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Database: PDB
Entry: 5X1C
LinkDB: 5X1C
Original site: 5X1C 
HEADER    PROTEIN BINDING                         25-JAN-17   5X1C              
TITLE     CRYSTAL STRUCTURE OF HUMAN CRMP-2 WITHOUT C-TERMINAL TAIL             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROPYRIMIDINASE-RELATED PROTEIN 2;                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 13-490;                                       
COMPND   5 SYNONYM: DRP-2,COLLAPSIN RESPONSE MEDIATOR PROTEIN 2,CRMP-2,N2A3,UNC-
COMPND   6 33-LIKE PHOSPHOPROTEIN 2,ULIP-2;                                     
COMPND   7 ENGINEERED: 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;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    DEVELOPMENTAL PROTEIN, PHOSPHOPROTEIN, MICROTUBULE ASSOCIATED         
KEYWDS   2 PROTEINS, NEUROGENESIS, DIHYDROPYRIMIDASE-RELATED PROTEIN, COLLAPSIN 
KEYWDS   3 RESPONSE MEDIATOR PROTEIN, PROTEIN BINDING                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.NITTA,Y.TOMABECHI,M.AOKI,M.SHIROUZU                                 
REVDAT   2   27-SEP-17 5X1C    1       REMARK                                   
REVDAT   1   20-SEP-17 5X1C    0                                                
JRNL        AUTH   S.NIWA,F.NAKAMURA,Y.TOMABECHI,M.AOKI,H.SHIGEMATSU,           
JRNL        AUTH 2 T.MATSUMOTO,A.YAMAGATA,S.FUKAI,N.HIROKAWA,Y.GOSHIMA,         
JRNL        AUTH 3 M.SHIROUZU,R.NITTA                                           
JRNL        TITL   STRUCTURAL BASIS FOR CRMP2-INDUCED AXONAL MICROTUBULE        
JRNL        TITL 2 FORMATION                                                    
JRNL        REF    SCI REP                       V.   7 10681 2017              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   28878401                                                     
JRNL        DOI    10.1038/S41598-017-11031-4                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.26                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 70576                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.890                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4864                            
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 43.2719 -  6.5213    1.00     2324   266  0.1574 0.1947        
REMARK   3     2  6.5213 -  5.1789    1.00     2202   258  0.1636 0.1823        
REMARK   3     3  5.1789 -  4.5251    1.00     2180   227  0.1313 0.1477        
REMARK   3     4  4.5251 -  4.1117    1.00     2147   257  0.1203 0.1501        
REMARK   3     5  4.1117 -  3.8172    1.00     2114   267  0.1341 0.1923        
REMARK   3     6  3.8172 -  3.5922    1.00     2151   231  0.1511 0.1900        
REMARK   3     7  3.5922 -  3.4124    1.00     2108   258  0.1650 0.1945        
REMARK   3     8  3.4124 -  3.2639    1.00     2104   250  0.1701 0.2175        
REMARK   3     9  3.2639 -  3.1383    1.00     2114   257  0.1881 0.2272        
REMARK   3    10  3.1383 -  3.0301    1.00     2120   237  0.1984 0.2227        
REMARK   3    11  3.0301 -  2.9353    1.00     2098   244  0.2003 0.2172        
REMARK   3    12  2.9353 -  2.8514    1.00     2123   236  0.2056 0.2360        
REMARK   3    13  2.8514 -  2.7764    1.00     2091   255  0.2040 0.2188        
REMARK   3    14  2.7764 -  2.7087    1.00     2106   210  0.2113 0.2373        
REMARK   3    15  2.7087 -  2.6471    1.00     2076   264  0.2018 0.2308        
REMARK   3    16  2.6471 -  2.5908    1.00     2118   233  0.1994 0.2161        
REMARK   3    17  2.5908 -  2.5389    1.00     2095   232  0.2006 0.2501        
REMARK   3    18  2.5389 -  2.4910    1.00     2139   203  0.2049 0.2577        
REMARK   3    19  2.4910 -  2.4466    1.00     2117   215  0.1929 0.2413        
REMARK   3    20  2.4466 -  2.4051    1.00     2091   239  0.2006 0.2312        
REMARK   3    21  2.4051 -  2.3663    1.00     2306    25  0.2039 0.2276        
REMARK   3    22  2.3663 -  2.3299    1.00     2315     0  0.2124 0.0000        
