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Database: PDB
Entry: 2CXE
LinkDB: 2CXE
Original site: 2CXE 
HEADER    LYASE                                   28-JUN-05   2CXE              
TITLE     CRYSTAL STRUCTURE OF OCTAMERIC RIBULOSE-1,5-BISPHOSPHATE              
TITLE    2 CARBOXYLASE/OXYGENASE (RUBISCO) FROM PYROCOCCUS HORIKOSHII OT3 (FORM-
TITLE    3 2 CRYSTAL)                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE;                         
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE, RUBISCO;   
COMPND   5 EC: 4.1.1.39;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;                          
SOURCE   3 ORGANISM_TAXID: 70601;                                               
SOURCE   4 STRAIN: OT3;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL   
KEYWDS   2 AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS        
KEYWDS   3 INITIATIVE, RSGI, LYASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.MIZOHATA,C.MISHIMA,R.AKASAKA,H.UDA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,  
AUTHOR   2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)               
REVDAT   5   13-JUL-11 2CXE    1       VERSN                                    
REVDAT   4   15-DEC-10 2CXE    1       MTRIX1 MTRIX2 MTRIX3                     
REVDAT   3   12-MAY-09 2CXE    1       MTRIX1 MTRIX2 MTRIX3                     
REVDAT   2   24-FEB-09 2CXE    1       VERSN                                    
REVDAT   1   28-DEC-05 2CXE    0                                                
JRNL        AUTH   E.MIZOHATA,C.MISHIMA,R.AKASAKA,H.UDA,T.TERADA,M.SHIROUZU,    
JRNL        AUTH 2 S.YOKOYAMA                                                   
JRNL        TITL   CRYSTAL STRUCTURE OF OCTAMERIC RIBULOSE-1,5-BISPHOSPHATE     
JRNL        TITL 2 CARBOXYLASE/OXYGENASE (RUBISCO) FROM PYROCOCCUS HORIKOSHII   
JRNL        TITL 3 OT3 (FORM-2 CRYSTAL)                                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 416476.720                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 36882                          
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 SET) : 0.295                           
REMARK   3   FREE R VALUE                     : 0.328                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1838                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.19                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 76.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5162                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5800                       
REMARK   3   BIN FREE R VALUE                    : 0.6060                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 290                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.036                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13144                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 204                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 88.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 11.96000                                             
REMARK   3    B22 (A**2) : -43.61000                                            
REMARK   3    B33 (A**2) : 31.66000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 46.05000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.68                            
REMARK   3   ESD FROM SIGMAA              (A) : 1.40                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.74                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 1.45                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.074                           
REMARK   3   BOND ANGLES            (DEGREES) : 5.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 3.11                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.31                                                 
REMARK   3   BSOL        : 39.28                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : CONSTR                                                  
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2CXE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUL-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB024733.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAY-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 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                       : BL44B2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39367                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM CHLORIDE, SODIUM CHLORIDE,     
REMARK 280  SODIUM ACETATE, PEG6000, TRIS, PH 5, VAPOR DIFFUSION, SITTING       
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       85.73900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       74.60350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       85.73900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       74.60350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS THE OCTAMER. ALTHOUGH THE         
REMARK 300 PRESENT ASYMMETIC UNIT IS TETRAMER, NCS CONSTRAINT IS APPLIED TO     
REMARK 300 PRODUCE MONOMER (SEGMENT ID A). THE SECOND, THIRD, AND FOURTH PART   
REMARK 300 IN THE ASYMMETRIC UNIT IS GENERATED BY MTRIX IN THE PDB FILE.        
REMARK 300 BIOLOGICAL ASSEMBLY IS GENERATED FROM THE ASYMMETRIC COMPONENT BY    
REMARK 300 OPERATOR -X, Y, -Z.                                                  
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: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6900 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
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   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 436  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH D 437  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     MET A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     ARG A     5                                                      
REMARK 465     MET A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     VAL A     8                                                      
REMARK 465     LYS A   425                                                      
REMARK 465     VAL A   426                                                      
REMARK 465     GLY A   427                                                      
REMARK 465     VAL A   428                                                      
REMARK 465     GLN A   429                                                      
REMARK 465     HIS A   430                                                      
REMARK 465     MET B     1                                                      
REMARK 465     MET B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     ARG B     5                                                      
REMARK 465     MET B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     VAL B     8                                                      
REMARK 465     LYS B   425                                                      
REMARK 465     VAL B   426                                                      
REMARK 465     GLY B   427                                                      
