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Database: PDB
Entry: 4DSH
LinkDB: 4DSH
Original site: 4DSH 
HEADER    ISOMERASE                               18-FEB-12   4DSH              
TITLE     CRYSTAL STRUCTURE OF REDUCED UDP-GALACTOPYRANOSE MUTASE               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UDP-GALACTOPYRANOSE MUTASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 5.4.99.9;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI;                              
SOURCE   3 ORGANISM_TAXID: 5693;                                                
SOURCE   4 GENE: TC00.1047053507993.160;                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ROSSMANN FOLD, FLAVIN ADENINE DINUCLEOTIDE, ISOMERASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.DHATWALIA,H.SINGH,J.J.TANNER                                        
REVDAT   3   13-SEP-23 4DSH    1       REMARK SEQADV                            
REVDAT   2   05-SEP-12 4DSH    1       JRNL                                     
REVDAT   1   13-JUN-12 4DSH    0                                                
JRNL        AUTH   R.DHATWALIA,H.SINGH,M.OPPENHEIMER,P.SOBRADO,J.J.TANNER       
JRNL        TITL   CRYSTAL STRUCTURES OF TRYPANOSOMA CRUZI UDP-GALACTOPYRANOSE  
JRNL        TITL 2 MUTASE IMPLICATE FLEXIBILITY OF THE HISTIDINE LOOP IN ENZYME 
JRNL        TITL 3 ACTIVATION.                                                  
JRNL        REF    BIOCHEMISTRY                  V.  51  4968 2012              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   22646091                                                     
JRNL        DOI    10.1021/BI300498C                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.6.2_432                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.90                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 102877                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5134                            
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 46.9117 -  4.8459    0.99    10348   557  0.1707 0.1876        
REMARK   3     2  4.8459 -  3.8469    1.00     9907   531  0.1304 0.1518        
REMARK   3     3  3.8469 -  3.3608    1.00     9809   516  0.1801 0.2059        
REMARK   3     4  3.3608 -  3.0536    1.00     9776   504  0.1994 0.2278        
REMARK   3     5  3.0536 -  2.8347    1.00     9694   515  0.1876 0.2247        
REMARK   3     6  2.8347 -  2.6676    1.00     9694   498  0.1936 0.2427        
REMARK   3     7  2.6676 -  2.5340    1.00     9663   543  0.2030 0.2386        
REMARK   3     8  2.5340 -  2.4237    1.00     9665   480  0.2125 0.2674        
REMARK   3     9  2.4237 -  2.3304    1.00     9603   496  0.2252 0.2782        
REMARK   3    10  2.3304 -  2.2500    1.00     9584   494  0.2381 0.2853        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.30                                          
REMARK   3   SHRINKAGE RADIUS   : 1.06                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 20.23                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.480           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.31090                                              
REMARK   3    B22 (A**2) : 3.31090                                              
REMARK   3    B33 (A**2) : -6.62170                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           7914                                  
REMARK   3   ANGLE     :  1.106          10820                                  
REMARK   3   CHIRALITY :  0.073           1138                                  
REMARK   3   PLANARITY :  0.005           1374                                  
REMARK   3   DIHEDRAL  : 15.538           2929                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  65.6826 -12.4597 -35.3515              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1531 T22:   0.0444                                     
