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Database: PDB
Entry: 3R5X
LinkDB: 3R5X
Original site: 3R5X 
HEADER    LIGASE                                  20-MAR-11   3R5X              
TITLE     CRYSTAL STRUCTURE OF D-ALANINE--D-ALANINE LIGASE FROM BACILLUS        
TITLE    2 ANTHRACIS COMPLEXED WITH ATP                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;                               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: D-ALA-D-ALA LIGASE, D-ALANYLALANINE SYNTHETASE;             
COMPND   5 EC: 6.3.2.4;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;                             
SOURCE   3 ORGANISM_COMMON: ANTHRAX,ANTHRAX BACTERIUM;                          
SOURCE   4 ORGANISM_TAXID: 1392;                                                
SOURCE   5 STRAIN: AMES;                                                        
SOURCE   6 GENE: BAS2435, BA_2610, DDL, DDLB, GBAA_2610;                        
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;                                
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    ALPHA-BETA STRUCTURE, LIGASE, CYTOSOL, STRUCTURAL GENOMICS, CENTER    
KEYWDS   2 FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.KIM,R.MULLIGAN,J.HASSEMAN,W.F.ANDERSON,A.JOACHIMIAK,CSGID           
REVDAT   1   06-APR-11 3R5X    0                                                
JRNL        AUTH   Y.KIM,J.HASSEMAN,W.F.ANDERSON,A.JOACHIMIAK,CSGID             
JRNL        TITL   CRYSTAL STRUCTURE OF D-ALANINE--D-ALANINE LIGASE FROM        
JRNL        TITL 2 BACILLUS ANTHRACIS COMPLEXED WITH ATP                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.77                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 84091                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4235                            
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 32.7796 -  6.2089    0.87     2412   107  0.1687 0.1905        
REMARK   3     2  6.2089 -  4.9336    0.99     2705   153  0.1571 0.1876        
REMARK   3     3  4.9336 -  4.3115    0.99     2694   137  0.1252 0.1767        
REMARK   3     4  4.3115 -  3.9180    0.99     2754   150  0.1348 0.1582        
REMARK   3     5  3.9180 -  3.6376    0.98     2654   166  0.1543 0.1833        
REMARK   3     6  3.6376 -  3.4234    0.98     2702   156  0.1670 0.2059        
REMARK   3     7  3.4234 -  3.2521    0.98     2701   141  0.1780 0.1993        
REMARK   3     8  3.2521 -  3.1106    0.98     2679   148  0.1801 0.2360        
REMARK   3     9  3.1106 -  2.9910    0.98     2684   159  0.1916 0.2453        
REMARK   3    10  2.9910 -  2.8878    0.98     2752   127  0.1825 0.2549        
REMARK   3    11  2.8878 -  2.7976    0.98     2663   150  0.1782 0.2334        
REMARK   3    12  2.7976 -  2.7176    0.98     2731   139  0.1828 0.2307        
REMARK   3    13  2.7176 -  2.6461    0.98     2663   124  0.1878 0.2823        
REMARK   3    14  2.6461 -  2.5816    0.98     2702   160  0.1946 0.2471        
REMARK   3    15  2.5816 -  2.5229    0.98     2721   121  0.1908 0.2686        
REMARK   3    16  2.5229 -  2.4693    0.98     2686   128  0.2076 0.2967        
REMARK   3    17  2.4693 -  2.4199    0.98     2720   113  0.2059 0.2589        
REMARK   3    18  2.4199 -  2.3742    0.98     2672   141  0.2000 0.2816        
REMARK   3    19  2.3742 -  2.3318    0.97     2690   147  0.1960 0.2651        
REMARK   3    20  2.3318 -  2.2923    0.98     2684   145  0.2070 0.2544        
REMARK   3    21  2.2923 -  2.2554    0.97     2635   153  0.2198 0.2783        
REMARK   3    22  2.2554 -  2.2207    0.97     2690   142  0.2379 0.3337        
REMARK   3    23  2.2207 -  2.1880    0.97     2682   148  0.2333 0.2603        
REMARK   3    24  2.1880 -  2.1572    0.97     2586   148  0.2388 0.2977        
REMARK   3    25  2.1572 -  2.1281    0.97     2739   146  0.2520 0.3049        
REMARK   3    26  2.1281 -  2.1004    0.97     2626   136  0.2668 0.3232        
REMARK   3    27  2.1004 -  2.0742    0.96     2663   138  0.2709 0.2991        
REMARK   3    28  2.0742 -  2.0492    0.95     2639   143  0.2876 0.3150        
REMARK   3    29  2.0492 -  2.0254    0.94     2558   145  0.3060 0.3423        
REMARK   3    30  2.0254 -  2.0000    0.86     2369   124  0.3177 0.3599        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.30                                          
REMARK   3   SHRINKAGE RADIUS   : 1.06                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 48.25                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 37.17                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 59.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.02830                                             
REMARK   3    B22 (A**2) : -2.21840                                             
REMARK   3    B33 (A**2) : 3.24670                                              
REMARK   3    B12 (A**2) : -2.26710                                             
REMARK   3    B13 (A**2) : 5.57960                                              
REMARK   3    B23 (A**2) : -16.28000                                            
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      :  0.010           9789                                  
REMARK   3   ANGLE     :  1.284          13253                                  
REMARK   3   CHIRALITY :  0.085           1511                                  
REMARK   3   PLANARITY :  0.007           1677                                  
REMARK   3   DIHEDRAL  : 16.867           3781                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  85.5771  74.3076  -4.7055              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3555 T22:   0.2563                                     
REMARK   3      T33:   0.2836 T12:  -0.0067                                     
REMARK   3      T13:   0.0193 T23:   0.0240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8700 L22:   0.9611                                     
REMARK   3      L33:   0.8950 L12:  -0.3988                                     
REMARK   3      L13:  -0.4749 L23:   0.9726                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0092 S12:  -0.0262 S13:  -0.1838                       
REMARK   3      S21:   0.1956 S22:  -0.0200 S23:   0.1142                       
REMARK   3      S31:   0.1036 S32:   0.0133 S33:   0.0329                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  86.6655  96.9733  15.8858              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4671 T22:   0.3404                                     
REMARK   3      T33:   0.2364 T12:  -0.0616                                     
REMARK   3      T13:   0.0500 T23:  -0.0276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0150 L22:   1.2412                                     
REMARK   3      L33:   0.9114 L12:   0.0778                                     
REMARK   3      L13:  -0.3054 L23:   1.2894                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1650 S12:  -0.2085 S13:   0.1591                       
REMARK   3      S21:   0.2689 S22:   0.0213 S23:   0.0727                       
REMARK   3      S31:  -0.1401 S32:   0.2373 S33:  -0.0415                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  46.0478  46.3889  43.2259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2909 T22:   0.2646                                     
REMARK   3      T33:   0.2957 T12:  -0.0394                                     
REMARK   3      T13:   0.0364 T23:  -0.0337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9525 L22:   0.9693                                     
REMARK   3      L33:   2.0302 L12:   0.2950                                     
REMARK   3      L13:   0.1611 L23:   0.9306                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0773 S12:   0.2627 S13:  -0.1927                       
REMARK   3      S21:  -0.0792 S22:   0.1580 S23:  -0.2333                       
