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LongText Report for: 3EBL-pdb

Name Class
3EBL-pdb
HEADER    HYDROLASE RECEPTOR                      28-AUG-08   3EBL              
TITLE     CRYSTAL STRUCTURE OF RICE GID1 COMPLEXED WITH GA4                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GIBBERELLIN RECEPTOR GID1;                                 
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: GIBBERELLIN-INSENSITIVE DWARF PROTEIN 1, PROTEIN            
COMPND   5 GIBBERELLIN INSENSITIVE DWARF1;                                      
COMPND   6 EC: 3.-.-.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ORYZA SATIVA SUBSP. JAPONICA;                   
SOURCE   3 ORGANISM_COMMON: RICE;                                               
SOURCE   4 GENE: GID1, OS05G0407500, LOC_OS05G33730, OJ1657_H11.10,             
SOURCE   5 P0040B10.6;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYS;                          
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET11B                                    
KEYWDS    ALPHA/BETA HYDROLASE, LIPASE, GIBBERELLIN SIGNALING PATHWAY,          
KEYWDS   2 HYDROLASE, NUCLEUS, RECEPTOR, HYDROLASE RECEPTOR                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.SHIMADA,T.NAKATSU,M.UEGUCHI-TANAKA,H.KATO,M.MATSUOKA                
REVDAT   1   25-NOV-08 3EBL    0                                                
JRNL        AUTH   A.SHIMADA,M.UEGUCHI-TANAKA,T.NAKATSU,M.NAKAJIMA,             
JRNL        AUTH 2 Y.NAOE,H.OHMIYA,H.KATO,M.MATSUOKA                            
JRNL        TITL   STRUCTURAL BASIS FOR GIBBERELLIN RECOGNITION BY              
JRNL        TITL 2 ITS RECEPTOR GID1                                            
JRNL        REF    NATURE                                                       
JRNL        REFN   ASTM NATUAS  UK ESSN 1476-4687                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.90 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 183960                         
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9761                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 12485                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2780                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 662                          
REMARK   3   BIN FREE R VALUE                    : 0.3200                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 16004                                   
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : 0.36000                                              
REMARK   3    B33 (A**2) : -1.60000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.53000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.142         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.139         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.108         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.718         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15244 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20780 ; 1.507 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1861 ; 6.006 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   719 ;31.682 ;22.656       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2222 ;14.117 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   126 ;16.973 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2262 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11855 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  7195 ; 0.200 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 10336 ; 0.312 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1241 ; 0.137 ; 0.200       
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):    32 ; 0.129 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    16 ; 0.082 ; 0.200       
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):  9551 ; 0.928 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14912 ; 1.569 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6437 ; 2.211 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5868 ; 3.188 ; 4.500       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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: NULL                                      
REMARK   4                                                                      
REMARK   4 3EBL COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007                        
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.                               
REMARK 100 THE RCSB ID CODE IS RCSB049119.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUN-2008                        
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ASDC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 193933                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 21.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG4000, 8% MPD, 0.2M NANO3,         
REMARK 280  0.1M HEPES PH7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE        
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,1/2+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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       66.94750            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                 
REMARK 465                                                                      
REMARK 465   M RES C  SSEQI                                                     
REMARK 465     ALA A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     VAL A     7                                                      
REMARK 465     ASN A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     ASN A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     CYS A    12                                                      
REMARK 465     LYS A    13                                                      
REMARK 465     THR A    14                                                      
REMARK 465     ALA A    85                                                      
REMARK 465     GLU A    86                                                      
REMARK 465     GLY A    87                                                      
REMARK 465     ASP A    88                                                      
REMARK 465     ALA A    89                                                      
REMARK 465     GLU A    90                                                      
REMARK 465     GLU A    91                                                      
REMARK 465     GLY A    92                                                      
REMARK 465     ALA A    93                                                      
REMARK 465     ALA A    94                                                      
REMARK 465     ALA A    95                                                      
REMARK 465     VAL A    96                                                      
REMARK 465     THR A    97                                                      
REMARK 465     ARG A    98                                                      
REMARK 465     PRO A    99                                                      
REMARK 465     ILE A   100                                                      
REMARK 465     TYR A   354                                                      
REMARK 465     GLY A   355                                                      
REMARK 465     SER A   356                                                      
REMARK 465     HIS A   357                                                      
REMARK 465     HIS A   358                                                      
REMARK 465     HIS A   359                                                      
REMARK 465     HIS A   360                                                      
REMARK 465     HIS A   361                                                      
REMARK 465     HIS A   362                                                      
REMARK 465     HIS A   363                                                      
REMARK 465     HIS A   364                                                      
REMARK 465     HIS A   365                                                      
REMARK 465     HIS A   366                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     VAL B     7                                                      
REMARK 465     ASN B     8                                                      
REMARK 465     ARG B     9                                                      
REMARK 465     ASN B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     CYS B    12                                                      
REMARK 465     LYS B    13                                                      
REMARK 465     ALA B    85                                                      
REMARK 465     GLU B    86                                                      
REMARK 465     GLY B    87                                                      
REMARK 465     ASP B    88                                                      
REMARK 465     ALA B    89                                                      
REMARK 465     GLU B    90                                                      
REMARK 465     GLU B    91                                                      
REMARK 465     GLY B    92                                                      
REMARK 465     ALA B    93                                                      
REMARK 465     ALA B    94                                                      
REMARK 465     ALA B    95                                                      
REMARK 465     VAL B    96                                                      
REMARK 465     THR B    97                                                      
REMARK 465     ARG B    98                                                      
REMARK 465     PRO B    99                                                      
REMARK 465     ILE B   100                                                      
REMARK 465     LEU B   101                                                      
