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Database: PDB
Entry: 5VM2
LinkDB: 5VM2
Original site: 5VM2 
HEADER    OXIDOREDUCTASE                          26-APR-17   5VM2              
TITLE     CRYSTAL STRUCTURE OF ECK1772, AN OXIDOREDUCTASE/DEHYDROGENASE OF      
TITLE    2 UNKNOWN SPECIFICITY INVOLVED IN MEMBRANE BIOGENESIS FROM ESCHERICHIA 
TITLE    3 COLI                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALCOHOL DEHYDROGENASE;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PUTATIVE OXIDOREDUCTASE;                                    
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: ARC77_00615, AU473_19815, BFL24_13020, ECS2483;                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-MAGIC;                           
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PMCSG53                                   
KEYWDS    NAD(H) OR NADP(H)-DEPENDENT OXIDOREDUCTASE, DEHYDROGENASE, ROSSMAN    
KEYWDS   2 FOLD, STRUCTURAL GENOMICS, CSGID, CENTER FOR STRUCTURAL GENOMICS OF  
KEYWDS   3 INFECTIOUS DISEASES, NIAID, NATIONAL INSTITUTE OF ALLERGY AND        
KEYWDS   4 INFECTIOUS DISEASES, OXIDOREDUCTASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.J.STOGIOS,T.SKARINA,C.MCCHESNEY,R.DI LEO,A.SAVCHENKO,W.F.ANDERSON,  
AUTHOR   2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)        
REVDAT   3   11-DEC-19 5VM2    1       REMARK                                   
REVDAT   2   13-SEP-17 5VM2    1       REMARK                                   
REVDAT   1   07-JUN-17 5VM2    0                                                
JRNL        AUTH   P.J.STOGIOS                                                  
JRNL        TITL   CRYSTAL STRUCTURE OF ECK1772, AN                             
JRNL        TITL 2 OXIDOREDUCTASE/DEHYDROGENASE OF UNKNOWN SPECIFICITY INVOLVED 
JRNL        TITL 3 IN MEMBRANE BIOGENESIS FROM ESCHERICHIA COLI                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.98 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_2733                                      
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) : 1.98                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.31                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 46646                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.180                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1950                            
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 39.3193 -  4.7765    0.99     3465   151  0.1713 0.2141        
REMARK   3     2  4.7765 -  3.7922    1.00     3341   147  0.1423 0.1763        
REMARK   3     3  3.7922 -  3.3132    1.00     3314   145  0.1608 0.2011        
REMARK   3     4  3.3132 -  3.0104    0.99     3277   141  0.1827 0.2125        
REMARK   3     5  3.0104 -  2.7946    1.00     3262   144  0.2046 0.2540        
REMARK   3     6  2.7946 -  2.6299    0.99     3252   142  0.2077 0.2756        
REMARK   3     7  2.6299 -  2.4982    0.99     3216   141  0.2104 0.2591        
REMARK   3     8  2.4982 -  2.3895    0.98     3182   139  0.2082 0.2726        
REMARK   3     9  2.3895 -  2.2975    0.98     3166   138  0.2049 0.2407        
REMARK   3    10  2.2975 -  2.2182    0.97     3143   140  0.2064 0.2680        
REMARK   3    11  2.2182 -  2.1489    0.96     3124   139  0.2103 0.2690        
REMARK   3    12  2.1489 -  2.0875    0.94     3063   133  0.2246 0.2644        
REMARK   3    13  2.0875 -  2.0325    0.93     3014   127  0.2340 0.3309        
REMARK   3    14  2.0325 -  1.9829    0.89     2877   123  0.2455 0.2672        
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)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.630           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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      :  0.005           5418                                  
REMARK   3   ANGLE     :  0.927           7340                                  
REMARK   3   CHIRALITY :  0.063            843                                  
REMARK   3   PLANARITY :  0.006            956                                  
REMARK   3   DIHEDRAL  : 21.913           2056                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1:76)                               
REMARK   3    ORIGIN FOR THE GROUP (A):   1.5310  -2.2675  35.0954              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6395 T22:   0.4611                                     
REMARK   3      T33:   0.3586 T12:   0.0001                                     
REMARK   3      T13:  -0.0704 T23:   0.0105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8986 L22:   3.3472                                     
REMARK   3      L33:   1.6035 L12:  -0.5022                                     
REMARK   3      L13:  -0.8181 L23:   1.1131                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0645 S12:  -0.0435 S13:   0.5384                       
REMARK   3      S21:   0.7248 S22:   0.1956 S23:  -0.4312                       
REMARK   3      S31:  -0.3662 S32:   0.3862 S33:  -0.2688                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 77:189)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.9090  -5.3856  22.1246              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2334 T22:   0.3117                                     
REMARK   3      T33:   0.3020 T12:   0.0277                                     
