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Database: PDB
Entry: 5HTV
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Original site: 5HTV 
HEADER    TRANSFERASE                             27-JAN-16   5HTV              
TITLE     PUTATIVE SUGAR KINASES FROM ARABIDOPSIS THALIANA IN COMPLEX WITH      
TITLE    2 AMPPNP                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE XYLULOSE KINASE;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 43-478;                                       
COMPND   5 SYNONYM: XYLULOSE KINASE LIKE PROTEIN,XYLULOSE KINASE-1;             
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS;                                    
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: XK-1, AT2G21370;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    PUTATIVE SUGAR KINASES, ARABIDOPSIS THALIANA, AMPPNP, TRANSFERASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.XIE,M.LI,W.CHANG                                                    
REVDAT   2   20-MAR-24 5HTV    1       REMARK                                   
REVDAT   1   08-JUN-16 5HTV    0                                                
JRNL        AUTH   Y.XIE,M.LI,W.CHANG                                           
JRNL        TITL   CRYSTAL STRUCTURES OF PUTATIVE SUGAR KINASES FROM            
JRNL        TITL 2 SYNECHOCOCCUS ELONGATUS PCC 7942 AND ARABIDOPSIS THALIANA    
JRNL        REF    PLOS ONE                      V.  11 56067 2016              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   27223615                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0156067                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.78 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) : 1.78                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.40                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 45067                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.204                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.430                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1997                            
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 38.4042 -  4.2212    0.99     3149   146  0.1668 0.1993        
REMARK   3     2  4.2212 -  3.3511    1.00     3086   143  0.1549 0.1682        
REMARK   3     3  3.3511 -  2.9277    1.00     3104   146  0.1727 0.2024        
REMARK   3     4  2.9277 -  2.6601    1.00     3111   140  0.1787 0.2214        
REMARK   3     5  2.6601 -  2.4695    1.00     3102   142  0.1787 0.1997        
REMARK   3     6  2.4695 -  2.3239    1.00     3066   150  0.1724 0.2217        
REMARK   3     7  2.3239 -  2.2075    1.00     3106   132  0.1607 0.2365        
REMARK   3     8  2.2075 -  2.1114    1.00     3098   148  0.1560 0.1846        
REMARK   3     9  2.1114 -  2.0302    0.99     3043   143  0.1602 0.1745        
REMARK   3    10  2.0302 -  1.9601    0.99     3064   148  0.1688 0.2305        
REMARK   3    11  1.9601 -  1.8988    0.99     3042   138  0.1755 0.2192        
REMARK   3    12  1.8988 -  1.8445    1.00     3077   141  0.1819 0.2367        
REMARK   3    13  1.8445 -  1.7960    0.99     3065   146  0.1957 0.2273        
REMARK   3    14  1.7960 -  1.7522    0.96     2957   134  0.2113 0.2556        
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)     : 0.150            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.480           
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      :  0.007           3361                                  
REMARK   3   ANGLE     :  1.145           4573                                  
REMARK   3   CHIRALITY :  0.042            513                                  
REMARK   3   PLANARITY :  0.005            583                                  
REMARK   3   DIHEDRAL  : 12.725           1234                                  
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 5HTV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217745.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97917                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45097                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
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     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.8100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AUTOSOL                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5, 20% W/V           
REMARK 280  POLYETHYLENE GLYCOL MONOMETHYL ETHER 5,000, VAPOR DIFFUSION,        
REMARK 280  SITTING DROP, TEMPERATURE 281K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       43.72700            