REMARK   3      S31:   0.1446 S32:  -0.0480 S33:  -0.0382                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  57.3223  71.6588  55.5291              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1148 T22:   0.2415                                     
REMARK   3      T33:   0.3796 T12:   0.0428                                     
REMARK   3      T13:  -0.0408 T23:  -0.0586                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5574 L22:   1.4651                                     
REMARK   3      L33:   1.3731 L12:   0.4179                                     
REMARK   3      L13:   0.1194 L23:   0.7553                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0339 S12:   0.0695 S13:   0.2355                       
REMARK   3      S21:   0.0591 S22:   0.1062 S23:  -0.2309                       
REMARK   3      S31:   0.0628 S32:   0.0211 S33:  -0.0229                       
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 3R5X COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB064529.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 84177                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 2.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.40800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.840                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: HKL3000, SHELXS,MLPHARE,BUCCANEER                     
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5, 20 % W/V          
REMARK 280  POLYETHYLENE GLYCOL MONOMETHYL ETHER 5000, VAPOR DIFFUSION,         
REMARK 280  SITTING DROP, TEMPERATURE 289K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11020 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 50580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -138.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -48.21969            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       25.22597            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000       88.50499            
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     SER A   139                                                      
REMARK 465     GLY A   140                                                      
REMARK 465     GLY A   141                                                      
REMARK 465     SER A   142                                                      
REMARK 465     PHE A   304                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     GLY B   141                                                      
REMARK 465     SER B   142                                                      
REMARK 465     SER B   143                                                      
REMARK 465     VAL B   144                                                      
REMARK 465     ASP B   203                                                      
REMARK 465     TYR B   204                                                      
REMARK 465     ASN B   205                                                      
REMARK 465     ALA B   206                                                      
REMARK 465     LYS B   207                                                      
REMARK 465     TYR B   208                                                      
REMARK 465     ASP B   209                                                      
REMARK 465     ASP B   210                                                      
REMARK 465     ALA B   211                                                      
REMARK 465     PHE B   304                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     ASN C    -1                                                      
REMARK 465     SER C   139                                                      
REMARK 465     GLY C   140                                                      
REMARK 465     GLY C   141                                                      
REMARK 465     SER C   142                                                      
REMARK 465     SER C   143                                                      
REMARK 465     VAL C   144                                                      
REMARK 465     ALA C   198                                                      
REMARK 465     ALA C   199                                                      
REMARK 465     GLU C   200                                                      
REMARK 465     PHE C   201                                                      
REMARK 465     PHE C   202                                                      
REMARK 465     ASP C   203                                                      
REMARK 465     TYR C   204                                                      
REMARK 465     ASN C   205                                                      
REMARK 465     ALA C   206                                                      
REMARK 465     LYS C   207                                                      
REMARK 465     TYR C   208                                                      
REMARK 465     ASP C   209                                                      
REMARK 465     ASP C   210                                                      
REMARK 465     ALA C   211                                                      
REMARK 465     SER C   212                                                      
REMARK 465     SER D    -2                                                      
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   O1G  ATP A   311     O    HOH A   646              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS C 241   CB    CYS C 241   SG     -0.113                       
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    SER A  11     -136.59     50.07                                   
REMARK 500    ASP A 203     -124.63     45.42                                   
REMARK 500    VAL A 243      -61.79     73.88                                   
REMARK 500    SER B  11     -137.76     55.82                                   
REMARK 500    VAL B 243      -62.11     73.17                                   
REMARK 500    SER C  11     -130.96     46.58                                   
REMARK 500    VAL C 243      -59.15     70.00                                   
REMARK 500    SER D  11     -131.18     47.49                                   
REMARK 500    VAL D 243      -61.63     73.53                                   
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 A 334        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH A 336        DISTANCE =  7.54 ANGSTROMS                       
REMARK 525    HOH A 357        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH C 347        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH C 349        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH D 307        DISTANCE =  5.31 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                              CA A 310  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP A 311   O2B                                                    
REMARK 620 2 GLU A 260   OE2  72.1                                              
REMARK 620 3 ATP A 311   O2A  74.0  90.5                                        
REMARK 620 4 ASP A 248   OD2 162.0  94.1 118.8                                  
REMARK 620 5 HOH A 689   O    71.7  50.2 134.0  90.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 313  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG C 299   O                                                      
REMARK 620 2 GLU C 302   O    82.7                                              
REMARK 620 3 HOH C 667   O    92.7  69.8                                        
REMARK 620 4 HOH C 668   O    72.3  92.3 158.3                                  
REMARK 620 5 HOH C 669   O   138.5 132.2 118.0  83.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 310  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP D 311   O3A                                                    