REMARK   3      T13:   0.0096 T23:   0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4935 L22:   2.5403                                     
REMARK   3      L33:   2.9069 L12:  -0.3701                                     
REMARK   3      L13:   0.0179 L23:   0.9755                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1215 S12:  -0.1476 S13:   0.0685                       
REMARK   3      S21:   0.4208 S22:   0.1236 S23:   0.1346                       
REMARK   3      S31:  -0.0407 S32:  -0.0706 S33:  -0.0077                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 190:235)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2808 -22.7611   4.4283              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2899 T22:   0.2279                                     
REMARK   3      T33:   0.3815 T12:   0.0258                                     
REMARK   3      T13:  -0.0415 T23:  -0.0282                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6732 L22:   3.9735                                     
REMARK   3      L33:   3.6303 L12:  -2.2299                                     
REMARK   3      L13:  -3.0057 L23:   0.1440                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0823 S12:   0.1356 S13:  -0.4105                       
REMARK   3      S21:  -0.1869 S22:  -0.2181 S23:  -0.2651                       
REMARK   3      S31:   0.3510 S32:   0.2617 S33:   0.1539                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 236:274)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   3.1605  -8.9534   1.7506              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1738 T22:   0.3654                                     
REMARK   3      T33:   0.3627 T12:  -0.0144                                     
REMARK   3      T13:  -0.0020 T23:   0.0189                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1601 L22:   7.1510                                     
REMARK   3      L33:   5.9935 L12:  -1.0250                                     
REMARK   3      L13:  -0.9870 L23:  -1.7727                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0248 S12:  -0.3020 S13:   0.1571                       
REMARK   3      S21:  -0.0141 S22:  -0.0176 S23:  -0.6927                       
REMARK   3      S31:  -0.3712 S32:   1.1607 S33:  -0.1051                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 275:321)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.1546 -10.5947  13.5065              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2562 T22:   0.2800                                     
REMARK   3      T33:   0.3233 T12:   0.0325                                     
REMARK   3      T13:  -0.0276 T23:  -0.0209                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6105 L22:   1.8849                                     
REMARK   3      L33:   4.7143 L12:   0.4235                                     
REMARK   3      L13:  -0.9069 L23:  -1.5776                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0622 S12:  -0.0487 S13:  -0.0579                       
REMARK   3      S21:   0.0987 S22:   0.0184 S23:  -0.0021                       
REMARK   3      S31:   0.1194 S32:   0.2255 S33:  -0.0590                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 322:347)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   8.2279 -16.1757  30.5421              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4789 T22:   0.4375                                     
REMARK   3      T33:   0.4703 T12:   0.1079                                     
REMARK   3      T13:  -0.1776 T23:  -0.0809                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1080 L22:   8.0462                                     
REMARK   3      L33:   6.7349 L12:   2.8667                                     
REMARK   3      L13:   5.6924 L23:   1.4626                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0302 S12:   0.0828 S13:  -0.1489                       
REMARK   3      S21:   1.1351 S22:   0.5118 S23:  -1.1786                       
REMARK   3      S31:   0.7295 S32:   1.0652 S33:  -0.4334                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 1:88)                               
REMARK   3    ORIGIN FOR THE GROUP (A): -31.9893 -26.3905 -22.8345              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5991 T22:   0.2286                                     
REMARK   3      T33:   0.2929 T12:   0.0665                                     
REMARK   3      T13:  -0.0670 T23:   0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4765 L22:   3.7038                                     
REMARK   3      L33:   4.1498 L12:   0.2409                                     
REMARK   3      L13:  -0.9466 L23:   0.5226                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1011 S12:   0.4624 S13:   0.3969                       
REMARK   3      S21:  -0.9264 S22:  -0.0929 S23:   0.1401                       
REMARK   3      S31:  -0.2256 S32:  -0.3042 S33:   0.1176                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 89:122)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -27.1087 -11.0992 -19.6038              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3776 T22:   0.2376                                     
REMARK   3      T33:   0.2367 T12:   0.0519                                     
