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Database: PDB
Entry: 3LWB
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HEADER    LIGASE                                  23-FEB-10   3LWB              
TITLE     CRYSTAL STRUCTURE OF APO D-ALANINE:D-ALANINE LIGASE (DDL) FROM        
TITLE    2 MYCOBACTERIUM TUBERCULOSIS                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: D-ALANYLALANINE SYNTHETASE, D-ALA-D-ALA LIGASE;             
COMPND   5 EC: 6.3.2.4;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 GENE: DDL, DDLA, MT3059, MTCY349.06, RV2981C;                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PVP16                                     
KEYWDS    D-ALANINE--D-ALANINE LIGASE, DDL, D-ALANYL--D-ALANINE LIGASE,         
KEYWDS   2 RV2981C, D-ALANINE, STRUCTURAL GENOMICS, TB STRUCTURAL GENOMICS      
KEYWDS   3 CONSORTIUM, TBSGC, ATP-BINDING, CELL SHAPE, CELL WALL BIOGENESIS,    
KEYWDS   4 DEGRADATION, LIGASE, MAGNESIUM, MANGANESE, METAL-BINDING,            
KEYWDS   5 NUCLEOTIDE-BINDING, PEPTIDOGLYCAN SYNTHESIS                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.B.BRUNING,A.C.MURILLO,O.CHACON,R.G.BARLETTA,J.C.SACCHETTINI,TB      
AUTHOR   2 STRUCTURAL GENOMICS CONSORTIUM (TBSGC)                               
REVDAT   4   08-NOV-17 3LWB    1       REMARK                                   
REVDAT   3   05-JAN-11 3LWB    1       JRNL                                     
REVDAT   2   08-DEC-10 3LWB    1       JRNL                                     
REVDAT   1   09-MAR-10 3LWB    0                                                
JRNL        AUTH   J.B.BRUNING,A.C.MURILLO,O.CHACON,R.G.BARLETTA,               
JRNL        AUTH 2 J.C.SACCHETTINI                                              
JRNL        TITL   STRUCTURE OF THE MYCOBACTERIUM TUBERCULOSIS                  
JRNL        TITL 2 D-ALANINE:D-ALANINE LIGASE, A TARGET OF THE ANTITUBERCULOSIS 
JRNL        TITL 3 DRUG D-CYCLOSERINE.                                          
JRNL        REF    ANTIMICROB.AGENTS CHEMOTHER.  V.  55   291 2011              
JRNL        REFN                   ISSN 0066-4804                               
JRNL        PMID   20956591                                                     
JRNL        DOI    10.1128/AAC.00558-10                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.20                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 38758                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.890                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1896                            
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 19.2040 -  8.5520    0.93      569     0  0.1700 0.0000        
REMARK   3     2  8.5520 -  6.8910    0.95      585     0  0.1540 0.0000        
REMARK   3     3  6.8910 -  6.0510    0.94      566     0  0.1820 0.0000        
REMARK   3     4  6.0510 -  5.5120    0.95      566     0  0.1900 0.0000        
REMARK   3     5  5.5120 -  5.1250    0.95      550     0  0.1670 0.0000        
REMARK   3     6  5.1250 -  4.8280    0.95      581     0  0.1450 0.0000        
REMARK   3     7  4.8280 -  4.5890    0.94      540     0  0.1320 0.0000        
REMARK   3     8  4.5890 -  4.3920    0.94      565     0  0.1290 0.0000        
REMARK   3     9  4.3920 -  4.2250    0.94      566     0  0.1440 0.0000        
REMARK   3    10  4.2250 -  4.0810    0.94      550     0  0.1470 0.0000        
REMARK   3    11  4.0810 -  3.9540    0.94      559     0  0.1490 0.0000        
REMARK   3    12  3.9540 -  3.8420    0.93      556     0  0.1420 0.0000        
REMARK   3    13  3.8420 -  3.7420    0.94      546     0  0.1520 0.0000        
REMARK   3    14  3.7420 -  3.6510    0.94      549     0  0.1610 0.0000        
REMARK   3    15  3.6510 -  3.5690    0.94      568     0  0.1660 0.0000        
REMARK   3    16  3.5690 -  3.4930    0.94      567     0  0.1480 0.0000        
REMARK   3    17  3.4930 -  3.4240    0.94      530     0  0.1640 0.0000        
REMARK   3    18  3.4240 -  3.3590    0.92      565     0  0.1660 0.0000        
REMARK   3    19  3.3590 -  3.3000    0.93      552     0  0.1670 0.0000        
REMARK   3    20  3.3000 -  3.2440    0.93      530     0  0.1830 0.0000        
REMARK   3    21  3.2440 -  3.1920    0.93      551     0  0.1830 0.0000        
REMARK   3    22  3.1920 -  3.1430    0.94      561     0  0.1670 0.0000        
REMARK   3    23  3.1430 -  3.0970    0.91      536     0  0.1710 0.0000        
REMARK   3    24  3.0970 -  3.0530    0.93      535     0  0.1790 0.0000        
REMARK   3    25  3.0530 -  3.0120    0.91      548     0  0.1910 0.0000        
REMARK   3    26  3.0120 -  2.9730    0.91      553     0  0.1830 0.0000        
REMARK   3    27  2.9730 -  2.9360    0.90      524     0  0.1860 0.0000        
REMARK   3    28  2.9360 -  2.9010    0.89      527     0  0.1650 0.0000        