REMARK 620 2 ASP D 248   OD2 166.1                                              
REMARK 620 3 HOH D 528   O    83.7  99.7                                        
REMARK 620 4 GLU D 260   OE2  86.3  80.2  90.6                                  
REMARK 620 5 ATP D 311   O3B  57.7 109.9 121.8  49.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 310  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 260   OE2                                                    
REMARK 620 2 ASP B 248   OD2  87.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 312  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 542   O                                                      
REMARK 620 2 TYR D 208   O    82.4                                              
REMARK 620 3 GLU D 200   OE1  87.0 127.3                                        
REMARK 620 4 ASP D 203   OD2 170.2  89.4  93.9                                  
REMARK 620 5 GLU D 200   OE2  82.3  77.2  50.3  90.8                            
REMARK 620 6 HOH D 543   O    84.5  71.8 157.7  97.9 147.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 312  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 108   OE1                                                    
REMARK 620 2 GLU C 108   OE2  51.0                                              
REMARK 620 3 HOH C 642   O    88.2  91.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 310  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 248   OD2                                                    
REMARK 620 2 HOH C 536   O    67.6                                              
REMARK 620 3 GLU C 260   OE1  98.2 117.2                                        
REMARK 620 4 ATP C 311   O1A 102.1  47.1  81.8                                  
REMARK 620 5 ATP C 311   O2B 158.3  94.4  78.8  56.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 312  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B 281   O                                                      
REMARK 620 2 HOH B 626   O    78.9                                              
REMARK 620 3 HOH B 628   O    74.4 102.2                                        
REMARK 620 4 HOH B 627   O   133.6  77.4 149.8                                  
REMARK 620 5 HOH B 630   O   145.0  77.1  86.3  64.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 310                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 310                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 312                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 310                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 312                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 313                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 310                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP D 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 312                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 313                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY D 314                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3R23   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN APO-FORM                                            
REMARK 900 RELATED ID: IDP01207   RELATED DB: TARGETDB                          
DBREF  3R5X A  313   304  UNP    Q81Q29   DDL_BACAN        1    304             
DBREF  3R5X B    1   304  UNP    Q81Q29   DDL_BACAN        1    304             
DBREF  3R5X C    1   304  UNP    Q81Q29   DDL_BACAN        1    304             
DBREF  3R5X D    1   304  UNP    Q81Q29   DDL_BACAN        1    304             
SEQADV 3R5X SER A   -2  UNP  Q81Q29              EXPRESSION TAG                 
SEQADV 3R5X ASN A   -1  UNP  Q81Q29              EXPRESSION TAG                 
SEQADV 3R5X ALA A    0  UNP  Q81Q29              EXPRESSION TAG                 
SEQADV 3R5X SER B   -2  UNP  Q81Q29              EXPRESSION TAG                 
SEQADV 3R5X ASN B   -1  UNP  Q81Q29              EXPRESSION TAG                 
SEQADV 3R5X ALA B    0  UNP  Q81Q29              EXPRESSION TAG                 
SEQADV 3R5X SER C   -2  UNP  Q81Q29              EXPRESSION TAG                 
SEQADV 3R5X ASN C   -1  UNP  Q81Q29              EXPRESSION TAG                 
SEQADV 3R5X ALA C    0  UNP  Q81Q29              EXPRESSION TAG                 
SEQADV 3R5X SER D   -2  UNP  Q81Q29              EXPRESSION TAG                 
SEQADV 3R5X ASN D   -1  UNP  Q81Q29              EXPRESSION TAG                 
SEQADV 3R5X ALA D    0  UNP  Q81Q29              EXPRESSION TAG                 
SEQRES   1 A  307  SER ASN ALA MSE ARG ILE GLY VAL ILE MSE GLY GLY VAL          
SEQRES   2 A  307  SER SER GLU LYS GLN VAL SER ILE MSE THR GLY ASN GLU          
SEQRES   3 A  307  MSE ILE ALA ASN LEU ASP LYS ASN LYS TYR GLU ILE VAL          
SEQRES   4 A  307  PRO ILE THR LEU ASN GLU LYS MSE ASP LEU ILE GLU LYS          
SEQRES   5 A  307  ALA LYS ASP ILE ASP PHE ALA LEU LEU ALA LEU HIS GLY          
SEQRES   6 A  307  LYS TYR GLY GLU ASP GLY THR VAL GLN GLY THR LEU GLU          
SEQRES   7 A  307  SER LEU GLY ILE PRO TYR SER GLY SER ASN MSE LEU SER          
SEQRES   8 A  307  SER GLY ILE CYS MSE ASP LYS ASN ILE SER LYS LYS ILE          
SEQRES   9 A  307  LEU ARG TYR GLU GLY ILE GLU THR PRO ASP TRP ILE GLU          
SEQRES  10 A  307  LEU THR LYS MSE GLU ASP LEU ASN PHE ASP GLU LEU ASP          
SEQRES  11 A  307  LYS LEU GLY PHE PRO LEU VAL VAL LYS PRO ASN SER GLY          
SEQRES  12 A  307  GLY SER SER VAL GLY VAL LYS ILE VAL TYR ASP LYS ASP          
SEQRES  13 A  307  GLU LEU ILE SER MSE LEU GLU THR VAL PHE GLU TRP ASP          
SEQRES  14 A  307  SER GLU VAL VAL ILE GLU LYS TYR ILE LYS GLY GLU GLU          
SEQRES  15 A  307  ILE THR CYS SER ILE PHE ASP GLY LYS GLN LEU PRO ILE          
SEQRES  16 A  307  ILE SER ILE ARG HIS ALA ALA GLU PHE PHE ASP TYR ASN          
SEQRES  17 A  307  ALA LYS TYR ASP ASP ALA SER THR ILE GLU GLU VAL ILE          
SEQRES  18 A  307  GLU LEU PRO ALA GLU LEU LYS GLU ARG VAL ASN LYS ALA          
SEQRES  19 A  307  SER LEU ALA CYS TYR LYS ALA LEU LYS CYS SER VAL TYR          
SEQRES  20 A  307  ALA ARG VAL ASP MSE MSE VAL LYS ASP GLY ILE PRO TYR          
SEQRES  21 A  307  VAL MSE GLU VAL ASN THR LEU PRO GLY MSE THR GLN ALA          
SEQRES  22 A  307  SER LEU LEU PRO LYS SER ALA ASP ALA ALA GLY ILE HIS          
SEQRES  23 A  307  TYR SER LYS LEU LEU ASP MSE ILE ILE GLU THR SER LEU          
SEQRES  24 A  307  ARG VAL ARG LYS GLU GLU GLY PHE                              
SEQRES   1 B  307  SER ASN ALA MSE ARG ILE GLY VAL ILE MSE GLY GLY VAL          
SEQRES   2 B  307  SER SER GLU LYS GLN VAL SER ILE MSE THR GLY ASN GLU          
SEQRES   3 B  307  MSE ILE ALA ASN LEU ASP LYS ASN LYS TYR GLU ILE VAL          
SEQRES   4 B  307  PRO ILE THR LEU ASN GLU LYS MSE ASP LEU ILE GLU LYS          
SEQRES   5 B  307  ALA LYS ASP ILE ASP PHE ALA LEU LEU ALA LEU HIS GLY          
SEQRES   6 B  307  LYS TYR GLY GLU ASP GLY THR VAL GLN GLY THR LEU GLU          
SEQRES   7 B  307  SER LEU GLY ILE PRO TYR SER GLY SER ASN MSE LEU SER          
SEQRES   8 B  307  SER GLY ILE CYS MSE ASP LYS ASN ILE SER LYS LYS ILE          
SEQRES   9 B  307  LEU ARG TYR GLU GLY ILE GLU THR PRO ASP TRP ILE GLU          
SEQRES  10 B  307  LEU THR LYS MSE GLU ASP LEU ASN PHE ASP GLU LEU ASP          
SEQRES  11 B  307  LYS LEU GLY PHE PRO LEU VAL VAL LYS PRO ASN SER GLY          
SEQRES  12 B  307  GLY SER SER VAL GLY VAL LYS ILE VAL TYR ASP LYS ASP          
SEQRES  13 B  307  GLU LEU ILE SER MSE LEU GLU THR VAL PHE GLU TRP ASP          
SEQRES  14 B  307  SER GLU VAL VAL ILE GLU LYS TYR ILE LYS GLY GLU GLU          
SEQRES  15 B  307  ILE THR CYS SER ILE PHE ASP GLY LYS GLN LEU PRO ILE          
SEQRES  16 B  307  ILE SER ILE ARG HIS ALA ALA GLU PHE PHE ASP TYR ASN          
SEQRES  17 B  307  ALA LYS TYR ASP ASP ALA SER THR ILE GLU GLU VAL ILE          
