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Database: PDB
Entry: 3T2S
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Original site: 3T2S 
HEADER    CHAPERONE                               23-JUL-11   3T2S              
TITLE     HSP90 N-TERMINAL DOMAIN BOUND TO AGS                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;                           
COMPND   3 CHAIN: A, B;                                                         
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   1   25-JAN-12 3T2S    0                                                
JRNL        AUTH   J.LI                                                         
JRNL        TITL   HSP90 N-TERMINAL DOMAIN BOUND TO AGS                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
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) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.27                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.070                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 76450                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.560                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1955                            
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 41.2863 -  3.6180    0.94     5392   142  0.2090 0.2195        
REMARK   3     2  3.6180 -  2.8719    0.96     5531   144  0.1922 0.2235        
REMARK   3     3  2.8719 -  2.5090    0.92     5308   140  0.1980 0.2495        
REMARK   3     4  2.5090 -  2.2796    0.95     5468   142  0.1866 0.2149        
REMARK   3     5  2.2796 -  2.1162    0.95     5511   143  0.1818 0.2200        
REMARK   3     6  2.1162 -  1.9914    0.95     5434   142  0.1706 0.2469        
REMARK   3     7  1.9914 -  1.8917    0.94     5450   143  0.1563 0.2159        
REMARK   3     8  1.8917 -  1.8094    0.93     5318   139  0.1524 0.1823        
REMARK   3     9  1.8094 -  1.7397    0.93     5343   140  0.1607 0.2310        
REMARK   3    10  1.7397 -  1.6797    0.92     5372   140  0.1589 0.2276        
REMARK   3    11  1.6797 -  1.6271    0.90     5168   138  0.1615 0.2352        
REMARK   3    12  1.6271 -  1.5806    0.90     5227   132  0.1568 0.2423        
REMARK   3    13  1.5806 -  1.5390    0.89     5078   135  0.1704 0.1993        
REMARK   3    14  1.5390 -  1.5015    0.85     4895   135  0.2015 0.3008        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.95                                          
REMARK   3   K_SOL              : 0.40                                          
REMARK   3   B_SOL              : 45.15                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.060           
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) : 0.04960                                              
REMARK   3    B22 (A**2) : -0.73670                                             
REMARK   3    B33 (A**2) : 0.68710                                              
REMARK   3    B12 (A**2) : 1.51140                                              
REMARK   3    B13 (A**2) : -0.48020                                             
REMARK   3    B23 (A**2) : 1.14640                                              
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      :  0.013           3446                                  
REMARK   3   ANGLE     :  1.470           4660                                  
REMARK   3   CHIRALITY :  0.096            532                                  
REMARK   3   PLANARITY :  0.007            584                                  
REMARK   3   DIHEDRAL  : 18.065           1286                                  
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 3T2S 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 RCSB066964.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 8.5                                
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   : 78308                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
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     (%) : 94.8                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.26800                            
REMARK 200  R SYM                      (I) : 0.26800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.3760                             
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   (%): 52.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20~25% PEG 4000,  200MM MAGNESIUM        
REMARK 280  CHLORIDE, 100MM TRIS PH 8.5, VAPOR DIFFUSION, HANGING DROP          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     PRO A    11                                                      
REMARK 465     MET A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     GLU A    15                                                      
REMARK 465     GLU A    16                                                      
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 465     ASP B     9                                                      
REMARK 465     GLN B    10                                                      
REMARK 465     PRO B    11                                                      
REMARK 465     MET B    12                                                      
REMARK 465     GLU B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     GLU B    15                                                      
REMARK 465     GLU B    16                                                      