REMARK   3    23  2.3299 -  2.2956    1.00     2324     0  0.2105 0.0000        
REMARK   3    24  2.2956 -  2.2633    1.00     2315     0  0.1993 0.0000        
REMARK   3    25  2.2633 -  2.2327    1.00     2342     0  0.2052 0.0000        
REMARK   3    26  2.2327 -  2.2037    1.00     2321     0  0.2112 0.0000        
REMARK   3    27  2.2037 -  2.1762    1.00     2308     0  0.2207 0.0000        
REMARK   3    28  2.1762 -  2.1500    1.00     2320     0  0.2244 0.0000        
REMARK   3    29  2.1500 -  2.1250    1.00     2319     0  0.2222 0.0000        
REMARK   3    30  2.1250 -  2.1011    0.96     2224     0  0.2266 0.0000        
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)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.160           
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      :  0.009           7549                                  
REMARK   3   ANGLE     :  1.199          10244                                  
REMARK   3   CHIRALITY :  0.047           1157                                  
REMARK   3   PLANARITY :  0.006           1334                                  
REMARK   3   DIHEDRAL  : 14.392           2757                                  
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: NULL                                      
REMARK   4                                                                      
REMARK   4 5X1C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300002775.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-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                       : BL32XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70654                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 9.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.5000                             
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: 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   (%): 56.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, TRIS PH 7.0, VAPOR     
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       63.34350            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       63.34350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       74.10950            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       63.34350            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       63.34350            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.10950            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       63.34350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       63.34350            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       74.10950            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       63.34350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       63.34350            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       74.10950            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
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                                                                      
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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000     -126.68700            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 623  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 719  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 852  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 599  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 683  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 825  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     VAL B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     PHE B     9                                                      
REMARK 465     GLN B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     PRO B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU B  125   CD                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   600     O    HOH A   790              1.80            
