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Database: PDB
Entry: 3T10
LinkDB: 3T10
Original site: 3T10 
HEADER    CHAPERONE                               21-JUL-11   3T10              
TITLE     HSP90 N-TERMINAL DOMAIN BOUND TO ACP                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 9-236;                                        
COMPND   5 SYNONYM: HEAT SHOCK 86 KDA, HSP 86, HSP86, RENAL CARCINOMA ANTIGEN   
COMPND   6 NY-REN-38;                                                           
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: HSP90A, HSP90AA1, HSPC1, HSPCA;                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    CHAPERONE, ATPASE                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LI                                                                  
REVDAT   2   28-NOV-12 3T10    1       JRNL                                     
REVDAT   1   25-JAN-12 3T10    0                                                
JRNL        AUTH   J.LI,L.SUN,C.XU,F.YU,H.ZHOU,Y.ZHAO,J.ZHANG,J.CAI,C.MAO,      
JRNL        AUTH 2 L.TANG,Y.XU,J.HE                                             
JRNL        TITL   STRUCTURE INSIGHTS INTO MECHANISMS OF ATP HYDROLYSIS AND THE 
JRNL        TITL 2 ACTIVATION OF HUMAN HEAT-SHOCK PROTEIN 90.                   
JRNL        REF    ACTA BIOCHIM BIOPHYS SIN      V.  44   300 2012              
JRNL        REF  2 (SHANGHAI)                                                   
JRNL        REFN                   ISSN 1672-9145                               
JRNL        PMID   22318716                                                     
JRNL        DOI    10.1093/ABBS/GMS001                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.24 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
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) : 1.24                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.82                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 61534                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.158                           
REMARK   3   R VALUE            (WORKING SET) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.172                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.140                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1931                            
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 26.8248 -  2.6707    0.97     6271   209  0.1755 0.1719        
REMARK   3     2  2.6707 -  2.1201    1.00     6347   204  0.1584 0.1743        
REMARK   3     3  2.1201 -  1.8522    0.99     6263   203  0.1452 0.1613        
REMARK   3     4  1.8522 -  1.6829    0.98     6227   198  0.1296 0.1560        
REMARK   3     5  1.6829 -  1.5623    0.97     6132   203  0.1248 0.1538        
REMARK   3     6  1.5623 -  1.4702    0.95     6036   190  0.1220 0.1776        
REMARK   3     7  1.4702 -  1.3965    0.94     5872   192  0.1272 0.1577        
REMARK   3     8  1.3965 -  1.3357    0.91     5802   190  0.1538 0.1835        
REMARK   3     9  1.3357 -  1.2843    0.88     5508   184  0.1919 0.2333        
REMARK   3    10  1.2843 -  1.2400    0.82     5145   158  0.2458 0.2589        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.47                                          
REMARK   3   B_SOL              : 38.00                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.630           
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) : 0.23320                                              
REMARK   3    B22 (A**2) : 2.11170                                              
REMARK   3    B33 (A**2) : -2.34490                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.00460                                             
REMARK   3    B23 (A**2) : 0.00000                                              
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      :  0.012           1747                                  
REMARK   3   ANGLE     :  1.499           2362                                  
REMARK   3   CHIRALITY :  0.088            269                                  
REMARK   3   PLANARITY :  0.007            296                                  
REMARK   3   DIHEDRAL  : 17.636            654                                  
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 3T10 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-AUG-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB066900.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
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) : NULL                               
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63893                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.240                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : 0.05400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 42.8940                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 1YES                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20~25% (W/V) PEG 2000 MONOMETHYL         
REMARK 280  ETHER, 200MM MAGNESIUM CHLORIDE, 100MM SODIUM CACODYLATE PH 6.5,,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
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       22.48600            
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 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     ASP A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     GLU A   225                                                      
REMARK 465     ARG A   226                                                      
REMARK 465     ASP A   227                                                      
REMARK 465     LYS A   228                                                      
REMARK 465     GLU A   229                                                      
REMARK 465     VAL A   230                                                      
REMARK 465     SER A   231                                                      
REMARK 465     ASP A   232                                                      
REMARK 465     ASP A   233                                                      
REMARK 465     GLU A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     GLU A   236                                                      
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   OD1  ASP A    54     O    HOH A   621              1.84            
REMARK 500   O    HOH A   594     O    HOH A   621              1.97            