REMARK 465     VAL B   428                                                      
REMARK 465     GLN B   429                                                      
REMARK 465     HIS B   430                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET C     2                                                      
REMARK 465     VAL C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     ARG C     5                                                      
REMARK 465     MET C     6                                                      
REMARK 465     LYS C     7                                                      
REMARK 465     VAL C     8                                                      
REMARK 465     LYS C   425                                                      
REMARK 465     VAL C   426                                                      
REMARK 465     GLY C   427                                                      
REMARK 465     VAL C   428                                                      
REMARK 465     GLN C   429                                                      
REMARK 465     HIS C   430                                                      
REMARK 465     MET D     1                                                      
REMARK 465     MET D     2                                                      
REMARK 465     VAL D     3                                                      
REMARK 465     LEU D     4                                                      
REMARK 465     ARG D     5                                                      
REMARK 465     MET D     6                                                      
REMARK 465     LYS D     7                                                      
REMARK 465     VAL D     8                                                      
REMARK 465     LYS D   425                                                      
REMARK 465     VAL D   426                                                      
REMARK 465     GLY D   427                                                      
REMARK 465     VAL D   428                                                      
REMARK 465     GLN D   429                                                      
REMARK 465     HIS D   430                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   436     O    HOH C   439              0.14            
REMARK 500   O    HOH C   431     O    HOH C   450              1.37            
REMARK 500   O    HOH A   447     O    HOH A   481              1.37            
REMARK 500   O    HOH D   431     O    HOH D   448              1.39            
REMARK 500   O    HOH B   447     O    HOH B   480              1.49            
REMARK 500   NH2  ARG C    23     NH1  ARG D    23              1.55            
REMARK 500   NH1  ARG C    23     NH2  ARG D    23              1.59            
REMARK 500   CD   ARG C   417     O    HOH C   481              1.65            
REMARK 500   OE2  GLU C    95     NH1  ARG D   131              1.81            
REMARK 500   NH1  ARG C   131     OE2  GLU D    95              1.90            
REMARK 500   OE1  GLU B    94     OG1  THR C   192              2.07            
REMARK 500   O    TRP B    10     N    LEU B    12              2.07            
REMARK 500   O    TRP C    10     N    LEU C    12              2.07            
REMARK 500   O    TRP A    10     N    LEU A    12              2.07            
REMARK 500   O    TRP D    10     N    LEU D    12              2.08            
REMARK 500   OE2  GLU C    95     OE2  GLU D   128              2.10            
REMARK 500   O    HOH B   466     O    HOH C   469              2.13            
REMARK 500   O    ASP D   188     N    ASN D   190              2.14            
REMARK 500   O    ASP B   188     N    ASN B   190              2.14            
REMARK 500   O    ASP A   188     N    ASN A   190              2.14            
REMARK 500   O    ASP C   188     N    ASN C   190              2.14            
REMARK 500   O    TYR D   127     N    TYR D   129              2.17            
REMARK 500   O    TYR C   127     N    TYR C   129              2.17            
REMARK 500   O    TYR A   127     N    TYR A   129              2.17            
REMARK 500   O    TYR B   127     N    TYR B   129              2.18            
REMARK 500   OG1  THR B   192     OE1  GLU C    94              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    THR B    56     CD1  LEU D   421     3444     0.58            
REMARK 500   OG   SER C   422     O    ALA D   424     3444     1.07            
REMARK 500   OG   SER C   422     C    ALA D   424     3444     1.34            
REMARK 500   NH1  ARG A    23     NH2  ARG B    23     2555     1.63            
REMARK 500   NH2  ARG A    23     NH1  ARG B    23     2555     1.66            
REMARK 500   OE1  GLU B     9     CD2  LEU D   421     3444     1.69            
REMARK 500   CD   GLU B     9     CD2  LEU D   421     3444     1.80            
REMARK 500   C    THR B    56     CD1  LEU D   421     3444     1.81            
REMARK 500   NH1  ARG A   131     OE2  GLU B    95     2555     1.90            
REMARK 500   OE2  GLU A    95     NH1  ARG B   131     2555     1.95            
REMARK 500   O    THR B    56     CG   LEU D   421     3444     1.98            
REMARK 500   CB   ALA A   424     O    VAL C    37     4445     2.03            
REMARK 500   OE1  GLU D    94     OG1  THR D   192     2555     2.09            
REMARK 500   O    HOH A   469     O    HOH A   469     2555     2.09            
REMARK 500   CB   SER C   422     O    ALA D   424     3444     2.11            
REMARK 500   OE2  GLU B     9     CD2  LEU D   421     3444     2.14            
REMARK 500   OE1  GLU A    94     OG1  THR A   192     2555     2.16            
REMARK 500   OE2  GLU A   128     OE2  GLU B    95     2555     2.17            
REMARK 500   O    HOH D   468     O    HOH D   468     2555     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP A  10   CE2   TRP A  10   CZ2     0.139                       
REMARK 500    TRP A  10   CD2   TRP A  10   CE3     0.111                       
REMARK 500    TYR A  11   CG    TYR A  11   CD1     0.112                       
REMARK 500    TYR A  11   CZ    TYR A  11   CE2     0.117                       
REMARK 500    PHE A  14   CB    PHE A  14   CG     -0.104                       
REMARK 500    PHE A  14   CG    PHE A  14   CD2    -0.095                       
REMARK 500    VAL A  15   CB    VAL A  15   CG1    -0.141                       
REMARK 500    ASP A  16   CB    ASP A  16   CG     -0.132                       
REMARK 500    ASN A  18   CB    ASN A  18   CG      0.199                       
REMARK 500    ASN A  18   CG    ASN A  18   ND2     0.169                       
REMARK 500    GLU A  20   CD    GLU A  20   OE1     0.093                       
REMARK 500    GLU A  20   C     GLU A  20   O       0.150                       
REMARK 500    PRO A  21   CA    PRO A  21   CB      0.123                       
REMARK 500    TYR A  31   CG    TYR A  31   CD2     0.090                       
REMARK 500    TYR A  31   CZ    TYR A  31   CE2     0.123                       
REMARK 500    TYR A  31   CE2   TYR A  31   CD2     0.129                       
