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Database: PDB
Entry: 5JX2
LinkDB: 5JX2
Original site: 5JX2 
HEADER    TRANSPORT PROTEIN                       12-MAY-16   5JX2              
TITLE     CRYSTAL STRUCTURE OF MGLB-2 (TP0684) FROM TREPONEMA PALLIDUM          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOSE/GALACTOSE-BINDING LIPOPROTEIN;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TREPONEMA PALLIDUM (STRAIN NICHOLS);            
SOURCE   3 ORGANISM_TAXID: 243276;                                              
SOURCE   4 STRAIN: NICHOLS;                                                     
SOURCE   5 GENE: MGLB, TPP38, TP_0684;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GLUCOSE-BINDING PROTEIN, TRANSPORT PROTEIN                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.A.BRAUTIGAM,R.K.DEKA,M.V.NORGARD                                    
REVDAT   4   15-NOV-23 5JX2    1       ATOM                                     
REVDAT   3   11-DEC-19 5JX2    1       REMARK                                   
REVDAT   2   06-SEP-17 5JX2    1       REMARK                                   
REVDAT   1   31-AUG-16 5JX2    0                                                
JRNL        AUTH   C.A.BRAUTIGAM,R.K.DEKA,W.Z.LIU,M.V.NORGARD                   
JRNL        TITL   THE TP0684 (MGLB-2) LIPOPROTEIN OF TREPONEMA PALLIDUM: A     
JRNL        TITL 2 GLUCOSE-BINDING PROTEIN WITH DIVERGENT TOPOLOGY.             
JRNL        REF    PLOS ONE                      V.  11 61022 2016              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   27536942                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0161022                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.4_1496                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.79                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 27622                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1393                            
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 36.7913 -  4.4152    1.00     2811   165  0.1477 0.1786        
REMARK   3     2  4.4152 -  3.5054    1.00     2729   138  0.1602 0.2279        
REMARK   3     3  3.5054 -  3.0625    1.00     2692   152  0.1909 0.2238        
REMARK   3     4  3.0625 -  2.7826    1.00     2677   153  0.2107 0.2327        
REMARK   3     5  2.7826 -  2.5832    1.00     2675   136  0.1951 0.2416        
REMARK   3     6  2.5832 -  2.4310    1.00     2673   134  0.1876 0.2530        
REMARK   3     7  2.4310 -  2.3092    1.00     2681   137  0.1956 0.2050        
REMARK   3     8  2.3092 -  2.2087    0.90     2409   115  0.3183 0.3494        
REMARK   3     9  2.2087 -  2.1237    0.94     2486   135  0.2134 0.2513        
REMARK   3    10  2.1237 -  2.0504    0.91     2396   128  0.2582 0.3033        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.190           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           2845                                  
REMARK   3   ANGLE     :  0.735           3851                                  
REMARK   3   CHIRALITY :  0.027            423                                  
REMARK   3   PLANARITY :  0.003            507                                  
REMARK   3   DIHEDRAL  : 14.159           1037                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 11 THROUGH 64 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  90.4943  10.6314  25.4780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3533 T22:   0.3271                                     
REMARK   3      T33:   0.3650 T12:  -0.0399                                     
REMARK   3      T13:  -0.0129 T23:  -0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8341 L22:   2.5318                                     
REMARK   3      L33:   2.8875 L12:  -1.0936                                     
REMARK   3      L13:   0.7487 L23:  -1.4841                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1443 S12:  -0.1290 S13:  -0.7285                       
REMARK   3      S21:   0.0166 S22:   0.0101 S23:   0.2855                       
REMARK   3      S31:   0.4273 S32:   0.0591 S33:  -0.2011                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 65 THROUGH 170 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  78.8146  27.5709   4.5208              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2562 T22:   0.3615                                     
REMARK   3      T33:   0.2332 T12:  -0.0194                                     
REMARK   3      T13:   0.0047 T23:  -0.0236                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1447 L22:   1.9283                                     
REMARK   3      L33:   2.3713 L12:   0.2550                                     
REMARK   3      L13:  -0.0042 L23:  -0.7267                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0084 S12:   0.2864 S13:  -0.0789                       
REMARK   3      S21:  -0.2144 S22:   0.0873 S23:   0.0730                       
REMARK   3      S31:   0.0437 S32:  -0.1976 S33:  -0.0873                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 171 THROUGH 258 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  96.9290  23.4040  19.7599              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1844 T22:   0.2861                                     