REMARK   3      T33:   0.0655 T12:  -0.0313                                     
REMARK   3      T13:   0.0031 T23:   0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1462 L22:   0.7861                                     
REMARK   3      L33:   0.2070 L12:   0.0230                                     
REMARK   3      L13:   0.0229 L23:  -0.4412                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0302 S12:  -0.0175 S13:  -0.0030                       
REMARK   3      S21:   0.1534 S22:   0.0018 S23:   0.0561                       
REMARK   3      S31:  -0.0977 S32:  -0.0087 S33:   0.0229                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  69.9004 -41.9500 -67.6645              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0395 T22:   0.0581                                     
REMARK   3      T33:   0.0402 T12:  -0.0201                                     
REMARK   3      T13:  -0.0293 T23:  -0.0145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4699 L22:   0.4046                                     
REMARK   3      L33:   0.2583 L12:  -0.0299                                     
REMARK   3      L13:   0.0635 L23:   0.0898                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0161 S12:  -0.0035 S13:   0.0524                       
REMARK   3      S21:  -0.0606 S22:   0.0181 S23:   0.0173                       
REMARK   3      S31:   0.0092 S32:   0.0604 S33:  -0.0320                       
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 4DSH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000070725.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-NOV-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 102978                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 8.200                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3UTE                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M AMMONIUM SULFATE, 0.5% PEG8000,    
REMARK 280  0.1 M HEPES, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE     
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 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   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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      236.25933            
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      118.12967            
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      177.19450            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       59.06483            
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      295.32417            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      236.25933            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      118.12967            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       59.06483            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      177.19450            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      295.32417            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ALA A    -2                                                      
REMARK 465     ILE A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     GLN A   477                                                      
REMARK 465     LYS A   478                                                      
REMARK 465     ASP A   479                                                      
REMARK 465     MET A   480                                                      
REMARK 465     VAL A   481                                                      
REMARK 465     ALA B    -2                                                      
REMARK 465     ILE B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     LEU B     5                                                      
REMARK 465     GLY B   466                                                      