REMARK 465     GLU B   102                                                      
REMARK 465     GLY B   185                                                      
REMARK 465     GLY B   186                                                      
REMARK 465     ASP B   187                                                      
REMARK 465     TYR B   353                                                      
REMARK 465     TYR B   354                                                      
REMARK 465     GLY B   355                                                      
REMARK 465     SER B   356                                                      
REMARK 465     HIS B   357                                                      
REMARK 465     HIS B   358                                                      
REMARK 465     HIS B   359                                                      
REMARK 465     HIS B   360                                                      
REMARK 465     HIS B   361                                                      
REMARK 465     HIS B   362                                                      
REMARK 465     HIS B   363                                                      
REMARK 465     HIS B   364                                                      
REMARK 465     HIS B   365                                                      
REMARK 465     HIS B   366                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     ASP C     5                                                      
REMARK 465     GLU C     6                                                      
REMARK 465     VAL C     7                                                      
REMARK 465     ASN C     8                                                      
REMARK 465     ARG C     9                                                      
REMARK 465     ASN C    10                                                      
REMARK 465     GLU C    11                                                      
REMARK 465     CYS C    12                                                      
REMARK 465     LYS C    13                                                      
REMARK 465     THR C    14                                                      
REMARK 465     VAL C    15                                                      
REMARK 465     ALA C    84                                                      
REMARK 465     ALA C    85                                                      
REMARK 465     GLU C    86                                                      
REMARK 465     GLY C    87                                                      
REMARK 465     ASP C    88                                                      
REMARK 465     ALA C    89                                                      
REMARK 465     GLU C    90                                                      
REMARK 465     GLU C    91                                                      
REMARK 465     GLY C    92                                                      
REMARK 465     ALA C    93                                                      
REMARK 465     ALA C    94                                                      
REMARK 465     ALA C    95                                                      
REMARK 465     VAL C    96                                                      
REMARK 465     THR C    97                                                      
REMARK 465     ARG C    98                                                      
REMARK 465     PRO C    99                                                      
REMARK 465     ILE C   100                                                      
REMARK 465     LEU C   101                                                      
REMARK 465     GLU C   102                                                      
REMARK 465     PHE C   103                                                      
REMARK 465     LEU C   104                                                      
REMARK 465     THR C   105                                                      
REMARK 465     ASP C   106                                                      
REMARK 465     ALA C   107                                                      
REMARK 465     PRO C   108                                                      
REMARK 465     ALA C   109                                                      
REMARK 465     ALA C   110                                                      
REMARK 465     GLU C   111                                                      
REMARK 465     PRO C   112                                                      
REMARK 465     SER C   184                                                      
REMARK 465     GLY C   185                                                      
REMARK 465     GLY C   186                                                      
REMARK 465     ASP C   187                                                      
REMARK 465     ALA C   188                                                      
REMARK 465     GLN C   189                                                      
REMARK 465     LEU C   352                                                      
REMARK 465     TYR C   353                                                      
REMARK 465     TYR C   354                                                      
REMARK 465     GLY C   355                                                      
REMARK 465     SER C   356                                                      
REMARK 465     HIS C   357                                                      
REMARK 465     HIS C   358                                                      
REMARK 465     HIS C   359                                                      
REMARK 465     HIS C   360                                                      
REMARK 465     HIS C   361                                                      
REMARK 465     HIS C   362                                                      
REMARK 465     HIS C   363                                                      
REMARK 465     HIS C   364                                                      
REMARK 465     HIS C   365                                                      
REMARK 465     HIS C   366                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     ASP D     5                                                      
REMARK 465     GLU D     6                                                      
REMARK 465     VAL D     7                                                      
REMARK 465     ASN D     8                                                      
REMARK 465     ARG D     9                                                      
REMARK 465     ASN D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     CYS D    12                                                      
REMARK 465     LYS D    13                                                      
REMARK 465     THR D    14                                                      
REMARK 465     ALA D    85                                                      
REMARK 465     GLU D    86                                                      
REMARK 465     GLY D    87                                                      
REMARK 465     ASP D    88                                                      
REMARK 465     ALA D    89                                                      
REMARK 465     GLU D    90                                                      
REMARK 465     GLU D    91                                                      
REMARK 465     GLY D    92                                                      
REMARK 465     ALA D    93                                                      
REMARK 465     ALA D    94                                                      
REMARK 465     ALA D    95                                                      
REMARK 465     VAL D    96                                                      
REMARK 465     THR D    97                                                      
REMARK 465     ARG D    98                                                      
REMARK 465     PRO D    99                                                      
REMARK 465     ILE D   100                                                      
REMARK 465     LEU D   101                                                      
REMARK 465     GLU D   102                                                      
REMARK 465     PHE D   103                                                      
REMARK 465     LEU D   104                                                      
REMARK 465     THR D   105                                                      
REMARK 465     ASP D   106                                                      
REMARK 465     ALA D   107                                                      
REMARK 465     PRO D   108                                                      
REMARK 465     TYR D   354                                                      
REMARK 465     GLY D   355                                                      
REMARK 465     SER D   356                                                      
REMARK 465     HIS D   357                                                      
REMARK 465     HIS D   358                                                      
REMARK 465     HIS D   359                                                      
REMARK 465     HIS D   360                                                      
REMARK 465     HIS D   361                                                      
REMARK 465     HIS D   362                                                      
REMARK 465     HIS D   363                                                      
REMARK 465     HIS D   364                                                      
REMARK 465     HIS D   365                                                      
REMARK 465     HIS D   366                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     GLY E     3                                                      