REMARK   3      T33:   0.2466 T12:  -0.0153                                     
REMARK   3      T13:   0.0227 T23:  -0.0305                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5553 L22:   0.9732                                     
REMARK   3      L33:   2.6196 L12:  -0.6793                                     
REMARK   3      L13:   0.9340 L23:  -0.7143                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0082 S12:  -0.0078 S13:  -0.1033                       
REMARK   3      S21:  -0.0028 S22:  -0.0022 S23:  -0.0887                       
REMARK   3      S31:   0.0505 S32:   0.2549 S33:   0.0159                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 259 THROUGH 293 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  96.3748  22.4775  24.2909              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2359 T22:   0.3583                                     
REMARK   3      T33:   0.2258 T12:   0.0257                                     
REMARK   3      T13:   0.0160 T23:  -0.0671                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8356 L22:   3.9179                                     
REMARK   3      L33:   3.7653 L12:  -0.0719                                     
REMARK   3      L13:   0.8800 L23:  -2.1891                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0728 S12:  -0.1005 S13:  -0.0559                       
REMARK   3      S21:  -0.0156 S22:   0.0080 S23:  -0.0187                       
REMARK   3      S31:  -0.0897 S32:   0.4150 S33:  -0.0529                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 294 THROUGH 378 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): 105.4524   3.3169  22.8695              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5290 T22:   0.5425                                     
REMARK   3      T33:   0.5886 T12:   0.1806                                     
REMARK   3      T13:   0.0374 T23:  -0.0537                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8024 L22:   3.3247                                     
REMARK   3      L33:   3.6470 L12:   0.2432                                     
REMARK   3      L13:   0.4899 L23:  -0.4464                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1349 S12:   0.2062 S13:  -0.8634                       
REMARK   3      S21:  -0.3110 S22:  -0.0888 S23:  -0.1533                       
REMARK   3      S31:   1.0069 S32:   0.4420 S33:  -0.0372                       
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 5JX2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000221366.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-FEB-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97932                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28333                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.07500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: HKL-3000                                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5 20% PEG MME        
REMARK 280  5000, VAPOR DIFFUSION, TEMPERATURE 293K                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.12500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.12500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       38.77800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       65.01250            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       38.77800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.01250            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       44.12500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       38.77800            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       65.01250            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       44.12500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       38.77800            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       65.01250            
REMARK 290   SMTRY3   8  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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 750 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 16060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 672  LIES ON A SPECIAL POSITION.                          
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    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     SER A    -6                                                      
REMARK 465     ASP A    -5                                                      
REMARK 465     LYS A    -4                                                      
REMARK 465     ILE A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     TYR A     7                                                      
REMARK 465     PHE A     8                                                      
REMARK 465     GLN A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     THR A    27                                                      
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    ASN A  19      -40.03     69.14                                   
REMARK 500    ASN A  36       31.40    -97.83                                   
