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Database: PDB
Entry: 2QWM
LinkDB: 2QWM
Original site: 2QWM 
HEADER    CHAPERONE                               10-AUG-07   2QWM              
TITLE     CRYSTAL STRUCTURE OF BOVINE HSC70 (1-394AA)IN THE ADP*VI STATE        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK COGNATE 71 KDA PROTEIN;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HEAT SHOCK 70 KDA PROTEIN 8;                                
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 GENE: HSPA8, HSC70;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRSET                                     
KEYWDS    CHAPERONE, ATP-BINDING, NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHORYLATION, 
KEYWDS   2 STRESS RESPONSE                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.JIANG,E.G.MAES,L.WANG,A.B.TAYLOR,A.P.HINCK,E.M.LAFER,R.SOUSA        
REVDAT   4   25-OCT-17 2QWM    1       REMARK                                   
REVDAT   3   13-JUL-11 2QWM    1       VERSN                                    
REVDAT   2   24-FEB-09 2QWM    1       VERSN                                    
REVDAT   1   18-DEC-07 2QWM    0                                                
JRNL        AUTH   J.JIANG,E.G.MAES,A.B.TAYLOR,L.WANG,A.P.HINCK,E.M.LAFER,      
JRNL        AUTH 2 R.SOUSA                                                      
JRNL        TITL   STRUCTURAL BASIS OF J COCHAPERONE BINDING AND REGULATION OF  
JRNL        TITL 2 HSP70.                                                       
JRNL        REF    MOL.CELL                      V.  28   422 2007              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   17996706                                                     
JRNL        DOI    10.1016/J.MOLCEL.2007.08.022                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.86 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.06                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 70206                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3541                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.86                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4913                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.69                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 257                          
REMARK   3   BIN FREE R VALUE                    : 0.3130                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5898                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 76                                      
REMARK   3   SOLVENT ATOMS            : 359                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.139         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.130         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.086         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.135         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.927                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6063 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8199 ; 1.173 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   760 ; 4.917 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   278 ;35.631 ;24.317       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1060 ;12.226 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;14.679 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   932 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4538 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2763 ; 0.193 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4215 ; 0.297 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   425 ; 0.116 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.124 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    63 ; 0.151 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    21 ; 0.178 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3774 ; 0.454 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6080 ; 0.839 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2327 ; 1.728 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2119 ; 2.740 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2QWM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-SEP-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000044136.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUL-06                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, D*TREK                      
REMARK 200  DATA SCALING SOFTWARE          : D*TREK, SCALEPACK                  
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70267                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.860                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, CALCIUM ACETATE, PH 8.0,        
