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Database: PDB
Entry: 5MLE
LinkDB: 5MLE
Original site: 5MLE 
HEADER    HYDROLASE                               06-DEC-16   5MLE              
TITLE     CRYSTAL STRUCTURE OF HUMAN DIHYDROPYRIMIDINEASE-LIKE 2 (DPYSL2A)      
TITLE    2 /COLLAPSIN RESPONSE MEDIATOR PROTEIN (CRMP2 13-516) MUTANT           
TITLE    3 Y479E/Y499E                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROPYRIMIDINASE-RELATED PROTEIN 2;                     
COMPND   3 CHAIN: C, A;                                                         
COMPND   4 SYNONYM: DRP-2,COLLAPSIN RESPONSE MEDIATOR PROTEIN 2,CRMP-2,N2A3,UNC-
COMPND   5 33-LIKE PHOSPHOPROTEIN 2,ULIP-2;                                     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DPYSL2, CRMP2, ULIP2;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CRMP2, PHOSPHO-MUTANT, OVARIAN CANCER, MICROTUBULE ASSOCIATED         
KEYWDS   2 PROTEIN, HYDROLASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.SETHI,Y.ZHENG,R.TALON,S.VELUPILLAI,C.H.ARROWSMITH,A.M.EDWARDS,      
AUTHOR   2 C.BOUNTRA,A.A.AHMED,F.VON DELFT                                      
REVDAT   3   16-OCT-19 5MLE    1       REMARK                                   
REVDAT   2   07-MAR-18 5MLE    1       JRNL                                     
REVDAT   1   22-FEB-17 5MLE    0                                                
JRNL        AUTH   Y.ZHENG,R.SETHI,L.S.MANGALA,C.TAYLOR,J.GOLDSMITH,M.WANG,     
JRNL        AUTH 2 K.MASUDA,M.KARAMINEJADRANJBAR,D.MANNION,F.MIRANDA,           
JRNL        AUTH 3 S.HERRERO-GONZALEZ,K.HELLNER,F.CHEN,A.ALSAADI,A.ALBUKHARI,   
JRNL        AUTH 4 D.C.FOTSO,C.YAU,D.JIANG,S.PRADEEP,C.RODRIGUEZ-AGUAYO,        
JRNL        AUTH 5 G.LOPEZ-BERESTEIN,S.KNAPP,N.S.GRAY,L.CAMPO,K.A.MYERS,S.DHAR, 
JRNL        AUTH 6 D.FERGUSON,R.C.BAST,A.K.SOOD,F.VON DELFT,A.A.AHMED           
JRNL        TITL   TUNING MICROTUBULE DYNAMICS TO ENHANCE CANCER THERAPY BY     
JRNL        TITL 2 MODULATING FER-MEDIATED CRMP2 PHOSPHORYLATION.               