REMARK 500    PHE A  32   CB    PHE A  32   CG     -0.116                       
REMARK 500    ASN A  35   C     ASN A  35   O       0.139                       
REMARK 500    VAL A  37   CB    VAL A  37   CG2     0.132                       
REMARK 500    GLU A  40   CG    GLU A  40   CD      0.106                       
REMARK 500    GLU A  40   CD    GLU A  40   OE1     0.089                       
REMARK 500    GLU A  40   CD    GLU A  40   OE2     0.106                       
REMARK 500    ARG A  45   CZ    ARG A  45   NH2     0.084                       
REMARK 500    ALA A  47   C     ALA A  47   O      -0.145                       
REMARK 500    SER A  48   CA    SER A  48   CB      0.100                       
REMARK 500    SER A  48   CB    SER A  48   OG      0.090                       
REMARK 500    GLU A  49   CG    GLU A  49   CD      0.129                       
REMARK 500    GLU A  49   CD    GLU A  49   OE1     0.080                       
REMARK 500    TRP A  55   CB    TRP A  55   CG     -0.138                       
REMARK 500    THR A  56   N     THR A  56   CA      0.137                       
REMARK 500    THR A  56   CA    THR A  56   CB      0.218                       
REMARK 500    THR A  56   CB    THR A  56   CG2     0.220                       
REMARK 500    THR A  56   CA    THR A  56   C       0.200                       
REMARK 500    THR A  56   C     THR A  56   O       0.132                       
REMARK 500    THR A  57   CA    THR A  57   CB      0.319                       
REMARK 500    TRP A  59   CD2   TRP A  59   CE3     0.106                       
REMARK 500    TRP A  59   CE3   TRP A  59   CZ3     0.121                       
REMARK 500    TRP A  59   CZ3   TRP A  59   CH2     0.103                       
REMARK 500    LEU A  61   CG    LEU A  61   CD2     0.259                       
REMARK 500    LEU A  61   CA    LEU A  61   C       0.172                       
REMARK 500    GLU A  63   CG    GLU A  63   CD      0.126                       
REMARK 500    GLU A  63   CD    GLU A  63   OE1     0.146                       
REMARK 500    GLU A  63   CD    GLU A  63   OE2     0.098                       
REMARK 500    MET A  64   SD    MET A  64   CE      1.172                       
REMARK 500    LYS A  66   CG    LYS A  66   CD      0.298                       
REMARK 500    LYS A  66   CD    LYS A  66   CE      0.289                       
REMARK 500    SER A  68   CA    SER A  68   CB      0.154                       
REMARK 500    SER A  68   CB    SER A  68   OG      0.112                       
REMARK 500    MET A  69   SD    MET A  69   CE      0.435                       
REMARK 500    GLU A  76   CB    GLU A  76   CG      0.149                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     996 BOND DEVIATIONS.                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A   9   OE1 -  CD  -  OE2 ANGL. DEV. =   8.6 DEGREES          
REMARK 500    LEU A  12   CB  -  CG  -  CD2 ANGL. DEV. =  11.6 DEGREES          
REMARK 500    ASP A  16   CB  -  CG  -  OD1 ANGL. DEV. = -11.0 DEGREES          
REMARK 500    LEU A  17   CA  -  CB  -  CG  ANGL. DEV. = -18.9 DEGREES          
REMARK 500    GLU A  20   N   -  CA  -  CB  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    PRO A  21   CA  -  N   -  CD  ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    PRO A  21   C   -  N   -  CA  ANGL. DEV. =  19.5 DEGREES          
REMARK 500    PRO A  21   O   -  C   -  N   ANGL. DEV. =  10.8 DEGREES          
REMARK 500    ASP A  24   CB  -  CG  -  OD2 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    LEU A  26   CA  -  CB  -  CG  ANGL. DEV. = -17.2 DEGREES          
REMARK 500    PRO A  39   C   -  N   -  CD  ANGL. DEV. = -15.8 DEGREES          
REMARK 500    GLY A  44   N   -  CA  -  C   ANGL. DEV. = -16.0 DEGREES          
REMARK 500    GLU A  49   CA  -  CB  -  CG  ANGL. DEV. = -13.7 DEGREES          
REMARK 500    THR A  56   C   -  N   -  CA  ANGL. DEV. =  18.2 DEGREES          
REMARK 500    LEU A  58   CB  -  CG  -  CD2 ANGL. DEV. = -12.7 DEGREES          
REMARK 500    LEU A  58   N   -  CA  -  C   ANGL. DEV. =  19.0 DEGREES          
REMARK 500    LEU A  61   CB  -  CG  -  CD1 ANGL. DEV. = -13.4 DEGREES          
REMARK 500    LEU A  61   CB  -  CG  -  CD2 ANGL. DEV. =  13.9 DEGREES          
REMARK 500    MET A  64   CG  -  SD  -  CE  ANGL. DEV. =  17.1 DEGREES          
REMARK 500    LYS A  66   CB  -  CG  -  CD  ANGL. DEV. =  17.3 DEGREES          
REMARK 500    SER A  68   CA  -  CB  -  OG  ANGL. DEV. =  19.7 DEGREES          
REMARK 500    MET A  69   CG  -  SD  -  CE  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    LEU A  75   CB  -  CG  -  CD1 ANGL. DEV. = -10.3 DEGREES          
REMARK 500    LEU A  75   CB  -  CG  -  CD2 ANGL. DEV. =  11.4 DEGREES          
REMARK 500    LEU A  75   N   -  CA  -  C   ANGL. DEV. = -17.7 DEGREES          
REMARK 500    GLU A  76   CG  -  CD  -  OE2 ANGL. DEV. =  13.4 DEGREES          
REMARK 500    GLU A  80   CG  -  CD  -  OE1 ANGL. DEV. =  17.0 DEGREES          
REMARK 500    GLU A  80   CG  -  CD  -  OE2 ANGL. DEV. = -13.8 DEGREES          
REMARK 500    GLY A  81   N   -  CA  -  C   ANGL. DEV. = -16.0 DEGREES          
REMARK 500    TYR A  82   CB  -  CG  -  CD1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    LYS A  85   CD  -  CE  -  NZ  ANGL. DEV. =  21.4 DEGREES          
REMARK 500    LYS A  85   N   -  CA  -  C   ANGL. DEV. = -20.8 DEGREES          
REMARK 500    PRO A  89   C   -  N   -  CA  ANGL. DEV. =  16.4 DEGREES          
REMARK 500    PRO A  89   C   -  N   -  CD  ANGL. DEV. = -15.9 DEGREES          
REMARK 500    THR A  91   CA  -  C   -  O   ANGL. DEV. =  14.1 DEGREES          
REMARK 500    LEU A  92   CB  -  CG  -  CD1 ANGL. DEV. = -19.8 DEGREES          
REMARK 500    LEU A  92   CB  -  CG  -  CD2 ANGL. DEV. =  13.2 DEGREES          
REMARK 500    THR A  91   CA  -  C   -  N   ANGL. DEV. = -18.1 DEGREES          
REMARK 500    GLU A  94   N   -  CA  -  C   ANGL. DEV. = -24.0 DEGREES          
REMARK 500    GLU A  95   N   -  CA  -  CB  ANGL. DEV. =  14.9 DEGREES          
REMARK 500    GLU A  95   CG  -  CD  -  OE2 ANGL. DEV. = -13.1 DEGREES          
REMARK 500    LEU A 101   CB  -  CG  -  CD2 ANGL. DEV. = -18.1 DEGREES          
REMARK 500    ARG A 119   CG  -  CD  -  NE  ANGL. DEV. = -16.9 DEGREES          
REMARK 500    ARG A 119   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    TYR A 127   CB  -  CA  -  C   ANGL. DEV. = -12.2 DEGREES          
REMARK 500    PRO A 126   CA  -  C   -  N   ANGL. DEV. =  14.2 DEGREES          
REMARK 500    TYR A 129   CB  -  CG  -  CD2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    TYR A 129   CB  -  CG  -  CD1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    LEU A 130   CB  -  CG  -  CD2 ANGL. DEV. =  18.6 DEGREES          
REMARK 500    ARG A 131   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     717 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  11       -7.50    -40.90                                   
REMARK 500    ASP A  16       96.64   -172.56                                   
REMARK 500    ARG A  23      -36.39    -32.22                                   
REMARK 500    ASP A  24       38.53    -97.33                                   