REMARK 280  MICROBATCH UNDER OIL, TEMPERATURE 289K                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       38.92050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     SER A   385                                                      
REMARK 465     GLU A   386                                                      
REMARK 465     ASN A   387                                                      
REMARK 465     VAL A   388                                                      
REMARK 465     GLN A   389                                                      
REMARK 465     ASP A   390                                                      
REMARK 465     LEU A   391                                                      
REMARK 465     LEU A   392                                                      
REMARK 465     LEU A   393                                                      
REMARK 465     LEU A   394                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     SER B   385                                                      
REMARK 465     GLU B   386                                                      
REMARK 465     ASN B   387                                                      
REMARK 465     VAL B   388                                                      
REMARK 465     GLN B   389                                                      
REMARK 465     ASP B   390                                                      
REMARK 465     LEU B   391                                                      
REMARK 465     LEU B   392                                                      
REMARK 465     LEU B   393                                                      
REMARK 465     LEU B   394                                                      
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  62       52.05   -147.78                                   
REMARK 500    THR A 140      -50.09   -123.11                                   
REMARK 500    ALA A 191     -132.34    -87.75                                   
REMARK 500    PHE A 217       78.24   -100.74                                   
REMARK 500    TYR A 288      119.94   -160.32                                   
REMARK 500    ASN B  62       50.75   -145.31                                   
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                              NA A 589  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  10   OD2                                                    
REMARK 620 2 TYR A  15   O   118.9                                              
REMARK 620 3 HOH A 656   O    73.7 165.8                                        
REMARK 620 4 HOH A 626   O    92.5  89.3  97.0                                  
REMARK 620 5 ADP A 486   O3B 123.4 107.1  58.8 120.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 590  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 204   OG1                                                    
REMARK 620 2 VO4 A 491   O1   93.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 689  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  10   OD2                                                    
REMARK 620 2 TYR B  15   O   117.0                                              
REMARK 620 3 HOH B 728   O    92.2  88.0                                        
REMARK 620 4 ADP B 486   O3B 123.4 109.0 121.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 690  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B 204   OG1                                                    
REMARK 620 2 ASP B 206   OD2  76.5                                              
REMARK 620 3 VO4 B 491   O1   90.1 113.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 587  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 600   O                                                      
REMARK 620 2 HOH A 656   O    98.5                                              
REMARK 620 3 VO4 A 491   O1   81.8 172.0                                        
REMARK 620 4 ADP A 486   O3B 174.5  80.9  99.5                                  
REMARK 620 5 HOH A 727   O    93.0  94.5  77.5  92.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 687  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 712   O                                                      
REMARK 620 2 ADP B 486   O3B  85.6                                              
REMARK 620 3 HOH B 840   O   176.3  90.8                                        
REMARK 620 4 VO4 B 491   O1   79.2  95.5 101.8                                  