REMARK 290   SMTRY3   2  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 TOTAL BURIED SURFACE AREA: 720 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 17870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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 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     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     VAL A     1                                                      
REMARK 465     MET A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     ASN A     9                                                      
REMARK 465     TYR A    10                                                      
REMARK 465     GLY A   435                                                      
REMARK 465     LEU A   436                                                      
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   752     O    HOH A   761              1.98            
REMARK 500   O    HOH A   639     O    HOH A   873              2.07            
REMARK 500   O    HOH A   852     O    HOH A   874              2.09            
REMARK 500   O    HOH A   633     O    HOH A   902              2.13            
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    SER A 171     -168.52   -128.73                                   
REMARK 500    ASP A 283     -124.25     50.63                                   
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 ANP A 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5HTN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HTJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HTP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HTR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HTX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HTY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HU2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HUX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HV7   RELATED DB: PDB                                   
DBREF  5HTV A    1   436  UNP    Q8L794   Q8L794_ARATH    43    478             
SEQADV 5HTV SER A   -2  UNP  Q8L794              EXPRESSION TAG                 
SEQADV 5HTV ASN A   -1  UNP  Q8L794              EXPRESSION TAG                 
SEQADV 5HTV ALA A    0  UNP  Q8L794              EXPRESSION TAG                 
SEQRES   1 A  439  SER ASN ALA VAL MET SER GLY ASN LYS GLY THR ASN TYR          
SEQRES   2 A  439  GLU LYS LEU TYR LEU GLY MET ASP PHE GLY THR SER GLY          
SEQRES   3 A  439  GLY ARG PHE THR VAL ILE ASP GLU GLN GLY GLU ILE LYS          
SEQRES   4 A  439  ALA GLN GLY LYS ARG GLU TYR PRO PRO PHE MET LYS GLU          
SEQRES   5 A  439  GLU SER MET GLY TRP ALA SER SER TRP LYS ALA THR LEU          
SEQRES   6 A  439  PHE SER LEU LEU GLU ASP ILE PRO VAL THR VAL ARG SER          
SEQRES   7 A  439  LEU VAL SER SER ILE SER LEU ASP GLY THR SER ALA THR          
SEQRES   8 A  439  THR LEU ILE LEU ASN SER GLU SER GLY GLU VAL LEU CYS          
SEQRES   9 A  439  GLN PRO TYR LEU TYR ASN GLN SER CYS PRO ASP ALA LEU          
SEQRES  10 A  439  PRO GLU VAL LYS SER ILE ALA PRO ALA ASN HIS THR VAL          
SEQRES  11 A  439  CYS SER GLY THR SER THR LEU CYS LYS LEU VAL SER TRP          
SEQRES  12 A  439  TRP ASN THR GLU VAL PRO ASN ARG GLU SER ALA VAL LEU          
SEQRES  13 A  439  LEU HIS GLN ALA ASP TRP LEU LEU TRP LEU LEU HIS GLY          
SEQRES  14 A  439  ARG LEU GLY VAL SER ASP TYR ASN ASN ALA LEU LYS VAL          
SEQRES  15 A  439  GLY TYR ASP PRO GLU SER GLU SER TYR PRO SER TRP LEU          
SEQRES  16 A  439  LEU GLY GLN PRO TYR SER GLN LEU LEU PRO LYS VAL GLN          
SEQRES  17 A  439  ALA PRO GLY THR SER ILE GLY ASN LEU LYS GLU SER PHE          
SEQRES  18 A  439  THR ARG GLN PHE GLY PHE PRO ASP ASP CYS ILE VAL CYS          
SEQRES  19 A  439  THR GLY THR THR ASP SER ILE ALA ALA PHE LEU ALA ALA          
SEQRES  20 A  439  ARG ALA THR GLU PRO GLY LYS ALA VAL THR SER LEU GLY          
SEQRES  21 A  439  SER THR LEU ALA ILE LYS LEU LEU SER THR LYS ARG VAL          
SEQRES  22 A  439  ASP ASP ALA ARG TYR GLY VAL TYR SER HIS ARG LEU ASP          
SEQRES  23 A  439  ASP LYS TRP LEU VAL GLY GLY ALA SER ASN THR GLY GLY          
SEQRES  24 A  439  ALA ILE LEU ARG GLN LEU PHE SER ASP GLU GLN LEU GLU          
SEQRES  25 A  439  ARG LEU SER GLN GLU ILE ASN PRO MET VAL GLY SER PRO          
SEQRES  26 A  439  LEU ASP TYR TYR PRO LEU GLN SER SER GLY GLU ARG PHE          
SEQRES  27 A  439  PRO ILE ALA ASP PRO ASN LEU ALA PRO ARG LEU LEU PRO          
SEQRES  28 A  439  ARG PRO GLU SER ASP VAL GLU PHE LEU HIS GLY ILE LEU          
SEQRES  29 A  439  GLU SER ILE ALA ARG ILE GLU GLY LYS GLY TYR LYS LEU          