SEQRES  18 B  307  GLU LEU PRO ALA GLU LEU LYS GLU ARG VAL ASN LYS ALA          
SEQRES  19 B  307  SER LEU ALA CYS TYR LYS ALA LEU LYS CYS SER VAL TYR          
SEQRES  20 B  307  ALA ARG VAL ASP MSE MSE VAL LYS ASP GLY ILE PRO TYR          
SEQRES  21 B  307  VAL MSE GLU VAL ASN THR LEU PRO GLY MSE THR GLN ALA          
SEQRES  22 B  307  SER LEU LEU PRO LYS SER ALA ASP ALA ALA GLY ILE HIS          
SEQRES  23 B  307  TYR SER LYS LEU LEU ASP MSE ILE ILE GLU THR SER LEU          
SEQRES  24 B  307  ARG VAL ARG LYS GLU GLU GLY PHE                              
SEQRES   1 C  307  SER ASN ALA MSE ARG ILE GLY VAL ILE MSE GLY GLY VAL          
SEQRES   2 C  307  SER SER GLU LYS GLN VAL SER ILE MSE THR GLY ASN GLU          
SEQRES   3 C  307  MSE ILE ALA ASN LEU ASP LYS ASN LYS TYR GLU ILE VAL          
SEQRES   4 C  307  PRO ILE THR LEU ASN GLU LYS MSE ASP LEU ILE GLU LYS          
SEQRES   5 C  307  ALA LYS ASP ILE ASP PHE ALA LEU LEU ALA LEU HIS GLY          
SEQRES   6 C  307  LYS TYR GLY GLU ASP GLY THR VAL GLN GLY THR LEU GLU          
SEQRES   7 C  307  SER LEU GLY ILE PRO TYR SER GLY SER ASN MSE LEU SER          
SEQRES   8 C  307  SER GLY ILE CYS MSE ASP LYS ASN ILE SER LYS LYS ILE          
SEQRES   9 C  307  LEU ARG TYR GLU GLY ILE GLU THR PRO ASP TRP ILE GLU          
SEQRES  10 C  307  LEU THR LYS MSE GLU ASP LEU ASN PHE ASP GLU LEU ASP          
SEQRES  11 C  307  LYS LEU GLY PHE PRO LEU VAL VAL LYS PRO ASN SER GLY          
SEQRES  12 C  307  GLY SER SER VAL GLY VAL LYS ILE VAL TYR ASP LYS ASP          
SEQRES  13 C  307  GLU LEU ILE SER MSE LEU GLU THR VAL PHE GLU TRP ASP          
SEQRES  14 C  307  SER GLU VAL VAL ILE GLU LYS TYR ILE LYS GLY GLU GLU          
SEQRES  15 C  307  ILE THR CYS SER ILE PHE ASP GLY LYS GLN LEU PRO ILE          
SEQRES  16 C  307  ILE SER ILE ARG HIS ALA ALA GLU PHE PHE ASP TYR ASN          
SEQRES  17 C  307  ALA LYS TYR ASP ASP ALA SER THR ILE GLU GLU VAL ILE          
SEQRES  18 C  307  GLU LEU PRO ALA GLU LEU LYS GLU ARG VAL ASN LYS ALA          
SEQRES  19 C  307  SER LEU ALA CYS TYR LYS ALA LEU LYS CYS SER VAL TYR          
SEQRES  20 C  307  ALA ARG VAL ASP MSE MSE VAL LYS ASP GLY ILE PRO TYR          
SEQRES  21 C  307  VAL MSE GLU VAL ASN THR LEU PRO GLY MSE THR GLN ALA          
SEQRES  22 C  307  SER LEU LEU PRO LYS SER ALA ASP ALA ALA GLY ILE HIS          
SEQRES  23 C  307  TYR SER LYS LEU LEU ASP MSE ILE ILE GLU THR SER LEU          
SEQRES  24 C  307  ARG VAL ARG LYS GLU GLU GLY PHE                              
SEQRES   1 D  307  SER ASN ALA MSE ARG ILE GLY VAL ILE MSE GLY GLY VAL          
SEQRES   2 D  307  SER SER GLU LYS GLN VAL SER ILE MSE THR GLY ASN GLU          
SEQRES   3 D  307  MSE ILE ALA ASN LEU ASP LYS ASN LYS TYR GLU ILE VAL          
SEQRES   4 D  307  PRO ILE THR LEU ASN GLU LYS MSE ASP LEU ILE GLU LYS          
SEQRES   5 D  307  ALA LYS ASP ILE ASP PHE ALA LEU LEU ALA LEU HIS GLY          
SEQRES   6 D  307  LYS TYR GLY GLU ASP GLY THR VAL GLN GLY THR LEU GLU          
SEQRES   7 D  307  SER LEU GLY ILE PRO TYR SER GLY SER ASN MSE LEU SER          
SEQRES   8 D  307  SER GLY ILE CYS MSE ASP LYS ASN ILE SER LYS LYS ILE          
SEQRES   9 D  307  LEU ARG TYR GLU GLY ILE GLU THR PRO ASP TRP ILE GLU          
SEQRES  10 D  307  LEU THR LYS MSE GLU ASP LEU ASN PHE ASP GLU LEU ASP          
SEQRES  11 D  307  LYS LEU GLY PHE PRO LEU VAL VAL LYS PRO ASN SER GLY          
SEQRES  12 D  307  GLY SER SER VAL GLY VAL LYS ILE VAL TYR ASP LYS ASP          
SEQRES  13 D  307  GLU LEU ILE SER MSE LEU GLU THR VAL PHE GLU TRP ASP          
SEQRES  14 D  307  SER GLU VAL VAL ILE GLU LYS TYR ILE LYS GLY GLU GLU          
SEQRES  15 D  307  ILE THR CYS SER ILE PHE ASP GLY LYS GLN LEU PRO ILE          
SEQRES  16 D  307  ILE SER ILE ARG HIS ALA ALA GLU PHE PHE ASP TYR ASN          
SEQRES  17 D  307  ALA LYS TYR ASP ASP ALA SER THR ILE GLU GLU VAL ILE          
SEQRES  18 D  307  GLU LEU PRO ALA GLU LEU LYS GLU ARG VAL ASN LYS ALA          
SEQRES  19 D  307  SER LEU ALA CYS TYR LYS ALA LEU LYS CYS SER VAL TYR          
SEQRES  20 D  307  ALA ARG VAL ASP MSE MSE VAL LYS ASP GLY ILE PRO TYR          
SEQRES  21 D  307  VAL MSE GLU VAL ASN THR LEU PRO GLY MSE THR GLN ALA          
SEQRES  22 D  307  SER LEU LEU PRO LYS SER ALA ASP ALA ALA GLY ILE HIS          
SEQRES  23 D  307  TYR SER LYS LEU LEU ASP MSE ILE ILE GLU THR SER LEU          
SEQRES  24 D  307  ARG VAL ARG LYS GLU GLU GLY PHE                              
MODRES 3R5X MSE A  313  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE A    7  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE A   19  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE A   24  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE A   44  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE A   86  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE A   93  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE A  118  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE A  158  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE A  249  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE A  250  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE A  259  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE A  267  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE A  290  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE B    7  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE B   19  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE B   24  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE B   44  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE B   86  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE B   93  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE B  118  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE B  158  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE B  249  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE B  250  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE B  259  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE B  267  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE B  290  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE C    1  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE C    7  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE C   19  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE C   24  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE C   44  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE C   86  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE C   93  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE C  118  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE C  158  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE C  249  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE C  250  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE C  259  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE C  267  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE C  290  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE D    1  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE D    7  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE D   19  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE D   24  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE D   44  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE D   86  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE D   93  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE D  118  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE D  158  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE D  249  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE D  250  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE D  259  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE D  267  MET  SELENOMETHIONINE                                   
MODRES 3R5X MSE D  290  MET  SELENOMETHIONINE                                   
HET    MSE  A 313       8                                                       
