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Database: PDB
Entry: 5XGQ
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Original site: 5XGQ 
HEADER    LIGASE                                  15-APR-17   5XGQ              
TITLE     CRYSTAL STRUCTURE OF APO FORM (FREE-STATE) MYCOBACTERIUM TUBERCULOSIS 
TITLE    2 METHIONYL-TRNA SYNTHETASE                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METHIONINE-TRNA LIGASE;                                    
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 SYNONYM: METHIONYL-TRNA SYNTHETASE,METRS;                            
COMPND   5 EC: 6.1.1.10;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25177 / 
SOURCE   3 H37RA);                                                              
SOURCE   4 ORGANISM_TAXID: 419947;                                              
SOURCE   5 STRAIN: ATCC 25177 / H37RA;                                          
SOURCE   6 GENE: METG, MRA_1016;                                                
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD (DE3)PLYSS AG;                   
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    METHIONYL-TRNA SYNTHETASE, PROTEIN TRANSLATION, MYCOBACTERIUM         
KEYWDS   2 TUBERCULOSIS, ANTICODON-BINDING DOMAIN OF TRNA, LIGASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.WANG,M.WANG,J.A.WOJDYLA,S.CUI                                       
REVDAT   2   01-AUG-18 5XGQ    1       JRNL                                     
REVDAT   1   11-JUL-18 5XGQ    0                                                
JRNL        AUTH   W.WANG,B.QIN,J.A.WOJDYLA,M.WANG,X.GAO,S.CUI                  
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF FREE-STATE AND                
JRNL        TITL 2 PRODUCT-STATEMYCOBACTERIUM TUBERCULOSISMETHIONYL-TRNA        
JRNL        TITL 3 SYNTHETASE REVEALS AN INDUCED-FIT LIGAND-RECOGNITION         
JRNL        TITL 4 MECHANISM                                                    
JRNL        REF    IUCRJ                         V.   5   478 2018              
JRNL        REFN                   ESSN 2052-2525                               
JRNL        PMID   30002848                                                     
JRNL        DOI    10.1107/S2052252518008217                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.69                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.290                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 158552                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7918                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.7017 -  5.8986    0.94     5105   266  0.1873 0.1767        
REMARK   3     2  5.8986 -  4.6831    0.94     5083   267  0.1709 0.2016        
REMARK   3     3  4.6831 -  4.0915    0.94     4968   263  0.1435 0.2018        
REMARK   3     4  4.0915 -  3.7175    0.92     4993   258  0.1597 0.1699        
REMARK   3     5  3.7175 -  3.4512    0.92     4928   261  0.1592 0.2027        
REMARK   3     6  3.4512 -  3.2477    0.92     4994   261  0.1714 0.1842        
REMARK   3     7  3.2477 -  3.0851    0.95     5100   267  0.1813 0.2247        
REMARK   3     8  3.0851 -  2.9508    0.95     5098   266  0.1917 0.2249        
REMARK   3     9  2.9508 -  2.8372    0.95     5194   276  0.1832 0.2289        
REMARK   3    10  2.8372 -  2.7393    0.95     5054   262  0.1874 0.2215        
REMARK   3    11  2.7393 -  2.6537    0.94     5057   266  0.2014 0.2634        
REMARK   3    12  2.6537 -  2.5778    0.95     5191   265  0.2115 0.2545        
REMARK   3    13  2.5778 -  2.5100    0.95     5102   266  0.2060 0.2558        
REMARK   3    14  2.5100 -  2.4488    0.95     5088   266  0.2103 0.2718        
REMARK   3    15  2.4488 -  2.3931    0.95     5175   273  0.2077 0.2513        
REMARK   3    16  2.3931 -  2.3422    0.95     5095   268  0.2147 0.2570        
REMARK   3    17  2.3422 -  2.2953    0.94     5141   269  0.2253 0.2832        
REMARK   3    18  2.2953 -  2.2520    0.93     5013   265  0.2353 0.2763        
REMARK   3    19  2.2520 -  2.2118    0.90     4878   254  0.2468 0.2958        
REMARK   3    20  2.2118 -  2.1743    0.94     5020   266  0.2384 0.2627        
REMARK   3    21  2.1743 -  2.1392    0.94     5121   277  0.2470 0.2851        
REMARK   3    22  2.1392 -  2.1063    0.94     5086   264  0.2478 0.2964        
REMARK   3    23  2.1063 -  2.0753    0.93     4981   265  0.2766 0.3227        
REMARK   3    24  2.0753 -  2.0461    0.88     4752   251  0.2934 0.3454        
REMARK   3    25  2.0461 -  2.0184    0.93     4963   262  0.2798 0.2860        
REMARK   3    26  2.0184 -  1.9922    0.95     5163   274  0.2729 0.2942        