REMARK 465     THR B   467                                                      
REMARK 465     ARG B   468                                                      
REMARK 465     ALA B   469                                                      
REMARK 465     THR B   470                                                      
REMARK 465     LEU B   476                                                      
REMARK 465     GLN B   477                                                      
REMARK 465     LYS B   478                                                      
REMARK 465     ASP B   479                                                      
REMARK 465     MET B   480                                                      
REMARK 465     VAL B   481                                                      
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     LYS A  31    CG   CD   CE   NZ                                   
REMARK 470     LYS A 115    CE   NZ                                             
REMARK 470     GLU A 131    OE1  OE2                                            
REMARK 470     GLU A 146    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 150    OD1  OD2                                            
REMARK 470     GLU A 171    CD   OE1  OE2                                       
REMARK 470     GLU A 174    OE1  OE2                                            
REMARK 470     GLU A 183    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 278    CD   CE   NZ                                        
REMARK 470     LYS A 336    NZ                                                  
REMARK 470     GLU A 341    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 354    CD   CE   NZ                                        
REMARK 470     GLU A 407    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 428    CZ   NH1  NH2                                       
REMARK 470     GLU A 454    OE1  OE2                                            
REMARK 470     ASN A 460    CG   OD1  ND2                                       
REMARK 470     ARG A 463    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  31    CE   NZ                                             
REMARK 470     GLU B  52    OE1  OE2                                            
REMARK 470     LYS B 115    CE   NZ                                             
REMARK 470     GLU B 131    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 171    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 174    OE1  OE2                                            
REMARK 470     ARG B 184    NH1  NH2                                            
REMARK 470     ARG B 187    NH1  NH2                                            
REMARK 470     GLU B 226    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 273    CE   NZ                                             
REMARK 470     LYS B 278    CG   CD   CE   NZ                                   
REMARK 470     GLU B 282    OE1  OE2                                            
REMARK 470     LYS B 336    NZ                                                  
REMARK 470     GLU B 341    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 354    CD   CE   NZ                                        
REMARK 470     GLU B 407    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 412    OE1  OE2                                            
REMARK 470     ARG B 428    CZ   NH1  NH2                                       
REMARK 470     GLU B 454    CD   OE1  OE2                                       
REMARK 470     ARG B 463    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 471    OG1  CG2                                            
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 152      -59.90   -123.30                                   
REMARK 500    ASN A 192       55.73     39.57                                   
REMARK 500    PHE A 234       40.08   -100.82                                   
