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Database: PDB
Entry: 6NHK
LinkDB: 6NHK
Original site: 6NHK 
HEADER    CHAPERONE                               23-DEC-18   6NHK              
TITLE     MORTALIN NUCLEOTIDE BINDING DOMAIN IN THE ADP-BOUND STATE             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: STRESS-70 PROTEIN, MITOCHONDRIAL;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: 75 KDA GLUCOSE-REGULATED PROTEIN,GRP-75,HEAT SHOCK 70 KDA   
COMPND   5 PROTEIN 9,MORTALIN,MOT,PEPTIDE-BINDING PROTEIN 74,PBP74;             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HSPA9, GRP75, HSPA9B, MT-HSP70;                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2(DE3)                             
KEYWDS    HSP70, MITOCHONDRIAL, CHAPERONE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.C.PAGE,M.A.MOSENG,J.C.NIX                                           
REVDAT   4   11-OCT-23 6NHK    1       LINK                                     
REVDAT   3   27-NOV-19 6NHK    1       REMARK                                   
REVDAT   2   08-MAY-19 6NHK    1       JRNL                                     
REVDAT   1   17-APR-19 6NHK    0                                                
JRNL        AUTH   M.A.MOSENG,J.C.NIX,R.C.PAGE                                  
JRNL        TITL   BIOPHYSICAL CONSEQUENCES OF EVEN-PLUS SYNDROME MUTATIONS FOR 
JRNL        TITL 2 THE FUNCTION OF MORTALIN.                                    
JRNL        REF    J.PHYS.CHEM.B                 V. 123  3383 2019              
JRNL        REFN                   ISSN 1089-5647                               
JRNL        PMID   30933555                                                     
JRNL        DOI    10.1021/ACS.JPCB.9B00071                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.78 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.13_2998                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.78                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.87                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 24273                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.259                           
REMARK   3   R VALUE            (WORKING SET) : 0.256                           
REMARK   3   FREE R VALUE                     : 0.296                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.190                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1989                            
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 56.8796 -  6.6907    0.99     1661   147  0.1715 0.2032        
REMARK   3     2  6.6907 -  5.3119    1.00     1631   146  0.2418 0.2717        
REMARK   3     3  5.3119 -  4.6408    1.00     1603   144  0.2325 0.2776        
REMARK   3     4  4.6408 -  4.2166    1.00     1602   143  0.2338 0.2762        
REMARK   3     5  4.2166 -  3.9144    1.00     1617   145  0.2531 0.2827        
REMARK   3     6  3.9144 -  3.6837    1.00     1595   143  0.2822 0.3050        
REMARK   3     7  3.6837 -  3.4992    1.00     1592   143  0.2916 0.3698        
REMARK   3     8  3.4992 -  3.3469    1.00     1585   141  0.3041 0.3688        
REMARK   3     9  3.3469 -  3.2181    1.00     1582   140  0.3103 0.3086        
REMARK   3    10  3.2181 -  3.1071    1.00     1604   142  0.3379 0.4333        
REMARK   3    11  3.1071 -  3.0099    0.99     1570   142  0.3578 0.3991        
REMARK   3    12  3.0099 -  2.9239    1.00     1590   143  0.3684 0.4244        
REMARK   3    13  2.9239 -  2.8469    0.99     1573   141  0.3926 0.4379        
REMARK   3    14  2.8469 -  2.7775    0.92     1479   129  0.4071 0.4524        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.540            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.200           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 73.51                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           5434                                  
REMARK   3   ANGLE     :  0.607           7424                                  
REMARK   3   CHIRALITY :  0.045            888                                  
REMARK   3   PLANARITY :  0.005            983                                  
REMARK   3   DIHEDRAL  : 12.630           1849                                  
