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Database: PDB
Entry: 6DGI
LinkDB: 6DGI
Original site: 6DGI 
HEADER    LIGASE                                  17-MAY-18   6DGI              
TITLE     THE CRYSTAL STRUCTURE OF D-ALANYL-ALANINE SYNTHETASE A FROM VIBRIO    
TITLE    2 CHOLERAE O1 BIOVAR ELTOR STR. N16961                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;                               
COMPND   3 CHAIN: A, B;                                                         
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: VIBRIO CHOLERAE SEROTYPE O1 (STRAIN ATCC 39315  
SOURCE   3 / EL TOR INABA N16961);                                              
SOURCE   4 ORGANISM_TAXID: 243277;                                              
SOURCE   5 STRAIN: ATCC 39315 / EL TOR INABA N16961;                            
SOURCE   6 GENE: DDL, VC_A0572;                                                 
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-PLYSS;                           
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMCSG19C                                  
KEYWDS    STRUCTURAL GENOMICS, THE CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS 
KEYWDS   2 DISEASES, CSGID, LIGASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.TAN,M.ZHOU,A.JOACHIMIAK,CENTER FOR STRUCTURAL GENOMICS OF           
AUTHOR   2 INFECTIOUS DISEASES (CSGID)                                          
REVDAT   2   18-DEC-19 6DGI    1       REMARK                                   
REVDAT   1   30-MAY-18 6DGI    0                                                
JRNL        AUTH   K.TAN,M.ZHOU,A.JOACHIMIAK                                    
JRNL        TITL   THE CRYSTAL STRUCTURE OF D-ALANYL-ALANINE SYNTHETASE A FROM  
JRNL        TITL 2 VIBRIO CHOLERAE O1 BIOVAR ELTOR STR. N16961                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.79                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 30054                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.750                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1429                            
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 43.7946 -  4.9531    0.94     2942   169  0.1582 0.2082        
REMARK   3     2  4.9531 -  3.9323    0.97     2939   129  0.1380 0.1801        
REMARK   3     3  3.9323 -  3.4354    0.97     2923   135  0.1624 0.1934        
REMARK   3     4  3.4354 -  3.1214    0.97     2874   151  0.1904 0.2009        
REMARK   3     5  3.1214 -  2.8977    0.98     2875   140  0.2027 0.2342        
REMARK   3     6  2.8977 -  2.7269    0.98     2890   136  0.2112 0.2487        
REMARK   3     7  2.7269 -  2.5904    0.98     2843   153  0.2075 0.2551        
REMARK   3     8  2.5904 -  2.4776    0.97     2822   150  0.2101 0.2732        
REMARK   3     9  2.4776 -  2.3822    0.95     2782   140  0.2092 0.2833        
REMARK   3    10  2.3822 -  2.3000    0.93     2735   126  0.2037 0.2698        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.860           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.35                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           5324                                  
REMARK   3   ANGLE     :  0.632           7221                                  
REMARK   3   CHIRALITY :  0.044            803                                  
REMARK   3   PLANARITY :  0.004            929                                  
REMARK   3   DIHEDRAL  :  6.717           4376                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 116 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  45.8614   2.3254   4.3186              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4471 T22:   0.3348                                     
REMARK   3      T33:   0.2117 T12:  -0.1014                                     
REMARK   3      T13:  -0.1201 T23:   0.0639                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4001 L22:   0.5803                                     