REMARK 500    CYS A 314      -78.79   -105.30                                   
REMARK 500    THR A 467     -168.42   -124.60                                   
REMARK 500    PHE B 152      -55.72   -125.84                                   
REMARK 500    PHE B 234       42.78   -103.88                                   
REMARK 500    CYS B 314      -83.05   -100.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FDA A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FDA B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 503                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DSG   RELATED DB: PDB                                   
DBREF  4DSH A    1   480  UNP    Q4E1W2   Q4E1W2_TRYCC     1    480             
DBREF  4DSH B    1   480  UNP    Q4E1W2   Q4E1W2_TRYCC     1    480             
SEQADV 4DSH ALA A   -2  UNP  Q4E1W2              EXPRESSION TAG                 
SEQADV 4DSH ILE A   -1  UNP  Q4E1W2              EXPRESSION TAG                 
SEQADV 4DSH ALA A    0  UNP  Q4E1W2              EXPRESSION TAG                 
SEQADV 4DSH VAL A  481  UNP  Q4E1W2              CLONING ARTIFACT               
SEQADV 4DSH ALA B   -2  UNP  Q4E1W2              EXPRESSION TAG                 
SEQADV 4DSH ILE B   -1  UNP  Q4E1W2              EXPRESSION TAG                 
SEQADV 4DSH ALA B    0  UNP  Q4E1W2              EXPRESSION TAG                 
SEQADV 4DSH VAL B  481  UNP  Q4E1W2              CLONING ARTIFACT               
SEQRES   1 A  484  ALA ILE ALA MET ALA GLU LEU LEU THR PRO LYS ILE VAL          
SEQRES   2 A  484  ILE ILE GLY ALA GLY PRO THR GLY LEU GLY ALA ALA VAL          
SEQRES   3 A  484  ARG LEU THR GLU LEU GLY TYR LYS ASN TRP HIS LEU TYR          
SEQRES   4 A  484  GLU CYS ASN ASP THR PRO GLY GLY LEU SER ARG SER PHE          
SEQRES   5 A  484  LEU ASP GLU ASN GLY PHE THR TRP ASP LEU GLY GLY HIS          
SEQRES   6 A  484  VAL ILE PHE SER HIS TYR GLN TYR PHE ASP ASP VAL MET          
SEQRES   7 A  484  ASP TRP ALA VAL GLN GLY TRP ASN VAL LEU GLN ARG GLU          
SEQRES   8 A  484  SER TRP VAL TRP VAL ARG GLY ARG TRP VAL PRO TYR PRO          
SEQRES   9 A  484  PHE GLN ASN ASN ILE HIS ARG LEU PRO GLU GLN ASP ARG          
SEQRES  10 A  484  LYS ARG CYS LEU ASP GLU LEU VAL ARG SER HIS ALA ARG          
SEQRES  11 A  484  THR TYR THR GLU PRO PRO ASN ASN PHE GLU GLU SER PHE          
SEQRES  12 A  484  THR ARG GLN PHE GLY GLU GLY ILE ALA ASP ILE PHE MET          
SEQRES  13 A  484  ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO PRO CYS          
SEQRES  14 A  484  LEU MET SER THR GLU TRP VAL GLU GLU ARG VAL ALA PRO          
SEQRES  15 A  484  VAL ASP LEU GLU ARG ILE ARG ARG ASN ILE GLN GLU ASN          
SEQRES  16 A  484  ARG ASP ASP LEU GLY TRP GLY PRO ASN ALA THR PHE ARG          
SEQRES  17 A  484  PHE PRO GLN ARG GLY GLY THR GLY ILE ILE TYR GLN ALA          
SEQRES  18 A  484  ILE LYS GLU LYS LEU PRO SER GLU LYS LEU THR PHE ASN          
SEQRES  19 A  484  SER GLY PHE GLN ALA ILE ALA ILE ASP ALA ASP ALA LYS          
SEQRES  20 A  484  THR ILE THR PHE SER ASN GLY GLU VAL VAL SER TYR ASP          
SEQRES  21 A  484  TYR LEU ILE SER THR VAL PRO PHE ASP ASN LEU LEU ARG          
SEQRES  22 A  484  MET THR LYS GLY THR GLY PHE LYS GLY TYR ASP GLU TRP          
SEQRES  23 A  484  PRO ALA ILE ALA ASP LYS MET VAL TYR SER SER THR ASN          
SEQRES  24 A  484  VAL ILE GLY ILE GLY VAL LYS GLY THR PRO PRO PRO HIS          
SEQRES  25 A  484  LEU LYS THR ALA CYS TRP LEU TYR PHE PRO GLU ASP THR          
SEQRES  26 A  484  SER PRO PHE TYR ARG ALA THR VAL PHE SER ASN TYR SER          
SEQRES  27 A  484  LYS TYR ASN VAL PRO GLU GLY HIS TRP SER LEU MET LEU          
SEQRES  28 A  484  GLU VAL SER GLU SER LYS TYR LYS PRO VAL ASN HIS SER          
SEQRES  29 A  484  THR LEU ILE GLU ASP CYS ILE VAL GLY CYS LEU ALA SER          
SEQRES  30 A  484  ASN LEU LEU LEU PRO GLU ASP LEU LEU VAL SER LYS TRP          
SEQRES  31 A  484  HIS TYR ARG ILE GLU LYS GLY TYR PRO THR PRO PHE ILE          