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 6NHK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000238365.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 4.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NOIR-1                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24320                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.777                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.870                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.6100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.78                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3ATU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17 M AMMONIUM ACETATE, 0.085 M         
REMARK 280  SODIUM CITRATE:HCL PH 5.6, 25.5% (W/V) PEG 4000, 15% (V/V)          
REMARK 280  GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.0K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       88.63150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.05100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       88.63150            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       30.05100            
REMARK 290   SMTRY3   4  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 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 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     GLY A    47                                                      
REMARK 465     ALA A    48                                                      
REMARK 465     MET A    49                                                      
REMARK 465     GLY A    50                                                      
REMARK 465     SER A    51                                                      
REMARK 465     LYS A    52                                                      
REMARK 465     GLY A    53                                                      
REMARK 465     GLY B    47                                                      
REMARK 465     ALA B    48                                                      
REMARK 465     MET B    49                                                      
REMARK 465     GLY B    50                                                      
REMARK 465     SER B    51                                                      
REMARK 465     LYS B    52                                                      
REMARK 465     GLY B    53                                                      
REMARK 465     GLY B    72                                                      
REMARK 465     LYS B    73                                                      
REMARK 465     SER B   235                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  71    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  73    CG   CD   CE   NZ                                   
REMARK 470     GLN A  74    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  76    CG   CD   CE   NZ                                   
REMARK 470     GLU A  98    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 127    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 135    CG   CD   CE   NZ                                   
REMARK 470     ILE A 137    CG1  CG2  CD1                                       
REMARK 470     LYS A 143    CG   CD   CE   NZ                                   
REMARK 470     ILE A 144    CG1  CG2  CD1                                       
REMARK 470     ARG A 146    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 155    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 159    CG   CD   CE   NZ                                   
REMARK 470     LEU A 160    CG   CD1  CD2                                       
REMARK 470     LYS A 175    CG   CD   CE   NZ                                   
REMARK 470     LYS A 187    CG   CD   CE   NZ                                   
REMARK 470     LYS A 234    CG   CD   CE   NZ                                   
REMARK 470     GLU A 236    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 237    CG   OD1  OD2                                       
REMARK 470     LYS A 238    CG   CD   CE   NZ                                   
REMARK 470     ILE A 257    CG1  CG2  CD1                                       
REMARK 470     LYS A 259    CG   CD   CE   NZ                                   
REMARK 470     VAL A 261    CG1  CG2                                            
REMARK 470     GLU A 263    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 265    CG   CD   CE   NZ                                   
REMARK 470     LYS A 291    CG   CD   CE   NZ                                   
REMARK 470     ARG A 292    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 293    CG   CD   OE1  OE2                                  