REMARK   3      L33:   1.9540 L12:  -0.5370                                     
REMARK   3      L13:  -0.3589 L23:   0.5121                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0601 S12:   0.2581 S13:  -0.0384                       
REMARK   3      S21:  -0.4494 S22:   0.0371 S23:   0.2082                       
REMARK   3      S31:   0.1216 S32:  -0.2973 S33:  -0.0628                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 117 THROUGH 233 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  39.2382  10.4748  31.7834              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1378 T22:   0.1675                                     
REMARK   3      T33:   0.3127 T12:  -0.0255                                     
REMARK   3      T13:  -0.0166 T23:   0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8961 L22:   1.1326                                     
REMARK   3      L33:   1.0045 L12:  -0.0899                                     
REMARK   3      L13:  -0.2765 L23:  -0.2099                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0819 S12:  -0.0876 S13:   0.0638                       
REMARK   3      S21:   0.0511 S22:   0.0799 S23:   0.1966                       
REMARK   3      S31:   0.0393 S32:  -0.1077 S33:   0.0156                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 234 THROUGH 254 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.2296  14.4064  20.0290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3458 T22:   0.5079                                     
REMARK   3      T33:   0.6333 T12:   0.0611                                     
REMARK   3      T13:   0.0533 T23:   0.1628                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0574 L22:   7.0615                                     
REMARK   3      L33:   0.4597 L12:   2.5383                                     
REMARK   3      L13:  -0.6647 L23:  -0.0202                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0489 S12:   0.3728 S13:   0.5195                       
REMARK   3      S21:  -0.1686 S22:   0.1461 S23:   0.5457                       
REMARK   3      S31:   0.2362 S32:  -0.2397 S33:   0.0458                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 255 THROUGH 332 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  41.3805  20.6404  15.8255              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3141 T22:   0.2297                                     
REMARK   3      T33:   0.3731 T12:  -0.0099                                     
REMARK   3      T13:  -0.0944 T23:   0.1489                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2759 L22:   2.1991                                     
REMARK   3      L33:   2.5198 L12:  -0.1951                                     
REMARK   3      L13:  -0.4770 L23:   0.7546                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1423 S12:   0.2802 S13:   0.5342                       
REMARK   3      S21:  -0.5980 S22:   0.1505 S23:   0.4055                       
REMARK   3      S31:  -0.3381 S32:  -0.2450 S33:  -0.1865                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 155 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  64.6911  -2.0036  18.3063              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2127 T22:   0.1905                                     
REMARK   3      T33:   0.1364 T12:  -0.0033                                     
REMARK   3      T13:   0.0052 T23:   0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2225 L22:   1.2221                                     
REMARK   3      L33:   1.9808 L12:   0.2214                                     
REMARK   3      L13:   0.2040 L23:   0.3454                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0360 S12:   0.2697 S13:  -0.0239                       
REMARK   3      S21:  -0.3167 S22:   0.0233 S23:  -0.0255                       