SEQRES  32 A  484  GLY ARG ASN ASN LEU LEU GLU LYS ALA GLN PRO GLU LEU          
SEQRES  33 A  484  MET SER ARG CYS ILE TYR SER ARG GLY ARG PHE GLY ALA          
SEQRES  34 A  484  TRP ARG TYR GLU VAL GLY ASN GLN ASP HIS SER PHE MET          
SEQRES  35 A  484  GLN GLY VAL GLU ALA ILE ASP HIS VAL LEU GLY LEU ALA          
SEQRES  36 A  484  THR GLU GLU THR THR VAL ALA ASN PRO GLY ARG VAL ASN          
SEQRES  37 A  484  GLY THR ARG ALA THR THR HIS PHE GLY LEU LEU GLN LYS          
SEQRES  38 A  484  ASP MET VAL                                                  
SEQRES   1 B  484  ALA ILE ALA MET ALA GLU LEU LEU THR PRO LYS ILE VAL          
SEQRES   2 B  484  ILE ILE GLY ALA GLY PRO THR GLY LEU GLY ALA ALA VAL          
SEQRES   3 B  484  ARG LEU THR GLU LEU GLY TYR LYS ASN TRP HIS LEU TYR          
SEQRES   4 B  484  GLU CYS ASN ASP THR PRO GLY GLY LEU SER ARG SER PHE          
SEQRES   5 B  484  LEU ASP GLU ASN GLY PHE THR TRP ASP LEU GLY GLY HIS          
SEQRES   6 B  484  VAL ILE PHE SER HIS TYR GLN TYR PHE ASP ASP VAL MET          
SEQRES   7 B  484  ASP TRP ALA VAL GLN GLY TRP ASN VAL LEU GLN ARG GLU          
SEQRES   8 B  484  SER TRP VAL TRP VAL ARG GLY ARG TRP VAL PRO TYR PRO          
SEQRES   9 B  484  PHE GLN ASN ASN ILE HIS ARG LEU PRO GLU GLN ASP ARG          
SEQRES  10 B  484  LYS ARG CYS LEU ASP GLU LEU VAL ARG SER HIS ALA ARG          
SEQRES  11 B  484  THR TYR THR GLU PRO PRO ASN ASN PHE GLU GLU SER PHE          
SEQRES  12 B  484  THR ARG GLN PHE GLY GLU GLY ILE ALA ASP ILE PHE MET          
SEQRES  13 B  484  ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO PRO CYS          
SEQRES  14 B  484  LEU MET SER THR GLU TRP VAL GLU GLU ARG VAL ALA PRO          
SEQRES  15 B  484  VAL ASP LEU GLU ARG ILE ARG ARG ASN ILE GLN GLU ASN          
SEQRES  16 B  484  ARG ASP ASP LEU GLY TRP GLY PRO ASN ALA THR PHE ARG          
SEQRES  17 B  484  PHE PRO GLN ARG GLY GLY THR GLY ILE ILE TYR GLN ALA          
SEQRES  18 B  484  ILE LYS GLU LYS LEU PRO SER GLU LYS LEU THR PHE ASN          
SEQRES  19 B  484  SER GLY PHE GLN ALA ILE ALA ILE ASP ALA ASP ALA LYS          
SEQRES  20 B  484  THR ILE THR PHE SER ASN GLY GLU VAL VAL SER TYR ASP          
SEQRES  21 B  484  TYR LEU ILE SER THR VAL PRO PHE ASP ASN LEU LEU ARG          
SEQRES  22 B  484  MET THR LYS GLY THR GLY PHE LYS GLY TYR ASP GLU TRP          
SEQRES  23 B  484  PRO ALA ILE ALA ASP LYS MET VAL TYR SER SER THR ASN          
SEQRES  24 B  484  VAL ILE GLY ILE GLY VAL LYS GLY THR PRO PRO PRO HIS          
SEQRES  25 B  484  LEU LYS THR ALA CYS TRP LEU TYR PHE PRO GLU ASP THR          
SEQRES  26 B  484  SER PRO PHE TYR ARG ALA THR VAL PHE SER ASN TYR SER          
SEQRES  27 B  484  LYS TYR ASN VAL PRO GLU GLY HIS TRP SER LEU MET LEU          
SEQRES  28 B  484  GLU VAL SER GLU SER LYS TYR LYS PRO VAL ASN HIS SER          
SEQRES  29 B  484  THR LEU ILE GLU ASP CYS ILE VAL GLY CYS LEU ALA SER          
SEQRES  30 B  484  ASN LEU LEU LEU PRO GLU ASP LEU LEU VAL SER LYS TRP          
SEQRES  31 B  484  HIS TYR ARG ILE GLU LYS GLY TYR PRO THR PRO PHE ILE          
SEQRES  32 B  484  GLY ARG ASN ASN LEU LEU GLU LYS ALA GLN PRO GLU LEU          
SEQRES  33 B  484  MET SER ARG CYS ILE TYR SER ARG GLY ARG PHE GLY ALA          
SEQRES  34 B  484  TRP ARG TYR GLU VAL GLY ASN GLN ASP HIS SER PHE MET          
SEQRES  35 B  484  GLN GLY VAL GLU ALA ILE ASP HIS VAL LEU GLY LEU ALA          
SEQRES  36 B  484  THR GLU GLU THR THR VAL ALA ASN PRO GLY ARG VAL ASN          
SEQRES  37 B  484  GLY THR ARG ALA THR THR HIS PHE GLY LEU LEU GLN LYS          
SEQRES  38 B  484  ASP MET VAL                                                  
HET    UDP  A 501      25                                                       
HET    FDA  A 502      53                                                       
HET    SO4  A 503       5                                                       
HET    SO4  A 504       5                                                       