REMARK 465     LYS B   228                                                      
REMARK 465     GLU B   229                                                      
REMARK 465     VAL B   230                                                      
REMARK 465     SER B   231                                                      
REMARK 465     ASP B   232                                                      
REMARK 465     ASP B   233                                                      
REMARK 465     GLU B   234                                                      
REMARK 465     ALA B   235                                                      
REMARK 465     GLU B   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   O    HOH A   666     O    HOH A   735              2.08            
REMARK 500   O    HOH A   533     O    HOH A   588              2.11            
REMARK 500   O    HOH B   511     O    HOH B   544              2.13            
REMARK 500   O    HOH A   553     O    HOH A   646              2.15            
REMARK 500   O    HOH B   544     O    HOH B   642              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   732     O    HOH B   719     1654     1.76            
REMARK 500   OD2  ASP A   227     O    HOH A   666     1655     1.89            
REMARK 500   O    HOH A   533     O    HOH B   511     1545     2.17            
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     -149.82     68.61                                   
REMARK 500    ARG A 182      137.55   -175.07                                   
REMARK 500    VAL A 222       62.32   -112.06                                   
REMARK 500    GLU A 223      -16.26    157.33                                   
REMARK 500    ALA B 166     -152.32     68.83                                   
REMARK 500    ARG B 182      139.54   -174.89                                   
REMARK 500    VAL B 222     -103.19     38.53                                   
REMARK 500    GLU B 223       59.12    146.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL B 222        24.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 ASN A  51   OD1                                                    
REMARK 620 2 AGS A 301   O1A  91.7                                              
REMARK 620 3 AGS A 301   O2B  96.2  86.8                                        
REMARK 620 4 HOH A 503   O    87.6  91.7 175.9                                  
REMARK 620 5 HOH A 513   O    86.2 176.8  90.9  90.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 AGS B 301   O1A                                                    
REMARK 620 2 ASN B  51   OD1  92.7                                              
REMARK 620 3 AGS B 301   O2B  87.5  95.6                                        
REMARK 620 4 HOH B 505   O    91.0  87.0 177.1                                  
REMARK 620 5 HOH B 712   O   176.7  85.1  90.2  91.4                            
REMARK 620 6 HOH B 711   O    96.5 168.0  92.5  85.2  86.1                      
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 AGS 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 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 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: 3T10   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3T1K   RELATED DB: PDB                                   
DBREF  3T2S A    9   236  UNP    P07900   HS90A_HUMAN      9    236             
DBREF  3T2S B    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                                  
SEQRES   1 B  228  ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR PHE ALA          
SEQRES   2 B  228  PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU ILE ILE          
SEQRES   3 B  228  ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU ARG GLU          
SEQRES   4 B  228  LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS ILE ARG          
SEQRES   5 B  228  TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP SER GLY          
SEQRES   6 B  228  LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS GLN ASP          
SEQRES   7 B  228  ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY MET THR          
SEQRES   8 B  228  LYS ALA ASP LEU ILE ASN ASN LEU GLY THR ILE ALA LYS          
SEQRES   9 B  228  SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN ALA GLY          
SEQRES  10 B  228  ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL GLY PHE          
SEQRES  11 B  228  TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR VAL ILE          
SEQRES  12 B  228  THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP GLU SER          
SEQRES  13 B  228  SER ALA GLY GLY SER PHE THR VAL ARG THR ASP THR GLY          
SEQRES  14 B  228  GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU HIS LEU          
SEQRES  15 B  228  LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG ARG ILE          
SEQRES  16 B  228  LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE GLY TYR          
SEQRES  17 B  228  PRO ILE THR LEU PHE VAL GLU LYS GLU ARG ASP LYS GLU          
SEQRES  18 B  228  VAL SER ASP ASP GLU ALA GLU                                  
HET    AGS  A 301      31                                                       
HET     MG  A 401       1                                                       
HET    AGS  B 301      31                                                       
