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Database: PDB
Entry: 5FWM
LinkDB: 5FWM
Original site: 5FWM 
HEADER    CHAPERONE                               18-FEB-16   5FWM              
TITLE     ATOMIC CRYOEM STRUCTURE OF HSP90-CDC37-CDK4 COMPLEX                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK PROTEIN HSP 90 BETA;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HSP 90, HEAT SHOCK 84 KDA, HSP 84, HSP84, HEAT SHOCK PROTEIN
COMPND   5 HSP 90 BETA;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: HSP90 CO-CHAPERONE CDC37;                                  
COMPND   9 CHAIN: E;                                                            
COMPND  10 SYNONYM: HSP90 CHAPERONE PROTEIN KINASE-TARGETING SUBUNIT, P50CDC37; 
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: CYCLIN-DEPENDENT KINASE 4;                                 
COMPND  14 CHAIN: K;                                                            
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFASTBACHT;                               
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PFASTBACHT;                               
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  24 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  26 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  27 EXPRESSION_SYSTEM_PLASMID: PFASTBACHT                                
KEYWDS    HSP90, CDC37, CDK4, CHAPERONE, KINASE, UNFOLDING                      
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    K.A.VERBA,R.Y.R.WANG,A.ARAKAWA,Y.LIU,S.YOKOYAMA,D.A.AGARD             
REVDAT   3   02-AUG-17 5FWM    1                                                
REVDAT   2   19-APR-17 5FWM    1       REMARK                                   
REVDAT   1   06-JUL-16 5FWM    0                                                
JRNL        AUTH   K.A.VERBA,R.Y.WANG,A.ARAKAWA,Y.LIU,M.SHIROUZU,S.YOKOYAMA,    
JRNL        AUTH 2 D.A.AGARD                                                    
JRNL        TITL   ATOMIC STRUCTURE OF HSP90-CDC37-CDK4 REVEALS THAT HSP90      
JRNL        TITL 2 TRAPS AND STABILIZES AN UNFOLDED KINASE.                     
JRNL        REF    SCIENCE                       V. 352  1542 2016              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   27339980                                                     
JRNL        DOI    10.1126/SCIENCE.AAF5023                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    8.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : ROSETTA, UCSF CHIMERA, RELION             
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : OTHER                               
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : METHOD--ROSETTA                                  
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 8.000                          
REMARK   3   NUMBER OF PARTICLES               : 61981                          
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: THIS MODEL WAS BUILT BASED ON 5FWK WITH CDK4 N-LOBE   
REMARK   3  RIGID BODY FIT INTO THE EM DENSITY. THE MODEL WAS THEN MINIMIZED    
REMARK   3  IN ROSETTA. SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-    
REMARK   3  3342. (DEPOSITION ID: 14285).                                       
REMARK   4                                                                      
REMARK   4 5FWM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.                               
REMARK 100 THE DEPOSITION ID IS D_1290066255.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE                      
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : COMPLEX OF HUMAN HSP90BETA,       
REMARK 245                                    HUMAN CDC37 AND HUMAN CDK4        
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.27                              
REMARK 245   SAMPLE SUPPORT DETAILS         : HOLEY CARBON                      
REMARK 245   SAMPLE VITRIFICATION DETAILS   : LIQUID ETHANE                     
REMARK 245   SAMPLE BUFFER                  : 20MM TRIS-HCL (PH 7.5), 150 MM    
REMARK 245                                    NACL, 10 MM KCL, 10 MM MGCL2,     
REMARK 245                                    20 MM NA2MOO4, 2MM DTT, 0.085MM   
REMARK 245                                    DDM                               
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 25-NOV-14                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : 1400.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 3800.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 44.00                          
REMARK 245   ILLUMINATION MODE                 : OTHER                          
REMARK 245   NOMINAL MAGNIFICATION             : 22500                          
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, K                            
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     GLY A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     PHE A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     VAL A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     ASP A   227                                                      
REMARK 465     ASP A   228                                                      
REMARK 465     GLU A   229                                                      
REMARK 465     ALA A   230                                                      
REMARK 465     GLU A   231                                                      
REMARK 465     GLU A   232                                                      
REMARK 465     GLU A   233                                                      
REMARK 465     LYS A   234                                                      
REMARK 465     GLY A   235                                                      
REMARK 465     GLU A   236                                                      
REMARK 465     LYS A   237                                                      
REMARK 465     GLU A   238                                                      
REMARK 465     GLU A   239                                                      
REMARK 465     GLU A   240                                                      
REMARK 465     ASP A   241                                                      
REMARK 465     LYS A   242                                                      
REMARK 465     ASP A   243                                                      
REMARK 465     ASP A   244                                                      
REMARK 465     GLU A   245                                                      
REMARK 465     GLU A   246                                                      
REMARK 465     LYS A   247                                                      
REMARK 465     PRO A   248                                                      
REMARK 465     LYS A   249                                                      
REMARK 465     ILE A   250                                                      
REMARK 465     GLU A   251                                                      
REMARK 465     ASP A   252                                                      
REMARK 465     VAL A   253                                                      
REMARK 465     GLY A   254                                                      
REMARK 465     SER A   255                                                      
REMARK 465     ASP A   256                                                      
REMARK 465     GLU A   257                                                      
REMARK 465     GLU A   258                                                      
REMARK 465     ASP A   259                                                      
REMARK 465     ASP A   260                                                      
REMARK 465     SER A   261                                                      
REMARK 465     GLY A   262                                                      
REMARK 465     LYS A   263                                                      
REMARK 465     ASP A   264                                                      
REMARK 465     LYS A   265                                                      
REMARK 465     LYS A   266                                                      