REMARK   3    27  1.9922 -  1.9673    0.94     5069   267  0.2983 0.3477        
REMARK   3    28  1.9673 -  1.9436    0.93     5051   272  0.3125 0.3224        
REMARK   3    29  1.9436 -  1.9210    0.94     4935   260  0.3480 0.3345        
REMARK   3    30  1.9210 -  1.8994    0.77     4236   221  0.4069 0.4774        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.150           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.23                          
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      :  0.003           8134                                  
REMARK   3   ANGLE     :  0.589          11083                                  
REMARK   3   CHIRALITY :  0.040           1200                                  
REMARK   3   PLANARITY :  0.004           1453                                  
REMARK   3   DIHEDRAL  : 13.982           4779                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5XGQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-APR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300003416.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-AUG-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000040                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 158725                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.899                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.686                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.1                               
REMARK 200  DATA REDUNDANCY                : 1.680                              
REMARK 200  R MERGE                    (I) : 0.09400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.6800                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.53                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.72300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.970                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 2X1L                                                 
REMARK 200                                                                      
REMARK 200 REMARK: PLATES                                                       
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CALCIUM ACETATE, 0.1M SODIUM        
REMARK 280  CACODYLATE, 16%PEG8000, PH 6.1, EVAPORATION, TEMPERATURE 293K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 APPLY THE FOLLOWING TO CHAINS: B, 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 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 B    -7                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     GLU B    50                                                      
REMARK 465     HIS B    51                                                      
REMARK 465     GLY B    52                                                      
REMARK 465     LEU B    53                                                      
REMARK 465     LYS B    54                                                      
REMARK 465     VAL B    55                                                      
REMARK 465     ALA B    56                                                      
REMARK 465     GLN B    57                                                      
REMARK 465     ALA B    58                                                      
REMARK 465     ALA B    59                                                      
REMARK 465     ALA B    60                                                      
REMARK 465     ALA B    61                                                      
REMARK 465     ALA B    62                                                      
REMARK 465     GLU B   298                                                      
REMARK 465     LYS B   299                                                      
REMARK 465     MET B   300                                                      
REMARK 465     SER B   301                                                      
REMARK 465     LYS B   302                                                      
REMARK 465     SER B   303                                                      
REMARK 465     VAL B   304                                                      
REMARK 465     GLY B   305                                                      
REMARK 465     ASN B   306                                                      
REMARK 465     GLN B   514                                                      
REMARK 465     PRO B   515                                                      
REMARK 465     PRO B   516                                                      
REMARK 465     GLU B   517                                                      
REMARK 465     GLY B   518                                                      
