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Database: PDB
Entry: 5YZA
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Original site: 5YZA 
HEADER    CYTOSOLIC PROTEIN                       13-DEC-17   5YZA              
TITLE     CRYSTAL STRUCTURE OF HUMAN CRMP-2 WITH S522D MUTATION                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROPYRIMIDINASE-RELATED PROTEIN 2;                     
COMPND   3 CHAIN: 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 BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    DEVELOPMENTAL PROTEIN, PHOSPHOP ASSOCIATED PROTEINS, NEUROGENESI      
KEYWDS   2 RELATED PROTEIN, COLLAPSIN RESPONSE, PROTEIN BINDING, CYTOSOLIC      
KEYWDS   3 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.SUMI,T.IMASAKI,M.AOKI,N.SAKAI,E.NITTA,M.SHIROUZU,R.NITTA            
REVDAT   1   21-MAR-18 5YZA    0                                                
JRNL        AUTH   T.SUMI,T.IMASAKI,M.AOKI,N.SAKAI,E.NITTA,M.SHIROUZU,R.NITTA   
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE ALTERING FUNCTION OF CRMP2 BY   
JRNL        TITL 2 PHOSPHORYLATION.                                             
JRNL        REF    CELL STRUCT. FUNCT.           V.  43    15 2018              
JRNL        REFN                   ISSN 1347-3700                               
JRNL        PMID   29479005                                                     
JRNL        DOI    10.1247/CSF.17025                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.12_2829: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.84                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 28103                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2654                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 39.8473 -  6.1254    1.00     2669   147  0.1421 0.1587        
REMARK   3     2  6.1254 -  4.8647    1.00     2686   138  0.1738 0.1961        
REMARK   3     3  4.8647 -  4.2505    1.00     2678   145  0.1429 0.1508        
REMARK   3     4  4.2505 -  3.8623    1.00     2659   138  0.1604 0.2445        
REMARK   3     5  3.8623 -  3.5856    1.00     2666   141  0.1844 0.2686        
REMARK   3     6  3.5856 -  3.3743    1.00     2686   140  0.2083 0.2561        
REMARK   3     7  3.3743 -  3.2054    1.00     2666   138  0.2164 0.2865        
REMARK   3     8  3.2054 -  3.0659    1.00     2642   138  0.2226 0.2541        
REMARK   3     9  3.0659 -  2.9480    1.00     2687   139  0.2017 0.2444        
REMARK   3    10  2.9480 -  2.8463    1.00     2670   143  0.2079 0.2233        
REMARK   3    11  2.8463 -  2.7573    1.00     2662   138  0.2152 0.3012        
REMARK   3    12  2.7573 -  2.6785    1.00     2660   139  0.2341 0.2774        
REMARK   3    13  2.6785 -  2.6080    0.99     2652   138  0.2455 0.3029        
REMARK   3    14  2.6080 -  2.5444    1.00     2675   143  0.2418 0.3041        
REMARK   3    15  2.5444 -  2.4865    1.00     2653   139  0.2397 0.3040        
REMARK   3    16  2.4865 -  2.4336    0.99     2676   139  0.2546 0.3664        
REMARK   3    17  2.4336 -  2.3849    0.99     2624   138  0.2670 0.2758        
REMARK   3    18  2.3849 -  2.3399    0.99     2643   139  0.2656 0.3649        
REMARK   3    19  2.3399 -  2.2982    0.96     2597   134  0.2688 0.3452        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.340           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           3875                                  
REMARK   3   ANGLE     :  0.862           5259                                  
REMARK   3   CHIRALITY :  0.052            591                                  
REMARK   3   PLANARITY :  0.006            687                                  
REMARK   3   DIHEDRAL  :  5.242           3212                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE STRUCTURE FACTOR FILE CONTAINS        
REMARK   3  FRIEDEL PAIRS IN I_PLUS/MINUS COLUMNS                               
REMARK   4                                                                      
REMARK   4 5YZA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300006149.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUL-14                          