REMARK   3    29  2.9010 -  2.8680    0.90      511     0  0.1750 0.0000        
REMARK   3    30  2.8680 -  2.8350    0.87      526     0  0.1860 0.0000        
REMARK   3    31  2.8350 -  2.8050    0.88      519     0  0.1880 0.0000        
REMARK   3    32  2.8050 -  2.7750    0.88      507     0  0.2020 0.0000        
REMARK   3    33  2.7750 -  2.7470    0.88      517     0  0.1790 0.0000        
REMARK   3    34  2.7470 -  2.7200    0.89      512     0  0.1740 0.0000        
REMARK   3    35  2.7200 -  2.6940    0.84      521     0  0.1760 0.0000        
REMARK   3    36  2.6940 -  2.6690    0.85      491     0  0.1880 0.0000        
REMARK   3    37  2.6690 -  2.6450    0.87      532     0  0.1860 0.0000        
REMARK   3    38  2.6450 -  2.6210    0.84      473     0  0.1670 0.0000        
REMARK   3    39  2.6210 -  2.5990    0.86      507     0  0.1740 0.0000        
REMARK   3    40  2.5990 -  2.5770    0.86      508     0  0.1860 0.0000        
REMARK   3    41  2.5770 -  2.5560    0.82      487     0  0.1850 0.0000        
REMARK   3    42  2.5560 -  2.5350    0.83      492     0  0.1900 0.0000        
REMARK   3    43  2.5350 -  2.5160    0.82      486     0  0.1680 0.0000        
REMARK   3    44  2.5160 -  2.4960    0.83      483     0  0.1590 0.0000        
REMARK   3    45  2.4960 -  2.4780    0.85      483     0  0.1700 0.0000        
REMARK   3    46  2.4780 -  2.4600    0.82      470     0  0.1650 0.0000        
REMARK   3    47  2.4600 -  2.4420    0.79      500     0  0.1800 0.0000        
REMARK   3    48  2.4420 -  2.4250    0.80      468     0  0.1750 0.0000        
REMARK   3    49  2.4250 -  2.4090    0.80      476     0  0.1580 0.0000        
REMARK   3    50  2.4090 -  2.3920    0.81      454     0  0.1720 0.0000        
REMARK   3    51  2.3920 -  2.3770    0.80      459     0  0.1780 0.0000        
REMARK   3    52  2.3770 -  2.3620    0.81      491     0  0.1710 0.0000        
REMARK   3    53  2.3620 -  2.3460    0.79      463     0  0.1700 0.0000        
REMARK   3    54  2.3460 -  2.3320    0.76      456     0  0.1770 0.0000        
REMARK   3    55  2.3320 -  2.3180    0.80      457     0  0.1900 0.0000        
REMARK   3    56  2.3180 -  2.3040    0.76      447     0  0.1900 0.0000        
REMARK   3    57  2.3040 -  2.2900    0.78      476     0  0.2060 0.0000        
REMARK   3    58  2.2900 -  2.2770    0.76      440     0  0.1950 0.0000        
REMARK   3    59  2.2770 -  2.2640    0.77      431     0  0.2000 0.0000        
REMARK   3    60  2.2640 -  2.2520    0.81      476     0  0.2250 0.0000        
REMARK   3    61  2.2520 -  2.2390    0.75      452     0  0.2310 0.0000        
REMARK   3    62  2.2390 -  2.2270    0.69      390     0  0.2220 0.0000        
REMARK   3    63  2.2270 -  2.2150    0.75      472     0  0.2200 0.0000        
REMARK   3    64  2.2150 -  2.2040    0.76      426     0  0.2240 0.0000        
REMARK   3    65  2.2040 -  2.1930    0.77      465     0  0.2350 0.0000        
REMARK   3    66  2.1930 -  2.1810    0.74      420     0  0.2450 0.0000        
REMARK   3    67  2.1810 -  2.1710    0.73      427     0  0.2470 0.0000        
REMARK   3    68  2.1710 -  2.1600    0.72      411     0  0.2590 0.0000        
REMARK   3    69  2.1600 -  2.1490    0.70      415     0  0.2500 0.0000        
REMARK   3    70  2.1490 -  2.1390    0.70      424     0  0.2690 0.0000        
REMARK   3    71  2.1390 -  2.1290    0.73      423     0  0.2660 0.0000        
REMARK   3    72  2.1290 -  2.1190    0.69      415     0  0.2690 0.0000        
REMARK   3    73  2.1190 -  2.1090    0.65      373     0  0.3020 0.0000        
REMARK   3    74  2.1090 -  2.1000    0.57      335     0  0.2910 0.0000        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 66.98                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.16                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.40100                                             
REMARK   3    B22 (A**2) : 0.82000                                              
REMARK   3    B33 (A**2) : -0.42000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.40400                                             
REMARK   3    B23 (A**2) : 0.00000                                              
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           NULL                                  
REMARK   3   ANGLE     :  0.622           NULL                                  
REMARK   3   CHIRALITY :  0.046           NULL                                  
REMARK   3   PLANARITY :  0.002           NULL                                  
REMARK   3   DIHEDRAL  :  9.793           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 7:187)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1404  12.0113   1.9266              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1148 T22:   0.0563                                     