REMARK 500    ASN A  35       67.64   -157.58                                   
REMARK 500    ALA A  42      -75.47    -79.43                                   
REMARK 500    ALA A  43       -9.39    -42.83                                   
REMARK 500    SER A  48      -78.09    -66.62                                   
REMARK 500    GLU A  49      -75.77    -30.11                                   
REMARK 500    SER A  50       27.53    -55.26                                   
REMARK 500    SER A  51     -112.58   -167.10                                   
REMARK 500    TRP A  55      123.93     63.80                                   
REMARK 500    THR A  56       59.55   -140.98                                   
REMARK 500    THR A  57      -92.51   -137.65                                   
REMARK 500    LYS A  60       86.26    -39.39                                   
REMARK 500    LEU A  61      125.61    -35.02                                   
REMARK 500    GLU A  63      -78.33    -41.16                                   
REMARK 500    MET A  64       11.57    -64.30                                   
REMARK 500    TYR A  74      142.08    169.94                                   
REMARK 500    LEU A  75       90.79   -164.22                                   
REMARK 500    GLU A  80       25.49    -69.71                                   
REMARK 500    LEU A  90       35.16    -58.84                                   
REMARK 500    LEU A 101      -67.50    -27.29                                   
REMARK 500    VAL A 105       37.12    -86.19                                   
REMARK 500    ALA A 106       16.91   -167.09                                   
REMARK 500    PHE A 110        7.62    -63.91                                   
REMARK 500    MET A 112      120.55    -20.25                                   
REMARK 500    ALA A 114       10.37    -48.54                                   
REMARK 500    TYR A 127      -80.30    -16.85                                   
REMARK 500    GLU A 128      -15.69    -20.99                                   
REMARK 500    ASP A 151      -62.47    -95.47                                   
REMARK 500    ARG A 152     -179.10    -44.92                                   
REMARK 500    GLU A 168      -75.53    -73.06                                   
REMARK 500    GLU A 169      -42.01    -28.82                                   
REMARK 500    TYR A 175      -38.15    -37.35                                   
REMARK 500    GLU A 189      -16.14    -15.48                                   
REMARK 500    THR A 192      -84.03   -121.34                                   
REMARK 500    PRO A 195      -55.01    -22.71                                   
REMARK 500    GLU A 216      -84.17    -49.78                                   
REMARK 500    MET A 281       -5.27    112.63                                   
REMARK 500    ALA A 283       -9.10    -48.42                                   
REMARK 500    PHE A 285      -28.03   -156.86                                   
REMARK 500    ARG A 287      -68.71    -96.20                                   
REMARK 500    LYS A 300      -61.94    -98.47                                   
REMARK 500    ALA A 315       79.90   -116.80                                   
REMARK 500    MET A 319       76.34   -106.09                                   
REMARK 500    ALA A 320       40.43    -62.98                                   
REMARK 500    ASN A 322       84.14    -33.98                                   
REMARK 500    TYR A 323       -6.76    -43.32                                   
REMARK 500    GLU A 325      -70.01    -76.78                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     245 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A  19         0.08    SIDE CHAIN                              
REMARK 500    PHE A  73         0.11    SIDE CHAIN                              
REMARK 500    PHE A 110         0.08    SIDE CHAIN                              
REMARK 500    TYR A 127         0.08    SIDE CHAIN                              
REMARK 500    TYR A 129         0.09    SIDE CHAIN                              
REMARK 500    HIS A 132         0.09    SIDE CHAIN                              
REMARK 500    PHE A 146         0.09    SIDE CHAIN                              
REMARK 500    TYR A 175         0.07    SIDE CHAIN                              
REMARK 500    TYR A 207         0.08    SIDE CHAIN                              
REMARK 500    ARG A 210         0.12    SIDE CHAIN                              
REMARK 500    TYR A 248         0.10    SIDE CHAIN                              
REMARK 500    TYR A 263         0.10    SIDE CHAIN                              
REMARK 500    PHE A 285         0.08    SIDE CHAIN                              
REMARK 500    PHE A 332         0.10    SIDE CHAIN                              
REMARK 500    PHE A 363         0.10    SIDE CHAIN                              
REMARK 500    TYR B  19         0.08    SIDE CHAIN                              
REMARK 500    PHE B  73         0.11    SIDE CHAIN                              
REMARK 500    PHE B 110         0.08    SIDE CHAIN                              
REMARK 500    TYR B 127         0.08    SIDE CHAIN                              
REMARK 500    TYR B 129         0.09    SIDE CHAIN                              
REMARK 500    HIS B 132         0.09    SIDE CHAIN                              
REMARK 500    PHE B 146         0.09    SIDE CHAIN                              
REMARK 500    TYR B 175         0.07    SIDE CHAIN                              
REMARK 500    TYR B 207         0.08    SIDE CHAIN                              
REMARK 500    ARG B 210         0.12    SIDE CHAIN                              
REMARK 500    TYR B 248         0.10    SIDE CHAIN                              
REMARK 500    TYR B 263         0.10    SIDE CHAIN                              
REMARK 500    PHE B 285         0.08    SIDE CHAIN                              
REMARK 500    PHE B 332         0.10    SIDE CHAIN                              
REMARK 500    PHE B 363         0.10    SIDE CHAIN                              
REMARK 500    TYR C  19         0.08    SIDE CHAIN                              
REMARK 500    PHE C  73         0.11    SIDE CHAIN                              
REMARK 500    PHE C 110         0.08    SIDE CHAIN                              
REMARK 500    TYR C 127         0.08    SIDE CHAIN                              
REMARK 500    TYR C 129         0.09    SIDE CHAIN                              
REMARK 500    HIS C 132         0.09    SIDE CHAIN                              
REMARK 500    PHE C 146         0.09    SIDE CHAIN                              
REMARK 500    TYR C 175         0.07    SIDE CHAIN                              
REMARK 500    TYR C 207         0.08    SIDE CHAIN                              
REMARK 500    ARG C 210         0.12    SIDE CHAIN                              
REMARK 500    TYR C 248         0.10    SIDE CHAIN                              
REMARK 500    TYR C 263         0.10    SIDE CHAIN                              
REMARK 500    PHE C 285         0.08    SIDE CHAIN                              
