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Database: PDB
Entry: 4LXF
LinkDB: 4LXF
Original site: 4LXF 
HEADER    ISOMERASE                               29-JUL-13   4LXF              
TITLE     CRYSTAL STRUCTURE OF M. TUBERCULOSIS TRES                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TREHALOSE SYNTHASE;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 5.4.99.16;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 83332;                                               
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 GENE: RV0126, RVBD_0126;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    (ALPHA/BETA) BARREL, AMYLASE, ISOMERASE, TREHALOSE, MALTOSE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.ROY,G.S.BESRA,K.FUTTERER                                            
REVDAT   3   25-DEC-13 4LXF    1       JRNL                                     
REVDAT   2   11-SEP-13 4LXF    1       JRNL                                     
REVDAT   1   21-AUG-13 4LXF    0                                                
JRNL        AUTH   R.ROY,V.USHA,A.KERMANI,D.J.SCOTT,E.I.HYDE,G.S.BESRA,         
JRNL        AUTH 2 L.J.ALDERWICK,K.FUTTERER                                     
JRNL        TITL   SYNTHESIS OF ALPHA-GLUCAN IN MYCOBACTERIA INVOLVES A         
JRNL        TITL 2 HETERO-OCTAMERIC COMPLEX OF TREHALOSE SYNTHASE TRES AND      
JRNL        TITL 3 MALTOKINASE PEP2.                                            
JRNL        REF    ACS CHEM.BIOL.                V.   8  2245 2013              
JRNL        REFN                   ISSN 1554-8929                               
JRNL        PMID   23901909                                                     
JRNL        DOI    10.1021/CB400508K                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 60392                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3226                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4293                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.52                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3600                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 222                          
REMARK   3   BIN FREE R VALUE                    : 0.3830                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8737                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 62                                      
REMARK   3   SOLVENT ATOMS            : 46                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 70.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 69.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.03000                                              
REMARK   3    B22 (A**2) : 3.03000                                              
REMARK   3    B33 (A**2) : -4.54000                                             
REMARK   3    B12 (A**2) : 1.51000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.336         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.244         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.225         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.115        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9063 ; 0.006 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12398 ; 1.003 ; 1.947       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1112 ; 5.061 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   451 ;34.095 ;23.304       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1226 ;17.292 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    65 ;16.354 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1314 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7252 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    10        A   600                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.8140 -47.5640 -23.0420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0232 T22:   0.2862                                     
REMARK   3      T33:   0.1747 T12:   0.0077                                     
REMARK   3      T13:  -0.0127 T23:   0.1598                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0750 L22:   0.5086                                     
REMARK   3      L33:   2.0591 L12:  -0.1644                                     
REMARK   3      L13:  -0.3794 L23:  -0.1076                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1096 S12:  -0.0956 S13:  -0.0920                       
REMARK   3      S21:   0.0164 S22:   0.1242 S23:   0.1566                       
REMARK   3      S31:  -0.0370 S32:  -0.5823 S33:  -0.2338                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    10        B   600                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.9370  -6.4360 -20.2210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1199 T22:   0.4419                                     
REMARK   3      T33:   0.1793 T12:   0.0986                                     
REMARK   3      T13:  -0.0081 T23:  -0.0138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9459 L22:   0.9675                                     
REMARK   3      L33:   2.3036 L12:  -0.7205                                     
REMARK   3      L13:   1.0406 L23:  -0.7184                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0837 S12:  -0.3547 S13:   0.1657                       
REMARK   3      S21:   0.2220 S22:   0.0458 S23:  -0.2698                       