REMARK 465     LYS A   267                                                      
REMARK 465     LYS A   268                                                      
REMARK 465     THR A   269                                                      
REMARK 465     ASP A   691                                                      
REMARK 465     GLU A   692                                                      
REMARK 465     ASP A   693                                                      
REMARK 465     GLU A   694                                                      
REMARK 465     VAL A   695                                                      
REMARK 465     ALA A   696                                                      
REMARK 465     ALA A   697                                                      
REMARK 465     GLU A   698                                                      
REMARK 465     GLU A   699                                                      
REMARK 465     PRO A   700                                                      
REMARK 465     ASN A   701                                                      
REMARK 465     ALA A   702                                                      
REMARK 465     ALA A   703                                                      
REMARK 465     VAL A   704                                                      
REMARK 465     PRO A   705                                                      
REMARK 465     ASP A   706                                                      
REMARK 465     GLU A   707                                                      
REMARK 465     ILE A   708                                                      
REMARK 465     PRO A   709                                                      
REMARK 465     PRO A   710                                                      
REMARK 465     LEU A   711                                                      
REMARK 465     GLU A   712                                                      
REMARK 465     GLY A   713                                                      
REMARK 465     ASP A   714                                                      
REMARK 465     GLU A   715                                                      
REMARK 465     ASP A   716                                                      
REMARK 465     ALA A   717                                                      
REMARK 465     SER A   718                                                      
REMARK 465     ARG A   719                                                      
REMARK 465     MET A   720                                                      
REMARK 465     GLU A   721                                                      
REMARK 465     GLU A   722                                                      
REMARK 465     VAL A   723                                                      
REMARK 465     ASP A   724                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     PHE B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     VAL B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     GLU B     9                                                      
REMARK 465     ARG B   221                                                      
REMARK 465     GLU B   222                                                      
REMARK 465     LYS B   223                                                      
REMARK 465     GLU B   224                                                      
REMARK 465     ILE B   225                                                      
REMARK 465     SER B   226                                                      
REMARK 465     ASP B   227                                                      
REMARK 465     ASP B   228                                                      
REMARK 465     GLU B   229                                                      
REMARK 465     ALA B   230                                                      
REMARK 465     GLU B   231                                                      
REMARK 465     GLU B   232                                                      
REMARK 465     GLU B   233                                                      
REMARK 465     LYS B   234                                                      
REMARK 465     GLY B   235                                                      
REMARK 465     GLU B   236                                                      
REMARK 465     LYS B   237                                                      
REMARK 465     GLU B   238                                                      
REMARK 465     GLU B   239                                                      
REMARK 465     GLU B   240                                                      
REMARK 465     ASP B   241                                                      
REMARK 465     LYS B   242                                                      
REMARK 465     ASP B   243                                                      
REMARK 465     ASP B   244                                                      
REMARK 465     GLU B   245                                                      
REMARK 465     GLU B   246                                                      
REMARK 465     LYS B   247                                                      
REMARK 465     PRO B   248                                                      
REMARK 465     LYS B   249                                                      
REMARK 465     ILE B   250                                                      
REMARK 465     GLU B   251                                                      
REMARK 465     ASP B   252                                                      
REMARK 465     VAL B   253                                                      
REMARK 465     GLY B   254                                                      
REMARK 465     SER B   255                                                      
REMARK 465     ASP B   256                                                      
REMARK 465     GLU B   257                                                      
REMARK 465     GLU B   258                                                      
REMARK 465     ASP B   259                                                      
REMARK 465     ASP B   260                                                      
REMARK 465     SER B   261                                                      
REMARK 465     GLY B   262                                                      
REMARK 465     LYS B   263                                                      
REMARK 465     ASP B   264                                                      
REMARK 465     LYS B   265                                                      
REMARK 465     LYS B   266                                                      
REMARK 465     LYS B   267                                                      
REMARK 465     LYS B   268                                                      
REMARK 465     THR B   269                                                      
REMARK 465     LYS B   270                                                      
REMARK 465     LYS B   271                                                      
REMARK 465     ILE B   272                                                      
REMARK 465     GLU B   692                                                      
REMARK 465     ASP B   693                                                      
REMARK 465     GLU B   694                                                      
REMARK 465     VAL B   695                                                      
REMARK 465     ALA B   696                                                      
REMARK 465     ALA B   697                                                      
REMARK 465     GLU B   698                                                      
REMARK 465     GLU B   699                                                      
REMARK 465     PRO B   700                                                      
REMARK 465     ASN B   701                                                      
REMARK 465     ALA B   702                                                      
