E 177                    
SITE     3 AF1 26 GLU E 178  TYR E 179  ILE E 180  ASP E 187                    
SITE     4 AF1 26 PHE E 210  ARG E 211  SER E 212  ASN E 213                    
SITE     5 AF1 26 LEU E 250  MET E 259   MG E 403  HOH E 502                    
SITE     6 AF1 26 HOH E 508  HOH E 550  HOH E 559  HOH E 564                    
SITE     7 AF1 26 HOH E 573  HOH E 585                                          
SITE     1 AF2 12 GLY G 185  CYS G 186  ASP G 187  ARG G 189                    
SITE     2 AF2 12 GLU G 202  ARG G 204  SER G 212  ASN G 213                    
SITE     3 AF2 12 LEU G 214  ALA G 219  HOH G 532  HOH G 576                    
SITE     1 AF3 23 LYS H 100  VAL H 139  LYS H 141  VAL H 151                    
SITE     2 AF3 23 GLN H 177  GLU H 178  TYR H 179  ILE H 180                    
SITE     3 AF3 23 ASP H 187  ARG H 203  PHE H 210  ARG H 211                    
SITE     4 AF3 23 SER H 212  LEU H 214  HIS H 215  ARG H 216                    
SITE     5 AF3 23 GLY H 217  GLY H 218  LEU H 250  MET H 259                    
SITE     6 AF3 23 GLU H 260   MG H 402  HOH H 547                               
CRYST1  212.618  121.628  119.741  90.00 118.74  90.00 C 1 2 1      32          
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      0.004703  0.000000  0.002579        0.00000                         
SCALE2      0.000000  0.008222  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009525        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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