REMARK   3      S31:   0.2212 S32:   0.0386 S33:  -0.0104                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 156 THROUGH 254 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  76.3304   9.1534  29.7644              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1859 T22:   0.2370                                     
REMARK   3      T33:   0.2785 T12:  -0.0363                                     
REMARK   3      T13:  -0.0358 T23:   0.0289                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9089 L22:   0.1401                                     
REMARK   3      L33:   0.6783 L12:  -0.1464                                     
REMARK   3      L13:  -0.2269 L23:  -0.2427                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0081 S12:   0.0237 S13:   0.1351                       
REMARK   3      S21:  -0.0117 S22:  -0.0622 S23:  -0.2301                       
REMARK   3      S31:  -0.0634 S32:   0.2228 S33:   0.0719                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 255 THROUGH 333 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  68.6727  -4.0816  34.6198              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1373 T22:   0.1156                                     
REMARK   3      T33:   0.1393 T12:  -0.0036                                     
REMARK   3      T13:   0.0350 T23:   0.0434                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8845 L22:   3.7740                                     
REMARK   3      L33:   3.2579 L12:  -0.1622                                     
REMARK   3      L13:   0.8963 L23:   1.7090                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0200 S12:   0.0231 S13:  -0.0011                       
REMARK   3      S21:   0.0092 S22:   0.0052 S23:  -0.0902                       
REMARK   3      S31:   0.2238 S32:   0.0548 S33:   0.0116                       
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 6DGI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000234580.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUL-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.9                                
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) : 0.97924                            
REMARK 200  MONOCHROMATOR                  : SI 111 CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
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   : 30876                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.70000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.510                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: HKL-3000                                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM FORMAT, 20% W/V           
REMARK 280  PEG3350, PH 5.9, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       31.79400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.58000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.43750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.58000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.79400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.43750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       63.58800            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     ALA A   333                                                      
REMARK 465     LYS A   334                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     ALA B   240                                                      
REMARK 465     ASN B   241                                                      
REMARK 465     SER B   242                                                      
REMARK 465     HIS B   243                                                      
REMARK 465     ALA B   244                                                      
REMARK 465     LYS B   334                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  36    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  46    CE   NZ                                             
REMARK 470     LYS A 220    NZ                                                  
REMARK 470     ASN A 241    CG   OD1  ND2                                       