REMARK 465     ALA B   703                                                      
REMARK 465     VAL B   704                                                      
REMARK 465     PRO B   705                                                      
REMARK 465     ASP B   706                                                      
REMARK 465     GLU B   707                                                      
REMARK 465     ILE B   708                                                      
REMARK 465     PRO B   709                                                      
REMARK 465     PRO B   710                                                      
REMARK 465     LEU B   711                                                      
REMARK 465     GLU B   712                                                      
REMARK 465     GLY B   713                                                      
REMARK 465     ASP B   714                                                      
REMARK 465     GLU B   715                                                      
REMARK 465     ASP B   716                                                      
REMARK 465     ALA B   717                                                      
REMARK 465     SER B   718                                                      
REMARK 465     ARG B   719                                                      
REMARK 465     MET B   720                                                      
REMARK 465     GLU B   721                                                      
REMARK 465     GLU B   722                                                      
REMARK 465     VAL B   723                                                      
REMARK 465     ASP B   724                                                      
REMARK 465     MET E     1                                                      
REMARK 465     GLU E   261                                                      
REMARK 465     ARG E   262                                                      
REMARK 465     VAL E   263                                                      
REMARK 465     ARG E   264                                                      
REMARK 465     GLY E   265                                                      
REMARK 465     ARG E   266                                                      
REMARK 465     ALA E   267                                                      
REMARK 465     LYS E   268                                                      
REMARK 465     LEU E   269                                                      
REMARK 465     ARG E   270                                                      
REMARK 465     ILE E   271                                                      
REMARK 465     GLU E   272                                                      
REMARK 465     LYS E   273                                                      
REMARK 465     ALA E   274                                                      
REMARK 465     MET E   275                                                      
REMARK 465     LYS E   276                                                      
REMARK 465     GLU E   277                                                      
REMARK 465     TYR E   278                                                      
REMARK 465     GLU E   279                                                      
REMARK 465     GLU E   280                                                      
REMARK 465     GLU E   281                                                      
REMARK 465     GLU E   282                                                      
REMARK 465     ARG E   283                                                      
REMARK 465     LYS E   284                                                      
REMARK 465     LYS E   285                                                      
REMARK 465     ARG E   286                                                      
REMARK 465     LEU E   287                                                      
REMARK 465     GLY E   288                                                      
REMARK 465     PRO E   289                                                      
REMARK 465     GLY E   290                                                      
REMARK 465     GLY E   291                                                      
REMARK 465     LEU E   292                                                      
REMARK 465     ASP E   293                                                      
REMARK 465     PRO E   294                                                      
REMARK 465     VAL E   295                                                      
REMARK 465     GLU E   296                                                      
REMARK 465     VAL E   297                                                      
REMARK 465     TYR E   298                                                      
REMARK 465     GLU E   299                                                      
REMARK 465     SER E   300                                                      
REMARK 465     LEU E   301                                                      
REMARK 465     PRO E   302                                                      
REMARK 465     GLU E   303                                                      
REMARK 465     GLU E   304                                                      
REMARK 465     LEU E   305                                                      
REMARK 465     GLN E   306                                                      
REMARK 465     LYS E   307                                                      
REMARK 465     CYS E   308                                                      
REMARK 465     PHE E   309                                                      
REMARK 465     ASP E   310                                                      
REMARK 465     VAL E   311                                                      
REMARK 465     LYS E   312                                                      
REMARK 465     ASP E   313                                                      
REMARK 465     VAL E   314                                                      
REMARK 465     GLN E   315                                                      
REMARK 465     MET E   316                                                      
REMARK 465     LEU E   317                                                      
REMARK 465     GLN E   318                                                      
REMARK 465     ASP E   319                                                      
REMARK 465     ALA E   320                                                      
REMARK 465     ILE E   321                                                      
REMARK 465     SER E   322                                                      
REMARK 465     LYS E   323                                                      
REMARK 465     MET E   324                                                      
REMARK 465     ASP E   325                                                      
REMARK 465     PRO E   326                                                      
REMARK 465     THR E   327                                                      
REMARK 465     ASP E   328                                                      
REMARK 465     ALA E   329                                                      
REMARK 465     LYS E   330                                                      
REMARK 465     TYR E   331                                                      
REMARK 465     HIS E   332                                                      
REMARK 465     MET E   333                                                      
REMARK 465     GLN E   334                                                      
REMARK 465     ARG E   335                                                      
REMARK 465     CYS E   336                                                      
REMARK 465     ILE E   337                                                      
REMARK 465     ASP E   338                                                      
REMARK 465     SER E   339                                                      
REMARK 465     GLY E   340                                                      
REMARK 465     LEU E   341                                                      