REMARK 470     THR A 294    OG1  CG2                                            
REMARK 470     VAL A 296    CG1  CG2                                            
REMARK 470     LYS A 300    CG   CD   CE   NZ                                   
REMARK 470     GLN A 324    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 340    CG   CD   CE   NZ                                   
REMARK 470     LYS A 345    CG   CD   CE   NZ                                   
REMARK 470     ARG A 360    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO A 365    CG   CD                                             
REMARK 470     LYS A 368    CG   CD   CE   NZ                                   
REMARK 470     GLU A 374    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 375    CG1  CG2                                            
REMARK 470     LYS A 377    CG   CD   CE   NZ                                   
REMARK 470     LYS A 409    CG   CD   CE   NZ                                   
REMARK 470     GLN B  74    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  76    CG   CD   CE   NZ                                   
REMARK 470     GLU B  82    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  96    CG   OD1  OD2                                       
REMARK 470     ARG B 127    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 129    CG   OD1  OD2                                       
REMARK 470     GLU B 132    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 138    CG   CD   CE   NZ                                   
REMARK 470     LYS B 143    CG   CD   CE   NZ                                   
REMARK 470     ARG B 146    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 159    CG   CD   CE   NZ                                   
REMARK 470     LYS B 173    CG   CD   CE   NZ                                   
REMARK 470     LYS B 175    CG   CD   CE   NZ                                   
REMARK 470     LEU B 182    CG   CD1  CD2                                       
REMARK 470     LYS B 187    CG   CD   CE   NZ                                   
REMARK 470     LYS B 206    CG   CD   CE   NZ                                   
REMARK 470     ARG B 218    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO B 223    CG   CD                                             
REMARK 470     LEU B 232    CG   CD1  CD2                                       
REMARK 470     ASP B 233    CG   OD1  OD2                                       
REMARK 470     LYS B 234    CG   CD   CE   NZ                                   
REMARK 470     GLU B 236    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 237    CG   OD1  OD2                                       
REMARK 470     LYS B 238    CG   CD   CE   NZ                                   
REMARK 470     VAL B 239    CG1  CG2                                            
REMARK 470     ILE B 240    CG1  CG2  CD1                                       
REMARK 470     ILE B 252    CG1  CG2  CD1                                       
REMARK 470     LEU B 255    CG   CD1  CD2                                       
REMARK 470     GLU B 256    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 257    CG1  CG2  CD1                                       
REMARK 470     GLN B 258    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 259    CG   CD   CE   NZ                                   
REMARK 470     VAL B 261    CG1  CG2                                            
REMARK 470     GLU B 263    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 265    CG   CD   CE   NZ                                   
REMARK 470     ARG B 284    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 288    CG   CD   CE   NZ                                   
REMARK 470     LYS B 291    CG   CD   CE   NZ                                   
REMARK 470     LYS B 300    CG   CD   CE   NZ                                   
REMARK 470     ARG B 309    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B 334    CG   SD   CE                                        
REMARK 470     ASP B 335    CG   OD1  OD2                                       
REMARK 470     SER B 336    OG                                                  
REMARK 470     LYS B 340    CG   CD   CE   NZ                                   
REMARK 470     LYS B 345    CG   CD   CE   NZ                                   
REMARK 470     ASP B 357    CG   OD1  OD2                                       
REMARK 470     ARG B 360    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 363    CG1  CG2  CD1                                       