REMARK   3      T33:   0.1175 T12:   0.0085                                     
REMARK   3      T13:   0.0032 T23:  -0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8244 L22:   0.8305                                     
REMARK   3      L33:   0.4929 L12:   0.1870                                     
REMARK   3      L13:   0.0426 L23:  -0.1246                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0357 S12:  -0.0533 S13:   0.2260                       
REMARK   3      S21:   0.1454 S22:   0.0107 S23:   0.1164                       
REMARK   3      S31:  -0.1717 S32:  -0.0181 S33:   0.0258                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 188:368)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  16.1267  -3.0499  -2.4732              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1252 T22:   0.0350                                     
REMARK   3      T33:   0.1094 T12:  -0.0032                                     
REMARK   3      T13:   0.0066 T23:  -0.0172                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7541 L22:   0.5992                                     
REMARK   3      L33:   1.0906 L12:  -0.1292                                     
REMARK   3      L13:   0.4830 L23:  -0.7162                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0409 S12:   0.0518 S13:  -0.0571                       
REMARK   3      S21:  -0.0579 S22:  -0.0297 S23:   0.0080                       
REMARK   3      S31:   0.2010 S32:   0.0277 S33:  -0.0099                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 10:129)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  18.1185  20.5808  33.6831              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7596 T22:   0.7020                                     
REMARK   3      T33:   0.5283 T12:  -0.0817                                     
REMARK   3      T13:   0.1832 T23:  -0.1233                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7205 L22:   0.6435                                     
REMARK   3      L33:   1.4012 L12:   0.0973                                     
REMARK   3      L13:  -2.4217 L23:  -0.3755                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5905 S12:  -0.1627 S13:   0.4739                       
REMARK   3      S21:  -0.3491 S22:   0.1334 S23:  -0.0767                       
REMARK   3      S31:  -0.6788 S32:   0.4941 S33:  -0.4717                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 130:373)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6611   6.4360  25.1753              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0968 T22:   0.1513                                     
REMARK   3      T33:   0.1029 T12:   0.0526                                     
REMARK   3      T13:   0.0147 T23:  -0.0101                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1168 L22:   0.4999                                     
REMARK   3      L33:   2.4430 L12:   0.0291                                     
REMARK   3      L13:   0.2416 L23:   0.0677                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0058 S12:  -0.0947 S13:   0.0452                       
REMARK   3      S21:   0.0461 S22:   0.0493 S23:   0.0120                       
REMARK   3      S31:   0.1143 S32:   0.2030 S33:  -0.0403                       
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 3LWB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000057810.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96411                            
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40957                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : 0.05200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.40600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: HOMOLOGY MODEL DERIVED FROM PDB ENTRY 2I87           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: WELL SOLUTION CONSISTED OF 20% PEG       
REMARK 280  3350, 0.1M POTASSIUM NITRATE. 1UL OF WELL SOLUTION WAS MIXED        
REMARK 280  WITH 1UL PROTEIN SOLUTION (10MG/ML) AND EQUILIBRATED OVER 500UL     
REMARK 280  WELL SOLUTION., PH 8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       54.15100            
REMARK 290   SMTRY3   2  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: 2100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     ARG A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     ASN A    22                                                      
REMARK 465     GLU A    23                                                      
REMARK 465     HIS A    24                                                      
REMARK 465     PRO A    63                                                      
REMARK 465     ASP A    64                                                      