REMARK 465     LYS B   519                                                      
REMARK 465     ARG B   520                                                      
REMARK 465     SER B   521                                                      
REMARK 465     HIS B   522                                                      
REMARK 465     HIS B   523                                                      
REMARK 465     HIS B   524                                                      
REMARK 465     HIS B   525                                                      
REMARK 465     HIS B   526                                                      
REMARK 465     HIS B   527                                                      
REMARK 465     MET A    -7                                                      
REMARK 465     GLY A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     GLU A    50                                                      
REMARK 465     HIS A    51                                                      
REMARK 465     GLY A    52                                                      
REMARK 465     LEU A    53                                                      
REMARK 465     LYS A    54                                                      
REMARK 465     VAL A    55                                                      
REMARK 465     ALA A    56                                                      
REMARK 465     GLN A    57                                                      
REMARK 465     ALA A    58                                                      
REMARK 465     ALA A    59                                                      
REMARK 465     ALA A    60                                                      
REMARK 465     ALA A    61                                                      
REMARK 465     ALA A    62                                                      
REMARK 465     GLY A   297                                                      
REMARK 465     GLU A   298                                                      
REMARK 465     LYS A   299                                                      
REMARK 465     MET A   300                                                      
REMARK 465     SER A   301                                                      
REMARK 465     LYS A   302                                                      
REMARK 465     SER A   303                                                      
REMARK 465     VAL A   304                                                      
REMARK 465     GLY A   305                                                      
REMARK 465     ASN A   306                                                      
REMARK 465     GLN A   514                                                      
REMARK 465     PRO A   515                                                      
REMARK 465     PRO A   516                                                      
REMARK 465     GLU A   517                                                      
REMARK 465     GLY A   518                                                      
REMARK 465     LYS A   519                                                      
REMARK 465     ARG A   520                                                      
REMARK 465     SER A   521                                                      
REMARK 465     HIS A   522                                                      
REMARK 465     HIS A   523                                                      
REMARK 465     HIS A   524                                                      
REMARK 465     HIS A   525                                                      
REMARK 465     HIS A   526                                                      
REMARK 465     HIS A   527                                                      
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   O    HOH B   737     O    HOH B  1118              1.59            
REMARK 500   O    HOH A   988     O    HOH A  1057              1.81            
REMARK 500   O    ARG B   509     O    HOH B   601              1.82            
REMARK 500   O    HOH B   827     O    HOH B  1072              1.82            
REMARK 500   O    VAL B    64     O    HOH B   602              1.83            
REMARK 500   O    HOH B  1009     O    HOH B  1199              1.84            
REMARK 500   O    HOH B   731     O    HOH B  1036              1.85            
REMARK 500   O    HOH A   607     O    HOH A   893              1.87            
REMARK 500   O    HOH A  1138     O    HOH A  1141              1.91            
REMARK 500   O    HOH A  1104     O    HOH A  1123              1.94            