REMARK   3      S31:  -0.0895 S32:   0.3026 S33:   0.0379                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4LXF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB081206.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAY-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63561                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : 0.06000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.66800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2ZE0, 1UOK, 2PWE, 1WZA                     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NACITRATE, 0.5 M (NH4)2SO4, 1 M    
REMARK 280  LI2SO4, PH 5.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 1 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -Y,-X,-Z+1/3                                            
REMARK 290       5555   -X+Y,Y,-Z+2/3                                           
REMARK 290       6555   X,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   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       92.74000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       46.37000            
REMARK 290   SMTRY1   4  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000       46.37000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       92.74000            
REMARK 290   SMTRY1   6  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12850 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 76760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -211.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -92.74000            
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   -18                                                      
REMARK 465     GLY A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     GLY A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     VAL A    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     ARG A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     VAL A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     LEU A   426                                                      
REMARK 465     GLY A   427                                                      
REMARK 465     ASP A   428                                                      
REMARK 465     ARG A   429                                                      
REMARK 465     ASP A   430                                                      
REMARK 465     HIS A   587                                                      
REMARK 465     GLU A   588                                                      
REMARK 465     VAL A   589                                                      
REMARK 465     GLY A   590                                                      
REMARK 465     ALA A   591                                                      
REMARK 465     PRO A   592                                                      
REMARK 465     PRO A   593                                                      
REMARK 465     THR A   594                                                      
REMARK 465     CYS A   595                                                      
REMARK 465     GLY A   596                                                      
REMARK 465     GLY A   597                                                      
REMARK 465     GLU A   598                                                      
REMARK 465     ARG A   599                                                      
REMARK 465     ARG A   600                                                      
REMARK 465     LEU A   601                                                      
REMARK 465     MET B   -18                                                      
REMARK 465     GLY B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     SER B    -7                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     VAL B    -4                                                      
REMARK 465     PRO B    -3                                                      
REMARK 465     ARG B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     VAL B     8                                                      
REMARK 465     GLU B     9                                                      
REMARK 465     HIS B    10                                                      
REMARK 465     PRO B    11                                                      
REMARK 465     THR B   353                                                      
REMARK 465     LEU B   354                                                      
REMARK 465     GLU B   355                                                      
REMARK 465     MET B   356                                                      
REMARK 465     VAL B   357                                                      
REMARK 465     THR B   358                                                      
REMARK 465     ASP B   359                                                      
REMARK 465     GLU B   360                                                      
REMARK 465     GLU B   361                                                      
REMARK 465     ARG B   362                                                      
REMARK 465     ASP B   363                                                      
REMARK 465     TYR B   364                                                      
REMARK 465     MET B   365                                                      
REMARK 465     TYR B   366                                                      
REMARK 465     ALA B   367                                                      
REMARK 465     GLU B   368                                                      
REMARK 465     TYR B   369                                                      
REMARK 465     ALA B   370                                                      
REMARK 465     LYS B   371                                                      
REMARK 465     ASP B   372                                                      