REMARK 465     ALA A    65                                                      
REMARK 465     LEU A    66                                                      
REMARK 465     THR A    67                                                      
REMARK 465     ILE A    68                                                      
REMARK 465     THR A    69                                                      
REMARK 465     ASN A    70                                                      
REMARK 465     ARG A    71                                                      
REMARK 465     GLU A    72                                                      
REMARK 465     LEU A    73                                                      
REMARK 465     PRO A    74                                                      
REMARK 465     GLN A    75                                                      
REMARK 465     VAL A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     SER A    78                                                      
REMARK 465     GLY A    79                                                      
REMARK 465     SER A    80                                                      
REMARK 465     GLY A    81                                                      
REMARK 465     THR A    82                                                      
REMARK 465     GLU A    83                                                      
REMARK 465     LEU A    84                                                      
REMARK 465     ALA A    85                                                      
REMARK 465     LEU A    86                                                      
REMARK 465     PRO A    87                                                      
REMARK 465     ALA A    88                                                      
REMARK 465     ASP A    89                                                      
REMARK 465     PRO A    90                                                      
REMARK 465     ARG A    91                                                      
REMARK 465     ARG A    92                                                      
REMARK 465     GLY A    93                                                      
REMARK 465     GLY A    94                                                      
REMARK 465     GLN A    95                                                      
REMARK 465     LEU A    96                                                      
REMARK 465     GLY A   369                                                      
REMARK 465     VAL A   370                                                      
REMARK 465     GLY A   371                                                      
REMARK 465     LEU A   372                                                      
REMARK 465     HIS A   373                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     ASN B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     ARG B     7                                                      
REMARK 465     ASP B     8                                                      
REMARK 465     ARG B     9                                                      
REMARK 465     GLY B    18                                                      
REMARK 465     GLY B    19                                                      
REMARK 465     ARG B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     ASN B    22                                                      
REMARK 465     GLU B    23                                                      
REMARK 465     ALA B    53                                                      
REMARK 465     GLY B    54                                                      
REMARK 465     SER B    55                                                      
REMARK 465     TRP B    56                                                      
REMARK 465     VAL B    57                                                      
REMARK 465     LEU B    58                                                      
REMARK 465     THR B    59                                                      
REMARK 465     ASP B    60                                                      
REMARK 465     ALA B    61                                                      
REMARK 465     ASN B    62                                                      
REMARK 465     PRO B    63                                                      
REMARK 465     ASP B    64                                                      
REMARK 465     ALA B    65                                                      
REMARK 465     LEU B    66                                                      
REMARK 465     THR B    67                                                      
REMARK 465     ILE B    68                                                      
