GenomeNet

Database: PDB
Entry: 2VM8
LinkDB: 2VM8
Original site: 2VM8 
HEADER    SIGNALING PROTEIN                       24-JAN-08   2VM8              
TITLE     HUMAN CRMP-2 CRYSTALLISED IN THE PRESENCE OF MG                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROPYRIMIDINASE-RELATED PROTEIN 2;                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUES 13-490;                                           
COMPND   5 SYNONYM: COLLAPSIN RESPONSE MEDIATOR PROTEIN 2, DRP-2, CRMP-2, N2A3; 
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
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: PNIC-BSA4                                 
KEYWDS    NEUROGENESIS, PHOSPHOPROTEIN, DIFFERENTIATION, CRMP, CYTOPLASM, TIM   
KEYWDS   2 BARREL, POLYMORPHISM, AXONAL PATHFINDING, DEVELOPMENTAL PROTEIN,     
KEYWDS   3 SIGNALING PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.KURSULA                                                             
REVDAT   5   17-JAN-18 2VM8    1       REMARK                                   
REVDAT   4   28-APR-09 2VM8    1       CRYST1                                   
REVDAT   3   24-FEB-09 2VM8    1       VERSN                                    
REVDAT   2   07-OCT-08 2VM8    1       JRNL                                     
REVDAT   1   26-AUG-08 2VM8    0                                                
JRNL        AUTH   V.MAJAVA,N.LOYTYNOJA,W.Q.CHEN,G.LUBEC,P.KURSULA              
JRNL        TITL   CRYSTAL AND SOLUTION STRUCTURE, STABILITY AND POST-          
JRNL        TITL 2 TRANSLATIONAL MODIFICATIONS OF COLLAPSIN RESPONSE MEDIATOR   
JRNL        TITL 3 PROTEIN 2.                                                   
JRNL        REF    FEBS J.                       V. 275  4583 2008              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   18699782                                                     
JRNL        DOI    10.1111/J.1742-4658.2008.06601.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0028                                      
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)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 162237                         
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) : 0.259                           
REMARK   3   R VALUE            (WORKING SET) : 0.256                           
REMARK   3   FREE R VALUE                     : 0.325                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8539                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10173                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3840                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 535                          
REMARK   3   BIN FREE R VALUE                    : 0.4190                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14674                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 1793                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.04000                                             
REMARK   3    B22 (A**2) : -0.41000                                             
REMARK   3    B33 (A**2) : 2.45000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.209         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.204         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.211         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.571         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.915                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.847                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15057 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A): 10053 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20454 ; 1.579 ; 1.951       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 24649 ; 0.984 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1929 ; 6.645 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   665 ;38.435 ;24.797       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2559 ;16.061 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    77 ;17.645 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2311 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 16902 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2907 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3900 ; 0.226 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 11546 ; 0.209 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  7390 ; 0.184 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  8123 ; 0.090 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1472 ; 0.245 ; 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):     7 ; 0.183 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    38 ; 0.236 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.176 ; 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): 12242 ; 1.471 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15384 ; 1.891 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6371 ; 2.670 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5056 ; 3.428 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. DUE TO PSEUDOTRANSLATIONAL SYMMETRY, THE R FACTORS       
REMARK   3  REMAINED HIGHER THAN EXPECTED DURING REFINEMENT.                    
REMARK   4                                                                      
REMARK   4 2VM8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JAN-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290035104.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0408                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 170498                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
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) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2GSE                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       43.25500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      104.87500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.12000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      104.87500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.25500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       63.12000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 10540 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 77000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL                        
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 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   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     VAL A     0                                                      
REMARK 465     ASP A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     ASN A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     TYR A     8                                                      
REMARK 465     PHE A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     MET A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     MET B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     SER B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     VAL B     0                                                      
REMARK 465     ASP B     1                                                      
REMARK 465     LEU B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     ASN B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     TYR B     8                                                      
REMARK 465     PHE B     9                                                      
REMARK 465     GLN B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     MET B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     MET C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     HIS C    -8                                                      
REMARK 465     HIS C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     SER C    -3                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     VAL C     0                                                      
REMARK 465     ASP C     1                                                      
REMARK 465     LEU C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     THR C     4                                                      
REMARK 465     GLU C     5                                                      
REMARK 465     ASN C     6                                                      
REMARK 465     LEU C     7                                                      
REMARK 465     TYR C     8                                                      
REMARK 465     PHE C     9                                                      
REMARK 465     GLN C    10                                                      