REMARK 465     PRO B   373                                                      
REMARK 465     ARG B   374                                                      
REMARK 465     MET B   375                                                      
REMARK 465     LYS B   376                                                      
REMARK 465     ALA B   377                                                      
REMARK 465     ASN B   378                                                      
REMARK 465     VAL B   379                                                      
REMARK 465     GLY B   380                                                      
REMARK 465     ILE B   381                                                      
REMARK 465     HIS B   587                                                      
REMARK 465     GLU B   588                                                      
REMARK 465     VAL B   589                                                      
REMARK 465     GLY B   590                                                      
REMARK 465     ALA B   591                                                      
REMARK 465     PRO B   592                                                      
REMARK 465     PRO B   593                                                      
REMARK 465     THR B   594                                                      
REMARK 465     CYS B   595                                                      
REMARK 465     GLY B   596                                                      
REMARK 465     GLY B   597                                                      
REMARK 465     GLU B   598                                                      
REMARK 465     ARG B   599                                                      
REMARK 465     ARG B   600                                                      
REMARK 465     LEU B   601                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL A  13    CG1  CG2                                            
REMARK 470     GLN A  14    OE1  NE2                                            
REMARK 470     GLU A  24    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  29    CG   CD   CE   NZ                                   
REMARK 470     SER A  33    OG                                                  
REMARK 470     SER A  61    OG                                                  
REMARK 470     SER A  65    OG                                                  
REMARK 470     ARG A  69    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A  73    CG   OD1  OD2                                       
REMARK 470     ARG A  97    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 108    CG   CD   CE   NZ                                   
REMARK 470     VAL A 123    CG1  CG2                                            
REMARK 470     SER A 145    OG                                                  
REMARK 470     ARG A 154    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 155    CG   OD1  OD2                                       
REMARK 470     ASP A 157    CG   OD1  OD2                                       
REMARK 470     SER A 167    OG                                                  
REMARK 470     SER A 170    OG                                                  
REMARK 470     GLU A 171    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 177    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 181    CG1  CG2                                            
REMARK 470     THR A 183    OG1  CG2                                            
REMARK 470     SER A 189    OG                                                  
REMARK 470     PRO A 192    CG   CD                                             
REMARK 470     VAL A 193    CG1  CG2                                            
REMARK 470     ARG A 195    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 263    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 266    CG   CD   CE   NZ                                   
REMARK 470     ARG A 319    CZ   NH1  NH2                                       
REMARK 470     ASP A 338    CG   OD1  OD2                                       
REMARK 470     MET A 339    SD   CE                                             
REMARK 470     GLU A 351    CD   OE1  OE2                                       
REMARK 470     GLU A 355    CD   OE1  OE2                                       
REMARK 470     LYS A 371    CG   CD   CE   NZ                                   
REMARK 470     ARG A 374    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 376    CE   NZ                                             
REMARK 470     TRP A 425    CE3  CZ2  CZ3  CH2                                  
REMARK 470     ARG A 433    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 442    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 453    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 476    CG   OD1  OD2                                       
REMARK 470     ASP A 523    CG   OD1  OD2                                       
REMARK 470     ASP A 524    CG   OD1  OD2                                       
REMARK 470     ARG A 564    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B  13    CG1  CG2                                            
REMARK 470     GLN B  14    CD   OE1  NE2                                       
REMARK 470     GLU B  24    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  27    CG   OD1  OD2                                       
REMARK 470     LYS B  29    CG   CD   CE   NZ                                   
REMARK 470     SER B  33    OG                                                  
REMARK 470     SER B  65    OG                                                  