REMARK 470     GLU A 251    CD   OE1  OE2                                       
REMARK 470     LYS B  46    CE   NZ                                             
REMARK 470     GLU B 109    OE1  OE2                                            
REMARK 470     LYS B 147    CE   NZ                                             
REMARK 470     GLU B 185    CD   OE1  OE2                                       
REMARK 470     LYS B 201    CE   NZ                                             
REMARK 470     SER B 239    OG                                                  
REMARK 470     ARG B 245    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 287    OE1  OE2                                            
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 167     -153.36   -115.18                                   
REMARK 500    HIS A 276      -56.10     74.75                                   
REMARK 500    SER A 278      146.45   -175.89                                   
REMARK 500    ASN A 293      -66.17    -97.52                                   
REMARK 500    VAL A 331      -65.58    -90.09                                   
REMARK 500    SER B 167     -142.05     52.11                                   
REMARK 500    MSE B 212      143.63   -174.61                                   
REMARK 500    HIS B 276      -55.67     69.56                                   
REMARK 500    SER B 278      148.71   -173.51                                   
REMARK 500    ASN B 293      -61.13    -92.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 403  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 524   O                                                      
REMARK 620 2 HOH A 535   O   101.7                                              
REMARK 620 3 HOH A 501   O    81.5  91.0                                        
REMARK 620 4 HOH A 506   O    69.1 167.8  79.9                                  
REMARK 620 5 HOH A 521   O    78.5 106.3 155.8  80.4                            
REMARK 620 6 HOH B 557   O   159.1  97.1  89.2  90.9 105.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 563   O                                                      
REMARK 620 2 HOH B 518   O    82.9                                              
REMARK 620 3 HOH B 522   O    93.2  77.6                                        
REMARK 620 4 HOH B 501   O    98.3 151.0  73.4                                  
REMARK 620 5 HOH B 508   O   157.5  75.1  77.6  98.6                            
REMARK 620 6 HOH A 545   O    81.4  80.2 157.6 128.8  99.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 402                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: CSGID-IDP01488   RELATED DB: TARGETTRACK                 
DBREF  6DGI A    1   334  UNP    Q9KM17   DDL_VIBCH        1    334             
DBREF  6DGI B    1   334  UNP    Q9KM17   DDL_VIBCH        1    334             
SEQADV 6DGI SER A   -2  UNP  Q9KM17              EXPRESSION TAG                 
SEQADV 6DGI ASN A   -1  UNP  Q9KM17              EXPRESSION TAG                 
SEQADV 6DGI ALA A    0  UNP  Q9KM17              EXPRESSION TAG                 
SEQADV 6DGI SER B   -2  UNP  Q9KM17              EXPRESSION TAG                 
SEQADV 6DGI ASN B   -1  UNP  Q9KM17              EXPRESSION TAG                 
SEQADV 6DGI ALA B    0  UNP  Q9KM17              EXPRESSION TAG                 
SEQRES   1 A  337  SER ASN ALA MSE THR LYS THR THR ILE LEU LEU LEU CYS          
SEQRES   2 A  337  GLY GLY GLY SER SER GLU HIS GLU ILE SER LEU VAL SER          
SEQRES   3 A  337  ALA ASN TYR ILE GLN GLN GLN LEU GLU LEU THR PRO GLU          
SEQRES   4 A  337  PHE HIS VAL ILE ARG VAL GLU MSE LYS LYS GLU GLY TRP          
SEQRES   5 A  337  PHE SER GLU GLN GLY ALA LEU VAL TYR LEU ASP THR ASN          
SEQRES   6 A  337  SER ALA THR LEU ASN SER ASP LYS ALA SER TYR PRO ILE          
SEQRES   7 A  337  ASP PHE VAL VAL PRO CYS ILE HIS GLY PHE PRO GLY GLU          
SEQRES   8 A  337  THR GLY ASP ILE GLN SER MSE LEU GLU LEU ALA GLY ILE          
SEQRES   9 A  337  PRO TYR LEU GLY CYS GLY PRO GLU ALA SER ALA ASN SER          