HET     MG  B 401       1                                                       
HETNAM     AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER                       
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     AGS ATP GAMMA-S                                                      
FORMUL   3  AGS    2(C10 H16 N5 O12 P3 S)                                       
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   7  HOH   *411(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    
HELIX   10  10 GLN B   23  THR B   36  1                                  14    
HELIX   11  11 GLU B   42  ASP B   66  1                                  25    
HELIX   12  12 PRO B   67  ASP B   71  5                                   5    
HELIX   13  13 THR B   99  LEU B  107  1                                   9    
HELIX   14  14 GLY B  114  ALA B  124  1                                  11    
HELIX   15  15 ASP B  127  GLY B  135  5                                   9    
HELIX   16  16 VAL B  136  LEU B  143  5                                   8    
HELIX   17  17 GLU B  192  LEU B  198  5                                   7    
HELIX   18  18 GLU B  199  SER B  211  1                                  13    
SHEET    1   A 9 GLU A  18  ALA A  21  0                                        
SHEET    2   A 9 SER A 169  THR A 174 -1  O  PHE A 170   N  PHE A  20           
SHEET    3   A 9 GLN A 159  SER A 164 -1  N  ALA A 161   O  ARG A 173           
SHEET    4   A 9 ALA A 145  LYS A 153 -1  N  VAL A 150   O  TRP A 162           
SHEET    5   A 9 GLY A 183  LEU A 190 -1  O  ILE A 187   N  THR A 149           
SHEET    6   A 9 THR A  88  ASP A  93 -1  N  ILE A  91   O  VAL A 186           
SHEET    7   A 9 ILE A  78  ASN A  83 -1  N  ASN A  79   O  VAL A  92           
SHEET    8   A 9 ILE A 218  LEU A 220  1  O  THR A 219   N  LEU A  80           
SHEET    9   A 9 LYS A 224  GLU A 225 -1  O  LYS A 224   N  LEU A 220           
SHEET    1   B 9 GLU B  18  ALA B  21  0                                        
SHEET    2   B 9 SER B 169  THR B 174 -1  O  PHE B 170   N  PHE B  20           
SHEET    3   B 9 GLN B 159  SER B 164 -1  N  ALA B 161   O  ARG B 173           
SHEET    4   B 9 ALA B 145  LYS B 153 -1  N  VAL B 150   O  TRP B 162           
SHEET    5   B 9 GLY B 183  LEU B 190 -1  O  ILE B 187   N  THR B 149           
SHEET    6   B 9 THR B  88  ASP B  93 -1  N  ILE B  91   O  VAL B 186           
SHEET    7   B 9 ILE B  78  ASN B  83 -1  N  ASN B  79   O  VAL B  92           
SHEET    8   B 9 ILE B 218  LEU B 220  1  O  THR B 219   N  LEU B  80           
SHEET    9   B 9 LYS B 224  ARG B 226 -1  O  ARG B 226   N  ILE B 218           
LINK         OD1 ASN A  51                MG    MG A 401     1555   1555  2.00  
LINK         O1A AGS B 301                MG    MG B 401     1555   1555  2.05  
LINK         O1A AGS A 301                MG    MG A 401     1555   1555  2.06  
LINK         O2B AGS A 301                MG    MG A 401     1555   1555  2.07  
LINK         OD1 ASN B  51                MG    MG B 401     1555   1555  2.08  
LINK         O2B AGS B 301                MG    MG B 401     1555   1555  2.08  
LINK        MG    MG A 401                 O   HOH A 503     1555   1555  2.05  
LINK        MG    MG B 401                 O   HOH B 505     1555   1555  2.08  
LINK        MG    MG A 401                 O   HOH A 513     1555   1555  2.16  
LINK        MG    MG B 401                 O   HOH B 712     1555   1555  2.17  
LINK        MG    MG B 401                 O   HOH B 711     1555   1555  2.19  
CISPEP   1 PHE A  221    VAL A  222          0        16.83                     
CISPEP   2 PHE B  221    VAL B  222          0       -25.56                     
SITE     1 AC1 27 GLU A  47  ASN A  51  ALA A  55  ASP A  93                    
SITE     2 AC1 27 MET A  98  ASN A 106  LEU A 107  GLY A 132                    
SITE     3 AC1 27 GLY A 135  VAL A 136  GLY A 137  PHE A 138                    
SITE     4 AC1 27 THR A 184   MG A 401  HOH A 502  HOH A 503                    
SITE     5 AC1 27 HOH A 506  HOH A 510  HOH A 513  HOH A 520                    
SITE     6 AC1 27 HOH A 569  HOH A 571  HOH A 578  HOH A 659                    
SITE     7 AC1 27 HOH A 681  HOH A 692  HOH A 721                               
SITE     1 AC2  4 ASN A  51  AGS A 301  HOH A 503  HOH A 513                    
SITE     1 AC3 24 ASN B  51  ALA B  55  ASP B  93  MET B  98                    
SITE     2 AC3 24 ASN B 106  LEU B 107  GLY B 135  VAL B 136                    
SITE     3 AC3 24 GLY B 137  PHE B 138  THR B 184   MG B 401                    
SITE     4 AC3 24 HOH B 501  HOH B 505  HOH B 506  HOH B 508                    
SITE     5 AC3 24 HOH B 552  HOH B 595  HOH B 621  HOH B 681                    
SITE     6 AC3 24 HOH B 700  HOH B 710  HOH B 711  HOH B 712                    
SITE     1 AC4  5 ASN B  51  AGS B 301  HOH B 505  HOH B 711                    
SITE     2 AC4  5 HOH B 712                                                     
CRYST1   43.237   55.939   60.550  93.61  95.60 112.61 P 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      0.023128  0.009632  0.003341        0.00000                         
SCALE2      0.000000  0.019365  0.002131        0.00000                         
SCALE3      0.000000  0.000000  0.016695        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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