REMARK 500    PHE C 332         0.10    SIDE CHAIN                              
REMARK 500    PHE C 363         0.10    SIDE CHAIN                              
REMARK 500    TYR D  19         0.08    SIDE CHAIN                              
REMARK 500    PHE D  73         0.11    SIDE CHAIN                              
REMARK 500    PHE D 110         0.08    SIDE CHAIN                              
REMARK 500    TYR D 127         0.08    SIDE CHAIN                              
REMARK 500    TYR D 129         0.09    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      60 PLANE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLU A 216        -10.18                                           
REMARK 500    GLU B 216        -10.16                                           
REMARK 500    GLU C 216        -10.13                                           
REMARK 500    GLU D 216        -10.20                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLU A  20        21.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE A  27        21.3      L          L   OUTSIDE RANGE           
REMARK 500    TRP A  55        25.0      L          L   OUTSIDE RANGE           
REMARK 500    THR A  57        23.0      L          L   OUTSIDE RANGE           
REMARK 500    LEU A  58        20.6      L          L   OUTSIDE RANGE           
REMARK 500    LYS A  60        24.3      L          L   OUTSIDE RANGE           
REMARK 500    LEU A  75        45.9      L          L   OUTSIDE RANGE           
REMARK 500    PRO A  89        45.3      L          L   OUTSIDE RANGE           
REMARK 500    GLU A  94        54.3      L          L   OUTSIDE RANGE           
REMARK 500    HIS A 124        24.9      L          L   OUTSIDE RANGE           
REMARK 500    PHE A 146        21.5      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 151        17.1      L          L   OUTSIDE RANGE           
REMARK 500    THR A 217        22.8      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 231        23.7      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 249        22.4      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 254        21.8      L          L   OUTSIDE RANGE           
REMARK 500    TRP A 258        24.2      L          L   OUTSIDE RANGE           
REMARK 500    PRO A 289        22.6      L          L   OUTSIDE RANGE           
REMARK 500    THR A 314        21.2      L          L   OUTSIDE RANGE           
REMARK 500    HIS A 339        23.1      L          L   OUTSIDE RANGE           
REMARK 500    PHE A 363        21.8      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 400        24.8      L          L   OUTSIDE RANGE           
REMARK 500    GLU B  20        21.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE B  27        21.3      L          L   OUTSIDE RANGE           
REMARK 500    TRP B  55        25.0      L          L   OUTSIDE RANGE           
REMARK 500    THR B  57        22.9      L          L   OUTSIDE RANGE           
REMARK 500    LEU B  58        20.6      L          L   OUTSIDE RANGE           
REMARK 500    LYS B  60        24.3      L          L   OUTSIDE RANGE           
REMARK 500    LEU B  75        45.9      L          L   OUTSIDE RANGE           
REMARK 500    PRO B  89        45.3      L          L   OUTSIDE RANGE           
REMARK 500    GLU B  94        54.3      L          L   OUTSIDE RANGE           
REMARK 500    HIS B 124        24.9      L          L   OUTSIDE RANGE           
REMARK 500    PHE B 146        21.5      L          L   OUTSIDE RANGE           
REMARK 500    ASP B 151        17.1      L          L   OUTSIDE RANGE           
REMARK 500    THR B 217        22.8      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 231        23.6      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 249        22.4      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 254        21.9      L          L   OUTSIDE RANGE           
REMARK 500    TRP B 258        24.2      L          L   OUTSIDE RANGE           
REMARK 500    PRO B 289        22.6      L          L   OUTSIDE RANGE           
REMARK 500    THR B 314        21.2      L          L   OUTSIDE RANGE           
REMARK 500    HIS B 339        23.1      L          L   OUTSIDE RANGE           
REMARK 500    PHE B 363        21.7      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 400        24.9      L          L   OUTSIDE RANGE           
REMARK 500    GLU C  20        21.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE C  27        21.3      L          L   OUTSIDE RANGE           
REMARK 500    TRP C  55        25.0      L          L   OUTSIDE RANGE           
REMARK 500    THR C  57        22.9      L          L   OUTSIDE RANGE           
REMARK 500    LEU C  58        20.6      L          L   OUTSIDE RANGE           
REMARK 500    LYS C  60        24.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      88 CHIRALITY DEVIATIONS.                         
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 435        DISTANCE =  5.68 ANGSTROMS                       
REMARK 525    HOH A 452        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH A 456        DISTANCE =  8.67 ANGSTROMS                       
REMARK 525    HOH A 461        DISTANCE = 10.89 ANGSTROMS                       
REMARK 525    HOH A 462        DISTANCE =  8.52 ANGSTROMS                       
REMARK 525    HOH A 472        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH A 479        DISTANCE =  7.78 ANGSTROMS                       
REMARK 525    HOH B 435        DISTANCE =  5.68 ANGSTROMS                       
REMARK 525    HOH B 452        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH B 456        DISTANCE =  8.67 ANGSTROMS                       
REMARK 525    HOH B 460        DISTANCE = 10.89 ANGSTROMS                       
REMARK 525    HOH B 461        DISTANCE =  8.52 ANGSTROMS                       
REMARK 525    HOH B 469        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH B 476        DISTANCE =  7.78 ANGSTROMS                       
REMARK 525    HOH C 438        DISTANCE =  5.68 ANGSTROMS                       
REMARK 525    HOH C 455        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH C 459        DISTANCE =  8.67 ANGSTROMS                       
REMARK 525    HOH C 463        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH C 464        DISTANCE =  8.52 ANGSTROMS                       
REMARK 525    HOH C 472        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH C 479        DISTANCE =  7.78 ANGSTROMS                       
REMARK 525    HOH D 436        DISTANCE =  5.68 ANGSTROMS                       
REMARK 525    HOH D 453        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH D 457        DISTANCE =  8.67 ANGSTROMS                       
REMARK 525    HOH D 460        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH D 461        DISTANCE =  8.52 ANGSTROMS                       
REMARK 525    HOH D 471        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH D 478        DISTANCE =  7.78 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2CWX   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN OF DIFFERENT SPACE GROUP.                           