SEQRES  10 A  337  PHE ASN LYS ILE THR SER LYS LEU TRP TYR ASP ALA LEU          
SEQRES  11 A  337  ASP ILE PRO ASN THR PRO TYR LEU PHE LEU THR GLN ASN          
SEQRES  12 A  337  THR PRO SER SER ILE ASP LYS ALA LYS GLN ALA PHE GLY          
SEQRES  13 A  337  HIS TRP GLY SER ILE PHE VAL LYS ALA ALA ARG GLN GLY          
SEQRES  14 A  337  SER SER VAL GLY CYS TYR LYS VAL THR THR GLU ASP GLN          
SEQRES  15 A  337  ILE ALA PRO ALA ILE GLU ALA ALA PHE GLY PHE SER GLU          
SEQRES  16 A  337  GLN VAL LEU VAL GLU GLN ALA VAL LYS PRO ARG GLU LEU          
SEQRES  17 A  337  GLU VAL SER ALA TYR GLU MSE ASN GLY LYS LEU TYR ILE          
SEQRES  18 A  337  SER LYS PRO GLY GLU VAL ILE ALA PRO GLU GLY THR PHE          
SEQRES  19 A  337  TYR SER TYR GLU GLU LYS TYR SER ALA ASN SER HIS ALA          
SEQRES  20 A  337  ARG THR VAL LEU GLU ALA GLU ASN LEU THR GLU LYS HIS          
SEQRES  21 A  337  LYS GLU LEU ILE GLN THR TYR ALA GLU ARG VAL PHE ILE          
SEQRES  22 A  337  HIS MSE LYS LEU ARG HIS LEU SER ARG ILE ASP PHE PHE          
SEQRES  23 A  337  LEU THR GLN GLU GLY GLN ILE TYR LEU ASN GLU VAL ASN          
SEQRES  24 A  337  THR PHE PRO GLY MSE THR PRO ILE SER MSE PHE PRO LYS          
SEQRES  25 A  337  MSE LEU GLU HIS ASN GLY HIS ARG PHE SER GLU PHE LEU          
SEQRES  26 A  337  VAL GLN CYS VAL THR ASN THR LEU VAL ASN ALA LYS              
SEQRES   1 B  337  SER ASN ALA MSE THR LYS THR THR ILE LEU LEU LEU CYS          
SEQRES   2 B  337  GLY GLY GLY SER SER GLU HIS GLU ILE SER LEU VAL SER          
SEQRES   3 B  337  ALA ASN TYR ILE GLN GLN GLN LEU GLU LEU THR PRO GLU          
SEQRES   4 B  337  PHE HIS VAL ILE ARG VAL GLU MSE LYS LYS GLU GLY TRP          
SEQRES   5 B  337  PHE SER GLU GLN GLY ALA LEU VAL TYR LEU ASP THR ASN          
SEQRES   6 B  337  SER ALA THR LEU ASN SER ASP LYS ALA SER TYR PRO ILE          
SEQRES   7 B  337  ASP PHE VAL VAL PRO CYS ILE HIS GLY PHE PRO GLY GLU          
SEQRES   8 B  337  THR GLY ASP ILE GLN SER MSE LEU GLU LEU ALA GLY ILE          
SEQRES   9 B  337  PRO TYR LEU GLY CYS GLY PRO GLU ALA SER ALA ASN SER          
SEQRES  10 B  337  PHE ASN LYS ILE THR SER LYS LEU TRP TYR ASP ALA LEU          
SEQRES  11 B  337  ASP ILE PRO ASN THR PRO TYR LEU PHE LEU THR GLN ASN          
SEQRES  12 B  337  THR PRO SER SER ILE ASP LYS ALA LYS GLN ALA PHE GLY          
SEQRES  13 B  337  HIS TRP GLY SER ILE PHE VAL LYS ALA ALA ARG GLN GLY          
SEQRES  14 B  337  SER SER VAL GLY CYS TYR LYS VAL THR THR GLU ASP GLN          
SEQRES  15 B  337  ILE ALA PRO ALA ILE GLU ALA ALA PHE GLY PHE SER GLU          
SEQRES  16 B  337  GLN VAL LEU VAL GLU GLN ALA VAL LYS PRO ARG GLU LEU          
SEQRES  17 B  337  GLU VAL SER ALA TYR GLU MSE ASN GLY LYS LEU TYR ILE          
SEQRES  18 B  337  SER LYS PRO GLY GLU VAL ILE ALA PRO GLU GLY THR PHE          
SEQRES  19 B  337  TYR SER TYR GLU GLU LYS TYR SER ALA ASN SER HIS ALA          
SEQRES  20 B  337  ARG THR VAL LEU GLU ALA GLU ASN LEU THR GLU LYS HIS          
SEQRES  21 B  337  LYS GLU LEU ILE GLN THR TYR ALA GLU ARG VAL PHE ILE          
SEQRES  22 B  337  HIS MSE LYS LEU ARG HIS LEU SER ARG ILE ASP PHE PHE          
SEQRES  23 B  337  LEU THR GLN GLU GLY GLN ILE TYR LEU ASN GLU VAL ASN          
SEQRES  24 B  337  THR PHE PRO GLY MSE THR PRO ILE SER MSE PHE PRO LYS          
SEQRES  25 B  337  MSE LEU GLU HIS ASN GLY HIS ARG PHE SER GLU PHE LEU          
SEQRES  26 B  337  VAL GLN CYS VAL THR ASN THR LEU VAL ASN ALA LYS              
MODRES 6DGI MSE A    1  MET  MODIFIED RESIDUE                                   
MODRES 6DGI MSE A   44  MET  MODIFIED RESIDUE                                   
MODRES 6DGI MSE A   95  MET  MODIFIED RESIDUE                                   
MODRES 6DGI MSE A  212  MET  MODIFIED RESIDUE                                   
MODRES 6DGI MSE A  272  MET  MODIFIED RESIDUE                                   
MODRES 6DGI MSE A  301  MET  MODIFIED RESIDUE                                   
MODRES 6DGI MSE A  306  MET  MODIFIED RESIDUE                                   