REMARK 470     ARG B  69    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B  86    CG1  CG2  CD1                                       
REMARK 470     LYS B 108    CG   CD   CE   NZ                                   
REMARK 470     THR B 115    OG1  CG2                                            
REMARK 470     VAL B 123    CG1  CG2                                            
REMARK 470     SER B 145    OG                                                  
REMARK 470     ARG B 154    NE   CZ   NH1  NH2                                  
REMARK 470     ASP B 155    CG   OD1  OD2                                       
REMARK 470     SER B 170    OG                                                  
REMARK 470     GLU B 171    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 175    CG   OD1  OD2                                       
REMARK 470     ARG B 177    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 182    CG   OD1  OD2                                       
REMARK 470     SER B 189    OG                                                  
REMARK 470     PHE B 190    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PRO B 192    CG   CD                                             
REMARK 470     VAL B 193    CG1  CG2                                            
REMARK 470     ARG B 195    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 204    OG                                                  
REMARK 470     ILE B 221    CG1  CG2  CD1                                       
REMARK 470     ARG B 263    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 266    CG   CD   CE   NZ                                   
REMARK 470     VAL B 288    CG1  CG2                                            
REMARK 470     ARG B 319    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B 339    SD   CE                                             
REMARK 470     HIS B 349    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP B 350    CG   OD1  OD2                                       
REMARK 470     LEU B 352    CG   CD1  CD2                                       
REMARK 470     ASP B 390    CG   OD1  OD2                                       
REMARK 470     TRP B 425    CD1  CD2  NE1  CE2  CE3  CZ2  CZ3                   
REMARK 470     TRP B 425    CH2                                                 
REMARK 470     ARG B 442    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 450    CG   OD1  ND2                                       
REMARK 470     ARG B 453    NE   CZ   NH1  NH2                                  
REMARK 470     THR B 477    OG1  CG2                                            
REMARK 470     SER B 478    OG                                                  
REMARK 470     ASP B 523    CG   OD1  OD2                                       
REMARK 470     ASP B 524    CG   OD1  OD2                                       
REMARK 470     GLN B 546    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 567    CG   CD   OE1  NE2                                  
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    PHE A 202     -127.40   -112.43                                   
REMARK 500    ALA A 281      115.44   -162.25                                   
REMARK 500    GLU A 301     -116.09   -130.71                                   
REMARK 500    MET A 339       51.87    -95.78                                   
REMARK 500    ASP A 359      112.61   -163.84                                   
REMARK 500    ARG A 433       45.04    -97.57                                   
REMARK 500    ASN A 443       15.27     59.29                                   
REMARK 500    ASP A 524       17.56     58.24                                   
REMARK 500    ASN A 550      -11.80     74.87                                   
REMARK 500    GLU B  19      130.86   -170.76                                   
REMARK 500    PHE B  57      -71.65    -73.92                                   
REMARK 500    LEU B  96       35.96     70.96                                   
REMARK 500    ASP B  98       57.30   -141.11                                   
REMARK 500    ASP B 175      -16.24     68.86                                   
REMARK 500    PHE B 202     -128.78   -104.85                                   
REMARK 500    GLU B 301     -116.22   -133.35                                   
REMARK 500    ASP B 350      -70.14   -115.36                                   
REMARK 500    ASP B 428     -101.52     59.44                                   
REMARK 500    ARG B 433       32.18    -92.30                                   
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 B 808        DISTANCE =  5.44 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 701  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 812   O                                                      
REMARK 620 2 ASP A 208   OD2 104.7                                              
REMARK 620 3 GLU A 245   OE2 153.1  89.9                                        
REMARK 620 4 TYR A 242   O   121.6 106.8  73.4                                  
REMARK 620 5 LEU A 243   O    73.6 178.3  91.8  73.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 701  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU B 243   O                                                      
REMARK 620 2 TYR B 242   O    74.3                                              
REMARK 620 3 ASP B 208   OD2 170.5  96.3                                        
REMARK 620 4 GLU B 245   OE1  89.7  79.4  90.3                                  
REMARK 620 5 GLU B 245   OE2  69.5 108.1 116.1  42.0                            
REMARK 620 N                    1     2     3     4                             