REMARK 900 RELATED ID: PHO001000939.1   RELATED DB: TARGETDB                    
DBREF  2CXE A    1   430  UNP    O58677   RBL_PYRHO        1    430             
DBREF  2CXE B    1   430  UNP    O58677   RBL_PYRHO        1    430             
DBREF  2CXE C    1   430  UNP    O58677   RBL_PYRHO        1    430             
DBREF  2CXE D    1   430  UNP    O58677   RBL_PYRHO        1    430             
SEQRES   1 A  430  MET MET VAL LEU ARG MET LYS VAL GLU TRP TYR LEU ASP          
SEQRES   2 A  430  PHE VAL ASP LEU ASN TYR GLU PRO GLY ARG ASP GLU LEU          
SEQRES   3 A  430  ILE VAL GLU TYR TYR PHE GLU PRO ASN GLY VAL SER PRO          
SEQRES   4 A  430  GLU GLU ALA ALA GLY ARG ILE ALA SER GLU SER SER ILE          
SEQRES   5 A  430  GLY THR TRP THR THR LEU TRP LYS LEU PRO GLU MET ALA          
SEQRES   6 A  430  LYS ARG SER MET ALA LYS VAL PHE TYR LEU GLU LYS HIS          
SEQRES   7 A  430  GLY GLU GLY TYR ILE ALA LYS ILE ALA TYR PRO LEU THR          
SEQRES   8 A  430  LEU PHE GLU GLU GLY SER LEU VAL GLN LEU PHE SER ALA          
SEQRES   9 A  430  VAL ALA GLY ASN VAL PHE GLY MET LYS ALA LEU LYS ASN          
SEQRES  10 A  430  LEU ARG LEU LEU ASP PHE HIS PRO PRO TYR GLU TYR LEU          
SEQRES  11 A  430  ARG HIS PHE LYS GLY PRO GLN PHE GLY VAL GLN GLY ILE          
SEQRES  12 A  430  ARG GLU PHE MET GLY VAL LYS ASP ARG PRO LEU THR ALA          
SEQRES  13 A  430  THR VAL PRO LYS PRO LYS MET GLY TRP SER VAL GLU GLU          
SEQRES  14 A  430  TYR ALA GLU ILE ALA TYR GLU LEU TRP SER GLY GLY ILE          
SEQRES  15 A  430  ASP LEU LEU LYS ASP ASP GLU ASN PHE THR SER PHE PRO          
SEQRES  16 A  430  PHE ASN ARG PHE GLU GLU ARG VAL ARG LYS LEU TYR ARG          
SEQRES  17 A  430  VAL ARG ASP ARG VAL GLU ALA GLU THR GLY GLU THR LYS          
SEQRES  18 A  430  GLU TYR LEU ILE ASN ILE THR GLY PRO VAL ASN ILE MET          
SEQRES  19 A  430  GLU LYS ARG ALA GLU MET VAL ALA ASN GLU GLY GLY GLN          
SEQRES  20 A  430  TYR VAL MET ILE ASP ILE VAL VAL ALA GLY TRP SER ALA          
SEQRES  21 A  430  LEU GLN TYR MET ARG GLU VAL THR GLU ASP LEU GLY LEU          
SEQRES  22 A  430  ALA ILE HIS ALA HIS ARG ALA MET HIS ALA ALA PHE THR          
SEQRES  23 A  430  ARG ASN PRO ARG HIS GLY ILE THR MET LEU ALA LEU ALA          
SEQRES  24 A  430  LYS ALA ALA ARG MET ILE GLY VAL ASP GLN ILE HIS THR          
SEQRES  25 A  430  GLY THR ALA VAL GLY LYS MET ALA GLY ASN TYR GLU GLU          
SEQRES  26 A  430  ILE LYS ARG ILE ASN ASP PHE LEU LEU SER LYS TRP GLU          
SEQRES  27 A  430  HIS ILE ARG PRO VAL PHE PRO VAL ALA SER GLY GLY LEU          
SEQRES  28 A  430  HIS PRO GLY LEU MET PRO GLU LEU ILE ARG LEU PHE GLY          
SEQRES  29 A  430  LYS ASP LEU VAL ILE GLN ALA GLY GLY GLY VAL MET GLY          
SEQRES  30 A  430  HIS PRO ASP GLY PRO ARG ALA GLY ALA LYS ALA LEU ARG          
SEQRES  31 A  430  ASP ALA ILE ASP ALA ALA ILE GLU GLY VAL ASP LEU ASP          
SEQRES  32 A  430  GLU LYS ALA LYS SER SER PRO GLU LEU LYS LYS SER LEU          
SEQRES  33 A  430  ARG GLU VAL GLY LEU SER LYS ALA LYS VAL GLY VAL GLN          
SEQRES  34 A  430  HIS                                                          
SEQRES   1 B  430  MET MET VAL LEU ARG MET LYS VAL GLU TRP TYR LEU ASP          
SEQRES   2 B  430  PHE VAL ASP LEU ASN TYR GLU PRO GLY ARG ASP GLU LEU          
SEQRES   3 B  430  ILE VAL GLU TYR TYR PHE GLU PRO ASN GLY VAL SER PRO          
SEQRES   4 B  430  GLU GLU ALA ALA GLY ARG ILE ALA SER GLU SER SER ILE          
SEQRES   5 B  430  GLY THR TRP THR THR LEU TRP LYS LEU PRO GLU MET ALA          
SEQRES   6 B  430  LYS ARG SER MET ALA LYS VAL PHE TYR LEU GLU LYS HIS          
SEQRES   7 B  430  GLY GLU GLY TYR ILE ALA LYS ILE ALA TYR PRO LEU THR          
SEQRES   8 B  430  LEU PHE GLU GLU GLY SER LEU VAL GLN LEU PHE SER ALA          
SEQRES   9 B  430  VAL ALA GLY ASN VAL PHE GLY MET LYS ALA LEU LYS ASN          
SEQRES  10 B  430  LEU ARG LEU LEU ASP PHE HIS PRO PRO TYR GLU TYR LEU          
SEQRES  11 B  430  ARG HIS PHE LYS GLY PRO GLN PHE GLY VAL GLN GLY ILE          
SEQRES  12 B  430  ARG GLU PHE MET GLY VAL LYS ASP ARG PRO LEU THR ALA          
SEQRES  13 B  430  THR VAL PRO LYS PRO LYS MET GLY TRP SER VAL GLU GLU          
SEQRES  14 B  430  TYR ALA GLU ILE ALA TYR GLU LEU TRP SER GLY GLY ILE          
SEQRES  15 B  430  ASP LEU LEU LYS ASP ASP GLU ASN PHE THR SER PHE PRO          
SEQRES  16 B  430  PHE ASN ARG PHE GLU GLU ARG VAL ARG LYS LEU TYR ARG          
SEQRES  17 B  430  VAL ARG ASP ARG VAL GLU ALA GLU THR GLY GLU THR LYS          
SEQRES  18 B  430  GLU TYR LEU ILE ASN ILE THR GLY PRO VAL ASN ILE MET          
SEQRES  19 B  430  GLU LYS ARG ALA GLU MET VAL ALA ASN GLU GLY GLY GLN          
SEQRES  20 B  430  TYR VAL MET ILE ASP ILE VAL VAL ALA GLY TRP SER ALA          
SEQRES  21 B  430  LEU GLN TYR MET ARG GLU VAL THR GLU ASP LEU GLY LEU          
SEQRES  22 B  430  ALA ILE HIS ALA HIS ARG ALA MET HIS ALA ALA PHE THR          
SEQRES  23 B  430  ARG ASN PRO ARG HIS GLY ILE THR MET LEU ALA LEU ALA          
SEQRES  24 B  430  LYS ALA ALA ARG MET ILE GLY VAL ASP GLN ILE HIS THR          
SEQRES  25 B  430  GLY THR ALA VAL GLY LYS MET ALA GLY ASN TYR GLU GLU          