REMARK 620 5 HOH B 803   O    93.3 172.1  90.2  92.0                            
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 MG A 587                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 687                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 589                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 590                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 689                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 690                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 A 491                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 B 491                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 486                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 486                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2QWL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2QWN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2QWO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2QWP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2QWQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2QWR   RELATED DB: PDB                                   
DBREF  2QWM A    1   394  UNP    P19120   HSP7C_BOVIN      1    394             
DBREF  2QWM B    1   394  UNP    P19120   HSP7C_BOVIN      1    394             
SEQRES   1 A  394  MET SER LYS GLY PRO ALA VAL GLY ILE ASP LEU GLY THR          
SEQRES   2 A  394  THR TYR SER CYS VAL GLY VAL PHE GLN HIS GLY LYS VAL          
SEQRES   3 A  394  GLU ILE ILE ALA ASN ASP GLN GLY ASN ARG THR THR PRO          
SEQRES   4 A  394  SER TYR VAL ALA PHE THR ASP THR GLU ARG LEU ILE GLY          
SEQRES   5 A  394  ASP ALA ALA LYS ASN GLN VAL ALA MET ASN PRO THR ASN          
SEQRES   6 A  394  THR VAL PHE ASP ALA LYS ARG LEU ILE GLY ARG ARG PHE          
SEQRES   7 A  394  ASP ASP ALA VAL VAL GLN SER ASP MET LYS HIS TRP PRO          
SEQRES   8 A  394  PHE MET VAL VAL ASN ASP ALA GLY ARG PRO LYS VAL GLN          
SEQRES   9 A  394  VAL GLU TYR LYS GLY GLU THR LYS SER PHE TYR PRO GLU          
SEQRES  10 A  394  GLU VAL SER SER MET VAL LEU THR LYS MET LYS GLU ILE          
SEQRES  11 A  394  ALA GLU ALA TYR LEU GLY LYS THR VAL THR ASN ALA VAL          
SEQRES  12 A  394  VAL THR VAL PRO ALA TYR PHE ASN ASP SER GLN ARG GLN          
SEQRES  13 A  394  ALA THR LYS ASP ALA GLY THR ILE ALA GLY LEU ASN VAL          
SEQRES  14 A  394  LEU ARG ILE ILE ASN GLU PRO THR ALA ALA ALA ILE ALA          
SEQRES  15 A  394  TYR GLY LEU ASP LYS LYS VAL GLY ALA GLU ARG ASN VAL          
SEQRES  16 A  394  LEU ILE PHE ASP LEU GLY GLY GLY THR PHE ASP VAL SER          
SEQRES  17 A  394  ILE LEU THR ILE GLU ASP GLY ILE PHE GLU VAL LYS SER          
SEQRES  18 A  394  THR ALA GLY ASP THR HIS LEU GLY GLY GLU ASP PHE ASP          
SEQRES  19 A  394  ASN ARG MET VAL ASN HIS PHE ILE ALA GLU PHE LYS ARG          
SEQRES  20 A  394  LYS HIS LYS LYS ASP ILE SER GLU ASN LYS ARG ALA VAL          
SEQRES  21 A  394  ARG ARG LEU ARG THR ALA CYS GLU ARG ALA LYS ARG THR          
SEQRES  22 A  394  LEU SER SER SER THR GLN ALA SER ILE GLU ILE ASP SER          
SEQRES  23 A  394  LEU TYR GLU GLY ILE ASP PHE TYR THR SER ILE THR ARG          
SEQRES  24 A  394  ALA ARG PHE GLU GLU LEU ASN ALA ASP LEU PHE ARG GLY          
SEQRES  25 A  394  THR LEU ASP PRO VAL GLU LYS ALA LEU ARG ASP ALA LYS          
SEQRES  26 A  394  LEU ASP LYS SER GLN ILE HIS ASP ILE VAL LEU VAL GLY          
SEQRES  27 A  394  GLY SER THR ARG ILE PRO LYS ILE GLN LYS LEU LEU GLN          
SEQRES  28 A  394  ASP PHE PHE ASN GLY LYS GLU LEU ASN LYS SER ILE ASN          
SEQRES  29 A  394  PRO ASP GLU ALA VAL ALA TYR GLY ALA ALA VAL GLN ALA          
SEQRES  30 A  394  ALA ILE LEU SER GLY ASP LYS SER GLU ASN VAL GLN ASP          
SEQRES  31 A  394  LEU LEU LEU LEU                                              
SEQRES   1 B  394  MET SER LYS GLY PRO ALA VAL GLY ILE ASP LEU GLY THR          
SEQRES   2 B  394  THR TYR SER CYS VAL GLY VAL PHE GLN HIS GLY LYS VAL          
SEQRES   3 B  394  GLU ILE ILE ALA ASN ASP GLN GLY ASN ARG THR THR PRO          
SEQRES   4 B  394  SER TYR VAL ALA PHE THR ASP THR GLU ARG LEU ILE GLY          
SEQRES   5 B  394  ASP ALA ALA LYS ASN GLN VAL ALA MET ASN PRO THR ASN          
SEQRES   6 B  394  THR VAL PHE ASP ALA LYS ARG LEU ILE GLY ARG ARG PHE          
SEQRES   7 B  394  ASP ASP ALA VAL VAL GLN SER ASP MET LYS HIS TRP PRO          
SEQRES   8 B  394  PHE MET VAL VAL ASN ASP ALA GLY ARG PRO LYS VAL GLN          
SEQRES   9 B  394  VAL GLU TYR LYS GLY GLU THR LYS SER PHE TYR PRO GLU          
SEQRES  10 B  394  GLU VAL SER SER MET VAL LEU THR LYS MET LYS GLU ILE          
SEQRES  11 B  394  ALA GLU ALA TYR LEU GLY LYS THR VAL THR ASN ALA VAL          