REMARK   3      T13:  -0.0167 T23:   0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1722 L22:   7.6504                                     
REMARK   3      L33:   6.5628 L12:   4.8043                                     
REMARK   3      L13:  -0.0083 L23:   0.7246                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2880 S12:   0.2209 S13:   0.2835                       
REMARK   3      S21:  -1.0112 S22:   0.1055 S23:   0.3954                       
REMARK   3      S31:  -0.1950 S32:  -0.1035 S33:   0.1927                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 123:194)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -25.1234 -21.6463  -5.0877              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2736 T22:   0.2321                                     
REMARK   3      T33:   0.2822 T12:   0.0177                                     
REMARK   3      T13:   0.0210 T23:   0.0322                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6477 L22:   2.4223                                     
REMARK   3      L33:   3.0099 L12:  -0.1292                                     
REMARK   3      L13:  -0.7142 L23:   1.2101                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0466 S12:   0.0496 S13:  -0.0096                       
REMARK   3      S21:  -0.1262 S22:   0.0345 S23:  -0.2287                       
REMARK   3      S31:   0.0991 S32:   0.1631 S33:   0.0052                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 195:236)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -36.9642 -18.9466  13.4679              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2607 T22:   0.1562                                     
REMARK   3      T33:   0.1576 T12:  -0.0185                                     
REMARK   3      T13:   0.0226 T23:   0.0337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4520 L22:   5.9157                                     
REMARK   3      L33:   4.1158 L12:  -0.9756                                     
REMARK   3      L13:  -1.9864 L23:   1.7519                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0911 S12:  -0.2909 S13:  -0.1050                       
REMARK   3      S21:   0.4511 S22:  -0.1310 S23:   0.0784                       
REMARK   3      S31:   0.0076 S32:   0.0372 S33:   0.0698                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 237:288)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -36.5986  -4.7367   5.1537              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1901 T22:   0.2190                                     
REMARK   3      T33:   0.3035 T12:  -0.0030                                     
REMARK   3      T13:  -0.0205 T23:  -0.0086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7233 L22:   6.8548                                     
REMARK   3      L33:   5.2186 L12:   0.1594                                     
REMARK   3      L13:  -1.5354 L23:  -0.7523                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1926 S12:   0.1912 S13:  -0.1658                       
REMARK   3      S21:  -0.1999 S22:  -0.1644 S23:   0.8497                       
REMARK   3      S31:  -0.0267 S32:  -0.6742 S33:  -0.0154                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN B AND RESID 289:347)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -33.3399 -28.4102  -7.7552              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2278 T22:   0.2232                                     
REMARK   3      T33:   0.2114 T12:   0.0268                                     
REMARK   3      T13:   0.0311 T23:  -0.0336                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3822 L22:   5.3933                                     
REMARK   3      L33:   3.0109 L12:   1.5892                                     
REMARK   3      L13:   0.8229 L23:   0.5063                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1194 S12:  -0.0076 S13:  -0.2695                       
REMARK   3      S21:  -0.1376 S22:  -0.1772 S23:   0.1902                       
REMARK   3      S31:   0.2598 S32:  -0.3110 S33:   0.0277                       
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 5VM2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227612.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-APR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
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) : 0.97860                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 X 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47841                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.980                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.10600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 1E3J                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM CHLORIDE, 0.1 M SODIUM      
REMARK 280  CITRATE PH 5.6, 1 MM MAGNESIUM CHLORIDE, 25% (W/V) PEG3350,         
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.44400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.73000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.44400            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.73000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CL    CL B 403  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 711  LIES ON A SPECIAL POSITION.                          