REMARK 500   O    HOH B   663     O    HOH B   801              1.85            
REMARK 500   O    HOH A   741     O    HOH A   814              1.94            
REMARK 500   O    HOH A   679     O    HOH A   759              1.95            
REMARK 500   OD1  ASP A    87     O    HOH A   501              1.99            
REMARK 500   O    HOH B   626     O    HOH B   802              2.00            
REMARK 500   O    HOH B   764     O    HOH B   766              2.02            
REMARK 500   O    HOH A   800     O    HOH B   761              2.04            
REMARK 500   O    HOH A   592     O    HOH A   827              2.07            
REMARK 500   O    HOH A   680     O    HOH A   796              2.09            
REMARK 500   OD2  ASP A   315     O    HOH A   502              2.14            
REMARK 500   O    HOH A   784     O    HOH B   780              2.16            
REMARK 500   O    HOH B   749     O    HOH B   816              2.16            
REMARK 500   OG   SER A    85     O    HOH A   503              2.17            
REMARK 500   O    HOH A   764     O    HOH A   857              2.17            
REMARK 500   O    HOH B   598     O    HOH B   622              2.18            
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 B   515     O    HOH B   787     2545     2.09            
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    LEU A   8   CA  -  CB  -  CG  ANGL. DEV. = -17.7 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    LEU A   8       86.51     18.49                                   
REMARK 500    SER A  14       36.24    -78.50                                   
REMARK 500    ASP A  15       31.96    -91.48                                   
REMARK 500    GLN A  77        8.39    121.58                                   
REMARK 500    ASP A  88     -165.78    -73.33                                   
REMARK 500    ASN A 162       22.13   -142.42                                   
REMARK 500    PHE A 170       64.60     62.71                                   
REMARK 500    ASP A 172      -18.44     79.72                                   
REMARK 500    ASN A 347      108.59   -162.46                                   
REMARK 500    SER A 385      -49.19   -144.00                                   
REMARK 500    ASN A 426       54.09    -92.30                                   
REMARK 500    GLN A 449       46.24     38.63                                   
REMARK 500    ASP B  15       54.39   -145.05                                   
REMARK 500    ARG B  16      105.37     53.07                                   
REMARK 500    ASP B 172      -36.39    140.53                                   
REMARK 500    ARG B 173      -55.65   -137.65                                   
REMARK 500    CYS B 334       70.70   -157.42                                   
REMARK 500    ASN B 347      107.13   -169.20                                   
REMARK 500    SER B 385      -48.74   -144.93                                   
REMARK 500    ASN B 393       39.04     72.01                                   
REMARK 500    ASN B 426       30.48    -99.31                                   
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 VAL A    7     LEU A    8                 -117.43                    
REMARK 500 ASP B  172     ARG B  173                 -146.87                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5X1A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5X1D   RELATED DB: PDB                                   
DBREF  5X1C A   13   490  UNP    Q16555   DPYL2_HUMAN     13    490             
DBREF  5X1C B   13   490  UNP    Q16555   DPYL2_HUMAN     13    490             
SEQADV 5X1C VAL A    7  UNP  Q16555              EXPRESSION TAG                 
SEQADV 5X1C LEU A    8  UNP  Q16555              EXPRESSION TAG                 
SEQADV 5X1C PHE A    9  UNP  Q16555              EXPRESSION TAG                 
SEQADV 5X1C GLN A   10  UNP  Q16555              EXPRESSION TAG                 