REMARK 500    ASP A  86      113.09   -167.16                                   
REMARK 500    GLN A 114       73.98   -107.68                                   
REMARK 500    ALA A 162     -121.86     48.35                                   
REMARK 500    ASP A 195      -31.50    132.02                                   
REMARK 500    GLU A 208      -76.84   -104.52                                   
REMARK 500    ASN A 279       17.54   -152.37                                   
REMARK 500    ALA A 317      -57.88   -121.16                                   
REMARK 500    SER A 368       30.07    -94.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  71   OD1                                                    
REMARK 620 2 ASN A  73   OD1  77.5                                              
REMARK 620 3 ASP A  75   OD1  82.5  67.6                                        
REMARK 620 4 ILE A  77   O    85.2 146.9  82.5                                  
REMARK 620 5 ASP A 166   OD2  99.7 139.0 153.3  71.3                            
REMARK 620 6 HOH A 505   O    93.4  66.2 133.4 143.7  73.2                      
REMARK 620 7 HOH A 516   O   177.0 105.3  99.2  92.6  77.7  87.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404                 
DBREF  5JX2 A   11   378  UNP    Q08255   MGLB_TREPA      36    403             
SEQADV 5JX2 MET A   -8  UNP  Q08255              INITIATING METHIONINE          
SEQADV 5JX2 GLY A   -7  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 SER A   -6  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 ASP A   -5  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 LYS A   -4  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 ILE A   -3  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 HIS A   -2  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 HIS A   -1  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 HIS A    0  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 HIS A    1  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 HIS A    2  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 HIS A    3  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 GLU A    4  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 ASN A    5  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 LEU A    6  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 TYR A    7  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 PHE A    8  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 GLN A    9  UNP  Q08255              EXPRESSION TAG                 
SEQADV 5JX2 GLY A   10  UNP  Q08255              EXPRESSION TAG                 
SEQRES   1 A  387  MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS GLU          
SEQRES   2 A  387  ASN LEU TYR PHE GLN GLY ARG ASP LYS PRO LEU VAL PHE          
SEQRES   3 A  387  PHE ASN ARG GLN PRO SER ASP PRO LEU THR GLY LYS VAL          
SEQRES   4 A  387  ASP MET ALA ALA MET ASN TRP ASN ASP LYS THR TYR TYR          
SEQRES   5 A  387  VAL GLY PHE ASP ALA LYS PHE GLY GLY SER ILE GLN GLY          
SEQRES   6 A  387  LYS MET ILE LEU ASP PHE LEU ALA SER SER GLU SER SER          
SEQRES   7 A  387  VAL ASP ARG ASN GLY ASP GLY ILE ILE GLY TYR VAL LEU          
SEQRES   8 A  387  CYS ILE GLY ASP VAL GLY HIS ASN ASP SER LYS VAL ARG          
SEQRES   9 A  387  THR GLU GLY ILE ARG ARG ALA LEU GLY THR TRP THR GLY          
SEQRES  10 A  387  SER SER ASP PRO GLY GLN ALA LYS GLU GLY GLN ALA VAL          
SEQRES  11 A  387  VAL GLY GLY LYS SER TYR LYS VAL VAL GLU LEU GLU GLY          
SEQRES  12 A  387  LYS ALA MET THR GLY THR ASP GLY SER THR TRP ASN THR          
SEQRES  13 A  387  ASN SER ALA THR GLU SER MET GLY SER TRP VAL ALA LYS          
SEQRES  14 A  387  PHE ALA ASP LYS ILE ASP LEU VAL ILE SER ASN ASN ASP          
SEQRES  15 A  387  GLY MET ALA MET GLY CYS LEU GLN ALA SER ASN TYR PRO          
SEQRES  16 A  387  ARG GLY LEU PRO ILE PHE GLY TYR ASP ALA ASN ALA ASP          
SEQRES  17 A  387  ALA VAL GLU SER VAL GLY LYS GLY GLU LEU THR GLY THR          
SEQRES  18 A  387  VAL SER GLN ASN VAL ASP ALA GLN ALA VAL ALA VAL LEU          
SEQRES  19 A  387  GLN ILE ILE ARG ASN LEU LEU ASP GLY SER SER GLY GLU          
SEQRES  20 A  387  ASP VAL VAL ALA ASN GLY ILE SER ARG PRO ASP ALA HIS          
SEQRES  21 A  387  GLY ASN ALY ILE SER ALA PRO VAL GLN TYR TRP GLU ASP          
SEQRES  22 A  387  VAL LYS ALA ILE MET ALA ASP ASN SER GLU VAL THR SER          
SEQRES  23 A  387  ALA ASN TRP LYS GLU TYR THR ARG GLY ALA ARG ASP ALA          
SEQRES  24 A  387  GLY VAL ARG GLN VAL SER ALA PRO THR LYS LYS VAL LEU          
SEQRES  25 A  387  LEU THR VAL HIS ASN ALA SER ASN ASP PHE LEU ALA SER          
SEQRES  26 A  387  ALA TYR LEU PRO ALA LEU LYS HIS TYR ALA PRO LEU LEU          
SEQRES  27 A  387  ASN VAL ASP LEU THR VAL VAL GLN GLY ASP GLY GLN ASN          
SEQRES  28 A  387  GLU LEU SER CYS LEU ASP LYS PHE THR ASN LEU ASP MET          
SEQRES  29 A  387  PHE ASP ALA PHE ALA VAL ASN MET VAL LYS THR ASN SER          
SEQRES  30 A  387  GLY ALA ASP TYR THR ASP LYS LEU LYS TYR                      
MODRES 5JX2 ALY A  254  LYS  MODIFIED RESIDUE                                   
HET    ALY  A 254      22                                                       
HET     CA  A 401       1                                                       