REMARK 465     SER E     4                                                      
REMARK 465     ASP E     5                                                      
REMARK 465     GLU E     6                                                      
REMARK 465     VAL E     7                                                      
REMARK 465     ASN E     8                                                      
REMARK 465     ARG E     9                                                      
REMARK 465     ASN E    10                                                      
REMARK 465     GLU E    11                                                      
REMARK 465     CYS E    12                                                      
REMARK 465     LYS E    13                                                      
REMARK 465     THR E    14                                                      
REMARK 465     VAL E    15                                                      
REMARK 465     ALA E    84                                                      
REMARK 465     ALA E    85                                                      
REMARK 465     GLU E    86                                                      
REMARK 465     GLY E    87                                                      
REMARK 465     ASP E    88                                                      
REMARK 465     ALA E    89                                                      
REMARK 465     GLU E    90                                                      
REMARK 465     GLU E    91                                                      
REMARK 465     GLY E    92                                                      
REMARK 465     ALA E    93                                                      
REMARK 465     ALA E    94                                                      
REMARK 465     ALA E    95                                                      
REMARK 465     VAL E    96                                                      
REMARK 465     THR E    97                                                      
REMARK 465     ARG E    98                                                      
REMARK 465     PRO E    99                                                      
REMARK 465     ILE E   100                                                      
REMARK 465     GLY E   185                                                      
REMARK 465     GLY E   186                                                      
REMARK 465     ASP E   187                                                      
REMARK 465     ALA E   188                                                      
REMARK 465     GLN E   189                                                      
REMARK 465     TYR E   353                                                      
REMARK 465     TYR E   354                                                      
REMARK 465     GLY E   355                                                      
REMARK 465     SER E   356                                                      
REMARK 465     HIS E   357                                                      
REMARK 465     HIS E   358                                                      
REMARK 465     HIS E   359                                                      
REMARK 465     HIS E   360                                                      
REMARK 465     HIS E   361                                                      
REMARK 465     HIS E   362                                                      
REMARK 465     HIS E   363                                                      
REMARK 465     HIS E   364                                                      
REMARK 465     HIS E   365                                                      
REMARK 465     HIS E   366                                                      
REMARK 465     ALA F     2                                                      
REMARK 465     GLY F     3                                                      
REMARK 465     SER F     4                                                      
REMARK 465     ASP F     5                                                      
REMARK 465     GLU F     6                                                      
REMARK 465     VAL F     7                                                      
REMARK 465     ASN F     8                                                      
REMARK 465     ARG F     9                                                      
REMARK 465     ASN F    10                                                      
REMARK 465     GLU F    11                                                      
REMARK 465     CYS F    12                                                      
REMARK 465     LYS F    13                                                      
REMARK 465     THR F    14                                                      
REMARK 465     ALA F    85                                                      
REMARK 465     GLU F    86                                                      
REMARK 465     GLY F    87                                                      
REMARK 465     ASP F    88                                                      
REMARK 465     ALA F    89                                                      
REMARK 465     GLU F    90                                                      
REMARK 465     GLU F    91                                                      
REMARK 465     GLY F    92                                                      
REMARK 465     ALA F    93                                                      
REMARK 465     ALA F    94                                                      
REMARK 465     ALA F    95                                                      
REMARK 465     VAL F    96                                                      
REMARK 465     THR F    97                                                      
REMARK 465     ARG F    98                                                      
REMARK 465     PRO F    99                                                      
REMARK 465     ILE F   100                                                      
REMARK 465     LEU F   101                                                      
REMARK 465     GLU F   102                                                      
REMARK 465     PHE F   103                                                      
REMARK 465     LEU F   104                                                      
REMARK 465     THR F   105                                                      
REMARK 465     ASP F   106                                                      
REMARK 465     ALA F   107                                                      
REMARK 465     PRO F   108                                                      
REMARK 465     ALA F   109                                                      
REMARK 465     ALA F   110                                                      
REMARK 465     GLU F   111                                                      
REMARK 465     PRO F   112                                                      
REMARK 465     SER F   184                                                      
REMARK 465     GLY F   185                                                      
REMARK 465     GLY F   186                                                      
REMARK 465     ASP F   187                                                      
REMARK 465     ALA F   188                                                      
REMARK 465     GLN F   189                                                      
REMARK 465     TYR F   354                                                      
REMARK 465     GLY F   355                                                      
REMARK 465     SER F   356                                                      
REMARK 465     HIS F   357                                                      
REMARK 465     HIS F   358                                                      
REMARK 465     HIS F   359                                                      
REMARK 465     HIS F   360                                                      
REMARK 465     HIS F   361                                                      
REMARK 465     HIS F   362                                                      
REMARK 465     HIS F   363                                                      
REMARK 465     HIS F   364                                                      
REMARK 465     HIS F   365                                                      
REMARK 465     HIS F   366                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  58    CD   NE   CZ   NH1  NH2                             
REMARK 470     LEU A 101    CG   CD1  CD2                                       
REMARK 470     GLU A 102    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 104    CG   CD1  CD2                                       
REMARK 470     GLU A 111    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 146    CD   CE   NZ                                        
REMARK 470     GLN A 189    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 217    CD   CE   NZ                                        
REMARK 470     LYS A 243    CE   NZ                                             
REMARK 470     TYR A 353    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR B  14    OG1  CG2                                            
REMARK 470     ARG B  58    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  82    CD   NE   CZ   NH1  NH2                             
REMARK 470     PHE B 103    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU B 104    CG   CD1  CD2                                       
REMARK 470     THR B 105    OG1  CG2                                            
REMARK 470     GLU B 111    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 146    CE   NZ                                             