REMARK 465     TRP E   342                                                      
REMARK 465     VAL E   343                                                      
REMARK 465     PRO E   344                                                      
REMARK 465     ASN E   345                                                      
REMARK 465     SER E   346                                                      
REMARK 465     LYS E   347                                                      
REMARK 465     ALA E   348                                                      
REMARK 465     SER E   349                                                      
REMARK 465     GLU E   350                                                      
REMARK 465     ALA E   351                                                      
REMARK 465     LYS E   352                                                      
REMARK 465     GLU E   353                                                      
REMARK 465     GLY E   354                                                      
REMARK 465     GLU E   355                                                      
REMARK 465     GLU E   356                                                      
REMARK 465     ALA E   357                                                      
REMARK 465     GLY E   358                                                      
REMARK 465     PRO E   359                                                      
REMARK 465     GLY E   360                                                      
REMARK 465     ASP E   361                                                      
REMARK 465     PRO E   362                                                      
REMARK 465     LEU E   363                                                      
REMARK 465     LEU E   364                                                      
REMARK 465     GLU E   365                                                      
REMARK 465     ALA E   366                                                      
REMARK 465     VAL E   367                                                      
REMARK 465     PRO E   368                                                      
REMARK 465     LYS E   369                                                      
REMARK 465     THR E   370                                                      
REMARK 465     GLY E   371                                                      
REMARK 465     ASP E   372                                                      
REMARK 465     GLU E   373                                                      
REMARK 465     LYS E   374                                                      
REMARK 465     ASP E   375                                                      
REMARK 465     VAL E   376                                                      
REMARK 465     SER E   377                                                      
REMARK 465     VAL E   378                                                      
REMARK 465     GLY K    -6                                                      
REMARK 465     ALA K    -5                                                      
REMARK 465     MET K    -4                                                      
REMARK 465     ASP K    -3                                                      
REMARK 465     PRO K    -2                                                      
REMARK 465     GLU K    -1                                                      
REMARK 465     PHE K     0                                                      
REMARK 465     MET K     1                                                      
REMARK 465     ALA K     2                                                      
REMARK 465     THR K     3                                                      
REMARK 465     SER K     4                                                      
REMARK 465     HIS K   296                                                      
REMARK 465     LYS K   297                                                      
REMARK 465     ASP K   298                                                      
REMARK 465     GLU K   299                                                      
REMARK 465     GLY K   300                                                      
REMARK 465     ASN K   301                                                      
REMARK 465     PRO K   302                                                      
REMARK 465     GLU K   303                                                      
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   HB3  GLN B   609     HG3  ARG B   612              1.30            
REMARK 500   O    ASP E   245     H    MET E   249              1.54            
REMARK 500   O    THR K   277     HE   ARG K   283              1.58            
REMARK 500   HZ3  LYS E   132     OE2  GLU E   134              1.59            
REMARK 500   CE   MET B   606     CZ   ARG B   612              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  62   C   -  N   -  CA  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    PRO A  79   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    PRO A 336   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO A 387   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    PRO A 630   C   -  N   -  CA  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    PRO A 633   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    PRO A 673   C   -  N   -  CA  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    PRO B  62   C   -  N   -  CA  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    PRO B  79   C   -  N   -  CA  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    PRO B 293   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    PRO B 588   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    PRO B 630   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO B 633   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    PRO B 673   C   -  N   -  CA  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    PRO E 230   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    PRO K  40   C   -  N   -  CD  ANGL. DEV. = -18.4 DEGREES          
REMARK 500    PRO K 108   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    PRO K 109   C   -  N   -  CA  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    PRO K 110   C   -  N   -  CA  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    PRO K 233   C   -  N   -  CD  ANGL. DEV. = -15.0 DEGREES          
REMARK 500    PRO K 234   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    PRO K 251   C   -  N   -  CA  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    PRO K 254   C   -  N   -  CA  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    PRO K 256   C   -  N   -  CD  ANGL. DEV. = -17.5 DEGREES          
REMARK 500    PRO K 262   C   -  N   -  CA  ANGL. DEV. =   9.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  61       89.71   -152.66                                   
REMARK 500    ARG A  82       43.11     70.34                                   
REMARK 500    ALA A 106       42.13     70.25                                   
REMARK 500    GLN A 128       74.42   -172.34                                   
REMARK 500    ASP A 170      119.22    -37.85                                   
REMARK 500    PRO A 174       98.65    -34.37                                   
REMARK 500    HIS A 205      -33.02   -139.24                                   
REMARK 500    PHE A 208       51.07   -116.74                                   
REMARK 500    GLU A 281      -27.76    -38.59                                   
REMARK 500    ASN A 310       84.44    -68.57                                   
REMARK 500    GLU A 313      132.05   -173.81                                   
REMARK 500    HIS A 315      170.45    -58.12                                   
REMARK 500    ASN A 351       26.37   -162.30                                   
REMARK 500    PHE A 376      -19.55   -150.07                                   
REMARK 500    GLN A 397       72.32     62.77                                   
REMARK 500    VAL A 585      -68.98   -122.77                                   
REMARK 500    ASN A 614       86.83    -69.76                                   