SEQRES  12 B  394  VAL THR VAL PRO ALA TYR PHE ASN ASP SER GLN ARG GLN          
SEQRES  13 B  394  ALA THR LYS ASP ALA GLY THR ILE ALA GLY LEU ASN VAL          
SEQRES  14 B  394  LEU ARG ILE ILE ASN GLU PRO THR ALA ALA ALA ILE ALA          
SEQRES  15 B  394  TYR GLY LEU ASP LYS LYS VAL GLY ALA GLU ARG ASN VAL          
SEQRES  16 B  394  LEU ILE PHE ASP LEU GLY GLY GLY THR PHE ASP VAL SER          
SEQRES  17 B  394  ILE LEU THR ILE GLU ASP GLY ILE PHE GLU VAL LYS SER          
SEQRES  18 B  394  THR ALA GLY ASP THR HIS LEU GLY GLY GLU ASP PHE ASP          
SEQRES  19 B  394  ASN ARG MET VAL ASN HIS PHE ILE ALA GLU PHE LYS ARG          
SEQRES  20 B  394  LYS HIS LYS LYS ASP ILE SER GLU ASN LYS ARG ALA VAL          
SEQRES  21 B  394  ARG ARG LEU ARG THR ALA CYS GLU ARG ALA LYS ARG THR          
SEQRES  22 B  394  LEU SER SER SER THR GLN ALA SER ILE GLU ILE ASP SER          
SEQRES  23 B  394  LEU TYR GLU GLY ILE ASP PHE TYR THR SER ILE THR ARG          
SEQRES  24 B  394  ALA ARG PHE GLU GLU LEU ASN ALA ASP LEU PHE ARG GLY          
SEQRES  25 B  394  THR LEU ASP PRO VAL GLU LYS ALA LEU ARG ASP ALA LYS          
SEQRES  26 B  394  LEU ASP LYS SER GLN ILE HIS ASP ILE VAL LEU VAL GLY          
SEQRES  27 B  394  GLY SER THR ARG ILE PRO LYS ILE GLN LYS LEU LEU GLN          
SEQRES  28 B  394  ASP PHE PHE ASN GLY LYS GLU LEU ASN LYS SER ILE ASN          
SEQRES  29 B  394  PRO ASP GLU ALA VAL ALA TYR GLY ALA ALA VAL GLN ALA          
SEQRES  30 B  394  ALA ILE LEU SER GLY ASP LYS SER GLU ASN VAL GLN ASP          
SEQRES  31 B  394  LEU LEU LEU LEU                                              
HET     MG  A 587       1                                                       
HET     NA  A 589       1                                                       
HET     NA  A 590       1                                                       
HET    VO4  A 491       5                                                       
HET    ADP  A 486      27                                                       
HET     MG  B 687       1                                                       
HET     NA  B 689       1                                                       
HET     NA  B 690       1                                                       
HET    VO4  B 491       5                                                       
HET    ADP  B 486      27                                                       
HET    GOL  B   1       6                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      NA SODIUM ION                                                       
HETNAM     VO4 VANADATE ION                                                     
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   4   NA    4(NA 1+)                                                     
FORMUL   6  VO4    2(O4 V 3-)                                                   
FORMUL   7  ADP    2(C10 H15 N5 O10 P2)                                         
FORMUL  13  GOL    C3 H8 O3                                                     
FORMUL  14  HOH   *359(H2 O)                                                    
HELIX    1   1 GLY A   52  GLN A   58  1                                   7    
HELIX    2   2 VAL A   59  THR A   64  5                                   6    
HELIX    3   3 ASP A   69  LEU A   73  5                                   5    
HELIX    4   4 ASP A   80  LYS A   88  1                                   9    
HELIX    5   5 TYR A  115  GLY A  136  1                                  22    
HELIX    6   6 ASN A  151  ALA A  165  1                                  15    
HELIX    7   7 GLU A  175  TYR A  183  1                                   9    
HELIX    8   8 GLY A  229  LYS A  250  1                                  22    
HELIX    9   9 ASN A  256  LEU A  274  1                                  19    
HELIX   10  10 ARG A  299  ASN A  306  1                                   8    
HELIX   11  11 ASN A  306  THR A  313  1                                   8    
HELIX   12  12 THR A  313  ALA A  324  1                                  12    
HELIX   13  13 ASP A  327  ILE A  331  5                                   5    
HELIX   14  14 GLY A  338  ARG A  342  5                                   5    
HELIX   15  15 ILE A  343  PHE A  354  1                                  12    
HELIX   16  16 GLU A  367  SER A  381  1                                  15    
HELIX   17  17 GLY B   52  GLN B   58  1                                   7    
HELIX   18  18 ASN B   62  THR B   64  5                                   3    
HELIX   19  19 ASP B   69  ILE B   74  1                                   6    
HELIX   20  20 ASP B   80  LYS B   88  1                                   9    