REMARK 470     LYS B 174    CE   NZ                                             
REMARK 470     PHE B 181    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN B 189    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 217    CD   CE   NZ                                        
REMARK 470     GLN B 249    CD   OE1  NE2                                       
REMARK 470     ARG C  58    NE   CZ   NH1  NH2                                  
REMARK 470     ARG C  82    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG C 140    CZ   NH1  NH2                                       
REMARK 470     LYS C 146    CE   NZ                                             
REMARK 470     LYS C 174    CD   CE   NZ                                        
REMARK 470     PHE C 181    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG C 183    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG C 191    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 217    CD   CE   NZ                                        
REMARK 470     GLU C 232    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 238    CZ   NH1  NH2                                       
REMARK 470     GLU C 261    CG   CD   OE1  OE2                                  
REMARK 470     VAL D  15    CG1  CG2                                            
REMARK 470     ARG D  58    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN D  72    CD   OE1  NE2                                       
REMARK 470     SER D  73    OG                                                  
REMARK 470     ARG D  82    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU D 111    CD   OE1  OE2                                       
REMARK 470     LYS D 146    CE   NZ                                             
REMARK 470     LYS D 174    CE   NZ                                             
REMARK 470     LYS D 217    CD   CE   NZ                                        
REMARK 470     GLU D 232    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 238    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS D 243    CD   CE   NZ                                        
REMARK 470     LYS D 256    CE   NZ                                             
REMARK 470     LYS D 287    CE   NZ                                             
REMARK 470     ARG D 310    CZ   NH1  NH2                                       
REMARK 470     ARG E  58    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN E  72    CD   OE1  NE2                                       
REMARK 470     SER E  73    OG                                                  
REMARK 470     ARG E  82    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU E 101    CG   CD1  CD2                                       
REMARK 470     GLU E 102    CG   CD   OE1  OE2                                  
REMARK 470     PHE E 103    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU E 104    CG   CD1  CD2                                       
REMARK 470     THR E 105    OG1  CG2                                            
REMARK 470     ASP E 106    CG   OD1  OD2                                       
REMARK 470     GLU E 111    CG   CD   OE1  OE2                                  
REMARK 470     ARG E 140    CZ   NH1  NH2                                       
REMARK 470     LYS E 143    CE   NZ                                             
REMARK 470     LYS E 174    CD   CE   NZ                                        
REMARK 470     PHE E 181    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG E 183    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG E 191    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E 214    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 217    CG   CD   CE   NZ                                   
REMARK 470     GLU E 232    CG   CD   OE1  OE2                                  
REMARK 470     ARG E 238    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E 243    CD   CE   NZ                                        
REMARK 470     GLN E 249    OE1  NE2                                            
REMARK 470     LYS E 256    CE   NZ                                             
REMARK 470     ASP E 262    CG   OD1  OD2                                       
REMARK 470     ASN E 276    CG   OD1  ND2                                       
REMARK 470     LYS E 287    CG   CD   CE   NZ                                   
REMARK 470     ARG E 310    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS E 315    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS E 317    CD   CE   NZ                                        
REMARK 470     ASN E 349    CG   OD1  ND2                                       
REMARK 470     VAL F  15    CG1  CG2                                            
REMARK 470     ARG F  58    CD   NE   CZ   NH1  NH2                             
REMARK 470     SER F  73    OG                                                  
REMARK 470     VAL F  74    CG1  CG2                                            
REMARK 470     ARG F  82    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG F 140    CZ   NH1  NH2                                       
REMARK 470     LYS F 143    CE   NZ                                             
REMARK 470     LYS F 146    CE   NZ                                             
REMARK 470     LYS F 174    CE   NZ                                             
REMARK 470     PHE F 181    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS F 217    CG   CD   CE   NZ                                   
REMARK 470     GLU F 232    CG   CD   OE1  OE2                                  
REMARK 470     ARG F 238    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS F 243    CE   NZ                                             
REMARK 470     GLN F 249    CD   OE1  NE2                                       
REMARK 470     LYS F 256    CE   NZ                                             
REMARK 470     GLU F 261    CD   OE1  OE2                                       
REMARK 470     CYS F 270    SG                                                  
REMARK 470     ARG F 279    CZ   NH1  NH2                                       
REMARK 470     ARG F 310    CZ   NH1  NH2                                       
REMARK 470     GLU F 322    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 106      150.99    -44.31                                   
REMARK 500    PHE A 124       -6.60     74.38                                   
REMARK 500    SER A 127      179.72     69.67                                   
REMARK 500    ALA A 188       68.78     26.70                                   
REMARK 500    SER A 198     -135.37     54.50                                   
REMARK 500    PHE A 245      -28.51     79.28                                   
REMARK 500    VAL B  15      -68.05     66.99                                   
REMARK 500    GLU B  61       43.34     35.09                                   
REMARK 500    ASP B  71      104.07   -163.79                                   
REMARK 500    PRO B 108      131.19    -34.81                                   
REMARK 500    PHE B 124      -11.25     78.79                                   
REMARK 500    SER B 127      178.05     73.75                                   
REMARK 500    SER B 198     -136.26     59.43                                   
REMARK 500    PHE B 245      -26.92     80.30                                   
REMARK 500    GLU C  61       56.34     31.16                                   
REMARK 500    PHE C 124       -7.91     74.23                                   
REMARK 500    SER C 127      173.25     74.21                                   
REMARK 500    SER C 198     -132.58     54.85                                   
REMARK 500    PHE C 245      -28.31     81.35                                   
REMARK 500    ALA C 286      152.35    -38.59                                   
REMARK 500    ASN C 333       15.98   -140.99                                   
REMARK 500    PHE D 124      -12.40     83.18                                   
REMARK 500    SER D 127      176.60     78.09                                   
REMARK 500    SER D 198     -131.13     53.22                                   
REMARK 500    PHE D 245      -27.24     76.82                                   
REMARK 500    GLU E  61       45.25     39.77                                   
REMARK 500    PRO E 108      155.52    -49.59                                   
REMARK 500    PHE E 124      -11.23     81.32                                   
REMARK 500    SER E 127      176.59     77.35                                   
REMARK 500    LYS E 146       29.61     48.85                                   
REMARK 500    SER E 198     -138.57     53.88                                   
REMARK 500    PHE E 245      -32.87     76.92                                   
REMARK 500    ASP E 264     -168.73   -126.03                                   
REMARK 500    PHE F 124      -12.58     75.37                                   
REMARK 500    SER F 127      172.61     73.96                                   
REMARK 500    SER F 198     -133.17     55.88                                   
REMARK 500    PHE F 245      -28.32     80.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GA4 A 401                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 501                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 601                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 602                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 603                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 604                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GA4 B 401                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 501                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 601                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 602                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 604                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 701                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GA4 C 401                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD C 501                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 601                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 602                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 603                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 C 604                 