REMARK 500    LYS A 623     -145.39    -93.61                                   
REMARK 500    ASP A 645      100.16   -170.29                                   
REMARK 500    ASP A 672       77.27   -171.40                                   
REMARK 500    ASN B  30      -47.40   -140.91                                   
REMARK 500    GLU B 274       82.90    -68.87                                   
REMARK 500    PHE B 376      -18.48   -151.43                                   
REMARK 500    GLN B 397       72.38     61.45                                   
REMARK 500    PRO B 544      123.46    -37.86                                   
REMARK 500    VAL B 585      -71.85   -122.86                                   
REMARK 500    CYS B 590      146.22   -170.03                                   
REMARK 500    ASP B 645       98.41   -170.96                                   
REMARK 500    ASP B 672       88.44   -152.70                                   
REMARK 500    ASP E  15       98.53    -68.60                                   
REMARK 500    MET E 128      126.94   -171.05                                   
REMARK 500    LYS E 132     -145.34    109.47                                   
REMARK 500    GLU E 134      111.49     78.10                                   
REMARK 500    LYS E 135      109.14    -39.44                                   
REMARK 500    ARG E 166      -40.25   -142.70                                   
REMARK 500    ASN E 178       55.66   -118.18                                   
REMARK 500    LYS E 202       58.95   -106.65                                   
REMARK 500    ASP E 245      147.97    -39.25                                   
REMARK 500    ALA K  10     -159.87   -141.78                                   
REMARK 500    PRO K  40     -143.99    -88.68                                   
REMARK 500    ASN K  41      -62.09   -153.56                                   
REMARK 500    ILE K  51     -110.47     53.54                                   
REMARK 500    SER K  52       75.65    170.57                                   
REMARK 500    ASP K  76      165.39     60.08                                   
REMARK 500    VAL K  77       25.09    -66.49                                   
REMARK 500    THR K  80      150.82    -49.11                                   
REMARK 500    THR K  83       86.72     73.25                                   
REMARK 500    ARG K  85       46.94     95.33                                   
REMARK 500    GLU K  86      -70.78    118.11                                   
REMARK 500    LYS K  88      114.17    166.28                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      66 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU K   86     ILE K   87                   41.73                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLU K  86        -20.06                                           
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 A1692  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A  46   OD1                                                    
REMARK 620 2 ATP A1691   O2B 127.1                                              
REMARK 620 3 ATP A1691   O2G 160.1  62.4                                        
REMARK 620 4 ATP A1691   O2A 116.2  64.0  48.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1693  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B  46   OD1                                                    
REMARK 620 2 ATP B1692   O1B 164.6                                              
REMARK 620 3 ATP B1692   O2B 113.7  72.6                                        
REMARK 620 4 ATP B1692   O2A 111.0  84.4  64.6                                  
REMARK 620 5 ATP B1692   PB  150.7  35.7  37.5  66.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 1691                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1692                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 1692                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1693                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5FWK   RELATED DB: PDB                                   
REMARK 900 ATOMIC CRYOEM STRUCTURE OF HSP90-CDC37-CDK4 COMPLEX                  
REMARK 900 RELATED ID: 5FWL   RELATED DB: PDB                                   
REMARK 900 ATOMIC CRYOEM STRUCTURE OF HSP90-CDC37-CDK4 COMPLEX                  
REMARK 900 RELATED ID: 5FWP   RELATED DB: PDB                                   
REMARK 900 ATOMIC CRYOEM STRUCTURE OF HSP90-CDC37-CDK4 COMPLEX                  
REMARK 900 RELATED ID: EMD-3342   RELATED DB: EMDB                              
REMARK 900 ATOMIC CRYOEM STRUCTURE OF HSP90-CDC37-CDK4 COMPLEX                  
DBREF  5FWM A    1   724  UNP    P08238   HS90B_HUMAN      1    724             
DBREF  5FWM B    1   724  UNP    P08238   HS90B_HUMAN      1    724             
DBREF  5FWM E    1   378  UNP    Q16543   CDC37_HUMAN      1    378             
DBREF  5FWM K    1   303  UNP    P11802   CDK4_HUMAN       1    303             
SEQADV 5FWM GLY A   -2  UNP  P08238              EXPRESSION TAG                 
SEQADV 5FWM GLY A   -1  UNP  P08238              EXPRESSION TAG                 
SEQADV 5FWM PHE A    0  UNP  P08238              EXPRESSION TAG                 
SEQADV 5FWM GLY B   -2  UNP  P08238              EXPRESSION TAG                 
SEQADV 5FWM GLY B   -1  UNP  P08238              EXPRESSION TAG                 
SEQADV 5FWM PHE B    0  UNP  P08238              EXPRESSION TAG                 
SEQADV 5FWM GLY K   -6  UNP  P11802              EXPRESSION TAG                 
SEQADV 5FWM ALA K   -5  UNP  P11802              EXPRESSION TAG                 
SEQADV 5FWM MET K   -4  UNP  P11802              EXPRESSION TAG                 
SEQADV 5FWM ASP K   -3  UNP  P11802              EXPRESSION TAG                 
SEQADV 5FWM PRO K   -2  UNP  P11802              EXPRESSION TAG                 
SEQADV 5FWM GLU K   -1  UNP  P11802              EXPRESSION TAG                 
SEQADV 5FWM PHE K    0  UNP  P11802              EXPRESSION TAG                 
SEQRES   1 A  727  GLY GLY PHE MET PRO GLU GLU VAL HIS HIS GLY GLU GLU          
SEQRES   2 A  727  GLU VAL GLU THR PHE ALA PHE GLN ALA GLU ILE ALA GLN          
SEQRES   3 A  727  LEU MET SER LEU ILE ILE ASN THR PHE TYR SER ASN LYS          
SEQRES   4 A  727  GLU ILE PHE LEU ARG GLU LEU ILE SER ASN ALA SER ASP          
SEQRES   5 A  727  ALA LEU ASP LYS ILE ARG TYR GLU SER LEU THR ASP PRO          
SEQRES   6 A  727  SER LYS LEU ASP SER GLY LYS GLU LEU LYS ILE ASP ILE          
SEQRES   7 A  727  ILE PRO ASN PRO GLN GLU ARG THR LEU THR LEU VAL ASP          
SEQRES   8 A  727  THR GLY ILE GLY MET THR LYS ALA ASP LEU ILE ASN ASN          
SEQRES   9 A  727  LEU GLY THR ILE ALA LYS SER GLY THR LYS ALA PHE MET          
SEQRES  10 A  727  GLU ALA LEU GLN ALA GLY ALA ASP ILE SER MET ILE GLY          
SEQRES  11 A  727  GLN PHE GLY VAL GLY PHE TYR SER ALA TYR LEU VAL ALA          
SEQRES  12 A  727  GLU LYS VAL VAL VAL ILE THR LYS HIS ASN ASP ASP GLU          
SEQRES  13 A  727  GLN TYR ALA TRP GLU SER SER ALA GLY GLY SER PHE THR          
SEQRES  14 A  727  VAL ARG ALA ASP HIS GLY GLU PRO ILE GLY ARG GLY THR          
SEQRES  15 A  727  LYS VAL ILE LEU HIS LEU LYS GLU ASP GLN THR GLU TYR          
SEQRES  16 A  727  LEU GLU GLU ARG ARG VAL LYS GLU VAL VAL LYS LYS HIS          
SEQRES  17 A  727  SER GLN PHE ILE GLY TYR PRO ILE THR LEU TYR LEU GLU          
SEQRES  18 A  727  LYS GLU ARG GLU LYS GLU ILE SER ASP ASP GLU ALA GLU          
SEQRES  19 A  727  GLU GLU LYS GLY GLU LYS GLU GLU GLU ASP LYS ASP ASP          
SEQRES  20 A  727  GLU GLU LYS PRO LYS ILE GLU ASP VAL GLY SER ASP GLU          
SEQRES  21 A  727  GLU ASP ASP SER GLY LYS ASP LYS LYS LYS LYS THR LYS          
SEQRES  22 A  727  LYS ILE LYS GLU LYS TYR ILE ASP GLN GLU GLU LEU ASN          
SEQRES  23 A  727  LYS THR LYS PRO ILE TRP THR ARG ASN PRO ASP ASP ILE          
SEQRES  24 A  727  THR GLN GLU GLU TYR GLY GLU PHE TYR LYS SER LEU THR          
SEQRES  25 A  727  ASN ASP TRP GLU ASP HIS LEU ALA VAL LYS HIS PHE SER          
SEQRES  26 A  727  VAL GLU GLY GLN LEU GLU PHE ARG ALA LEU LEU PHE ILE          
SEQRES  27 A  727  PRO ARG ARG ALA PRO PHE ASP LEU PHE GLU ASN LYS LYS          