SEQADV 5X1C GLY A   11  UNP  Q16555              EXPRESSION TAG                 
SEQADV 5X1C PRO A   12  UNP  Q16555              EXPRESSION TAG                 
SEQADV 5X1C VAL B    7  UNP  Q16555              EXPRESSION TAG                 
SEQADV 5X1C LEU B    8  UNP  Q16555              EXPRESSION TAG                 
SEQADV 5X1C PHE B    9  UNP  Q16555              EXPRESSION TAG                 
SEQADV 5X1C GLN B   10  UNP  Q16555              EXPRESSION TAG                 
SEQADV 5X1C GLY B   11  UNP  Q16555              EXPRESSION TAG                 
SEQADV 5X1C PRO B   12  UNP  Q16555              EXPRESSION TAG                 
SEQRES   1 A  484  VAL LEU PHE GLN GLY PRO THR SER ASP ARG LEU LEU ILE          
SEQRES   2 A  484  LYS GLY GLY LYS ILE VAL ASN ASP ASP GLN SER PHE TYR          
SEQRES   3 A  484  ALA ASP ILE TYR MET GLU ASP GLY LEU ILE LYS GLN ILE          
SEQRES   4 A  484  GLY GLU ASN LEU ILE VAL PRO GLY GLY VAL LYS THR ILE          
SEQRES   5 A  484  GLU ALA HIS SER ARG MET VAL ILE PRO GLY GLY ILE ASP          
SEQRES   6 A  484  VAL HIS THR ARG PHE GLN MET PRO ASP GLN GLY MET THR          
SEQRES   7 A  484  SER ALA ASP ASP PHE PHE GLN GLY THR LYS ALA ALA LEU          
SEQRES   8 A  484  ALA GLY GLY THR THR MET ILE ILE ASP HIS VAL VAL PRO          
SEQRES   9 A  484  GLU PRO GLY THR SER LEU LEU ALA ALA PHE ASP GLN TRP          
SEQRES  10 A  484  ARG GLU TRP ALA ASP SER LYS SER CYS CYS ASP TYR SER          
SEQRES  11 A  484  LEU HIS VAL ASP ILE SER GLU TRP HIS LYS GLY ILE GLN          
SEQRES  12 A  484  GLU GLU MET GLU ALA LEU VAL LYS ASP HIS GLY VAL ASN          
SEQRES  13 A  484  SER PHE LEU VAL TYR MET ALA PHE LYS ASP ARG PHE GLN          
SEQRES  14 A  484  LEU THR ASP CYS GLN ILE TYR GLU VAL LEU SER VAL ILE          
SEQRES  15 A  484  ARG ASP ILE GLY ALA ILE ALA GLN VAL HIS ALA GLU ASN          
SEQRES  16 A  484  GLY ASP ILE ILE ALA GLU GLU GLN GLN ARG ILE LEU ASP          
SEQRES  17 A  484  LEU GLY ILE THR GLY PRO GLU GLY HIS VAL LEU SER ARG          
SEQRES  18 A  484  PRO GLU GLU VAL GLU ALA GLU ALA VAL ASN ARG ALA ILE          
SEQRES  19 A  484  THR ILE ALA ASN GLN THR ASN CYS PRO LEU TYR ILE THR          
SEQRES  20 A  484  LYS VAL MET SER LYS SER SER ALA GLU VAL ILE ALA GLN          
SEQRES  21 A  484  ALA ARG LYS LYS GLY THR VAL VAL TYR GLY GLU PRO ILE          
SEQRES  22 A  484  THR ALA SER LEU GLY THR ASP GLY SER HIS TYR TRP SER          
SEQRES  23 A  484  LYS ASN TRP ALA LYS ALA ALA ALA PHE VAL THR SER PRO          
SEQRES  24 A  484  PRO LEU SER PRO ASP PRO THR THR PRO ASP PHE LEU ASN          
SEQRES  25 A  484  SER LEU LEU SER CYS GLY ASP LEU GLN VAL THR GLY SER          
SEQRES  26 A  484  ALA HIS CYS THR PHE ASN THR ALA GLN LYS ALA VAL GLY          
SEQRES  27 A  484  LYS ASP ASN PHE THR LEU ILE PRO GLU GLY THR ASN GLY          
SEQRES  28 A  484  THR GLU GLU ARG MET SER VAL ILE TRP ASP LYS ALA VAL          
SEQRES  29 A  484  VAL THR GLY LYS MET ASP GLU ASN GLN PHE VAL ALA VAL          
SEQRES  30 A  484  THR SER THR ASN ALA ALA LYS VAL PHE ASN LEU TYR PRO          
SEQRES  31 A  484  ARG LYS GLY ARG ILE ALA VAL GLY SER ASP ALA ASP LEU          
SEQRES  32 A  484  VAL ILE TRP ASP PRO ASP SER VAL LYS THR ILE SER ALA          
SEQRES  33 A  484  LYS THR HIS ASN SER SER LEU GLU TYR ASN ILE PHE GLU          
SEQRES  34 A  484  GLY MET GLU CYS ARG GLY SER PRO LEU VAL VAL ILE SER          
SEQRES  35 A  484  GLN GLY LYS ILE VAL LEU GLU ASP GLY THR LEU HIS VAL          
SEQRES  36 A  484  THR GLU GLY SER GLY ARG TYR ILE PRO ARG LYS PRO PHE          
SEQRES  37 A  484  PRO ASP PHE VAL TYR LYS ARG ILE LYS ALA ARG SER ARG          
SEQRES  38 A  484  LEU ALA GLU                                                  
SEQRES   1 B  484  VAL LEU PHE GLN GLY PRO THR SER ASP ARG LEU LEU ILE          
SEQRES   2 B  484  LYS GLY GLY LYS ILE VAL ASN ASP ASP GLN SER PHE TYR          
SEQRES   3 B  484  ALA ASP ILE TYR MET GLU ASP GLY LEU ILE LYS GLN ILE          
SEQRES   4 B  484  GLY GLU ASN LEU ILE VAL PRO GLY GLY VAL LYS THR ILE          