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GA4 D 401                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD D 501                 
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 D 601                 
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 D 602                 
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 D 603                 
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 701                 
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GA4 E 401                 
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD E 501                 
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 E 601                 
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GA4 F 401                 
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD F 501                 
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 F 601                 
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 F 602                 
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 F 603                 
DBREF  3EBL A    2   354  UNP    Q6L545   GID1_ORYSJ       2    354             
DBREF  3EBL B    2   354  UNP    Q6L545   GID1_ORYSJ       2    354             
DBREF  3EBL C    2   354  UNP    Q6L545   GID1_ORYSJ       2    354             
DBREF  3EBL D    2   354  UNP    Q6L545   GID1_ORYSJ       2    354             
DBREF  3EBL E    2   354  UNP    Q6L545   GID1_ORYSJ       2    354             
DBREF  3EBL F    2   354  UNP    Q6L545   GID1_ORYSJ       2    354             
SEQADV 3EBL GLY A  355  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL SER A  356  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS A  357  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS A  358  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS A  359  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS A  360  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS A  361  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS A  362  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS A  363  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS A  364  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS A  365  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS A  366  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL GLY B  355  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL SER B  356  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS B  357  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS B  358  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS B  359  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS B  360  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS B  361  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS B  362  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS B  363  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS B  364  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS B  365  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS B  366  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL GLY C  355  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL SER C  356  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS C  357  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS C  358  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS C  359  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS C  360  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS C  361  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS C  362  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS C  363  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS C  364  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS C  365  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS C  366  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL GLY D  355  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL SER D  356  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS D  357  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS D  358  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS D  359  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS D  360  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS D  361  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS D  362  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS D  363  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS D  364  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS D  365  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS D  366  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL GLY E  355  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL SER E  356  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS E  357  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS E  358  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS E  359  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS E  360  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS E  361  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS E  362  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS E  363  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS E  364  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS E  365  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS E  366  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL GLY F  355  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL SER F  356  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS F  357  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS F  358  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS F  359  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS F  360  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS F  361  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS F  362  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS F  363  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS F  364  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS F  365  UNP  Q6L545              EXPRESSION TAG                 
SEQADV 3EBL HIS F  366  UNP  Q6L545              EXPRESSION TAG                 
SEQRES   1 A  365  ALA GLY SER ASP GLU VAL ASN ARG ASN GLU CYS LYS THR          
SEQRES   2 A  365  VAL VAL PRO LEU HIS THR TRP VAL LEU ILE SER ASN PHE          
SEQRES   3 A  365  LYS LEU SER TYR ASN ILE LEU ARG ARG ALA ASP GLY THR          
SEQRES   4 A  365  PHE GLU ARG ASP LEU GLY GLU TYR LEU ASP ARG ARG VAL          
SEQRES   5 A  365  PRO ALA ASN ALA ARG PRO LEU GLU GLY VAL SER SER PHE          
SEQRES   6 A  365  ASP HIS ILE ILE ASP GLN SER VAL GLY LEU GLU VAL ARG          
SEQRES   7 A  365  ILE TYR ARG ALA ALA ALA GLU GLY ASP ALA GLU GLU GLY          
SEQRES   8 A  365  ALA ALA ALA VAL THR ARG PRO ILE LEU GLU PHE LEU THR          
SEQRES   9 A  365  ASP ALA PRO ALA ALA GLU PRO PHE PRO VAL ILE ILE PHE          
SEQRES  10 A  365  PHE HIS GLY GLY SER PHE VAL HIS SER SER ALA SER SER          
SEQRES  11 A  365  THR ILE TYR ASP SER LEU CYS ARG ARG PHE VAL LYS LEU          
SEQRES  12 A  365  SER LYS GLY VAL VAL VAL SER VAL ASN TYR ARG ARG ALA          
SEQRES  13 A  365  PRO GLU HIS ARG TYR PRO CYS ALA TYR ASP ASP GLY TRP          
SEQRES  14 A  365  THR ALA LEU LYS TRP VAL MET SER GLN PRO PHE MET ARG          
SEQRES  15 A  365  SER GLY GLY ASP ALA GLN ALA ARG VAL PHE LEU SER GLY          
SEQRES  16 A  365  ASP SER SER GLY GLY ASN ILE ALA HIS HIS VAL ALA VAL          
SEQRES  17 A  365  ARG ALA ALA ASP GLU GLY VAL LYS VAL CYS GLY ASN ILE          
SEQRES  18 A  365  LEU LEU ASN ALA MET PHE GLY GLY THR GLU ARG THR GLU          
SEQRES  19 A  365  SER GLU ARG ARG LEU ASP GLY LYS TYR PHE VAL THR LEU          
SEQRES  20 A  365  GLN ASP ARG ASP TRP TYR TRP LYS ALA TYR LEU PRO GLU          
SEQRES  21 A  365  ASP ALA ASP ARG ASP HIS PRO ALA CYS ASN PRO PHE GLY          
SEQRES  22 A  365  PRO ASN GLY ARG ARG LEU GLY GLY LEU PRO PHE ALA LYS          
SEQRES  23 A  365  SER LEU ILE ILE VAL SER GLY LEU ASP LEU THR CYS ASP          
SEQRES  24 A  365  ARG GLN LEU ALA TYR ALA ASP ALA LEU ARG GLU ASP GLY          
SEQRES  25 A  365  HIS HIS VAL LYS VAL VAL GLN CYS GLU ASN ALA THR VAL          
SEQRES  26 A  365  GLY PHE TYR LEU LEU PRO ASN THR VAL HIS TYR HIS GLU          
SEQRES  27 A  365  VAL MET GLU GLU ILE SER ASP PHE LEU ASN ALA ASN LEU          
SEQRES  28 A  365  TYR TYR GLY SER HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES  29 A  365  HIS                                                          
SEQRES   1 B  365  ALA GLY SER ASP GLU VAL ASN ARG ASN GLU CYS LYS THR          
SEQRES   2 B  365  VAL VAL PRO LEU HIS THR TRP VAL LEU ILE SER ASN PHE          
SEQRES   3 B  365  LYS LEU SER TYR ASN ILE LEU ARG ARG ALA ASP GLY THR          
SEQRES   4 B  365  PHE GLU ARG ASP LEU GLY GLU TYR LEU ASP ARG ARG VAL          
SEQRES   5 B  365  PRO ALA ASN ALA ARG PRO LEU GLU GLY VAL SER SER PHE          
SEQRES   6 B  365  ASP HIS ILE ILE ASP GLN SER VAL GLY LEU GLU VAL ARG          
SEQRES   7 B  365  ILE TYR ARG ALA ALA ALA GLU GLY ASP ALA GLU GLU GLY          
SEQRES   8 B  365  ALA ALA ALA VAL THR ARG PRO ILE LEU GLU PHE LEU THR          
SEQRES   9 B  365  ASP ALA PRO ALA ALA GLU PRO PHE PRO VAL ILE ILE PHE          
SEQRES  10 B  365  PHE HIS GLY GLY SER PHE VAL HIS SER SER ALA SER SER          
SEQRES  11 B  365  THR ILE TYR ASP SER LEU CYS ARG ARG PHE VAL LYS LEU          
SEQRES  12 B  365  SER LYS GLY VAL VAL VAL SER VAL ASN TYR ARG ARG ALA          
SEQRES  13 B  365  PRO GLU HIS ARG TYR PRO CYS ALA TYR ASP ASP GLY TRP          
SEQRES  14 B  365  THR ALA LEU LYS TRP VAL MET SER GLN PRO PHE MET ARG          