SEQRES  28 A  727  LYS LYS ASN ASN ILE LYS LEU TYR VAL ARG ARG VAL PHE          
SEQRES  29 A  727  ILE MET ASP SER CYS ASP GLU LEU ILE PRO GLU TYR LEU          
SEQRES  30 A  727  ASN PHE ILE ARG GLY VAL VAL ASP SER GLU ASP LEU PRO          
SEQRES  31 A  727  LEU ASN ILE SER ARG GLU MET LEU GLN GLN SER LYS ILE          
SEQRES  32 A  727  LEU LYS VAL ILE ARG LYS ASN ILE VAL LYS LYS CYS LEU          
SEQRES  33 A  727  GLU LEU PHE SER GLU LEU ALA GLU ASP LYS GLU ASN TYR          
SEQRES  34 A  727  LYS LYS PHE TYR GLU ALA PHE SER LYS ASN LEU LYS LEU          
SEQRES  35 A  727  GLY ILE HIS GLU ASP SER THR ASN ARG ARG ARG LEU SER          
SEQRES  36 A  727  GLU LEU LEU ARG TYR HIS THR SER GLN SER GLY ASP GLU          
SEQRES  37 A  727  MET THR SER LEU SER GLU TYR VAL SER ARG MET LYS GLU          
SEQRES  38 A  727  THR GLN LYS SER ILE TYR TYR ILE THR GLY GLU SER LYS          
SEQRES  39 A  727  GLU GLN VAL ALA ASN SER ALA PHE VAL GLU ARG VAL ARG          
SEQRES  40 A  727  LYS ARG GLY PHE GLU VAL VAL TYR MET THR GLU PRO ILE          
SEQRES  41 A  727  ASP GLU TYR CYS VAL GLN GLN LEU LYS GLU PHE ASP GLY          
SEQRES  42 A  727  LYS SER LEU VAL SER VAL THR LYS GLU GLY LEU GLU LEU          
SEQRES  43 A  727  PRO GLU ASP GLU GLU GLU LYS LYS LYS MET GLU GLU SER          
SEQRES  44 A  727  LYS ALA LYS PHE GLU ASN LEU CYS LYS LEU MET LYS GLU          
SEQRES  45 A  727  ILE LEU ASP LYS LYS VAL GLU LYS VAL THR ILE SER ASN          
SEQRES  46 A  727  ARG LEU VAL SER SER PRO CYS CYS ILE VAL THR SER THR          
SEQRES  47 A  727  TYR GLY TRP THR ALA ASN MET GLU ARG ILE MET LYS ALA          
SEQRES  48 A  727  GLN ALA LEU ARG ASP ASN SER THR MET GLY TYR MET MET          
SEQRES  49 A  727  ALA LYS LYS HIS LEU GLU ILE ASN PRO ASP HIS PRO ILE          
SEQRES  50 A  727  VAL GLU THR LEU ARG GLN LYS ALA GLU ALA ASP LYS ASN          
SEQRES  51 A  727  ASP LYS ALA VAL LYS ASP LEU VAL VAL LEU LEU PHE GLU          
SEQRES  52 A  727  THR ALA LEU LEU SER SER GLY PHE SER LEU GLU ASP PRO          
SEQRES  53 A  727  GLN THR HIS SER ASN ARG ILE TYR ARG MET ILE LYS LEU          
SEQRES  54 A  727  GLY LEU GLY ILE ASP GLU ASP GLU VAL ALA ALA GLU GLU          
SEQRES  55 A  727  PRO ASN ALA ALA VAL PRO ASP GLU ILE PRO PRO LEU GLU          
SEQRES  56 A  727  GLY ASP GLU ASP ALA SER ARG MET GLU GLU VAL ASP              
SEQRES   1 B  727  GLY GLY PHE MET PRO GLU GLU VAL HIS HIS GLY GLU GLU          
SEQRES   2 B  727  GLU VAL GLU THR PHE ALA PHE GLN ALA GLU ILE ALA GLN          
SEQRES   3 B  727  LEU MET SER LEU ILE ILE ASN THR PHE TYR SER ASN LYS          
SEQRES   4 B  727  GLU ILE PHE LEU ARG GLU LEU ILE SER ASN ALA SER ASP          
SEQRES   5 B  727  ALA LEU ASP LYS ILE ARG TYR GLU SER LEU THR ASP PRO          
SEQRES   6 B  727  SER LYS LEU ASP SER GLY LYS GLU LEU LYS ILE ASP ILE          
SEQRES   7 B  727  ILE PRO ASN PRO GLN GLU ARG THR LEU THR LEU VAL ASP          
SEQRES   8 B  727  THR GLY ILE GLY MET THR LYS ALA ASP LEU ILE ASN ASN          
SEQRES   9 B  727  LEU GLY THR ILE ALA LYS SER GLY THR LYS ALA PHE MET          
SEQRES  10 B  727  GLU ALA LEU GLN ALA GLY ALA ASP ILE SER MET ILE GLY          
SEQRES  11 B  727  GLN PHE GLY VAL GLY PHE TYR SER ALA TYR LEU VAL ALA          
SEQRES  12 B  727  GLU LYS VAL VAL VAL ILE THR LYS HIS ASN ASP ASP GLU          
SEQRES  13 B  727  GLN TYR ALA TRP GLU SER SER ALA GLY GLY SER PHE THR          
SEQRES  14 B  727  VAL ARG ALA ASP HIS GLY GLU PRO ILE GLY ARG GLY THR          
SEQRES  15 B  727  LYS VAL ILE LEU HIS LEU LYS GLU ASP GLN THR GLU TYR          
SEQRES  16 B  727  LEU GLU GLU ARG ARG VAL LYS GLU VAL VAL LYS LYS HIS          
SEQRES  17 B  727  SER GLN PHE ILE GLY TYR PRO ILE THR LEU TYR LEU GLU          
SEQRES  18 B  727  LYS GLU ARG GLU LYS GLU ILE SER ASP ASP GLU ALA GLU          
SEQRES  19 B  727  GLU GLU LYS GLY GLU LYS GLU GLU GLU ASP LYS ASP ASP          
SEQRES  20 B  727  GLU GLU LYS PRO LYS ILE GLU ASP VAL GLY SER ASP GLU          
SEQRES  21 B  727  GLU ASP ASP SER GLY LYS ASP LYS LYS LYS LYS THR LYS          
SEQRES  22 B  727  LYS ILE LYS GLU LYS TYR ILE ASP GLN GLU GLU LEU ASN          
SEQRES  23 B  727  LYS THR LYS PRO ILE TRP THR ARG ASN PRO ASP ASP ILE          
SEQRES  24 B  727  THR GLN GLU GLU TYR GLY GLU PHE TYR LYS SER LEU THR          
SEQRES  25 B  727  ASN ASP TRP GLU ASP HIS LEU ALA VAL LYS HIS PHE SER          
SEQRES  26 B  727  VAL GLU GLY GLN LEU GLU PHE ARG ALA LEU LEU PHE ILE          
SEQRES  27 B  727  PRO ARG ARG ALA PRO PHE ASP LEU PHE GLU ASN LYS LYS          
SEQRES  28 B  727  LYS LYS ASN ASN ILE LYS LEU TYR VAL ARG ARG VAL PHE          
SEQRES  29 B  727  ILE MET ASP SER CYS ASP GLU LEU ILE PRO GLU TYR LEU          
SEQRES  30 B  727  ASN PHE ILE ARG GLY VAL VAL ASP SER GLU ASP LEU PRO          
SEQRES  31 B  727  LEU ASN ILE SER ARG GLU MET LEU GLN GLN SER LYS ILE          
SEQRES  32 B  727  LEU LYS VAL ILE ARG LYS ASN ILE VAL LYS LYS CYS LEU          
SEQRES  33 B  727  GLU LEU PHE SER GLU LEU ALA GLU ASP LYS GLU ASN TYR          
SEQRES  34 B  727  LYS LYS PHE TYR GLU ALA PHE SER LYS ASN LEU LYS LEU          
SEQRES  35 B  727  GLY ILE HIS GLU ASP SER THR ASN ARG ARG ARG LEU SER          
SEQRES  36 B  727  GLU LEU LEU ARG TYR HIS THR SER GLN SER GLY ASP GLU          
SEQRES  37 B  727  MET THR SER LEU SER GLU TYR VAL SER ARG MET LYS GLU          
SEQRES  38 B  727  THR GLN LYS SER ILE TYR TYR ILE THR GLY GLU SER LYS          
SEQRES  39 B  727  GLU GLN VAL ALA ASN SER ALA PHE VAL GLU ARG VAL ARG          
SEQRES  40 B  727  LYS ARG GLY PHE GLU VAL VAL TYR MET THR GLU PRO ILE          
SEQRES  41 B  727  ASP GLU TYR CYS VAL GLN GLN LEU LYS GLU PHE ASP GLY          
SEQRES  42 B  727  LYS SER LEU VAL SER VAL THR LYS GLU GLY LEU GLU LEU          
SEQRES  43 B  727  PRO GLU ASP GLU GLU GLU LYS LYS LYS MET GLU GLU SER          
SEQRES  44 B  727  LYS ALA LYS PHE GLU ASN LEU CYS LYS LEU MET LYS GLU          
SEQRES  45 B  727  ILE LEU ASP LYS LYS VAL GLU LYS VAL THR ILE SER ASN          
SEQRES  46 B  727  ARG LEU VAL SER SER PRO CYS CYS ILE VAL THR SER THR          
SEQRES  47 B  727  TYR GLY TRP THR ALA ASN MET GLU ARG ILE MET LYS ALA          
SEQRES  48 B  727  GLN ALA LEU ARG ASP ASN SER THR MET GLY TYR MET MET          
SEQRES  49 B  727  ALA LYS LYS HIS LEU GLU ILE ASN PRO ASP HIS PRO ILE          
SEQRES  50 B  727  VAL GLU THR LEU ARG GLN LYS ALA GLU ALA ASP LYS ASN          
SEQRES  51 B  727  ASP LYS ALA VAL LYS ASP LEU VAL VAL LEU LEU PHE GLU          
SEQRES  52 B  727  THR ALA LEU LEU SER SER GLY PHE SER LEU GLU ASP PRO          
SEQRES  53 B  727  GLN THR HIS SER ASN ARG ILE TYR ARG MET ILE LYS LEU          
SEQRES  54 B  727  GLY LEU GLY ILE ASP GLU ASP GLU VAL ALA ALA GLU GLU          
SEQRES  55 B  727  PRO ASN ALA ALA VAL PRO ASP GLU ILE PRO PRO LEU GLU          
SEQRES  56 B  727  GLY ASP GLU ASP ALA SER ARG MET GLU GLU VAL ASP              
SEQRES   1 E  378  MET VAL ASP TYR SER VAL TRP ASP HIS ILE GLU VAL SEP          
SEQRES   2 E  378  ASP ASP GLU ASP GLU THR HIS PRO ASN ILE ASP THR ALA          
SEQRES   3 E  378  SER LEU PHE ARG TRP ARG HIS GLN ALA ARG VAL GLU ARG          
SEQRES   4 E  378  MET GLU GLN PHE GLN LYS GLU LYS GLU GLU LEU ASP ARG          
SEQRES   5 E  378  GLY CYS ARG GLU CYS LYS ARG LYS VAL ALA GLU CYS GLN          
SEQRES   6 E  378  ARG LYS LEU LYS GLU LEU GLU VAL ALA GLU GLY GLY LYS          
SEQRES   7 E  378  ALA GLU LEU GLU ARG LEU GLN ALA GLU ALA GLN GLN LEU          
SEQRES   8 E  378  ARG LYS GLU GLU ARG SER TRP GLU GLN LYS LEU GLU GLU          
SEQRES   9 E  378  MET ARG LYS LYS GLU LYS SER MET PRO TRP ASN VAL ASP          
SEQRES  10 E  378  THR LEU SER LYS ASP GLY PHE SER LYS SER MET VAL ASN          
SEQRES  11 E  378  THR LYS PRO GLU LYS THR GLU GLU ASP SER GLU GLU VAL          
SEQRES  12 E  378  ARG GLU GLN LYS HIS LYS THR PHE VAL GLU LYS TYR GLU          
SEQRES  13 E  378  LYS GLN ILE LYS HIS PHE GLY MET LEU ARG ARG TRP ASP          
SEQRES  14 E  378  ASP SER GLN LYS TYR LEU SER ASP ASN VAL HIS LEU VAL          
SEQRES  15 E  378  CYS GLU GLU THR ALA ASN TYR LEU VAL ILE TRP CYS ILE          
SEQRES  16 E  378  ASP LEU GLU VAL GLU GLU LYS CYS ALA LEU MET GLU GLN          
SEQRES  17 E  378  VAL ALA HIS GLN THR ILE VAL MET GLN PHE ILE LEU GLU          
SEQRES  18 E  378  LEU ALA LYS SER LEU LYS VAL ASP PRO ARG ALA CYS PHE          