SEQRES  26 B  430  ILE LYS ARG ILE ASN ASP PHE LEU LEU SER LYS TRP GLU          
SEQRES  27 B  430  HIS ILE ARG PRO VAL PHE PRO VAL ALA SER GLY GLY LEU          
SEQRES  28 B  430  HIS PRO GLY LEU MET PRO GLU LEU ILE ARG LEU PHE GLY          
SEQRES  29 B  430  LYS ASP LEU VAL ILE GLN ALA GLY GLY GLY VAL MET GLY          
SEQRES  30 B  430  HIS PRO ASP GLY PRO ARG ALA GLY ALA LYS ALA LEU ARG          
SEQRES  31 B  430  ASP ALA ILE ASP ALA ALA ILE GLU GLY VAL ASP LEU ASP          
SEQRES  32 B  430  GLU LYS ALA LYS SER SER PRO GLU LEU LYS LYS SER LEU          
SEQRES  33 B  430  ARG GLU VAL GLY LEU SER LYS ALA LYS VAL GLY VAL GLN          
SEQRES  34 B  430  HIS                                                          
SEQRES   1 C  430  MET MET VAL LEU ARG MET LYS VAL GLU TRP TYR LEU ASP          
SEQRES   2 C  430  PHE VAL ASP LEU ASN TYR GLU PRO GLY ARG ASP GLU LEU          
SEQRES   3 C  430  ILE VAL GLU TYR TYR PHE GLU PRO ASN GLY VAL SER PRO          
SEQRES   4 C  430  GLU GLU ALA ALA GLY ARG ILE ALA SER GLU SER SER ILE          
SEQRES   5 C  430  GLY THR TRP THR THR LEU TRP LYS LEU PRO GLU MET ALA          
SEQRES   6 C  430  LYS ARG SER MET ALA LYS VAL PHE TYR LEU GLU LYS HIS          
SEQRES   7 C  430  GLY GLU GLY TYR ILE ALA LYS ILE ALA TYR PRO LEU THR          
SEQRES   8 C  430  LEU PHE GLU GLU GLY SER LEU VAL GLN LEU PHE SER ALA          
SEQRES   9 C  430  VAL ALA GLY ASN VAL PHE GLY MET LYS ALA LEU LYS ASN          
SEQRES  10 C  430  LEU ARG LEU LEU ASP PHE HIS PRO PRO TYR GLU TYR LEU          
SEQRES  11 C  430  ARG HIS PHE LYS GLY PRO GLN PHE GLY VAL GLN GLY ILE          
SEQRES  12 C  430  ARG GLU PHE MET GLY VAL LYS ASP ARG PRO LEU THR ALA          
SEQRES  13 C  430  THR VAL PRO LYS PRO LYS MET GLY TRP SER VAL GLU GLU          
SEQRES  14 C  430  TYR ALA GLU ILE ALA TYR GLU LEU TRP SER GLY GLY ILE          
SEQRES  15 C  430  ASP LEU LEU LYS ASP ASP GLU ASN PHE THR SER PHE PRO          
SEQRES  16 C  430  PHE ASN ARG PHE GLU GLU ARG VAL ARG LYS LEU TYR ARG          
SEQRES  17 C  430  VAL ARG ASP ARG VAL GLU ALA GLU THR GLY GLU THR LYS          
SEQRES  18 C  430  GLU TYR LEU ILE ASN ILE THR GLY PRO VAL ASN ILE MET          
SEQRES  19 C  430  GLU LYS ARG ALA GLU MET VAL ALA ASN GLU GLY GLY GLN          
SEQRES  20 C  430  TYR VAL MET ILE ASP ILE VAL VAL ALA GLY TRP SER ALA          
SEQRES  21 C  430  LEU GLN TYR MET ARG GLU VAL THR GLU ASP LEU GLY LEU          
SEQRES  22 C  430  ALA ILE HIS ALA HIS ARG ALA MET HIS ALA ALA PHE THR          
SEQRES  23 C  430  ARG ASN PRO ARG HIS GLY ILE THR MET LEU ALA LEU ALA          
SEQRES  24 C  430  LYS ALA ALA ARG MET ILE GLY VAL ASP GLN ILE HIS THR          
SEQRES  25 C  430  GLY THR ALA VAL GLY LYS MET ALA GLY ASN TYR GLU GLU          
SEQRES  26 C  430  ILE LYS ARG ILE ASN ASP PHE LEU LEU SER LYS TRP GLU          
SEQRES  27 C  430  HIS ILE ARG PRO VAL PHE PRO VAL ALA SER GLY GLY LEU          
SEQRES  28 C  430  HIS PRO GLY LEU MET PRO GLU LEU ILE ARG LEU PHE GLY          
SEQRES  29 C  430  LYS ASP LEU VAL ILE GLN ALA GLY GLY GLY VAL MET GLY          
SEQRES  30 C  430  HIS PRO ASP GLY PRO ARG ALA GLY ALA LYS ALA LEU ARG          
SEQRES  31 C  430  ASP ALA ILE ASP ALA ALA ILE GLU GLY VAL ASP LEU ASP          
SEQRES  32 C  430  GLU LYS ALA LYS SER SER PRO GLU LEU LYS LYS SER LEU          
SEQRES  33 C  430  ARG GLU VAL GLY LEU SER LYS ALA LYS VAL GLY VAL GLN          
SEQRES  34 C  430  HIS                                                          
SEQRES   1 D  430  MET MET VAL LEU ARG MET LYS VAL GLU TRP TYR LEU ASP          
SEQRES   2 D  430  PHE VAL ASP LEU ASN TYR GLU PRO GLY ARG ASP GLU LEU          
SEQRES   3 D  430  ILE VAL GLU TYR TYR PHE GLU PRO ASN GLY VAL SER PRO          
SEQRES   4 D  430  GLU GLU ALA ALA GLY ARG ILE ALA SER GLU SER SER ILE          
SEQRES   5 D  430  GLY THR TRP THR THR LEU TRP LYS LEU PRO GLU MET ALA          
SEQRES   6 D  430  LYS ARG SER MET ALA LYS VAL PHE TYR LEU GLU LYS HIS          
SEQRES   7 D  430  GLY GLU GLY TYR ILE ALA LYS ILE ALA TYR PRO LEU THR          
SEQRES   8 D  430  LEU PHE GLU GLU GLY SER LEU VAL GLN LEU PHE SER ALA          
SEQRES   9 D  430  VAL ALA GLY ASN VAL PHE GLY MET LYS ALA LEU LYS ASN          
SEQRES  10 D  430  LEU ARG LEU LEU ASP PHE HIS PRO PRO TYR GLU TYR LEU          
SEQRES  11 D  430  ARG HIS PHE LYS GLY PRO GLN PHE GLY VAL GLN GLY ILE          
SEQRES  12 D  430  ARG GLU PHE MET GLY VAL LYS ASP ARG PRO LEU THR ALA          
SEQRES  13 D  430  THR VAL PRO LYS PRO LYS MET GLY TRP SER VAL GLU GLU          
SEQRES  14 D  430  TYR ALA GLU ILE ALA TYR GLU LEU TRP SER GLY GLY ILE          
SEQRES  15 D  430  ASP LEU LEU LYS ASP ASP GLU ASN PHE THR SER PHE PRO          
SEQRES  16 D  430  PHE ASN ARG PHE GLU GLU ARG VAL ARG LYS LEU TYR ARG          
SEQRES  17 D  430  VAL ARG ASP ARG VAL GLU ALA GLU THR GLY GLU THR LYS          
SEQRES  18 D  430  GLU TYR LEU ILE ASN ILE THR GLY PRO VAL ASN ILE MET          
SEQRES  19 D  430  GLU LYS ARG ALA GLU MET VAL ALA ASN GLU GLY GLY GLN          
SEQRES  20 D  430  TYR VAL MET ILE ASP ILE VAL VAL ALA GLY TRP SER ALA          