JRNL        REF    NAT COMMUN                    V.   9   476 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   29396402                                                     
JRNL        DOI    10.1038/S41467-017-02811-7                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.48 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.48                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 83.98                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 44041                          
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) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2328                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.48                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3214                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3800                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 175                          
REMARK   3   BIN FREE R VALUE                    : 0.4110                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7206                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 63                                      
REMARK   3   SOLVENT ATOMS            : 175                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.04000                                              
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : -0.02000                                             
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): 0.377         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.264         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.278         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.430        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7418 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  6865 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10039 ; 1.667 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 15967 ; 1.042 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   943 ; 6.482 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   321 ;37.580 ;24.984       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1242 ;17.308 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;20.298 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1136 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8244 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1422 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3763 ; 2.392 ; 3.918       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3762 ; 2.369 ; 3.917       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4700 ; 3.792 ; 5.866       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  4701 ; 3.795 ; 5.868       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3655 ; 2.591 ; 4.219       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3655 ; 2.589 ; 4.219       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  5337 ; 4.234 ; 6.187       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  7845 ; 7.871 ;45.812       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  7846 ; 7.871 ;45.820       
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 : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5MLE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-DEC-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200002641.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.920                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46370                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.480                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 83.980                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.2100                             
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: REFMAC                                                
REMARK 200 STARTING MODEL: 2GSE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: (0.2M MAGNESIUM CHLORIDE, 25% PEG 3350   
REMARK 280  AND 0.1M BIS-TRIS BUFFER PH 6.5, VAPOR DIFFUSION, SITTING DROP,     