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   NZ   LYS B   335     O    HOH B   501              1.40            
REMARK 500   O    HOH B   575     O    HOH B   809              2.08            
REMARK 500   OE2  GLU B   203     O    HOH B   502              2.14            
REMARK 500   O    HOH B   748     O    HOH B   845              2.15            
REMARK 500   O    HOH A   632     O    HOH A   662              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OH   TYR B    35     OE1  GLN B   211     2545     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 119   C   -  N   -  CA  ANGL. DEV. = -11.0 DEGREES          
REMARK 500    ILE B  52   N   -  CA  -  C   ANGL. DEV. = -18.0 DEGREES          
REMARK 500    PRO B  53   C   -  N   -  CA  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    PRO B  54   C   -  N   -  CA  ANGL. DEV. = -12.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A 269     -129.82     64.96                                   
REMARK 500    VAL A 270       78.19     62.22                                   
REMARK 500    ARG A 292     -116.61     53.08                                   
REMARK 500    ASP A 323       31.23    -92.06                                   
REMARK 500    ASN A 334       47.91   -104.48                                   
REMARK 500    GLN B   9      -75.10    -73.92                                   
REMARK 500    SER B  48       23.61   -143.57                                   
REMARK 500    ILE B  52       67.45     63.51                                   
REMARK 500    LYS B  55       16.96    -69.89                                   
REMARK 500    ASP B  56      103.95   -161.08                                   
REMARK 500    GLN B 118      -53.76    -23.18                                   
REMARK 500    ARG B 292     -116.27     52.63                                   
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 794        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH A 795        DISTANCE =  6.44 ANGSTROMS                       
REMARK 525    HOH B 857        DISTANCE =  6.71 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  66   OE1                                                    
REMARK 620 2 GLU A 152   OE1  98.8                                              
REMARK 620 3 HOH A 705   O   108.6 107.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  95   SG                                                     
REMARK 620 2 CYS A  98   SG  109.0                                              
REMARK 620 3 CYS A 101   SG  118.6 106.2                                        
REMARK 620 4 CYS A 109   SG  103.9 114.5 105.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  66   OE1                                                    
REMARK 620 2 GLU B 152   OE1  97.7                                              
REMARK 620 3 HOH B 650   O   103.4 108.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 402  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  95   SG                                                     
REMARK 620 2 CYS B  98   SG  111.3                                              
REMARK 620 3 CYS B 101   SG  116.0 105.8                                        