SEQRES  21 D  430  LEU GLN TYR MET ARG GLU VAL THR GLU ASP LEU GLY LEU          
SEQRES  22 D  430  ALA ILE HIS ALA HIS ARG ALA MET HIS ALA ALA PHE THR          
SEQRES  23 D  430  ARG ASN PRO ARG HIS GLY ILE THR MET LEU ALA LEU ALA          
SEQRES  24 D  430  LYS ALA ALA ARG MET ILE GLY VAL ASP GLN ILE HIS THR          
SEQRES  25 D  430  GLY THR ALA VAL GLY LYS MET ALA GLY ASN TYR GLU GLU          
SEQRES  26 D  430  ILE LYS ARG ILE ASN ASP PHE LEU LEU SER LYS TRP GLU          
SEQRES  27 D  430  HIS ILE ARG PRO VAL PHE PRO VAL ALA SER GLY GLY LEU          
SEQRES  28 D  430  HIS PRO GLY LEU MET PRO GLU LEU ILE ARG LEU PHE GLY          
SEQRES  29 D  430  LYS ASP LEU VAL ILE GLN ALA GLY GLY GLY VAL MET GLY          
SEQRES  30 D  430  HIS PRO ASP GLY PRO ARG ALA GLY ALA LYS ALA LEU ARG          
SEQRES  31 D  430  ASP ALA ILE ASP ALA ALA ILE GLU GLY VAL ASP LEU ASP          
SEQRES  32 D  430  GLU LYS ALA LYS SER SER PRO GLU LEU LYS LYS SER LEU          
SEQRES  33 D  430  ARG GLU VAL GLY LEU SER LYS ALA LYS VAL GLY VAL GLN          
SEQRES  34 D  430  HIS                                                          
FORMUL   5  HOH   *204(H2 O)                                                    
HELIX    1   1 SER A   38  SER A   50  1                                  13    
HELIX    2   2 PRO A   62  LYS A   66  5                                   5    
HELIX    3   3 SER A   97  ALA A  106  1                                  10    
HELIX    4   4 PRO A  126  ARG A  131  1                                   6    
HELIX    5   5 PHE A  138  GLY A  148  1                                  11    
HELIX    6   6 SER A  166  GLY A  181  1                                  16    
HELIX    7   7 ARG A  198  GLY A  218  1                                  21    
HELIX    8   8 PRO A  230  GLU A  244  1                                  15    
HELIX    9   9 ASP A  252  GLY A  257  1                                   6    
HELIX   10  10 GLY A  257  GLY A  272  1                                  16    
HELIX   11  11 MET A  281  PHE A  285  5                                   5    
HELIX   12  12 THR A  294  ILE A  305  1                                  12    
HELIX   13  13 ASN A  322  SER A  335  1                                  14    
HELIX   14  14 LEU A  355  GLY A  364  1                                  10    
HELIX   15  15 ALA A  371  GLY A  377  1                                   7    
HELIX   16  16 GLY A  381  GLU A  398  1                                  18    
HELIX   17  17 ASP A  401  ALA A  406  1                                   6    
HELIX   18  18 SER A  409  LEU A  421  1                                  13    
SHEET    1   A 5 LYS A  71  HIS A  78  0                                        
SHEET    2   A 5 GLY A  81  PRO A  89 -1  O  ALA A  87   N  LYS A  71           
SHEET    3   A 5 GLU A  25  PRO A  34 -1  N  LEU A  26   O  TYR A  88           
SHEET    4   A 5 LEU A 115  HIS A 124 -1  O  ARG A 119   N  TYR A  31           
SHEET    5   A 5 GLY A 292  ILE A 293  1  O  GLY A 292   N  LEU A 120           
SHEET    1   B 6 GLU A 222  LEU A 224  0                                        
SHEET    2   B 6 LEU A 184  LYS A 186  1  N  LEU A 185   O  LEU A 224           
SHEET    3   B 6 LEU A 154  THR A 157  1  N  THR A 155   O  LEU A 184           
SHEET    4   B 6 VAL A 368  GLN A 370  1  O  ILE A 369   N  LEU A 154           
SHEET    5   B 6 PRO A 345  SER A 348  1  N  ALA A 347   O  VAL A 368           
SHEET    6   B 6 ILE A 310  HIS A 311  1  N  ILE A 310   O  VAL A 346           
SHEET    1   C 2 TYR A 248  ILE A 251  0                                        
SHEET    2   C 2 ALA A 274  ALA A 277  1  O  HIS A 276   N  ILE A 251           
CISPEP   1 LYS A  160    PRO A  161          0         0.02                     
CISPEP   2 LYS B  160    PRO B  161          0        -0.03                     
CISPEP   3 LYS C  160    PRO C  161          0        -0.02                     
CISPEP   4 LYS D  160    PRO D  161          0         0.09                     
CRYST1  171.478  149.207  107.461  90.00 127.37  90.00 C 1 2 1      16          
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      0.005832  0.000000  0.004453        0.00000                         
SCALE2      0.000000  0.006702  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011709        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.250050  0.863740 -0.437520      -30.09503    1                    
MTRIX2   2 -0.866420 -0.002100 -0.499310       34.80614    1                    
MTRIX3   2 -0.432190  0.503930  0.747840      -17.49799    1                    
MTRIX1   3 -0.250730  0.864320  0.435990      -30.10256    1                    
MTRIX2   3  0.868390  0.001770  0.495890       34.89288    1                    
MTRIX3   3  0.427830  0.502940 -0.751000      -17.44243    1                    
MTRIX1   4 -0.492800  0.005350 -0.870120       -0.05093    1                    
MTRIX2   4  0.000240 -0.999980 -0.006280       69.68140    1                    
MTRIX3   4 -0.870140 -0.003300  0.492790       -0.02970    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system