HELIX   21  21 TYR B  115  GLY B  136  1                                  22    
HELIX   22  22 ASN B  151  ALA B  165  1                                  15    
HELIX   23  23 GLU B  175  TYR B  183  1                                   9    
HELIX   24  24 GLY B  229  LYS B  250  1                                  22    
HELIX   25  25 ASN B  256  LEU B  274  1                                  19    
HELIX   26  26 ARG B  299  ASN B  306  1                                   8    
HELIX   27  27 ASN B  306  THR B  313  1                                   8    
HELIX   28  28 THR B  313  LYS B  325  1                                  13    
HELIX   29  29 ASP B  327  ILE B  331  5                                   5    
HELIX   30  30 GLY B  338  ARG B  342  5                                   5    
HELIX   31  31 ILE B  343  PHE B  354  1                                  12    
HELIX   32  32 GLU B  367  SER B  381  1                                  15    
SHEET    1   A 3 LYS A  25  ILE A  28  0                                        
SHEET    2   A 3 TYR A  15  GLN A  22 -1  N  VAL A  20   O  GLU A  27           
SHEET    3   A 3 THR A  38  PRO A  39 -1  O  THR A  38   N  SER A  16           
SHEET    1   B 5 LYS A  25  ILE A  28  0                                        
SHEET    2   B 5 TYR A  15  GLN A  22 -1  N  VAL A  20   O  GLU A  27           
SHEET    3   B 5 VAL A   7  ASP A  10 -1  N  GLY A   8   O  GLY A  19           
SHEET    4   B 5 ASN A 141  VAL A 146  1  O  VAL A 143   N  ILE A   9           
SHEET    5   B 5 ASN A 168  ASN A 174  1  O  LEU A 170   N  ALA A 142           
SHEET    1   C 3 ARG A  49  ILE A  51  0                                        
SHEET    2   C 3 VAL A  42  PHE A  44 -1  N  ALA A  43   O  LEU A  50           
SHEET    3   C 3 THR A  66  VAL A  67 -1  O  VAL A  67   N  VAL A  42           
SHEET    1   D 3 MET A  93  ASP A  97  0                                        
SHEET    2   D 3 ARG A 100  TYR A 107 -1  O  LYS A 102   N  VAL A  95           
SHEET    3   D 3 GLU A 110  PHE A 114 -1  O  GLU A 110   N  TYR A 107           
SHEET    1   E 4 ILE A 216  ASP A 225  0                                        
SHEET    2   E 4 PHE A 205  GLU A 213 -1  N  VAL A 207   O  ALA A 223           
SHEET    3   E 4 ARG A 193  LEU A 200 -1  N  VAL A 195   O  LEU A 210           
SHEET    4   E 4 ASP A 333  VAL A 337  1  O  VAL A 335   N  LEU A 196           
SHEET    1   F 2 GLN A 279  TYR A 288  0                                        
SHEET    2   F 2 ILE A 291  THR A 298 -1  O  PHE A 293   N  ILE A 284           
SHEET    1   G 3 LYS B  25  ILE B  28  0                                        
SHEET    2   G 3 TYR B  15  GLN B  22 -1  N  VAL B  20   O  GLU B  27           
SHEET    3   G 3 THR B  38  PRO B  39 -1  O  THR B  38   N  SER B  16           
SHEET    1   H 5 LYS B  25  ILE B  28  0                                        
SHEET    2   H 5 TYR B  15  GLN B  22 -1  N  VAL B  20   O  GLU B  27           
SHEET    3   H 5 VAL B   7  ASP B  10 -1  N  ASP B  10   O  CYS B  17           
SHEET    4   H 5 ASN B 141  VAL B 146  1  O  VAL B 143   N  ILE B   9           
SHEET    5   H 5 ASN B 168  ASN B 174  1  O  LEU B 170   N  ALA B 142           
SHEET    1   I 3 ARG B  49  ILE B  51  0                                        
SHEET    2   I 3 VAL B  42  PHE B  44 -1  N  ALA B  43   O  LEU B  50           
SHEET    3   I 3 THR B  66  VAL B  67 -1  O  VAL B  67   N  VAL B  42           
SHEET    1   J 3 MET B  93  ASP B  97  0                                        
SHEET    2   J 3 ARG B 100  TYR B 107 -1  O  LYS B 102   N  VAL B  95           
SHEET    3   J 3 GLU B 110  PHE B 114 -1  O  LYS B 112   N  VAL B 105           
SHEET    1   K 4 ILE B 216  ASP B 225  0                                        
SHEET    2   K 4 PHE B 205  GLU B 213 -1  N  VAL B 207   O  ALA B 223           
SHEET    3   K 4 ARG B 193  LEU B 200 -1  N  VAL B 195   O  LEU B 210           
SHEET    4   K 4 ASP B 333  VAL B 337  1  O  VAL B 335   N  PHE B 198           
SHEET    1   L 2 GLN B 279  TYR B 288  0                                        
SHEET    2   L 2 ILE B 291  THR B 298 -1  O  PHE B 293   N  ILE B 284           
LINK         OD2 ASP A  10                NA    NA A 589     1555   1555  2.59  
LINK         O   TYR A  15                NA    NA A 589     1555   1555  2.67  
LINK         OG1 THR A 204                NA    NA A 590     1555   1555  2.65  
LINK         OD2 ASP B  10                NA    NA B 689     1555   1555  2.67  
LINK         O   TYR B  15                NA    NA B 689     1555   1555  2.66  
LINK         OG1 THR B 204                NA    NA B 690     1555   1555  2.71  
LINK         OD2 ASP B 206                NA    NA B 690     1555   1555  2.92  