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       98.15500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       98.15500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       35.45000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       92.91000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       35.45000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       92.91000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       98.15500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       35.45000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       92.91000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       98.15500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       35.45000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       92.91000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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     THR C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     HIS C   145                                                      
REMARK 465     ALA C   484                                                      
REMARK 465     ARG C   485                                                      
REMARK 465     SER C   486                                                      
REMARK 465     ARG C   487                                                      
REMARK 465     LEU C   488                                                      
REMARK 465     ALA C   489                                                      
REMARK 465     GLU C   490                                                      
REMARK 465     LEU C   491                                                      
REMARK 465     ARG C   492                                                      
REMARK 465     GLY C   493                                                      
REMARK 465     VAL C   494                                                      
REMARK 465     PRO C   495                                                      
REMARK 465     ARG C   496                                                      
REMARK 465     GLY C   497                                                      
REMARK 465     LEU C   498                                                      
REMARK 465     GLU C   499                                                      
REMARK 465     ASP C   500                                                      
REMARK 465     GLY C   501                                                      
REMARK 465     PRO C   502                                                      
REMARK 465     VAL C   503                                                      
REMARK 465     CYS C   504                                                      
REMARK 465     GLU C   505                                                      
REMARK 465     VAL C   506                                                      
REMARK 465     SER C   507                                                      
REMARK 465     VAL C   508                                                      
REMARK 465     THR C   509                                                      
REMARK 465     PRO C   510                                                      
REMARK 465     LYS C   511                                                      
REMARK 465     THR C   512                                                      
REMARK 465     VAL C   513                                                      
REMARK 465     THR C   514                                                      
REMARK 465     PRO C   515                                                      
REMARK 465     ALA C   516                                                      
REMARK 465     THR A    13                                                      
REMARK 465     SER A   486                                                      
REMARK 465     ARG A   487                                                      
REMARK 465     LEU A   488                                                      
REMARK 465     ALA A   489                                                      
REMARK 465     GLU A   490                                                      
REMARK 465     LEU A   491                                                      
REMARK 465     ARG A   492                                                      
REMARK 465     GLY A   493                                                      
REMARK 465     VAL A   494                                                      
REMARK 465     PRO A   495                                                      
REMARK 465     ARG A   496                                                      
REMARK 465     GLY A   497                                                      