REMARK 620 4 CYS B 109   SG  102.2 113.3 108.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 403                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: CSGID-IDP95672   RELATED DB: TARGETTRACK                 
REMARK 900 RELATED ID: IDP95672   RELATED DB: TARGETTRACK                       
DBREF  5VM2 A    1   347  UNP    C3T6X7   C3T6X7_ECOLX     1    347             
DBREF  5VM2 B    1   347  UNP    C3T6X7   C3T6X7_ECOLX     1    347             
SEQRES   1 A  347  MET LYS ASN SER LYS ALA ILE LEU GLN VAL PRO GLY THR          
SEQRES   2 A  347  MET LYS ILE ILE SER ALA GLU ILE PRO VAL PRO LYS GLU          
SEQRES   3 A  347  ASP GLU VAL LEU ILE LYS VAL GLU TYR VAL GLY ILE CSO          
SEQRES   4 A  347  GLY SER ASP VAL HIS GLY PHE GLU SER GLY PRO PHE ILE          
SEQRES   5 A  347  PRO PRO LYS ASP PRO ASN GLN GLU ILE GLY LEU GLY HIS          
SEQRES   6 A  347  GLU CYS ALA GLY THR VAL VAL ALA VAL GLY SER ARG VAL          
SEQRES   7 A  347  ARG LYS PHE LYS PRO GLY ASP ARG VAL ASN ILE GLU PRO          
SEQRES   8 A  347  GLY VAL PRO CYS GLY HIS CYS ARG TYR CYS LEU GLU GLY          
SEQRES   9 A  347  LYS TYR ASN ILE CYS PRO ASP VAL ASP PHE MET ALA THR          
SEQRES  10 A  347  GLN PRO ASN TYR ARG GLY ALA LEU THR HIS TYR LEU CYS          
SEQRES  11 A  347  HIS PRO GLU SER PHE THR TYR LYS LEU PRO ASP ASN MET          
SEQRES  12 A  347  ASP THR MET GLU GLY THR LEU VAL GLU PRO ALA ALA VAL          
SEQRES  13 A  347  GLY MET HIS ALA ALA MET LEU ALA ASP VAL LYS PRO GLY          
SEQRES  14 A  347  LYS LYS ILE ILE ILE LEU GLY ALA GLY CYS ILE GLY LEU          
SEQRES  15 A  347  MET THR LEU GLN ALA CYS LYS CYS LEU GLY ALA THR GLU          
SEQRES  16 A  347  ILE ALA VAL VAL ASP VAL LEU GLU LYS ARG LEU ALA MET          
SEQRES  17 A  347  ALA GLU GLN LEU GLY ALA THR VAL VAL ILE ASN GLY ALA          
SEQRES  18 A  347  LYS GLU ASP THR ILE ALA ARG CYS GLN GLN PHE THR GLU          
SEQRES  19 A  347  ASP MET GLY ALA ASP ILE VAL PHE GLU THR ALA GLY SER          
SEQRES  20 A  347  ALA VAL THR VAL LYS GLN ALA PRO TYR LEU VAL MET ARG          
SEQRES  21 A  347  GLY GLY LYS ILE MET ILE VAL GLY THR VAL PRO GLY ALA          
SEQRES  22 A  347  SER ALA ILE ASN PHE LEU LYS ILE ASN ARG GLU VAL THR          
SEQRES  23 A  347  ILE GLN THR VAL PHE ARG TYR ALA ASN ARG TYR PRO VAL          
SEQRES  24 A  347  THR ILE GLU ALA ILE SER SER GLY ARG PHE ASP VAL LYS          
SEQRES  25 A  347  SER MET VAL THR HIS ILE TYR ASP TYR ARG ASP VAL GLN          
SEQRES  26 A  347  GLN ALA PHE GLU GLU SER VAL ASN ASN LYS ARG ASP ILE          
SEQRES  27 A  347  ILE LYS GLY VAL ILE LYS ILE SER ASP                          
SEQRES   1 B  347  MET LYS ASN SER LYS ALA ILE LEU GLN VAL PRO GLY THR          
SEQRES   2 B  347  MET LYS ILE ILE SER ALA GLU ILE PRO VAL PRO LYS GLU          
SEQRES   3 B  347  ASP GLU VAL LEU ILE LYS VAL GLU TYR VAL GLY ILE CSO          
SEQRES   4 B  347  GLY SER ASP VAL HIS GLY PHE GLU SER GLY PRO PHE ILE          
SEQRES   5 B  347  PRO PRO LYS ASP PRO ASN GLN GLU ILE GLY LEU GLY HIS          
SEQRES   6 B  347  GLU CYS ALA GLY THR VAL VAL ALA VAL GLY SER ARG VAL          
SEQRES   7 B  347  ARG LYS PHE LYS PRO GLY ASP ARG VAL ASN ILE GLU PRO          
SEQRES   8 B  347  GLY VAL PRO CYS GLY HIS CYS ARG TYR CYS LEU GLU GLY          
SEQRES   9 B  347  LYS TYR ASN ILE CYS PRO ASP VAL ASP PHE MET ALA THR          
SEQRES  10 B  347  GLN PRO ASN TYR ARG GLY ALA LEU THR HIS TYR LEU CYS          