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 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 708                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 705                 
DBREF  4LXF A    1   601  UNP    I6X8K8   I6X8K8_MYCTU     1    601             
DBREF  4LXF B    1   601  UNP    I6X8K8   I6X8K8_MYCTU     1    601             
SEQADV 4LXF MET A  -18  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF GLY A  -17  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF SER A  -16  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF SER A  -15  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF HIS A  -14  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF HIS A  -13  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF HIS A  -12  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF HIS A  -11  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF HIS A  -10  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF HIS A   -9  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF SER A   -8  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF SER A   -7  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF GLY A   -6  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF LEU A   -5  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF VAL A   -4  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF PRO A   -3  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF ARG A   -2  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF GLY A   -1  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF SER A    0  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF MET B  -18  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF GLY B  -17  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF SER B  -16  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF SER B  -15  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF HIS B  -14  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF HIS B  -13  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF HIS B  -12  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF HIS B  -11  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF HIS B  -10  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF HIS B   -9  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF SER B   -8  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF SER B   -7  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF GLY B   -6  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF LEU B   -5  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF VAL B   -4  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF PRO B   -3  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF ARG B   -2  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF GLY B   -1  UNP  I6X8K8              EXPRESSION TAG                 
SEQADV 4LXF SER B    0  UNP  I6X8K8              EXPRESSION TAG                 
SEQRES   1 A  620  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  620  LEU VAL PRO ARG GLY SER MET ASN GLU ALA GLU HIS SER          
SEQRES   3 A  620  VAL GLU HIS PRO PRO VAL GLN GLY SER HIS VAL GLU GLY          
SEQRES   4 A  620  GLY VAL VAL GLU HIS PRO ASP ALA LYS ASP PHE GLY SER          
SEQRES   5 A  620  ALA ALA ALA LEU PRO ALA ASP PRO THR TRP PHE LYS HIS          
SEQRES   6 A  620  ALA VAL PHE TYR GLU VAL LEU VAL ARG ALA PHE PHE ASP          
SEQRES   7 A  620  ALA SER ALA ASP GLY SER GLY ASP LEU ARG GLY LEU ILE          
SEQRES   8 A  620  ASP ARG LEU ASP TYR LEU GLN TRP LEU GLY ILE ASP CYS          
SEQRES   9 A  620  ILE TRP LEU PRO PRO PHE TYR ASP SER PRO LEU ARG ASP          
SEQRES  10 A  620  GLY GLY TYR ASP ILE ARG ASP PHE TYR LYS VAL LEU PRO          
SEQRES  11 A  620  GLU PHE GLY THR VAL ASP ASP PHE VAL ALA LEU VAL ASP          
SEQRES  12 A  620  ALA ALA HIS ARG ARG GLY ILE ARG ILE ILE THR ASP LEU          
SEQRES  13 A  620  VAL MET ASN HIS THR SER GLU SER HIS PRO TRP PHE GLN          
SEQRES  14 A  620  GLU SER ARG ARG ASP PRO ASP GLY PRO TYR GLY ASP TYR          
SEQRES  15 A  620  TYR VAL TRP SER ASP THR SER GLU ARG TYR THR ASP ALA          
SEQRES  16 A  620  ARG ILE ILE PHE VAL ASP THR GLU GLU SER ASN TRP SER          
SEQRES  17 A  620  PHE ASP PRO VAL ARG ARG GLN PHE TYR TRP HIS ARG PHE          
SEQRES  18 A  620  PHE SER HIS GLN PRO ASP LEU ASN TYR ASP ASN PRO ALA          
SEQRES  19 A  620  VAL GLN GLU ALA MET ILE ASP VAL ILE ARG PHE TRP LEU          
SEQRES  20 A  620  GLY LEU GLY ILE ASP GLY PHE ARG LEU ASP ALA VAL PRO          
SEQRES  21 A  620  TYR LEU PHE GLU ARG GLU GLY THR ASN CYS GLU ASN LEU          
SEQRES  22 A  620  PRO GLU THR HIS ALA PHE LEU LYS ARG VAL ARG LYS VAL          
SEQRES  23 A  620  VAL ASP ASP GLU PHE PRO GLY ARG VAL LEU LEU ALA GLU          
SEQRES  24 A  620  ALA ASN GLN TRP PRO GLY ASP VAL VAL GLU TYR PHE GLY          
SEQRES  25 A  620  ASP PRO ASN THR GLY GLY ASP GLU CYS HIS MET ALA PHE          
SEQRES  26 A  620  HIS PHE PRO LEU MET PRO ARG ILE PHE MET ALA VAL ARG          
SEQRES  27 A  620  ARG GLU SER ARG PHE PRO ILE SER GLU ILE ILE ALA GLN          
SEQRES  28 A  620  THR PRO PRO ILE PRO ASP MET ALA GLN TRP GLY ILE PHE          
SEQRES  29 A  620  LEU ARG ASN HIS ASP GLU LEU THR LEU GLU MET VAL THR          
SEQRES  30 A  620  ASP GLU GLU ARG ASP TYR MET TYR ALA GLU TYR ALA LYS          
SEQRES  31 A  620  ASP PRO ARG MET LYS ALA ASN VAL GLY ILE ARG ARG ARG          
SEQRES  32 A  620  LEU ALA PRO LEU LEU ASP ASN ASP ARG ASN GLN ILE GLU          
SEQRES  33 A  620  LEU PHE THR ALA LEU LEU LEU SER LEU PRO GLY SER PRO          
SEQRES  34 A  620  VAL LEU TYR TYR GLY ASP GLU ILE GLY MET GLY ASP VAL          
SEQRES  35 A  620  ILE TRP LEU GLY ASP ARG ASP GLY VAL ARG ILE PRO MET          
SEQRES  36 A  620  GLN TRP THR PRO ASP ARG ASN ALA GLY PHE SER THR ALA          
