GenomeNet

Database: PDB
Entry: 4M6J
LinkDB: 4M6J
Original site: 4M6J 
HEADER    OXIDOREDUCTASE                          09-AUG-13   4M6J              
TITLE     CRYSTAL STRUCTURE OF HUMAN DIHYDROFOLATE REDUCTASE (DHFR) BOUND TO    
TITLE    2 NADPH                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIHYDROFOLATE REDUCTASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.5.1.3;                                                         
COMPND   5 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: DHFR;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PDNAY;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21A                                    
KEYWDS    ROSSMANN FOLD, NADPH BINDING, FOLATE BINDING, OXIDOREDUCTASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.BHABHA,D.C.EKIERT,P.E.WRIGHT,I.A.WILSON                             
REVDAT   3   20-NOV-13 4M6J    1       JRNL                                     
REVDAT   2   16-OCT-13 4M6J    1       JRNL                                     
REVDAT   1   25-SEP-13 4M6J    0                                                
JRNL        AUTH   G.BHABHA,D.C.EKIERT,M.JENNEWEIN,C.M.ZMASEK,L.M.TUTTLE,       
JRNL        AUTH 2 G.KROON,H.J.DYSON,A.GODZIK,I.A.WILSON,P.E.WRIGHT             
JRNL        TITL   DIVERGENT EVOLUTION OF PROTEIN CONFORMATIONAL DYNAMICS IN    
JRNL        TITL 2 DIHYDROFOLATE REDUCTASE.                                     
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  20  1243 2013              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   24077226                                                     
JRNL        DOI    10.1038/NSMB.2676                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.49                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 59264                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.184                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3008                            
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 33.4994 -  3.3124    0.92     2717   150  0.1960 0.1790        
REMARK   3     2  3.3124 -  2.6295    0.99     2811   158  0.1687 0.2082        
REMARK   3     3  2.6295 -  2.2972    1.00     2804   159  0.1670 0.2213        
REMARK   3     4  2.2972 -  2.0872    1.00     2767   170  0.1466 0.1774        
REMARK   3     5  2.0872 -  1.9376    1.00     2765   158  0.1421 0.1333        
REMARK   3     6  1.9376 -  1.8234    1.00     2751   146  0.1358 0.1639        
REMARK   3     7  1.8234 -  1.7321    1.00     2774   133  0.1360 0.1881        
REMARK   3     8  1.7321 -  1.6567    1.00     2779   140  0.1352 0.1579        
REMARK   3     9  1.6567 -  1.5929    1.00     2755   150  0.1292 0.1586        
REMARK   3    10  1.5929 -  1.5379    1.00     2776   143  0.1245 0.1654        
REMARK   3    11  1.5379 -  1.4898    1.00     2719   158  0.1304 0.1747        
REMARK   3    12  1.4898 -  1.4472    1.00     2772   135  0.1310 0.1696        
REMARK   3    13  1.4472 -  1.4091    1.00     2736   140  0.1338 0.1551        
REMARK   3    14  1.4091 -  1.3748    1.00     2767   149  0.1413 0.1777        
REMARK   3    15  1.3748 -  1.3435    1.00     2721   159  0.1443 0.2056        
REMARK   3    16  1.3435 -  1.3149    1.00     2699   147  0.1534 0.1662        
REMARK   3    17  1.3149 -  1.2886    0.98     2744   131  0.1571 0.2048        
REMARK   3    18  1.2886 -  1.2643    0.95     2570   141  0.1737 0.2176        
REMARK   3    19  1.2643 -  1.2417    0.91     2506   136  0.1979 0.2254        
REMARK   3    20  1.2417 -  1.2207    0.84     2304    99  0.2097 0.2466        
REMARK   3    21  1.2207 -  1.2010    0.73     2019   106  0.2297 0.2394        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.30                                          
REMARK   3   SHRINKAGE RADIUS   : 1.00                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.110            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.750           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.60                          
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           1746                                  
REMARK   3   ANGLE     :  1.480           2397                                  
REMARK   3   CHIRALITY :  0.086            256                                  
REMARK   3   PLANARITY :  0.007            311                                  
REMARK   3   DIHEDRAL  : 14.705            711                                  
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 4M6J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB081528.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-JUN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59318                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 76.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.54000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1DLS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG6000, 100 MM TRIS, PH 9.5,        
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                     
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       76.12550            
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       76.12550            