SEQRES  15 B  365  SER GLY GLY ASP ALA GLN ALA ARG VAL PHE LEU SER GLY          
SEQRES  16 B  365  ASP SER SER GLY GLY ASN ILE ALA HIS HIS VAL ALA VAL          
SEQRES  17 B  365  ARG ALA ALA ASP GLU GLY VAL LYS VAL CYS GLY ASN ILE          
SEQRES  18 B  365  LEU LEU ASN ALA MET PHE GLY GLY THR GLU ARG THR GLU          
SEQRES  19 B  365  SER GLU ARG ARG LEU ASP GLY LYS TYR PHE VAL THR LEU          
SEQRES  20 B  365  GLN ASP ARG ASP TRP TYR TRP LYS ALA TYR LEU PRO GLU          
SEQRES  21 B  365  ASP ALA ASP ARG ASP HIS PRO ALA CYS ASN PRO PHE GLY          
SEQRES  22 B  365  PRO ASN GLY ARG ARG LEU GLY GLY LEU PRO PHE ALA LYS          
SEQRES  23 B  365  SER LEU ILE ILE VAL SER GLY LEU ASP LEU THR CYS ASP          
SEQRES  24 B  365  ARG GLN LEU ALA TYR ALA ASP ALA LEU ARG GLU ASP GLY          
SEQRES  25 B  365  HIS HIS VAL LYS VAL VAL GLN CYS GLU ASN ALA THR VAL          
SEQRES  26 B  365  GLY PHE TYR LEU LEU PRO ASN THR VAL HIS TYR HIS GLU          
SEQRES  27 B  365  VAL MET GLU GLU ILE SER ASP PHE LEU ASN ALA ASN LEU          
SEQRES  28 B  365  TYR TYR GLY SER HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES  29 B  365  HIS                                                          
SEQRES   1 C  365  ALA GLY SER ASP GLU VAL ASN ARG ASN GLU CYS LYS THR          
SEQRES   2 C  365  VAL VAL PRO LEU HIS THR TRP VAL LEU ILE SER ASN PHE          
SEQRES   3 C  365  LYS LEU SER TYR ASN ILE LEU ARG ARG ALA ASP GLY THR          
SEQRES   4 C  365  PHE GLU ARG ASP LEU GLY GLU TYR LEU ASP ARG ARG VAL          
SEQRES   5 C  365  PRO ALA ASN ALA ARG PRO LEU GLU GLY VAL SER SER PHE          
SEQRES   6 C  365  ASP HIS ILE ILE ASP GLN SER VAL GLY LEU GLU VAL ARG          
SEQRES   7 C  365  ILE TYR ARG ALA ALA ALA GLU GLY ASP ALA GLU GLU GLY          
SEQRES   8 C  365  ALA ALA ALA VAL THR ARG PRO ILE LEU GLU PHE LEU THR          
SEQRES   9 C  365  ASP ALA PRO ALA ALA GLU PRO PHE PRO VAL ILE ILE PHE          
SEQRES  10 C  365  PHE HIS GLY GLY SER PHE VAL HIS SER SER ALA SER SER          
SEQRES  11 C  365  THR ILE TYR ASP SER LEU CYS ARG ARG PHE VAL LYS LEU          
SEQRES  12 C  365  SER LYS GLY VAL VAL VAL SER VAL ASN TYR ARG ARG ALA          
SEQRES  13 C  365  PRO GLU HIS ARG TYR PRO CYS ALA TYR ASP ASP GLY TRP          
SEQRES  14 C  365  THR ALA LEU LYS TRP VAL MET SER GLN PRO PHE MET ARG          
SEQRES  15 C  365  SER GLY GLY ASP ALA GLN ALA ARG VAL PHE LEU SER GLY          
SEQRES  16 C  365  ASP SER SER GLY GLY ASN ILE ALA HIS HIS VAL ALA VAL          
SEQRES  17 C  365  ARG ALA ALA ASP GLU GLY VAL LYS VAL CYS GLY ASN ILE          
SEQRES  18 C  365  LEU LEU ASN ALA MET PHE GLY GLY THR GLU ARG THR GLU          
SEQRES  19 C  365  SER GLU ARG ARG LEU ASP GLY LYS TYR PHE VAL THR LEU          
SEQRES  20 C  365  GLN ASP ARG ASP TRP TYR TRP LYS ALA TYR LEU PRO GLU          
SEQRES  21 C  365  ASP ALA ASP ARG ASP HIS PRO ALA CYS ASN PRO PHE GLY          
SEQRES  22 C  365  PRO ASN GLY ARG ARG LEU GLY GLY LEU PRO PHE ALA LYS          
SEQRES  23 C  365  SER LEU ILE ILE VAL SER GLY LEU ASP LEU THR CYS ASP          
SEQRES  24 C  365  ARG GLN LEU ALA TYR ALA ASP ALA LEU ARG GLU ASP GLY          
SEQRES  25 C  365  HIS HIS VAL LYS VAL VAL GLN CYS GLU ASN ALA THR VAL          
SEQRES  26 C  365  GLY PHE TYR LEU LEU PRO ASN THR VAL HIS TYR HIS GLU          
SEQRES  27 C  365  VAL MET GLU GLU ILE SER ASP PHE LEU ASN ALA ASN LEU          
SEQRES  28 C  365  TYR TYR GLY SER HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES  29 C  365  HIS                                                          
SEQRES   1 D  365  ALA GLY SER ASP GLU VAL ASN ARG ASN GLU CYS LYS THR          
SEQRES   2 D  365  VAL VAL PRO LEU HIS THR TRP VAL LEU ILE SER ASN PHE          
SEQRES   3 D  365  LYS LEU SER TYR ASN ILE LEU ARG ARG ALA ASP GLY THR          
SEQRES   4 D  365  PHE GLU ARG ASP LEU GLY GLU TYR LEU ASP ARG ARG VAL          
SEQRES   5 D  365  PRO ALA ASN ALA ARG PRO LEU GLU GLY VAL SER SER PHE          
SEQRES   6 D  365  ASP HIS ILE ILE ASP GLN SER VAL GLY LEU GLU VAL ARG          
SEQRES   7 D  365  ILE TYR ARG ALA ALA ALA GLU GLY ASP ALA GLU GLU GLY          
SEQRES   8 D  365  ALA ALA ALA VAL THR ARG PRO ILE LEU GLU PHE LEU THR          
SEQRES   9 D  365  ASP ALA PRO ALA ALA GLU PRO PHE PRO VAL ILE ILE PHE          
SEQRES  10 D  365  PHE HIS GLY GLY SER PHE VAL HIS SER SER ALA SER SER          
SEQRES  11 D  365  THR ILE TYR ASP SER LEU CYS ARG ARG PHE VAL LYS LEU          
SEQRES  12 D  365  SER LYS GLY VAL VAL VAL SER VAL ASN TYR ARG ARG ALA          
SEQRES  13 D  365  PRO GLU HIS ARG TYR PRO CYS ALA TYR ASP ASP GLY TRP          
SEQRES  14 D  365  THR ALA LEU LYS TRP VAL MET SER GLN PRO PHE MET ARG          
SEQRES  15 D  365  SER GLY GLY ASP ALA GLN ALA ARG VAL PHE LEU SER GLY          
SEQRES  16 D  365  ASP SER SER GLY GLY ASN ILE ALA HIS HIS VAL ALA VAL          
SEQRES  17 D  365  ARG ALA ALA ASP GLU GLY VAL LYS VAL CYS GLY ASN ILE          
SEQRES  18 D  365  LEU LEU ASN ALA MET PHE GLY GLY THR GLU ARG THR GLU          
SEQRES  19 D  365  SER GLU ARG ARG LEU ASP GLY LYS TYR PHE VAL THR LEU          
SEQRES  20 D  365  GLN ASP ARG ASP TRP TYR TRP LYS ALA TYR LEU PRO GLU          
SEQRES  21 D  365  ASP ALA ASP ARG ASP HIS PRO ALA CYS ASN PRO PHE GLY          
SEQRES  22 D  365  PRO ASN GLY ARG ARG LEU GLY GLY LEU PRO PHE ALA LYS          
SEQRES  23 D  365  SER LEU ILE ILE VAL SER GLY LEU ASP LEU THR CYS ASP          
SEQRES  24 D  365  ARG GLN LEU ALA TYR ALA ASP ALA LEU ARG GLU ASP GLY          
SEQRES  25 D  365  HIS HIS VAL LYS VAL VAL GLN CYS GLU ASN ALA THR VAL          
SEQRES  26 D  365  GLY PHE TYR LEU LEU PRO ASN THR VAL HIS TYR HIS GLU          
SEQRES  27 D  365  VAL MET GLU GLU ILE SER ASP PHE LEU ASN ALA ASN LEU          
SEQRES  28 D  365  TYR TYR GLY SER HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES  29 D  365  HIS                                                          
SEQRES   1 E  365  ALA GLY SER ASP GLU VAL ASN ARG ASN GLU CYS LYS THR          
SEQRES   2 E  365  VAL VAL PRO LEU HIS THR TRP VAL LEU ILE SER ASN PHE          
SEQRES   3 E  365  LYS LEU SER TYR ASN ILE LEU ARG ARG ALA ASP GLY THR          
SEQRES   4 E  365  PHE GLU ARG ASP LEU GLY GLU TYR LEU ASP ARG ARG VAL          
SEQRES   5 E  365  PRO ALA ASN ALA ARG PRO LEU GLU GLY VAL SER SER PHE          
SEQRES   6 E  365  ASP HIS ILE ILE ASP GLN SER VAL GLY LEU GLU VAL ARG          
SEQRES   7 E  365  ILE TYR ARG ALA ALA ALA GLU GLY ASP ALA GLU GLU GLY          
SEQRES   8 E  365  ALA ALA ALA VAL THR ARG PRO ILE LEU GLU PHE LEU THR          
SEQRES   9 E  365  ASP ALA PRO ALA ALA GLU PRO PHE PRO VAL ILE ILE PHE          
SEQRES  10 E  365  PHE HIS GLY GLY SER PHE VAL HIS SER SER ALA SER SER          
SEQRES  11 E  365  THR ILE TYR ASP SER LEU CYS ARG ARG PHE VAL LYS LEU          
SEQRES  12 E  365  SER LYS GLY VAL VAL VAL SER VAL ASN TYR ARG ARG ALA          
SEQRES  13 E  365  PRO GLU HIS ARG TYR PRO CYS ALA TYR ASP ASP GLY TRP          
SEQRES  14 E  365  THR ALA LEU LYS TRP VAL MET SER GLN PRO PHE MET ARG          
SEQRES  15 E  365  SER GLY GLY ASP ALA GLN ALA ARG VAL PHE LEU SER GLY          
SEQRES  16 E  365  ASP SER SER GLY GLY ASN ILE ALA HIS HIS VAL ALA VAL          
SEQRES  17 E  365  ARG ALA ALA ASP GLU GLY VAL LYS VAL CYS GLY ASN ILE          
SEQRES  18 E  365  LEU LEU ASN ALA MET PHE GLY GLY THR GLU ARG THR GLU          
SEQRES  19 E  365  SER GLU ARG ARG LEU ASP GLY LYS TYR PHE VAL THR LEU          
SEQRES  20 E  365  GLN ASP ARG ASP TRP TYR TRP LYS ALA TYR LEU PRO GLU          
SEQRES  21 E  365  ASP ALA ASP ARG ASP HIS PRO ALA CYS ASN PRO PHE GLY          
SEQRES  22 E  365  PRO ASN GLY ARG ARG LEU GLY GLY LEU PRO PHE ALA LYS          
SEQRES  23 E  365  SER LEU ILE ILE VAL SER GLY LEU ASP LEU THR CYS ASP          
SEQRES  24 E  365  ARG GLN LEU ALA TYR ALA ASP ALA LEU ARG GLU ASP GLY          
SEQRES  25 E  365  HIS HIS VAL LYS VAL VAL GLN CYS GLU ASN ALA THR VAL          
SEQRES  26 E  365  GLY PHE TYR LEU LEU PRO ASN THR VAL HIS TYR HIS GLU          
SEQRES  27 E  365  VAL MET GLU GLU ILE SER ASP PHE LEU ASN ALA ASN LEU          
SEQRES  28 E  365  TYR TYR GLY SER HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES  29 E  365  HIS                                                          
SEQRES   1 F  365  ALA GLY SER ASP GLU VAL ASN ARG ASN GLU CYS LYS THR          
SEQRES   2 F  365  VAL VAL PRO LEU HIS THR TRP VAL LEU ILE SER ASN PHE          
SEQRES   3 F  365  LYS LEU SER TYR ASN ILE LEU ARG ARG ALA ASP GLY THR          
SEQRES   4 F  365  PHE GLU ARG ASP LEU GLY GLU TYR LEU ASP ARG ARG VAL          
SEQRES   5 F  365  PRO ALA ASN ALA ARG PRO LEU GLU GLY VAL SER SER PHE          
SEQRES   6 F  365  ASP HIS ILE ILE ASP GLN SER VAL GLY LEU GLU VAL ARG          
SEQRES   7 F  365  ILE TYR ARG ALA ALA ALA GLU GLY ASP ALA GLU GLU GLY          
SEQRES   8 F  365  ALA ALA ALA VAL THR ARG PRO ILE LEU GLU PHE LEU THR          
SEQRES   9 F  365  ASP ALA PRO ALA ALA GLU PRO PHE PRO VAL ILE ILE PHE          
SEQRES  10 F  365  PHE HIS GLY GLY SER PHE VAL HIS SER SER ALA SER SER          
SEQRES  11 F  365  THR ILE TYR ASP SER LEU CYS ARG ARG PHE VAL LYS LEU          
SEQRES  12 F  365  SER LYS GLY VAL VAL VAL SER VAL ASN TYR ARG ARG ALA          
SEQRES  13 F  365  PRO GLU HIS ARG TYR PRO CYS ALA TYR ASP ASP GLY TRP          
SEQRES  14 F  365  THR ALA LEU LYS TRP VAL MET SER GLN PRO PHE MET ARG          
SEQRES  15 F  365  SER GLY GLY ASP ALA GLN ALA ARG VAL PHE LEU SER GLY          
SEQRES  16 F  365  ASP SER SER GLY GLY ASN ILE ALA HIS HIS VAL ALA VAL          
SEQRES  17 F  365  ARG ALA ALA ASP GLU GLY VAL LYS VAL CYS GLY ASN ILE          
SEQRES  18 F  365  LEU LEU ASN ALA MET PHE GLY GLY THR GLU ARG THR GLU          
SEQRES  19 F  365  SER GLU ARG ARG LEU ASP GLY LYS TYR PHE VAL THR LEU          
SEQRES  20 F  365  GLN ASP ARG ASP TRP TYR TRP LYS ALA TYR LEU PRO GLU          
SEQRES  21 F  365  ASP ALA ASP ARG ASP HIS PRO ALA CYS ASN PRO PHE GLY          
SEQRES  22 F  365  PRO ASN GLY ARG ARG LEU GLY GLY LEU PRO PHE ALA LYS          
SEQRES  23 F  365  SER LEU ILE ILE VAL SER GLY LEU ASP LEU THR CYS ASP          
SEQRES  24 F  365  ARG GLN LEU ALA TYR ALA ASP ALA LEU ARG GLU ASP GLY          