REMARK 470     PRO B 365    CG   CD                                             
REMARK 470     GLN B 367    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 368    CG   CD   CE   NZ                                   
REMARK 470     GLN B 371    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 374    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 375    CG1  CG2                                            
REMARK 470     SER B 376    OG                                                  
REMARK 470     LYS B 377    CG   CD   CE   NZ                                   
REMARK 470     SER B 378    OG                                                  
REMARK 470     ILE B 380    CG1  CG2  CD1                                       
REMARK 470     VAL B 383    CG1  CG2                                            
REMARK 470     VAL B 386    CG1  CG2                                            
REMARK 470     LEU B 402    CG   CD1  CD2                                       
REMARK 470     LYS B 409    CG   CD   CE   NZ                                   
REMARK 470     GLN B 424    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 427    CG1  CG2                                            
REMARK 470     LEU B 428    CG   CD1  CD2                                       
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    ASN A  80     -165.57    -77.50                                   
REMARK 500    ARG A 107        4.92    -69.27                                   
REMARK 500    ASN A 115       30.52    -90.52                                   
REMARK 500    TYR A 181      -63.60    -97.81                                   
REMARK 500    HIS A 184     -130.99     57.60                                   
REMARK 500    GLU A 236      -65.60    -94.71                                   
REMARK 500    LYS A 259       14.65     59.43                                   
REMARK 500    LYS A 409       46.85   -106.70                                   
REMARK 500    ASN B 112       74.14   -119.44                                   
REMARK 500    ASN B 115       30.67    -85.56                                   
REMARK 500    TYR B 181      -67.64    -95.15                                   
REMARK 500    HIS B 184     -154.25   -105.90                                   
REMARK 500    ALA B 186       78.75   -103.06                                   
REMARK 500    LYS B 259       18.10     56.06                                   
REMARK 500    TYR B 331       71.58     58.36                                   
REMARK 500    ASP B 335        5.93     82.49                                   
REMARK 500    LYS B 409       35.48    -98.44                                   
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 503  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 501   O1B                                                    
REMARK 620 2 PO4 A 502   O1   77.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 602  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 244   OD2                                                    
REMARK 620 2 ADP B 600   O1B 165.3                                              
REMARK 620 3 PO4 B 601   O1  114.0  80.7                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP B 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 602                  
DBREF  6NHK A   54   429  UNP    P38646   GRP75_HUMAN     54    429             
DBREF  6NHK B   54   429  UNP    P38646   GRP75_HUMAN     54    429             
SEQADV 6NHK GLY A   47  UNP  P38646              EXPRESSION TAG                 
SEQADV 6NHK ALA A   48  UNP  P38646              EXPRESSION TAG                 
SEQADV 6NHK MET A   49  UNP  P38646              EXPRESSION TAG                 
SEQADV 6NHK GLY A   50  UNP  P38646              EXPRESSION TAG                 
SEQADV 6NHK SER A   51  UNP  P38646              EXPRESSION TAG                 
SEQADV 6NHK LYS A   52  UNP  P38646              EXPRESSION TAG                 
SEQADV 6NHK GLY A   53  UNP  P38646              EXPRESSION TAG                 
SEQADV 6NHK GLY B   47  UNP  P38646              EXPRESSION TAG                 
SEQADV 6NHK ALA B   48  UNP  P38646              EXPRESSION TAG                 
SEQADV 6NHK MET B   49  UNP  P38646              EXPRESSION TAG                 
SEQADV 6NHK GLY B   50  UNP  P38646              EXPRESSION TAG                 
SEQADV 6NHK SER B   51  UNP  P38646              EXPRESSION TAG                 
SEQADV 6NHK LYS B   52  UNP  P38646              EXPRESSION TAG                 