SEQRES  19 E  378  ARG GLN PHE PHE THR LYS ILE LYS THR ALA ASP ARG GLN          
SEQRES  20 E  378  TYR MET GLU GLY PHE ASN ASP GLU LEU GLU ALA PHE LYS          
SEQRES  21 E  378  GLU ARG VAL ARG GLY ARG ALA LYS LEU ARG ILE GLU LYS          
SEQRES  22 E  378  ALA MET LYS GLU TYR GLU GLU GLU GLU ARG LYS LYS ARG          
SEQRES  23 E  378  LEU GLY PRO GLY GLY LEU ASP PRO VAL GLU VAL TYR GLU          
SEQRES  24 E  378  SER LEU PRO GLU GLU LEU GLN LYS CYS PHE ASP VAL LYS          
SEQRES  25 E  378  ASP VAL GLN MET LEU GLN ASP ALA ILE SER LYS MET ASP          
SEQRES  26 E  378  PRO THR ASP ALA LYS TYR HIS MET GLN ARG CYS ILE ASP          
SEQRES  27 E  378  SER GLY LEU TRP VAL PRO ASN SER LYS ALA SER GLU ALA          
SEQRES  28 E  378  LYS GLU GLY GLU GLU ALA GLY PRO GLY ASP PRO LEU LEU          
SEQRES  29 E  378  GLU ALA VAL PRO LYS THR GLY ASP GLU LYS ASP VAL SER          
SEQRES  30 E  378  VAL                                                          
SEQRES   1 K  310  GLY ALA MET ASP PRO GLU PHE MET ALA THR SER ARG TYR          
SEQRES   2 K  310  GLU PRO VAL ALA GLU ILE GLY VAL GLY ALA TYR GLY THR          
SEQRES   3 K  310  VAL TYR LYS ALA ARG ASP PRO HIS SER GLY HIS PHE VAL          
SEQRES   4 K  310  ALA LEU LYS SER VAL ARG VAL PRO ASN GLY GLY GLY GLY          
SEQRES   5 K  310  GLY GLY GLY LEU PRO ILE SER THR VAL ARG GLU VAL ALA          
SEQRES   6 K  310  LEU LEU ARG ARG LEU GLU ALA PHE GLU HIS PRO ASN VAL          
SEQRES   7 K  310  VAL ARG LEU MET ASP VAL CYS ALA THR SER ARG THR ASP          
SEQRES   8 K  310  ARG GLU ILE LYS VAL THR LEU VAL PHE GLU HIS VAL ASP          
SEQRES   9 K  310  GLN ASP LEU ARG THR TYR LEU ASP LYS ALA PRO PRO PRO          
SEQRES  10 K  310  GLY LEU PRO ALA GLU THR ILE LYS ASP LEU MET ARG GLN          
SEQRES  11 K  310  PHE LEU ARG GLY LEU ASP PHE LEU HIS ALA ASN CYS ILE          
SEQRES  12 K  310  VAL HIS ARG ASP LEU LYS PRO GLU ASN ILE LEU VAL THR          
SEQRES  13 K  310  SER GLY GLY THR VAL LYS LEU ALA ASP PHE GLY LEU ALA          
SEQRES  14 K  310  ARG ILE TYR SER TYR GLN MET ALA LEU THR PRO VAL VAL          
SEQRES  15 K  310  VAL THR LEU TRP TYR ARG ALA PRO GLU VAL LEU LEU GLN          
SEQRES  16 K  310  SER THR TYR ALA THR PRO VAL ASP MET TRP SER VAL GLY          
SEQRES  17 K  310  CYS ILE PHE ALA GLU MET PHE ARG ARG LYS PRO LEU PHE          
SEQRES  18 K  310  CYS GLY ASN SER GLU ALA ASP GLN LEU GLY LYS ILE PHE          
SEQRES  19 K  310  ASP LEU ILE GLY LEU PRO PRO GLU ASP ASP TRP PRO ARG          
SEQRES  20 K  310  ASP VAL SER LEU PRO ARG GLY ALA PHE PRO PRO ARG GLY          
SEQRES  21 K  310  PRO ARG PRO VAL GLN SER VAL VAL PRO GLU MET GLU GLU          
SEQRES  22 K  310  SER GLY ALA GLN LEU LEU LEU GLU MET LEU THR PHE ASN          
SEQRES  23 K  310  PRO HIS LYS ARG ILE SER ALA PHE ARG ALA LEU GLN HIS          
SEQRES  24 K  310  SER TYR LEU HIS LYS ASP GLU GLY ASN PRO GLU                  
MODRES 5FWM SEP E   13  SER  PHOSPHOSERINE                                      
HET    SEP  E  13      14                                                       
HET    ATP  A1691      31                                                       
HET     MG  A1692       1                                                       
HET    ATP  B1692      31                                                       
HET     MG  B1693       1                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   3  SEP    C3 H8 N O6 P                                                 
FORMUL   5  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL   6   MG    2(MG 2+)                                                     
HELIX    1   1 GLU A   20  THR A   31  1                                  12    
HELIX    2   2 GLU A   37  ASP A   61  1                                  25    
HELIX    3   3 PRO A   62  ASP A   66  5                                   5    
HELIX    4   4 THR A   94  ASN A  101  1                                   8    
HELIX    5   5 GLY A  109  LEU A  117  1                                   9    
HELIX    6   6 VAL A  131  LEU A  138  5                                   8    
HELIX    7   7 GLN A  189  LEU A  193  5                                   5    
HELIX    8   8 GLU A  194  LYS A  203  1                                  10    
HELIX    9   9 GLU A  280  LYS A  284  5                                   5    
HELIX   10  10 ASN A  292  ILE A  296  5                                   5    
HELIX   11  11 THR A  297  THR A  309  1                                  13    
HELIX   12  12 SER A  365  ILE A  370  1                                   6    
HELIX   13  13 PRO A  371  ASN A  375  5                                   5    
HELIX   14  14 SER A  398  ASP A  422  1                                  25    
HELIX   15  15 ASP A  422  ASP A  444  1                                  23    
HELIX   16  16 ASN A  447  SER A  452  1                                   6    
HELIX   17  17 LEU A  469  ARG A  475  1                                   7    
HELIX   18  18 SER A  490  ALA A  495  1                                   6    
HELIX   19  19 ASN A  496  PHE A  499  5                                   4    
HELIX   20  20 VAL A  500  ARG A  506  1                                   7    
HELIX   21  21 GLU A  515  LEU A  525  1                                  11    
HELIX   22  22 ASP A  546  PHE A  560  1                                  15    
HELIX   23  23 PHE A  560  LEU A  571  1                                  12    
HELIX   24  24 ASN A  601  ALA A  610  1                                  10    
HELIX   25  25 ASN A  614  MET A  621  1                                   8    
HELIX   26  26 HIS A  632  ASP A  645  1                                  14    
HELIX   27  27 ASP A  648  SER A  666  1                                  19    
HELIX   28  28 ASP A  672  GLY A  689  1                                  18    
HELIX   29  29 GLU B   20  ILE B   29  1                                  10    
HELIX   30  30 ILE B   38  ASP B   61  1                                  24    
HELIX   31  31 PRO B   62  ASP B   66  5                                   5    
HELIX   32  32 THR B   94  ASN B  101  1                                   8    
HELIX   33  33 SER B  108  LEU B  117  1                                  10    
HELIX   34  34 GLN B  118  GLY B  120  5                                   3    
HELIX   35  35 VAL B  131  LEU B  138  5                                   8    
HELIX   36  36 GLU B  187  LEU B  193  5                                   7    
HELIX   37  37 GLU B  194  SER B  206  1                                  13    
HELIX   38  38 GLU B  280  LYS B  284  5                                   5    
HELIX   39  39 ASN B  292  ILE B  296  5                                   5    
HELIX   40  40 THR B  297  ASN B  310  1                                  14    
HELIX   41  41 SER B  365  ILE B  370  1                                   6    
HELIX   42  42 PRO B  371  ASN B  375  5                                   5    
HELIX   43  43 SER B  398  ASP B  422  1                                  25    
HELIX   44  44 ASP B  422  ASP B  444  1                                  23    
HELIX   45  45 ASN B  447  GLU B  453  1                                   7    
HELIX   46  46 LEU B  469  ARG B  475  1                                   7    
HELIX   47  47 SER B  490  ASN B  496  1                                   7    
HELIX   48  48 SER B  497  PHE B  499  5                                   3    
HELIX   49  49 VAL B  500  ARG B  506  1                                   7    
HELIX   50  50 ILE B  517  LEU B  525  1                                   9    
HELIX   51  51 ASP B  546  PHE B  560  1                                  15    
HELIX   52  52 PHE B  560  LEU B  571  1                                  12    
HELIX   53  53 THR B  599  ALA B  608  1                                  10    
HELIX   54  54 ASP B  613  MET B  620  5                                   8    
HELIX   55  55 HIS B  632  LYS B  646  1                                  15    
HELIX   56  56 ASP B  648  SER B  666  1                                  19    
HELIX   57  57 ASP B  672  GLY B  689  1                                  18    
HELIX   58  58 TYR E    4  ASP E    8  5                                   5    