REMARK 465     SER C    11                                                      
REMARK 465     MET C    12                                                      
REMARK 465     THR C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     MET D   -10                                                      
REMARK 465     HIS D    -9                                                      
REMARK 465     HIS D    -8                                                      
REMARK 465     HIS D    -7                                                      
REMARK 465     HIS D    -6                                                      
REMARK 465     HIS D    -5                                                      
REMARK 465     HIS D    -4                                                      
REMARK 465     SER D    -3                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     VAL D     0                                                      
REMARK 465     ASP D     1                                                      
REMARK 465     LEU D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     THR D     4                                                      
REMARK 465     GLU D     5                                                      
REMARK 465     ASN D     6                                                      
REMARK 465     LEU D     7                                                      
REMARK 465     TYR D     8                                                      
REMARK 465     PHE D     9                                                      
REMARK 465     GLN D    10                                                      
REMARK 465     SER D    11                                                      
REMARK 465     MET D    12                                                      
REMARK 465     THR D    13                                                      
REMARK 465     SER D    14                                                      
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 C  2075     O    HOH C  2375              2.00            
REMARK 500   OG   SER C   142     O    HOH C  2153              2.03            
REMARK 500   O    HOH A  2266     O    HOH A  2269              2.03            
REMARK 500   O    HOH C  2351     O    HOH D  2297              2.04            
REMARK 500   O    HOH D  2040     O    HOH D  2041              2.04            
REMARK 500   O    HOH B  2100     O    HOH B  2116              2.07            
REMARK 500   O    HOH C  2104     O    HOH C  2289              2.08            
REMARK 500   OE1  GLU C   143     O    HOH C  2157              2.10            
REMARK 500   O    HOH C  2314     O    HOH C  2316              2.11            
REMARK 500   O    HOH B  2213     O    HOH B  2263              2.12            
REMARK 500   O    HOH C  2376     O    HOH C  2377              2.12            
REMARK 500   OD2  ASP D   413     OG   SER D   416              2.13            
REMARK 500   O    GLY D   399     O    HOH D  2390              2.14            
REMARK 500   O    GLN C    81     O    HOH C  2078              2.15            
REMARK 500   O    HOH B  2149     O    HOH B  2307              2.15            
REMARK 500   NZ   LYS C   341     O    HOH C  2364              2.15            
REMARK 500   OE1  GLU C   229     OG   SER C   259              2.16            
REMARK 500   O    HOH D  2072     O    HOH D  2074              2.16            
REMARK 500   O    HOH A  2376     O    HOH A  2381              2.16            
REMARK 500   CG   HIS D   333     O    HOH D  2356              2.16            
REMARK 500   OD2  ASP C    80     O    HOH C  2075              2.16            
REMARK 500   OE2  GLU B   490     O    HOH B  2395              2.16            
REMARK 500   O    HOH C  2273     O    HOH C  2274              2.17            
REMARK 500   O    VAL A   224     O    HOH A  2224              2.17            
REMARK 500   O    THR D   355     O    HOH D  2356              2.17            
REMARK 500   O    HOH B  2208     O    HOH B  2211              2.17            
REMARK 500   O    HOH D  2177     O    HOH D  2375              2.18            
REMARK 500   O    HOH C  2325     O    HOH C  2327              2.18            
REMARK 500   O    HOH C  2256     O    HOH C  2257              2.19            
REMARK 500   O    HOH B  2260     O    HOH B  2296              2.19            
REMARK 500   O    HOH C  2184     O    HOH C  2409              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    CYS C 334   CB    CYS C 334   SG     -0.098                       
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    ASP A  15     -178.28     66.32                                   
REMARK 500    ASN A  48       54.78     38.52                                   
REMARK 500    PRO A  52     -178.33    -57.53                                   
REMARK 500    GLN A  77       52.13     37.61                                   
REMARK 500    GLN A  81       49.69     30.61                                   
REMARK 500    PHE A 170       62.10     63.41                                   
REMARK 500    ASP A 172       13.87     50.62                                   
REMARK 500    ARG A 173      -57.07   -123.13                                   
REMARK 500    SER A 385      -53.97   -138.16                                   
REMARK 500    ASN A 426       48.64    -99.40                                   
REMARK 500    GLU A 435      119.25    -34.76                                   
REMARK 500    LEU A 488      173.19    -58.85                                   
REMARK 500    GLN B  29      155.47    179.13                                   
REMARK 500    GLU B  38      122.85   -174.94                                   
REMARK 500    GLU B  47       47.52   -106.84                                   
REMARK 500    ASN B  48      -16.43    164.41                                   
REMARK 500    LEU B  49      114.38      0.51                                   
REMARK 500    GLN B  77       37.06     30.77                                   
REMARK 500    PHE B 170       64.01     75.73                                   
REMARK 500    ARG B 173      -71.35   -174.82                                   
REMARK 500    ARG B 173      -71.07   -174.99                                   
REMARK 500    THR B 285     -157.26   -157.65                                   
REMARK 500    ASP B 310      109.29    -57.20                                   
REMARK 500    ASN B 347      101.31   -172.72                                   
REMARK 500    SER B 385      -47.87   -140.98                                   
REMARK 500    LEU B 444      -55.23   -129.60                                   
REMARK 500    ASP B 456       51.01     38.28                                   
REMARK 500    GLU C  38      115.67   -167.61                                   
REMARK 500    ASN C  48       70.85     45.60                                   
REMARK 500    PRO C  52     -166.97    -52.68                                   
REMARK 500    PHE C 170       58.41     70.02                                   
REMARK 500    ASP C 172       -0.28     60.19                                   
REMARK 500    ARG C 173      -69.55   -109.50                                   
REMARK 500    ALA C 239      -70.73    -41.36                                   
REMARK 500    ASN C 347      104.14   -167.65                                   
REMARK 500    SER C 385      -45.56   -145.59                                   
REMARK 500    ASN C 393       31.97     71.58                                   
REMARK 500    ASN C 426       44.79    -80.01                                   
REMARK 500    ASP C 456       40.13     37.39                                   
REMARK 500    ALA C 489     -160.76    -72.66                                   
REMARK 500    GLU D  38      149.44   -175.47                                   
REMARK 500    PRO D  52     -145.38    -67.35                                   
REMARK 500    VAL D  72        3.27    -69.39                                   
REMARK 500    HIS D  73       87.93   -154.92                                   
REMARK 500    ARG D  75       57.43   -145.13                                   
REMARK 500    GLN D  81       41.70     35.53                                   
REMARK 500    PHE D 170       64.14     64.14                                   
REMARK 500    ARG D 173      -68.28   -155.55                                   
REMARK 500    GLU D 277       78.02   -119.55                                   
REMARK 500    ALA D 332       46.25     35.45                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      57 RAMACHANDRAN OUTLIERS.                        