REMARK 500   O    HOH B  1057     O    HOH B  1094              1.95            
REMARK 500   O    HOH B  1013     O    HOH B  1064              1.97            
REMARK 500   O    HOH A  1019     O    HOH A  1081              1.97            
REMARK 500   O    HOH B   638     O    HOH B  1123              1.98            
REMARK 500   O    HOH A   947     O    HOH A  1019              1.99            
REMARK 500   O    HOH B   620     O    HOH B   824              1.99            
REMARK 500   O    ALA A   440     O    HOH A   601              1.99            
REMARK 500   O    GLY A   151     O    HOH A   602              2.00            
REMARK 500   O    HOH A   985     O    HOH A  1023              2.00            
REMARK 500   O    HOH A  1069     O    HOH A  1106              2.00            
REMARK 500   O    HOH A   875     O    HOH A   907              2.00            
REMARK 500   O    HOH B  1122     O    HOH B  1159              2.01            
REMARK 500   N    ALA B    67     O    HOH B   602              2.02            
REMARK 500   O    HOH A   933     O    HOH A   965              2.03            
REMARK 500   O    HOH B  1112     O    HOH B  1192              2.03            
REMARK 500   O    HOH B   947     O    HOH B  1108              2.03            
REMARK 500   O    HOH B  1056     O    HOH B  1172              2.05            
REMARK 500   O    HOH B   961     O    HOH B   992              2.06            
REMARK 500   O    HOH A   635     O    HOH A   993              2.06            
REMARK 500   O    HOH A   941     O    HOH A  1000              2.07            
REMARK 500   ND2  ASN A    85     OE2  GLU A   469              2.07            
REMARK 500   OE2  GLU B   412     O    HOH B   603              2.08            
REMARK 500   O    HOH A   624     O    HOH A   639              2.08            
REMARK 500   O    HOH B   939     O    HOH B  1074              2.09            
REMARK 500   O    HOH B   995     O    HOH B  1139              2.09            
REMARK 500   O    HOH A   970     O    HOH A   992              2.10            
REMARK 500   O    HOH B   807     O    HOH B  1025              2.10            
REMARK 500   O    HOH B   724     O    HOH B   998              2.11            
REMARK 500   O    HOH A   746     O    HOH A  1017              2.11            
REMARK 500   O    HOH B   823     O    HOH B  1101              2.11            
REMARK 500   O    HOH B   804     O    HOH B   809              2.12            
REMARK 500   O    HOH B   848     O    HOH B  1155              2.12            
REMARK 500   O    HOH B   702     O    HOH B   744              2.12            
REMARK 500   O    HOH B   818     O    HOH B  1160              2.13            
REMARK 500   O    HOH A   622     O    HOH A   774              2.13            
REMARK 500   O    HOH B   619     O    HOH B  1098              2.13            
REMARK 500   O    HOH A   645     O    HOH A  1095              2.13            
REMARK 500   O    HOH B  1024     O    HOH B  1154              2.13            
REMARK 500   OD1  ASP A   309     O    HOH A   603              2.14            
REMARK 500   O    HOH A   719     O    HOH A  1065              2.14            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      74 CLOSE CONTACTS                                
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   O    HOH B   966     O    HOH A   810     1655     1.85            
REMARK 500   O    HOH B   826     O    HOH B   916     1455     1.85            
REMARK 500   O    HOH A   944     O    HOH A  1063     1655     2.02            
REMARK 500   O    HOH A   813     O    HOH A   926     1655     2.05            
REMARK 500   O    HOH B   809     O    HOH B   972     1445     2.13            
REMARK 500   O    HOH B   605     O    HOH B  1091     1455     2.17            
REMARK 500   O    HOH B  1033     O    HOH B  1091     1455     2.19            
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    HIS B  18      -41.99     73.77                                   
REMARK 500    SER B  87       53.67   -106.18                                   
REMARK 500    ASP B 142       71.97   -151.51                                   
REMARK 500    GLU B 219       -5.26     73.66                                   
REMARK 500    ASN B 353      -64.32    -95.20                                   
REMARK 500    ALA B 406       65.25   -113.72                                   
REMARK 500    HIS A  18      -41.01     69.28                                   
REMARK 500    SER A  87       53.98   -107.54                                   
REMARK 500    VAL A 270      -67.42   -121.23                                   
REMARK 500    LEU A 351      -62.32    -92.81                                   