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               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL26B2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225-HS                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28103                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.700                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 4000, 0.1M SODIUM CITRATE PH     
REMARK 280  5.6, 0.1M LITHIUM SULFATE, VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
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       56.21000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       56.21000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       97.98200            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       56.21000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       48.99100            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       56.21000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      146.97300            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       56.21000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      146.97300            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.21000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       48.99100            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       56.21000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       56.21000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       97.98200            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       56.21000            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       56.21000            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       97.98200            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       56.21000            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      146.97300            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       56.21000            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       48.99100            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       56.21000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       48.99100            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       56.21000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      146.97300            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       56.21000            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       56.21000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       97.98200            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14120 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 63460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000      112.42000            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      112.42000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000      112.42000            
REMARK 350   BIOMT2   3  0.000000 -1.000000  0.000000      112.42000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 665  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 667  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     TYR A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     ASN A     8                                                      
REMARK 465     ILE A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     ARG A    11                                                      
REMARK 465     ILE A    12                                                      
REMARK 465     THR A    13                                                      
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 465     SER A   517                                                      
REMARK 465     SER A   518                                                      
REMARK 465     ALA A   519                                                      
REMARK 465     LYS A   520                                                      
REMARK 465     THR A   521                                                      
REMARK 465     ASP A   522                                                      
REMARK 465     PRO A   523                                                      
REMARK 465     ALA A   524                                                      
REMARK 465     LYS A   525                                                      
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   OE2  GLU A   230     O    HOH A   601              1.95            