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 A2017        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH A2020        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH A2033        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH A2037        DISTANCE =  8.22 ANGSTROMS                       
REMARK 525    HOH A2038        DISTANCE =  7.67 ANGSTROMS                       
REMARK 525    HOH A2039        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH A2049        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH A2115        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH A2120        DISTANCE =  7.04 ANGSTROMS                       
REMARK 525    HOH A2195        DISTANCE =  6.69 ANGSTROMS                       
REMARK 525    HOH B2005        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH B2006        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH B2020        DISTANCE =  6.91 ANGSTROMS                       
REMARK 525    HOH B2038        DISTANCE =  7.07 ANGSTROMS                       
REMARK 525    HOH B2041        DISTANCE =  6.10 ANGSTROMS                       
REMARK 525    HOH B2049        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH B2053        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH B2074        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH B2106        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH B2159        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH C2011        DISTANCE =  7.09 ANGSTROMS                       
REMARK 525    HOH C2019        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH C2022        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH C2024        DISTANCE =  6.42 ANGSTROMS                       
REMARK 525    HOH C2034        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH C2036        DISTANCE =  6.99 ANGSTROMS                       
REMARK 525    HOH C2041        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH C2058        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH C2187        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH C2218        DISTANCE =  7.14 ANGSTROMS                       
REMARK 525    HOH C2224        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH C2239        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH D2006        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH D2017        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH D2018        DISTANCE =  6.95 ANGSTROMS                       
REMARK 525    HOH D2025        DISTANCE =  8.33 ANGSTROMS                       
REMARK 525    HOH D2060        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH D2062        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH D2068        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH D2159        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH D2160        DISTANCE =  6.74 ANGSTROMS                       
REMARK 525    HOH D2161        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH D2162        DISTANCE =  7.18 ANGSTROMS                       
REMARK 525    HOH D2195        DISTANCE =  6.90 ANGSTROMS                       
REMARK 525    HOH D2196        DISTANCE =  6.66 ANGSTROMS                       
REMARK 525    HOH D2199        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH D2234        DISTANCE =  6.94 ANGSTROMS                       
REMARK 525    HOH D2235        DISTANCE =  5.97 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1491  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2322   O                                                      
REMARK 620 2 HOH A2061   O    82.2                                              
REMARK 620 3 HOH A2317   O    70.9 134.0                                        
REMARK 620 4 HOH A2062   O   160.4  85.4 108.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1491  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2059   O                                                      
REMARK 620 2 HOH B2058   O    79.6                                              
REMARK 620 3 HOH B2292   O    95.9 150.8                                        
REMARK 620 4 HOH B2293   O   138.7  82.0  82.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C1491  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C2375   O                                                      
REMARK 620 2 HOH C2374   O    83.9                                              
REMARK 620 3 HOH C2076   O    72.9  92.6                                        
REMARK 620 N                    1     2                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1491                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1491                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 1491                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2GSE   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIHYDROPYRIMIDINEASE -LIKE 2              
DBREF  2VM8 A  -10    12  PDB    2VM8     2VM8           -10     12             
DBREF  2VM8 A   13   490  UNP    Q16555   DPYL2_HUMAN     13    490             
DBREF  2VM8 B  -10    12  PDB    2VM8     2VM8           -10     12             
DBREF  2VM8 B   13   490  UNP    Q16555   DPYL2_HUMAN     13    490             
DBREF  2VM8 C  -10    12  PDB    2VM8     2VM8           -10     12             
DBREF  2VM8 C   13   490  UNP    Q16555   DPYL2_HUMAN     13    490             
DBREF  2VM8 D  -10    12  PDB    2VM8     2VM8           -10     12             