REMARK 500    ASN A 353      -60.22    -98.15                                   
REMARK 500    ALA A 406       65.19   -105.92                                   
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 B1210        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH B1211        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH B1212        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH B1213        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH B1214        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH B1215        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH B1216        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH B1217        DISTANCE =  6.71 ANGSTROMS                       
REMARK 525    HOH B1218        DISTANCE =  6.73 ANGSTROMS                       
REMARK 525    HOH B1219        DISTANCE =  7.10 ANGSTROMS                       
REMARK 525    HOH B1220        DISTANCE =  7.11 ANGSTROMS                       
REMARK 525    HOH B1221        DISTANCE =  7.30 ANGSTROMS                       
REMARK 525    HOH A1128        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH A1129        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH A1130        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH A1131        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH A1132        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH A1133        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH A1134        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH A1135        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH A1136        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH A1137        DISTANCE =  7.12 ANGSTROMS                       
REMARK 525    HOH A1138        DISTANCE =  7.29 ANGSTROMS                       
REMARK 525    HOH A1139        DISTANCE =  7.63 ANGSTROMS                       
REMARK 525    HOH A1140        DISTANCE =  7.68 ANGSTROMS                       
REMARK 525    HOH A1141        DISTANCE =  8.05 ANGSTROMS                       
REMARK 525    HOH A1142        DISTANCE =  8.07 ANGSTROMS                       
DBREF  5XGQ B    1   519  UNP    A5U150   A5U150_MYCTA     1    519             
DBREF  5XGQ A    1   519  UNP    A5U150   A5U150_MYCTA     1    519             
SEQADV 5XGQ MET B   -7  UNP  A5U150              INITIATING METHIONINE          
SEQADV 5XGQ GLY B   -6  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS B   -5  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS B   -4  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS B   -3  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS B   -2  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS B   -1  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS B    0  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ ARG B  520  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ SER B  521  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS B  522  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS B  523  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS B  524  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS B  525  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS B  526  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS B  527  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ MET A   -7  UNP  A5U150              INITIATING METHIONINE          
SEQADV 5XGQ GLY A   -6  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS A   -5  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS A   -4  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS A   -3  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS A   -2  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS A   -1  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS A    0  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ ARG A  520  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ SER A  521  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS A  522  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS A  523  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS A  524  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS A  525  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS A  526  UNP  A5U150              EXPRESSION TAG                 
SEQADV 5XGQ HIS A  527  UNP  A5U150              EXPRESSION TAG                 
SEQRES   1 B  535  MET GLY HIS HIS HIS HIS HIS HIS MET LYS PRO TYR TYR          
SEQRES   2 B  535  VAL THR THR ALA ILE ALA TYR PRO ASN ALA ALA PRO HIS          
SEQRES   3 B  535  VAL GLY HIS ALA TYR GLU TYR ILE ALA THR ASP ALA ILE          
SEQRES   4 B  535  ALA ARG PHE LYS ARG LEU ASP ARG TYR ASP VAL ARG PHE          