REMARK 465     THR B    69                                                      
REMARK 465     ASN B    70                                                      
REMARK 465     ARG B    71                                                      
REMARK 465     GLU B    72                                                      
REMARK 465     LEU B    73                                                      
REMARK 465     PRO B    74                                                      
REMARK 465     GLN B    75                                                      
REMARK 465     VAL B    76                                                      
REMARK 465     LYS B    77                                                      
REMARK 465     SER B    78                                                      
REMARK 465     GLY B    79                                                      
REMARK 465     SER B    80                                                      
REMARK 465     GLY B    81                                                      
REMARK 465     THR B    82                                                      
REMARK 465     GLU B    83                                                      
REMARK 465     LEU B    84                                                      
REMARK 465     ALA B    85                                                      
REMARK 465     LEU B    86                                                      
REMARK 465     PRO B    87                                                      
REMARK 465     ALA B    88                                                      
REMARK 465     ASP B    89                                                      
REMARK 465     PRO B    90                                                      
REMARK 465     ARG B    91                                                      
REMARK 465     ARG B    92                                                      
REMARK 465     GLY B    93                                                      
REMARK 465     GLY B    94                                                      
REMARK 465     GLN B    95                                                      
REMARK 465     LEU B    96                                                      
REMARK 465     VAL B    97                                                      
REMARK 465     SER B    98                                                      
REMARK 465     LEU B    99                                                      
REMARK 465     PRO B   100                                                      
REMARK 465     PRO B   101                                                      
REMARK 465     GLY B   102                                                      
REMARK 465     ALA B   103                                                      
REMARK 465     GLY B   104                                                      
REMARK 465     GLU B   105                                                      
REMARK 465     GLY B   119                                                      
REMARK 465     PRO B   120                                                      
REMARK 465     TYR B   121                                                      
REMARK 465     GLY B   122                                                      
REMARK 465     GLU B   123                                                      
REMARK 465     ASP B   124                                                      
REMARK 465     GLY B   125                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A   7    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A   8    CG   OD1  OD2                                       
REMARK 470     ARG A   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A  26    CG1  CG2  CD1                                       
REMARK 470     VAL A  97    CB   CG1  CG2                                       
REMARK 470     SER A  98    CB   OG                                             
REMARK 470     LEU A  99    CG   CD1  CD2                                       
REMARK 470     MET A 150    CG   SD   CE                                        
REMARK 470     HIS A 180    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 181    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 182    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 185    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 263    CG1  CG2                                            
REMARK 470     ARG A 266    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  10    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  12    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B  15    CG1  CG2                                            
REMARK 470     VAL B  16    CG1  CG2                                            