DBREF  2VM8 D   13   490  UNP    Q16555   DPYL2_HUMAN     13    490             
SEQRES   1 A  501  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  501  GLY THR GLU ASN LEU TYR PHE GLN SER MET THR SER ASP          
SEQRES   3 A  501  ARG LEU LEU ILE LYS GLY GLY LYS ILE VAL ASN ASP ASP          
SEQRES   4 A  501  GLN SER PHE TYR ALA ASP ILE TYR MET GLU ASP GLY LEU          
SEQRES   5 A  501  ILE LYS GLN ILE GLY GLU ASN LEU ILE VAL PRO GLY GLY          
SEQRES   6 A  501  VAL LYS THR ILE GLU ALA HIS SER ARG MET VAL ILE PRO          
SEQRES   7 A  501  GLY GLY ILE ASP VAL HIS THR ARG PHE GLN MET PRO ASP          
SEQRES   8 A  501  GLN GLY MET THR SER ALA ASP ASP PHE PHE GLN GLY THR          
SEQRES   9 A  501  LYS ALA ALA LEU ALA GLY GLY THR THR MET ILE ILE ASP          
SEQRES  10 A  501  HIS VAL VAL PRO GLU PRO GLY THR SER LEU LEU ALA ALA          
SEQRES  11 A  501  PHE ASP GLN TRP ARG GLU TRP ALA ASP SER LYS SER CYS          
SEQRES  12 A  501  CYS ASP TYR SER LEU HIS VAL ASP ILE SER GLU TRP HIS          
SEQRES  13 A  501  LYS GLY ILE GLN GLU GLU MET GLU ALA LEU VAL LYS ASP          
SEQRES  14 A  501  HIS GLY VAL ASN SER PHE LEU VAL TYR MET ALA PHE LYS          
SEQRES  15 A  501  ASP ARG PHE GLN LEU THR ASP CYS GLN ILE TYR GLU VAL          
SEQRES  16 A  501  LEU SER VAL ILE ARG ASP ILE GLY ALA ILE ALA GLN VAL          
SEQRES  17 A  501  HIS ALA GLU ASN GLY ASP ILE ILE ALA GLU GLU GLN GLN          
SEQRES  18 A  501  ARG ILE LEU ASP LEU GLY ILE THR GLY PRO GLU GLY HIS          
SEQRES  19 A  501  VAL LEU SER ARG PRO GLU GLU VAL GLU ALA GLU ALA VAL          
SEQRES  20 A  501  ASN ARG ALA ILE THR ILE ALA ASN GLN THR ASN CYS PRO          
SEQRES  21 A  501  LEU TYR ILE THR LYS VAL MET SER LYS SER SER ALA GLU          
SEQRES  22 A  501  VAL ILE ALA GLN ALA ARG LYS LYS GLY THR VAL VAL TYR          
SEQRES  23 A  501  GLY GLU PRO ILE THR ALA SER LEU GLY THR ASP GLY SER          
SEQRES  24 A  501  HIS TYR TRP SER LYS ASN TRP ALA LYS ALA ALA ALA PHE          
SEQRES  25 A  501  VAL THR SER PRO PRO LEU SER PRO ASP PRO THR THR PRO          
SEQRES  26 A  501  ASP PHE LEU ASN SER LEU LEU SER CYS GLY ASP LEU GLN          
SEQRES  27 A  501  VAL THR GLY SER ALA HIS CYS THR PHE ASN THR ALA GLN          
SEQRES  28 A  501  LYS ALA VAL GLY LYS ASP ASN PHE THR LEU ILE PRO GLU          
SEQRES  29 A  501  GLY THR ASN GLY THR GLU GLU ARG MET SER VAL ILE TRP          
SEQRES  30 A  501  ASP LYS ALA VAL VAL THR GLY LYS MET ASP GLU ASN GLN          
SEQRES  31 A  501  PHE VAL ALA VAL THR SER THR ASN ALA ALA LYS VAL PHE          
SEQRES  32 A  501  ASN LEU TYR PRO ARG LYS GLY ARG ILE ALA VAL GLY SER          
SEQRES  33 A  501  ASP ALA ASP LEU VAL ILE TRP ASP PRO ASP SER VAL LYS          
SEQRES  34 A  501  THR ILE SER ALA LYS THR HIS ASN SER SER LEU GLU TYR          
SEQRES  35 A  501  ASN ILE PHE GLU GLY MET GLU CYS ARG GLY SER PRO LEU          
SEQRES  36 A  501  VAL VAL ILE SER GLN GLY LYS ILE VAL LEU GLU ASP GLY          
SEQRES  37 A  501  THR LEU HIS VAL THR GLU GLY SER GLY ARG TYR ILE PRO          
SEQRES  38 A  501  ARG LYS PRO PHE PRO ASP PHE VAL TYR LYS ARG ILE LYS          
SEQRES  39 A  501  ALA ARG SER ARG LEU ALA GLU                                  
SEQRES   1 B  501  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  501  GLY THR GLU ASN LEU TYR PHE GLN SER MET THR SER ASP          
SEQRES   3 B  501  ARG LEU LEU ILE LYS GLY GLY LYS ILE VAL ASN ASP ASP          
SEQRES   4 B  501  GLN SER PHE TYR ALA ASP ILE TYR MET GLU ASP GLY LEU          
SEQRES   5 B  501  ILE LYS GLN ILE GLY GLU ASN LEU ILE VAL PRO GLY GLY          
SEQRES   6 B  501  VAL LYS THR ILE GLU ALA HIS SER ARG MET VAL ILE PRO          
SEQRES   7 B  501  GLY GLY ILE ASP VAL HIS THR ARG PHE GLN MET PRO ASP          
SEQRES   8 B  501  GLN GLY MET THR SER ALA ASP ASP PHE PHE GLN GLY THR          
SEQRES   9 B  501  LYS ALA ALA LEU ALA GLY GLY THR THR MET ILE ILE ASP          
SEQRES  10 B  501  HIS VAL VAL PRO GLU PRO GLY THR SER LEU LEU ALA ALA          
SEQRES  11 B  501  PHE ASP GLN TRP ARG GLU TRP ALA ASP SER LYS SER CYS          
SEQRES  12 B  501  CYS ASP TYR SER LEU HIS VAL ASP ILE SER GLU TRP HIS          
SEQRES  13 B  501  LYS GLY ILE GLN GLU GLU MET GLU ALA LEU VAL LYS ASP          
SEQRES  14 B  501  HIS GLY VAL ASN SER PHE LEU VAL TYR MET ALA PHE LYS          
SEQRES  15 B  501  ASP ARG PHE GLN LEU THR ASP CYS GLN ILE TYR GLU VAL          
SEQRES  16 B  501  LEU SER VAL ILE ARG ASP ILE GLY ALA ILE ALA GLN VAL          
SEQRES  17 B  501  HIS ALA GLU ASN GLY ASP ILE ILE ALA GLU GLU GLN GLN          
SEQRES  18 B  501  ARG ILE LEU ASP LEU GLY ILE THR GLY PRO GLU GLY HIS          
SEQRES  19 B  501  VAL LEU SER ARG PRO GLU GLU VAL GLU ALA GLU ALA VAL          
SEQRES  20 B  501  ASN ARG ALA ILE THR ILE ALA ASN GLN THR ASN CYS PRO          
SEQRES  21 B  501  LEU TYR ILE THR LYS VAL MET SER LYS SER SER ALA GLU          
SEQRES  22 B  501  VAL ILE ALA GLN ALA ARG LYS LYS GLY THR VAL VAL TYR          
SEQRES  23 B  501  GLY GLU PRO ILE THR ALA SER LEU GLY THR ASP GLY SER          
SEQRES  24 B  501  HIS TYR TRP SER LYS ASN TRP ALA LYS ALA ALA ALA PHE          
SEQRES  25 B  501  VAL THR SER PRO PRO LEU SER PRO ASP PRO THR THR PRO          
SEQRES  26 B  501  ASP PHE LEU ASN SER LEU LEU SER CYS GLY ASP LEU GLN          
SEQRES  27 B  501  VAL THR GLY SER ALA HIS CYS THR PHE ASN THR ALA GLN          
SEQRES  28 B  501  LYS ALA VAL GLY LYS ASP ASN PHE THR LEU ILE PRO GLU          
SEQRES  29 B  501  GLY THR ASN GLY THR GLU GLU ARG MET SER VAL ILE TRP          
SEQRES  30 B  501  ASP LYS ALA VAL VAL THR GLY LYS MET ASP GLU ASN GLN          