SEQRES   5 B  484  GLU ALA HIS SER ARG MET VAL ILE PRO GLY GLY ILE ASP          
SEQRES   6 B  484  VAL HIS THR ARG PHE GLN MET PRO ASP GLN GLY MET THR          
SEQRES   7 B  484  SER ALA ASP ASP PHE PHE GLN GLY THR LYS ALA ALA LEU          
SEQRES   8 B  484  ALA GLY GLY THR THR MET ILE ILE ASP HIS VAL VAL PRO          
SEQRES   9 B  484  GLU PRO GLY THR SER LEU LEU ALA ALA PHE ASP GLN TRP          
SEQRES  10 B  484  ARG GLU TRP ALA ASP SER LYS SER CYS CYS ASP TYR SER          
SEQRES  11 B  484  LEU HIS VAL ASP ILE SER GLU TRP HIS LYS GLY ILE GLN          
SEQRES  12 B  484  GLU GLU MET GLU ALA LEU VAL LYS ASP HIS GLY VAL ASN          
SEQRES  13 B  484  SER PHE LEU VAL TYR MET ALA PHE LYS ASP ARG PHE GLN          
SEQRES  14 B  484  LEU THR ASP CYS GLN ILE TYR GLU VAL LEU SER VAL ILE          
SEQRES  15 B  484  ARG ASP ILE GLY ALA ILE ALA GLN VAL HIS ALA GLU ASN          
SEQRES  16 B  484  GLY ASP ILE ILE ALA GLU GLU GLN GLN ARG ILE LEU ASP          
SEQRES  17 B  484  LEU GLY ILE THR GLY PRO GLU GLY HIS VAL LEU SER ARG          
SEQRES  18 B  484  PRO GLU GLU VAL GLU ALA GLU ALA VAL ASN ARG ALA ILE          
SEQRES  19 B  484  THR ILE ALA ASN GLN THR ASN CYS PRO LEU TYR ILE THR          
SEQRES  20 B  484  LYS VAL MET SER LYS SER SER ALA GLU VAL ILE ALA GLN          
SEQRES  21 B  484  ALA ARG LYS LYS GLY THR VAL VAL TYR GLY GLU PRO ILE          
SEQRES  22 B  484  THR ALA SER LEU GLY THR ASP GLY SER HIS TYR TRP SER          
SEQRES  23 B  484  LYS ASN TRP ALA LYS ALA ALA ALA PHE VAL THR SER PRO          
SEQRES  24 B  484  PRO LEU SER PRO ASP PRO THR THR PRO ASP PHE LEU ASN          
SEQRES  25 B  484  SER LEU LEU SER CYS GLY ASP LEU GLN VAL THR GLY SER          
SEQRES  26 B  484  ALA HIS CYS THR PHE ASN THR ALA GLN LYS ALA VAL GLY          
SEQRES  27 B  484  LYS ASP ASN PHE THR LEU ILE PRO GLU GLY THR ASN GLY          
SEQRES  28 B  484  THR GLU GLU ARG MET SER VAL ILE TRP ASP LYS ALA VAL          
SEQRES  29 B  484  VAL THR GLY LYS MET ASP GLU ASN GLN PHE VAL ALA VAL          
SEQRES  30 B  484  THR SER THR ASN ALA ALA LYS VAL PHE ASN LEU TYR PRO          
SEQRES  31 B  484  ARG LYS GLY ARG ILE ALA VAL GLY SER ASP ALA ASP LEU          
SEQRES  32 B  484  VAL ILE TRP ASP PRO ASP SER VAL LYS THR ILE SER ALA          
SEQRES  33 B  484  LYS THR HIS ASN SER SER LEU GLU TYR ASN ILE PHE GLU          
SEQRES  34 B  484  GLY MET GLU CYS ARG GLY SER PRO LEU VAL VAL ILE SER          
SEQRES  35 B  484  GLN GLY LYS ILE VAL LEU GLU ASP GLY THR LEU HIS VAL          
SEQRES  36 B  484  THR GLU GLY SER GLY ARG TYR ILE PRO ARG LYS PRO PHE          
SEQRES  37 B  484  PRO ASP PHE VAL TYR LYS ARG ILE LYS ALA ARG SER ARG          
SEQRES  38 B  484  LEU ALA GLU                                                  
FORMUL   3  HOH   *701(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 HIS A  145  HIS A  159  1                                  15    
HELIX    4 AA4 THR A  177  GLY A  192  1                                  16    
HELIX    5 AA5 ASN A  201  LEU A  215  1                                  15    
HELIX    6 AA6 PRO A  220  SER A  226  1                                   7    
HELIX    7 AA7 GLU A  229  ASN A  247  1                                  19    
HELIX    8 AA8 SER A  257  LYS A  270  1                                  14    
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  ARG A  487  1                                  13    
HELIX   20 AC2 ASP B   88  GLY B   99  1                                  12    
HELIX   21 AC3 SER B  115  SER B  131  1                                  17    
HELIX   22 AC4 HIS B  145  HIS B  159  1                                  15    
HELIX   23 AC5 THR B  177  GLY B  192  1                                  16    
HELIX   24 AC6 ASN B  201  LEU B  215  1                                  15    
HELIX   25 AC7 PRO B  220  SER B  226  1                                   7    
HELIX   26 AC8 PRO B  228  ASN B  247  1                                  20    
HELIX   27 AC9 SER B  257  LYS B  270  1                                  14    