SEQADV 6NHK GLY B   53  UNP  P38646              EXPRESSION TAG                 
SEQRES   1 A  383  GLY ALA MET GLY SER LYS GLY ALA VAL VAL GLY ILE ASP          
SEQRES   2 A  383  LEU GLY THR THR ASN SER CYS VAL ALA VAL MET GLU GLY          
SEQRES   3 A  383  LYS GLN ALA LYS VAL LEU GLU ASN ALA GLU GLY ALA ARG          
SEQRES   4 A  383  THR THR PRO SER VAL VAL ALA PHE THR ALA ASP GLY GLU          
SEQRES   5 A  383  ARG LEU VAL GLY MET PRO ALA LYS ARG GLN ALA VAL THR          
SEQRES   6 A  383  ASN PRO ASN ASN THR PHE TYR ALA THR LYS ARG LEU ILE          
SEQRES   7 A  383  GLY ARG ARG TYR ASP ASP PRO GLU VAL GLN LYS ASP ILE          
SEQRES   8 A  383  LYS ASN VAL PRO PHE LYS ILE VAL ARG ALA SER ASN GLY          
SEQRES   9 A  383  ASP ALA TRP VAL GLU ALA HIS GLY LYS LEU TYR SER PRO          
SEQRES  10 A  383  SER GLN ILE GLY ALA PHE VAL LEU MET LYS MET LYS GLU          
SEQRES  11 A  383  THR ALA GLU ASN TYR LEU GLY HIS THR ALA LYS ASN ALA          
SEQRES  12 A  383  VAL ILE THR VAL PRO ALA TYR PHE ASN ASP SER GLN ARG          
SEQRES  13 A  383  GLN ALA THR LYS ASP ALA GLY GLN ILE SER GLY LEU ASN          
SEQRES  14 A  383  VAL LEU ARG VAL ILE ASN GLU PRO THR ALA ALA ALA LEU          
SEQRES  15 A  383  ALA TYR GLY LEU ASP LYS SER GLU ASP LYS VAL ILE ALA          
SEQRES  16 A  383  VAL TYR ASP LEU GLY GLY GLY THR PHE ASP ILE SER ILE          
SEQRES  17 A  383  LEU GLU ILE GLN LYS GLY VAL PHE GLU VAL LYS SER THR          
SEQRES  18 A  383  ASN GLY ASP THR PHE LEU GLY GLY GLU ASP PHE ASP GLN          
SEQRES  19 A  383  ALA LEU LEU ARG HIS ILE VAL LYS GLU PHE LYS ARG GLU          
SEQRES  20 A  383  THR GLY VAL ASP LEU THR LYS ASP ASN MET ALA LEU GLN          
SEQRES  21 A  383  ARG VAL ARG GLU ALA ALA GLU LYS ALA LYS CYS GLU LEU          
SEQRES  22 A  383  SER SER SER VAL GLN THR ASP ILE ASN LEU PRO TYR LEU          
SEQRES  23 A  383  THR MET ASP SER SER GLY PRO LYS HIS LEU ASN MET LYS          
SEQRES  24 A  383  LEU THR ARG ALA GLN PHE GLU GLY ILE VAL THR ASP LEU          
SEQRES  25 A  383  ILE ARG ARG THR ILE ALA PRO CYS GLN LYS ALA MET GLN          
SEQRES  26 A  383  ASP ALA GLU VAL SER LYS SER ASP ILE GLY GLU VAL ILE          
SEQRES  27 A  383  LEU VAL GLY GLY MET THR ARG MET PRO LYS VAL GLN GLN          
SEQRES  28 A  383  THR VAL GLN ASP LEU PHE GLY ARG ALA PRO SER LYS ALA          
SEQRES  29 A  383  VAL ASN PRO ASP GLU ALA VAL ALA ILE GLY ALA ALA ILE          
SEQRES  30 A  383  GLN GLY GLY VAL LEU ALA                                      
SEQRES   1 B  383  GLY ALA MET GLY SER LYS GLY ALA VAL VAL GLY ILE ASP          
SEQRES   2 B  383  LEU GLY THR THR ASN SER CYS VAL ALA VAL MET GLU GLY          
SEQRES   3 B  383  LYS GLN ALA LYS VAL LEU GLU ASN ALA GLU GLY ALA ARG          
SEQRES   4 B  383  THR THR PRO SER VAL VAL ALA PHE THR ALA ASP GLY GLU          
SEQRES   5 B  383  ARG LEU VAL GLY MET PRO ALA LYS ARG GLN ALA VAL THR          
SEQRES   6 B  383  ASN PRO ASN ASN THR PHE TYR ALA THR LYS ARG LEU ILE          
SEQRES   7 B  383  GLY ARG ARG TYR ASP ASP PRO GLU VAL GLN LYS ASP ILE          
SEQRES   8 B  383  LYS ASN VAL PRO PHE LYS ILE VAL ARG ALA SER ASN GLY          
SEQRES   9 B  383  ASP ALA TRP VAL GLU ALA HIS GLY LYS LEU TYR SER PRO          
SEQRES  10 B  383  SER GLN ILE GLY ALA PHE VAL LEU MET LYS MET LYS GLU          
SEQRES  11 B  383  THR ALA GLU ASN TYR LEU GLY HIS THR ALA LYS ASN ALA          
SEQRES  12 B  383  VAL ILE THR VAL PRO ALA TYR PHE ASN ASP SER GLN ARG          
SEQRES  13 B  383  GLN ALA THR LYS ASP ALA GLY GLN ILE SER GLY LEU ASN          
SEQRES  14 B  383  VAL LEU ARG VAL ILE ASN GLU PRO THR ALA ALA ALA LEU          
SEQRES  15 B  383  ALA TYR GLY LEU ASP LYS SER GLU ASP LYS VAL ILE ALA          
SEQRES  16 B  383  VAL TYR ASP LEU GLY GLY GLY THR PHE ASP ILE SER ILE          
SEQRES  17 B  383  LEU GLU ILE GLN LYS GLY VAL PHE GLU VAL LYS SER THR          
SEQRES  18 B  383  ASN GLY ASP THR PHE LEU GLY GLY GLU ASP PHE ASP GLN          
SEQRES  19 B  383  ALA LEU LEU ARG HIS ILE VAL LYS GLU PHE LYS ARG GLU          
SEQRES  20 B  383  THR GLY VAL ASP LEU THR LYS ASP ASN MET ALA LEU GLN          
SEQRES  21 B  383  ARG VAL ARG GLU ALA ALA GLU LYS ALA LYS CYS GLU LEU          
SEQRES  22 B  383  SER SER SER VAL GLN THR ASP ILE ASN LEU PRO TYR LEU          
SEQRES  23 B  383  THR MET ASP SER SER GLY PRO LYS HIS LEU ASN MET LYS          
SEQRES  24 B  383  LEU THR ARG ALA GLN PHE GLU GLY ILE VAL THR ASP LEU          
SEQRES  25 B  383  ILE ARG ARG THR ILE ALA PRO CYS GLN LYS ALA MET GLN          
SEQRES  26 B  383  ASP ALA GLU VAL SER LYS SER ASP ILE GLY GLU VAL ILE          