REMARK 470     HIS B  24    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ILE B  26    CG1  CG2  CD1                                       
REMARK 470     SER B  27    OG                                                  
REMARK 470     VAL B  29    CG1  CG2                                            
REMARK 470     SER B  33    OG                                                  
REMARK 470     ARG B  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  41    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B  46    CG1  CG2  CD1                                       
REMARK 470     ILE B  50    CG1  CG2  CD1                                       
REMARK 470     PRO B  52    CG   CD                                             
REMARK 470     VAL B 106    CG1  CG2                                            
REMARK 470     LEU B 107    CG   CD1  CD2                                       
REMARK 470     VAL B 116    CG1  CG2                                            
REMARK 470     LEU B 117    CG   CD1  CD2                                       
REMARK 470     HIS B 118    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR B 126    OG1  CG2                                            
REMARK 470     ILE B 127    CG1  CG2  CD1                                       
REMARK 470     GLN B 182    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 263    CG1  CG2                                            
REMARK 470     ARG B 264    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 266    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 280    CG   OD1  OD2                                       
REMARK 470     GLN B 293    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 370    CG1  CG2                                            
REMARK 470     HIS B 373    CG   ND1  CD2  CE1  NE2                             
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    ASN A  62   N   -  CA  -  C   ANGL. DEV. = -20.9 DEGREES          
REMARK 500    PRO B  52   N   -  CA  -  CB  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    PRO B  52   N   -  CA  -  C   ANGL. DEV. = -21.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP B  39      101.63    -47.37                                   
REMARK 500    THR B  51      158.03    -44.06                                   
REMARK 500    LEU B 107      158.85     73.79                                   
REMARK 500    GLU B 108     -179.95     74.45                                   
REMARK 500    SER B 109       -5.22     58.08                                   
REMARK 500    VAL B 143      -78.39    -41.96                                   
REMARK 500    SER B 200       74.25   -106.56                                   
REMARK 500    SER B 201      -51.24   -147.07                                   
REMARK 500    ALA B 261      150.93     70.46                                   
REMARK 500    VAL B 263     -171.40    165.81                                   
REMARK 500    ARG B 264      -70.10   -101.37                                   
REMARK 500    ARG B 266        3.73     51.62                                   
REMARK 500    ARG B 368      -60.83    -95.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR B   51     PRO B   52                 -135.78                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 374                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 374                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: RV2981C   RELATED DB: TARGETDB                           
DBREF  3LWB A    1   373  UNP    P95114   DDL_MYCTU        1    373             
DBREF  3LWB B    1   373  UNP    P95114   DDL_MYCTU        1    373             
SEQRES   1 A  373  MET SER ALA ASN ASP ARG ARG ASP ARG ARG VAL ARG VAL          
SEQRES   2 A  373  ALA VAL VAL PHE GLY GLY ARG SER ASN GLU HIS ALA ILE          
SEQRES   3 A  373  SER CYS VAL SER ALA GLY SER ILE LEU ARG ASN LEU ASP          
SEQRES   4 A  373  SER ARG ARG PHE ASP VAL ILE ALA VAL GLY ILE THR PRO          
SEQRES   5 A  373  ALA GLY SER TRP VAL LEU THR ASP ALA ASN PRO ASP ALA          
SEQRES   6 A  373  LEU THR ILE THR ASN ARG GLU LEU PRO GLN VAL LYS SER          
SEQRES   7 A  373  GLY SER GLY THR GLU LEU ALA LEU PRO ALA ASP PRO ARG          
SEQRES   8 A  373  ARG GLY GLY GLN LEU VAL SER LEU PRO PRO GLY ALA GLY          
SEQRES   9 A  373  GLU VAL LEU GLU SER VAL ASP VAL VAL PHE PRO VAL LEU          
SEQRES  10 A  373  HIS GLY PRO TYR GLY GLU ASP GLY THR ILE GLN GLY LEU          
SEQRES  11 A  373  LEU GLU LEU ALA GLY VAL PRO TYR VAL GLY ALA GLY VAL          
SEQRES  12 A  373  LEU ALA SER ALA VAL GLY MET ASP LYS GLU PHE THR LYS          
SEQRES  13 A  373  LYS LEU LEU ALA ALA ASP GLY LEU PRO VAL GLY ALA TYR          
SEQRES  14 A  373  ALA VAL LEU ARG PRO PRO ARG SER THR LEU HIS ARG GLN          
SEQRES  15 A  373  GLU CYS GLU ARG LEU GLY LEU PRO VAL PHE VAL LYS PRO          