SEQRES  31 B  501  PHE VAL ALA VAL THR SER THR ASN ALA ALA LYS VAL PHE          
SEQRES  32 B  501  ASN LEU TYR PRO ARG LYS GLY ARG ILE ALA VAL GLY SER          
SEQRES  33 B  501  ASP ALA ASP LEU VAL ILE TRP ASP PRO ASP SER VAL LYS          
SEQRES  34 B  501  THR ILE SER ALA LYS THR HIS ASN SER SER LEU GLU TYR          
SEQRES  35 B  501  ASN ILE PHE GLU GLY MET GLU CYS ARG GLY SER PRO LEU          
SEQRES  36 B  501  VAL VAL ILE SER GLN GLY LYS ILE VAL LEU GLU ASP GLY          
SEQRES  37 B  501  THR LEU HIS VAL THR GLU GLY SER GLY ARG TYR ILE PRO          
SEQRES  38 B  501  ARG LYS PRO PHE PRO ASP PHE VAL TYR LYS ARG ILE LYS          
SEQRES  39 B  501  ALA ARG SER ARG LEU ALA GLU                                  
SEQRES   1 C  501  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 C  501  GLY THR GLU ASN LEU TYR PHE GLN SER MET THR SER ASP          
SEQRES   3 C  501  ARG LEU LEU ILE LYS GLY GLY LYS ILE VAL ASN ASP ASP          
SEQRES   4 C  501  GLN SER PHE TYR ALA ASP ILE TYR MET GLU ASP GLY LEU          
SEQRES   5 C  501  ILE LYS GLN ILE GLY GLU ASN LEU ILE VAL PRO GLY GLY          
SEQRES   6 C  501  VAL LYS THR ILE GLU ALA HIS SER ARG MET VAL ILE PRO          
SEQRES   7 C  501  GLY GLY ILE ASP VAL HIS THR ARG PHE GLN MET PRO ASP          
SEQRES   8 C  501  GLN GLY MET THR SER ALA ASP ASP PHE PHE GLN GLY THR          
SEQRES   9 C  501  LYS ALA ALA LEU ALA GLY GLY THR THR MET ILE ILE ASP          
SEQRES  10 C  501  HIS VAL VAL PRO GLU PRO GLY THR SER LEU LEU ALA ALA          
SEQRES  11 C  501  PHE ASP GLN TRP ARG GLU TRP ALA ASP SER LYS SER CYS          
SEQRES  12 C  501  CYS ASP TYR SER LEU HIS VAL ASP ILE SER GLU TRP HIS          
SEQRES  13 C  501  LYS GLY ILE GLN GLU GLU MET GLU ALA LEU VAL LYS ASP          
SEQRES  14 C  501  HIS GLY VAL ASN SER PHE LEU VAL TYR MET ALA PHE LYS          
SEQRES  15 C  501  ASP ARG PHE GLN LEU THR ASP CYS GLN ILE TYR GLU VAL          
SEQRES  16 C  501  LEU SER VAL ILE ARG ASP ILE GLY ALA ILE ALA GLN VAL          
SEQRES  17 C  501  HIS ALA GLU ASN GLY ASP ILE ILE ALA GLU GLU GLN GLN          
SEQRES  18 C  501  ARG ILE LEU ASP LEU GLY ILE THR GLY PRO GLU GLY HIS          
SEQRES  19 C  501  VAL LEU SER ARG PRO GLU GLU VAL GLU ALA GLU ALA VAL          
SEQRES  20 C  501  ASN ARG ALA ILE THR ILE ALA ASN GLN THR ASN CYS PRO          
SEQRES  21 C  501  LEU TYR ILE THR LYS VAL MET SER LYS SER SER ALA GLU          
SEQRES  22 C  501  VAL ILE ALA GLN ALA ARG LYS LYS GLY THR VAL VAL TYR          
SEQRES  23 C  501  GLY GLU PRO ILE THR ALA SER LEU GLY THR ASP GLY SER          
SEQRES  24 C  501  HIS TYR TRP SER LYS ASN TRP ALA LYS ALA ALA ALA PHE          
SEQRES  25 C  501  VAL THR SER PRO PRO LEU SER PRO ASP PRO THR THR PRO          
SEQRES  26 C  501  ASP PHE LEU ASN SER LEU LEU SER CYS GLY ASP LEU GLN          
SEQRES  27 C  501  VAL THR GLY SER ALA HIS CYS THR PHE ASN THR ALA GLN          
SEQRES  28 C  501  LYS ALA VAL GLY LYS ASP ASN PHE THR LEU ILE PRO GLU          
SEQRES  29 C  501  GLY THR ASN GLY THR GLU GLU ARG MET SER VAL ILE TRP          
SEQRES  30 C  501  ASP LYS ALA VAL VAL THR GLY LYS MET ASP GLU ASN GLN          
SEQRES  31 C  501  PHE VAL ALA VAL THR SER THR ASN ALA ALA LYS VAL PHE          
SEQRES  32 C  501  ASN LEU TYR PRO ARG LYS GLY ARG ILE ALA VAL GLY SER          
SEQRES  33 C  501  ASP ALA ASP LEU VAL ILE TRP ASP PRO ASP SER VAL LYS          
SEQRES  34 C  501  THR ILE SER ALA LYS THR HIS ASN SER SER LEU GLU TYR          
SEQRES  35 C  501  ASN ILE PHE GLU GLY MET GLU CYS ARG GLY SER PRO LEU          
SEQRES  36 C  501  VAL VAL ILE SER GLN GLY LYS ILE VAL LEU GLU ASP GLY          
SEQRES  37 C  501  THR LEU HIS VAL THR GLU GLY SER GLY ARG TYR ILE PRO          
SEQRES  38 C  501  ARG LYS PRO PHE PRO ASP PHE VAL TYR LYS ARG ILE LYS          
SEQRES  39 C  501  ALA ARG SER ARG LEU ALA GLU                                  
SEQRES   1 D  501  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 D  501  GLY THR GLU ASN LEU TYR PHE GLN SER MET THR SER ASP          
SEQRES   3 D  501  ARG LEU LEU ILE LYS GLY GLY LYS ILE VAL ASN ASP ASP          
SEQRES   4 D  501  GLN SER PHE TYR ALA ASP ILE TYR MET GLU ASP GLY LEU          
SEQRES   5 D  501  ILE LYS GLN ILE GLY GLU ASN LEU ILE VAL PRO GLY GLY          
SEQRES   6 D  501  VAL LYS THR ILE GLU ALA HIS SER ARG MET VAL ILE PRO          
SEQRES   7 D  501  GLY GLY ILE ASP VAL HIS THR ARG PHE GLN MET PRO ASP          
SEQRES   8 D  501  GLN GLY MET THR SER ALA ASP ASP PHE PHE GLN GLY THR          
SEQRES   9 D  501  LYS ALA ALA LEU ALA GLY GLY THR THR MET ILE ILE ASP          
SEQRES  10 D  501  HIS VAL VAL PRO GLU PRO GLY THR SER LEU LEU ALA ALA          
SEQRES  11 D  501  PHE ASP GLN TRP ARG GLU TRP ALA ASP SER LYS SER CYS          
SEQRES  12 D  501  CYS ASP TYR SER LEU HIS VAL ASP ILE SER GLU TRP HIS          
SEQRES  13 D  501  LYS GLY ILE GLN GLU GLU MET GLU ALA LEU VAL LYS ASP          
SEQRES  14 D  501  HIS GLY VAL ASN SER PHE LEU VAL TYR MET ALA PHE LYS          
SEQRES  15 D  501  ASP ARG PHE GLN LEU THR ASP CYS GLN ILE TYR GLU VAL          
SEQRES  16 D  501  LEU SER VAL ILE ARG ASP ILE GLY ALA ILE ALA GLN VAL          
SEQRES  17 D  501  HIS ALA GLU ASN GLY ASP ILE ILE ALA GLU GLU GLN GLN          
SEQRES  18 D  501  ARG ILE LEU ASP LEU GLY ILE THR GLY PRO GLU GLY HIS          
SEQRES  19 D  501  VAL LEU SER ARG PRO GLU GLU VAL GLU ALA GLU ALA VAL          
SEQRES  20 D  501  ASN ARG ALA ILE THR ILE ALA ASN GLN THR ASN CYS PRO          
SEQRES  21 D  501  LEU TYR ILE THR LYS VAL MET SER LYS SER SER ALA GLU          
SEQRES  22 D  501  VAL ILE ALA GLN ALA ARG LYS LYS GLY THR VAL VAL TYR          