REMARK 500   O    HOH A   551     O    HOH A   557              2.02            
REMARK 500   O    HOH A   596     O    HOH A   621              2.13            
REMARK 500   O    HOH A   551     O    HOH A   684              2.15            
REMARK 500   O    HOH A   551     O    HOH A   584              2.19            
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    ALA A 166     -148.72     66.28                                   
REMARK 500    ARG A 182      139.78   -171.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 740        DISTANCE =  5.77 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ACP A 301   O3G                                                    
REMARK 620 2 ASN A  51   OD1 175.0                                              
REMARK 620 3 HOH A 516   O    89.5  88.5                                        
REMARK 620 4 ACP A 301   O2B  89.9  92.3 177.7                                  
REMARK 620 5 ACP A 301   O1A  96.6  88.1  91.6  86.2                            
REMARK 620 6 HOH A 527   O    92.5  83.1  95.2  87.0 168.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 401                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3T0H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3T0Z   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3T1K   RELATED DB: PDB                                   
DBREF  3T10 A    9   236  UNP    P07900   HS90A_HUMAN      9    236             
SEQRES   1 A  228  ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR PHE ALA          
SEQRES   2 A  228  PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU ILE ILE          
SEQRES   3 A  228  ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU ARG GLU          
SEQRES   4 A  228  LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS ILE ARG          
SEQRES   5 A  228  TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP SER GLY          
SEQRES   6 A  228  LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS GLN ASP          
SEQRES   7 A  228  ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY MET THR          
SEQRES   8 A  228  LYS ALA ASP LEU ILE ASN ASN LEU GLY THR ILE ALA LYS          
SEQRES   9 A  228  SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN ALA GLY          
SEQRES  10 A  228  ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL GLY PHE          
SEQRES  11 A  228  TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR VAL ILE          
SEQRES  12 A  228  THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP GLU SER          
SEQRES  13 A  228  SER ALA GLY GLY SER PHE THR VAL ARG THR ASP THR GLY          
SEQRES  14 A  228  GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU HIS LEU          
SEQRES  15 A  228  LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG ARG ILE          
SEQRES  16 A  228  LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE GLY TYR          
SEQRES  17 A  228  PRO ILE THR LEU PHE VAL GLU LYS GLU ARG ASP LYS GLU          
SEQRES  18 A  228  VAL SER ASP ASP GLU ALA GLU                                  
HET    ACP  A 301      41                                                       
HET     MG  A 401       1                                                       
HETNAM     ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER                     
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE                 
FORMUL   2  ACP    C11 H18 N5 O12 P3                                            
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  HOH   *242(H2 O)                                                    
HELIX    1   1 GLN A   23  THR A   36  1                                  14    
HELIX    2   2 GLU A   42  ASP A   66  1                                  25    
HELIX    3   3 PRO A   67  ASP A   71  5                                   5    
HELIX    4   4 THR A   99  LEU A  107  1                                   9    
HELIX    5   5 GLY A  114  ALA A  124  1                                  11    
HELIX    6   6 ASP A  127  GLY A  135  5                                   9    
HELIX    7   7 VAL A  136  LEU A  143  5                                   8    
HELIX    8   8 GLU A  192  LEU A  198  5                                   7    
HELIX    9   9 GLU A  199  SER A  211  1                                  13    
SHEET    1   A 8 GLU A  18  ALA A  21  0                                        
SHEET    2   A 8 SER A 169  THR A 174 -1  O  PHE A 170   N  PHE A  20           
SHEET    3   A 8 GLN A 159  SER A 164 -1  N  ALA A 161   O  ARG A 173           
SHEET    4   A 8 ALA A 145  LYS A 153 -1  N  VAL A 150   O  TRP A 162           
SHEET    5   A 8 GLY A 183  LEU A 190 -1  O  ILE A 187   N  THR A 149           
SHEET    6   A 8 THR A  88  ASP A  93 -1  N  LEU A  89   O  LEU A 188           
SHEET    7   A 8 ILE A  78  ASN A  83 -1  N  ASN A  79   O  VAL A  92           
SHEET    8   A 8 ILE A 218  LEU A 220  1  O  THR A 219   N  LEU A  80           
LINK         O3G ACP A 301                MG    MG A 401     1555   1555  1.95  
LINK         OD1 ASN A  51                MG    MG A 401     1555   1555  2.04  
LINK        MG    MG A 401                 O   HOH A 516     1555   1555  2.06  
LINK         O2B ACP A 301                MG    MG A 401     1555   1555  2.09  
LINK         O1A ACP A 301                MG    MG A 401     1555   1555  2.09  
LINK        MG    MG A 401                 O   HOH A 527     1555   1555  2.24  
SITE     1 AC1 26 GLU A  47  ASN A  51  ALA A  55  ASP A  93                    
SITE     2 AC1 26 MET A  98  ASN A 106  LEU A 107  GLY A 132                    
SITE     3 AC1 26 GLY A 135  VAL A 136  GLY A 137  PHE A 138                    
SITE     4 AC1 26 THR A 184   MG A 401  HOH A 502  HOH A 505                    
SITE     5 AC1 26 HOH A 510  HOH A 515  HOH A 516  HOH A 527                    
SITE     6 AC1 26 HOH A 615  HOH A 645  HOH A 648  HOH A 684                    
SITE     7 AC1 26 HOH A 689  HOH A 708                                          
SITE     1 AC2  4 ASN A  51  ACP A 301  HOH A 516  HOH A 527                    
CRYST1   53.170   44.972   53.854  90.00 115.15  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      0.018808  0.000000  0.008830        0.00000                         
SCALE2      0.000000  0.022236  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020513        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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