SEQRES  16 A  373  ALA ARG GLY GLY SER SER ILE GLY VAL SER ARG VAL SER          
SEQRES  17 A  373  SER TRP ASP GLN LEU PRO ALA ALA VAL ALA ARG ALA ARG          
SEQRES  18 A  373  ARG HIS ASP PRO LYS VAL ILE VAL GLU ALA ALA ILE SER          
SEQRES  19 A  373  GLY ARG GLU LEU GLU CYS GLY VAL LEU GLU MET PRO ASP          
SEQRES  20 A  373  GLY THR LEU GLU ALA SER THR LEU GLY GLU ILE ARG VAL          
SEQRES  21 A  373  ALA GLY VAL ARG GLY ARG GLU ASP SER PHE TYR ASP PHE          
SEQRES  22 A  373  ALA THR LYS TYR LEU ASP ASP ALA ALA GLU LEU ASP VAL          
SEQRES  23 A  373  PRO ALA LYS VAL ASP ASP GLN VAL ALA GLU ALA ILE ARG          
SEQRES  24 A  373  GLN LEU ALA ILE ARG ALA PHE ALA ALA ILE ASP CYS ARG          
SEQRES  25 A  373  GLY LEU ALA ARG VAL ASP PHE PHE LEU THR ASP ASP GLY          
SEQRES  26 A  373  PRO VAL ILE ASN GLU ILE ASN THR MET PRO GLY PHE THR          
SEQRES  27 A  373  THR ILE SER MET TYR PRO ARG MET TRP ALA ALA SER GLY          
SEQRES  28 A  373  VAL ASP TYR PRO THR LEU LEU ALA THR MET ILE GLU THR          
SEQRES  29 A  373  THR LEU ALA ARG GLY VAL GLY LEU HIS                          
SEQRES   1 B  373  MET SER ALA ASN ASP ARG ARG ASP ARG ARG VAL ARG VAL          
SEQRES   2 B  373  ALA VAL VAL PHE GLY GLY ARG SER ASN GLU HIS ALA ILE          
SEQRES   3 B  373  SER CYS VAL SER ALA GLY SER ILE LEU ARG ASN LEU ASP          
SEQRES   4 B  373  SER ARG ARG PHE ASP VAL ILE ALA VAL GLY ILE THR PRO          
SEQRES   5 B  373  ALA GLY SER TRP VAL LEU THR ASP ALA ASN PRO ASP ALA          
SEQRES   6 B  373  LEU THR ILE THR ASN ARG GLU LEU PRO GLN VAL LYS SER          
SEQRES   7 B  373  GLY SER GLY THR GLU LEU ALA LEU PRO ALA ASP PRO ARG          
SEQRES   8 B  373  ARG GLY GLY GLN LEU VAL SER LEU PRO PRO GLY ALA GLY          
SEQRES   9 B  373  GLU VAL LEU GLU SER VAL ASP VAL VAL PHE PRO VAL LEU          
SEQRES  10 B  373  HIS GLY PRO TYR GLY GLU ASP GLY THR ILE GLN GLY LEU          
SEQRES  11 B  373  LEU GLU LEU ALA GLY VAL PRO TYR VAL GLY ALA GLY VAL          
SEQRES  12 B  373  LEU ALA SER ALA VAL GLY MET ASP LYS GLU PHE THR LYS          
SEQRES  13 B  373  LYS LEU LEU ALA ALA ASP GLY LEU PRO VAL GLY ALA TYR          
SEQRES  14 B  373  ALA VAL LEU ARG PRO PRO ARG SER THR LEU HIS ARG GLN          
SEQRES  15 B  373  GLU CYS GLU ARG LEU GLY LEU PRO VAL PHE VAL LYS PRO          
SEQRES  16 B  373  ALA ARG GLY GLY SER SER ILE GLY VAL SER ARG VAL SER          
SEQRES  17 B  373  SER TRP ASP GLN LEU PRO ALA ALA VAL ALA ARG ALA ARG          
SEQRES  18 B  373  ARG HIS ASP PRO LYS VAL ILE VAL GLU ALA ALA ILE SER          
SEQRES  19 B  373  GLY ARG GLU LEU GLU CYS GLY VAL LEU GLU MET PRO ASP          
SEQRES  20 B  373  GLY THR LEU GLU ALA SER THR LEU GLY GLU ILE ARG VAL          
SEQRES  21 B  373  ALA GLY VAL ARG GLY ARG GLU ASP SER PHE TYR ASP PHE          
SEQRES  22 B  373  ALA THR LYS TYR LEU ASP ASP ALA ALA GLU LEU ASP VAL          
SEQRES  23 B  373  PRO ALA LYS VAL ASP ASP GLN VAL ALA GLU ALA ILE ARG          
SEQRES  24 B  373  GLN LEU ALA ILE ARG ALA PHE ALA ALA ILE ASP CYS ARG          
SEQRES  25 B  373  GLY LEU ALA ARG VAL ASP PHE PHE LEU THR ASP ASP GLY          
SEQRES  26 B  373  PRO VAL ILE ASN GLU ILE ASN THR MET PRO GLY PHE THR          
SEQRES  27 B  373  THR ILE SER MET TYR PRO ARG MET TRP ALA ALA SER GLY          
SEQRES  28 B  373  VAL ASP TYR PRO THR LEU LEU ALA THR MET ILE GLU THR          
SEQRES  29 B  373  THR LEU ALA ARG GLY VAL GLY LEU HIS                          
HET    NO3  A 374       4                                                       
HET    NO3  B 374       4                                                       
HETNAM     NO3 NITRATE ION                                                      
FORMUL   3  NO3    2(N O3 1-)                                                   
FORMUL   5  HOH   *383(H2 O)                                                    
HELIX    1   1 ALA A   25  LEU A   38  1                                  14    
HELIX    2   2 GLY A  102  SER A  109  1                                   8    
HELIX    3   3 GLY A  125  GLY A  135  1                                  11    
HELIX    4   4 GLY A  142  ASP A  151  1                                  10    
HELIX    5   5 ASP A  151  ASP A  162  1                                  12    
HELIX    6   6 HIS A  180  GLY A  188  1                                   9    
HELIX    7   7 SER A  209  ASP A  211  5                                   3    
HELIX    8   8 GLN A  212  ARG A  222  1                                  11    
HELIX    9   9 ASP A  272  LEU A  278  1                                   7    
HELIX   10  10 ASP A  291  ILE A  309  1                                  19    
HELIX   11  11 SER A  341  SER A  350  1                                  10    
HELIX   12  12 ASP A  353  ARG A  368  1                                  16    