HELIX   59  59 ASP E   24  ALA E   74  1                                  51    
HELIX   60  60 GLY E   77  MET E  112  1                                  36    
HELIX   61  61 ASP E  139  TYR E  155  1                                  17    
HELIX   62  62 TYR E  155  MET E  164  1                                  10    
HELIX   63  63 ARG E  167  ASN E  178  1                                  12    
HELIX   64  64 VAL E  179  VAL E  182  5                                   4    
HELIX   65  65 CYS E  183  GLU E  200  1                                  18    
HELIX   66  66 LYS E  202  LEU E  226  1                                  25    
HELIX   67  67 ASP E  229  CYS E  233  5                                   5    
HELIX   68  68 PHE E  234  LYS E  242  1                                   9    
HELIX   69  69 ASP E  245  LYS E  260  1                                  16    
HELIX   70  70 SER K   52  GLU K   67  1                                  16    
HELIX   71  71 ASP K   99  ALA K  107  1                                   9    
HELIX   72  72 PRO K  113  ASN K  134  1                                  22    
HELIX   73  73 LYS K  142  GLU K  144  5                                   3    
HELIX   74  74 GLY K  160  ILE K  164  5                                   5    
HELIX   75  75 ALA K  182  LEU K  187  1                                   6    
HELIX   76  76 ALA K  192  ARG K  210  1                                  19    
HELIX   77  77 SER K  218  GLY K  231  1                                  14    
HELIX   78  78 PRO K  256  VAL K  261  1                                   6    
HELIX   79  79 GLU K  265  THR K  277  1                                  13    
HELIX   80  80 SER K  285  GLN K  291  1                                   7    
SHEET    1  AA 9 GLU A  13  ALA A  16  0                                        
SHEET    2  AA 9 SER B 164  ALA B 169 -1  O  PHE B 165   N  PHE A  15           
SHEET    3  AA 9 GLN B 154  SER B 159 -1  O  ALA B 156   N  ARG B 168           
SHEET    4  AA 9 ALA B 140  LYS B 148 -1  O  VAL B 143   N  SER B 159           
SHEET    5  AA 9 THR B 179  LEU B 185 -1  O  LYS B 180   N  ILE B 146           
SHEET    6  AA 9 THR B  83  ASP B  88 -1  O  LEU B  84   N  LEU B 183           
SHEET    7  AA 9 ILE B  73  ASN B  78 -1  O  ASP B  74   N  VAL B  87           
SHEET    8  AA 9 ILE B 213  LYS B 219  1  O  THR B 214   N  ILE B  75           
SHEET    9  AA 9 LYS B 275  GLN B 279 -1  O  LYS B 275   N  LYS B 219           
SHEET    1  AB 2 GLN A  18  ALA A  19  0                                        
SHEET    2  AB 2 THR B 104  ILE B 105  1  N  ILE B 105   O  GLN A  18           
SHEET    1  AC 9 TYR A 276  ASP A 278  0                                        
SHEET    2  AC 9 ILE A 213  GLU A 218 -1  O  LEU A 217   N  ILE A 277           
SHEET    3  AC 9 ILE A  73  ASN A  78  1  O  ILE A  73   N  THR A 214           
SHEET    4  AC 9 THR A  83  ASP A  88 -1  O  THR A  83   N  ASN A  78           
SHEET    5  AC 9 THR A 179  LEU A 185 -1  O  THR A 179   N  ASP A  88           
SHEET    6  AC 9 ALA A 140  THR A 147 -1  N  GLU A 141   O  HIS A 184           
SHEET    7  AC 9 TYR A 155  SER A 159 -1  O  TYR A 155   N  THR A 147           
SHEET    8  AC 9 SER A 164  ALA A 169 -1  O  THR A 166   N  GLU A 158           
SHEET    9  AC 9 VAL B  12  ALA B  16 -1  O  GLU B  13   N  VAL A 167           
SHEET    1  AD 2 THR A 104  ILE A 105  0                                        
SHEET    2  AD 2 GLN B  18  ALA B  19  1  O  GLN B  18   N  ILE A 105           
SHEET    1  AE 5 ALA A 317  VAL A 323  0                                        
SHEET    2  AE 5 PHE A 329  ILE A 335 -1  O  PHE A 329   N  VAL A 323           
SHEET    3  AE 5 ARG A 378  SER A 383 -1  O  ARG A 378   N  PHE A 334           
SHEET    4  AE 5 ILE A 353  VAL A 357  1  O  LYS A 354   N  VAL A 381           
SHEET    5  AE 5 VAL A 360  MET A 363 -1  O  VAL A 360   N  VAL A 357           
SHEET    1  AF 6 MET A 466  SER A 468  0                                        
SHEET    2  AF 6 ARG A 456  THR A 459 -1  O  TYR A 457   N  THR A 467           
SHEET    3  AF 6 VAL A 510  MET A 513 -1  O  TYR A 512   N  HIS A 458           
SHEET    4  AF 6 SER A 482  THR A 487  1  O  TYR A 484   N  VAL A 511           
SHEET    5  AF 6 LYS A 531  SER A 535  1  O  SER A 532   N  ILE A 483           
SHEET    6  AF 6 GLU A 527  PHE A 528 -1  O  PHE A 528   N  LYS A 531           
SHEET    1  AG 3 LYS A 577  ILE A 580  0                                        
SHEET    2  AG 3 HIS A 625  ILE A 628  1  O  LEU A 626   N  THR A 579           
SHEET    3  AG 3 CYS A 589  VAL A 592 -1  O  CYS A 590   N  GLU A 627           
SHEET    1  BA 6 VAL B 360  MET B 363  0                                        
SHEET    2  BA 6 ILE B 353  VAL B 357 -1  O  LEU B 355   N  ILE B 362           
SHEET    3  BA 6 ARG B 378  SER B 383  1  O  GLY B 379   N  LYS B 354           
SHEET    4  BA 6 PHE B 329  ILE B 335 -1  O  ARG B 330   N  ASP B 382           
SHEET    5  BA 6 ALA B 317  GLY B 325 -1  O  ALA B 317   N  ILE B 335           
SHEET    6  BA 6 SER E 120  VAL E 129 -1  N  LYS E 121   O  GLU B 324           
SHEET    1  BB 6 THR B 467  SER B 468  0                                        
SHEET    2  BB 6 ARG B 456  THR B 459 -1  O  TYR B 457   N  THR B 467           
SHEET    3  BB 6 VAL B 510  MET B 513 -1  O  TYR B 512   N  HIS B 458           
SHEET    4  BB 6 SER B 482  THR B 487  1  O  TYR B 484   N  VAL B 511           
SHEET    5  BB 6 LYS B 531  SER B 535  1  O  SER B 532   N  ILE B 483           
SHEET    6  BB 6 GLU B 527  PHE B 528 -1  O  PHE B 528   N  LYS B 531           
SHEET    1  BC 3 LYS B 577  ILE B 580  0                                        
SHEET    2  BC 3 LYS B 624  ILE B 628  1  O  LEU B 626   N  THR B 579           
SHEET    3  BC 3 CYS B 589  THR B 593 -1  O  CYS B 590   N  GLU B 627           
SHEET    1  KA 3 GLU K   7  GLY K  15  0                                        
SHEET    2  KA 3 GLY K  18  ARG K  24 -1  O  GLY K  18   N  GLY K  15           
SHEET    3  KA 3 PHE K  31  LEU K  34 -1  O  VAL K  32   N  ALA K  23           
SHEET    1  KB 2 ILE K 146  VAL K 148  0                                        
SHEET    2  KB 2 VAL K 154  LEU K 156 -1  O  LYS K 155   N  LEU K 147           
LINK         OD1 ASN A  46                MG    MG A1692     1555   1555  1.25  
LINK         O2B ATP A1691                MG    MG A1692     1555   1555  1.99  
LINK         O2G ATP A1691                MG    MG A1692     1555   1555  2.63  
LINK         O2A ATP A1691                MG    MG A1692     1555   1555  2.06  
LINK         OD1 ASN B  46                MG    MG B1693     1555   1555  1.50  
LINK         O1B ATP B1692                MG    MG B1693     1555   1555  2.39  
LINK         O2B ATP B1692                MG    MG B1693     1555   1555  2.03  
LINK         O2A ATP B1692                MG    MG B1693     1555   1555  2.05  
LINK         PB  ATP B1692                MG    MG B1693     1555   1555  2.48  
LINK         C   VAL E  12                 N   SEP E  13     1555   1555  1.34  
LINK         C   SEP E  13                 N   ASP E  14     1555   1555  1.33  
CISPEP   1 LYS E  132    PRO E  133          0        -1.59                     
SITE     1 AC1 18 GLU A  42  ASN A  46  ALA A  50  ASP A  88                    
SITE     2 AC1 18 MET A  93  ASN A 101  SER A 108  GLY A 109                    
SITE     3 AC1 18 THR A 110  GLY A 127  GLN A 128  PHE A 129                    
SITE     4 AC1 18 GLY A 130  VAL A 131  GLY A 132  PHE A 133                    
SITE     5 AC1 18 THR A 179   MG A1692                                          
SITE     1 AC2  2 ASN A  46  ATP A1691                                          
SITE     1 AC3 20 GLU B  42  ASN B  46  ALA B  50  LYS B  53                    
SITE     2 AC3 20 ASP B  88  MET B  93  ASN B 101  SER B 108                    
SITE     3 AC3 20 GLY B 109  THR B 110  GLY B 127  GLN B 128                    
SITE     4 AC3 20 PHE B 129  GLY B 130  VAL B 131  GLY B 132                    
SITE     5 AC3 20 PHE B 133  THR B 179  ARG B 392   MG B1693                    
SITE     1 AC4  2 ASN B  46  ATP B1692                                          
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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