HET    SO4  A 505       5                                                       
HET    EPE  A 506      15                                                       
HET    FDA  B 501      53                                                       
HET    UDP  B 502      25                                                       
HET    SO4  B 503       5                                                       
HETNAM     UDP URIDINE-5'-DIPHOSPHATE                                           
HETNAM     FDA DIHYDROFLAVINE-ADENINE DINUCLEOTIDE                              
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETSYN     EPE HEPES                                                            
FORMUL   3  UDP    2(C9 H14 N2 O12 P2)                                          
FORMUL   4  FDA    2(C27 H35 N9 O15 P2)                                         
FORMUL   5  SO4    4(O4 S 2-)                                                   
FORMUL   8  EPE    C8 H18 N2 O4 S                                               
FORMUL  12  HOH   *246(H2 O)                                                    
HELIX    1   1 GLY A   15  GLY A   29  1                                  15    
HELIX    2   2 GLY A   43  SER A   46  5                                   4    
HELIX    3   3 TYR A   68  VAL A   79  1                                  12    
HELIX    4   4 PRO A  101  LEU A  109  5                                   9    
HELIX    5   5 PRO A  110  ALA A  126  1                                  17    
HELIX    6   6 ASN A  135  PHE A  152  1                                  18    
HELIX    7   7 PHE A  152  ALA A  162  1                                  11    
HELIX    8   8 PRO A  164  MET A  168  5                                   5    
HELIX    9   9 THR A  170  GLU A  174  5                                   5    
HELIX   10  10 ASP A  181  ASN A  192  1                                  12    
HELIX   11  11 THR A  212  LEU A  223  1                                  12    
HELIX   12  12 PRO A  224  GLU A  226  5                                   3    
HELIX   13  13 SER A  232  PHE A  234  5                                   3    
HELIX   14  14 PRO A  264  MET A  271  1                                   8    
HELIX   15  15 GLY A  279  ASP A  281  5                                   3    
HELIX   16  16 GLU A  282  MET A  290  1                                   9    
HELIX   17  17 PRO A  307  LYS A  311  5                                   5    
HELIX   18  18 PHE A  331  TYR A  334  5                                   4    
HELIX   19  19 SER A  335  VAL A  339  5                                   5    
HELIX   20  20 THR A  362  SER A  374  1                                  13    
HELIX   21  21 GLY A  401  SER A  415  1                                  15    
HELIX   22  22 ARG A  428  GLY A  432  5                                   5    
HELIX   23  23 ASN A  433  LEU A  449  1                                  17    
HELIX   24  24 GLU A  455  ASN A  460  1                                   6    
HELIX   25  25 ASN A  460  THR A  467  1                                   8    
HELIX   26  26 GLY B   15  LEU B   28  1                                  14    
HELIX   27  27 GLY B   43  SER B   46  5                                   4    
HELIX   28  28 TYR B   68  VAL B   79  1                                  12    
HELIX   29  29 PRO B  101  LEU B  109  5                                   9    
HELIX   30  30 PRO B  110  ARG B  127  1                                  18    
HELIX   31  31 ASN B  135  PHE B  152  1                                  18    
HELIX   32  32 PHE B  152  ALA B  162  1                                  11    
HELIX   33  33 PRO B  164  MET B  168  5                                   5    
HELIX   34  34 THR B  170  GLU B  174  5                                   5    
HELIX   35  35 ASP B  181  ASN B  192  1                                  12    