HELIX   13  13 ALA B   25  LEU B   38  1                                  14    
HELIX   14  14 THR B  126  LEU B  133  1                                   8    
HELIX   15  15 GLY B  142  ASP B  151  1                                  10    
HELIX   16  16 ASP B  151  ASP B  162  1                                  12    
HELIX   17  17 HIS B  180  GLY B  188  1                                   9    
HELIX   18  18 SER B  209  ASP B  211  5                                   3    
HELIX   19  19 GLN B  212  ARG B  222  1                                  11    
HELIX   20  20 ASP B  272  ASP B  279  1                                   8    
HELIX   21  21 ASP B  291  ILE B  309  1                                  19    
HELIX   22  22 SER B  341  ALA B  349  1                                   9    
HELIX   23  23 ASP B  353  GLY B  369  1                                  17    
SHEET    1   A 4 TRP A  56  THR A  59  0                                        
SHEET    2   A 4 PHE A  43  ILE A  50 -1  N  GLY A  49   O  VAL A  57           
SHEET    3   A 4 VAL A  11  GLY A  18  1  N  VAL A  11   O  ASP A  44           
SHEET    4   A 4 VAL A 112  PRO A 115  1  O  PHE A 114   N  ALA A  14           
SHEET    1   B 2 HIS A 118  GLY A 119  0                                        
SHEET    2   B 2 GLY A 122  GLU A 123 -1  O  GLY A 122   N  GLY A 119           
SHEET    1   C 4 TYR A 169  LEU A 172  0                                        
SHEET    2   C 4 VAL A 227  ALA A 231 -1  O  VAL A 227   N  LEU A 172           
SHEET    3   C 4 VAL A 191  PRO A 195 -1  N  LYS A 194   O  ILE A 228           
SHEET    4   C 4 SER A 205  VAL A 207 -1  O  VAL A 207   N  VAL A 191           
SHEET    1   D 4 LEU A 250  ALA A 252  0                                        
SHEET    2   D 4 SER A 234  GLU A 244 -1  N  LEU A 243   O  GLU A 251           
SHEET    3   D 4 GLY A 256  ARG A 259 -1  O  GLY A 256   N  GLU A 239           
SHEET    4   D 4 GLU A 283  ASP A 285 -1  O  ASP A 285   N  GLU A 257           
SHEET    1   E 4 GLU A 267  ASP A 268  0                                        
SHEET    2   E 4 SER A 234  GLU A 244 -1  N  GLY A 235   O  GLU A 267           
SHEET    3   E 4 LEU A 314  THR A 322 -1  O  PHE A 319   N  LEU A 238           
SHEET    4   E 4 GLY A 325  ASN A 332 -1  O  ASN A 332   N  ARG A 316           
SHEET    1   F 3 PHE B  43  VAL B  48  0                                        
SHEET    2   F 3 VAL B  11  VAL B  16  1  N  VAL B  13   O  ASP B  44           
SHEET    3   F 3 VAL B 112  PRO B 115  1  O  PHE B 114   N  ALA B  14           
SHEET    1   G 4 TYR B 169  LEU B 172  0                                        
SHEET    2   G 4 VAL B 227  ALA B 231 -1  O  VAL B 227   N  LEU B 172           
SHEET    3   G 4 VAL B 191  PRO B 195 -1  N  PHE B 192   O  GLU B 230           
SHEET    4   G 4 SER B 205  VAL B 207 -1  O  VAL B 207   N  VAL B 191           
SHEET    1   H 4 LEU B 250  ALA B 252  0                                        
SHEET    2   H 4 SER B 234  GLU B 244 -1  N  LEU B 243   O  GLU B 251           
SHEET    3   H 4 GLY B 256  ARG B 259 -1  O  GLY B 256   N  GLU B 239           
SHEET    4   H 4 GLU B 283  ASP B 285 -1  O  ASP B 285   N  GLU B 257           
SHEET    1   I 4 GLU B 267  ASP B 268  0                                        
SHEET    2   I 4 SER B 234  GLU B 244 -1  N  GLY B 235   O  GLU B 267           
SHEET    3   I 4 LEU B 314  THR B 322 -1  O  PHE B 319   N  LEU B 238           
SHEET    4   I 4 GLY B 325  ASN B 332 -1  O  ASN B 332   N  ARG B 316           
CISPEP   1 PRO A  174    PRO A  175          0         3.69                     
CISPEP   2 LEU A  189    PRO A  190          0        -1.66                     
CISPEP   3 VAL A  286    PRO A  287          0         6.23                     
CISPEP   4 LEU B  107    GLU B  108          0        10.85                     
CISPEP   5 PRO B  174    PRO B  175          0         4.54                     
CISPEP   6 LEU B  189    PRO B  190          0        -0.93                     
CISPEP   7 VAL B  286    PRO B  287          0         1.71                     
CISPEP   8 GLY B  369    VAL B  370          0         0.85                     
SITE     1 AC1  6 ARG A 316  PRO A 335  GLY A 336  SER A 341                    
SITE     2 AC1  6 MET A 342  TYR A 343                                          
SITE     1 AC2  5 ARG B 316  PRO B 335  GLY B 336  MET B 342                    
SITE     2 AC2  5 TYR B 343                                                     
CRYST1   51.720  108.302   69.064  90.00  99.92  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019335  0.000000  0.003382        0.00000                         
SCALE2      0.000000  0.009233  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014699        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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