SEQRES  23 D  501  GLY GLU PRO ILE THR ALA SER LEU GLY THR ASP GLY SER          
SEQRES  24 D  501  HIS TYR TRP SER LYS ASN TRP ALA LYS ALA ALA ALA PHE          
SEQRES  25 D  501  VAL THR SER PRO PRO LEU SER PRO ASP PRO THR THR PRO          
SEQRES  26 D  501  ASP PHE LEU ASN SER LEU LEU SER CYS GLY ASP LEU GLN          
SEQRES  27 D  501  VAL THR GLY SER ALA HIS CYS THR PHE ASN THR ALA GLN          
SEQRES  28 D  501  LYS ALA VAL GLY LYS ASP ASN PHE THR LEU ILE PRO GLU          
SEQRES  29 D  501  GLY THR ASN GLY THR GLU GLU ARG MET SER VAL ILE TRP          
SEQRES  30 D  501  ASP LYS ALA VAL VAL THR GLY LYS MET ASP GLU ASN GLN          
SEQRES  31 D  501  PHE VAL ALA VAL THR SER THR ASN ALA ALA LYS VAL PHE          
SEQRES  32 D  501  ASN LEU TYR PRO ARG LYS GLY ARG ILE ALA VAL GLY SER          
SEQRES  33 D  501  ASP ALA ASP LEU VAL ILE TRP ASP PRO ASP SER VAL LYS          
SEQRES  34 D  501  THR ILE SER ALA LYS THR HIS ASN SER SER LEU GLU TYR          
SEQRES  35 D  501  ASN ILE PHE GLU GLY MET GLU CYS ARG GLY SER PRO LEU          
SEQRES  36 D  501  VAL VAL ILE SER GLN GLY LYS ILE VAL LEU GLU ASP GLY          
SEQRES  37 D  501  THR LEU HIS VAL THR GLU GLY SER GLY ARG TYR ILE PRO          
SEQRES  38 D  501  ARG LYS PRO PHE PRO ASP PHE VAL TYR LYS ARG ILE LYS          
SEQRES  39 D  501  ALA ARG SER ARG LEU ALA GLU                                  
HET     MG  A1491       1                                                       
HET     MG  B1491       1                                                       
HET     MG  C1491       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   5   MG    3(MG 2+)                                                     
FORMUL   8  HOH   *1793(H2 O)                                                   
HELIX    1   1 ASP A   88  GLY A   99  1                                  12    
HELIX    2   2 SER A  115  SER A  131  1                                  17    
HELIX    3   3 HIS A  145  HIS A  159  1                                  15    
HELIX    4   4 THR A  177  GLY A  192  1                                  16    
HELIX    5   5 ASN A  201  ASP A  214  1                                  14    
HELIX    6   6 PRO A  220  ARG A  227  1                                   8    
HELIX    7   7 PRO A  228  ASN A  247  1                                  20    
HELIX    8   8 SER A  257  LYS A  270  1                                  14    
HELIX    9   9 ILE A  279  THR A  285  1                                   7    
HELIX   10  10 ASP A  286  SER A  292  5                                   7    
HELIX   11  11 ASN A  294  PHE A  301  1                                   8    
HELIX   12  12 THR A  312  CYS A  323  1                                  12    
HELIX   13  13 ASN A  337  ALA A  342  1                                   6    
HELIX   14  14 VAL A  343  LYS A  345  5                                   3    
HELIX   15  15 ASN A  347  ILE A  351  5                                   5    
HELIX   16  16 GLU A  360  VAL A  370  1                                  11    
HELIX   17  17 ASP A  376  SER A  385  1                                  10    
HELIX   18  18 SER A  385  ASN A  393  1                                   9    
HELIX   19  19 PRO A  475  LEU A  488  1                                  14    
HELIX   20  20 ASP B   88  GLY B   99  1                                  12    
HELIX   21  21 SER B  115  SER B  131  1                                  17    
HELIX   22  22 GLY B  147  HIS B  159  1                                  13    
HELIX   23  23 THR B  177  GLY B  192  1                                  16    
HELIX   24  24 ASN B  201  LEU B  215  1                                  15    
HELIX   25  25 PRO B  220  SER B  226  1                                   7    
HELIX   26  26 PRO B  228  ASN B  247  1                                  20    
HELIX   27  27 SER B  257  LYS B  270  1                                  14    
HELIX   28  28 ILE B  279  THR B  285  1                                   7    
HELIX   29  29 ASP B  286  SER B  292  5                                   7    
HELIX   30  30 ASN B  294  ALA B  299  1                                   6    
HELIX   31  31 ALA B  300  VAL B  302  5                                   3    
HELIX   32  32 THR B  312  CYS B  323  1                                  12    
HELIX   33  33 ASN B  337  ALA B  342  1                                   6    
HELIX   34  34 VAL B  343  LYS B  345  5                                   3    
HELIX   35  35 ASN B  347  ILE B  351  5                                   5    
HELIX   36  36 GLU B  360  VAL B  370  1                                  11    
HELIX   37  37 ASP B  376  SER B  385  1                                  10    
HELIX   38  38 SER B  385  PHE B  392  1                                   8    
HELIX   39  39 PRO B  475  ARG B  487  1                                  13    
HELIX   40  40 ASP C   88  GLY C   99  1                                  12    
HELIX   41  41 SER C  115  SER C  131  1                                  17    
HELIX   42  42 GLY C  147  HIS C  159  1                                  13    
HELIX   43  43 THR C  177  GLY C  192  1                                  16    
HELIX   44  44 ASN C  201  LEU C  215  1                                  15    
HELIX   45  45 PRO C  220  ARG C  227  1                                   8    
HELIX   46  46 PRO C  228  ASN C  247  1                                  20    
HELIX   47  47 SER C  257  LYS C  270  1                                  14    