REMARK 465     LEU A   498                                                      
REMARK 465     GLU A   499                                                      
REMARK 465     ASP A   500                                                      
REMARK 465     GLY A   501                                                      
REMARK 465     PRO A   502                                                      
REMARK 465     VAL A   503                                                      
REMARK 465     CYS A   504                                                      
REMARK 465     GLU A   505                                                      
REMARK 465     VAL A   506                                                      
REMARK 465     SER A   507                                                      
REMARK 465     VAL A   508                                                      
REMARK 465     THR A   509                                                      
REMARK 465     PRO A   510                                                      
REMARK 465     LYS A   511                                                      
REMARK 465     THR A   512                                                      
REMARK 465     VAL A   513                                                      
REMARK 465     THR A   514                                                      
REMARK 465     PRO A   515                                                      
REMARK 465     ALA A   516                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN C  81    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 480    CG   CD   CE   NZ                                   
REMARK 470     GLN A  81    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 146    CG   CD   CE   NZ                                   
REMARK 470     ARG A 485    CG   CD   NE   CZ   NH1  NH2                        
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    LEU A   137     NH2  ARG A   471              2.13            
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    HOH C   796     O    HOH C   796     3555     0.52            
REMARK 500   O    HOH C   803     O    HOH C   803     3555     1.97            
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    ARG A 189   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
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    ASN C  48       74.46     49.66                                   
REMARK 500    PRO C  52     -168.09    -65.28                                   
REMARK 500    ARG C  75       56.33   -143.49                                   
REMARK 500    ASP C  80      118.46   -172.71                                   
REMARK 500    ILE C 148      -35.58    -38.51                                   
REMARK 500    ASN C 162       27.24   -149.98                                   
REMARK 500    PHE C 170       83.65     65.64                                   
REMARK 500    ARG C 173      -78.47   -126.88                                   
REMARK 500    SER C 385      -54.38   -146.19                                   
REMARK 500    ASN C 426       50.06    -94.29                                   
REMARK 500    GLN C 449       25.96     49.25                                   
REMARK 500    ARG C 481       40.72    -91.74                                   
REMARK 500    GLN A  29      162.34    179.66                                   
REMARK 500    ASN A  48       85.13     62.91                                   
REMARK 500    PRO A  52     -174.26    -50.73                                   
REMARK 500    ASP A  80      107.50   -163.03                                   
REMARK 500    ASN A 162       29.51   -140.71                                   
REMARK 500    PHE A 170       69.38     77.90                                   
REMARK 500    CYS A 334       87.46   -153.33                                   
REMARK 500    VAL A 343      -39.73    -35.90                                   
REMARK 500    ASN A 347      104.88   -166.63                                   
REMARK 500    SER A 385      -53.37   -150.05                                   
REMARK 500    ASN A 426       41.63    -98.12                                   
REMARK 500    PHE A 434       31.60    -93.04                                   
REMARK 500    LYS A 483     -118.89   -166.37                                   