SEQRES  25 F  365  HIS HIS VAL LYS VAL VAL GLN CYS GLU ASN ALA THR VAL          
SEQRES  26 F  365  GLY PHE TYR LEU LEU PRO ASN THR VAL HIS TYR HIS GLU          
SEQRES  27 F  365  VAL MET GLU GLU ILE SER ASP PHE LEU ASN ALA ASN LEU          
SEQRES  28 F  365  TYR TYR GLY SER HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES  29 F  365  HIS                                                          
HET    GA4  A 401      24                                                       
HET    MPD  A 501       8                                                       
HET    NO3  A 601       4                                                       
HET    NO3  A 602       4                                                       
HET    NO3  A 603       4                                                       
HET    NO3  A 604       4                                                       
HET    GA4  B 401      24                                                       
HET    MPD  B 501       8                                                       
HET    NO3  B 601       4                                                       
HET    NO3  B 602       4                                                       
HET    NO3  B 604       4                                                       
HET    PO4  B 701       5                                                       
HET    GA4  C 401      24                                                       
HET    MPD  C 501       8                                                       
HET    NO3  C 601       4                                                       
HET    NO3  C 602       4                                                       
HET    NO3  C 603       4                                                       
HET    NO3  C 604       4                                                       
HET    GA4  D 401      24                                                       
HET    MPD  D 501       8                                                       
HET    NO3  D 601       4                                                       
HET    NO3  D 602       4                                                       
HET    NO3  D 603       4                                                       
HET    PO4  E 701       5                                                       
HET    GA4  E 401      24                                                       
HET    MPD  E 501       8                                                       
HET    NO3  E 601       4                                                       
HET    GA4  F 401      24                                                       
HET    MPD  F 501       8                                                       
HET    NO3  F 601       4                                                       
HET    NO3  F 602       4                                                       
HET    NO3  F 603       4                                                       
HETNAM     GA4 GIBBERELLIN A4                                                   
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
HETNAM     NO3 NITRATE ION                                                      
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   7  GA4    6(C19 H24 O5)                                                
FORMUL   8  MPD    6(C6 H14 O2)                                                 
FORMUL   9  NO3    18(N O3 1-)                                                  
FORMUL  18  PO4    2(O4 P 3-)                                                   
FORMUL  39  HOH   *1133(H2 O)                                                   
HELIX    1   1 PRO A   17  ARG A   35  1                                  19    
HELIX    2   2 GLU A   42  ASP A   50  1                                   9    
HELIX    3   3 LEU A  101  ASP A  106  5                                   6    
HELIX    4   4 SER A  131  LYS A  146  1                                  16    
HELIX    5   5 PRO A  163  GLN A  179  1                                  17    
HELIX    6   6 SER A  199  GLU A  214  1                                  16    
HELIX    7   7 THR A  234  ASP A  241  1                                   8    
HELIX    8   8 THR A  247  LEU A  259  1                                  13    
HELIX    9   9 THR A  298  ASP A  312  1                                  15    
HELIX   10  10 GLY A  327  LEU A  331  5                                   5    
HELIX   11  11 THR A  334  TYR A  353  1                                  20    
HELIX   12  12 PRO B   17  ARG B   35  1                                  19    
HELIX   13  13 GLU B   42  ASP B   50  1                                   9    
HELIX   14  14 SER B  131  LYS B  146  1                                  16    
HELIX   15  15 PRO B  163  SER B  178  1                                  16    
HELIX   16  16 GLN B  179  ARG B  183  5                                   5    
HELIX   17  17 SER B  198  GLU B  214  1                                  17    
HELIX   18  18 THR B  234  ASP B  241  1                                   8    
HELIX   19  19 THR B  247  LEU B  259  1                                  13    
HELIX   20  20 THR B  298  ASP B  312  1                                  15    
HELIX   21  21 GLY B  327  LEU B  331  5                                   5    
HELIX   22  22 THR B  334  ASN B  351  1                                  18    
HELIX   23  23 PRO C   17  ARG C   35  1                                  19    
HELIX   24  24 GLU C   42  ASP C   50  1                                   9    
HELIX   25  25 SER C  131  LYS C  146  1                                  16    
HELIX   26  26 PRO C  163  GLN C  179  1                                  17    
HELIX   27  27 PRO C  180  ARG C  183  5                                   4    
HELIX   28  28 SER C  198  GLU C  214  1                                  17    
HELIX   29  29 THR C  234  ASP C  241  1                                   8    
HELIX   30  30 THR C  247  LEU C  259  1                                  13    
HELIX   31  31 THR C  298  ASP C  312  1                                  15    
HELIX   32  32 GLY C  327  LEU C  331  5                                   5    
HELIX   33  33 THR C  334  ASN C  351  1                                  18    
HELIX   34  34 PRO D   17  ARG D   35  1                                  19    
HELIX   35  35 GLU D   42  ASP D   50  1                                   9    
HELIX   36  36 SER D  131  LYS D  146  1                                  16    
HELIX   37  37 PRO D  163  GLN D  179  1                                  17    
HELIX   38  38 PRO D  180  ARG D  183  5                                   4    
HELIX   39  39 SER D  199  GLU D  214  1                                  16    
HELIX   40  40 THR D  234  ASP D  241  1                                   8    
HELIX   41  41 THR D  247  LEU D  259  1                                  13    
HELIX   42  42 THR D  298  ASP D  312  1                                  15    
HELIX   43  43 GLY D  327  LEU D  331  5                                   5    
HELIX   44  44 THR D  334  LEU D  352  1                                  19    
HELIX   45  45 PRO E   17  ILE E   33  1                                  17    
HELIX   46  46 GLU E   42  ASP E   50  1                                   9    
HELIX   47  47 LEU E  101  ASP E  106  5                                   6    
HELIX   48  48 SER E  131  LYS E  146  1                                  16    
HELIX   49  49 PRO E  163  SER E  178  1                                  16    
HELIX   50  50 GLN E  179  ARG E  183  5                                   5    
HELIX   51  51 SER E  199  GLU E  214  1                                  16    
HELIX   52  52 THR E  234  ASP E  241  1                                   8    
HELIX   53  53 THR E  247  LEU E  259  1                                  13    
HELIX   54  54 THR E  298  ASP E  312  1                                  15    
HELIX   55  55 GLY E  327  LEU E  331  5                                   5    
HELIX   56  56 THR E  334  ASN E  351  1                                  18    
HELIX   57  57 PRO F   17  ARG F   35  1                                  19    
HELIX   58  58 GLU F   42  ASP F   50  1                                   9    
HELIX   59  59 SER F  131  LYS F  146  1                                  16    
HELIX   60  60 PRO F  163  SER F  178  1                                  16    
HELIX   61  61 GLN F  179  ARG F  183  5                                   5    
HELIX   62  62 SER F  198  GLU F  214  1                                  17    
HELIX   63  63 THR F  234  ASP F  241  1                                   8    
HELIX   64  64 THR F  247  LEU F  259  1                                  13    
HELIX   65  65 THR F  298  ASP F  312  1                                  15    
HELIX   66  66 GLY F  327  LEU F  331  5                                   5    
HELIX   67  67 THR F  334  ASN F  351  1                                  18    
SHEET    1   A 6 VAL A  63  ASP A  71  0                                        
SHEET    2   A 6 LEU A  76  ALA A  83 -1  O  LEU A  76   N  ILE A  70           
SHEET    3   A 6 VAL A 148  VAL A 152 -1  O  SER A 151   N  ARG A  79           
SHEET    4   A 6 PRO A 114  PHE A 119  1  N  ILE A 116   O  VAL A 150           
SHEET    5   A 6 GLN A 189  ASP A 197  1  O  PHE A 193   N  ILE A 117           
SHEET    6   A 6 ARG A 183  SER A 184 -1  N  SER A 184   O  GLN A 189           
SHEET    1   B 8 VAL A  63  ASP A  71  0                                        
SHEET    2   B 8 LEU A  76  ALA A  83 -1  O  LEU A  76   N  ILE A  70           
SHEET    3   B 8 VAL A 148  VAL A 152 -1  O  SER A 151   N  ARG A  79           
SHEET    4   B 8 PRO A 114  PHE A 119  1  N  ILE A 116   O  VAL A 150           
SHEET    5   B 8 GLN A 189  ASP A 197  1  O  PHE A 193   N  ILE A 117           
SHEET    6   B 8 GLY A 220  LEU A 224  1  O  ILE A 222   N  LEU A 194           
SHEET    7   B 8 SER A 288  SER A 293  1  O  ILE A 291   N  LEU A 223           