SEQRES   5 B  535  LEU THR GLY THR ASP GLU HIS GLY LEU LYS VAL ALA GLN          
SEQRES   6 B  535  ALA ALA ALA ALA ALA GLY VAL PRO THR ALA ALA LEU ALA          
SEQRES   7 B  535  ARG ARG ASN SER ASP VAL PHE GLN ARG MET GLN GLU ALA          
SEQRES   8 B  535  LEU ASN ILE SER PHE ASP ARG PHE ILE ARG THR THR ASP          
SEQRES   9 B  535  ALA ASP HIS HIS GLU ALA SER LYS GLU LEU TRP ARG ARG          
SEQRES  10 B  535  MET SER ALA ALA GLY ASP ILE TYR LEU ASP ASN TYR SER          
SEQRES  11 B  535  GLY TRP TYR SER VAL ARG ASP GLU ARG PHE PHE VAL GLU          
SEQRES  12 B  535  SER GLU THR GLN LEU VAL ASP GLY THR ARG LEU THR VAL          
SEQRES  13 B  535  GLU THR GLY THR PRO VAL THR TRP THR GLU GLU GLN THR          
SEQRES  14 B  535  TYR PHE PHE ARG LEU SER ALA TYR THR ASP LYS LEU LEU          
SEQRES  15 B  535  ALA HIS TYR HIS ALA ASN PRO ASP PHE ILE ALA PRO GLU          
SEQRES  16 B  535  THR ARG ARG ASN GLU VAL ILE SER PHE VAL SER GLY GLY          
SEQRES  17 B  535  LEU ASP ASP LEU SER ILE SER ARG THR SER PHE ASP TRP          
SEQRES  18 B  535  GLY VAL GLN VAL PRO GLU HIS PRO ASP HIS VAL MET TYR          
SEQRES  19 B  535  VAL TRP VAL ASP ALA LEU THR ASN TYR LEU THR GLY ALA          
SEQRES  20 B  535  GLY PHE PRO ASP THR ASP SER GLU LEU PHE ARG ARG TYR          
SEQRES  21 B  535  TRP PRO ALA ASP LEU HIS MET ILE GLY LYS ASP ILE ILE          
SEQRES  22 B  535  ARG PHE HIS ALA VAL TYR TRP PRO ALA PHE LEU MET SER          
SEQRES  23 B  535  ALA GLY ILE GLU LEU PRO ARG ARG ILE PHE ALA HIS GLY          
SEQRES  24 B  535  PHE LEU HIS ASN ARG GLY GLU LYS MET SER LYS SER VAL          
SEQRES  25 B  535  GLY ASN ILE VAL ASP PRO VAL ALA LEU ALA GLU ALA LEU          
SEQRES  26 B  535  GLY VAL ASP GLN VAL ARG TYR PHE LEU LEU ARG GLU VAL          
SEQRES  27 B  535  PRO PHE GLY GLN ASP GLY SER TYR SER ASP GLU ALA ILE          
SEQRES  28 B  535  VAL THR ARG ILE ASN THR ASP LEU ALA ASN GLU LEU GLY          
SEQRES  29 B  535  ASN LEU ALA GLN ARG SER LEU SER MET VAL ALA LYS ASN          
SEQRES  30 B  535  LEU ASP GLY ARG VAL PRO ASN PRO GLY GLU PHE ALA ASP          
SEQRES  31 B  535  ALA ASP ALA ALA LEU LEU ALA THR ALA ASP GLY LEU LEU          
SEQRES  32 B  535  GLU ARG VAL ARG GLY HIS PHE ASP ALA GLN ALA MET HIS          
SEQRES  33 B  535  LEU ALA LEU GLU ALA ILE TRP LEU MET LEU GLY ASP ALA          
SEQRES  34 B  535  ASN LYS TYR PHE SER VAL GLN GLN PRO TRP VAL LEU ARG          
SEQRES  35 B  535  LYS SER GLU SER GLU ALA ASP GLN ALA ARG PHE ARG THR          
SEQRES  36 B  535  THR LEU TYR VAL THR CYS GLU VAL VAL ARG ILE ALA ALA          
SEQRES  37 B  535  LEU LEU ILE GLN PRO VAL MET PRO GLU SER ALA GLY LYS          
SEQRES  38 B  535  ILE LEU ASP LEU LEU GLY GLN ALA PRO ASN GLN ARG SER          
SEQRES  39 B  535  PHE ALA ALA VAL GLY VAL ARG LEU THR PRO GLY THR ALA          
SEQRES  40 B  535  LEU PRO PRO PRO THR GLY VAL PHE PRO ARG TYR GLN PRO          
SEQRES  41 B  535  PRO GLN PRO PRO GLU GLY LYS ARG SER HIS HIS HIS HIS          
SEQRES  42 B  535  HIS HIS                                                      
SEQRES   1 A  535  MET GLY HIS HIS HIS HIS HIS HIS MET LYS PRO TYR TYR          
SEQRES   2 A  535  VAL THR THR ALA ILE ALA TYR PRO ASN ALA ALA PRO HIS          
SEQRES   3 A  535  VAL GLY HIS ALA TYR GLU TYR ILE ALA THR ASP ALA ILE          
SEQRES   4 A  535  ALA ARG PHE LYS ARG LEU ASP ARG TYR ASP VAL ARG PHE          
SEQRES   5 A  535  LEU THR GLY THR ASP GLU HIS GLY LEU LYS VAL ALA GLN          
SEQRES   6 A  535  ALA ALA ALA ALA ALA GLY VAL PRO THR ALA ALA LEU ALA          
SEQRES   7 A  535  ARG ARG ASN SER ASP VAL PHE GLN ARG MET GLN GLU ALA          
SEQRES   8 A  535  LEU ASN ILE SER PHE ASP ARG PHE ILE ARG THR THR ASP          
SEQRES   9 A  535  ALA ASP HIS HIS GLU ALA SER LYS GLU LEU TRP ARG ARG          
SEQRES  10 A  535  MET SER ALA ALA GLY ASP ILE TYR LEU ASP ASN TYR SER          
SEQRES  11 A  535  GLY TRP TYR SER VAL ARG ASP GLU ARG PHE PHE VAL GLU          
SEQRES  12 A  535  SER GLU THR GLN LEU VAL ASP GLY THR ARG LEU THR VAL          
SEQRES  13 A  535  GLU THR GLY THR PRO VAL THR TRP THR GLU GLU GLN THR          
SEQRES  14 A  535  TYR PHE PHE ARG LEU SER ALA TYR THR ASP LYS LEU LEU          
SEQRES  15 A  535  ALA HIS TYR HIS ALA ASN PRO ASP PHE ILE ALA PRO GLU          
SEQRES  16 A  535  THR ARG ARG ASN GLU VAL ILE SER PHE VAL SER GLY GLY          
SEQRES  17 A  535  LEU ASP ASP LEU SER ILE SER ARG THR SER PHE ASP TRP          
SEQRES  18 A  535  GLY VAL GLN VAL PRO GLU HIS PRO ASP HIS VAL MET TYR          
SEQRES  19 A  535  VAL TRP VAL ASP ALA LEU THR ASN TYR LEU THR GLY ALA          
SEQRES  20 A  535  GLY PHE PRO ASP THR ASP SER GLU LEU PHE ARG ARG TYR          