SEQRES  37 A  620  ASN PRO GLY ARG LEU TYR LEU PRO PRO SER GLN ASP PRO          
SEQRES  38 A  620  VAL TYR GLY TYR GLN ALA VAL ASN VAL GLU ALA GLN ARG          
SEQRES  39 A  620  ASP THR SER THR SER LEU LEU ASN PHE THR ARG THR MET          
SEQRES  40 A  620  LEU ALA VAL ARG ARG ARG HIS PRO ALA PHE ALA VAL GLY          
SEQRES  41 A  620  ALA PHE GLN GLU LEU GLY GLY SER ASN PRO SER VAL LEU          
SEQRES  42 A  620  ALA TYR VAL ARG GLN VAL ALA GLY ASP ASP GLY ASP THR          
SEQRES  43 A  620  VAL LEU CYS VAL ASN ASN LEU SER ARG PHE PRO GLN PRO          
SEQRES  44 A  620  ILE GLU LEU ASP LEU GLN GLN TRP THR ASN TYR THR PRO          
SEQRES  45 A  620  VAL GLU LEU THR GLY HIS VAL GLU PHE PRO ARG ILE GLY          
SEQRES  46 A  620  GLN VAL PRO TYR LEU LEU THR LEU PRO GLY HIS GLY PHE          
SEQRES  47 A  620  TYR TRP PHE GLN LEU THR THR HIS GLU VAL GLY ALA PRO          
SEQRES  48 A  620  PRO THR CYS GLY GLY GLU ARG ARG LEU                          
SEQRES   1 B  620  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  620  LEU VAL PRO ARG GLY SER MET ASN GLU ALA GLU HIS SER          
SEQRES   3 B  620  VAL GLU HIS PRO PRO VAL GLN GLY SER HIS VAL GLU GLY          
SEQRES   4 B  620  GLY VAL VAL GLU HIS PRO ASP ALA LYS ASP PHE GLY SER          
SEQRES   5 B  620  ALA ALA ALA LEU PRO ALA ASP PRO THR TRP PHE LYS HIS          
SEQRES   6 B  620  ALA VAL PHE TYR GLU VAL LEU VAL ARG ALA PHE PHE ASP          
SEQRES   7 B  620  ALA SER ALA ASP GLY SER GLY ASP LEU ARG GLY LEU ILE          
SEQRES   8 B  620  ASP ARG LEU ASP TYR LEU GLN TRP LEU GLY ILE ASP CYS          
SEQRES   9 B  620  ILE TRP LEU PRO PRO PHE TYR ASP SER PRO LEU ARG ASP          
SEQRES  10 B  620  GLY GLY TYR ASP ILE ARG ASP PHE TYR LYS VAL LEU PRO          
SEQRES  11 B  620  GLU PHE GLY THR VAL ASP ASP PHE VAL ALA LEU VAL ASP          
SEQRES  12 B  620  ALA ALA HIS ARG ARG GLY ILE ARG ILE ILE THR ASP LEU          
SEQRES  13 B  620  VAL MET ASN HIS THR SER GLU SER HIS PRO TRP PHE GLN          
SEQRES  14 B  620  GLU SER ARG ARG ASP PRO ASP GLY PRO TYR GLY ASP TYR          
SEQRES  15 B  620  TYR VAL TRP SER ASP THR SER GLU ARG TYR THR ASP ALA          
SEQRES  16 B  620  ARG ILE ILE PHE VAL ASP THR GLU GLU SER ASN TRP SER          
SEQRES  17 B  620  PHE ASP PRO VAL ARG ARG GLN PHE TYR TRP HIS ARG PHE          
SEQRES  18 B  620  PHE SER HIS GLN PRO ASP LEU ASN TYR ASP ASN PRO ALA          
SEQRES  19 B  620  VAL GLN GLU ALA MET ILE ASP VAL ILE ARG PHE TRP LEU          
SEQRES  20 B  620  GLY LEU GLY ILE ASP GLY PHE ARG LEU ASP ALA VAL PRO          
SEQRES  21 B  620  TYR LEU PHE GLU ARG GLU GLY THR ASN CYS GLU ASN LEU          
SEQRES  22 B  620  PRO GLU THR HIS ALA PHE LEU LYS ARG VAL ARG LYS VAL          
SEQRES  23 B  620  VAL ASP ASP GLU PHE PRO GLY ARG VAL LEU LEU ALA GLU          
SEQRES  24 B  620  ALA ASN GLN TRP PRO GLY ASP VAL VAL GLU TYR PHE GLY          
SEQRES  25 B  620  ASP PRO ASN THR GLY GLY ASP GLU CYS HIS MET ALA PHE          
SEQRES  26 B  620  HIS PHE PRO LEU MET PRO ARG ILE PHE MET ALA VAL ARG          
SEQRES  27 B  620  ARG GLU SER ARG PHE PRO ILE SER GLU ILE ILE ALA GLN          
SEQRES  28 B  620  THR PRO PRO ILE PRO ASP MET ALA GLN TRP GLY ILE PHE          
SEQRES  29 B  620  LEU ARG ASN HIS ASP GLU LEU THR LEU GLU MET VAL THR          
SEQRES  30 B  620  ASP GLU GLU ARG ASP TYR MET TYR ALA GLU TYR ALA LYS          
SEQRES  31 B  620  ASP PRO ARG MET LYS ALA ASN VAL GLY ILE ARG ARG ARG          
SEQRES  32 B  620  LEU ALA PRO LEU LEU ASP ASN ASP ARG ASN GLN ILE GLU          
SEQRES  33 B  620  LEU PHE THR ALA LEU LEU LEU SER LEU PRO GLY SER PRO          
SEQRES  34 B  620  VAL LEU TYR TYR GLY ASP GLU ILE GLY MET GLY ASP VAL          
SEQRES  35 B  620  ILE TRP LEU GLY ASP ARG ASP GLY VAL ARG ILE PRO MET          
SEQRES  36 B  620  GLN TRP THR PRO ASP ARG ASN ALA GLY PHE SER THR ALA          
SEQRES  37 B  620  ASN PRO GLY ARG LEU TYR LEU PRO PRO SER GLN ASP PRO          
SEQRES  38 B  620  VAL TYR GLY TYR GLN ALA VAL ASN VAL GLU ALA GLN ARG          
SEQRES  39 B  620  ASP THR SER THR SER LEU LEU ASN PHE THR ARG THR MET          
SEQRES  40 B  620  LEU ALA VAL ARG ARG ARG HIS PRO ALA PHE ALA VAL GLY          
SEQRES  41 B  620  ALA PHE GLN GLU LEU GLY GLY SER ASN PRO SER VAL LEU          
SEQRES  42 B  620  ALA TYR VAL ARG GLN VAL ALA GLY ASP ASP GLY ASP THR          
SEQRES  43 B  620  VAL LEU CYS VAL ASN ASN LEU SER ARG PHE PRO GLN PRO          
SEQRES  44 B  620  ILE GLU LEU ASP LEU GLN GLN TRP THR ASN TYR THR PRO          
SEQRES  45 B  620  VAL GLU LEU THR GLY HIS VAL GLU PHE PRO ARG ILE GLY          
SEQRES  46 B  620  GLN VAL PRO TYR LEU LEU THR LEU PRO GLY HIS GLY PHE          
SEQRES  47 B  620  TYR TRP PHE GLN LEU THR THR HIS GLU VAL GLY ALA PRO          
SEQRES  48 B  620  PRO THR CYS GLY GLY GLU ARG ARG LEU                          
HET     CA  A 701       1                                                       
HET    GOL  A 702       6                                                       
HET    GOL  A 703       6                                                       
HET    GOL  A 704       6                                                       
HET    GOL  A 705       6                                                       
HET    SO4  A 706       5                                                       
HET    SO4  A 707       5                                                       
HET    SO4  A 708       5                                                       
HET     CA  B 701       1                                                       
HET    GOL  B 702       6                                                       
HET    SO4  B 703       5                                                       
HET    SO4  B 704       5                                                       