HELIX   48  48 ILE C  279  THR C  285  1                                   7    
HELIX   49  49 ASP C  286  TRP C  291  5                                   6    
HELIX   50  50 ASN C  294  PHE C  301  1                                   8    
HELIX   51  51 THR C  312  CYS C  323  1                                  12    
HELIX   52  52 ASN C  337  VAL C  343  1                                   7    
HELIX   53  53 GLY C  344  ILE C  351  5                                   8    
HELIX   54  54 GLU C  360  VAL C  370  1                                  11    
HELIX   55  55 ASP C  376  VAL C  383  1                                   8    
HELIX   56  56 SER C  385  PHE C  392  1                                   8    
HELIX   57  57 PRO C  475  LEU C  488  1                                  14    
HELIX   58  58 ASP D   88  ALA D   98  1                                  11    
HELIX   59  59 SER D  115  SER D  131  1                                  17    
HELIX   60  60 GLY D  147  HIS D  159  1                                  13    
HELIX   61  61 THR D  177  GLY D  192  1                                  16    
HELIX   62  62 ASN D  201  ASP D  214  1                                  14    
HELIX   63  63 PRO D  220  SER D  226  1                                   7    
HELIX   64  64 PRO D  228  ASN D  247  1                                  20    
HELIX   65  65 SER D  257  LYS D  270  1                                  14    
HELIX   66  66 ILE D  279  THR D  285  1                                   7    
HELIX   67  67 ASP D  286  SER D  292  5                                   7    
HELIX   68  68 ASN D  294  PHE D  301  1                                   8    
HELIX   69  69 THR D  312  CYS D  323  1                                  12    
HELIX   70  70 ASN D  337  ALA D  342  1                                   6    
HELIX   71  71 VAL D  343  LYS D  345  5                                   3    
HELIX   72  72 ASN D  347  ILE D  351  5                                   5    
HELIX   73  73 GLU D  360  VAL D  370  1                                  11    
HELIX   74  74 ASP D  376  SER D  385  1                                  10    
HELIX   75  75 SER D  385  PHE D  392  1                                   8    
HELIX   76  76 PRO D  475  LEU D  488  1                                  14    
SHEET    1  AA 4 LEU A  41  GLY A  46  0                                        
SHEET    2  AA 4 SER A  30  GLU A  38 -1  O  ASP A  34   N  GLY A  46           
SHEET    3  AA 4 LEU A  17  VAL A  25 -1  O  LEU A  17   N  MET A  37           
SHEET    4  AA 4 THR A  57  GLU A  59  1  O  ILE A  58   N  LYS A  20           
SHEET    1  AB 8 LEU A  41  GLY A  46  0                                        
SHEET    2  AB 8 SER A  30  GLU A  38 -1  O  ASP A  34   N  GLY A  46           
SHEET    3  AB 8 LEU A  17  VAL A  25 -1  O  LEU A  17   N  MET A  37           
SHEET    4  AB 8 MET A  64  PRO A  67  1  O  VAL A  65   N  VAL A  25           
SHEET    5  AB 8 LEU A 409  THR A 419 -1  O  VAL A 410   N  ILE A  66           
SHEET    6  AB 8 GLU A 438  SER A 448 -1  O  CYS A 439   N  LYS A 418           
SHEET    7  AB 8 LYS A 451  GLU A 455 -1  O  LYS A 451   N  SER A 448           
SHEET    8  AB 8 THR A 458  LEU A 459 -1  O  THR A 458   N  GLU A 455           
SHEET    1  AC 7 GLY A  69  THR A  74  0                                        
SHEET    2  AC 7 THR A 101  VAL A 108  1  N  THR A 102   O  GLY A  69           
SHEET    3  AC 7 ASP A 134  ASP A 140  1  O  ASP A 134   N  ILE A 104           
SHEET    4  AC 7 SER A 163  TYR A 167  1  O  SER A 163   N  VAL A 139           
SHEET    5  AC 7 ILE A 194  HIS A 198  1  O  ILE A 194   N  PHE A 164           
SHEET    6  AC 7 LEU A 250  VAL A 255  1  O  TYR A 251   N  VAL A 197           
SHEET    7  AC 7 VAL A 274  PRO A 278  1  O  TYR A 275   N  ILE A 252           
SHEET    1  AD 2 PRO A  79  ASP A  80  0                                        
SHEET    2  AD 2 MET A  83  THR A  84 -1  O  MET A  83   N  ASP A  80           
SHEET    1  BA 4 LEU B  41  GLY B  46  0                                        
SHEET    2  BA 4 ASP B  34  GLU B  38 -1  O  ASP B  34   N  GLY B  46           
SHEET    3  BA 4 LEU B  17  LYS B  20 -1  O  LEU B  17   N  MET B  37           
SHEET    4  BA 4 LYS B  56  GLU B  59  1  O  LYS B  56   N  LEU B  18           
SHEET    1  BB 7 SER B  30  TYR B  32  0                                        
SHEET    2  BB 7 LYS B  23  VAL B  25 -1  O  ILE B  24   N  PHE B  31           
SHEET    3  BB 7 MET B  64  PRO B  67  1  O  VAL B  65   N  VAL B  25           
SHEET    4  BB 7 LEU B 409  THR B 419 -1  O  VAL B 410   N  ILE B  66           
SHEET    5  BB 7 GLU B 438  SER B 448 -1  O  CYS B 439   N  LYS B 418           
SHEET    6  BB 7 LYS B 451  GLU B 455 -1  O  LYS B 451   N  SER B 448           
SHEET    7  BB 7 THR B 458  LEU B 459 -1  O  THR B 458   N  GLU B 455           
SHEET    1  BC 7 GLY B  69  ASP B  71  0                                        
SHEET    2  BC 7 THR B 101  VAL B 108  1  N  THR B 102   O  GLY B  69           
SHEET    3  BC 7 ASP B 134  ASP B 140  1  O  ASP B 134   N  ILE B 104           
SHEET    4  BC 7 SER B 163  TYR B 167  1  O  SER B 163   N  VAL B 139           
SHEET    5  BC 7 ILE B 194  HIS B 198  1  O  ILE B 194   N  PHE B 164           
SHEET    6  BC 7 LEU B 250  VAL B 255  1  O  TYR B 251   N  VAL B 197           
SHEET    7  BC 7 VAL B 274  PRO B 278  1  O  TYR B 275   N  ILE B 252           
SHEET    1  BD 2 PRO B  79  ASP B  80  0                                        
SHEET    2  BD 2 MET B  83  THR B  84 -1  O  MET B  83   N  ASP B  80           