LINK        MG    MG A 587                 O   HOH A 600     1555   1555  2.22  
LINK        MG    MG A 587                 O   HOH A 656     1555   1555  2.08  
LINK        MG    MG A 587                 O1  VO4 A 491     1555   1555  1.82  
LINK        MG    MG A 587                 O3B ADP A 486     1555   1555  1.94  
LINK        MG    MG A 587                 O   HOH A 727     1555   1555  2.01  
LINK        MG    MG B 687                 O   HOH B 712     1555   1555  2.09  
LINK        MG    MG B 687                 O3B ADP B 486     1555   1555  2.03  
LINK        MG    MG B 687                 O   HOH B 840     1555   1555  2.00  
LINK        MG    MG B 687                 O1  VO4 B 491     1555   1555  1.87  
LINK        MG    MG B 687                 O   HOH B 803     1555   1555  1.99  
LINK        NA    NA A 589                 O   HOH A 656     1555   1555  2.65  
LINK        NA    NA A 589                 O   HOH A 626     1555   1555  2.51  
LINK        NA    NA A 589                 O3B ADP A 486     1555   1555  2.66  
LINK        NA    NA A 590                 O1  VO4 A 491     1555   1555  2.61  
LINK        NA    NA B 689                 O   HOH B 728     1555   1555  2.65  
LINK        NA    NA B 689                 O3B ADP B 486     1555   1555  2.67  
LINK        NA    NA B 690                 O1  VO4 B 491     1555   1555  2.53  
SITE     1 AC1  6 ADP A 486  VO4 A 491   NA A 589  HOH A 600                    
SITE     2 AC1  6 HOH A 656  HOH A 727                                          
SITE     1 AC2  6 ADP B 486  VO4 B 491   NA B 689  HOH B 712                    
SITE     2 AC2  6 HOH B 803  HOH B 840                                          
SITE     1 AC3  6 ASP A  10  TYR A  15  ADP A 486   MG A 587                    
SITE     2 AC3  6 HOH A 626  HOH A 656                                          
SITE     1 AC4  5 ASP A 199  THR A 204  ASP A 206  VO4 A 491                    
SITE     2 AC4  5 HOH A 727                                                     
SITE     1 AC5  6 ASP B  10  TYR B  15  ADP B 486   MG B 687                    
SITE     2 AC5  6 HOH B 728  HOH B 840                                          
SITE     1 AC6  4 ASP B 199  THR B 204  ASP B 206  VO4 B 491                    
SITE     1 AC7 13 GLY A  12  THR A  13  LYS A  71  PRO A 147                    
SITE     2 AC7 13 GLU A 175  THR A 204  ADP A 486   MG A 587                    
SITE     3 AC7 13  NA A 590  HOH A 597  HOH A 600  HOH A 640                    
SITE     4 AC7 13 HOH A 727                                                     
SITE     1 AC8 14 GLY B  12  THR B  13  LYS B  71  PRO B 147                    
SITE     2 AC8 14 GLU B 175  THR B 204  ADP B 486   MG B 687                    
SITE     3 AC8 14  NA B 690  HOH B 707  HOH B 712  HOH B 714                    
SITE     4 AC8 14 HOH B 803  HOH B 840                                          
SITE     1 AC9 28 GLY A  12  THR A  13  THR A  14  TYR A  15                    
SITE     2 AC9 28 GLY A 201  GLY A 202  GLY A 230  GLU A 268                    
SITE     3 AC9 28 LYS A 271  ARG A 272  SER A 275  GLY A 338                    
SITE     4 AC9 28 GLY A 339  SER A 340  ARG A 342  ILE A 343                    
SITE     5 AC9 28 ASP A 366  VO4 A 491   MG A 587   NA A 589                    
SITE     6 AC9 28 HOH A 591  HOH A 597  HOH A 622  HOH A 626                    
SITE     7 AC9 28 HOH A 656  HOH A 663  HOH A 720  HOH A 727                    
SITE     1 BC1 28 GLY B  12  THR B  13  THR B  14  TYR B  15                    
SITE     2 BC1 28 GLY B 201  GLY B 202  GLY B 230  GLU B 268                    
SITE     3 BC1 28 LYS B 271  ARG B 272  SER B 275  GLY B 338                    
SITE     4 BC1 28 GLY B 339  SER B 340  ARG B 342  ILE B 343                    
SITE     5 BC1 28 ASP B 366  VO4 B 491   MG B 687   NA B 689                    
SITE     6 BC1 28 HOH B 701  HOH B 707  HOH B 712  HOH B 728                    
SITE     7 BC1 28 HOH B 799  HOH B 824  HOH B 829  HOH B 840                    
SITE     1 BC2  9 GLU A 318  LYS A 328  ARG B 311  LEU B 314                    
SITE     2 BC2  9 LEU B 349  ASP B 352  PHE B 353  HOH B 736                    
SITE     3 BC2  9 HOH B 818                                                     
CRYST1   73.336   77.841   75.793  90.00 101.53  90.00 P 1 21 1      4          
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      0.013636  0.000000  0.002782        0.00000                         
SCALE2      0.000000  0.012847  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013466        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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