SHEET    8   B 8 VAL A 316  CYS A 321  1  O  CYS A 321   N  VAL A 292           
SHEET    1   C 8 VAL B  63  ASP B  71  0                                        
SHEET    2   C 8 LEU B  76  ALA B  83 -1  O  ILE B  80   N  PHE B  66           
SHEET    3   C 8 VAL B 148  ASN B 153 -1  O  SER B 151   N  ARG B  79           
SHEET    4   C 8 PRO B 114  PHE B 119  1  N  ILE B 116   O  VAL B 148           
SHEET    5   C 8 ARG B 191  ASP B 197  1  O  PHE B 193   N  ILE B 117           
SHEET    6   C 8 GLY B 220  LEU B 224  1  O  ILE B 222   N  LEU B 194           
SHEET    7   C 8 SER B 288  SER B 293  1  O  ILE B 291   N  LEU B 223           
SHEET    8   C 8 VAL B 316  CYS B 321  1  O  CYS B 321   N  VAL B 292           
SHEET    1   D 8 SER C  64  ASP C  71  0                                        
SHEET    2   D 8 LEU C  76  ARG C  82 -1  O  ILE C  80   N  PHE C  66           
SHEET    3   D 8 VAL C 148  ASN C 153 -1  O  SER C 151   N  ARG C  79           
SHEET    4   D 8 PRO C 114  PHE C 119  1  N  ILE C 116   O  VAL C 148           
SHEET    5   D 8 ARG C 191  ASP C 197  1  O  PHE C 193   N  ILE C 117           
SHEET    6   D 8 GLY C 220  LEU C 224  1  O  LEU C 224   N  GLY C 196           
SHEET    7   D 8 LYS C 287  SER C 293  1  O  ILE C 291   N  LEU C 223           
SHEET    8   D 8 VAL C 316  CYS C 321  1  O  CYS C 321   N  VAL C 292           
SHEET    1   E 8 VAL D  63  ASP D  71  0                                        
SHEET    2   E 8 LEU D  76  ALA D  83 -1  O  ILE D  80   N  PHE D  66           
SHEET    3   E 8 VAL D 148  VAL D 152 -1  O  SER D 151   N  ARG D  79           
SHEET    4   E 8 PRO D 114  PHE D 119  1  N  ILE D 116   O  VAL D 150           
SHEET    5   E 8 ARG D 191  ASP D 197  1  O  PHE D 193   N  ILE D 117           
SHEET    6   E 8 GLY D 220  LEU D 224  1  O  ILE D 222   N  LEU D 194           
SHEET    7   E 8 SER D 288  SER D 293  1  O  ILE D 291   N  LEU D 223           
SHEET    8   E 8 VAL D 316  CYS D 321  1  O  LYS D 317   N  ILE D 290           
SHEET    1   F 8 SER E  64  ASP E  71  0                                        
SHEET    2   F 8 LEU E  76  ARG E  82 -1  O  ARG E  82   N  SER E  64           
SHEET    3   F 8 VAL E 148  ASN E 153 -1  O  SER E 151   N  ARG E  79           
SHEET    4   F 8 PRO E 114  PHE E 119  1  N  ILE E 116   O  VAL E 150           
SHEET    5   F 8 ARG E 191  SER E 198  1  O  ARG E 191   N  VAL E 115           
SHEET    6   F 8 GLY E 220  ALA E 226  1  O  ILE E 222   N  LEU E 194           
SHEET    7   F 8 SER E 288  SER E 293  1  O  LEU E 289   N  ASN E 221           
SHEET    8   F 8 VAL E 316  CYS E 321  1  O  LYS E 317   N  SER E 288           
SHEET    1   G 8 VAL F  63  ASP F  71  0                                        
SHEET    2   G 8 LEU F  76  ALA F  83 -1  O  ILE F  80   N  PHE F  66           
SHEET    3   G 8 VAL F 148  VAL F 152 -1  O  SER F 151   N  ARG F  79           
SHEET    4   G 8 PRO F 114  PHE F 119  1  N  ILE F 116   O  VAL F 150           
SHEET    5   G 8 ARG F 191  ASP F 197  1  O  PHE F 193   N  ILE F 117           
SHEET    6   G 8 GLY F 220  LEU F 224  1  O  ILE F 222   N  LEU F 194           
SHEET    7   G 8 SER F 288  SER F 293  1  O  ILE F 291   N  LEU F 223           
SHEET    8   G 8 VAL F 316  CYS F 321  1  O  CYS F 321   N  VAL F 292           
CISPEP   1 ALA A  157    PRO A  158          0        -5.07                     
CISPEP   2 TYR A  162    PRO A  163          0         1.19                     
CISPEP   3 ALA B  157    PRO B  158          0        -4.01                     
CISPEP   4 TYR B  162    PRO B  163          0         0.33                     
CISPEP   5 ALA C  157    PRO C  158          0        -3.88                     
CISPEP   6 TYR C  162    PRO C  163          0        -0.29                     
CISPEP   7 ALA D  157    PRO D  158          0        -0.69                     
CISPEP   8 TYR D  162    PRO D  163          0         0.88                     
CISPEP   9 ALA E  157    PRO E  158          0        -4.04                     
CISPEP  10 TYR E  162    PRO E  163          0         3.80                     
CISPEP  11 ALA F  157    PRO F  158          0        -8.10                     
CISPEP  12 TYR F  162    PRO F  163          0         3.82                     
SITE     1 AC1 16 ILE A  24  PHE A  27  GLY A 122  SER A 123                    
SITE     2 AC1 16 ILE A 133  TYR A 134  ASP A 197  SER A 198                    
SITE     3 AC1 16 VAL A 246  ARG A 251  TYR A 254  VAL A 326                    
SITE     4 AC1 16 GLY A 327  TYR A 329  HOH A 605  HOH A 607                    
SITE     1 AC2  6 LEU A  23  LEU A  49  ASP A  50  ARG A  51                    
SITE     2 AC2  6 HOH A 640  MPD B 501                                          
SITE     1 AC3  3 ARG A  35  HOH A 785  HOH A 848                               
SITE     1 AC4  4 THR A 231  ASP A 264  ARG A 265  HOH A 698                    
SITE     1 AC5  3 ARG A  51  LEU A 331  NO3 A 604                               
SITE     1 AC6  6 HIS A  19  LEU A  23  ARG A  51  NO3 A 603                    
SITE     2 AC6  6 ASN B  26  SER B  30                                          
SITE     1 AC7 14 ILE B  24  PHE B  27  GLY B 122  SER B 123                    
SITE     2 AC7 14 ILE B 133  TYR B 134  ASP B 197  SER B 198                    
SITE     3 AC7 14 ARG B 251  TYR B 254  VAL B 326  GLY B 327                    
SITE     4 AC7 14 TYR B 329  HOH B 702                                          
SITE     1 AC8  6 MPD A 501  LEU B  23  SER B  30  LEU B  49                    
SITE     2 AC8  6 ARG B  51  HOH B 719                                          
SITE     1 AC9  3 ARG B  35  TRP B 253  HOH B 891                               
SITE     1 BC1  4 THR B 231  ASP B 264  ARG B 265  HOH B 789                    
SITE     1 BC2  6 ASN A  26  SER A  30  HIS B  19  LEU B  23                    
SITE     2 BC2  6 ARG B  51  PO4 B 701                                          
SITE     1 BC3  5 ARG B  51  LEU B 330  LEU B 331  NO3 B 604                    
SITE     2 BC3  5 HOH B 724                                                     
SITE     1 BC4 16 PHE C  27  ARG C  35  GLY C 122  SER C 123                    
SITE     2 BC4 16 ILE C 133  TYR C 134  ASP C 197  SER C 198                    
SITE     3 BC4 16 VAL C 246  ARG C 251  TYR C 254  VAL C 326                    
SITE     4 BC4 16 GLY C 327  TYR C 329  HOH C 605  HOH C 607                    
SITE     1 BC5  8 ASN C  26  SER C  30  LEU C  49  ASP C  50                    
SITE     2 BC5  8 ARG C  51  HOH C 638  ASN D  26  ARG D  51                    
SITE     1 BC6  2 ARG C  35  TRP C 253                                          
SITE     1 BC7  4 THR C 231  ASP C 264  ARG C 265  HOH C 697                    
SITE     1 BC8  3 ARG C  51  LEU C 330  HOH C 642                               
SITE     1 BC9  5 ASN C  26  SER C  30  HIS D  19  LEU D  23                    
SITE     2 BC9  5 ARG D  51                                                     
SITE     1 CC1 16 ILE D  24  PHE D  27  ARG D  35  GLY D 122                    
SITE     2 CC1 16 SER D 123  ILE D 133  TYR D 134  ASP D 197                    
SITE     3 CC1 16 SER D 198  ARG D 251  TYR D 254  VAL D 326                    
SITE     4 CC1 16 GLY D 327  TYR D 329  HOH D 604  HOH D 606                    
SITE     1 CC2  6 LEU D  23  ASN D  26  LEU D  49  ASP D  50                    
SITE     2 CC2  6 ARG D  51  HOH D 630                                          
SITE     1 CC3  4 ARG D  35  GLN D 249  TRP D 253  HOH D 704                    
SITE     1 CC4  4 THR D 231  ASP D 264  ARG D 265  HOH D 721                    
SITE     1 CC5  2 ARG D  51  LEU D 331                                          
SITE     1 CC6  3 ARG E  51  SER E 136  LEU E 330                               
SITE     1 CC7 15 PHE E  27  ARG E  35  GLY E 122  SER E 123                    
SITE     2 CC7 15 ILE E 133  TYR E 134  ASP E 197  SER E 198                    
SITE     3 CC7 15 ARG E 251  TYR E 254  VAL E 326  GLY E 327                    
SITE     4 CC7 15 TYR E 329  HOH E 702  HOH E 730                               
SITE     1 CC8  6 ASN E  26  SER E  30  LEU E  49  ARG E  51                    
SITE     2 CC8  6 HOH E 711  MPD F 501                                          
SITE     1 CC9  4 ARG E  35  GLN E 249  TRP E 253  HOH E 796                    
SITE     1 DC1 15 PHE F  27  GLY F 122  SER F 123  ILE F 133                    
SITE     2 DC1 15 TYR F 134  ASP F 197  SER F 198  PHE F 245                    
SITE     3 DC1 15 ARG F 251  TYR F 254  VAL F 326  GLY F 327                    
SITE     4 DC1 15 TYR F 329  HOH F 604  HOH F 625                               
SITE     1 DC2  6 MPD E 501  LEU F  23  SER F  30  LEU F  49                    
SITE     2 DC2  6 ARG F  51  HOH F 626                                          
SITE     1 DC3  2 ARG F  35  HOH F 752                                          
SITE     1 DC4  3 THR F 231  ASP F 264  ARG F 265                               
SITE     1 DC5  3 LEU F 330  LEU F 331  HOH F 631                               
CRYST1   82.760  133.895  118.886  90.00 104.95  90.00 P 1 21 1     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      0.012083  0.000000  0.003226        0.00000                         
SCALE2      0.000000  0.007469  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008706        0.00000                         
TER    2539      TYR A 353                                                      
TER    5023      LEU B 352                                                      
TER    7384      ASN C 351                                                      
TER    9835      TYR D 353                                                      
TER   12228      LEU E 352                                                      
TER   14603      TYR F 353                                                      
MASTER      801    0   32   67   54    0   60    616004    6  274  174          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
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