HET    SO4  B 705       5                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   4  GOL    5(C3 H8 O3)                                                  
FORMUL   8  SO4    6(O4 S 2-)                                                   
FORMUL  16  HOH   *46(H2 O)                                                     
HELIX    1   1 ASP A   27  PHE A   31  5                                   5    
HELIX    2   2 THR A   42  HIS A   46  5                                   5    
HELIX    3   3 LEU A   53  PHE A   58  1                                   6    
HELIX    4   4 ASP A   67  ARG A   74  1                                   8    
HELIX    5   5 ARG A   74  GLY A   82  1                                   9    
HELIX    6   6 PRO A  111  GLY A  114  5                                   4    
HELIX    7   7 THR A  115  ARG A  128  1                                  14    
HELIX    8   8 HIS A  146  ASP A  155  1                                  10    
HELIX    9   9 ASN A  213  GLY A  231  1                                  19    
HELIX   10  10 ALA A  239  LEU A  243  5                                   5    
HELIX   11  11 LEU A  254  PHE A  272  1                                  19    
HELIX   12  12 ASP A  287  GLY A  293  5                                   7    
HELIX   13  13 ASP A  294  GLY A  298  5                                   5    
HELIX   14  14 PRO A  309  GLU A  321  1                                  13    
HELIX   15  15 ARG A  323  GLN A  332  1                                  10    
HELIX   16  16 ALA A  367  ASP A  372  1                                   6    
HELIX   17  17 ASP A  372  ALA A  377  1                                   6    
HELIX   18  18 ARG A  384  LEU A  389  1                                   6    
HELIX   19  19 ASP A  392  LEU A  406  1                                  15    
HELIX   20  20 ASP A  441  PHE A  446  5                                   6    
HELIX   21  21 ASN A  450  LEU A  454  5                                   5    
HELIX   22  22 ASN A  470  THR A  477  1                                   8    
HELIX   23  23 SER A  480  ARG A  494  1                                  15    
HELIX   24  24 PRO A  496  GLY A  501  1                                   6    
HELIX   25  25 LEU A  545  THR A  549  5                                   5    
HELIX   26  26 ASP B   27  PHE B   31  5                                   5    
HELIX   27  27 THR B   42  ALA B   47  1                                   6    
HELIX   28  28 LEU B   53  PHE B   58  1                                   6    
HELIX   29  29 ASP B   67  ARG B   74  1                                   8    
HELIX   30  30 ARG B   74  GLY B   82  1                                   9    
HELIX   31  31 PRO B  111  GLY B  114  5                                   4    
HELIX   32  32 THR B  115  ARG B  129  1                                  15    
HELIX   33  33 HIS B  146  ASP B  155  1                                  10    
HELIX   34  34 ASN B  213  GLY B  231  1                                  19    
HELIX   35  35 ALA B  239  LEU B  243  5                                   5    
HELIX   36  36 LEU B  254  PHE B  272  1                                  19    
HELIX   37  37 ASP B  287  GLY B  293  5                                   7    
HELIX   38  38 ASP B  294  GLY B  298  5                                   5    
HELIX   39  39 PRO B  309  GLU B  321  1                                  13    
HELIX   40  40 ARG B  323  THR B  333  1                                  11    
HELIX   41  41 ARG B  384  LEU B  389  1                                   6    
HELIX   42  42 ASP B  392  LEU B  406  1                                  15    
HELIX   43  43 GLY B  415  GLY B  419  5                                   5    
HELIX   44  44 VAL B  423  GLY B  427  5                                   5    
HELIX   45  45 ASP B  441  PHE B  446  5                                   6    
HELIX   46  46 ASN B  470  ASP B  476  1                                   7    
HELIX   47  47 SER B  480  ARG B  494  1                                  15    
HELIX   48  48 PRO B  496  GLY B  501  1                                   6    
HELIX   49  49 LEU B  545  THR B  549  5                                   5    
SHEET    1   A 2 HIS A  17  VAL A  18  0                                        
SHEET    2   A 2 VAL A  23  GLU A  24 -1  O  GLU A  24   N  HIS A  17           
SHEET    1   B 9 PHE A  49  GLU A  51  0                                        
SHEET    2   B 9 CYS A  85  LEU A  88  1  O  TRP A  87   N  TYR A  50           
SHEET    3   B 9 ARG A 132  VAL A 138  1  O  ARG A 132   N  ILE A  86           
SHEET    4   B 9 GLY A 234  ASP A 238  1  O  ASP A 238   N  LEU A 137           
SHEET    5   B 9 VAL A 276  ALA A 279  1  O  LEU A 278   N  LEU A 237           
SHEET    6   B 9 MET A 304  PHE A 306  1  O  MET A 304   N  ALA A 279           
SHEET    7   B 9 GLN A 341  ILE A 344  1  O  GLY A 343   N  ALA A 305           
SHEET    8   B 9 SER A 409  TYR A 413  1  O  SER A 409   N  TRP A 342           
SHEET    9   B 9 PHE A  49  GLU A  51  1  N  PHE A  49   O  LEU A 412           
SHEET    1   C 2 TYR A  92  ASP A  93  0                                        
SHEET    2   C 2 ASP A 105  VAL A 109 -1  O  LYS A 108   N  ASP A  93           
SHEET    1   D 3 TRP A 166  SER A 167  0                                        
SHEET    2   D 3 PHE A 197  TRP A 199 -1  O  PHE A 197   N  SER A 167           
SHEET    3   D 3 TRP A 188  PHE A 190 -1  N  SER A 189   O  TYR A 198           
SHEET    1   E 5 ALA A 502  GLU A 505  0                                        
SHEET    2   E 5 VAL A 513  GLN A 519 -1  O  GLN A 519   N  ALA A 502           