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 C 803        DISTANCE =  6.69 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NI C 608                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 607                  
DBREF  5MLE C   13   516  UNP    Q16555   DPYL2_HUMAN     13    516             
DBREF  5MLE A   13   516  UNP    Q16555   DPYL2_HUMAN     13    516             
SEQADV 5MLE GLU C  479  UNP  Q16555    TYR   479 ENGINEERED MUTATION            
SEQADV 5MLE GLU C  499  UNP  Q16555    TYR   499 ENGINEERED MUTATION            
SEQADV 5MLE GLU A  479  UNP  Q16555    TYR   479 ENGINEERED MUTATION            
SEQADV 5MLE GLU A  499  UNP  Q16555    TYR   499 ENGINEERED MUTATION            
SEQRES   1 C  504  THR SER ASP ARG LEU LEU ILE LYS GLY GLY LYS ILE VAL          
SEQRES   2 C  504  ASN ASP ASP GLN SER PHE TYR ALA ASP ILE TYR MET GLU          
SEQRES   3 C  504  ASP GLY LEU ILE LYS GLN ILE GLY GLU ASN LEU ILE VAL          
SEQRES   4 C  504  PRO GLY GLY VAL LYS THR ILE GLU ALA HIS SER ARG MET          
SEQRES   5 C  504  VAL ILE PRO GLY GLY ILE ASP VAL HIS THR ARG PHE GLN          
SEQRES   6 C  504  MET PRO ASP GLN GLY MET THR SER ALA ASP ASP PHE PHE          
SEQRES   7 C  504  GLN GLY THR LYS ALA ALA LEU ALA GLY GLY THR THR MET          
SEQRES   8 C  504  ILE ILE ASP HIS VAL VAL PRO GLU PRO GLY THR SER LEU          
SEQRES   9 C  504  LEU ALA ALA PHE ASP GLN TRP ARG GLU TRP ALA ASP SER          
SEQRES  10 C  504  LYS SER CYS CYS ASP TYR SER LEU HIS VAL ASP ILE SER          
SEQRES  11 C  504  GLU TRP HIS LYS GLY ILE GLN GLU GLU MET GLU ALA LEU          
SEQRES  12 C  504  VAL LYS ASP HIS GLY VAL ASN SER PHE LEU VAL TYR MET          
SEQRES  13 C  504  ALA PHE LYS ASP ARG PHE GLN LEU THR ASP CYS GLN ILE          
SEQRES  14 C  504  TYR GLU VAL LEU SER VAL ILE ARG ASP ILE GLY ALA ILE          
SEQRES  15 C  504  ALA GLN VAL HIS ALA GLU ASN GLY ASP ILE ILE ALA GLU          
SEQRES  16 C  504  GLU GLN GLN ARG ILE LEU ASP LEU GLY ILE THR GLY PRO          
SEQRES  17 C  504  GLU GLY HIS VAL LEU SER ARG PRO GLU GLU VAL GLU ALA          
SEQRES  18 C  504  GLU ALA VAL ASN ARG ALA ILE THR ILE ALA ASN GLN THR          
SEQRES  19 C  504  ASN CYS PRO LEU TYR ILE THR LYS VAL MET SER LYS SER          
SEQRES  20 C  504  SER ALA GLU VAL ILE ALA GLN ALA ARG LYS LYS GLY THR          
SEQRES  21 C  504  VAL VAL TYR GLY GLU PRO ILE THR ALA SER LEU GLY THR          
SEQRES  22 C  504  ASP GLY SER HIS TYR TRP SER LYS ASN TRP ALA LYS ALA          
SEQRES  23 C  504  ALA ALA PHE VAL THR SER PRO PRO LEU SER PRO ASP PRO          
SEQRES  24 C  504  THR THR PRO ASP PHE LEU ASN SER LEU LEU SER CYS GLY          
SEQRES  25 C  504  ASP LEU GLN VAL THR GLY SER ALA HIS CYS THR PHE ASN          
SEQRES  26 C  504  THR ALA GLN LYS ALA VAL GLY LYS ASP ASN PHE THR LEU          
SEQRES  27 C  504  ILE PRO GLU GLY THR ASN GLY THR GLU GLU ARG MET SER          
SEQRES  28 C  504  VAL ILE TRP ASP LYS ALA VAL VAL THR GLY LYS MET ASP          
SEQRES  29 C  504  GLU ASN GLN PHE VAL ALA VAL THR SER THR ASN ALA ALA          
SEQRES  30 C  504  LYS VAL PHE ASN LEU TYR PRO ARG LYS GLY ARG ILE ALA          
SEQRES  31 C  504  VAL GLY SER ASP ALA ASP LEU VAL ILE TRP ASP PRO ASP          
SEQRES  32 C  504  SER VAL LYS THR ILE SER ALA LYS THR HIS ASN SER SER          
SEQRES  33 C  504  LEU GLU TYR ASN ILE PHE GLU GLY MET GLU CYS ARG GLY          
SEQRES  34 C  504  SER PRO LEU VAL VAL ILE SER GLN GLY LYS ILE VAL LEU          
SEQRES  35 C  504  GLU ASP GLY THR LEU HIS VAL THR GLU GLY SER GLY ARG          
SEQRES  36 C  504  TYR ILE PRO ARG LYS PRO PHE PRO ASP PHE VAL GLU LYS          
SEQRES  37 C  504  ARG ILE LYS ALA ARG SER ARG LEU ALA GLU LEU ARG GLY          
SEQRES  38 C  504  VAL PRO ARG GLY LEU GLU ASP GLY PRO VAL CYS GLU VAL          
SEQRES  39 C  504  SER VAL THR PRO LYS THR VAL THR PRO ALA                      
SEQRES   1 A  504  THR SER ASP ARG LEU LEU ILE LYS GLY GLY LYS ILE VAL          
SEQRES   2 A  504  ASN ASP ASP GLN SER PHE TYR ALA ASP ILE TYR MET GLU          
SEQRES   3 A  504  ASP GLY LEU ILE LYS GLN ILE GLY GLU ASN LEU ILE VAL          
SEQRES   4 A  504  PRO GLY GLY VAL LYS THR ILE GLU ALA HIS SER ARG MET          
SEQRES   5 A  504  VAL ILE PRO GLY GLY ILE ASP VAL HIS THR ARG PHE GLN          
SEQRES   6 A  504  MET PRO ASP GLN GLY MET THR SER ALA ASP ASP PHE PHE          
SEQRES   7 A  504  GLN GLY THR LYS ALA ALA LEU ALA GLY GLY THR THR MET          
SEQRES   8 A  504  ILE ILE ASP HIS VAL VAL PRO GLU PRO GLY THR SER LEU          