HET    MSE  A   7       8                                                       
HET    MSE  A  19       8                                                       
HET    MSE  A  24       8                                                       
HET    MSE  A  44       8                                                       
HET    MSE  A  86       8                                                       
HET    MSE  A  93       8                                                       
HET    MSE  A 118       8                                                       
HET    MSE  A 158       8                                                       
HET    MSE  A 249       8                                                       
HET    MSE  A 250       8                                                       
HET    MSE  A 259      16                                                       
HET    MSE  A 267       8                                                       
HET    MSE  A 290       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B   7       8                                                       
HET    MSE  B  19       8                                                       
HET    MSE  B  24       8                                                       
HET    MSE  B  44       8                                                       
HET    MSE  B  86       8                                                       
HET    MSE  B  93       8                                                       
HET    MSE  B 118       8                                                       
HET    MSE  B 158       8                                                       
HET    MSE  B 249       8                                                       
HET    MSE  B 250       8                                                       
HET    MSE  B 259      16                                                       
HET    MSE  B 267       8                                                       
HET    MSE  B 290       8                                                       
HET    MSE  C   1       8                                                       
HET    MSE  C   7       8                                                       
HET    MSE  C  19       8                                                       
HET    MSE  C  24       8                                                       
HET    MSE  C  44       8                                                       
HET    MSE  C  86      16                                                       
HET    MSE  C  93       8                                                       
HET    MSE  C 118       8                                                       
HET    MSE  C 158       8                                                       
HET    MSE  C 249       8                                                       
HET    MSE  C 250       8                                                       
HET    MSE  C 259      16                                                       
HET    MSE  C 267       8                                                       
HET    MSE  C 290       8                                                       
HET    MSE  D   1       8                                                       
HET    MSE  D   7       8                                                       
HET    MSE  D  19      16                                                       
HET    MSE  D  24       8                                                       
HET    MSE  D  44       8                                                       
HET    MSE  D  86      16                                                       
HET    MSE  D  93       8                                                       
HET    MSE  D 118       8                                                       
HET    MSE  D 158      16                                                       
HET    MSE  D 249       8                                                       
HET    MSE  D 250      16                                                       
HET    MSE  D 259       8                                                       
HET    MSE  D 267       8                                                       
HET    MSE  D 290       8                                                       
HET     CA  A 310       1                                                       
HET    ATP  A 311      31                                                       
HET     CA  B 310       1                                                       
HET    ATP  B 311      31                                                       
HET     CA  B 312       1                                                       
HET     CA  C 310       1                                                       
HET    ATP  C 311      31                                                       
HET     CA  C 312       1                                                       
HET     MG  C 313       1                                                       
HET     CA  D 310       1                                                       
HET    ATP  D 311      31                                                       
HET     CA  D 312       1                                                       
HET    EDO  D 313       4                                                       
HET    ACY  D 314       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CA CALCIUM ION                                                      
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     ACY ACETIC ACID                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  MSE    56(C5 H11 N O2 SE)                                           
FORMUL   5   CA    7(CA 2+)                                                     
FORMUL   6  ATP    4(C10 H16 N5 O13 P3)                                         
FORMUL  13   MG    MG 2+                                                        
FORMUL  17  EDO    C2 H6 O2                                                     
FORMUL  18  ACY    C2 H4 O2                                                     
FORMUL  19  HOH   *750(H2 O)                                                    
HELIX    1   1 VAL A   10  LEU A   28  1                                  19    
HELIX    2   2 GLU A   42  MSE A   44  5                                   3    
HELIX    3   3 ASP A   45  ALA A   50  1                                   6    
HELIX    4   4 GLY A   62  ASP A   67  1                                   6    
HELIX    5   5 GLY A   68  GLY A   78  1                                  11    
HELIX    6   6 ASN A   85  ASP A   94  1                                  10    
HELIX    7   7 ASP A   94  GLU A  105  1                                  12    
HELIX    8   8 ASN A  122  GLY A  130  1                                   9    
HELIX    9   9 ASP A  151  ASP A  166  1                                  16    
HELIX   10  10 PRO A  221  LEU A  239  1                                  19    
HELIX   11  11 SER A  271  ALA A  280  1                                  10    
HELIX   12  12 HIS A  283  GLY A  303  1                                  21    
HELIX   13  13 VAL B   10  LEU B   28  1                                  19    
HELIX   14  14 GLU B   42  MSE B   44  5                                   3    
HELIX   15  15 ASP B   45  ALA B   50  1                                   6    
HELIX   16  16 LYS B   51  ILE B   53  5                                   3    
HELIX   17  17 GLY B   62  ASP B   67  1                                   6    
HELIX   18  18 GLY B   68  LEU B   77  1                                  10    
HELIX   19  19 ASN B   85  ASP B   94  1                                  10    
HELIX   20  20 ASP B   94  GLU B  105  1                                  12    
HELIX   21  21 ASN B  122  GLY B  130  1                                   9    
HELIX   22  22 ASP B  151  ASP B  166  1                                  16    