SEQRES  27 B  383  LEU VAL GLY GLY MET THR ARG MET PRO LYS VAL GLN GLN          
SEQRES  28 B  383  THR VAL GLN ASP LEU PHE GLY ARG ALA PRO SER LYS ALA          
SEQRES  29 B  383  VAL ASN PRO ASP GLU ALA VAL ALA ILE GLY ALA ALA ILE          
SEQRES  30 B  383  GLN GLY GLY VAL LEU ALA                                      
HET    ADP  A 501      27                                                       
HET    PO4  A 502       5                                                       
HET     MG  A 503       1                                                       
HET    GOL  A 504       6                                                       
HET    ADP  B 600      27                                                       
HET    PO4  B 601       5                                                       
HET     MG  B 602       1                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  ADP    2(C10 H15 N5 O10 P2)                                         
FORMUL   4  PO4    2(O4 P 3-)                                                   
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   6  GOL    C3 H8 O3                                                     
FORMUL  10  HOH   *8(H2 O)                                                      
HELIX    1 AA1 GLY A  102  ARG A  107  1                                   6    
HELIX    2 AA2 THR A  120  LEU A  123  5                                   4    
HELIX    3 AA3 ASP A  130  ASN A  139  1                                  10    
HELIX    4 AA4 SER A  162  GLY A  183  1                                  22    
HELIX    5 AA5 ASN A  198  SER A  212  1                                  15    
HELIX    6 AA6 GLU A  222  TYR A  230  1                                   9    
HELIX    7 AA7 GLY A  231  SER A  235  5                                   5    
HELIX    8 AA8 GLY A  274  ARG A  292  1                                  19    
HELIX    9 AA9 ASP A  297  LYS A  300  5                                   4    
HELIX   10 AB1 ASP A  301  LEU A  319  1                                  19    
HELIX   11 AB2 ARG A  348  VAL A  355  1                                   8    
HELIX   12 AB3 VAL A  355  ARG A  361  1                                   7    
HELIX   13 AB4 THR A  362  ALA A  373  1                                  12    
HELIX   14 AB5 GLY A  387  ARG A  391  5                                   5    
HELIX   15 AB6 MET A  392  GLY A  404  1                                  13    
HELIX   16 AB7 GLU A  415  ALA A  429  1                                  15    
HELIX   17 AB8 GLY B  102  ARG B  107  1                                   6    
HELIX   18 AB9 THR B  120  LEU B  123  5                                   4    
HELIX   19 AC1 ASP B  130  ASN B  139  1                                  10    
HELIX   20 AC2 SER B  162  LEU B  182  1                                  21    
HELIX   21 AC3 ASN B  198  GLY B  213  1                                  16    
HELIX   22 AC4 GLU B  222  TYR B  230  1                                   9    
HELIX   23 AC5 GLY B  274  GLY B  295  1                                  22    
HELIX   24 AC6 ASP B  297  LYS B  300  5                                   4    
HELIX   25 AC7 ASP B  301  LEU B  319  1                                  19    
HELIX   26 AC8 ARG B  348  VAL B  355  1                                   8    
HELIX   27 AC9 VAL B  355  ARG B  361  1                                   7    
HELIX   28 AD1 THR B  362  GLU B  374  1                                  13    
HELIX   29 AD2 GLY B  387  ARG B  391  5                                   5    
HELIX   30 AD3 MET B  392  GLY B  404  1                                  13    
HELIX   31 AD4 GLU B  415  ALA B  429  1                                  15    
SHEET    1 AA1 3 GLN A  74  VAL A  77  0                                        
SHEET    2 AA1 3 ASN A  64  GLU A  71 -1  N  GLU A  71   O  GLN A  74           
SHEET    3 AA1 3 THR A  87  PRO A  88 -1  O  THR A  87   N  SER A  65           
SHEET    1 AA2 5 GLN A  74  VAL A  77  0                                        
SHEET    2 AA2 5 ASN A  64  GLU A  71 -1  N  GLU A  71   O  GLN A  74           
SHEET    3 AA2 5 VAL A  55  ASP A  59 -1  N  GLY A  57   O  ALA A  68           
SHEET    4 AA2 5 ASN A 188  VAL A 193  1  O  VAL A 190   N  ILE A  58           
SHEET    5 AA2 5 ASN A 215  ASN A 221  1  O  ASN A 215   N  ALA A 189           
SHEET    1 AA3 3 ARG A  99  VAL A 101  0                                        
SHEET    2 AA3 3 VAL A  90  PHE A  93 -1  N  ALA A  92   O  LEU A 100           