SEQRES  11 B  347  HIS PRO GLU SER PHE THR TYR LYS LEU PRO ASP ASN MET          
SEQRES  12 B  347  ASP THR MET GLU GLY THR LEU VAL GLU PRO ALA ALA VAL          
SEQRES  13 B  347  GLY MET HIS ALA ALA MET LEU ALA ASP VAL LYS PRO GLY          
SEQRES  14 B  347  LYS LYS ILE ILE ILE LEU GLY ALA GLY CYS ILE GLY LEU          
SEQRES  15 B  347  MET THR LEU GLN ALA CYS LYS CYS LEU GLY ALA THR GLU          
SEQRES  16 B  347  ILE ALA VAL VAL ASP VAL LEU GLU LYS ARG LEU ALA MET          
SEQRES  17 B  347  ALA GLU GLN LEU GLY ALA THR VAL VAL ILE ASN GLY ALA          
SEQRES  18 B  347  LYS GLU ASP THR ILE ALA ARG CYS GLN GLN PHE THR GLU          
SEQRES  19 B  347  ASP MET GLY ALA ASP ILE VAL PHE GLU THR ALA GLY SER          
SEQRES  20 B  347  ALA VAL THR VAL LYS GLN ALA PRO TYR LEU VAL MET ARG          
SEQRES  21 B  347  GLY GLY LYS ILE MET ILE VAL GLY THR VAL PRO GLY ALA          
SEQRES  22 B  347  SER ALA ILE ASN PHE LEU LYS ILE ASN ARG GLU VAL THR          
SEQRES  23 B  347  ILE GLN THR VAL PHE ARG TYR ALA ASN ARG TYR PRO VAL          
SEQRES  24 B  347  THR ILE GLU ALA ILE SER SER GLY ARG PHE ASP VAL LYS          
SEQRES  25 B  347  SER MET VAL THR HIS ILE TYR ASP TYR ARG ASP VAL GLN          
SEQRES  26 B  347  GLN ALA PHE GLU GLU SER VAL ASN ASN LYS ARG ASP ILE          
SEQRES  27 B  347  ILE LYS GLY VAL ILE LYS ILE SER ASP                          
MODRES 5VM2 CSO A   39  CYS  MODIFIED RESIDUE                                   
MODRES 5VM2 CSO B   39  CYS  MODIFIED RESIDUE                                   
HET    CSO  A  39       7                                                       
HET    CSO  B  39      14                                                       
HET     MG  A 401       1                                                       
HET     ZN  A 402       1                                                       
HET     MG  B 401       1                                                       
HET     ZN  B 402       1                                                       
HET     CL  B 403       1                                                       
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  CSO    2(C3 H7 N O3 S)                                              
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   4   ZN    2(ZN 2+)                                                     
FORMUL   7   CL    CL 1-                                                        
FORMUL   8  HOH   *652(H2 O)                                                    
HELIX    1 AA1 CSO A   39  GLY A   49  1                                  11    
HELIX    2 AA2 CYS A   98  GLU A  103  1                                   6    
HELIX    3 AA3 LYS A  105  CYS A  109  5                                   5    
HELIX    4 AA4 ASP A  144  ALA A  164  1                                  21    
HELIX    5 AA5 GLY A  178  LEU A  191  1                                  14    
HELIX    6 AA6 LEU A  202  LEU A  212  1                                  11    
HELIX    7 AA7 ASP A  224  THR A  233  1                                  10    
HELIX    8 AA8 SER A  247  ALA A  254  1                                   8    
HELIX    9 AA9 ASN A  277  ASN A  282  5                                   6    
HELIX   10 AB1 ARG A  296  SER A  306  1                                  11    