REMARK 500   O    LYS A   146     O    HOH A   602              2.09            
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   OE1  GLU A   221     NH2  ARG A   496    10665     2.10            
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     -147.99   -138.07                                   
REMARK 500    ASN A  48       55.82     39.79                                   
REMARK 500    GLN A  77       45.76     36.97                                   
REMARK 500    HIS A 145     -159.25   -160.07                                   
REMARK 500    ALA A 169     -165.14   -110.22                                   
REMARK 500    ARG A 173      -68.39   -120.14                                   
REMARK 500    ASP A 214       -9.52    -59.40                                   
REMARK 500    CYS A 334       81.72   -154.17                                   
REMARK 500    ASN A 347      105.26   -163.81                                   
REMARK 500    SER A 385      -48.37   -148.08                                   
REMARK 500    ASN A 426       39.89    -75.83                                   
REMARK 500    GLU A 455      134.15   -170.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP A   15     ARG A   16                 -147.70                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5YZA A    1   525  UNP    Q16555   DPYL2_HUMAN      1    525             
SEQADV 5YZA ASP A  522  UNP  Q16555    SER   522 ENGINEERED MUTATION            
SEQRES   1 A  525  MET SER TYR GLN GLY LYS LYS ASN ILE PRO ARG ILE THR          
SEQRES   2 A  525  SER ASP ARG LEU LEU ILE LYS GLY GLY LYS ILE VAL ASN          
SEQRES   3 A  525  ASP ASP GLN SER PHE TYR ALA ASP ILE TYR MET GLU ASP          
SEQRES   4 A  525  GLY LEU ILE LYS GLN ILE GLY GLU ASN LEU ILE VAL PRO          
SEQRES   5 A  525  GLY GLY VAL LYS THR ILE GLU ALA HIS SER ARG MET VAL          
SEQRES   6 A  525  ILE PRO GLY GLY ILE ASP VAL HIS THR ARG PHE GLN MET          
SEQRES   7 A  525  PRO ASP GLN GLY MET THR SER ALA ASP ASP PHE PHE GLN          
SEQRES   8 A  525  GLY THR LYS ALA ALA LEU ALA GLY GLY THR THR MET ILE          
SEQRES   9 A  525  ILE ASP HIS VAL VAL PRO GLU PRO GLY THR SER LEU LEU          
SEQRES  10 A  525  ALA ALA PHE ASP GLN TRP ARG GLU TRP ALA ASP SER LYS          
SEQRES  11 A  525  SER CYS CYS ASP TYR SER LEU HIS VAL ASP ILE SER GLU          
SEQRES  12 A  525  TRP HIS LYS GLY ILE GLN GLU GLU MET GLU ALA LEU VAL          
SEQRES  13 A  525  LYS ASP HIS GLY VAL ASN SER PHE LEU VAL TYR MET ALA          
SEQRES  14 A  525  PHE LYS ASP ARG PHE GLN LEU THR ASP CYS GLN ILE TYR          
SEQRES  15 A  525  GLU VAL LEU SER VAL ILE ARG ASP ILE GLY ALA ILE ALA          
SEQRES  16 A  525  GLN VAL HIS ALA GLU ASN GLY ASP ILE ILE ALA GLU GLU          
SEQRES  17 A  525  GLN GLN ARG ILE LEU ASP LEU GLY ILE THR GLY PRO GLU          
SEQRES  18 A  525  GLY HIS VAL LEU SER ARG PRO GLU GLU VAL GLU ALA GLU          
SEQRES  19 A  525  ALA VAL ASN ARG ALA ILE THR ILE ALA ASN GLN THR ASN          
SEQRES  20 A  525  CYS PRO LEU TYR ILE THR LYS VAL MET SER LYS SER SER          
SEQRES  21 A  525  ALA GLU VAL ILE ALA GLN ALA ARG LYS LYS GLY THR VAL          
SEQRES  22 A  525  VAL TYR GLY GLU PRO ILE THR ALA SER LEU GLY THR ASP          
SEQRES  23 A  525  GLY SER HIS TYR TRP SER LYS ASN TRP ALA LYS ALA ALA          
SEQRES  24 A  525  ALA PHE VAL THR SER PRO PRO LEU SER PRO ASP PRO THR          
SEQRES  25 A  525  THR PRO ASP PHE LEU ASN SER LEU LEU SER CYS GLY ASP          
SEQRES  26 A  525  LEU GLN VAL THR GLY SER ALA HIS CYS THR PHE ASN THR          
SEQRES  27 A  525  ALA GLN LYS ALA VAL GLY LYS ASP ASN PHE THR LEU ILE          
SEQRES  28 A  525  PRO GLU GLY THR ASN GLY THR GLU GLU ARG MET SER VAL          
SEQRES  29 A  525  ILE TRP ASP LYS ALA VAL VAL THR GLY LYS MET ASP GLU          
SEQRES  30 A  525  ASN GLN PHE VAL ALA VAL THR SER THR ASN ALA ALA LYS          
SEQRES  31 A  525  VAL PHE ASN LEU TYR PRO ARG LYS GLY ARG ILE ALA VAL          
SEQRES  32 A  525  GLY SER ASP ALA ASP LEU VAL ILE TRP ASP PRO ASP SER          
SEQRES  33 A  525  VAL LYS THR ILE SER ALA LYS THR HIS ASN SER SER LEU          
SEQRES  34 A  525  GLU TYR ASN ILE PHE GLU GLY MET GLU CYS ARG GLY SER          
SEQRES  35 A  525  PRO LEU VAL VAL ILE SER GLN GLY LYS ILE VAL LEU GLU          