SEQRES   9 A  504  LEU ALA ALA PHE ASP GLN TRP ARG GLU TRP ALA ASP SER          
SEQRES  10 A  504  LYS SER CYS CYS ASP TYR SER LEU HIS VAL ASP ILE SER          
SEQRES  11 A  504  GLU TRP HIS LYS GLY ILE GLN GLU GLU MET GLU ALA LEU          
SEQRES  12 A  504  VAL LYS ASP HIS GLY VAL ASN SER PHE LEU VAL TYR MET          
SEQRES  13 A  504  ALA PHE LYS ASP ARG PHE GLN LEU THR ASP CYS GLN ILE          
SEQRES  14 A  504  TYR GLU VAL LEU SER VAL ILE ARG ASP ILE GLY ALA ILE          
SEQRES  15 A  504  ALA GLN VAL HIS ALA GLU ASN GLY ASP ILE ILE ALA GLU          
SEQRES  16 A  504  GLU GLN GLN ARG ILE LEU ASP LEU GLY ILE THR GLY PRO          
SEQRES  17 A  504  GLU GLY HIS VAL LEU SER ARG PRO GLU GLU VAL GLU ALA          
SEQRES  18 A  504  GLU ALA VAL ASN ARG ALA ILE THR ILE ALA ASN GLN THR          
SEQRES  19 A  504  ASN CYS PRO LEU TYR ILE THR LYS VAL MET SER LYS SER          
SEQRES  20 A  504  SER ALA GLU VAL ILE ALA GLN ALA ARG LYS LYS GLY THR          
SEQRES  21 A  504  VAL VAL TYR GLY GLU PRO ILE THR ALA SER LEU GLY THR          
SEQRES  22 A  504  ASP GLY SER HIS TYR TRP SER LYS ASN TRP ALA LYS ALA          
SEQRES  23 A  504  ALA ALA PHE VAL THR SER PRO PRO LEU SER PRO ASP PRO          
SEQRES  24 A  504  THR THR PRO ASP PHE LEU ASN SER LEU LEU SER CYS GLY          
SEQRES  25 A  504  ASP LEU GLN VAL THR GLY SER ALA HIS CYS THR PHE ASN          
SEQRES  26 A  504  THR ALA GLN LYS ALA VAL GLY LYS ASP ASN PHE THR LEU          
SEQRES  27 A  504  ILE PRO GLU GLY THR ASN GLY THR GLU GLU ARG MET SER          
SEQRES  28 A  504  VAL ILE TRP ASP LYS ALA VAL VAL THR GLY LYS MET ASP          
SEQRES  29 A  504  GLU ASN GLN PHE VAL ALA VAL THR SER THR ASN ALA ALA          
SEQRES  30 A  504  LYS VAL PHE ASN LEU TYR PRO ARG LYS GLY ARG ILE ALA          
SEQRES  31 A  504  VAL GLY SER ASP ALA ASP LEU VAL ILE TRP ASP PRO ASP          
SEQRES  32 A  504  SER VAL LYS THR ILE SER ALA LYS THR HIS ASN SER SER          
SEQRES  33 A  504  LEU GLU TYR ASN ILE PHE GLU GLY MET GLU CYS ARG GLY          
SEQRES  34 A  504  SER PRO LEU VAL VAL ILE SER GLN GLY LYS ILE VAL LEU          
SEQRES  35 A  504  GLU ASP GLY THR LEU HIS VAL THR GLU GLY SER GLY ARG          
SEQRES  36 A  504  TYR ILE PRO ARG LYS PRO PHE PRO ASP PHE VAL GLU LYS          
SEQRES  37 A  504  ARG ILE LYS ALA ARG SER ARG LEU ALA GLU LEU ARG GLY          
SEQRES  38 A  504  VAL PRO ARG GLY LEU GLU ASP GLY PRO VAL CYS GLU VAL          
SEQRES  39 A  504  SER VAL THR PRO LYS THR VAL THR PRO ALA                      
HET    PEG  C 601       7                                                       
HET    EDO  C 602       4                                                       
HET    EDO  C 603       4                                                       
HET    EDO  C 604       4                                                       
HET    EDO  C 605       4                                                       
HET    EDO  C 606       4                                                       
HET    EDO  C 607       4                                                       
HET     NI  C 608       1                                                       
HET    PEG  A 601       7                                                       
HET    PEG  A 602       7                                                       
HET    EDO  A 603       4                                                       
HET    EDO  A 604       4                                                       
HET    EDO  A 605       4                                                       
HET    EDO  A 606       4                                                       
HET     NI  A 607       1                                                       
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      NI NICKEL (II) ION                                                  
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  PEG    3(C4 H10 O3)                                                 
FORMUL   4  EDO    10(C2 H6 O2)                                                 
FORMUL  10   NI    2(NI 2+)                                                     
FORMUL  18  HOH   *175(H2 O)                                                    
HELIX    1 AA1 ASP C   88  GLY C   99  1                                  12    
HELIX    2 AA2 SER C  115  SER C  129  1                                  15    
HELIX    3 AA3 GLY C  147  HIS C  159  1                                  13    