HET    BTB  A 402      33                                                       
HET    EDO  A 403      10                                                       
HET    EDO  A 404      10                                                       
HETNAM     ALY N(6)-ACETYLLYSINE                                                
HETNAM      CA CALCIUM ION                                                      
HETNAM     BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-                 
HETNAM   2 BTB  PROPANE-1,3-DIOL                                                
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     BTB BIS-TRIS BUFFER                                                  
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  ALY    C8 H16 N2 O3                                                 
FORMUL   2   CA    CA 2+                                                        
FORMUL   3  BTB    C8 H19 N O5                                                  
FORMUL   4  EDO    2(C2 H6 O2)                                                  
FORMUL   6  HOH   *194(H2 O)                                                    
HELIX    1 AA1 ASP A   31  ASN A   36  1                                   6    
HELIX    2 AA2 PHE A   50  SER A   65  1                                  16    
HELIX    3 AA3 GLU A   67  ASP A   71  5                                   5    
HELIX    4 AA4 HIS A   89  LEU A  103  1                                  15    
HELIX    5 AA5 ASN A  146  ALA A  162  1                                  17    
HELIX    6 AA6 ASN A  172  LEU A  180  1                                   9    
HELIX    7 AA7 ASN A  197  LYS A  206  1                                  10    
HELIX    8 AA8 ASN A  216  ASP A  233  1                                  18    
HELIX    9 AA9 GLY A  237  ASN A  243  1                                   7    
HELIX   10 AB1 GLU A  263  VAL A  265  5                                   3    
HELIX   11 AB2 ASN A  279  TYR A  283  5                                   5    
HELIX   12 AB3 ASN A  311  ALA A  317  1                                   7    
HELIX   13 AB4 ALA A  317  ALA A  326  1                                  10    
HELIX   14 AB5 PRO A  327  LEU A  329  5                                   3    
HELIX   15 AB6 GLU A  343  ASP A  348  1                                   6    
HELIX   16 AB7 ASN A  352  PHE A  356  5                                   5    
HELIX   17 AB8 SER A  368  LEU A  376  1                                   9    
SHEET    1 AA1 7 VAL A 259  TRP A 262  0                                        
SHEET    2 AA1 7 ALA A 267  ALA A 270 -1  O  ALA A 267   N  TRP A 262           
SHEET    3 AA1 7 THR A  41  PHE A  46  1  N  TYR A  43   O  ILE A 268           
SHEET    4 AA1 7 LEU A  15  PHE A  18  1  N  PHE A  17   O  TYR A  42           
SHEET    5 AA1 7 ALA A 358  VAL A 361  1  O  PHE A 359   N  VAL A  16           
SHEET    6 AA1 7 LYS A 300  VAL A 306  1  N  THR A 305   O  ALA A 360           
SHEET    7 AA1 7 VAL A 331  GLN A 337  1  O  THR A 334   N  LEU A 304           
SHEET    1 AA2 5 GLY A 118  VAL A 122  0                                        
SHEET    2 AA2 5 LYS A 125  ALA A 136 -1  O  VAL A 129   N  GLY A 118           
SHEET    3 AA2 5 ILE A  77  ILE A  84  1  N  ILE A  78   O  LYS A 128           
SHEET    4 AA2 5 ILE A 165  SER A 170  1  O  ASP A 166   N  GLY A  79           
SHEET    5 AA2 5 ILE A 191  PHE A 192  1  O  PHE A 192   N  VAL A 168           
SHEET    1 AA3 2 THR A 212  SER A 214  0                                        
SHEET    2 AA3 2 SER A 273  VAL A 275 -1  O  SER A 273   N  SER A 214           
LINK         C   ASN A 253                 N   ALY A 254     1555   1555  1.33  
LINK         C   ALY A 254                 N   ILE A 255     1555   1555  1.33  
LINK         OD1 ASP A  71                CA    CA A 401     1555   1555  2.37  
LINK         OD1 ASN A  73                CA    CA A 401     1555   1555  2.50  
LINK         OD1 ASP A  75                CA    CA A 401     1555   1555  2.45  
LINK         O   ILE A  77                CA    CA A 401     1555   1555  2.30  
LINK         OD2 ASP A 166                CA    CA A 401     1555   1555  2.66  
LINK        CA    CA A 401                 O   HOH A 505     1555   1555  2.51  
LINK        CA    CA A 401                 O   HOH A 516     1555   1555  2.46  
SITE     1 AC1  7 ASP A  71  ASN A  73  ASP A  75  ILE A  77                    
SITE     2 AC1  7 ASP A 166  HOH A 505  HOH A 516                               
SITE     1 AC2  5 HIS A  89  ASP A  91  ARG A  95  ASN A 172                    
SITE     2 AC2  5 ASP A 195                                                     
SITE     1 AC3  4 ALA A  48  ASP A  91  ARG A  95  TYR A 194                    
SITE     1 AC4  5 PHE A  50  GLU A  97  ARG A 101  TRP A 262                    
SITE     2 AC4  5 HOH A 538                                                     
CRYST1   77.556  130.025   88.250  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012894  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007691  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011331        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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