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       19.47900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       32.76250            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       19.47900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       32.76250            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       76.12550            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       19.47900            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       32.76250            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       76.12550            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       19.47900            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       32.76250            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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 459  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     0                                                      
REMARK 465     VAL A     1                                                      
REMARK 465     GLY A     2                                                      
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 110      -84.77    -93.65                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4M6K   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4M6L   RELATED DB: PDB                                   
DBREF  4M6J A    0   186  UNP    P00374   DYR_HUMAN        1    187             
SEQRES   1 A  187  MET VAL GLY SER LEU ASN CYS ILE VAL ALA VAL SER GLN          
SEQRES   2 A  187  ASN MET GLY ILE GLY LYS ASN GLY ASP LEU PRO TRP PRO          
SEQRES   3 A  187  PRO LEU ARG ASN GLU PHE ARG TYR PHE GLN ARG MET THR          
SEQRES   4 A  187  THR THR SER SER VAL GLU GLY LYS GLN ASN LEU VAL ILE          
SEQRES   5 A  187  MET GLY LYS LYS THR TRP PHE SER ILE PRO GLU LYS ASN          
SEQRES   6 A  187  ARG PRO LEU LYS GLY ARG ILE ASN LEU VAL LEU SER ARG          
SEQRES   7 A  187  GLU LEU LYS GLU PRO PRO GLN GLY ALA HIS PHE LEU SER          
SEQRES   8 A  187  ARG SER LEU ASP ASP ALA LEU LYS LEU THR GLU GLN PRO          
SEQRES   9 A  187  GLU LEU ALA ASN LYS VAL ASP MET VAL TRP ILE VAL GLY          
SEQRES  10 A  187  GLY SER SER VAL TYR LYS GLU ALA MET ASN HIS PRO GLY          
SEQRES  11 A  187  HIS LEU LYS LEU PHE VAL THR ARG ILE MET GLN ASP PHE          
SEQRES  12 A  187  GLU SER ASP THR PHE PHE PRO GLU ILE ASP LEU GLU LYS          
SEQRES  13 A  187  TYR LYS LEU LEU PRO GLU TYR PRO GLY VAL LEU SER ASP          
SEQRES  14 A  187  VAL GLN GLU GLU LYS GLY ILE LYS TYR LYS PHE GLU VAL          
SEQRES  15 A  187  TYR GLU LYS ASN ASP                                          
HET    NDP  A 201      48                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
FORMUL   2  NDP    C21 H30 N7 O17 P3                                            
FORMUL   3  HOH   *195(H2 O)                                                    
HELIX    1   1 LEU A   27  THR A   40  1                                  14    
HELIX    2   2 LYS A   54  ILE A   60  1                                   7    
HELIX    3   3 PRO A   61  ARG A   65  5                                   5    
HELIX    4   4 SER A   92  GLU A  101  1                                  10    
HELIX    5   5 GLN A  102  ASN A  107  1                                   6    
HELIX    6   6 GLY A  117  MET A  125  1                                   9    
SHEET    1   A 8 PHE A  88  SER A  90  0                                        
SHEET    2   A 8 ILE A  71  LEU A  75  1  N  VAL A  74   O  PHE A  88           
SHEET    3   A 8 GLN A  47  GLY A  53  1  N  VAL A  50   O  ILE A  71           
SHEET    4   A 8 VAL A 109  ILE A 114  1  O  TRP A 113   N  LEU A  49           
SHEET    5   A 8 LEU A   4  VAL A  10  1  N  ASN A   5   O  ILE A 114           
SHEET    6   A 8 HIS A 130  ILE A 138  1  O  PHE A 134   N  CYS A   6           
SHEET    7   A 8 ILE A 175  ASN A 185 -1  O  GLU A 180   N  VAL A 135           
SHEET    8   A 8 LYS A 157  LEU A 158 -1  N  LYS A 157   O  GLU A 183           
SHEET    1   B 8 PHE A  88  SER A  90  0                                        
SHEET    2   B 8 ILE A  71  LEU A  75  1  N  VAL A  74   O  PHE A  88           
SHEET    3   B 8 GLN A  47  GLY A  53  1  N  VAL A  50   O  ILE A  71           
SHEET    4   B 8 VAL A 109  ILE A 114  1  O  TRP A 113   N  LEU A  49           
SHEET    5   B 8 LEU A   4  VAL A  10  1  N  ASN A   5   O  ILE A 114           
SHEET    6   B 8 HIS A 130  ILE A 138  1  O  PHE A 134   N  CYS A   6           
SHEET    7   B 8 ILE A 175  ASN A 185 -1  O  GLU A 180   N  VAL A 135           
SHEET    8   B 8 GLN A 170  GLU A 172 -1  N  GLN A 170   O  TYR A 177           
SHEET    1   C 2 GLY A  15  GLY A  17  0                                        
SHEET    2   C 2 THR A 146  PHE A 147 -1  O  THR A 146   N  ILE A  16           
CISPEP   1 ARG A   65    PRO A   66          0        -8.81                     
CISPEP   2 GLY A  116    GLY A  117          0         3.72                     
SITE     1 AC1 32 VAL A   8  ALA A   9  ILE A  16  GLY A  17                    
SITE     2 AC1 32 GLY A  20  ASP A  21  LEU A  22  GLY A  53                    
SITE     3 AC1 32 LYS A  54  LYS A  55  THR A  56  LEU A  75                    
SITE     4 AC1 32 SER A  76  ARG A  77  GLU A  78  ARG A  91                    
SITE     5 AC1 32 SER A  92  VAL A 115  GLY A 117  SER A 118                    
SITE     6 AC1 32 SER A 119  VAL A 120  TYR A 121  HOH A 307                    
SITE     7 AC1 32 HOH A 313  HOH A 319  HOH A 332  HOH A 339                    
SITE     8 AC1 32 HOH A 412  HOH A 422  HOH A 445  HOH A 488                    
CRYST1   38.958   65.525  152.251  90.00  90.00  90.00 C 2 2 21      8          
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      0.025669  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015261  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006568        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system