HELIX   23  23 PRO B  221  LEU B  239  1                                  19    
HELIX   24  24 SER B  271  ALA B  280  1                                  10    
HELIX   25  25 HIS B  283  GLY B  303  1                                  21    
HELIX   26  26 VAL C   10  LEU C   28  1                                  19    
HELIX   27  27 GLU C   42  MSE C   44  5                                   3    
HELIX   28  28 ASP C   45  ALA C   50  1                                   6    
HELIX   29  29 LYS C   51  ILE C   53  5                                   3    
HELIX   30  30 GLY C   62  ASP C   67  1                                   6    
HELIX   31  31 GLY C   68  LEU C   77  1                                  10    
HELIX   32  32 ASN C   85  ASP C   94  1                                  10    
HELIX   33  33 ASP C   94  GLU C  105  1                                  12    
HELIX   34  34 ASN C  122  GLY C  130  1                                   9    
HELIX   35  35 ASP C  151  ASP C  166  1                                  16    
HELIX   36  36 PRO C  221  LEU C  239  1                                  19    
HELIX   37  37 SER C  271  ALA C  280  1                                  10    
HELIX   38  38 HIS C  283  GLU C  302  1                                  20    
HELIX   39  39 VAL D   10  LEU D   28  1                                  19    
HELIX   40  40 GLU D   42  MSE D   44  5                                   3    
HELIX   41  41 ASP D   45  ALA D   50  1                                   6    
HELIX   42  42 GLY D   62  ASP D   67  1                                   6    
HELIX   43  43 GLY D   68  LEU D   77  1                                  10    
HELIX   44  44 ASN D   85  ASP D   94  1                                  10    
HELIX   45  45 ASP D   94  GLU D  105  1                                  12    
HELIX   46  46 ASN D  122  GLY D  130  1                                   9    
HELIX   47  47 ASP D  151  ASP D  166  1                                  16    
HELIX   48  48 ALA D  198  PHE D  202  5                                   5    
HELIX   49  49 PRO D  221  LEU D  239  1                                  19    
HELIX   50  50 SER D  271  ALA D  280  1                                  10    
HELIX   51  51 HIS D  283  GLU D  302  1                                  20    
SHEET    1   A 3 TYR A  33  THR A  39  0                                        
SHEET    2   A 3 MSE A 313  MSE A   7  1  N  MSE A   7   O  ILE A  38           
SHEET    3   A 3 PHE A  55  LEU A  58  1  O  PHE A  55   N  GLY A   4           
SHEET    1   B 4 TRP A 112  THR A 116  0                                        
SHEET    2   B 4 GLU A 168  LYS A 173 -1  O  ILE A 171   N  ILE A 113           
SHEET    3   B 4 LEU A 133  PRO A 137 -1  N  LYS A 136   O  VAL A 170           
SHEET    4   B 4 LYS A 147  VAL A 149 -1  O  LYS A 147   N  VAL A 135           
SHEET    1   C 4 LYS A 188  GLN A 189  0                                        
SHEET    2   C 4 GLU A 178  PHE A 185 -1  N  PHE A 185   O  LYS A 188           
SHEET    3   C 4 ILE A 193  PHE A 202 -1  O  ILE A 195   N  GLU A 179           
SHEET    4   C 4 ASN A 205  VAL A 217 -1  O  ILE A 214   N  ARG A 196           
SHEET    1   D 4 LYS A 188  GLN A 189  0                                        
SHEET    2   D 4 GLU A 178  PHE A 185 -1  N  PHE A 185   O  LYS A 188           
SHEET    3   D 4 TYR A 244  LYS A 252 -1  O  VAL A 251   N  GLU A 178           
SHEET    4   D 4 ILE A 255  ASN A 262 -1  O  ASN A 262   N  ARG A 246           
SHEET    1   E 3 TYR B  33  THR B  39  0                                        
SHEET    2   E 3 MSE B   1  MSE B   7  1  N  ILE B   3   O  VAL B  36           
SHEET    3   E 3 PHE B  55  LEU B  58  1  O  LEU B  57   N  GLY B   4           
SHEET    1   F 4 TRP B 112  THR B 116  0                                        
SHEET    2   F 4 GLU B 168  LYS B 173 -1  O  VAL B 169   N  LEU B 115           
SHEET    3   F 4 LEU B 133  PRO B 137 -1  N  VAL B 134   O  GLU B 172           
SHEET    4   F 4 ILE B 148  VAL B 149 -1  O  VAL B 149   N  LEU B 133           
SHEET    1   G 4 LYS B 188  GLN B 189  0                                        
SHEET    2   G 4 GLU B 178  PHE B 185 -1  N  PHE B 185   O  LYS B 188           
SHEET    3   G 4 ILE B 193  HIS B 197 -1  O  ILE B 195   N  GLU B 179           
SHEET    4   G 4 THR B 213  VAL B 217 -1  O  GLU B 216   N  SER B 194           
SHEET    1   H 4 LYS B 188  GLN B 189  0                                        
SHEET    2   H 4 GLU B 178  PHE B 185 -1  N  PHE B 185   O  LYS B 188           
SHEET    3   H 4 TYR B 244  LYS B 252 -1  O  VAL B 247   N  CYS B 182           
SHEET    4   H 4 ILE B 255  ASN B 262 -1  O  ASN B 262   N  ARG B 246           
SHEET    1   I 3 TYR C  33  LEU C  40  0                                        
SHEET    2   I 3 MSE C   1  GLY C   8  1  N  MSE C   7   O  ILE C  38           
SHEET    3   I 3 PHE C  55  LEU C  58  1  O  LEU C  57   N  GLY C   4           
SHEET    1   J 4 TRP C 112  THR C 116  0                                        
SHEET    2   J 4 GLU C 168  LYS C 173 -1  O  ILE C 171   N  ILE C 113           
SHEET    3   J 4 LEU C 133  PRO C 137 -1  N  LYS C 136   O  VAL C 170           
SHEET    4   J 4 LYS C 147  VAL C 149 -1  O  VAL C 149   N  LEU C 133           
SHEET    1   K 4 LYS C 188  GLN C 189  0                                        
SHEET    2   K 4 GLU C 178  PHE C 185 -1  N  PHE C 185   O  LYS C 188           
SHEET    3   K 4 ILE C 193  ARG C 196 -1  O  ILE C 195   N  GLU C 179           
SHEET    4   K 4 ILE C 214  VAL C 217 -1  O  GLU C 216   N  SER C 194           
SHEET    1   L 4 LYS C 188  GLN C 189  0                                        
SHEET    2   L 4 GLU C 178  PHE C 185 -1  N  PHE C 185   O  LYS C 188           
SHEET    3   L 4 TYR C 244  LYS C 252 -1  O  ALA C 245   N  ILE C 184           
SHEET    4   L 4 ILE C 255  ASN C 262 -1  O  ASN C 262   N  ARG C 246           
SHEET    1   M 3 TYR D  33  LEU D  40  0                                        
SHEET    2   M 3 MSE D   1  GLY D   8  1  N  MSE D   7   O  LEU D  40           
SHEET    3   M 3 PHE D  55  LEU D  58  1  O  LEU D  57   N  GLY D   4           
SHEET    1   N 4 TRP D 112  THR D 116  0                                        
SHEET    2   N 4 GLU D 168  LYS D 173 -1  O  VAL D 169   N  LEU D 115           
SHEET    3   N 4 LEU D 133  PRO D 137 -1  N  LYS D 136   O  VAL D 170           
SHEET    4   N 4 LYS D 147  VAL D 149 -1  O  VAL D 149   N  LEU D 133           
SHEET    1   O 4 LYS D 188  GLN D 189  0                                        
SHEET    2   O 4 GLU D 178  PHE D 185 -1  N  PHE D 185   O  LYS D 188           
SHEET    3   O 4 ILE D 193  ARG D 196 -1  O  ILE D 193   N  THR D 181           
SHEET    4   O 4 ILE D 214  VAL D 217 -1  O  GLU D 216   N  SER D 194           
SHEET    1   P 4 LYS D 188  GLN D 189  0                                        
SHEET    2   P 4 GLU D 178  PHE D 185 -1  N  PHE D 185   O  LYS D 188           
SHEET    3   P 4 TYR D 244  LYS D 252 -1  O  VAL D 247   N  CYS D 182           
SHEET    4   P 4 ILE D 255  ASN D 262 -1  O  ASN D 262   N  ARG D 246           
LINK         C   ALA A   0                 N   MSE A 313     1555   1555  1.33  
LINK         C   MSE A 313                 N   ARG A   2     1555   1555  1.33  
LINK         C   ILE A   6                 N   MSE A   7     1555   1555  1.33  
LINK         C   MSE A   7                 N   GLY A   8     1555   1555  1.33  
LINK         C   ILE A  18                 N   MSE A  19     1555   1555  1.33  
LINK         C   MSE A  19                 N   THR A  20     1555   1555  1.33  
LINK         C   GLU A  23                 N   MSE A  24     1555   1555  1.33  
LINK         C   MSE A  24                 N   ILE A  25     1555   1555  1.32  
LINK         C   LYS A  43                 N   MSE A  44     1555   1555  1.32  
LINK         C   MSE A  44                 N   ASP A  45     1555   1555  1.34  