HELIX    4 AA4 THR C  177  GLY C  192  1                                  16    
HELIX    5 AA5 ASN C  201  LEU C  215  1                                  15    
HELIX    6 AA6 PRO C  220  SER C  226  1                                   7    
HELIX    7 AA7 PRO C  228  ASN C  247  1                                  20    
HELIX    8 AA8 SER C  257  LYS C  270  1                                  14    
HELIX    9 AA9 ILE C  279  THR C  285  1                                   7    
HELIX   10 AB1 ASP C  286  SER C  292  5                                   7    
HELIX   11 AB2 ASN C  294  PHE C  301  1                                   8    
HELIX   12 AB3 THR C  312  CYS C  323  1                                  12    
HELIX   13 AB4 ASN C  337  ALA C  342  1                                   6    
HELIX   14 AB5 VAL C  343  LYS C  345  5                                   3    
HELIX   15 AB6 ASN C  347  ILE C  351  5                                   5    
HELIX   16 AB7 GLU C  360  VAL C  370  1                                  11    
HELIX   17 AB8 ASP C  376  SER C  385  1                                  10    
HELIX   18 AB9 SER C  385  PHE C  392  1                                   8    
HELIX   19 AC1 PRO C  475  ARG C  481  1                                   7    
HELIX   20 AC2 ASP A   88  GLY A   99  1                                  12    
HELIX   21 AC3 SER A  115  SER A  131  1                                  17    
HELIX   22 AC4 GLY A  147  HIS A  159  1                                  13    
HELIX   23 AC5 THR A  177  GLY A  192  1                                  16    
HELIX   24 AC6 ASN A  201  ASP A  214  1                                  14    
HELIX   25 AC7 GLY A  219  SER A  226  1                                   8    
HELIX   26 AC8 PRO A  228  ASN A  247  1                                  20    
HELIX   27 AC9 SER A  257  LYS A  270  1                                  14    
HELIX   28 AD1 ILE A  279  THR A  285  1                                   7    
HELIX   29 AD2 ASP A  286  SER A  292  5                                   7    
HELIX   30 AD3 ASN A  294  PHE A  301  1                                   8    
HELIX   31 AD4 THR A  312  CYS A  323  1                                  12    
HELIX   32 AD5 ASN A  337  VAL A  343  1                                   7    
HELIX   33 AD6 ASN A  347  ILE A  351  5                                   5    
HELIX   34 AD7 GLU A  360  VAL A  370  1                                  11    
HELIX   35 AD8 ASP A  376  SER A  385  1                                  10    
HELIX   36 AD9 SER A  385  PHE A  392  1                                   8    
HELIX   37 AE1 PRO A  475  LYS A  480  1                                   6    
SHEET    1 AA1 4 LEU C  41  GLY C  46  0                                        
SHEET    2 AA1 4 SER C  30  GLU C  38 -1  N  ASP C  34   O  GLY C  46           
SHEET    3 AA1 4 LEU C  17  VAL C  25 -1  N  ILE C  19   O  ILE C  35           
SHEET    4 AA1 4 LYS C  56  GLU C  59  1  O  ILE C  58   N  LEU C  18           
SHEET    1 AA2 8 LEU C  41  GLY C  46  0                                        
SHEET    2 AA2 8 SER C  30  GLU C  38 -1  N  ASP C  34   O  GLY C  46           
SHEET    3 AA2 8 LEU C  17  VAL C  25 -1  N  ILE C  19   O  ILE C  35           
SHEET    4 AA2 8 MET C  64  PRO C  67  1  O  VAL C  65   N  LYS C  23           
SHEET    5 AA2 8 LEU C 409  THR C 419 -1  O  VAL C 410   N  ILE C  66           
SHEET    6 AA2 8 GLU C 438  SER C 448 -1  O  SER C 442   N  ASP C 413           
SHEET    7 AA2 8 LYS C 451  GLU C 455 -1  O  LYS C 451   N  SER C 448           
SHEET    8 AA2 8 THR C 458  LEU C 459 -1  O  THR C 458   N  GLU C 455           
SHEET    1 AA3 7 GLY C  69  THR C  74  0                                        
SHEET    2 AA3 7 THR C 101  VAL C 108  1  O  MET C 103   N  ASP C  71           
SHEET    3 AA3 7 ASP C 134  ASP C 140  1  O  HIS C 138   N  VAL C 108           
SHEET    4 AA3 7 SER C 163  TYR C 167  1  O  LEU C 165   N  VAL C 139           
SHEET    5 AA3 7 ILE C 194  HIS C 198  1  O  GLN C 196   N  PHE C 164           
SHEET    6 AA3 7 LEU C 250  VAL C 255  1  O  TYR C 251   N  ALA C 195           
SHEET    7 AA3 7 VAL C 274  PRO C 278  1  O  GLU C 277   N  VAL C 255           
SHEET    1 AA4 2 PRO C  79  ASP C  80  0                                        
SHEET    2 AA4 2 MET C  83  THR C  84 -1  O  MET C  83   N  ASP C  80           