SHEET    3 AA3 3 THR A 116  TYR A 118 -1  O  PHE A 117   N  VAL A  91           
SHEET    1 AA4 3 LYS A 143  ARG A 146  0                                        
SHEET    2 AA4 3 ALA A 152  ALA A 156 -1  O  TRP A 153   N  VAL A 145           
SHEET    3 AA4 3 LYS A 159  TYR A 161 -1  O  TYR A 161   N  VAL A 154           
SHEET    1 AA5 4 VAL A 261  ASP A 270  0                                        
SHEET    2 AA5 4 PHE A 250  GLN A 258 -1  N  PHE A 250   O  ASP A 270           
SHEET    3 AA5 4 ASP A 237  LEU A 245 -1  N  ILE A 240   O  LEU A 255           
SHEET    4 AA5 4 ILE A 380  VAL A 386  1  O  VAL A 386   N  TYR A 243           
SHEET    1 AA6 2 GLN A 324  MET A 334  0                                        
SHEET    2 AA6 2 PRO A 339  THR A 347 -1  O  LEU A 342   N  LEU A 329           
SHEET    1 AA7 3 LYS B  76  VAL B  77  0                                        
SHEET    2 AA7 3 ASN B  64  VAL B  69 -1  N  VAL B  69   O  LYS B  76           
SHEET    3 AA7 3 THR B  87  PRO B  88 -1  O  THR B  87   N  SER B  65           
SHEET    1 AA8 5 LYS B  76  VAL B  77  0                                        
SHEET    2 AA8 5 ASN B  64  VAL B  69 -1  N  VAL B  69   O  LYS B  76           
SHEET    3 AA8 5 VAL B  55  ASP B  59 -1  N  GLY B  57   O  ALA B  68           
SHEET    4 AA8 5 ASN B 188  VAL B 193  1  O  VAL B 190   N  ILE B  58           
SHEET    5 AA8 5 ASN B 215  ASN B 221  1  O  ASN B 215   N  ALA B 189           
SHEET    1 AA9 3 ARG B  99  VAL B 101  0                                        
SHEET    2 AA9 3 VAL B  90  PHE B  93 -1  N  ALA B  92   O  LEU B 100           
SHEET    3 AA9 3 THR B 116  TYR B 118 -1  O  PHE B 117   N  VAL B  91           
SHEET    1 AB1 3 LYS B 143  ARG B 146  0                                        
SHEET    2 AB1 3 ALA B 152  ALA B 156 -1  O  TRP B 153   N  VAL B 145           
SHEET    3 AB1 3 LYS B 159  TYR B 161 -1  O  TYR B 161   N  VAL B 154           
SHEET    1 AB2 4 VAL B 261  ASN B 268  0                                        
SHEET    2 AB2 4 PHE B 250  GLN B 258 -1  N  ILE B 254   O  LYS B 265           
SHEET    3 AB2 4 LYS B 238  LEU B 245 -1  N  VAL B 242   O  SER B 253           
SHEET    4 AB2 4 ILE B 380  VAL B 386  1  O  GLY B 381   N  VAL B 239           
SHEET    1 AB3 2 GLN B 324  THR B 333  0                                        
SHEET    2 AB3 2 LYS B 340  THR B 347 -1  O  LEU B 346   N  THR B 325           
LINK         O1B ADP A 501                MG    MG A 503     1555   1555  2.35  
LINK         O1  PO4 A 502                MG    MG A 503     1555   1555  1.80  
LINK         OD2 ASP B 244                MG    MG B 602     1555   1555  2.92  
LINK         O1B ADP B 600                MG    MG B 602     1555   1555  2.39  
LINK         O1  PO4 B 601                MG    MG B 602     1555   1555  2.06  
CISPEP   1 SER B  337    GLY B  338          0        19.57                     
SITE     1 AC1 14 THR A  63  ASN A  64  GLY A 247  GLU A 313                    
SITE     2 AC1 14 LYS A 316  CYS A 317  SER A 320  GLY A 388                    
SITE     3 AC1 14 MET A 389  ARG A 391  ASP A 414  PO4 A 502                    
SITE     4 AC1 14  MG A 503  HOH A 605                                          
SITE     1 AC2  8 GLY A  61  THR A  62  LYS A 121  GLU A 222                    
SITE     2 AC2  8 THR A 249  ASP A 251  ADP A 501   MG A 503                    
SITE     1 AC3  3 ASP A 244  ADP A 501  PO4 A 502                               
SITE     1 AC4  6 TYR A 196  ASP A 251  THR A 267  ASN A 268                    
SITE     2 AC4  6 GLY A 269  HOH A 601                                          
SITE     1 AC5 15 THR B  63  ASN B  64  GLY B 246  GLY B 247                    
SITE     2 AC5 15 GLU B 313  LYS B 316  CYS B 317  SER B 320                    
SITE     3 AC5 15 GLY B 387  GLY B 388  MET B 389  ARG B 391                    
SITE     4 AC5 15 ASP B 414  PO4 B 601   MG B 602                               
SITE     1 AC6  8 GLY B  61  THR B  62  LYS B 121  GLU B 222                    
SITE     2 AC6  8 THR B 249  ASP B 251  ADP B 600   MG B 602                    
SITE     1 AC7  3 ASP B 244  ADP B 600  PO4 B 601                               
CRYST1  177.263   60.102   91.699  90.00  97.56  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005641  0.000000  0.000749        0.00000                         
SCALE2      0.000000  0.016638  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011001        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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