MODRES 6DGI MSE A  310  MET  MODIFIED RESIDUE                                   
MODRES 6DGI MSE B    1  MET  MODIFIED RESIDUE                                   
MODRES 6DGI MSE B   44  MET  MODIFIED RESIDUE                                   
MODRES 6DGI MSE B   95  MET  MODIFIED RESIDUE                                   
MODRES 6DGI MSE B  212  MET  MODIFIED RESIDUE                                   
MODRES 6DGI MSE B  272  MET  MODIFIED RESIDUE                                   
MODRES 6DGI MSE B  301  MET  MODIFIED RESIDUE                                   
MODRES 6DGI MSE B  306  MET  MODIFIED RESIDUE                                   
MODRES 6DGI MSE B  310  MET  MODIFIED RESIDUE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  44       8                                                       
HET    MSE  A  95       8                                                       
HET    MSE  A 212       8                                                       
HET    MSE  A 272       8                                                       
HET    MSE  A 301       8                                                       
HET    MSE  A 306       8                                                       
HET    MSE  A 310       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B  44       8                                                       
HET    MSE  B  95       8                                                       
HET    MSE  B 212       8                                                       
HET    MSE  B 272       8                                                       
HET    MSE  B 301       8                                                       
HET    MSE  B 306       8                                                       
HET    MSE  B 310       8                                                       
HET    GOL  A 401       6                                                       
HET    ACT  A 402       4                                                       
HET     MG  A 403       1                                                       
HET    GOL  B 401       6                                                       
HET     MG  B 402       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     GOL GLYCEROL                                                         
HETNAM     ACT ACETATE ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    16(C5 H11 N O2 SE)                                           
FORMUL   3  GOL    2(C3 H8 O3)                                                  
FORMUL   4  ACT    C2 H3 O2 1-                                                  
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   8  HOH   *110(H2 O)                                                    
HELIX    1 AA1 GLU A   16  GLU A   32  1                                  17    
HELIX    2 AA2 GLY A   90  GLY A  100  1                                  11    
HELIX    3 AA3 GLY A  107  ASN A  116  1                                  10    
HELIX    4 AA4 ASN A  116  LEU A  127  1                                  12    
HELIX    5 AA5 THR A  141  GLY A  156  1                                  16    
HELIX    6 AA6 THR A  176  ASP A  178  5                                   3    
HELIX    7 AA7 GLN A  179  GLY A  189  1                                  11    
HELIX    8 AA8 SER A  233  SER A  239  5                                   7    
HELIX    9 AA9 THR A  254  MSE A  272  1                                  19    
HELIX   10 AB1 SER A  305  ASN A  314  1                                  10    
HELIX   11 AB2 ARG A  317  ASN A  332  1                                  16    
HELIX   12 AB3 GLU B   16  GLU B   32  1                                  17    
HELIX   13 AB4 GLY B   90  GLY B  100  1                                  11    
HELIX   14 AB5 GLY B  107  ASN B  116  1                                  10    
HELIX   15 AB6 ASN B  116  LEU B  127  1                                  12    
HELIX   16 AB7 THR B  141  GLY B  156  1                                  16    
HELIX   17 AB8 THR B  176  ASP B  178  5                                   3    