SHEET    1  CA 4 LEU C  41  GLY C  46  0                                        
SHEET    2  CA 4 ASP C  34  GLU C  38 -1  O  ASP C  34   N  GLY C  46           
SHEET    3  CA 4 LEU C  17  LYS C  20 -1  O  LEU C  17   N  MET C  37           
SHEET    4  CA 4 LYS C  56  GLU C  59  1  O  LYS C  56   N  LEU C  18           
SHEET    1  CB 7 SER C  30  TYR C  32  0                                        
SHEET    2  CB 7 LYS C  23  VAL C  25 -1  O  ILE C  24   N  PHE C  31           
SHEET    3  CB 7 MET C  64  PRO C  67  1  O  VAL C  65   N  VAL C  25           
SHEET    4  CB 7 LEU C 409  ILE C 420 -1  O  VAL C 410   N  ILE C  66           
SHEET    5  CB 7 MET C 437  SER C 448 -1  O  MET C 437   N  ILE C 420           
SHEET    6  CB 7 LYS C 451  GLU C 455 -1  O  LYS C 451   N  SER C 448           
SHEET    7  CB 7 THR C 458  LEU C 459 -1  O  THR C 458   N  GLU C 455           
SHEET    1  CC 7 GLY C  69  ASP C  71  0                                        
SHEET    2  CC 7 THR C 101  VAL C 108  1  N  THR C 102   O  GLY C  69           
SHEET    3  CC 7 ASP C 134  ILE C 141  1  O  ASP C 134   N  ILE C 104           
SHEET    4  CC 7 SER C 163  TYR C 167  1  O  SER C 163   N  VAL C 139           
SHEET    5  CC 7 ILE C 194  HIS C 198  1  O  ILE C 194   N  PHE C 164           
SHEET    6  CC 7 LEU C 250  VAL C 255  1  O  TYR C 251   N  VAL C 197           
SHEET    7  CC 7 VAL C 274  PRO C 278  1  O  TYR C 275   N  ILE C 252           
SHEET    1  CD 2 PRO C  79  ASP C  80  0                                        
SHEET    2  CD 2 MET C  83  THR C  84 -1  O  MET C  83   N  ASP C  80           
SHEET    1  DA 4 LEU D  41  GLY D  46  0                                        
SHEET    2  DA 4 ASP D  34  GLU D  38 -1  O  ASP D  34   N  GLY D  46           
SHEET    3  DA 4 LEU D  17  LYS D  20 -1  O  LEU D  17   N  MET D  37           
SHEET    4  DA 4 THR D  57  GLU D  59  1  O  ILE D  58   N  LYS D  20           
SHEET    1  DB 7 SER D  30  TYR D  32  0                                        
SHEET    2  DB 7 LYS D  23  VAL D  25 -1  O  ILE D  24   N  PHE D  31           
SHEET    3  DB 7 MET D  64  PRO D  67  1  O  VAL D  65   N  VAL D  25           
SHEET    4  DB 7 LEU D 409  ILE D 420 -1  O  VAL D 410   N  ILE D  66           
SHEET    5  DB 7 MET D 437  SER D 448 -1  O  MET D 437   N  ILE D 420           
SHEET    6  DB 7 LYS D 451  GLU D 455 -1  O  LYS D 451   N  SER D 448           
SHEET    7  DB 7 THR D 458  LEU D 459 -1  O  THR D 458   N  GLU D 455           
SHEET    1  DC 7 GLY D  69  ASP D  71  0                                        
SHEET    2  DC 7 THR D 101  VAL D 108  1  N  THR D 102   O  GLY D  69           
SHEET    3  DC 7 ASP D 134  ASP D 140  1  O  ASP D 134   N  ILE D 104           
SHEET    4  DC 7 SER D 163  TYR D 167  1  O  SER D 163   N  VAL D 139           
SHEET    5  DC 7 ILE D 194  HIS D 198  1  O  ILE D 194   N  PHE D 164           
SHEET    6  DC 7 LEU D 250  VAL D 255  1  O  TYR D 251   N  VAL D 197           
SHEET    7  DC 7 VAL D 274  PRO D 278  1  O  TYR D 275   N  ILE D 252           
SHEET    1  DD 2 PRO D  79  ASP D  80  0                                        
SHEET    2  DD 2 MET D  83  THR D  84 -1  O  MET D  83   N  ASP D  80           
LINK        MG    MG A1491                 O   HOH A2322     1555   1555  2.31  
LINK        MG    MG A1491                 O   HOH A2061     1555   1555  2.24  
LINK        MG    MG A1491                 O   HOH A2317     1555   1555  2.49  
LINK        MG    MG A1491                 O   HOH A2062     1555   1555  2.32  
LINK        MG    MG B1491                 O   HOH B2059     1555   1555  2.51  
LINK        MG    MG B1491                 O   HOH B2058     1555   1555  2.68  
LINK        MG    MG B1491                 O   HOH B2292     1555   1555  1.97  
LINK        MG    MG B1491                 O   HOH B2293     1555   1555  2.16  
LINK        MG    MG C1491                 O   HOH C2375     1555   1555  2.37  
LINK        MG    MG C1491                 O   HOH C2374     1555   1555  1.91  
LINK        MG    MG C1491                 O   HOH C2076     1555   1555  2.55  
CISPEP   1 SER A  304    PRO A  305          0        -1.76                     
CISPEP   2 TYR A  395    PRO A  396          0         4.49                     
CISPEP   3 SER B  304    PRO B  305          0        -7.63                     
CISPEP   4 TYR B  395    PRO B  396          0         1.05                     
CISPEP   5 SER C  304    PRO C  305          0        -4.90                     
CISPEP   6 TYR C  395    PRO C  396          0         0.06                     
CISPEP   7 SER D  304    PRO D  305          0        -5.56                     
CISPEP   8 TYR D  395    PRO D  396          0        -2.43                     
SITE     1 AC1  5 GLU B 353  HOH B2058  HOH B2059  HOH B2292                    
SITE     2 AC1  5 HOH B2293                                                     
SITE     1 AC2  6 GLN A  81  GLU A 353  HOH A2061  HOH A2062                    
SITE     2 AC2  6 HOH A2317  HOH A2322                                          
SITE     1 AC3  5 GLN C  81  THR C 349  HOH C2076  HOH C2374                    
SITE     2 AC3  5 HOH C2375                                                     
CRYST1   86.510  126.240  209.750  90.00  90.00  90.00 P 21 21 21   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      0.011559  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007921  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004768        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system