HELIX   36  36 THR B  212  LEU B  223  1                                  12    
HELIX   37  37 PRO B  224  GLU B  226  5                                   3    
HELIX   38  38 SER B  232  PHE B  234  5                                   3    
HELIX   39  39 PRO B  264  MET B  271  1                                   8    
HELIX   40  40 GLY B  279  ASP B  281  5                                   3    
HELIX   41  41 GLU B  282  MET B  290  1                                   9    
HELIX   42  42 PRO B  307  LYS B  311  5                                   5    
HELIX   43  43 PHE B  331  TYR B  334  5                                   4    
HELIX   44  44 SER B  335  VAL B  339  5                                   5    
HELIX   45  45 THR B  362  SER B  374  1                                  13    
HELIX   46  46 GLY B  401  ARG B  416  1                                  16    
HELIX   47  47 ARG B  428  GLY B  432  5                                   5    
HELIX   48  48 ASN B  433  LEU B  449  1                                  17    
HELIX   49  49 GLU B  455  ASN B  460  1                                   6    
HELIX   50  50 ASN B  460  ASN B  465  1                                   6    
SHEET    1   A 5 LEU A 228  PHE A 230  0                                        
SHEET    2   A 5 TRP A  33  GLU A  37  1  N  GLU A  37   O  THR A 229           
SHEET    3   A 5 ILE A   9  ILE A  12  1  N  ILE A  11   O  TYR A  36           
SHEET    4   A 5 TYR A 258  SER A 261  1  O  ILE A 260   N  VAL A  10           
SHEET    5   A 5 ILE A 418  SER A 420  1  O  TYR A 419   N  LEU A 259           
SHEET    1   B 2 SER A  48  LEU A  50  0                                        
SHEET    2   B 2 THR A  56  ASP A  58 -1  O  TRP A  57   N  PHE A  49           
SHEET    1   C 2 TRP A  82  GLN A  86  0                                        
SHEET    2   C 2 THR A 203  PRO A 207 -1  O  PHE A 206   N  ASN A  83           
SHEET    1   D 7 ARG A  96  PRO A  99  0                                        
SHEET    2   D 7 TRP A  90  VAL A  93 -1  N  VAL A  91   O  VAL A  98           
SHEET    3   D 7 TRP A 315  TYR A 317  1  O  TYR A 317   N  TRP A  92           
SHEET    4   D 7 ARG A 327  THR A 329 -1  O  ALA A 328   N  LEU A 316           
SHEET    5   D 7 HIS A 343  GLU A 352 -1  O  MET A 347   N  THR A 329           
SHEET    6   D 7 TYR A 292  LYS A 303 -1  N  ILE A 298   O  LEU A 348           
SHEET    7   D 7 LEU A 383  PRO A 396 -1  O  ILE A 391   N  THR A 295           
SHEET    1   E 4 VAL A 253  SER A 255  0                                        
SHEET    2   E 4 THR A 245  PHE A 248 -1  N  ILE A 246   O  VAL A 254           
SHEET    3   E 4 ALA A 236  ASP A 240 -1  N  ALA A 238   O  THR A 247           
SHEET    4   E 4 THR A 272  LYS A 273  1  O  LYS A 273   N  ILE A 239           
SHEET    1   F 5 LEU B 228  PHE B 230  0                                        
SHEET    2   F 5 TRP B  33  GLU B  37  1  N  GLU B  37   O  THR B 229           
SHEET    3   F 5 ILE B   9  ILE B  12  1  N  ILE B  11   O  HIS B  34           
SHEET    4   F 5 TYR B 258  SER B 261  1  O  ILE B 260   N  VAL B  10           
SHEET    5   F 5 ILE B 418  SER B 420  1  O  TYR B 419   N  LEU B 259           
SHEET    1   G 2 SER B  48  LEU B  50  0                                        
SHEET    2   G 2 THR B  56  ASP B  58 -1  O  TRP B  57   N  PHE B  49           
SHEET    1   H 2 TRP B  82  GLN B  86  0                                        
SHEET    2   H 2 THR B 203  PRO B 207 -1  O  PHE B 204   N  LEU B  85           
SHEET    1   I 7 ARG B  96  PRO B  99  0                                        
SHEET    2   I 7 TRP B  90  VAL B  93 -1  N  VAL B  91   O  VAL B  98           
SHEET    3   I 7 TRP B 315  TYR B 317  1  O  TYR B 317   N  TRP B  90           
SHEET    4   I 7 ARG B 327  THR B 329 -1  O  ALA B 328   N  LEU B 316           
SHEET    5   I 7 HIS B 343  GLU B 352 -1  O  MET B 347   N  THR B 329           