HELIX   28 AD1 ILE B  279  THR B  285  1                                   7    
HELIX   29 AD2 ASP B  286  SER B  292  5                                   7    
HELIX   30 AD3 ASN B  294  PHE B  301  1                                   8    
HELIX   31 AD4 THR B  312  CYS B  323  1                                  12    
HELIX   32 AD5 ASN B  337  ALA B  342  1                                   6    
HELIX   33 AD6 VAL B  343  LYS B  345  5                                   3    
HELIX   34 AD7 ASN B  347  ILE B  351  5                                   5    
HELIX   35 AD8 GLU B  360  VAL B  370  1                                  11    
HELIX   36 AD9 ASP B  376  SER B  385  1                                  10    
HELIX   37 AE1 SER B  385  PHE B  392  1                                   8    
HELIX   38 AE2 PRO B  475  ARG B  487  1                                  13    
SHEET    1 AA1 4 LEU A  41  GLY A  46  0                                        
SHEET    2 AA1 4 SER A  30  GLU A  38 -1  N  TYR A  36   O  LYS A  43           
SHEET    3 AA1 4 ARG A  16  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  TYR A  36   O  LYS A  43           
SHEET    3 AA2 8 ARG A  16  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  VAL A  25           
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  LEU A 444   N  ILE A 411           
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  VAL A 108           
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  THR A 253   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 4 LEU B  41  GLY B  46  0                                        
SHEET    2 AA4 4 SER B  30  GLU B  38 -1  N  TYR B  36   O  GLN B  44           
SHEET    3 AA4 4 LEU B  17  VAL B  25 -1  N  LEU B  17   O  MET B  37           
SHEET    4 AA4 4 LYS B  56  GLU B  59  1  O  ILE B  58   N  LYS B  20           
SHEET    1 AA5 8 LEU B  41  GLY B  46  0                                        
SHEET    2 AA5 8 SER B  30  GLU B  38 -1  N  TYR B  36   O  GLN B  44           
SHEET    3 AA5 8 LEU B  17  VAL B  25 -1  N  LEU B  17   O  MET B  37           
SHEET    4 AA5 8 MET B  64  PRO B  67  1  O  VAL B  65   N  VAL B  25           
SHEET    5 AA5 8 LEU B 409  THR B 419 -1  O  VAL B 410   N  ILE B  66           
SHEET    6 AA5 8 GLU B 438  SER B 448 -1  O  LEU B 444   N  ILE B 411           
SHEET    7 AA5 8 LYS B 451  GLU B 455 -1  O  VAL B 453   N  VAL B 446           
SHEET    8 AA5 8 THR B 458  LEU B 459 -1  O  THR B 458   N  GLU B 455           
SHEET    1 AA6 7 GLY B  69  THR B  74  0                                        
SHEET    2 AA6 7 THR B 101  VAL B 108  1  O  ILE B 105   N  ASP B  71           
SHEET    3 AA6 7 ASP B 134  ASP B 140  1  O  HIS B 138   N  VAL B 108           
SHEET    4 AA6 7 SER B 163  TYR B 167  1  O  SER B 163   N  VAL B 139           
SHEET    5 AA6 7 ILE B 194  HIS B 198  1  O  GLN B 196   N  PHE B 164           
SHEET    6 AA6 7 LEU B 250  VAL B 255  1  O  TYR B 251   N  VAL B 197           
SHEET    7 AA6 7 VAL B 274  PRO B 278  1  O  TYR B 275   N  ILE B 252           
SHEET    1 AA7 2 PRO B  79  ASP B  80  0                                        
SHEET    2 AA7 2 MET B  83  THR B  84 -1  O  MET B  83   N  ASP B  80           
CISPEP   1 GLY A   11    PRO A   12          0         7.00                     
CISPEP   2 SER A  304    PRO A  305          0        -6.69                     
CISPEP   3 TYR A  395    PRO A  396          0         3.75                     
CISPEP   4 SER B  304    PRO B  305          0        -8.09                     
CISPEP   5 TYR B  395    PRO B  396          0         1.65                     
CRYST1  126.687  126.687  148.219  90.00  90.00  90.00 P 42 21 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      0.007893  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007893  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006747        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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