SHEET    1 AA5 4 LEU A  41  GLY A  46  0                                        
SHEET    2 AA5 4 SER A  30  GLU A  38 -1  N  ASP A  34   O  GLY A  46           
SHEET    3 AA5 4 LEU A  17  VAL A  25 -1  N  LEU A  17   O  MET A  37           
SHEET    4 AA5 4 THR A  57  GLU A  59  1  O  ILE A  58   N  LEU A  18           
SHEET    1 AA6 8 LEU A  41  GLY A  46  0                                        
SHEET    2 AA6 8 SER A  30  GLU A  38 -1  N  ASP A  34   O  GLY A  46           
SHEET    3 AA6 8 LEU A  17  VAL A  25 -1  N  LEU A  17   O  MET A  37           
SHEET    4 AA6 8 MET A  64  PRO A  67  1  O  VAL A  65   N  LYS A  23           
SHEET    5 AA6 8 LEU A 409  THR A 419 -1  O  VAL A 410   N  ILE A  66           
SHEET    6 AA6 8 GLU A 438  SER A 448 -1  O  LEU A 444   N  ILE A 411           
SHEET    7 AA6 8 LYS A 451  GLU A 455 -1  O  VAL A 453   N  VAL A 446           
SHEET    8 AA6 8 THR A 458  LEU A 459 -1  O  THR A 458   N  GLU A 455           
SHEET    1 AA7 7 GLY A  69  THR A  74  0                                        
SHEET    2 AA7 7 THR A 101  VAL A 108  1  O  MET A 103   N  ASP A  71           
SHEET    3 AA7 7 ASP A 134  ASP A 140  1  O  HIS A 138   N  ASP A 106           
SHEET    4 AA7 7 SER A 163  TYR A 167  1  O  LEU A 165   N  VAL A 139           
SHEET    5 AA7 7 ILE A 194  HIS A 198  1  O  GLN A 196   N  PHE A 164           
SHEET    6 AA7 7 LEU A 250  VAL A 255  1  O  TYR A 251   N  VAL A 197           
SHEET    7 AA7 7 VAL A 274  PRO A 278  1  O  TYR A 275   N  ILE A 252           
SHEET    1 AA8 2 PRO A  79  ASP A  80  0                                        
SHEET    2 AA8 2 MET A  83  THR A  84 -1  O  MET A  83   N  ASP A  80           
CISPEP   1 SER C  304    PRO C  305          0         1.90                     
CISPEP   2 TYR C  395    PRO C  396          0        -3.31                     
CISPEP   3 SER A  304    PRO A  305          0        -4.14                     
CISPEP   4 TYR A  395    PRO A  396          0         0.12                     
SITE     1 AC1  6 SER C 142  ASP C 172  ARG C 173  PHE C 174                    
SITE     2 AC1  6 GLN C 175  HOH C 790                                          
SITE     1 AC2  8 PRO C  67  GLY C  68  ARG C 397  LYS C 398                    
SITE     2 AC2  8 GLY C 399  ARG C 400  ASP C 406  ASP C 408                    
SITE     1 AC3  2 GLU C 221  HOH C 770                                          
SITE     1 AC4  3 ASN C 244  ASN C 247  GLY C 271                               
SITE     1 AC5  4 LYS C 297  TYR C 431  ASN C 432  GLU C 435                    
SITE     1 AC6  7 ARG C  75  PHE C  76  MET C  78  ASP C 106                    
SITE     2 AC6  7 HIS C 107  VAL C 109  TRP C 123                               
SITE     1 AC7  7 MET C 256  SER C 282  THR C 285  LEU C 307                    
SITE     2 AC7  7 SER C 308  THR C 313  PRO C 314                               
SITE     1 AC8  6 VAL C  72  HIS C  73  HIS C 107  HIS C 138                    
SITE     2 AC8  6 GLN C 196  GLU C 277                                          
SITE     1 AC9  6 PHE A 170  LYS A 171  GLN A 209  ARG A 227                    
SITE     2 AC9  6 GLU A 353  EDO A 606                                          
SITE     1 AD1  9 GLY A  40  THR A 102  ASP A 134  LYS A 398                    
SITE     2 AD1  9 ASP A 406  ASP A 408  SER A 448  GLN A 449                    
SITE     3 AD1  9 ARG A 467                                                     
SITE     1 AD2  3 SER A 416  VAL A 417  LYS A 418                               
SITE     1 AD3  4 ASN A 244  ASN A 247  GLY A 271  ARG A 485                    
SITE     1 AD4  3 ASN A 426  GLU C 455  HOH C 785                               
SITE     1 AD5  7 GLN A 209  HIS A 223  ARG A 227  PHE A 348                    
SITE     2 AD5  7 THR A 349  GLU A 353  PEG A 601                               
SITE     1 AD6  6 VAL A  72  HIS A  73  HIS A 107  HIS A 138                    
SITE     2 AD6  6 GLN A 196  GLU A 277                                          
CRYST1   70.900  185.820  196.310  90.00  90.00  90.00 C 2 2 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      0.014104  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005382  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005094        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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