SEQRES  21 A  535  TRP PRO ALA ASP LEU HIS MET ILE GLY LYS ASP ILE ILE          
SEQRES  22 A  535  ARG PHE HIS ALA VAL TYR TRP PRO ALA PHE LEU MET SER          
SEQRES  23 A  535  ALA GLY ILE GLU LEU PRO ARG ARG ILE PHE ALA HIS GLY          
SEQRES  24 A  535  PHE LEU HIS ASN ARG GLY GLU LYS MET SER LYS SER VAL          
SEQRES  25 A  535  GLY ASN ILE VAL ASP PRO VAL ALA LEU ALA GLU ALA LEU          
SEQRES  26 A  535  GLY VAL ASP GLN VAL ARG TYR PHE LEU LEU ARG GLU VAL          
SEQRES  27 A  535  PRO PHE GLY GLN ASP GLY SER TYR SER ASP GLU ALA ILE          
SEQRES  28 A  535  VAL THR ARG ILE ASN THR ASP LEU ALA ASN GLU LEU GLY          
SEQRES  29 A  535  ASN LEU ALA GLN ARG SER LEU SER MET VAL ALA LYS ASN          
SEQRES  30 A  535  LEU ASP GLY ARG VAL PRO ASN PRO GLY GLU PHE ALA ASP          
SEQRES  31 A  535  ALA ASP ALA ALA LEU LEU ALA THR ALA ASP GLY LEU LEU          
SEQRES  32 A  535  GLU ARG VAL ARG GLY HIS PHE ASP ALA GLN ALA MET HIS          
SEQRES  33 A  535  LEU ALA LEU GLU ALA ILE TRP LEU MET LEU GLY ASP ALA          
SEQRES  34 A  535  ASN LYS TYR PHE SER VAL GLN GLN PRO TRP VAL LEU ARG          
SEQRES  35 A  535  LYS SER GLU SER GLU ALA ASP GLN ALA ARG PHE ARG THR          
SEQRES  36 A  535  THR LEU TYR VAL THR CYS GLU VAL VAL ARG ILE ALA ALA          
SEQRES  37 A  535  LEU LEU ILE GLN PRO VAL MET PRO GLU SER ALA GLY LYS          
SEQRES  38 A  535  ILE LEU ASP LEU LEU GLY GLN ALA PRO ASN GLN ARG SER          
SEQRES  39 A  535  PHE ALA ALA VAL GLY VAL ARG LEU THR PRO GLY THR ALA          
SEQRES  40 A  535  LEU PRO PRO PRO THR GLY VAL PHE PRO ARG TYR GLN PRO          
SEQRES  41 A  535  PRO GLN PRO PRO GLU GLY LYS ARG SER HIS HIS HIS HIS          
SEQRES  42 A  535  HIS HIS                                                      
FORMUL   3  HOH   *1163(H2 O)                                                   
HELIX    1 AA1 HIS B   21  ASP B   38  1                                  18    
HELIX    2 AA2 VAL B   64  ASN B   85  1                                  22    
HELIX    3 AA3 THR B   94  HIS B   99  1                                   6    
HELIX    4 AA4 HIS B  100  ALA B  113  1                                  14    
HELIX    5 AA5 VAL B  134  SER B  136  5                                   3    
HELIX    6 AA6 LEU B  166  ALA B  168  5                                   3    
HELIX    7 AA7 TYR B  169  ASN B  180  1                                  12    
HELIX    8 AA8 PRO B  186  GLY B  199  1                                  14    
HELIX    9 AA9 TYR B  226  THR B  233  1                                   8    
HELIX   10 AB1 THR B  233  GLY B  238  1                                   6    
HELIX   11 AB2 SER B  246  TRP B  253  1                                   8    
HELIX   12 AB3 ILE B  264  VAL B  270  1                                   7    
HELIX   13 AB4 VAL B  270  GLY B  280  1                                  11    
HELIX   14 AB5 ASP B  309  GLY B  318  1                                  10    
HELIX   15 AB6 GLY B  318  VAL B  330  1                                  13    
HELIX   16 AB7 SER B  339  THR B  349  1                                  11    
HELIX   17 AB8 LEU B  355  LEU B  370  1                                  16    
HELIX   18 AB9 ALA B  381  GLY B  393  1                                  13    
HELIX   19 AC1 GLY B  393  ALA B  404  1                                  12    
HELIX   20 AC2 ALA B  406  GLN B  429  1                                  24    
HELIX   21 AC3 GLN B  429  ARG B  434  1                                   6    
HELIX   22 AC4 GLU B  439  GLN B  464  1                                  26    
HELIX   23 AC5 MET B  467  LEU B  478  1                                  12    
HELIX   24 AC6 ALA B  481  ARG B  485  5                                   5    
HELIX   25 AC7 SER B  486  VAL B  490  5                                   5    
HELIX   26 AC8 HIS A   21  ASP A   38  1                                  18    
HELIX   27 AC9 VAL A   64  ASN A   85  1                                  22    
HELIX   28 AD1 THR A   94  HIS A   99  1                                   6    
HELIX   29 AD2 HIS A  100  ALA A  113  1                                  14    
HELIX   30 AD3 VAL A  134  SER A  136  5                                   3    
HELIX   31 AD4 LEU A  166  ALA A  168  5                                   3    
HELIX   32 AD5 TYR A  169  ASN A  180  1                                  12    
HELIX   33 AD6 PRO A  186  GLY A  199  1                                  14    
HELIX   34 AD7 TYR A  226  THR A  233  1                                   8    
HELIX   35 AD8 THR A  233  GLY A  238  1                                   6    
HELIX   36 AD9 SER A  246  TRP A  253  1                                   8    