LINK         C   ASN A  85                 N   MSE A  86     1555   1555  1.34  
LINK         C   MSE A  86                 N   LEU A  87     1555   1555  1.33  
LINK         C   CYS A  92                 N   MSE A  93     1555   1555  1.32  
LINK         C   MSE A  93                 N   ASP A  94     1555   1555  1.32  
LINK         C   LYS A 117                 N   MSE A 118     1555   1555  1.33  
LINK         C   MSE A 118                 N   GLU A 119     1555   1555  1.32  
LINK         C   SER A 157                 N   MSE A 158     1555   1555  1.33  
LINK         C   MSE A 158                 N   LEU A 159     1555   1555  1.33  
LINK         C   ASP A 248                 N   MSE A 249     1555   1555  1.34  
LINK         C   MSE A 249                 N   MSE A 250     1555   1555  1.33  
LINK         C   MSE A 250                 N   VAL A 251     1555   1555  1.34  
LINK         C   VAL A 258                 N  AMSE A 259     1555   1555  1.33  
LINK         C   VAL A 258                 N  BMSE A 259     1555   1555  1.33  
LINK         C  AMSE A 259                 N   GLU A 260     1555   1555  1.33  
LINK         C  BMSE A 259                 N   GLU A 260     1555   1555  1.33  
LINK         C   GLY A 266                 N   MSE A 267     1555   1555  1.32  
LINK         C   MSE A 267                 N   THR A 268     1555   1555  1.32  
LINK         C   ASP A 289                 N   MSE A 290     1555   1555  1.33  
LINK         C   MSE A 290                 N   ILE A 291     1555   1555  1.33  
LINK         C   ALA B   0                 N   MSE B   1     1555   1555  1.33  
LINK         C   MSE B   1                 N   ARG B   2     1555   1555  1.33  
LINK         C   ILE B   6                 N   MSE B   7     1555   1555  1.32  
LINK         C   MSE B   7                 N   GLY B   8     1555   1555  1.33  
LINK         C   ILE B  18                 N   MSE B  19     1555   1555  1.33  
LINK         C   MSE B  19                 N   THR B  20     1555   1555  1.33  
LINK         C   GLU B  23                 N   MSE B  24     1555   1555  1.33  
LINK         C   MSE B  24                 N   ILE B  25     1555   1555  1.33  
LINK         C   LYS B  43                 N   MSE B  44     1555   1555  1.33  
LINK         C   MSE B  44                 N   ASP B  45     1555   1555  1.33  
LINK         C   ASN B  85                 N   MSE B  86     1555   1555  1.33  
LINK         C   MSE B  86                 N   LEU B  87     1555   1555  1.33  
LINK         C   CYS B  92                 N   MSE B  93     1555   1555  1.32  
LINK         C   MSE B  93                 N   ASP B  94     1555   1555  1.33  
LINK         C   LYS B 117                 N   MSE B 118     1555   1555  1.33  
LINK         C   MSE B 118                 N   GLU B 119     1555   1555  1.33  
LINK         C   SER B 157                 N   MSE B 158     1555   1555  1.33  
LINK         C   MSE B 158                 N   LEU B 159     1555   1555  1.32  
LINK         C   ASP B 248                 N   MSE B 249     1555   1555  1.33  
LINK         C   MSE B 249                 N   MSE B 250     1555   1555  1.33  
LINK         C   MSE B 250                 N   VAL B 251     1555   1555  1.33  
LINK         C   VAL B 258                 N  AMSE B 259     1555   1555  1.33  
LINK         C   VAL B 258                 N  BMSE B 259     1555   1555  1.33  
LINK         C  AMSE B 259                 N   GLU B 260     1555   1555  1.33  
LINK         C  BMSE B 259                 N   GLU B 260     1555   1555  1.33  
LINK         C   GLY B 266                 N   MSE B 267     1555   1555  1.32  
LINK         C   MSE B 267                 N   THR B 268     1555   1555  1.33  
LINK         C   ASP B 289                 N   MSE B 290     1555   1555  1.34  
LINK         C   MSE B 290                 N   ILE B 291     1555   1555  1.33  
LINK         C   ALA C   0                 N   MSE C   1     1555   1555  1.33  
LINK         C   MSE C   1                 N   ARG C   2     1555   1555  1.33  
LINK         C   ILE C   6                 N   MSE C   7     1555   1555  1.32  
LINK         C   MSE C   7                 N   GLY C   8     1555   1555  1.33  
LINK         C   ILE C  18                 N   MSE C  19     1555   1555  1.33  
LINK         C   MSE C  19                 N   THR C  20     1555   1555  1.33  
LINK         C   GLU C  23                 N   MSE C  24     1555   1555  1.34  
LINK         C   MSE C  24                 N   ILE C  25     1555   1555  1.32  
LINK         C   LYS C  43                 N   MSE C  44     1555   1555  1.34  
LINK         C   MSE C  44                 N   ASP C  45     1555   1555  1.32  
LINK         C   ASN C  85                 N  AMSE C  86     1555   1555  1.33  
LINK         C   ASN C  85                 N  BMSE C  86     1555   1555  1.33  
LINK         C  AMSE C  86                 N   LEU C  87     1555   1555  1.33  
LINK         C  BMSE C  86                 N   LEU C  87     1555   1555  1.33  
LINK         C   CYS C  92                 N   MSE C  93     1555   1555  1.33  
LINK         C   MSE C  93                 N   ASP C  94     1555   1555  1.34  
LINK         C   LYS C 117                 N   MSE C 118     1555   1555  1.33  
LINK         C   MSE C 118                 N   GLU C 119     1555   1555  1.33  
LINK         C   SER C 157                 N   MSE C 158     1555   1555  1.33  
LINK         C   MSE C 158                 N   LEU C 159     1555   1555  1.32  
LINK         C   ASP C 248                 N   MSE C 249     1555   1555  1.33  
LINK         C   MSE C 249                 N   MSE C 250     1555   1555  1.33  
LINK         C   MSE C 250                 N   VAL C 251     1555   1555  1.33  
LINK         C   VAL C 258                 N  AMSE C 259     1555   1555  1.33  
LINK         C   VAL C 258                 N  BMSE C 259     1555   1555  1.34  
LINK         C  AMSE C 259                 N   GLU C 260     1555   1555  1.33  
LINK         C  BMSE C 259                 N   GLU C 260     1555   1555  1.33  
LINK         C   GLY C 266                 N   MSE C 267     1555   1555  1.32  
LINK         C   MSE C 267                 N   THR C 268     1555   1555  1.32  
LINK         C   ASP C 289                 N   MSE C 290     1555   1555  1.33  
LINK         C   MSE C 290                 N   ILE C 291     1555   1555  1.34  
LINK         C   ALA D   0                 N   MSE D   1     1555   1555  1.32  
LINK         C   MSE D   1                 N   ARG D   2     1555   1555  1.33  
LINK         C   ILE D   6                 N   MSE D   7     1555   1555  1.33  
LINK         C   MSE D   7                 N   GLY D   8     1555   1555  1.33  
LINK         C   ILE D  18                 N  AMSE D  19     1555   1555  1.34  
LINK         C   ILE D  18                 N  BMSE D  19     1555   1555  1.33  
LINK         C  AMSE D  19                 N   THR D  20     1555   1555  1.33  
LINK         C  BMSE D  19                 N   THR D  20     1555   1555  1.33  
LINK         C   GLU D  23                 N   MSE D  24     1555   1555  1.33  
LINK         C   MSE D  24                 N   ILE D  25     1555   1555  1.32  
LINK         C   LYS D  43                 N   MSE D  44     1555   1555  1.33  
LINK         C   MSE D  44                 N   ASP D  45     1555   1555  1.34  
LINK         C   ASN D  85                 N  AMSE D  86     1555   1555  1.33  
LINK         C   ASN D  85                 N  BMSE D  86     1555   1555  1.33  
LINK         C  AMSE D  86                 N   LEU D  87     1555   1555  1.32  
LINK         C  BMSE D  86                 N   LEU D  87     1555   1555  1.33  
LINK         C   CYS D  92                 N   MSE D  93     1555   1555  1.33  
LINK         C   MSE D  93                 N   ASP D  94     1555   1555  1.34  
LINK         C   LYS D 117                 N   MSE D 118     1555   1555  1.33  
LINK         C   MSE D 118                 N   GLU D 119     1555   1555  1.33  