SEQRES  36 A  525  ASP GLY THR LEU HIS VAL THR GLU GLY SER GLY ARG TYR          
SEQRES  37 A  525  ILE PRO ARG LYS PRO PHE PRO ASP PHE VAL TYR LYS ARG          
SEQRES  38 A  525  ILE LYS ALA ARG SER ARG LEU ALA GLU LEU ARG GLY VAL          
SEQRES  39 A  525  PRO ARG GLY LEU TYR ASP GLY PRO VAL CYS GLU VAL SER          
SEQRES  40 A  525  VAL THR PRO LYS THR VAL THR PRO ALA SER SER ALA LYS          
SEQRES  41 A  525  THR ASP PRO ALA LYS                                          
FORMUL   2  HOH   *83(H2 O)                                                     
HELIX    1 AA1 ASP A   88  GLY A   99  1                                  12    
HELIX    2 AA2 SER A  115  SER A  131  1                                  17    
HELIX    3 AA3 GLY A  147  GLY A  160  1                                  14    
HELIX    4 AA4 THR A  177  ILE A  191  1                                  15    
HELIX    5 AA5 ASN A  201  ASP A  214  1                                  14    
HELIX    6 AA6 GLY A  219  SER A  226  1                                   8    
HELIX    7 AA7 PRO A  228  ASN A  247  1                                  20    
HELIX    8 AA8 SER A  257  GLY A  271  1                                  15    
HELIX    9 AA9 ILE A  279  THR A  285  1                                   7    
HELIX   10 AB1 ASP A  286  SER A  292  5                                   7    
HELIX   11 AB2 ASN A  294  PHE A  301  1                                   8    
HELIX   12 AB3 THR A  312  CYS A  323  1                                  12    
HELIX   13 AB4 ASN A  337  ALA A  342  1                                   6    
HELIX   14 AB5 VAL A  343  LYS A  345  5                                   3    
HELIX   15 AB6 ASN A  347  ILE A  351  5                                   5    
HELIX   16 AB7 GLU A  360  VAL A  370  1                                  11    
HELIX   17 AB8 ASP A  376  SER A  385  1                                  10    
HELIX   18 AB9 SER A  385  PHE A  392  1                                   8    
HELIX   19 AC1 PRO A  475  LEU A  488  1                                  14    
SHEET    1 AA1 4 LEU A  41  GLY A  46  0                                        
SHEET    2 AA1 4 SER A  30  GLU A  38 -1  N  ASP A  34   O  GLY A  46           
SHEET    3 AA1 4 LEU A  17  VAL A  25 -1  N  LEU A  17   O  MET A  37           
SHEET    4 AA1 4 LYS A  56  GLU A  59  1  O  ILE A  58   N  LYS A  20           
SHEET    1 AA2 8 LEU A  41  GLY A  46  0                                        
SHEET    2 AA2 8 SER A  30  GLU A  38 -1  N  ASP A  34   O  GLY A  46           
SHEET    3 AA2 8 LEU A  17  VAL A  25 -1  N  LEU A  17   O  MET A  37           
SHEET    4 AA2 8 MET A  64  PRO A  67  1  O  VAL A  65   N  LYS A  23           
SHEET    5 AA2 8 LEU A 409  THR A 419 -1  O  VAL A 410   N  ILE A  66           
SHEET    6 AA2 8 GLU A 438  SER A 448 -1  O  SER A 442   N  ASP A 413           
SHEET    7 AA2 8 LYS A 451  GLU A 455 -1  O  LYS A 451   N  SER A 448           
SHEET    8 AA2 8 THR A 458  LEU A 459 -1  O  THR A 458   N  GLU A 455           
SHEET    1 AA3 7 GLY A  69  THR A  74  0                                        
SHEET    2 AA3 7 THR A 101  VAL A 108  1  O  MET A 103   N  ASP A  71           
SHEET    3 AA3 7 ASP A 134  ASP A 140  1  O  HIS A 138   N  ASP A 106           
SHEET    4 AA3 7 SER A 163  TYR A 167  1  O  SER A 163   N  VAL A 139           
SHEET    5 AA3 7 ILE A 194  HIS A 198  1  O  GLN A 196   N  PHE A 164           
SHEET    6 AA3 7 LEU A 250  VAL A 255  1  O  TYR A 251   N  VAL A 197           
SHEET    7 AA3 7 VAL A 274  PRO A 278  1  O  TYR A 275   N  ILE A 252           
SHEET    1 AA4 2 PRO A  79  ASP A  80  0                                        
SHEET    2 AA4 2 MET A  83  THR A  84 -1  O  MET A  83   N  ASP A  80           
CISPEP   1 SER A  304    PRO A  305          0        -5.16                     
CISPEP   2 TYR A  395    PRO A  396          0         7.51                     
CRYST1  112.420  112.420  195.964  90.00  90.00  90.00 I 41 2 2     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      0.008895  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008895  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005103        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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