HELIX   18 AB9 GLN B  179  PHE B  188  1                                  10    
HELIX   19 AC1 GLU B  228  TYR B  232  5                                   5    
HELIX   20 AC2 THR B  254  MSE B  272  1                                  19    
HELIX   21 AC3 SER B  305  ASN B  314  1                                  10    
HELIX   22 AC4 ARG B  317  ASN B  332  1                                  16    
SHEET    1 AA1 7 SER A  72  PRO A  74  0                                        
SHEET    2 AA1 7 THR A  65  ASN A  67 -1  N  LEU A  66   O  TYR A  73           
SHEET    3 AA1 7 LEU A  56  ASP A  60 -1  N  ASP A  60   O  THR A  65           
SHEET    4 AA1 7 GLY A  48  SER A  51 -1  N  TRP A  49   O  VAL A  57           
SHEET    5 AA1 7 PHE A  37  LYS A  45 -1  N  GLU A  43   O  PHE A  50           
SHEET    6 AA1 7 THR A   4  GLY A  11  1  N  LEU A   8   O  ILE A  40           
SHEET    7 AA1 7 PHE A  77  CYS A  81  1  O  PHE A  77   N  LEU A   7           
SHEET    1 AA2 4 TYR A 134  LEU A 137  0                                        
SHEET    2 AA2 4 VAL A 194  GLN A 198 -1  O  VAL A 196   N  LEU A 135           
SHEET    3 AA2 4 ILE A 158  ALA A 162 -1  N  LYS A 161   O  LEU A 195           
SHEET    4 AA2 4 CYS A 171  VAL A 174 -1  O  TYR A 172   N  VAL A 160           
SHEET    1 AA3 4 LYS A 215  ILE A 218  0                                        
SHEET    2 AA3 4 ARG A 203  MSE A 212 -1  N  MSE A 212   O  LYS A 215           
SHEET    3 AA3 4 GLY A 222  ILE A 225 -1  O  GLY A 222   N  GLU A 206           
SHEET    4 AA3 4 ARG A 245  VAL A 247 -1  O  VAL A 247   N  GLU A 223           
SHEET    1 AA4 4 LYS A 215  ILE A 218  0                                        
SHEET    2 AA4 4 ARG A 203  MSE A 212 -1  N  MSE A 212   O  LYS A 215           
SHEET    3 AA4 4 LEU A 277  LEU A 284 -1  O  PHE A 282   N  LEU A 205           
SHEET    4 AA4 4 ILE A 290  ASN A 296 -1  O  ASN A 296   N  ARG A 279           
SHEET    1 AA5 7 SER B  72  PRO B  74  0                                        
SHEET    2 AA5 7 THR B  65  ASN B  67 -1  N  LEU B  66   O  TYR B  73           
SHEET    3 AA5 7 LEU B  56  ASP B  60 -1  N  TYR B  58   O  ASN B  67           
SHEET    4 AA5 7 GLY B  48  SER B  51 -1  N  TRP B  49   O  VAL B  57           
SHEET    5 AA5 7 PHE B  37  LYS B  45 -1  N  LYS B  45   O  GLY B  48           
SHEET    6 AA5 7 THR B   4  GLY B  11  1  N  LEU B   8   O  ILE B  40           
SHEET    7 AA5 7 PHE B  77  CYS B  81  1  O  PHE B  77   N  LEU B   7           
SHEET    1 AA6 4 TYR B 134  LEU B 137  0                                        
SHEET    2 AA6 4 VAL B 194  GLN B 198 -1  O  VAL B 196   N  LEU B 135           
SHEET    3 AA6 4 ILE B 158  ALA B 162 -1  N  LYS B 161   O  LEU B 195           
SHEET    4 AA6 4 CYS B 171  VAL B 174 -1  O  VAL B 174   N  ILE B 158           
SHEET    1 AA7 4 LYS B 215  ILE B 218  0                                        
SHEET    2 AA7 4 ARG B 203  MSE B 212 -1  N  TYR B 210   O  TYR B 217           
SHEET    3 AA7 4 GLY B 222  VAL B 224 -1  O  GLY B 222   N  GLU B 206           
SHEET    4 AA7 4 THR B 246  VAL B 247 -1  O  VAL B 247   N  GLU B 223           
SHEET    1 AA8 4 LYS B 215  ILE B 218  0                                        
SHEET    2 AA8 4 ARG B 203  MSE B 212 -1  N  TYR B 210   O  TYR B 217           
SHEET    3 AA8 4 LEU B 277  LEU B 284 -1  O  PHE B 282   N  LEU B 205           
SHEET    4 AA8 4 ILE B 290  ASN B 296 -1  O  ASN B 296   N  ARG B 279           
LINK         C   ALA A   0                 N   MSE A   1     1555   1555  1.33  
LINK         C   MSE A   1                 N   THR A   2     1555   1555  1.33  
LINK         C   GLU A  43                 N   MSE A  44     1555   1555  1.33  
LINK         C   MSE A  44                 N   LYS A  45     1555   1555  1.33  
LINK         C   SER A  94                 N   MSE A  95     1555   1555  1.33  
LINK         C   MSE A  95                 N   LEU A  96     1555   1555  1.34  
LINK         C   GLU A 211                 N   MSE A 212     1555   1555  1.33  