SEQRES  30 A  439  LEU LYS GLU LEU GLY ALA THR GLU ALA GLU GLU VAL LEU          
SEQRES  31 A  439  THR ALA GLY GLY GLY ALA LYS ASN ASP LYS TRP ILE LYS          
SEQRES  32 A  439  ILE ARG GLN ARG VAL LEU GLY LEU PRO VAL LYS LYS ALA          
SEQRES  33 A  439  VAL HIS THR GLU ALA SER TYR GLY ALA SER LEU LEU ALA          
SEQRES  34 A  439  LEU LYS GLY ALA LYS GLN ASN SER GLY LEU                      
HET    ANP  A 501      31                                                       
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
FORMUL   2  ANP    C10 H17 N6 O12 P3                                            
FORMUL   3  HOH   *324(H2 O)                                                    
HELIX    1 AA1 GLY A   53  ILE A   69  1                                  17    
HELIX    2 AA2 PRO A   70  SER A   75  1                                   6    
HELIX    3 AA3 CYS A  110  ASP A  112  5                                   3    
HELIX    4 AA4 ALA A  113  ALA A  121  1                                   9    
HELIX    5 AA5 SER A  132  THR A  143  1                                  12    
HELIX    6 AA6 ASN A  147  GLU A  149  5                                   3    
HELIX    7 AA7 GLN A  156  GLY A  166  1                                  11    
HELIX    8 AA8 ALA A  176  GLY A  180  5                                   5    
HELIX    9 AA9 PRO A  189  GLY A  194  1                                   6    
HELIX   10 AB1 GLN A  195  LEU A  201  5                                   7    
HELIX   11 AB2 LYS A  215  GLY A  223  1                                   9    
HELIX   12 AB3 ASP A  236  ALA A  243  1                                   8    
HELIX   13 AB4 ASP A  272  GLY A  276  5                                   5    
HELIX   14 AB5 GLY A  295  PHE A  303  1                                   9    
HELIX   15 AB6 SER A  304  GLU A  314  1                                  11    
HELIX   16 AB7 SER A  352  LEU A  378  1                                  27    
HELIX   17 AB8 GLY A  390  LYS A  394  5                                   5    
HELIX   18 AB9 ASN A  395  GLY A  407  1                                  13    
HELIX   19 AC1 GLU A  417  SER A  434  1                                  18    
SHEET    1 AA1 6 ILE A  35  GLU A  42  0                                        
SHEET    2 AA1 6 GLY A  23  ILE A  29 -1  N  VAL A  28   O  LYS A  36           
SHEET    3 AA1 6 LEU A  13  PHE A  19 -1  N  GLY A  16   O  THR A  27           
SHEET    4 AA1 6 VAL A  77  GLY A  84  1  O  SER A  78   N  LEU A  13           
SHEET    5 AA1 6 ILE A 229  CYS A 231  1  O  CYS A 231   N  ILE A  80           
SHEET    6 AA1 6 SER A 210  ASN A 213 -1  N  ILE A 211   O  VAL A 230           
SHEET    1 AA2 5 ILE A  35  GLU A  42  0                                        
SHEET    2 AA2 5 GLY A  23  ILE A  29 -1  N  VAL A  28   O  LYS A  36           
SHEET    3 AA2 5 LEU A  13  PHE A  19 -1  N  GLY A  16   O  THR A  27           
SHEET    4 AA2 5 VAL A  77  GLY A  84  1  O  SER A  78   N  LEU A  13           
SHEET    5 AA2 5 THR A 234  THR A 235  1  O  THR A 234   N  GLY A  84           
SHEET    1 AA3 2 THR A  89  ASN A  93  0                                        
SHEET    2 AA3 2 ALA A 151  HIS A 155 -1  O  LEU A 154   N  LEU A  90           
SHEET    1 AA4 2 VAL A 170  ASP A 172  0                                        
SHEET    2 AA4 2 LYS A 203  GLN A 205  1  O  LYS A 203   N  SER A 171           
SHEET    1 AA5 6 TYR A 278  LEU A 282  0                                        
SHEET    2 AA5 6 LYS A 285  SER A 292 -1  O  LEU A 287   N  HIS A 280           
SHEET    3 AA5 6 LEU A 260  SER A 266 -1  N  SER A 266   O  TRP A 286           
SHEET    4 AA5 6 LYS A 251  LEU A 256 -1  N  SER A 255   O  ALA A 261           
SHEET    5 AA5 6 GLU A 385  ALA A 389  1  O  LEU A 387   N  ALA A 252           
SHEET    6 AA5 6 VAL A 410  LYS A 412  1  O  LYS A 411   N  VAL A 386           
CISPEP   1 PHE A  335    PRO A  336          0         5.67                     
CISPEP   2 LEU A  347    PRO A  348          0        -3.71                     
SITE     1 AC1 12 GLY A 257  SER A 258  GLY A 296  ARG A 300                    
SITE     2 AC1 12 ASP A 305  LEU A 308  GLY A 390  GLY A 391                    
SITE     3 AC1 12 LYS A 394  ASN A 395  TRP A 398  HOH A 636                    
CRYST1   49.565   87.454   53.364  90.00  96.78  90.00 P 1 21 1      2          
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      0.020176  0.000000  0.002400        0.00000                         
SCALE2      0.000000  0.011435  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018871        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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