LINK         C   SER D 157                 N  AMSE D 158     1555   1555  1.33  
LINK         C   SER D 157                 N  BMSE D 158     1555   1555  1.33  
LINK         C  AMSE D 158                 N   LEU D 159     1555   1555  1.33  
LINK         C  BMSE D 158                 N   LEU D 159     1555   1555  1.34  
LINK         C   ASP D 248                 N   MSE D 249     1555   1555  1.33  
LINK         C   MSE D 249                 N  AMSE D 250     1555   1555  1.33  
LINK         C   MSE D 249                 N  BMSE D 250     1555   1555  1.33  
LINK         C  AMSE D 250                 N   VAL D 251     1555   1555  1.33  
LINK         C  BMSE D 250                 N   VAL D 251     1555   1555  1.33  
LINK         C   VAL D 258                 N   MSE D 259     1555   1555  1.33  
LINK         C   MSE D 259                 N   GLU D 260     1555   1555  1.33  
LINK         C   GLY D 266                 N   MSE D 267     1555   1555  1.32  
LINK         C   MSE D 267                 N   THR D 268     1555   1555  1.33  
LINK         C   ASP D 289                 N   MSE D 290     1555   1555  1.33  
LINK         C   MSE D 290                 N   ILE D 291     1555   1555  1.33  
LINK        CA    CA A 310                 O2B ATP A 311     1555   1555  2.10  
LINK         OE2 GLU A 260                CA    CA A 310     1555   1555  2.15  
LINK        CA    CA A 310                 O2A ATP A 311     1555   1555  2.16  
LINK         OD2 ASP A 248                CA    CA A 310     1555   1555  2.19  
LINK         O   ARG C 299                MG    MG C 313     1555   1555  2.29  
LINK        CA    CA D 310                 O3A ATP D 311     1555   1555  2.30  
LINK         OD2 ASP D 248                CA    CA D 310     1555   1555  2.32  
LINK        CA    CA D 310                 O   HOH D 528     1555   1555  2.34  
LINK         OE2 GLU B 260                CA    CA B 310     1555   1555  2.38  
LINK        CA    CA D 312                 O   HOH D 542     1555   1555  2.42  
LINK         OD2 ASP B 248                CA    CA B 310     1555   1555  2.44  
LINK         OE2 GLU D 260                CA    CA D 310     1555   1555  2.46  
LINK         O   TYR D 208                CA    CA D 312     1555   1555  2.48  
LINK         OE1 GLU C 108                CA    CA C 312     1555   1555  2.53  
LINK         OD2 ASP C 248                CA    CA C 310     1555   1555  2.55  
LINK         OE1 GLU D 200                CA    CA D 312     1555   1555  2.55  
LINK         O   GLU C 302                MG    MG C 313     1555   1555  2.56  
LINK         OD2AASP D 203                CA    CA D 312     1555   1555  2.58  
LINK         OE2 GLU D 200                CA    CA D 312     1555   1555  2.59  
LINK         OE2 GLU C 108                CA    CA C 312     1555   1555  2.64  
LINK        CA    CA C 312                 O   HOH C 642     1555   1555  2.64  
LINK        MG    MG C 313                 O   HOH C 667     1555   1555  2.64  
LINK         O   GLY B 281                CA    CA B 312     1555   1555  2.64  
LINK        CA    CA D 312                 O   HOH D 543     1555   1555  2.65  
LINK        MG    MG C 313                 O   HOH C 668     1555   1555  2.67  
LINK        CA    CA B 312                 O   HOH B 626     1555   1555  2.71  
LINK        CA    CA B 312                 O   HOH B 628     1555   1555  2.72  
LINK        CA    CA C 310                 O   HOH C 536     1555   1555  2.72  
LINK         OE1 GLU C 260                CA    CA C 310     1555   1555  2.73  
LINK        CA    CA C 310                 O1A ATP C 311     1555   1555  2.78  
LINK        CA    CA C 310                 O2B ATP C 311     1555   1555  2.78  
LINK        CA    CA B 312                 O   HOH B 627     1555   1555  2.79  
LINK        MG    MG C 313                 O   HOH C 669     1555   1555  2.80  
LINK         OD2BASP D 203                CA    CA D 312     1555   1555  2.87  
LINK        CA    CA A 310                 O   HOH A 689     1555   1555  3.00  
LINK        CA    CA B 312                 O   HOH B 630     1555   1555  3.01  
LINK        CA    CA D 310                 O3B ATP D 311     1555   1555  3.03  
CISPEP   1 PHE A  131    PRO A  132          0        -3.74                     
CISPEP   2 PHE B  131    PRO B  132          0        -6.14                     
CISPEP   3 PHE C  131    PRO C  132          0        -4.01                     
CISPEP   4 PHE D  131    PRO D  132          0        -3.27                     
SITE     1 AC1  4 ASP A 248  GLU A 260  ATP A 311  HOH A 689                    
SITE     1 AC2 18 LYS A  95  VAL A 134  LYS A 136  VAL A 146                    
SITE     2 AC2 18 GLU A 172  LYS A 173  TYR A 174  ILE A 175                    
SITE     3 AC2 18 GLU A 179  MSE A 259  GLU A 260  ASN A 262                    
SITE     4 AC2 18  CA A 310  HOH A 383  HOH A 408  HOH A 645                    
SITE     5 AC2 18 HOH A 646  HOH A 689                                          
SITE     1 AC3  3 ASP B 248  GLU B 260  ATP B 311                               
SITE     1 AC4 17 GLU B  66  LYS B  95  VAL B 134  LYS B 136                    
SITE     2 AC4 17 GLY B 145  VAL B 146  GLU B 172  LYS B 173                    
SITE     3 AC4 17 TYR B 174  ILE B 175  GLU B 179  MSE B 250                    
SITE     4 AC4 17 MSE B 259  GLU B 260  ASN B 262   CA B 310                    
SITE     5 AC4 17 HOH B 742                                                     
SITE     1 AC5  7 ASN A  31  HOH A 629  GLY B 281  HOH B 626                    
SITE     2 AC5  7 HOH B 627  HOH B 628  HOH B 630                               
SITE     1 AC6  5 ARG C 246  ASP C 248  GLU C 260  ATP C 311                    
SITE     2 AC6  5 HOH C 536                                                     
SITE     1 AC7 16 LYS C  63  LYS C  95  VAL C 134  LYS C 136                    
SITE     2 AC7 16 VAL C 146  GLU C 172  LYS C 173  TYR C 174                    
SITE     3 AC7 16 ILE C 175  GLU C 179  MSE C 250  MSE C 259                    
SITE     4 AC7 16 GLU C 260   CA C 310  HOH C 536  HOH C 538                    
SITE     1 AC8  5 PHE A 131  HOH A 439  HOH A 641  GLU C 108                    
SITE     2 AC8  5 HOH C 642                                                     
SITE     1 AC9  5 ARG C 299  GLU C 302  HOH C 667  HOH C 668                    
SITE     2 AC9  5 HOH C 669                                                     
SITE     1 BC1  6 ASP A 203  HOH A 335  ASP D 248  GLU D 260                    
SITE     2 BC1  6 ATP D 311  HOH D 528                                          
SITE     1 BC2 26 PHE A 201  ASP A 203  HOH A 335  HOH A 379                    
SITE     2 BC2 26 HOH A 545  LYS D  95  VAL D 134  LYS D 136                    
SITE     3 BC2 26 VAL D 146  GLU D 172  LYS D 173  TYR D 174                    
SITE     4 BC2 26 ILE D 175  GLU D 179  MSE D 250  MSE D 259                    
SITE     5 BC2 26 GLU D 260  ASN D 262   CA D 310  HOH D 336                    
SITE     6 BC2 26 HOH D 424  HOH D 434  HOH D 528  HOH D 567                    
SITE     7 BC2 26 HOH D 621  HOH D 671                                          
SITE     1 BC3  6 ASP A 253  GLU D 200  ASP D 203  TYR D 208                    
SITE     2 BC3  6 HOH D 542  HOH D 543                                          
SITE     1 BC4  5 GLU D  75  ARG D 299  GLU D 302  PHE D 304                    
SITE     2 BC4  5 HOH D 747                                                     
SITE     1 BC5  2 ASP D 111  HOH D 432                                          
CRYST1   56.336   68.992   92.387  73.36  84.96  75.46 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017751 -0.004603 -0.000316        0.00000                         
SCALE2      0.000000  0.014974 -0.004268        0.00000                         
SCALE3      0.000000  0.000000  0.011299        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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