SHEET    3   E 5 THR A 527  ASN A 533 -1  O  ASN A 532   N  LEU A 514           
SHEET    4   E 5 PHE A 579  THR A 585 -1  O  LEU A 584   N  THR A 527           
SHEET    5   E 5 THR A 552  GLU A 555 -1  N  THR A 552   O  THR A 585           
SHEET    1   F 2 GLN A 539  LEU A 543  0                                        
SHEET    2   F 2 TYR A 570  LEU A 574 -1  O  TYR A 570   N  LEU A 543           
SHEET    1   G 2 HIS B  17  VAL B  18  0                                        
SHEET    2   G 2 VAL B  23  GLU B  24 -1  O  GLU B  24   N  HIS B  17           
SHEET    1   H 9 PHE B  49  GLU B  51  0                                        
SHEET    2   H 9 CYS B  85  LEU B  88  1  O  TRP B  87   N  TYR B  50           
SHEET    3   H 9 ARG B 132  VAL B 138  1  O  ARG B 132   N  ILE B  86           
SHEET    4   H 9 GLY B 234  ASP B 238  1  O  ARG B 236   N  LEU B 137           
SHEET    5   H 9 VAL B 276  ALA B 279  1  O  LEU B 278   N  LEU B 237           
SHEET    6   H 9 MET B 304  PHE B 306  1  O  MET B 304   N  ALA B 279           
SHEET    7   H 9 GLN B 341  PHE B 345  1  O  GLY B 343   N  ALA B 305           
SHEET    8   H 9 SER B 409  TYR B 413  1  O  SER B 409   N  TRP B 342           
SHEET    9   H 9 PHE B  49  GLU B  51  1  N  PHE B  49   O  LEU B 412           
SHEET    1   I 2 TYR B  92  ASP B  93  0                                        
SHEET    2   I 2 ASP B 105  VAL B 109 -1  O  LYS B 108   N  ASP B  93           
SHEET    1   J 3 TRP B 166  SER B 167  0                                        
SHEET    2   J 3 PHE B 197  TRP B 199 -1  O  PHE B 197   N  SER B 167           
SHEET    3   J 3 TRP B 188  PHE B 190 -1  N  SER B 189   O  TYR B 198           
SHEET    1   K 6 ALA B 502  GLU B 505  0                                        
SHEET    2   K 6 VAL B 513  GLN B 519 -1  O  GLN B 519   N  ALA B 502           
SHEET    3   K 6 THR B 527  ASN B 533 -1  O  CYS B 530   N  TYR B 516           
SHEET    4   K 6 PHE B 579  THR B 585 -1  O  PHE B 582   N  LEU B 529           
SHEET    5   K 6 THR B 552  GLU B 555 -1  N  VAL B 554   O  GLN B 583           
SHEET    6   K 6 VAL B 560  GLU B 561 -1  O  VAL B 560   N  GLU B 555           
SHEET    1   L 2 GLN B 539  LEU B 543  0                                        
SHEET    2   L 2 TYR B 570  LEU B 574 -1  O  LEU B 572   N  ILE B 541           
LINK        CA    CA A 701                 O   HOH A 812     1555   1555  2.40  
LINK         OD2 ASP A 208                CA    CA A 701     1555   1555  2.43  
LINK         OE2 GLU A 245                CA    CA A 701     1555   1555  2.47  
LINK         O   TYR A 242                CA    CA A 701     1555   1555  2.49  
LINK         O   LEU B 243                CA    CA B 701     1555   1555  2.60  
LINK         O   LEU A 243                CA    CA A 701     1555   1555  2.63  
LINK         O   TYR B 242                CA    CA B 701     1555   1555  2.66  
LINK         OD2 ASP B 208                CA    CA B 701     1555   1555  2.70  
LINK         OE1 GLU B 245                CA    CA B 701     1555   1555  2.97  
LINK         OE2 GLU B 245                CA    CA B 701     1555   1555  3.13  
CISPEP   1 GLU A   19    GLY A   20          0        -5.63                     
CISPEP   2 GLU B   19    GLY B   20          0        -4.28                     
CISPEP   3 GLU B  351    LEU B  352          0         0.63                     
SITE     1 AC1  6 ASN A 140  ASP A 208  TYR A 242  LEU A 243                    
SITE     2 AC1  6 GLU A 245  HOH A 812                                          
SITE     1 AC2  4 ARG A 494  HIS A 495  HIS A 559  GLN A 583                    
SITE     1 AC3  3 THR A  42  LYS A  45  HIS A  46                               
SITE     1 AC4  8 LEU A 346  ARG A 347  ARG A 382  ARG A 383                    
SITE     2 AC4  8 ARG A 384  LEU A 385  ASP A 416  GOL A 705                    
SITE     1 AC5 11 LEU A 346  ARG A 347  ASN A 348  HIS A 349                    
SITE     2 AC5 11 ASN A 378  VAL A 379  GLY A 380  ILE A 381                    
SITE     3 AC5 11 ARG A 382  ARG A 383  GOL A 704                               
SITE     1 AC6  3 SER A  94  PRO A  95  ARG A 104                               
SITE     1 AC7  2 ARG A 128  ARG A 129                                          
SITE     1 AC8  8 GLU A  51  TRP A  87  TYR A 101  ARG A 236                    
SITE     2 AC8  8 ARG A 347  ASP A 350  GLU A 351  ARG A 382                    
SITE     1 AC9  5 ASN B 140  ASP B 208  TYR B 242  LEU B 243                    
SITE     2 AC9  5 GLU B 245                                                     
SITE     1 BC1  5 ARG B 494  HIS B 495  LEU B 556  HIS B 559                    
SITE     2 BC1  5 GLN B 583                                                     
SITE     1 BC2  7 GLU B  51  TRP B  87  ARG B 236  ARG B 347                    
SITE     2 BC2  7 ASP B 350  ARG B 382  ARG B 433                               
SITE     1 BC3  3 THR B  42  HIS B  46  VAL B 500                               
SITE     1 BC4  1 ARG B 104                                                     
CRYST1  161.640  161.640  139.110  90.00  90.00 120.00 P 32 1 2     12          
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      0.006187  0.003572  0.000000        0.00000                         
SCALE2      0.000000  0.007144  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007189        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2 -0.992654  0.061440 -0.104229       78.05856    1                    
MTRIX2   2 -0.039932 -0.979566 -0.197118      -57.41048    1                    
MTRIX3   2 -0.114210 -0.191508  0.974824       -1.70678    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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