SHEET    6   I 7 TYR B 292  LYS B 303 -1  N  SER B 294   O  GLU B 352           
SHEET    7   I 7 LEU B 383  PRO B 396 -1  O  TRP B 387   N  GLY B 299           
SHEET    1   J 4 VAL B 253  SER B 255  0                                        
SHEET    2   J 4 THR B 245  PHE B 248 -1  N  ILE B 246   O  VAL B 254           
SHEET    3   J 4 ALA B 236  ASP B 240 -1  N  ALA B 238   O  THR B 247           
SHEET    4   J 4 THR B 272  LYS B 273  1  O  LYS B 273   N  ILE B 239           
SSBOND   1 CYS A  166    CYS B  166                          1555   1555  2.11  
CISPEP   1 TYR A  100    PRO A  101          0        -4.88                     
CISPEP   2 TYR B  100    PRO B  101          0        -1.24                     
SITE     1 AC1 20 TYR A 100  PRO A 101  PHE A 102  GLN A 103                    
SITE     2 AC1 20 PHE A 152  MET A 153  ASN A 157  TRP A 161                    
SITE     3 AC1 20 ARG A 176  VAL A 177  TYR A 317  ARG A 327                    
SITE     4 AC1 20 TYR A 395  TYR A 429  HOH A 616  HOH A 630                    
SITE     5 AC1 20 HOH A 632  HOH A 633  HOH A 634  HOH A 671                    
SITE     1 AC2 35 ILE A  12  GLY A  13  GLY A  15  PRO A  16                    
SITE     2 AC2 35 THR A  17  GLU A  37  CYS A  38  ASN A  39                    
SITE     3 AC2 35 GLY A  44  LEU A  45  SER A  46  LEU A  59                    
SITE     4 AC2 35 GLY A  61  HIS A  62  VAL A  63  PHE A  65                    
SITE     5 AC2 35 PHE A 234  GLN A 235  ALA A 236  VAL A 263                    
SITE     6 AC2 35 GLU A 349  GLY A 394  GLY A 422  ARG A 423                    
SITE     7 AC2 35 GLY A 432  ASN A 433  GLN A 434  SER A 437                    
SITE     8 AC2 35 HOH A 601  HOH A 605  HOH A 617  HOH A 619                    
SITE     9 AC2 35 HOH A 660  HOH A 664  HOH A 715                               
SITE     1 AC3  4 ARG A 270  TYR A 292  HOH A 644  HOH A 665                    
SITE     1 AC4  4 HIS A 388  TYR A 389  ARG A 390  EPE A 506                    
SITE     1 AC5  4 VAL A 358  ASN A 359  HIS A 360  SER A 361                    
SITE     1 AC6  7 HIS A 388  TYR A 389  ARG A 390  GLU A 392                    
SITE     2 AC6  7 SO4 A 504  HOH A 668  HOH A 709                               
SITE     1 AC7 35 ILE B  12  GLY B  13  GLY B  15  PRO B  16                    
SITE     2 AC7 35 THR B  17  GLU B  37  CYS B  38  ASN B  39                    
SITE     3 AC7 35 GLY B  43  GLY B  44  LEU B  45  SER B  46                    
SITE     4 AC7 35 LEU B  59  GLY B  61  HIS B  62  VAL B  63                    
SITE     5 AC7 35 PHE B 234  GLN B 235  ALA B 236  THR B 262                    
SITE     6 AC7 35 VAL B 263  GLU B 349  GLY B 394  GLY B 422                    
SITE     7 AC7 35 ARG B 423  GLY B 432  ASN B 433  GLN B 434                    
SITE     8 AC7 35 SER B 437  HOH B 602  HOH B 605  HOH B 628                    
SITE     9 AC7 35 HOH B 629  HOH B 632  HOH B 671                               
SITE     1 AC8 20 TYR B 100  PRO B 101  PHE B 102  GLN B 103                    
SITE     2 AC8 20 PHE B 152  MET B 153  ASN B 157  TRP B 161                    
SITE     3 AC8 20 ARG B 176  VAL B 177  TYR B 317  ARG B 327                    
SITE     4 AC8 20 TYR B 395  TYR B 429  HOH B 603  HOH B 604                    
SITE     5 AC8 20 HOH B 641  HOH B 642  HOH B 644  HOH B 668                    
SITE     1 AC9  5 ASP B 266  ARG B 270  TYR B 292  HOH B 664                    
SITE     2 AC9  5 HOH B 703                                                     
CRYST1  143.840  143.840  354.389  90.00  90.00 120.00 P 65 2 2     24          
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      0.006952  0.004014  0.000000        0.00000                         
SCALE2      0.000000  0.008028  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002822        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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