HELIX   11 AB2 VAL A  311  SER A  313  5                                   3    
HELIX   12 AB3 ASP A  323  ASN A  334  1                                  12    
HELIX   13 AB4 LYS A  335  ILE A  338  5                                   4    
HELIX   14 AB5 CSO B   39  GLY B   49  1                                  11    
HELIX   15 AB6 CYS B   98  GLU B  103  1                                   6    
HELIX   16 AB7 LYS B  105  CYS B  109  5                                   5    
HELIX   17 AB8 ASP B  144  ALA B  164  1                                  21    
HELIX   18 AB9 GLY B  178  LEU B  191  1                                  14    
HELIX   19 AC1 LEU B  202  LEU B  212  1                                  11    
HELIX   20 AC2 ASP B  224  THR B  233  1                                  10    
HELIX   21 AC3 SER B  247  ALA B  254  1                                   8    
HELIX   22 AC4 PHE B  278  ASN B  282  5                                   5    
HELIX   23 AC5 ARG B  296  SER B  306  1                                  11    
HELIX   24 AC6 ASP B  323  ASN B  334  1                                  12    
HELIX   25 AC7 LYS B  335  ILE B  338  5                                   4    
SHEET    1 AA1 2 ASN A   3  VAL A  10  0                                        
SHEET    2 AA1 2 THR A  13  ALA A  19 -1  O  LYS A  15   N  ILE A   7           
SHEET    1 AA2 5 TYR A 128  PRO A 132  0                                        
SHEET    2 AA2 5 GLU A  28  ILE A  38 -1  N  VAL A  29   O  HIS A 131           
SHEET    3 AA2 5 CYS A  67  VAL A  74 -1  O  VAL A  72   N  LEU A  30           
SHEET    4 AA2 5 ARG A  86  ILE A  89 -1  O  VAL A  87   N  GLY A  69           
SHEET    5 AA2 5 THR A 136  LYS A 138 -1  O  TYR A 137   N  ASN A  88           
SHEET    1 AA3 4 TYR A 128  PRO A 132  0                                        
SHEET    2 AA3 4 GLU A  28  ILE A  38 -1  N  VAL A  29   O  HIS A 131           
SHEET    3 AA3 4 LYS A 340  LYS A 344 -1  O  ILE A 343   N  VAL A  36           
SHEET    4 AA3 4 VAL A 315  ASP A 320  1  N  TYR A 319   O  LYS A 344           
SHEET    1 AA4 2 GLY A  92  VAL A  93  0                                        
SHEET    2 AA4 2 ASP A 113  PHE A 114 -1  O  ASP A 113   N  VAL A  93           
SHEET    1 AA5 6 VAL A 216  ASN A 219  0                                        
SHEET    2 AA5 6 GLU A 195  ASP A 200  1  N  VAL A 198   O  ILE A 218           
SHEET    3 AA5 6 LYS A 171  LEU A 175  1  N  ILE A 174   O  ALA A 197           
SHEET    4 AA5 6 ALA A 238  GLU A 243  1  O  PHE A 242   N  LEU A 175           
SHEET    5 AA5 6 VAL A 258  VAL A 267  1  O  MET A 265   N  GLU A 243           
SHEET    6 AA5 6 THR A 286  VAL A 290  1  O  THR A 286   N  ILE A 264           
SHEET    1 AA6 2 ASN B   3  VAL B  10  0                                        
SHEET    2 AA6 2 THR B  13  ALA B  19 -1  O  LYS B  15   N  ILE B   7           
SHEET    1 AA7 5 TYR B 128  PRO B 132  0                                        
SHEET    2 AA7 5 GLU B  28  ILE B  38 -1  N  ILE B  31   O  LEU B 129           
SHEET    3 AA7 5 GLU B  66  VAL B  74 -1  O  ALA B  73   N  LEU B  30           
SHEET    4 AA7 5 ARG B  86  ILE B  89 -1  O  VAL B  87   N  GLY B  69           
SHEET    5 AA7 5 THR B 136  LYS B 138 -1  O  TYR B 137   N  ASN B  88           
SHEET    1 AA8 4 TYR B 128  PRO B 132  0                                        