LINK         C   MSE A 212                 N   ASN A 213     1555   1555  1.34  
LINK         C   HIS A 271                 N   MSE A 272     1555   1555  1.33  
LINK         C   MSE A 272                 N   LYS A 273     1555   1555  1.33  
LINK         C   GLY A 300                 N   MSE A 301     1555   1555  1.33  
LINK         C   MSE A 301                 N   THR A 302     1555   1555  1.33  
LINK         C   SER A 305                 N   MSE A 306     1555   1555  1.33  
LINK         C   MSE A 306                 N   PHE A 307     1555   1555  1.33  
LINK         C   LYS A 309                 N   MSE A 310     1555   1555  1.33  
LINK         C   MSE A 310                 N   LEU A 311     1555   1555  1.33  
LINK         C   MSE B   1                 N   THR B   2     1555   1555  1.33  
LINK         C   GLU B  43                 N   MSE B  44     1555   1555  1.33  
LINK         C   MSE B  44                 N   LYS B  45     1555   1555  1.33  
LINK         C   SER B  94                 N   MSE B  95     1555   1555  1.33  
LINK         C   MSE B  95                 N   LEU B  96     1555   1555  1.34  
LINK         C   GLU B 211                 N   MSE B 212     1555   1555  1.33  
LINK         C   MSE B 212                 N   ASN B 213     1555   1555  1.34  
LINK         C   HIS B 271                 N   MSE B 272     1555   1555  1.32  
LINK         C   MSE B 272                 N   LYS B 273     1555   1555  1.34  
LINK         C   GLY B 300                 N   MSE B 301     1555   1555  1.33  
LINK         C   MSE B 301                 N   THR B 302     1555   1555  1.33  
LINK         C   SER B 305                 N   MSE B 306     1555   1555  1.33  
LINK         C   MSE B 306                 N   PHE B 307     1555   1555  1.34  
LINK         C   LYS B 309                 N   MSE B 310     1555   1555  1.33  
LINK         C   MSE B 310                 N   LEU B 311     1555   1555  1.33  
LINK        MG    MG A 403                 O   HOH A 524     1555   1555  2.19  
LINK        MG    MG A 403                 O   HOH A 535     1555   1555  2.17  
LINK        MG    MG A 403                 O   HOH A 501     1555   1555  2.23  
LINK        MG    MG A 403                 O   HOH A 506     1555   1555  2.19  
LINK        MG    MG A 403                 O   HOH A 521     1555   1555  2.13  
LINK        MG    MG B 402                 O   HOH B 563     1555   1555  2.13  
LINK        MG    MG B 402                 O   HOH B 518     1555   1555  1.95  
LINK        MG    MG B 402                 O   HOH B 522     1555   1555  2.43  
LINK        MG    MG B 402                 O   HOH B 501     1555   1555  2.25  
LINK        MG    MG B 402                 O   HOH B 508     1555   1555  2.02  
LINK        MG    MG A 403                 O   HOH B 557     1555   1455  2.11  
LINK        MG    MG B 402                 O   HOH A 545     1555   1655  2.17  
CISPEP   1 PHE A   85    PRO A   86          0         0.56                     
CISPEP   2 PHE B   85    PRO B   86          0        -3.18                     
SITE     1 AC1  7 GLY A  90  SER A  94  PRO A 108  ALA A 112                    
SITE     2 AC1  7 THR B  89  SER B  94  PRO B 108                               
SITE     1 AC2  4 GLU A  16  GLU A  88  GLY A 166  ASN A 296                    
SITE     1 AC3  6 HOH A 501  HOH A 506  HOH A 521  HOH A 524                    
SITE     2 AC3  6 HOH A 535  HOH B 557                                          
SITE     1 AC4  6 GLU B  16  GLY B  84  GLU B  88  SER B 167                    
SITE     2 AC4  6 ASN B 296  HOH B 529                                          
SITE     1 AC5  6 HOH A 545  HOH B 501  HOH B 508  HOH B 518                    
SITE     2 AC5  6 HOH B 522  HOH B 563                                          
CRYST1   63.588   64.875  165.160  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015726  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015414  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006055        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system