HELIX   37 AE1 ILE A  264  VAL A  270  1                                   7    
HELIX   38 AE2 VAL A  270  GLY A  280  1                                  11    
HELIX   39 AE3 ASP A  309  GLY A  318  1                                  10    
HELIX   40 AE4 GLY A  318  VAL A  330  1                                  13    
HELIX   41 AE5 SER A  339  THR A  349  1                                  11    
HELIX   42 AE6 LEU A  355  LEU A  370  1                                  16    
HELIX   43 AE7 ALA A  381  GLY A  393  1                                  13    
HELIX   44 AE8 GLY A  393  ALA A  404  1                                  12    
HELIX   45 AE9 ALA A  406  GLN A  429  1                                  24    
HELIX   46 AF1 GLN A  429  ARG A  434  1                                   6    
HELIX   47 AF2 SER A  438  GLN A  464  1                                  27    
HELIX   48 AF3 MET A  467  LEU A  478  1                                  12    
HELIX   49 AF4 ALA A  481  ARG A  485  5                                   5    
HELIX   50 AF5 SER A  486  VAL A  490  5                                   5    
SHEET    1 AA1 5 TYR B  40  LEU B  45  0                                        
SHEET    2 AA1 5 LYS B   2  THR B   7  1  N  TYR B   4   O  ARG B  43           
SHEET    3 AA1 5 LEU B 257  GLY B 261  1  O  MET B 259   N  THR B   7           
SHEET    4 AA1 5 ILE B 287  HIS B 290  1  O  HIS B 290   N  ILE B 260           
SHEET    5 AA1 5 ILE B 184  ALA B 185  1  N  ALA B 185   O  ALA B 289           
SHEET    1 AA2 4 ARG B 131  PHE B 133  0                                        
SHEET    2 AA2 4 ILE B 116  SER B 126 -1  N  TRP B 124   O  PHE B 133           
SHEET    3 AA2 4 THR B 155  PHE B 164 -1  O  PHE B 163   N  TYR B 117           
SHEET    4 AA2 4 LEU B 204  SER B 205 -1  O  LEU B 204   N  PHE B 164           
SHEET    1 AA3 2 THR B 138  LEU B 140  0                                        
SHEET    2 AA3 2 ARG B 145  THR B 147 -1  O  LEU B 146   N  GLN B 139           
SHEET    1 AA4 3 SER B 207  THR B 209  0                                        
SHEET    2 AA4 3 HIS B 220  MET B 225 -1  O  VAL B 224   N  ARG B 208           
SHEET    3 AA4 3 GLN B 216  VAL B 217 -1  N  VAL B 217   O  HIS B 223           
SHEET    1 AA5 2 LEU B 293  ASN B 295  0                                        
SHEET    2 AA5 2 GLY B 336  TYR B 338  1  O  TYR B 338   N  HIS B 294           
SHEET    1 AA6 5 TYR A  40  LEU A  45  0                                        
SHEET    2 AA6 5 LYS A   2  THR A   7  1  N  TYR A   4   O  ARG A  43           
SHEET    3 AA6 5 LEU A 257  GLY A 261  1  O  MET A 259   N  THR A   7           
SHEET    4 AA6 5 ILE A 287  HIS A 290  1  O  PHE A 288   N  ILE A 260           
SHEET    5 AA6 5 ILE A 184  ALA A 185  1  N  ALA A 185   O  ALA A 289           
SHEET    1 AA7 4 ARG A 131  PHE A 133  0                                        
SHEET    2 AA7 4 ILE A 116  SER A 126 -1  N  TRP A 124   O  PHE A 133           
SHEET    3 AA7 4 THR A 155  PHE A 164 -1  O  PHE A 163   N  TYR A 117           
SHEET    4 AA7 4 LEU A 204  SER A 205 -1  O  LEU A 204   N  PHE A 164           
SHEET    1 AA8 2 THR A 138  LEU A 140  0                                        
SHEET    2 AA8 2 ARG A 145  THR A 147 -1  O  LEU A 146   N  GLN A 139           
SHEET    1 AA9 3 SER A 207  THR A 209  0                                        
SHEET    2 AA9 3 HIS A 220  MET A 225 -1  O  VAL A 224   N  ARG A 208           
SHEET    3 AA9 3 GLN A 216  VAL A 217 -1  N  VAL A 217   O  HIS A 223           
SHEET    1 AB1 2 LEU A 293  ASN A 295  0                                        
SHEET    2 AB1 2 GLY A 336  TYR A 338  1  O  TYR A 338   N  HIS A 294           
CISPEP   1 TYR B   12    PRO B   13          0         2.70                     
CISPEP   2 ALA B  185    PRO B  186          0        -2.19                     
CISPEP   3 PHE B  241    PRO B  242          0         9.59                     
CISPEP   4 TRP B  253    PRO B  254          0         5.27                     
CISPEP   5 TYR A   12    PRO A   13          0         4.53                     
CISPEP   6 ALA A  185    PRO A  186          0        -2.41                     
CISPEP   7 PHE A  241    PRO A  242          0         8.55                     
CISPEP   8 TRP A  253    PRO A  254          0         5.75                     
CRYST1   49.983   72.727   78.376  98.90  90.05  98.47 P 1           2          
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      0.020007  0.002980  0.000489        0.00000                         
SCALE2      0.000000  0.013902  0.002202        0.00000                         
SCALE3      0.000000  0.000000  0.012918        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system