SHEET    2 AA8 4 GLU B  28  ILE B  38 -1  N  ILE B  31   O  LEU B 129           
SHEET    3 AA8 4 LYS B 340  LYS B 344 -1  O  ILE B 343   N  VAL B  36           
SHEET    4 AA8 4 VAL B 315  ASP B 320  1  N  TYR B 319   O  LYS B 344           
SHEET    1 AA9 2 GLY B  92  VAL B  93  0                                        
SHEET    2 AA9 2 ASP B 113  PHE B 114 -1  O  ASP B 113   N  VAL B  93           
SHEET    1 AB1 6 VAL B 216  ASN B 219  0                                        
SHEET    2 AB1 6 ILE B 196  ASP B 200  1  N  VAL B 198   O  ILE B 218           
SHEET    3 AB1 6 ILE B 172  LEU B 175  1  N  ILE B 172   O  ALA B 197           
SHEET    4 AB1 6 ALA B 238  GLU B 243  1  O  PHE B 242   N  LEU B 175           
SHEET    5 AB1 6 VAL B 258  VAL B 267  1  O  MET B 265   N  GLU B 243           
SHEET    6 AB1 6 THR B 286  VAL B 290  1  O  THR B 286   N  ILE B 264           
LINK         C   ILE A  38                 N   CSO A  39     1555   1555  1.34  
LINK         C   CSO A  39                 N   GLY A  40     1555   1555  1.33  
LINK         OE1 GLU A  66                MG    MG A 401     1555   1555  2.26  
LINK         SG  CYS A  95                ZN    ZN A 402     1555   1555  2.37  
LINK         SG  CYS A  98                ZN    ZN A 402     1555   1555  2.34  
LINK         SG  CYS A 101                ZN    ZN A 402     1555   1555  2.42  
LINK         SG  CYS A 109                ZN    ZN A 402     1555   1555  2.30  
LINK         OE1 GLU A 152                MG    MG A 401     1555   1555  2.03  
LINK         C   ILE B  38                 N  ACSO B  39     1555   1555  1.33  
LINK         C   ILE B  38                 N  BCSO B  39     1555   1555  1.33  
LINK         C  ACSO B  39                 N   GLY B  40     1555   1555  1.33  
LINK         C  BCSO B  39                 N   GLY B  40     1555   1555  1.34  
LINK         OE1 GLU B  66                MG    MG B 401     1555   1555  2.29  
LINK         SG  CYS B  95                ZN    ZN B 402     1555   1555  2.37  
LINK         SG  CYS B  98                ZN    ZN B 402     1555   1555  2.38  
LINK         SG  CYS B 101                ZN    ZN B 402     1555   1555  2.38  
LINK         SG  CYS B 109                ZN    ZN B 402     1555   1555  2.31  
LINK         OE1 GLU B 152                MG    MG B 401     1555   1555  2.12  
LINK        MG    MG A 401                 O   HOH A 705     1555   1555  1.91  
LINK        MG    MG B 401                 O   HOH B 650     1555   1555  1.94  
SITE     1 AC1  4 HIS A  65  GLU A  66  GLU A 152  HOH A 705                    
SITE     1 AC2  4 CYS A  95  CYS A  98  CYS A 101  CYS A 109                    
SITE     1 AC3  5 CSO B  39  HIS B  65  GLU B  66  GLU B 152                    
SITE     2 AC3  5 HOH B 650                                                     
SITE     1 AC4  4 CYS B  95  CYS B  98  CYS B 101  CYS B 109                    
SITE     1 AC5  3 LYS B 312  SER B 313  VAL B 315                               
CRYST1   63.994   70.888  149.460  90.00  90.00  90.00 P 2 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      0.015626  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014107  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006691        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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